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Log page index: User:ProteinBoxBot/PBB_Log_Index
[edit] Protein Status Quick Log - Date: 20:08, 17 November 2007 (UTC)
[edit] Proteins without matches (8)
[edit] Proteins with a High Potential Match (11)
[edit] Redirected Proteins (6)
[edit] Manual Inspection (Page not found) (19)
[edit] Updated (6)
[edit] Protein Status Grid - Date: 20:08, 17 November 2007 (UTC)
[edit] Vebose Log - Date: 20:08, 17 November 2007 (UTC)
- INFO: Beginning work on ACTN4... {November 17, 2007 11:46:45 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:47:19 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ACTN4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1wlx.
| PDB = {{PDB2|1wlx}}, {{PDB2|2eyi}}, {{PDB2|2eyn}}
| Name = Actinin, alpha 4
| HGNCid = 166
| Symbol = ACTN4
| AltSymbols =; DKFZp686K23158; FSGS; FSGS1
| OMIM = 604638
| ECnumber =
| Homologene = 55857
| MGIid = 1890773
| GeneAtlas_image1 = PBB_GE_ACTN4_200601_at_tn.png
| Function = {{GNF_GO|id=GO:0001882 |text = nucleoside binding}} {{GNF_GO|id=GO:0005178 |text = integrin binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0051015 |text = actin filament binding}}
| Component = {{GNF_GO|id=GO:0001725 |text = stress fiber}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0030863 |text = cortical cytoskeleton}} {{GNF_GO|id=GO:0031143 |text = pseudopodium}} {{GNF_GO|id=GO:0043234 |text = protein complex}} {{GNF_GO|id=GO:0048471 |text = perinuclear region of cytoplasm}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0032417 |text = positive regulation of sodium:hydrogen antiporter activity}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0048549 |text = positive regulation of pinocytosis}} {{GNF_GO|id=GO:0051017 |text = actin filament bundle formation}} {{GNF_GO|id=GO:0051271 |text = negative regulation of cell motility}} {{GNF_GO|id=GO:0051272 |text = positive regulation of cell motility}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 81
| Hs_Ensembl = ENSG00000130402
| Hs_RefseqProtein = NP_004915
| Hs_RefseqmRNA = NM_004924
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 43830167
| Hs_GenLoc_end = 43913010
| Hs_Uniprot = O43707
| Mm_EntrezGene = 60595
| Mm_Ensembl = ENSMUSG00000054808
| Mm_RefseqmRNA = NM_021895
| Mm_RefseqProtein = NP_068695
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 28602011
| Mm_GenLoc_end = 28671040
| Mm_Uniprot = Q1A602
}}
}}
'''Actinin, alpha 4''', also known as '''ACTN4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACTN4 actinin, alpha 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=81| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments. This gene encodes a nonmuscle, alpha actinin isoform which is concentrated in the cytoplasm, and thought to be involved in metastatic processes. Mutations in this gene have been associated with focal and segmental glomerulosclerosis.<ref name="entrez">{{cite web | title = Entrez Gene: ACTN4 actinin, alpha 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=81| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi= }}
*{{cite journal | author=Yürüker B, Niggli V |title=Alpha-actinin and vinculin in human neutrophils: reorganization during adhesion and relation to the actin network. |journal=J. Cell. Sci. |volume=101 ( Pt 2) |issue= |pages= 403-14 |year= 1992 |pmid= 1629252 |doi= }}
*{{cite journal | author=Otey CA, Pavalko FM, Burridge K |title=An interaction between alpha-actinin and the beta 1 integrin subunit in vitro. |journal=J. Cell Biol. |volume=111 |issue= 2 |pages= 721-9 |year= 1990 |pmid= 2116421 |doi= }}
*{{cite journal | author=Pavalko FM, LaRoche SM |title=Activation of human neutrophils induces an interaction between the integrin beta 2-subunit (CD18) and the actin binding protein alpha-actinin. |journal=J. Immunol. |volume=151 |issue= 7 |pages= 3795-807 |year= 1993 |pmid= 8104223 |doi= }}
*{{cite journal | author=Mathis BJ, Kim SH, Calabrese K, ''et al.'' |title=A locus for inherited focal segmental glomerulosclerosis maps to chromosome 19q13. |journal=Kidney Int. |volume=53 |issue= 2 |pages= 282-6 |year= 1998 |pmid= 9461087 |doi= 10.1046/j.1523-1755.1998.00828.x }}
*{{cite journal | author=Honda K, Yamada T, Endo R, ''et al.'' |title=Actinin-4, a novel actin-bundling protein associated with cell motility and cancer invasion. |journal=J. Cell Biol. |volume=140 |issue= 6 |pages= 1383-93 |year= 1998 |pmid= 9508771 |doi= }}
*{{cite journal | author=Zhang H, Wang L, Kao S, ''et al.'' |title=Functional interaction between the cytoplasmic leucine-zipper domain of HIV-1 gp41 and p115-RhoGEF. |journal=Curr. Biol. |volume=9 |issue= 21 |pages= 1271-4 |year= 1999 |pmid= 10556093 |doi= }}
*{{cite journal | author=Nikolopoulos SN, Spengler BA, Kisselbach K, ''et al.'' |title=The human non-muscle alpha-actinin protein encoded by the ACTN4 gene suppresses tumorigenicity of human neuroblastoma cells. |journal=Oncogene |volume=19 |issue= 3 |pages= 380-6 |year= 2000 |pmid= 10656685 |doi= 10.1038/sj.onc.1203310 }}
*{{cite journal | author=El-Husseini AE, Kwasnicka D, Yamada T, ''et al.'' |title=BERP, a novel ring finger protein, binds to alpha-actinin-4. |journal=Biochem. Biophys. Res. Commun. |volume=267 |issue= 3 |pages= 906-11 |year= 2000 |pmid= 10673389 |doi= 10.1006/bbrc.1999.2045 }}
*{{cite journal | author=Kaplan JM, Kim SH, North KN, ''et al.'' |title=Mutations in ACTN4, encoding alpha-actinin-4, cause familial focal segmental glomerulosclerosis. |journal=Nat. Genet. |volume=24 |issue= 3 |pages= 251-6 |year= 2000 |pmid= 10700177 |doi= 10.1038/73456 }}
*{{cite journal | author=Vallenius T, Luukko K, Mäkelä TP |title=CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4. |journal=J. Biol. Chem. |volume=275 |issue= 15 |pages= 11100-5 |year= 2000 |pmid= 10753915 |doi= }}
*{{cite journal | author=Holliday LS, Lu M, Lee BS, ''et al.'' |title=The amino-terminal domain of the B subunit of vacuolar H+-ATPase contains a filamentous actin binding site. |journal=J. Biol. Chem. |volume=275 |issue= 41 |pages= 32331-7 |year= 2000 |pmid= 10915794 |doi= 10.1074/jbc.M004795200 }}
*{{cite journal | author=Walikonis RS, Oguni A, Khorosheva EM, ''et al.'' |title=Densin-180 forms a ternary complex with the (alpha)-subunit of Ca2+/calmodulin-dependent protein kinase II and (alpha)-actinin. |journal=J. Neurosci. |volume=21 |issue= 2 |pages= 423-33 |year= 2001 |pmid= 11160423 |doi= }}
*{{cite journal | author=Echchakir H, Mami-Chouaib F, Vergnon I, ''et al.'' |title=A point mutation in the alpha-actinin-4 gene generates an antigenic peptide recognized by autologous cytolytic T lymphocytes on a human lung carcinoma. |journal=Cancer Res. |volume=61 |issue= 10 |pages= 4078-83 |year= 2001 |pmid= 11358829 |doi= }}
*{{cite journal | author=Xu F, Zhao R, Peng Y, ''et al.'' |title=Association of tyrosine phosphatase SHP-2 with F-actin at low cell densities. |journal=J. Biol. Chem. |volume=276 |issue= 31 |pages= 29479-84 |year= 2001 |pmid= 11382784 |doi= 10.1074/jbc.M104428200 }}
*{{cite journal | author=Hüttelmaier S, Illenberger S, Grosheva I, ''et al.'' |title=Raver1, a dual compartment protein, is a ligand for PTB/hnRNPI and microfilament attachment proteins. |journal=J. Cell Biol. |volume=155 |issue= 5 |pages= 775-86 |year= 2002 |pmid= 11724819 |doi= 10.1083/jcb.200105044 }}
*{{cite journal | author=Renoult C, Blondin L, Fattoum A, ''et al.'' |title=Binding of gelsolin domain 2 to actin. An actin interface distinct from that of gelsolin domain 1 and from ADF/cofilin. |journal=Eur. J. Biochem. |volume=268 |issue= 23 |pages= 6165-75 |year= 2002 |pmid= 11733011 |doi= }}
*{{cite journal | author=Gonzalez AM, Otey C, Edlund M, Jones JC |title=Interactions of a hemidesmosome component and actinin family members. |journal=J. Cell. Sci. |volume=114 |issue= Pt 23 |pages= 4197-206 |year= 2002 |pmid= 11739652 |doi= }}
*{{cite journal | author=Lukoyanova N, VanLoock MS, Orlova A, ''et al.'' |title=Each actin subunit has three nebulin binding sites: implications for steric blocking. |journal=Curr. Biol. |volume=12 |issue= 5 |pages= 383-8 |year= 2002 |pmid= 11882289 |doi= }}
*{{cite journal | author=Kim JH, Lee-Kwon W, Park JB, ''et al.'' |title=Ca(2+)-dependent inhibition of Na+/H+ exchanger 3 (NHE3) requires an NHE3-E3KARP-alpha-actinin-4 complex for oligomerization and endocytosis. |journal=J. Biol. Chem. |volume=277 |issue= 26 |pages= 23714-24 |year= 2002 |pmid= 11948184 |doi= 10.1074/jbc.M200835200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ADCYAP1... {November 17, 2007 11:47:19 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:47:49 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ADCYAP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2d2p.
| PDB = {{PDB2|2d2p}}, {{PDB2|2jod}}
| Name = Adenylate cyclase activating polypeptide 1 (pituitary)
| HGNCid = 241
| Symbol = ADCYAP1
| AltSymbols =; MGC126852; PACAP
| OMIM = 102980
| ECnumber =
| Homologene = 869
| MGIid = 105094
| GeneAtlas_image1 = PBB_GE_ADCYAP1_206281_at_tn.png
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}} {{GNF_GO|id=GO:0005184 |text = neuropeptide hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0007190 |text = adenylate cyclase activation}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007565 |text = female pregnancy}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 116
| Hs_Ensembl = ENSG00000141433
| Hs_RefseqProtein = NP_001108
| Hs_RefseqmRNA = NM_001117
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 18
| Hs_GenLoc_start = 895387
| Hs_GenLoc_end = 901054
| Hs_Uniprot = P18509
| Mm_EntrezGene = 11516
| Mm_Ensembl = ENSMUSG00000024256
| Mm_RefseqmRNA = NM_009625
| Mm_RefseqProtein = NP_033755
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 93503312
| Mm_GenLoc_end = 93510828
| Mm_Uniprot = Q3UYH8
}}
}}
'''Adenylate cyclase activating polypeptide 1 (pituitary)''', also known as '''ADCYAP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ADCYAP1 adenylate cyclase activating polypeptide 1 (pituitary)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=116| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes adenylate cyclase activating polypeptide 1. Mediated by adenylate cyclase activating polypeptide 1 receptors, this polypeptide stimulates adenylate cyclase and subsequently increases the cAMP level in target cells. Adenylate cyclase activating polypeptide 1 is not only a hypophysiotropic hormone, but also functions as a neurotransmitter and neuromodulator. In addition, it plays a role in paracrine and autocrine regulation of certain types of cells. This gene is composed of five exons. Exons 1 and 2 encode the 5' UTR and signal peptide, respectively; exon 4 encodes an adenylate cyclase activating polypeptide 1-related peptide; and exon 5 encodes the mature peptide and 3' UTR. This gene encodes three different mature peptides, including two isotypes: a shorter form and a longer form.<ref name="entrez">{{cite web | title = Entrez Gene: ADCYAP1 adenylate cyclase activating polypeptide 1 (pituitary)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=116| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Geng L, Ju G |title=[The discovery of pituitary adenylate cyclase activating polypeptide (PACAP) and its research progress] |journal=Sheng li ke xue jin zhan [Progress in physiology] |volume=28 |issue= 1 |pages= 29-34 |year= 2000 |pmid= 10921074 |doi= }}
*{{cite journal | author=Fahrenkrug J |title=Gut/brain peptides in the genital tract: VIP and PACAP. |journal=Scand. J. Clin. Lab. Invest. Suppl. |volume=234 |issue= |pages= 35-9 |year= 2002 |pmid= 11713978 |doi= }}
*{{cite journal | author=Waschek JA |title=Multiple actions of pituitary adenylyl cyclase activating peptide in nervous system development and regeneration. |journal=Dev. Neurosci. |volume=24 |issue= 1 |pages= 14-23 |year= 2002 |pmid= 12145407 |doi= }}
*{{cite journal | author=Fahrenkrug J |title=PACAP--a multifacetted neuropeptide. |journal=Chronobiol. Int. |volume=23 |issue= 1-2 |pages= 53-61 |year= 2006 |pmid= 16687279 |doi= 10.1080/07420520500464569 }}
*{{cite journal | author=Conconi MT, Spinazzi R, Nussdorfer GG |title=Endogenous ligands of PACAP/VIP receptors in the autocrine-paracrine regulation of the adrenal gland. |journal=Int. Rev. Cytol. |volume=249 |issue= |pages= 1-51 |year= 2006 |pmid= 16697281 |doi= 10.1016/S0074-7696(06)49001-X }}
*{{cite journal | author=Nakata M, Yada T |title=PACAP in the glucose and energy homeostasis: physiological role and therapeutic potential. |journal=Curr. Pharm. Des. |volume=13 |issue= 11 |pages= 1105-12 |year= 2007 |pmid= 17430174 |doi= }}
*{{cite journal | author=Felley CP, Qian JM, Mantey S, ''et al.'' |title=Chief cells possess a receptor with high affinity for PACAP and VIP that stimulates pepsinogen release. |journal=Am. J. Physiol. |volume=263 |issue= 6 Pt 1 |pages= G901-7 |year= 1993 |pmid= 1335692 |doi= }}
*{{cite journal | author=Inooka H, Endo S, Kitada C, ''et al.'' |title=Pituitary adenylate cyclase activating polypeptide (PACAP) with 27 residues. Conformation determined by 1H NMR and CD spectroscopies and distance geometry in 25% methanol solution. |journal=Int. J. Pept. Protein Res. |volume=40 |issue= 5 |pages= 456-64 |year= 1993 |pmid= 1483839 |doi= }}
*{{cite journal | author=Hosoya M, Kimura C, Ogi K, ''et al.'' |title=Structure of the human pituitary adenylate cyclase activating polypeptide (PACAP) gene. |journal=Biochim. Biophys. Acta |volume=1129 |issue= 2 |pages= 199-206 |year= 1992 |pmid= 1730060 |doi= }}
*{{cite journal | author=Ohkubo S, Kimura C, Ogi K, ''et al.'' |title=Primary structure and characterization of the precursor to human pituitary adenylate cyclase activating polypeptide. |journal=DNA Cell Biol. |volume=11 |issue= 1 |pages= 21-30 |year= 1992 |pmid= 1739432 |doi= }}
*{{cite journal | author=Kimura C, Ohkubo S, Ogi K, ''et al.'' |title=A novel peptide which stimulates adenylate cyclase: molecular cloning and characterization of the ovine and human cDNAs. |journal=Biochem. Biophys. Res. Commun. |volume=166 |issue= 1 |pages= 81-9 |year= 1990 |pmid= 2302217 |doi= }}
*{{cite journal | author=Cross SH, Charlton JA, Nan X, Bird AP |title=Purification of CpG islands using a methylated DNA binding column. |journal=Nat. Genet. |volume=6 |issue= 3 |pages= 236-44 |year= 1994 |pmid= 8012384 |doi= 10.1038/ng0394-236 }}
*{{cite journal | author=Inagaki N, Yoshida H, Mizuta M, ''et al.'' |title=Cloning and functional characterization of a third pituitary adenylate cyclase-activating polypeptide receptor subtype expressed in insulin-secreting cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 7 |pages= 2679-83 |year= 1994 |pmid= 8146174 |doi= }}
*{{cite journal | author=Ohtaki T, Masuda Y, Ishibashi Y, ''et al.'' |title=Purification and characterization of the receptor for pituitary adenylate cyclase-activating polypeptide. |journal=J. Biol. Chem. |volume=268 |issue= 35 |pages= 26650-7 |year= 1994 |pmid= 8253796 |doi= }}
*{{cite journal | author=Pérez-Jurado LA, Francke U |title=Dinucleotide repeat polymorphism at the human pituitary adenylate cyclase activating polypeptide (PACAP) gene. |journal=Hum. Mol. Genet. |volume=2 |issue= 6 |pages= 827 |year= 1993 |pmid= 8353512 |doi= }}
*{{cite journal | author=Weber B, Riess O, Daneshvar H, ''et al.'' |title=(CA)n-dinucleotide repeat at the PDEB locus in 4p16.3. |journal=Hum. Mol. Genet. |volume=2 |issue= 6 |pages= 827 |year= 1993 |pmid= 8394765 |doi= }}
*{{cite journal | author=Wray V, Kakoschke C, Nokihara K, Naruse S |title=Solution structure of pituitary adenylate cyclase activating polypeptide by nuclear magnetic resonance spectroscopy. |journal=Biochemistry |volume=32 |issue= 22 |pages= 5832-41 |year= 1993 |pmid= 8504103 |doi= }}
*{{cite journal | author=Gourlet P, Vandermeers A, Robberecht P, Deschodt-Lanckman M |title=Vasoactive intestinal peptide (VIP) and pituitary adenylate cyclase-activating peptide (PACAP-27, but not PACAP-38) degradation by the neutral endopeptidase EC 3.4.24.11. |journal=Biochem. Pharmacol. |volume=54 |issue= 4 |pages= 509-15 |year= 1997 |pmid= 9313778 |doi= }}
*{{cite journal | author=Zeng N, Athmann C, Kang T, ''et al.'' |title=PACAP type I receptor activation regulates ECL cells and gastric acid secretion. |journal=J. Clin. Invest. |volume=104 |issue= 10 |pages= 1383-91 |year= 1999 |pmid= 10562300 |doi= }}
*{{cite journal | author=Dautzenberg FM, Mevenkamp G, Wille S, Hauger RL |title=N-terminal splice variants of the type I PACAP receptor: isolation, characterization and ligand binding/selectivity determinants. |journal=J. Neuroendocrinol. |volume=11 |issue= 12 |pages= 941-9 |year= 2000 |pmid= 10583729 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on AP2M1... {November 17, 2007 11:50:20 AM PST}
- SEARCH REDIRECT: Control Box Found: AP2M1 {November 17, 2007 11:50:45 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:50:46 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:50:46 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:50:46 AM PST}
- UPDATED: Updated protein page: AP2M1 {November 17, 2007 11:50:53 AM PST}
- INFO: Beginning work on AREG... {November 17, 2007 11:47:50 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:48:18 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Amphiregulin (schwannoma-derived growth factor)
| HGNCid = 651
| Symbol = AREG
| AltSymbols =; AR; CRDGF; MGC13647; SDGF
| OMIM = 104640
| ECnumber =
| Homologene = 1252
| MGIid = 88068
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 374
| Hs_Ensembl =
| Hs_RefseqProtein = NP_001648
| Hs_RefseqmRNA = NM_001657
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 11839
| Mm_Ensembl = ENSMUSG00000029378
| Mm_RefseqmRNA = NM_009704
| Mm_RefseqProtein = NP_033834
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 92214799
| Mm_GenLoc_end = 92223623
| Mm_Uniprot = Q4FJT2
}}
}}
'''Amphiregulin (schwannoma-derived growth factor)''', also known as '''AREG''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AREG amphiregulin (schwannoma-derived growth factor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=374| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the epidermal growth factor family. It is an autocrine growth factor as well as a mitogen for astrocytes, Schwann cells, and fibroblasts. It is related to epidermal growth factor (EGF) and transforming growth factor alpha (TGF-alpha). This protein interacts with the EGF/TGF-alpha receptor to promote the growth of normal epithelial cells and inhibits the growth of certain aggressive carcinoma cell lines. This encoded protein is associated with a psoriasis-like skin phenotype.<ref name="entrez">{{cite web | title = Entrez Gene: AREG amphiregulin (schwannoma-derived growth factor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=374| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Culouscou JM, Remacle-Bonnet M, Carlton GW, ''et al.'' |title=Colorectum cell-derived growth factor (CRDGF) is homologous to amphiregulin, a member of the epidermal growth factor family. |journal=Growth Factors |volume=7 |issue= 3 |pages= 195-205 |year= 1993 |pmid= 1333777 |doi= }}
*{{cite journal | author=Cook PW, Mattox PA, Keeble WW, ''et al.'' |title=A heparin sulfate-regulated human keratinocyte autocrine factor is similar or identical to amphiregulin. |journal=Mol. Cell. Biol. |volume=11 |issue= 5 |pages= 2547-57 |year= 1991 |pmid= 2017164 |doi= }}
*{{cite journal | author=Kimura H, Fischer WH, Schubert D |title=Structure, expression and function of a schwannoma-derived growth factor. |journal=Nature |volume=348 |issue= 6298 |pages= 257-60 |year= 1990 |pmid= 2234093 |doi= 10.1038/348257a0 }}
*{{cite journal | author=Plowman GD, Green JM, McDonald VL, ''et al.'' |title=The amphiregulin gene encodes a novel epidermal growth factor-related protein with tumor-inhibitory activity. |journal=Mol. Cell. Biol. |volume=10 |issue= 5 |pages= 1969-81 |year= 1990 |pmid= 2325643 |doi= }}
*{{cite journal | author=Shoyab M, Plowman GD, McDonald VL, ''et al.'' |title=Structure and function of human amphiregulin: a member of the epidermal growth factor family. |journal=Science |volume=243 |issue= 4894 Pt 1 |pages= 1074-6 |year= 1989 |pmid= 2466334 |doi= }}
*{{cite journal | author=Shoyab M, McDonald VL, Bradley JG, Todaro GJ |title=Amphiregulin: a bifunctional growth-modulating glycoprotein produced by the phorbol 12-myristate 13-acetate-treated human breast adenocarcinoma cell line MCF-7. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 17 |pages= 6528-32 |year= 1988 |pmid= 3413110 |doi= }}
*{{cite journal | author=Chen CS, Bejcek BE, Kersey JH |title=A mapping study of 13 genes on human chromosome bands 4q11-->q25. |journal=Cytogenet. Cell Genet. |volume=69 |issue= 3-4 |pages= 260-5 |year= 1995 |pmid= 7698025 |doi= }}
*{{cite journal | author=Cook PW, Piepkorn M, Clegg CH, ''et al.'' |title=Transgenic expression of the human amphiregulin gene induces a psoriasis-like phenotype. |journal=J. Clin. Invest. |volume=100 |issue= 9 |pages= 2286-94 |year= 1997 |pmid= 9410906 |doi= }}
*{{cite journal | author=Wong L, Deb TB, Thompson SA, ''et al.'' |title=A differential requirement for the COOH-terminal region of the epidermal growth factor (EGF) receptor in amphiregulin and EGF mitogenic signaling. |journal=J. Biol. Chem. |volume=274 |issue= 13 |pages= 8900-9 |year= 1999 |pmid= 10085134 |doi= }}
*{{cite journal | author=Reddy KB, Krueger JS, Kondapaka SB, Diglio CA |title=Mitogen-activated protein kinase (MAPK) regulates the expression of progelatinase B (MMP-9) in breast epithelial cells. |journal=Int. J. Cancer |volume=82 |issue= 2 |pages= 268-73 |year= 1999 |pmid= 10389762 |doi= }}
*{{cite journal | author=Fernandes AM, Hamburger AW, Gerwin BI |title=Production of epidermal growth factor related ligands in tumorigenic and benign human lung epithelial cells. |journal=Cancer Lett. |volume=142 |issue= 1 |pages= 55-63 |year= 1999 |pmid= 10424781 |doi= }}
*{{cite journal | author=Lee SB, Huang K, Palmer R, ''et al.'' |title=The Wilms tumor suppressor WT1 encodes a transcriptional activator of amphiregulin. |journal=Cell |volume=98 |issue= 5 |pages= 663-73 |year= 1999 |pmid= 10490105 |doi= }}
*{{cite journal | author=Tokumaru S, Higashiyama S, Endo T, ''et al.'' |title=Ectodomain shedding of epidermal growth factor receptor ligands is required for keratinocyte migration in cutaneous wound healing. |journal=J. Cell Biol. |volume=151 |issue= 2 |pages= 209-20 |year= 2000 |pmid= 11038170 |doi= }}
*{{cite journal | author=Ebert MP, Hernberg S, Fei G, ''et al.'' |title=Induction and expression of cyclin D3 in human pancreatic cancer. |journal=J. Cancer Res. Clin. Oncol. |volume=127 |issue= 7 |pages= 449-54 |year= 2001 |pmid= 11469683 |doi= }}
*{{cite journal | author=Berquin IM, Dziubinski ML, Nolan GP, Ethier SP |title=A functional screen for genes inducing epidermal growth factor autonomy of human mammary epithelial cells confirms the role of amphiregulin. |journal=Oncogene |volume=20 |issue= 30 |pages= 4019-28 |year= 2001 |pmid= 11494130 |doi= 10.1038/sj.onc.1204537 }}
*{{cite journal | author=Thøgersen VB, Sørensen BS, Poulsen SS, ''et al.'' |title=A subclass of HER1 ligands are prognostic markers for survival in bladder cancer patients. |journal=Cancer Res. |volume=61 |issue= 16 |pages= 6227-33 |year= 2001 |pmid= 11507076 |doi= }}
*{{cite journal | author=Wolfgang CD, Essand M, Lee B, Pastan I |title=T-cell receptor gamma chain alternate reading frame protein (TARP) expression in prostate cancer cells leads to an increased growth rate and induction of caveolins and amphiregulin. |journal=Cancer Res. |volume=61 |issue= 22 |pages= 8122-6 |year= 2001 |pmid= 11719440 |doi= }}
*{{cite journal | author=Schiemann U, Konturek J, Assert R, ''et al.'' |title=mRNA expression of EGF receptor ligands in atrophic gastritis before and after Helicobacter pylori eradication. |journal=Med. Sci. Monit. |volume=8 |issue= 2 |pages= CR53-8 |year= 2002 |pmid= 11859273 |doi= }}
*{{cite journal | author=Tørring N, Møller-Ernst Jensen K, Lund L, ''et al.'' |title=Possible autocrine loop of the epidermal growth factor system in patients with benign prostatic hyperplasia treated with finasteride: a placebo-controlled randomized study. |journal=BJU Int. |volume=89 |issue= 6 |pages= 583-90 |year= 2002 |pmid= 11942969 |doi= }}
*{{cite journal | author=Hurbin A, Dubrez L, Coll JL, Favrot MC |title=Inhibition of apoptosis by amphiregulin via an insulin-like growth factor-1 receptor-dependent pathway in non-small cell lung cancer cell lines. |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 49127-33 |year= 2003 |pmid= 12356750 |doi= 10.1074/jbc.M207584200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ATP1A2... {November 17, 2007 11:48:50 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:49:20 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ATP1A2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1q3i.
| PDB = {{PDB2|1q3i}}
| Name = ATPase, Na+/K+ transporting, alpha 2 (+) polypeptide
| HGNCid = 800
| Symbol = ATP1A2
| AltSymbols =; FHM2; MGC59864; MHP2
| OMIM = 182340
| ECnumber =
| Homologene = 47947
| MGIid = 88106
| GeneAtlas_image1 = PBB_GE_ATP1A2_203296_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ATP1A2_203295_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0005391 |text = sodium:potassium-exchanging ATPase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0015077 |text = monovalent inorganic cation transmembrane transporter activity}} {{GNF_GO|id=GO:0015662 |text = ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016820 |text = hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances}} {{GNF_GO|id=GO:0030955 |text = potassium ion binding}} {{GNF_GO|id=GO:0031402 |text = sodium ion binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005890 |text = sodium:potassium-exchanging ATPase complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0001504 |text = neurotransmitter uptake}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}} {{GNF_GO|id=GO:0006814 |text = sodium ion transport}} {{GNF_GO|id=GO:0006942 |text = regulation of striated muscle contraction}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0015672 |text = monovalent inorganic cation transport}} {{GNF_GO|id=GO:0015991 |text = ATP hydrolysis coupled proton transport}} {{GNF_GO|id=GO:0030317 |text = sperm motility}} {{GNF_GO|id=GO:0030641 |text = cellular hydrogen ion homeostasis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 477
| Hs_Ensembl = ENSG00000018625
| Hs_RefseqProtein = NP_000693
| Hs_RefseqmRNA = NM_000702
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 158352172
| Hs_GenLoc_end = 158379996
| Hs_Uniprot = P50993
| Mm_EntrezGene = 98660
| Mm_Ensembl = ENSMUSG00000007097
| Mm_RefseqmRNA = NM_178405
| Mm_RefseqProtein = NP_848492
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 174108384
| Mm_GenLoc_end = 174142391
| Mm_Uniprot = Q3UHK5
}}
}}
'''ATPase, Na+/K+ transporting, alpha 2 (+) polypeptide''', also known as '''ATP1A2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP1A2 ATPase, Na+/K+ transporting, alpha 2 (+) polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=477| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the family of P-type cation transport ATPases, and to the subfamily of Na+/K+ -ATPases. Na+/K+ -ATPase is an integral membrane protein responsible for establishing and maintaining the electrochemical gradients of Na and K ions across the plasma membrane. These gradients are essential for osmoregulation, for sodium-coupled transport of a variety of organic and inorganic molecules, and for electrical excitability of nerve and muscle. This enzyme is composed of two subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The catalytic subunit of Na+/K+ -ATPase is encoded by multiple genes. This gene encodes an alpha 2 subunit.<ref name="entrez">{{cite web | title = Entrez Gene: ATP1A2 ATPase, Na+/K+ transporting, alpha 2 (+) polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=477| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lingrel JB, Orlowski J, Shull MM, Price EM |title=Molecular genetics of Na,K-ATPase. |journal=Prog. Nucleic Acid Res. Mol. Biol. |volume=38 |issue= |pages= 37-89 |year= 1990 |pmid= 2158121 |doi= }}
*{{cite journal | author=Dunbar LA, Caplan MJ |title=Ion pumps in polarized cells: sorting and regulation of the Na+, K+- and H+, K+-ATPases. |journal=J. Biol. Chem. |volume=276 |issue= 32 |pages= 29617-20 |year= 2001 |pmid= 11404365 |doi= 10.1074/jbc.R100023200 }}
*{{cite journal | author=Shull MM, Pugh DG, Lingrel JB |title=Characterization of the human Na,K-ATPase alpha 2 gene and identification of intragenic restriction fragment length polymorphisms. |journal=J. Biol. Chem. |volume=264 |issue= 29 |pages= 17532-43 |year= 1989 |pmid= 2477373 |doi= }}
*{{cite journal | author=Sverdlov ED, Bessarab DA, Malyshev IV, ''et al.'' |title=Family of human Na+,K+-ATPase genes. Structure of the putative regulatory region of the alpha+-gene. |journal=FEBS Lett. |volume=244 |issue= 2 |pages= 481-3 |year= 1989 |pmid= 2537767 |doi= }}
*{{cite journal | author=Yang-Feng TL, Schneider JW, Lindgren V, ''et al.'' |title=Chromosomal localization of human Na+, K+-ATPase alpha- and beta-subunit genes. |journal=Genomics |volume=2 |issue= 2 |pages= 128-38 |year= 1988 |pmid= 2842249 |doi= }}
*{{cite journal | author=Shull MM, Lingrel JB |title=Multiple genes encode the human Na+,K+-ATPase catalytic subunit. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 12 |pages= 4039-43 |year= 1987 |pmid= 3035563 |doi= }}
*{{cite journal | author=Sverdlov ED, Monastyrskaya GS, Broude NE, ''et al.'' |title=The family of human Na+,K+-ATPase genes. No less than five genes and/or pseudogenes related to the alpha-subunit. |journal=FEBS Lett. |volume=217 |issue= 2 |pages= 275-8 |year= 1987 |pmid= 3036582 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Zahler R, Gilmore-Hebert M, Baldwin JC, ''et al.'' |title=Expression of alpha isoforms of the Na,K-ATPase in human heart. |journal=Biochim. Biophys. Acta |volume=1149 |issue= 2 |pages= 189-94 |year= 1993 |pmid= 8391840 |doi= }}
*{{cite journal | author=Stengelin MK, Hoffman JF |title=Na,K-ATPase subunit isoforms in human reticulocytes: evidence from reverse transcription-PCR for the presence of alpha1, alpha3, beta2, beta3, and gamma. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 11 |pages= 5943-8 |year= 1997 |pmid= 9159180 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Ducros A, Joutel A, Vahedi K, ''et al.'' |title=Mapping of a second locus for familial hemiplegic migraine to 1q21-q23 and evidence of further heterogeneity. |journal=Ann. Neurol. |volume=42 |issue= 6 |pages= 885-90 |year= 1998 |pmid= 9403481 |doi= 10.1002/ana.410420610 }}
*{{cite journal | author=Terwindt GM, Ophoff RA, Lindhout D, ''et al.'' |title=Partial cosegregation of familial hemiplegic migraine and a benign familial infantile epileptic syndrome. |journal=Epilepsia |volume=38 |issue= 8 |pages= 915-21 |year= 1998 |pmid= 9579893 |doi= }}
*{{cite journal | author=Nagase T, Ishikawa K, Suyama M, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=5 |issue= 5 |pages= 277-86 |year= 1999 |pmid= 9872452 |doi= }}
*{{cite journal | author=Katzmarzyk PT, Rankinen T, Pérusse L, ''et al.'' |title=Linkage and association of the sodium potassium-adenosine triphosphatase alpha2 and beta1 genes with respiratory quotient and resting metabolic rate in the Québec Family Study. |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 6 |pages= 2093-7 |year= 1999 |pmid= 10372716 |doi= }}
*{{cite journal | author=Rankinen T, Pérusse L, Borecki I, ''et al.'' |title=The Na(+)-K(+)-ATPase alpha2 gene and trainability of cardiorespiratory endurance: the HERITAGE family study. |journal=J. Appl. Physiol. |volume=88 |issue= 1 |pages= 346-51 |year= 2000 |pmid= 10642400 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Ukkola O, Joanisse DR, Tremblay A, Bouchard C |title=Na+-K+-ATPase alpha 2-gene and skeletal muscle characteristics in response to long-term overfeeding. |journal=J. Appl. Physiol. |volume=94 |issue= 5 |pages= 1870-4 |year= 2003 |pmid= 12496141 |doi= 10.1152/japplphysiol.00942.2002 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on C5AR1... {November 17, 2007 11:49:20 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:49:53 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Complement component 5a receptor 1
| HGNCid = 1338
| Symbol = C5AR1
| AltSymbols =; C5A; C5AR; C5R1; CD88
| OMIM = 113995
| ECnumber =
| Homologene = 20413
| MGIid = 88232
| GeneAtlas_image1 = PBB_GE_C5AR1_220088_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004944 |text = C5a anaphylatoxin receptor activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0000187 |text = activation of MAPK activity}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007202 |text = phospholipase C activation}} {{GNF_GO|id=GO:0007204 |text = elevation of cytosolic calcium ion concentration}} {{GNF_GO|id=GO:0007606 |text = sensory perception of chemical stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 728
| Hs_Ensembl = ENSG00000197405
| Hs_RefseqProtein = NP_001727
| Hs_RefseqmRNA = NM_001736
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 52504971
| Hs_GenLoc_end = 52517172
| Hs_Uniprot = P21730
| Mm_EntrezGene = 12273
| Mm_Ensembl = ENSMUSG00000049130
| Mm_RefseqmRNA = NM_007577
| Mm_RefseqProtein = NP_031603
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 15405265
| Mm_GenLoc_end = 15417773
| Mm_Uniprot = Q3TZ86
}}
}}
'''Complement component 5a receptor 1''', also known as '''C5AR1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: C5AR1 complement component 5a receptor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=728| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sengeløv H |title=Complement receptors in neutrophils. |journal=Crit. Rev. Immunol. |volume=15 |issue= 2 |pages= 107-31 |year= 1996 |pmid= 8573284 |doi= }}
*{{cite journal | author=Beil WJ, Schulz M, Wefelmeyer U |title=Mast cell granule composition and tissue location--a close correlation. |journal=Histol. Histopathol. |volume=15 |issue= 3 |pages= 937-46 |year= 2001 |pmid= 10963136 |doi= }}
*{{cite journal | author=Yamamoto T |title=Roles of the ribosomal protein S19 dimer and the C5a receptor in pathophysiological functions of phagocytic leukocytes. |journal=Pathol. Int. |volume=57 |issue= 1 |pages= 1-11 |year= 2007 |pmid= 17199736 |doi= 10.1111/j.1440-1827.2007.02049.x }}
*{{cite journal | author=Bao L, Gerard NP, Eddy RL, ''et al.'' |title=Mapping of genes for the human C5a receptor (C5AR), human FMLP receptor (FPR), and two FMLP receptor homologue orphan receptors (FPRH1, FPRH2) to chromosome 19. |journal=Genomics |volume=13 |issue= 2 |pages= 437-40 |year= 1992 |pmid= 1612600 |doi= }}
*{{cite journal | author=Gerard NP, Gerard C |title=The chemotactic receptor for human C5a anaphylatoxin. |journal=Nature |volume=349 |issue= 6310 |pages= 614-7 |year= 1991 |pmid= 1847994 |doi= 10.1038/349614a0 }}
*{{cite journal | author=Boulay F, Mery L, Tardif M, ''et al.'' |title=Expression cloning of a receptor for C5a anaphylatoxin on differentiated HL-60 cells. |journal=Biochemistry |volume=30 |issue= 12 |pages= 2993-9 |year= 1991 |pmid= 2007135 |doi= }}
*{{cite journal | author=Wahl SM, Allen JB, Gartner S, ''et al.'' |title=HIV-1 and its envelope glycoprotein down-regulate chemotactic ligand receptors and chemotactic function of peripheral blood monocytes. |journal=J. Immunol. |volume=142 |issue= 10 |pages= 3553-9 |year= 1989 |pmid= 2541200 |doi= }}
*{{cite journal | author=Foreman KE, Vaporciyan AA, Bonish BK, ''et al.'' |title=C5a-induced expression of P-selectin in endothelial cells. |journal=J. Clin. Invest. |volume=94 |issue= 3 |pages= 1147-55 |year= 1994 |pmid= 7521884 |doi= }}
*{{cite journal | author=Giannini E, Brouchon L, Boulay F |title=Identification of the major phosphorylation sites in human C5a anaphylatoxin receptor in vivo. |journal=J. Biol. Chem. |volume=270 |issue= 32 |pages= 19166-72 |year= 1995 |pmid= 7642584 |doi= }}
*{{cite journal | author=Buhl AM, Osawa S, Johnson GL |title=Mitogen-activated protein kinase activation requires two signal inputs from the human anaphylatoxin C5a receptor. |journal=J. Biol. Chem. |volume=270 |issue= 34 |pages= 19828-32 |year= 1995 |pmid= 7649993 |doi= }}
*{{cite journal | author=Wennogle LP, Conder L, Winter C, ''et al.'' |title=Stabilization of C5a receptor--G-protein interactions through ligand binding. |journal=J. Cell. Biochem. |volume=55 |issue= 3 |pages= 380-8 |year= 1994 |pmid= 7962171 |doi= 10.1002/jcb.240550316 }}
*{{cite journal | author=Gerard NP, Bao L, Xiao-Ping H, ''et al.'' |title=Human chemotaxis receptor genes cluster at 19q13.3-13.4. Characterization of the human C5a receptor gene. |journal=Biochemistry |volume=32 |issue= 5 |pages= 1243-50 |year= 1993 |pmid= 8383526 |doi= }}
*{{cite journal | author=Ames RS, Li Y, Sarau HM, ''et al.'' |title=Molecular cloning and characterization of the human anaphylatoxin C3a receptor. |journal=J. Biol. Chem. |volume=271 |issue= 34 |pages= 20231-4 |year= 1996 |pmid= 8702752 |doi= }}
*{{cite journal | author=Werfel T, Zwirner J, Oppermann M, ''et al.'' |title=CD88 antibodies specifically bind to C5aR on dermal CD117+ and CD14+ cells and react with a desmosomal antigen in human skin. |journal=J. Immunol. |volume=157 |issue= 4 |pages= 1729-35 |year= 1996 |pmid= 8759762 |doi= }}
*{{cite journal | author=Höpken UE, Lu B, Gerard NP, Gerard C |title=The C5a chemoattractant receptor mediates mucosal defence to infection. |journal=Nature |volume=383 |issue= 6595 |pages= 86-9 |year= 1996 |pmid= 8779720 |doi= 10.1038/383086a0 }}
*{{cite journal | author=Chen Z, Zhang X, Gonnella NC, ''et al.'' |title=Residues 21-30 within the extracellular N-terminal region of the C5a receptor represent a binding domain for the C5a anaphylatoxin. |journal=J. Biol. Chem. |volume=273 |issue= 17 |pages= 10411-9 |year= 1998 |pmid= 9553099 |doi= }}
*{{cite journal | author=Floreani AA, Heires AJ, Welniak LA, ''et al.'' |title=Expression of receptors for C5a anaphylatoxin (CD88) on human bronchial epithelial cells: enhancement of C5a-mediated release of IL-8 upon exposure to cigarette smoke. |journal=J. Immunol. |volume=160 |issue= 10 |pages= 5073-81 |year= 1998 |pmid= 9590258 |doi= }}
*{{cite journal | author=Ottonello L, Corcione A, Tortolina G, ''et al.'' |title=rC5a directs the in vitro migration of human memory and naive tonsillar B lymphocytes: implications for B cell trafficking in secondary lymphoid tissues. |journal=J. Immunol. |volume=162 |issue= 11 |pages= 6510-7 |year= 1999 |pmid= 10352266 |doi= }}
*{{cite journal | author=Kohleisen B, Shumay E, Sutter G, ''et al.'' |title=Stable expression of HIV-1 Nef induces changes in growth properties and activation state of human astrocytes. |journal=AIDS |volume=13 |issue= 17 |pages= 2331-41 |year= 2000 |pmid= 10597774 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CHRM1... {November 17, 2007 11:49:53 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:50:20 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cholinergic receptor, muscarinic 1
| HGNCid = 1950
| Symbol = CHRM1
| AltSymbols =; HM1; M1; MGC30125
| OMIM = 118510
| ECnumber =
| Homologene = 20189
| MGIid = 88396
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004435 |text = phosphoinositide phospholipase C activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004981 |text = muscarinic acetylcholine receptor activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0045211 |text = postsynaptic membrane}}
| Process = {{GNF_GO|id=GO:0006464 |text = protein modification process}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007205 |text = protein kinase C activation}} {{GNF_GO|id=GO:0007207 |text = muscarinic acetylcholine receptor, phospholipase C activating pathway}} {{GNF_GO|id=GO:0007213 |text = acetylcholine receptor signaling, muscarinic pathway}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0040012 |text = regulation of locomotion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1128
| Hs_Ensembl = ENSG00000168539
| Hs_RefseqProtein = NP_000729
| Hs_RefseqmRNA = NM_000738
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 62432728
| Hs_GenLoc_end = 62445588
| Hs_Uniprot = P11229
| Mm_EntrezGene = 12669
| Mm_Ensembl = ENSMUSG00000032773
| Mm_RefseqmRNA = NM_007698
| Mm_RefseqProtein = NP_031724
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 8731396
| Mm_GenLoc_end = 8748612
| Mm_Uniprot = Q52KQ0
}}
}}
'''Cholinergic receptor, muscarinic 1''', also known as '''CHRM1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CHRM1 cholinergic receptor, muscarinic 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1128| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The muscarinic cholinergic receptors belong to a larger family of G protein-coupled receptors. The functional diversity of these receptors is defined by the binding of acetylcholine and includes cellular responses such as adenylate cyclase inhibition, phosphoinositide degeneration, and potassium channel mediation. Muscarinic receptors influence many effects of acetylcholine in the central and peripheral nervous system. The muscarinic cholinergic receptor 1 is involved in mediation of vagally-induced bronchoconstriction and in the acid secretion of the gastrointestinal tract. The gene encoding this receptor is localized to 11q13.<ref name="entrez">{{cite web | title = Entrez Gene: CHRM1 cholinergic receptor, muscarinic 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1128| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Goyal RK |title=Muscarinic receptor subtypes. Physiology and clinical implications. |journal=N. Engl. J. Med. |volume=321 |issue= 15 |pages= 1022-9 |year= 1989 |pmid= 2674717 |doi= }}
*{{cite journal | author=Brann MR, Ellis J, Jørgensen H, ''et al.'' |title=Muscarinic acetylcholine receptor subtypes: localization and structure/function. |journal=Prog. Brain Res. |volume=98 |issue= |pages= 121-7 |year= 1994 |pmid= 8248499 |doi= }}
*{{cite journal | author=Nitsch RM, Slack BE, Wurtman RJ, Growdon JH |title=Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors. |journal=Science |volume=258 |issue= 5080 |pages= 304-7 |year= 1992 |pmid= 1411529 |doi= }}
*{{cite journal | author=Arden JR, Nagata O, Shockley MS, ''et al.'' |title=Mutational analysis of third cytoplasmic loop domains in G-protein coupling of the HM1 muscarinic receptor. |journal=Biochem. Biophys. Res. Commun. |volume=188 |issue= 3 |pages= 1111-5 |year= 1992 |pmid= 1445347 |doi= }}
*{{cite journal | author=Gutkind JS, Novotny EA, Brann MR, Robbins KC |title=Muscarinic acetylcholine receptor subtypes as agonist-dependent oncogenes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 11 |pages= 4703-7 |year= 1991 |pmid= 1905013 |doi= }}
*{{cite journal | author=Chapman CG, Browne MJ |title=Isolation of the human ml (Hml) muscarinic acetylcholine receptor gene by PCR amplification. |journal=Nucleic Acids Res. |volume=18 |issue= 8 |pages= 2191 |year= 1990 |pmid= 2336407 |doi= }}
*{{cite journal | author=Ashkenazi A, Ramachandran J, Capon DJ |title=Acetylcholine analogue stimulates DNA synthesis in brain-derived cells via specific muscarinic receptor subtypes. |journal=Nature |volume=340 |issue= 6229 |pages= 146-50 |year= 1989 |pmid= 2739737 |doi= 10.1038/340146a0 }}
*{{cite journal | author=Bonner TI, Buckley NJ, Young AC, Brann MR |title=Identification of a family of muscarinic acetylcholine receptor genes. |journal=Science |volume=237 |issue= 4814 |pages= 527-32 |year= 1987 |pmid= 3037705 |doi= }}
*{{cite journal | author=Peralta EG, Ashkenazi A, Winslow JW, ''et al.'' |title=Distinct primary structures, ligand-binding properties and tissue-specific expression of four human muscarinic acetylcholine receptors. |journal=EMBO J. |volume=6 |issue= 13 |pages= 3923-9 |year= 1988 |pmid= 3443095 |doi= }}
*{{cite journal | author=Allard WJ, Sigal IS, Dixon RA |title=Sequence of the gene encoding the human M1 muscarinic acetylcholine receptor. |journal=Nucleic Acids Res. |volume=15 |issue= 24 |pages= 10604 |year= 1988 |pmid= 3697105 |doi= }}
*{{cite journal | author=Svoboda P, Milligan G |title=Agonist-induced transfer of the alpha subunits of the guanine-nucleotide-binding regulatory proteins Gq and G11 and of muscarinic m1 acetylcholine receptors from plasma membranes to a light-vesicular membrane fraction. |journal=Eur. J. Biochem. |volume=224 |issue= 2 |pages= 455-62 |year= 1994 |pmid= 7925360 |doi= }}
*{{cite journal | author=Crespo P, Xu N, Daniotti JL, ''et al.'' |title=Signaling through transforming G protein-coupled receptors in NIH 3T3 cells involves c-Raf activation. Evidence for a protein kinase C-independent pathway. |journal=J. Biol. Chem. |volume=269 |issue= 33 |pages= 21103-9 |year= 1994 |pmid= 8063729 |doi= }}
*{{cite journal | author=Russell M, Winitz S, Johnson GL |title=Acetylcholine muscarinic m1 receptor regulation of cyclic AMP synthesis controls growth factor stimulation of Raf activity. |journal=Mol. Cell. Biol. |volume=14 |issue= 4 |pages= 2343-51 |year= 1994 |pmid= 8139539 |doi= }}
*{{cite journal | author=Offermanns S, Wieland T, Homann D, ''et al.'' |title=Transfected muscarinic acetylcholine receptors selectively couple to Gi-type G proteins and Gq/11. |journal=Mol. Pharmacol. |volume=45 |issue= 5 |pages= 890-8 |year= 1994 |pmid= 8190105 |doi= }}
*{{cite journal | author=Mullaney I, Mitchell FM, McCallum JF, ''et al.'' |title=The human muscarinic M1 acetylcholine receptor, when express in CHO cells, activates and downregulates both Gq alpha and G11 alpha equally and non-selectively. |journal=FEBS Lett. |volume=324 |issue= 2 |pages= 241-5 |year= 1993 |pmid= 8508928 |doi= }}
*{{cite journal | author=Courseaux A, Grosgeorge J, Gaudray P, ''et al.'' |title=Definition of the minimal MEN1 candidate area based on a 5-Mb integrated map of proximal 11q13. The European Consortium on Men1, (GENEM 1; Groupe d'Etude des Néoplasies Endocriniennes Multiples de type 1). |journal=Genomics |volume=37 |issue= 3 |pages= 354-65 |year= 1997 |pmid= 8938448 |doi= }}
*{{cite journal | author=Ishiyama A, López I, Wackym PA |title=Molecular characterization of muscarinic receptors in the human vestibular periphery. Implications for pharmacotherapy. |journal=The American journal of otology |volume=18 |issue= 5 |pages= 648-54 |year= 1998 |pmid= 9303164 |doi= }}
*{{cite journal | author=Ishizaka N, Noda M, Yokoyama S, ''et al.'' |title=Muscarinic acetylcholine receptor subtypes in the human iris. |journal=Brain Res. |volume=787 |issue= 2 |pages= 344-7 |year= 1998 |pmid= 9518684 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DAG1... {November 17, 2007 11:50:53 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:51:25 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_DAG1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1u2c.
| PDB = {{PDB2|1u2c}}
| Name = Dystroglycan 1 (dystrophin-associated glycoprotein 1)
| HGNCid = 2666
| Symbol = DAG1
| AltSymbols =; 156DAG; A3a; AGRNR; DAG
| OMIM = 128239
| ECnumber =
| Homologene = 3234
| MGIid = 101864
| GeneAtlas_image1 = PBB_GE_DAG1_205417_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DAG1_212128_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005055 |text = laminin receptor activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005626 |text = insoluble fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}} {{GNF_GO|id=GO:0016011 |text = dystroglycan complex}}
| Process = {{GNF_GO|id=GO:0002011 |text = morphogenesis of an epithelial sheet}} {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0006936 |text = muscle contraction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1605
| Hs_Ensembl = ENSG00000173402
| Hs_RefseqProtein = NP_004384
| Hs_RefseqmRNA = NM_004393
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 49482595
| Hs_GenLoc_end = 49548048
| Hs_Uniprot = Q14118
| Mm_EntrezGene = 13138
| Mm_Ensembl = ENSMUSG00000039952
| Mm_RefseqmRNA = NM_010017
| Mm_RefseqProtein = NP_034147
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 108064056
| Mm_GenLoc_end = 108122025
| Mm_Uniprot = Q544G5
}}
}}
'''Dystroglycan 1 (dystrophin-associated glycoprotein 1)''', also known as '''DAG1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DAG1 dystroglycan 1 (dystrophin-associated glycoprotein 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1605| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Dystroglycan is a laminin binding component of the dystrophin-glycoprotein complex which provides a linkage between the subsarcolemmal cytoskeleton and the extracellular matrix. Dystroglycan 1 is a candidate gene for the site of the mutation in autosomal recessive muscular dystrophies. The dramatic reduction of dystroglycan 1 in Duchenne muscular dystrophy leads to a loss of linkage between the sarcolemma and extracellular matrix, rendering muscle fibers more susceptible to necrosis. Dystroglycan also functions as dual receptor for agrin and laminin-2 in the Schwann cell membrane. The muscle and nonmuscle isoforms of dystroglycan differ by carbohydrate moieties but not protein sequence.<ref name="entrez">{{cite web | title = Entrez Gene: DAG1 dystroglycan 1 (dystrophin-associated glycoprotein 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1605| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Matsumura K, Tomé FM, Collin H, ''et al.'' |title=Deficiency of the 50K dystrophin-associated glycoprotein in severe childhood autosomal recessive muscular dystrophy. |journal=Nature |volume=359 |issue= 6393 |pages= 320-2 |year= 1992 |pmid= 1406935 |doi= 10.1038/359320a0 }}
*{{cite journal | author=Ibraghimov-Beskrovnaya O, Ervasti JM, Leveille CJ, ''et al.'' |title=Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix. |journal=Nature |volume=355 |issue= 6362 |pages= 696-702 |year= 1992 |pmid= 1741056 |doi= 10.1038/355696a0 }}
*{{cite journal | author=Apel ED, Roberds SL, Campbell KP, Merlie JP |title=Rapsyn may function as a link between the acetylcholine receptor and the agrin-binding dystrophin-associated glycoprotein complex. |journal=Neuron |volume=15 |issue= 1 |pages= 115-26 |year= 1995 |pmid= 7619516 |doi= }}
*{{cite journal | author=Yang B, Jung D, Motto D, ''et al.'' |title=SH3 domain-mediated interaction of dystroglycan and Grb2. |journal=J. Biol. Chem. |volume=270 |issue= 20 |pages= 11711-4 |year= 1995 |pmid= 7744812 |doi= }}
*{{cite journal | author=Skynner MJ, Gangadharan U, Coulton GR, ''et al.'' |title=Genetic mapping of the mouse neuromuscular mutation kyphoscoliosis. |journal=Genomics |volume=25 |issue= 1 |pages= 207-13 |year= 1995 |pmid= 7774920 |doi= }}
*{{cite journal | author=Yamada H, Shimizu T, Tanaka T, ''et al.'' |title=Dystroglycan is a binding protein of laminin and merosin in peripheral nerve. |journal=FEBS Lett. |volume=352 |issue= 1 |pages= 49-53 |year= 1994 |pmid= 7925941 |doi= }}
*{{cite journal | author=Gee SH, Montanaro F, Lindenbaum MH, Carbonetto S |title=Dystroglycan-alpha, a dystrophin-associated glycoprotein, is a functional agrin receptor. |journal=Cell |volume=77 |issue= 5 |pages= 675-86 |year= 1994 |pmid= 8205617 |doi= }}
*{{cite journal | author=Ibraghimov-Beskrovnaya O, Milatovich A, Ozcelik T, ''et al.'' |title=Human dystroglycan: skeletal muscle cDNA, genomic structure, origin of tissue specific isoforms and chromosomal localization. |journal=Hum. Mol. Genet. |volume=2 |issue= 10 |pages= 1651-7 |year= 1994 |pmid= 8268918 |doi= }}
*{{cite journal | author=Yamada H, Denzer AJ, Hori H, ''et al.'' |title=Dystroglycan is a dual receptor for agrin and laminin-2 in Schwann cell membrane. |journal=J. Biol. Chem. |volume=271 |issue= 38 |pages= 23418-23 |year= 1996 |pmid= 8798547 |doi= }}
*{{cite journal | author=Tian M, Jacobson C, Gee SH, ''et al.'' |title=Dystroglycan in the cerebellum is a laminin alpha 2-chain binding protein at the glial-vascular interface and is expressed in Purkinje cells. |journal=Eur. J. Neurosci. |volume=8 |issue= 12 |pages= 2739-47 |year= 1997 |pmid= 8996823 |doi= }}
*{{cite journal | author=Matsumura K, Chiba A, Yamada H, ''et al.'' |title=A role of dystroglycan in schwannoma cell adhesion to laminin. |journal=J. Biol. Chem. |volume=272 |issue= 21 |pages= 13904-10 |year= 1997 |pmid= 9153251 |doi= }}
*{{cite journal | author=Pirozzi G, McConnell SJ, Uveges AJ, ''et al.'' |title=Identification of novel human WW domain-containing proteins by cloning of ligand targets. |journal=J. Biol. Chem. |volume=272 |issue= 23 |pages= 14611-6 |year= 1997 |pmid= 9169421 |doi= }}
*{{cite journal | author=Gesemann M, Brancaccio A, Schumacher B, Ruegg MA |title=Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue. |journal=J. Biol. Chem. |volume=273 |issue= 1 |pages= 600-5 |year= 1998 |pmid= 9417121 |doi= }}
*{{cite journal | author=Rambukkana A, Yamada H, Zanazzi G, ''et al.'' |title=Role of alpha-dystroglycan as a Schwann cell receptor for Mycobacterium leprae. |journal=Science |volume=282 |issue= 5396 |pages= 2076-9 |year= 1998 |pmid= 9851927 |doi= }}
*{{cite journal | author=Cao W, Henry MD, Borrow P, ''et al.'' |title=Identification of alpha-dystroglycan as a receptor for lymphocytic choriomeningitis virus and Lassa fever virus. |journal=Science |volume=282 |issue= 5396 |pages= 2079-81 |year= 1998 |pmid= 9851928 |doi= }}
*{{cite journal | author=Shimizu H, Hosokawa H, Ninomiya H, ''et al.'' |title=Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan. |journal=J. Biol. Chem. |volume=274 |issue= 17 |pages= 11995-2000 |year= 1999 |pmid= 10207021 |doi= }}
*{{cite journal | author=Rentschler S, Linn H, Deininger K, ''et al.'' |title=The WW domain of dystrophin requires EF-hands region to interact with beta-dystroglycan. |journal=Biol. Chem. |volume=380 |issue= 4 |pages= 431-42 |year= 1999 |pmid= 10355629 |doi= }}
*{{cite journal | author=Tommasi di Vignano A, Di Zenzo G, Sudol M, ''et al.'' |title=Contribution of the different modules in the utrophin carboxy-terminal region to the formation and regulation of the DAP complex. |journal=FEBS Lett. |volume=471 |issue= 2-3 |pages= 229-34 |year= 2000 |pmid= 10767429 |doi= }}
*{{cite journal | author=James M, Nuttall A, Ilsley JL, ''et al.'' |title=Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin. |journal=J. Cell. Sci. |volume=113 ( Pt 10) |issue= |pages= 1717-26 |year= 2000 |pmid= 10769203 |doi= }}
*{{cite journal | author=Russo K, Di Stasio E, Macchia G, ''et al.'' |title=Characterization of the beta-dystroglycan-growth factor receptor 2 (Grb2) interaction. |journal=Biochem. Biophys. Res. Commun. |volume=274 |issue= 1 |pages= 93-8 |year= 2000 |pmid= 10903901 |doi= 10.1006/bbrc.2000.3103 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DBH... {November 17, 2007 11:51:25 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:51:47 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Dopamine beta-hydroxylase (dopamine beta-monooxygenase)
| HGNCid = 2689
| Symbol = DBH
| AltSymbols =; DBM
| OMIM = 609312
| ECnumber =
| Homologene = 615
| MGIid = 94864
| GeneAtlas_image1 = PBB_GE_DBH_206450_at_tn.png
| Function = {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0004500 |text = dopamine beta-monooxygenase activity}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0031418 |text = L-ascorbic acid binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0042583 |text = chromaffin granule}}
| Process = {{GNF_GO|id=GO:0001816 |text = cytokine production}} {{GNF_GO|id=GO:0001974 |text = blood vessel remodeling}} {{GNF_GO|id=GO:0001975 |text = response to amphetamine}} {{GNF_GO|id=GO:0002443 |text = leukocyte mediated immunity}} {{GNF_GO|id=GO:0006548 |text = histidine catabolic process}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007613 |text = memory}} {{GNF_GO|id=GO:0007626 |text = locomotory behavior}} {{GNF_GO|id=GO:0008306 |text = associative learning}} {{GNF_GO|id=GO:0008542 |text = visual learning}} {{GNF_GO|id=GO:0042127 |text = regulation of cell proliferation}} {{GNF_GO|id=GO:0042309 |text = homoiothermy}} {{GNF_GO|id=GO:0042420 |text = dopamine catabolic process}} {{GNF_GO|id=GO:0042421 |text = norepinephrine biosynthetic process}} {{GNF_GO|id=GO:0042593 |text = glucose homeostasis}} {{GNF_GO|id=GO:0042596 |text = fear response}} {{GNF_GO|id=GO:0042711 |text = maternal behavior}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0045907 |text = positive regulation of vasoconstriction}} {{GNF_GO|id=GO:0048149 |text = behavioral response to ethanol}} {{GNF_GO|id=GO:0048265 |text = response to pain}} {{GNF_GO|id=GO:0050900 |text = leukocyte migration}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1621
| Hs_Ensembl = ENSG00000123454
| Hs_RefseqProtein = NP_000778
| Hs_RefseqmRNA = NM_000787
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 135491306
| Hs_GenLoc_end = 135514287
| Hs_Uniprot = P09172
| Mm_EntrezGene = 13166
| Mm_Ensembl = ENSMUSG00000000889
| Mm_RefseqmRNA = NM_138942
| Mm_RefseqProtein = NP_620392
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 26987242
| Mm_GenLoc_end = 27004928
| Mm_Uniprot = Q3V1U4
}}
}}
'''Dopamine beta-hydroxylase (dopamine beta-monooxygenase)''', also known as '''DBH''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DBH dopamine beta-hydroxylase (dopamine beta-monooxygenase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1621| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is an oxidoreductase belonging to the copper type II, ascorbate-dependent monooxygenase family. It is present in the synaptic vesicles of postganglionic sympathetic neurons and converts dopamine to norepinephrine. It exists in both soluble and membrane-bound forms, depending on the absence or presence, respectively, of a signal peptide.<ref name="entrez">{{cite web | title = Entrez Gene: DBH dopamine beta-hydroxylase (dopamine beta-monooxygenase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1621| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kopecková M, Paclt I, Goetz P |title=Polymorphisms and low plasma activity of dopamine-beta-hydroxylase in ADHD children. |journal=Neuro Endocrinol. Lett. |volume=27 |issue= 6 |pages= 748-54 |year= 2007 |pmid= 17187001 |doi= }}
*{{cite journal | author=Man in 't Veld AJ, Boomsma F, Moleman P, Schalekamp MA |title=Congenital dopamine-beta-hydroxylase deficiency. A novel orthostatic syndrome. |journal=Lancet |volume=1 |issue= 8526 |pages= 183-8 |year= 1987 |pmid= 2880016 |doi= }}
*{{cite journal | author=Kobayashi K, Kurosawa Y, Fujita K, Nagatsu T |title=Human dopamine beta-hydroxylase gene: two mRNA types having different 3'-terminal regions are produced through alternative polyadenylation. |journal=Nucleic Acids Res. |volume=17 |issue= 3 |pages= 1089-102 |year= 1989 |pmid= 2922261 |doi= }}
*{{cite journal | author=Craig SP, Buckle VJ, Lamouroux A, ''et al.'' |title=Localization of the human dopamine beta hydroxylase (DBH) gene to chromosome 9q34. |journal=Cytogenet. Cell Genet. |volume=48 |issue= 1 |pages= 48-50 |year= 1988 |pmid= 3180847 |doi= }}
*{{cite journal | author=Lamouroux A, Vigny A, Faucon Biguet N, ''et al.'' |title=The primary structure of human dopamine-beta-hydroxylase: insights into the relationship between the soluble and the membrane-bound forms of the enzyme. |journal=EMBO J. |volume=6 |issue= 13 |pages= 3931-7 |year= 1988 |pmid= 3443096 |doi= }}
*{{cite journal | author=Saxena A, Hensley P, Osborne JC, Fleming PJ |title=The pH-dependent subunit dissociation and catalytic activity of bovine dopamine beta-hydroxylase. |journal=J. Biol. Chem. |volume=260 |issue= 6 |pages= 3386-92 |year= 1985 |pmid= 3972830 |doi= }}
*{{cite journal | author=Houhou L, Lamouroux A, Biguet NF, Mallet J |title=Expression of human dopamine beta-hydroxylase in mammalian cells infected by recombinant vaccinia virus. Mechanisms for membrane attachment. |journal=J. Biol. Chem. |volume=270 |issue= 21 |pages= 12601-6 |year= 1995 |pmid= 7759508 |doi= }}
*{{cite journal | author=Robertson JG, Adams GW, Medzihradszky KF, ''et al.'' |title=Complete assignment of disulfide bonds in bovine dopamine beta-hydroxylase. |journal=Biochemistry |volume=33 |issue= 38 |pages= 11563-75 |year= 1994 |pmid= 7918370 |doi= }}
*{{cite journal | author=Li B, Tsing S, Kosaka AH, ''et al.'' |title=Expression of human dopamine beta-hydroxylase in Drosophila Schneider 2 cells. |journal=Biochem. J. |volume=313 ( Pt 1) |issue= |pages= 57-64 |year= 1996 |pmid= 8546710 |doi= }}
*{{cite journal | author=Dixon JS, Jen PY, Gosling JA |title=Immunohistochemical characteristics of human paraganglion cells and sensory corpuscles associated with the urinary bladder. A developmental study in the male fetus, neonate and infant. |journal=J. Anat. |volume=192 ( Pt 3) |issue= |pages= 407-15 |year= 1998 |pmid= 9688506 |doi= }}
*{{cite journal | author=Kim HS, Seo H, Yang C, ''et al.'' |title=Noradrenergic-specific transcription of the dopamine beta-hydroxylase gene requires synergy of multiple cis-acting elements including at least two Phox2a-binding sites. |journal=J. Neurosci. |volume=18 |issue= 20 |pages= 8247-60 |year= 1998 |pmid= 9763470 |doi= }}
*{{cite journal | author=Chen Z, Jia W, Kaufman PL, Cynader M |title=Immunohistochemical localization of dopamine-beta-hydroxylase in human and monkey eyes. |journal=Curr. Eye Res. |volume=18 |issue= 1 |pages= 39-48 |year= 1999 |pmid= 10075201 |doi= }}
*{{cite journal | author=Cargill M, Altshuler D, Ireland J, ''et al.'' |title=Characterization of single-nucleotide polymorphisms in coding regions of human genes. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 231-8 |year= 1999 |pmid= 10391209 |doi= 10.1038/10290 }}
*{{cite journal | author=Halushka MK, Fan JB, Bentley K, ''et al.'' |title=Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 239-47 |year= 1999 |pmid= 10391210 |doi= 10.1038/10297 }}
*{{cite journal | author=Williams HJ, Bray N, Murphy KC, ''et al.'' |title=No evidence for allelic association between schizophrenia and a functional variant of the human dopamine beta-hydroxylase gene (DBH). |journal=Am. J. Med. Genet. |volume=88 |issue= 5 |pages= 557-9 |year= 1999 |pmid= 10490716 |doi= }}
*{{cite journal | author=Gilbert JR, Kumar A, Newey S, ''et al.'' |title=Physical and cDNA mapping in the DBH region of human chromosome 9q34. |journal=Hum. Hered. |volume=50 |issue= 3 |pages= 151-7 |year= 2000 |pmid= 10686491 |doi= }}
*{{cite journal | author=Zhou X, Espey MG, Chen JX, ''et al.'' |title=Inhibitory effects of nitric oxide and nitrosative stress on dopamine-beta-hydroxylase. |journal=J. Biol. Chem. |volume=275 |issue= 28 |pages= 21241-6 |year= 2000 |pmid= 10887204 |doi= 10.1074/jbc.M904498199 }}
*{{cite journal | author=Zabetian CP, Anderson GM, Buxbaum SG, ''et al.'' |title=A quantitative-trait analysis of human plasma-dopamine beta-hydroxylase activity: evidence for a major functional polymorphism at the DBH locus. |journal=Am. J. Hum. Genet. |volume=68 |issue= 2 |pages= 515-22 |year= 2001 |pmid= 11170900 |doi= }}
*{{cite journal | author=Kim CH, Zabetian CP, Cubells JF, ''et al.'' |title=Mutations in the dopamine beta-hydroxylase gene are associated with human norepinephrine deficiency. |journal=Am. J. Med. Genet. |volume=108 |issue= 2 |pages= 140-7 |year= 2002 |pmid= 11857564 |doi= }}
*{{cite journal | author=Adachi M, Lewis EJ |title=The paired-like homeodomain protein, Arix, mediates protein kinase A-stimulated dopamine beta-hydroxylase gene transcription through its phosphorylation status. |journal=J. Biol. Chem. |volume=277 |issue= 25 |pages= 22915-24 |year= 2002 |pmid= 11943777 |doi= 10.1074/jbc.M201695200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GAL... {November 17, 2007 12:00:51 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:01:26 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Galanin
| HGNCid = 4114
| Symbol = GAL
| AltSymbols =; GALN; GLNN; MGC40167
| OMIM = 137035
| ECnumber =
| Homologene = 7724
| MGIid = 95637
| GeneAtlas_image1 = PBB_GE_GAL_214240_at_tn.png
| Function = {{GNF_GO|id=GO:0005184 |text = neuropeptide hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006939 |text = smooth muscle contraction}} {{GNF_GO|id=GO:0007218 |text = neuropeptide signaling pathway}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0030073 |text = insulin secretion}} {{GNF_GO|id=GO:0030252 |text = growth hormone secretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 51083
| Hs_Ensembl = ENSG00000069482
| Hs_RefseqProtein = NP_057057
| Hs_RefseqmRNA = NM_015973
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 68208602
| Hs_GenLoc_end = 68215218
| Hs_Uniprot = P22466
| Mm_EntrezGene = 14419
| Mm_Ensembl = ENSMUSG00000024907
| Mm_RefseqmRNA = NM_010253
| Mm_RefseqProtein = NP_034383
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 3410095
| Mm_GenLoc_end = 3414112
| Mm_Uniprot = Q3V002
}}
}}
'''Galanin''', also known as '''GAL''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GAL galanin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51083| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wynick D, Thompson SW, McMahon SB |title=The role of galanin as a multi-functional neuropeptide in the nervous system. |journal=Current opinion in pharmacology |volume=1 |issue= 1 |pages= 73-7 |year= 2002 |pmid= 11712539 |doi= }}
*{{cite journal | author=Vrontakis ME |title=Galanin: a biologically active peptide. |journal=Current drug targets. CNS and neurological disorders |volume=1 |issue= 6 |pages= 531-41 |year= 2003 |pmid= 12769595 |doi= }}
*{{cite journal | author=Mufson EJ, Counts SE, Perez SE, Binder L |title=Galanin plasticity in the cholinergic basal forebrain in Alzheimer's disease and transgenic mice. |journal=Neuropeptides |volume=39 |issue= 3 |pages= 233-7 |year= 2005 |pmid= 15893372 |doi= 10.1016/j.npep.2004.12.005 }}
*{{cite journal | author=Berger A, Santic R, Hauser-Kronberger C, ''et al.'' |title=Galanin and galanin receptors in human cancers. |journal=Neuropeptides |volume=39 |issue= 3 |pages= 353-9 |year= 2005 |pmid= 15944034 |doi= 10.1016/j.npep.2004.12.016 }}
*{{cite journal | author=Robinson JK, Bartfai T, Langel U |title=Galanin/GALP receptors and CNS homeostatic processes. |journal=CNS & neurological disorders drug targets |volume=5 |issue= 3 |pages= 327-34 |year= 2006 |pmid= 16787232 |doi= }}
*{{cite journal | author=McKnight GL, Karlsen AE, Kowalyk S, ''et al.'' |title=Sequence of human galanin and its inhibition of glucose-stimulated insulin secretion from RIN cells. |journal=Diabetes |volume=41 |issue= 1 |pages= 82-7 |year= 1992 |pmid= 1370155 |doi= }}
*{{cite journal | author=Gai WP, Geffen LB, Blessing WW |title=Galanin immunoreactive neurons in the human hypothalamus: colocalization with vasopressin-containing neurons. |journal=J. Comp. Neurol. |volume=298 |issue= 3 |pages= 265-80 |year= 1990 |pmid= 1698834 |doi= 10.1002/cne.902980302 }}
*{{cite journal | author=Burleigh DE, Furness JB |title=Distribution and actions of galanin and vasoactive intestinal peptide in the human colon. |journal=Neuropeptides |volume=16 |issue= 2 |pages= 77-82 |year= 1991 |pmid= 1701228 |doi= }}
*{{cite journal | author=Fried G, Meister B, Rådestad A |title=Peptide-containing nerves in the human pregnant uterine cervix: an immunohistochemical study exploring the effect of RU 486 (mifepristone). |journal=Hum. Reprod. |volume=5 |issue= 7 |pages= 870-6 |year= 1991 |pmid= 1702449 |doi= }}
*{{cite journal | author=Bersani M, Johnsen AH, Højrup P, ''et al.'' |title=Human galanin: primary structure and identification of two molecular forms. |journal=FEBS Lett. |volume=283 |issue= 2 |pages= 189-94 |year= 1991 |pmid= 1710578 |doi= }}
*{{cite journal | author=Hyde JF, Engle MG, Maley BE |title=Colocalization of galanin and prolactin within secretory granules of anterior pituitary cells in estrogen-treated Fischer 344 rats. |journal=Endocrinology |volume=129 |issue= 1 |pages= 270-6 |year= 1991 |pmid= 1711463 |doi= }}
*{{cite journal | author=Bennet WM, Hill SF, Ghatei MA, Bloom SR |title=Galanin in the normal human pituitary and brain and in pituitary adenomas. |journal=J. Endocrinol. |volume=130 |issue= 3 |pages= 463-7 |year= 1991 |pmid= 1719117 |doi= }}
*{{cite journal | author=Schmidt WE, Kratzin H, Eckart K, ''et al.'' |title=Isolation and primary structure of pituitary human galanin, a 30-residue nonamidated neuropeptide. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 24 |pages= 11435-9 |year= 1992 |pmid= 1722333 |doi= }}
*{{cite journal | author=Bauer FE, Christofides ND, Hacker GW, ''et al.'' |title=Distribution of galanin immunoreactivity in the genitourinary tract of man and rat. |journal=Peptides |volume=7 |issue= 1 |pages= 5-10 |year= 1986 |pmid= 2423990 |doi= }}
*{{cite journal | author=Bauer FE, Adrian TE, Christofides ND, ''et al.'' |title=Distribution and molecular heterogeneity of galanin in human, pig, guinea pig, and rat gastrointestinal tracts. |journal=Gastroenterology |volume=91 |issue= 4 |pages= 877-83 |year= 1986 |pmid= 2427385 |doi= }}
*{{cite journal | author=Tainio H, Vaalasti A, Rechardt L |title=The distribution of substance P-, CGRP-, galanin- and ANP-like immunoreactive nerves in human sweat glands. |journal=Histochem. J. |volume=19 |issue= 6-7 |pages= 375-80 |year= 1987 |pmid= 2444569 |doi= }}
*{{cite journal | author=Maggi CA, Santicioli P, Patacchini R, ''et al.'' |title=Galanin: a potent modulator of excitatory neurotransmission in the human urinary bladder. |journal=Eur. J. Pharmacol. |volume=143 |issue= 1 |pages= 135-7 |year= 1988 |pmid= 2446889 |doi= }}
*{{cite journal | author=Marti E, Gibson SJ, Polak JM, ''et al.'' |title=Ontogeny of peptide- and amine-containing neurones in motor, sensory, and autonomic regions of rat and human spinal cord, dorsal root ganglia, and rat skin. |journal=J. Comp. Neurol. |volume=266 |issue= 3 |pages= 332-59 |year= 1988 |pmid= 2447134 |doi= 10.1002/cne.902660304 }}
*{{cite journal | author=Beal MF, Clevens RA, Chattha GK, ''et al.'' |title=Galanin-like immunoreactivity is unchanged in Alzheimer's disease and Parkinson's disease dementia cerebral cortex. |journal=J. Neurochem. |volume=51 |issue= 6 |pages= 1935-41 |year= 1988 |pmid= 2460590 |doi= }}
*{{cite journal | author=Berrettini WH, Kaye WH, Sunderland T, ''et al.'' |title=Galanin immunoreactivity in human CSF: studies in eating disorders and Alzheimer's disease. |journal=Neuropsychobiology |volume=19 |issue= 2 |pages= 64-8 |year= 1989 |pmid= 2465504 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GDF15... {November 17, 2007 12:00:11 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:00:51 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Growth differentiation factor 15
| HGNCid = 30142
| Symbol = GDF15
| AltSymbols =; PDF; GDF-15; MIC-1; MIC1; NAG-1; PLAB; PTGFB
| OMIM = 605312
| ECnumber =
| Homologene = 3576
| MGIid = 1346047
| GeneAtlas_image1 = PBB_GE_GDF15_221577_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007179 |text = transforming growth factor beta receptor signaling pathway}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9518
| Hs_Ensembl = ENSG00000130513
| Hs_RefseqProtein = NP_004855
| Hs_RefseqmRNA = NM_004864
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 18357968
| Hs_GenLoc_end = 18360987
| Hs_Uniprot = Q99988
| Mm_EntrezGene = 23886
| Mm_Ensembl = ENSMUSG00000038508
| Mm_RefseqmRNA = NM_011819
| Mm_RefseqProtein = NP_035949
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 73558380
| Mm_GenLoc_end = 73561084
| Mm_Uniprot = Q3TU76
}}
}}
'''Growth differentiation factor 15''', also known as '''GDF15''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GDF15 growth differentiation factor 15| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9518| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Bone morphogenetic proteins (e.g., BMP5; MIM 112265) are members of the transforming growth factor-beta (see TGFB1; MIM 190180) superfamily and regulate tissue differentiation and maintenance. They are synthesized as precursor molecules that are processed at a dibasic cleavage site to release C-terminal domains containing a characteristic motif of 7 conserved cysteines in the mature protein.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: GDF15 growth differentiation factor 15| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9518| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Bootcov MR, Bauskin AR, Valenzuela SM, ''et al.'' |title=MIC-1, a novel macrophage inhibitory cytokine, is a divergent member of the TGF-beta superfamily. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 21 |pages= 11514-9 |year= 1997 |pmid= 9326641 |doi= }}
*{{cite journal | author=Yokoyama-Kobayashi M, Saeki M, Sekine S, Kato S |title=Human cDNA encoding a novel TGF-beta superfamily protein highly expressed in placenta. |journal=J. Biochem. |volume=122 |issue= 3 |pages= 622-6 |year= 1998 |pmid= 9348093 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Hromas R, Hufford M, Sutton J, ''et al.'' |title=PLAB, a novel placental bone morphogenetic protein. |journal=Biochim. Biophys. Acta |volume=1354 |issue= 1 |pages= 40-4 |year= 1997 |pmid= 9375789 |doi= }}
*{{cite journal | author=Lawton LN, Bonaldo MF, Jelenc PC, ''et al.'' |title=Identification of a novel member of the TGF-beta superfamily highly expressed in human placenta. |journal=Gene |volume=203 |issue= 1 |pages= 17-26 |year= 1998 |pmid= 9426002 |doi= }}
*{{cite journal | author=Paralkar VM, Vail AL, Grasser WA, ''et al.'' |title=Cloning and characterization of a novel member of the transforming growth factor-beta/bone morphogenetic protein family. |journal=J. Biol. Chem. |volume=273 |issue= 22 |pages= 13760-7 |year= 1998 |pmid= 9593718 |doi= }}
*{{cite journal | author=Böttner M, Laaff M, Schechinger B, ''et al.'' |title=Characterization of the rat, mouse, and human genes of growth/differentiation factor-15/macrophage inhibiting cytokine-1 (GDF-15/MIC-1). |journal=Gene |volume=237 |issue= 1 |pages= 105-11 |year= 1999 |pmid= 10524241 |doi= }}
*{{cite journal | author=Li PX, Wong J, Ayed A, ''et al.'' |title=Placental transforming growth factor-beta is a downstream mediator of the growth arrest and apoptotic response of tumor cells to DNA damage and p53 overexpression. |journal=J. Biol. Chem. |volume=275 |issue= 26 |pages= 20127-35 |year= 2000 |pmid= 10777512 |doi= 10.1074/jbc.M909580199 }}
*{{cite journal | author=Bauskin AR, Zhang HP, Fairlie WD, ''et al.'' |title=The propeptide of macrophage inhibitory cytokine (MIC-1), a TGF-beta superfamily member, acts as a quality control determinant for correctly folded MIC-1. |journal=EMBO J. |volume=19 |issue= 10 |pages= 2212-20 |year= 2000 |pmid= 10811612 |doi= 10.1093/emboj/19.10.2212 }}
*{{cite journal | author=Strelau J, Sullivan A, Böttner M, ''et al.'' |title=Growth/differentiation factor-15/macrophage inhibitory cytokine-1 is a novel trophic factor for midbrain dopaminergic neurons in vivo. |journal=J. Neurosci. |volume=20 |issue= 23 |pages= 8597-603 |year= 2001 |pmid= 11102463 |doi= }}
*{{cite journal | author=Moore AG, Brown DA, Fairlie WD, ''et al.'' |title=The transforming growth factor-ss superfamily cytokine macrophage inhibitory cytokine-1 is present in high concentrations in the serum of pregnant women. |journal=J. Clin. Endocrinol. Metab. |volume=85 |issue= 12 |pages= 4781-8 |year= 2001 |pmid= 11134143 |doi= }}
*{{cite journal | author=Fairlie WD, Russell PK, Wu WM, ''et al.'' |title=Epitope mapping of the transforming growth factor-beta superfamily protein, macrophage inhibitory cytokine-1 (MIC-1): identification of at least five distinct epitope specificities. |journal=Biochemistry |volume=40 |issue= 1 |pages= 65-73 |year= 2001 |pmid= 11141057 |doi= }}
*{{cite journal | author=Baek SJ, Kim KS, Nixon JB, ''et al.'' |title=Cyclooxygenase inhibitors regulate the expression of a TGF-beta superfamily member that has proapoptotic and antitumorigenic activities. |journal=Mol. Pharmacol. |volume=59 |issue= 4 |pages= 901-8 |year= 2001 |pmid= 11259636 |doi= }}
*{{cite journal | author=Fairlie WD, Zhang HP, Wu WM, ''et al.'' |title=The propeptide of the transforming growth factor-beta superfamily member, macrophage inhibitory cytokine-1 (MIC-1), is a multifunctional domain that can facilitate protein folding and secretion. |journal=J. Biol. Chem. |volume=276 |issue= 20 |pages= 16911-8 |year= 2001 |pmid= 11278594 |doi= 10.1074/jbc.M010000200 }}
*{{cite journal | author=Baek SJ, Horowitz JM, Eling TE |title=Molecular cloning and characterization of human nonsteroidal anti-inflammatory drug-activated gene promoter. Basal transcription is mediated by Sp1 and Sp3. |journal=J. Biol. Chem. |volume=276 |issue= 36 |pages= 33384-92 |year= 2001 |pmid= 11445565 |doi= 10.1074/jbc.M101814200 }}
*{{cite journal | author=Baek SJ, Wilson LC, Eling TE |title=Resveratrol enhances the expression of non-steroidal anti-inflammatory drug-activated gene (NAG-1) by increasing the expression of p53. |journal=Carcinogenesis |volume=23 |issue= 3 |pages= 425-34 |year= 2002 |pmid= 11895857 |doi= }}
*{{cite journal | author=Graichen R, Liu D, Sun Y, ''et al.'' |title=Autocrine human growth hormone inhibits placental transforming growth factor-beta gene transcription to prevent apoptosis and allow cell cycle progression of human mammary carcinoma cells. |journal=J. Biol. Chem. |volume=277 |issue= 29 |pages= 26662-72 |year= 2002 |pmid= 11994274 |doi= 10.1074/jbc.M109931200 }}
*{{cite journal | author=Wong J, Li PX, Klamut HJ |title=A novel p53 transcriptional repressor element (p53TRE) and the asymmetrical contribution of two p53 binding sites modulate the response of the placental transforming growth factor-beta promoter to p53. |journal=J. Biol. Chem. |volume=277 |issue= 29 |pages= 26699-707 |year= 2002 |pmid= 12011055 |doi= 10.1074/jbc.M203020200 }}
*{{cite journal | author=Albertoni M, Shaw PH, Nozaki M, ''et al.'' |title=Anoxia induces macrophage inhibitory cytokine-1 (MIC-1) in glioblastoma cells independently of p53 and HIF-1. |journal=Oncogene |volume=21 |issue= 27 |pages= 4212-9 |year= 2002 |pmid= 12082608 |doi= 10.1038/sj.onc.1205610 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LAMC2... {November 17, 2007 11:51:47 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:52:45 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Laminin, gamma 2
| HGNCid = 6493
| Symbol = LAMC2
| AltSymbols =; B2T; BM600; EBR2; EBR2A; LAMB2T; LAMNB2; MGC138491; MGC141938
| OMIM = 150292
| ECnumber =
| Homologene = 4062
| MGIid = 99913
| GeneAtlas_image1 = PBB_GE_LAMC2_202267_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008201 |text = heparin binding}}
| Component = {{GNF_GO|id=GO:0005604 |text = basement membrane}} {{GNF_GO|id=GO:0005610 |text = laminin-5 complex}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0008544 |text = epidermis development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3918
| Hs_Ensembl = ENSG00000058085
| Hs_RefseqProtein = NP_005553
| Hs_RefseqmRNA = NM_005562
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 181422022
| Hs_GenLoc_end = 181480662
| Hs_Uniprot = Q13753
| Mm_EntrezGene = 16782
| Mm_Ensembl = ENSMUSG00000026479
| Mm_RefseqmRNA = NM_008485
| Mm_RefseqProtein = NP_032511
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 154886248
| Mm_GenLoc_end = 154948205
| Mm_Uniprot = Q3UI29
}}
}}
'''Laminin, gamma 2''', also known as '''LAMC2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LAMC2 laminin, gamma 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3918| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the gamma chain isoform laminin, gamma 2. The gamma 2 chain, formerly thought to be a truncated version of beta chain (B2t), is highly homologous to the gamma 1 chain; however, it lacks domain VI, and domains V, IV and III are shorter. It is expressed in several fetal tissues but differently from gamma 1, and is specifically localized to epithelial cells in skin, lung and kidney. The gamma 2 chain together with alpha 3 and beta 3 chains constitute laminin 5 (earlier known as kalinin), which is an integral part of the anchoring filaments that connect epithelial cells to the underlying basement membrane. The epithelium-specific expression of the gamma 2 chain implied its role as an epithelium attachment molecule, and mutations in this gene have been associated with junctional epidermolysis bullosa, a skin disease characterized<ref name="entrez">{{cite web | title = Entrez Gene: LAMC2 laminin, gamma 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3918| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kallunki P, Sainio K, Eddy R, ''et al.'' |title=A truncated laminin chain homologous to the B2 chain: structure, spatial expression, and chromosomal assignment. |journal=J. Cell Biol. |volume=119 |issue= 3 |pages= 679-93 |year= 1992 |pmid= 1383240 |doi= }}
*{{cite journal | author=Baudoin C, Miquel C, Gagnoux-Palacios L, ''et al.'' |title=A novel homozygous nonsense mutation in the LAMC2 gene in patients with the Herlitz junctional epidermolysis bullosa. |journal=Hum. Mol. Genet. |volume=3 |issue= 10 |pages= 1909-10 |year= 1995 |pmid= 7849725 |doi= }}
*{{cite journal | author=Burgeson RE, Chiquet M, Deutzmann R, ''et al.'' |title=A new nomenclature for the laminins. |journal=Matrix Biol. |volume=14 |issue= 3 |pages= 209-11 |year= 1994 |pmid= 7921537 |doi= }}
*{{cite journal | author=Gedde-Dahl T, Dupuy BM, Jonassen R, ''et al.'' |title=Junctional epidermolysis bullosa inversa (locus EBR2A) assigned to 1q31 by linkage and association to LAMC1. |journal=Hum. Mol. Genet. |volume=3 |issue= 8 |pages= 1387-91 |year= 1995 |pmid= 7987320 |doi= }}
*{{cite journal | author=Pulkkinen L, Christiano AM, Airenne T, ''et al.'' |title=Mutations in the gamma 2 chain gene (LAMC2) of kalinin/laminin 5 in the junctional forms of epidermolysis bullosa. |journal=Nat. Genet. |volume=6 |issue= 3 |pages= 293-7 |year= 1994 |pmid= 8012393 |doi= 10.1038/ng0394-293 }}
*{{cite journal | author=Aberdam D, Galliano MF, Vailly J, ''et al.'' |title=Herlitz's junctional epidermolysis bullosa is linked to mutations in the gene (LAMC2) for the gamma 2 subunit of nicein/kalinin (LAMININ-5). |journal=Nat. Genet. |volume=6 |issue= 3 |pages= 299-304 |year= 1994 |pmid= 8012394 |doi= 10.1038/ng0394-299 }}
*{{cite journal | author=Miyazaki K, Kikkawa Y, Nakamura A, ''et al.'' |title=A large cell-adhesive scatter factor secreted by human gastric carcinoma cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 24 |pages= 11767-71 |year= 1994 |pmid= 8265624 |doi= }}
*{{cite journal | author=Vailly J, Verrando P, Champliaud MF, ''et al.'' |title=The 100-kDa chain of nicein/kalinin is a laminin B2 chain variant. |journal=Eur. J. Biochem. |volume=219 |issue= 1-2 |pages= 209-18 |year= 1994 |pmid= 8306988 |doi= }}
*{{cite journal | author=Airenne T, Haakana H, Sainio K, ''et al.'' |title=Structure of the human laminin gamma 2 chain gene (LAMC2): alternative splicing with different tissue distribution of two transcripts. |journal=Genomics |volume=32 |issue= 1 |pages= 54-64 |year= 1996 |pmid= 8786121 |doi= 10.1006/geno.1996.0076 }}
*{{cite journal | author=Mizushima H, Miyagi Y, Kikkawa Y, ''et al.'' |title=Differential expression of laminin-5/ladsin subunits in human tissues and cancer cell lines and their induction by tumor promoter and growth factors. |journal=J. Biochem. |volume=120 |issue= 6 |pages= 1196-202 |year= 1997 |pmid= 9010770 |doi= }}
*{{cite journal | author=Mizushima H, Koshikawa N, Moriyama K, ''et al.'' |title=Wide distribution of laminin-5 gamma 2 chain in basement membranes of various human tissues. |journal=Horm. Res. |volume=50 Suppl 2 |issue= |pages= 7-14 |year= 1998 |pmid= 9721586 |doi= }}
*{{cite journal | author=Chen M, Marinkovich MP, Jones JC, ''et al.'' |title=NC1 domain of type VII collagen binds to the beta3 chain of laminin 5 via a unique subdomain within the fibronectin-like repeats. |journal=J. Invest. Dermatol. |volume=112 |issue= 2 |pages= 177-83 |year= 1999 |pmid= 9989793 |doi= 10.1046/j.1523-1747.1999.00491.x }}
*{{cite journal | author=Miller KA, Chung J, Lo D, ''et al.'' |title=Inhibition of laminin-5 production in breast epithelial cells by overexpression of p300. |journal=J. Biol. Chem. |volume=275 |issue= 11 |pages= 8176-82 |year= 2000 |pmid= 10713141 |doi= }}
*{{cite journal | author=Olsen J, Lefebvre O, Fritsch C, ''et al.'' |title=Involvement of activator protein 1 complexes in the epithelium-specific activation of the laminin gamma2-chain gene promoter by hepatocyte growth factor (scatter factor). |journal=Biochem. J. |volume=347 |issue= Pt 2 |pages= 407-17 |year= 2001 |pmid= 10749670 |doi= }}
*{{cite journal | author=Hirosaki T, Mizushima H, Tsubota Y, ''et al.'' |title=Structural requirement of carboxyl-terminal globular domains of laminin alpha 3 chain for promotion of rapid cell adhesion and migration by laminin-5. |journal=J. Biol. Chem. |volume=275 |issue= 29 |pages= 22495-502 |year= 2000 |pmid= 10801807 |doi= 10.1074/jbc.M001326200 }}
*{{cite journal | author=Amano S, Scott IC, Takahara K, ''et al.'' |title=Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma 2 chain. |journal=J. Biol. Chem. |volume=275 |issue= 30 |pages= 22728-35 |year= 2000 |pmid= 10806203 |doi= 10.1074/jbc.M002345200 }}
*{{cite journal | author=Takizawa Y, Pulkkinen L, Chao SC, ''et al.'' |title=Mutation report: complete paternal uniparental isodisomy of chromosome 1: a novel mechanism for Herlitz junctional epidermolysis bullosa. |journal=J. Invest. Dermatol. |volume=115 |issue= 2 |pages= 307-11 |year= 2000 |pmid= 10951251 |doi= 10.1046/j.1523-1747.2000.00052.x }}
*{{cite journal | author=Manda R, Kohno T, Niki T, ''et al.'' |title=Differential expression of the LAMB3 and LAMC2 genes between small cell and non-small cell lung carcinomas. |journal=Biochem. Biophys. Res. Commun. |volume=275 |issue= 2 |pages= 440-5 |year= 2000 |pmid= 10964684 |doi= 10.1006/bbrc.2000.3331 }}
*{{cite journal | author=Spirito F, Chavanas S, Prost-Squarcioni C, ''et al.'' |title=Reduced expression of the epithelial adhesion ligand laminin 5 in the skin causes intradermal tissue separation. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 18828-35 |year= 2001 |pmid= 11279058 |doi= 10.1074/jbc.M100381200 }}
*{{cite journal | author=McArthur CP, Wang Y, Heruth D, Gustafson S |title=Amplification of extracellular matrix and oncogenes in tat-transfected human salivary gland cell lines with expression of laminin, fibronectin, collagens I, III, IV, c-myc and p53. |journal=Arch. Oral Biol. |volume=46 |issue= 6 |pages= 545-55 |year= 2001 |pmid= 11311202 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MDK... {November 17, 2007 11:52:46 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:53:16 AM PST}
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{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_MDK_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1mkc.
| PDB = {{PDB2|1mkc}}, {{PDB2|1mkn}}
| Name = Midkine (neurite growth-promoting factor 2)
| HGNCid = 6972
| Symbol = MDK
| AltSymbols =; MK; FLJ27379; NEGF2
| OMIM = 162096
| ECnumber =
| Homologene = 1792
| MGIid = 96949
| GeneAtlas_image1 = PBB_GE_MDK_209035_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0009611 |text = response to wounding}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0030325 |text = adrenal gland development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4192
| Hs_Ensembl = ENSG00000110492
| Hs_RefseqProtein = NP_001012333
| Hs_RefseqmRNA = NM_001012333
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 46359194
| Hs_GenLoc_end = 46361948
| Hs_Uniprot = P21741
| Mm_EntrezGene = 17242
| Mm_Ensembl = ENSMUSG00000027239
| Mm_RefseqmRNA = NM_001012335
| Mm_RefseqProtein = NP_001012335
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 91730660
| Mm_GenLoc_end = 91733121
| Mm_Uniprot = Q2LEK5
}}
}}
'''Midkine (neurite growth-promoting factor 2)''', also known as '''MDK''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MDK midkine (neurite growth-promoting factor 2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4192| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Uehara K, Matsubara S, Kadomatsu K, ''et al.'' |title=Genomic structure of human midkine (MK), a retinoic acid-responsive growth/differentiation factor. |journal=J. Biochem. |volume=111 |issue= 5 |pages= 563-7 |year= 1992 |pmid= 1639750 |doi= }}
*{{cite journal | author=Wujek JR, Haleem-Smith H, Yamada Y, ''et al.'' |title=Evidence that the B2 chain of laminin is responsible for the neurite outgrowth-promoting activity of astrocyte extracellular matrix. |journal=Brain Res. Dev. Brain Res. |volume=55 |issue= 2 |pages= 237-47 |year= 1991 |pmid= 1701366 |doi= }}
*{{cite journal | author=Kretschmer PJ, Fairhurst JL, Decker MM, ''et al.'' |title=Cloning, characterization and developmental regulation of two members of a novel human gene family of neurite outgrowth-promoting proteins. |journal=Growth Factors |volume=5 |issue= 2 |pages= 99-114 |year= 1992 |pmid= 1768439 |doi= }}
*{{cite journal | author=Shoyab M, McDonald VL, Dick K, ''et al.'' |title=Amphiregulin-associated protein: complete amino acid sequence of a protein produced by the 12-0-tetradecanoylphorbol-13-acetate-treated human breast adenocarcinoma cell line MCF-7. |journal=Biochem. Biophys. Res. Commun. |volume=179 |issue= 1 |pages= 572-8 |year= 1991 |pmid= 1883381 |doi= }}
*{{cite journal | author=Tsutsui J, Uehara K, Kadomatsu K, ''et al.'' |title=A new family of heparin-binding factors: strong conservation of midkine (MK) sequences between the human and the mouse. |journal=Biochem. Biophys. Res. Commun. |volume=176 |issue= 2 |pages= 792-7 |year= 1991 |pmid= 2025291 |doi= }}
*{{cite journal | author=O'Hara B, Jenkins NA, Gilbert DJ, ''et al.'' |title=Chromosomal assignment of the heparin-binding cytokine genes MDK and PTN in mouse and man. |journal=Cytogenet. Cell Genet. |volume=69 |issue= 1-2 |pages= 40-3 |year= 1995 |pmid= 7835084 |doi= }}
*{{cite journal | author=Kaname T, Kuwano A, Murano I, ''et al.'' |title=Midkine gene (MDK), a gene for prenatal differentiation and neuroregulation, maps to band 11p11.2 by fluorescence in situ hybridization. |journal=Genomics |volume=17 |issue= 2 |pages= 514-5 |year= 1993 |pmid= 8406506 |doi= 10.1006/geno.1993.1359 }}
*{{cite journal | author=Fairhurst JL, Kretschmer PJ, Kovacs E, ''et al.'' |title=Structure of the gene coding for the human retinoic acid-inducible factor, MK. |journal=DNA Cell Biol. |volume=12 |issue= 2 |pages= 139-47 |year= 1993 |pmid= 8471163 |doi= }}
*{{cite journal | author=Kojima T, Katsumi A, Yamazaki T, ''et al.'' |title=Human ryudocan from endothelium-like cells binds basic fibroblast growth factor, midkine, and tissue factor pathway inhibitor. |journal=J. Biol. Chem. |volume=271 |issue= 10 |pages= 5914-20 |year= 1996 |pmid= 8621465 |doi= }}
*{{cite journal | author=Mahoney SA, Perry M, Seddon A, ''et al.'' |title=Transglutaminase forms midkine homodimers in cerebellar neurons and modulates the neurite-outgrowth response. |journal=Biochem. Biophys. Res. Commun. |volume=224 |issue= 1 |pages= 147-52 |year= 1996 |pmid= 8694802 |doi= 10.1006/bbrc.1996.0998 }}
*{{cite journal | author=Nakanishi T, Kadomatsu K, Okamoto T, ''et al.'' |title=Expression of syndecan-1 and -3 during embryogenesis of the central nervous system in relation to binding with midkine. |journal=J. Biochem. |volume=121 |issue= 2 |pages= 197-205 |year= 1997 |pmid= 9089390 |doi= }}
*{{cite journal | author=Iwasaki W, Nagata K, Hatanaka H, ''et al.'' |title=Solution structure of midkine, a new heparin-binding growth factor. |journal=EMBO J. |volume=16 |issue= 23 |pages= 6936-46 |year= 1998 |pmid= 9384573 |doi= 10.1093/emboj/16.23.6936 }}
*{{cite journal | author=Ratovitski EA, Kotzbauer PT, Milbrandt J, ''et al.'' |title=Midkine induces tumor cell proliferation and binds to a high affinity signaling receptor associated with JAK tyrosine kinases. |journal=J. Biol. Chem. |volume=273 |issue= 6 |pages= 3654-60 |year= 1998 |pmid= 9452495 |doi= }}
*{{cite journal | author=Maeda N, Ichihara-Tanaka K, Kimura T, ''et al.'' |title=A receptor-like protein-tyrosine phosphatase PTPzeta/RPTPbeta binds a heparin-binding growth factor midkine. Involvement of arginine 78 of midkine in the high affinity binding to PTPzeta. |journal=J. Biol. Chem. |volume=274 |issue= 18 |pages= 12474-9 |year= 1999 |pmid= 10212223 |doi= }}
*{{cite journal | author=Meng K, Rodriguez-Peña A, Dimitrov T, ''et al.'' |title=Pleiotrophin signals increased tyrosine phosphorylation of beta beta-catenin through inactivation of the intrinsic catalytic activity of the receptor-type protein tyrosine phosphatase beta/zeta. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 6 |pages= 2603-8 |year= 2000 |pmid= 10706604 |doi= 10.1073/pnas.020487997 }}
*{{cite journal | author=Muramatsu H, Zou K, Sakaguchi N, ''et al.'' |title=LDL receptor-related protein as a component of the midkine receptor. |journal=Biochem. Biophys. Res. Commun. |volume=270 |issue= 3 |pages= 936-41 |year= 2000 |pmid= 10772929 |doi= 10.1006/bbrc.2000.2549 }}
*{{cite journal | author=Kato M, Maeta H, Kato S, ''et al.'' |title=Immunohistochemical and in situ hybridization analyses of midkine expression in thyroid papillary carcinoma. |journal=Mod. Pathol. |volume=13 |issue= 10 |pages= 1060-5 |year= 2001 |pmid= 11048798 |doi= 10.1038/modpathol.3880195 }}
*{{cite journal | author=Hayashi K, Kadomatsu K, Muramatsu T |title=Requirement of chondroitin sulfate/dermatan sulfate recognition in midkine-dependent migration of macrophages. |journal=Glycoconj. J. |volume=18 |issue= 5 |pages= 401-6 |year= 2002 |pmid= 11925507 |doi= }}
*{{cite journal | author=Sumi Y, Muramatsu H, Takei Y, ''et al.'' |title=Midkine, a heparin-binding growth factor, promotes growth and glycosaminoglycan synthesis of endothelial cells through its action on smooth muscle cells in an artificial blood vessel model. |journal=J. Cell. Sci. |volume=115 |issue= Pt 13 |pages= 2659-67 |year= 2002 |pmid= 12077357 |doi= }}
*{{cite journal | author=Stoica GE, Kuo A, Powers C, ''et al.'' |title=Midkine binds to anaplastic lymphoma kinase (ALK) and acts as a growth factor for different cell types. |journal=J. Biol. Chem. |volume=277 |issue= 39 |pages= 35990-8 |year= 2002 |pmid= 12122009 |doi= 10.1074/jbc.M205749200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MUC4... {November 17, 2007 11:53:16 AM PST}
- SEARCH REDIRECT: Control Box Found: MUC4 {November 17, 2007 11:53:39 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:53:42 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:53:42 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:53:42 AM PST}
- UPDATED: Updated protein page: MUC4 {November 17, 2007 11:53:48 AM PST}
- INFO: Beginning work on NCF2... {November 17, 2007 11:53:48 AM PST}
- SEARCH REDIRECT: Control Box Found: NCF2 {November 17, 2007 11:54:10 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:54:11 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:54:11 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:54:11 AM PST}
- UPDATED: Updated protein page: NCF2 {November 17, 2007 11:54:17 AM PST}
- INFO: Beginning work on PAX2... {November 17, 2007 11:54:17 AM PST}
- SEARCH REDIRECT: Control Box Found: PAX2 {November 17, 2007 11:54:47 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:54:49 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:54:49 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:54:49 AM PST}
- UPDATED: Updated protein page: PAX2 {November 17, 2007 11:54:58 AM PST}
- INFO: Beginning work on PMS2... {November 17, 2007 11:55:37 AM PST}
- SEARCH REDIRECT: Control Box Found: PMS2 {November 17, 2007 11:56:14 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:56:15 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:56:15 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:56:15 AM PST}
- UPDATED: Updated protein page: PMS2 {November 17, 2007 11:56:22 AM PST}
- INFO: Beginning work on POLA1... {November 17, 2007 11:56:22 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:56:44 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_POLA1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1k0p.
| PDB = {{PDB2|1k0p}}, {{PDB2|1k18}}, {{PDB2|1n5g}}
| Name = Polymerase (DNA directed), alpha 1
| HGNCid = 9173
| Symbol = POLA1
| AltSymbols =; DKFZp686K1672; POLA
| OMIM = 312040
| ECnumber =
| Homologene = 6802
| MGIid = 99660
| GeneAtlas_image1 = PBB_GE_POLA1_204835_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0003889 |text = alpha DNA polymerase activity}} {{GNF_GO|id=GO:0003896 |text = DNA primase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008408 |text = 3'-5' exonuclease activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0000785 |text = chromatin}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005635 |text = nuclear envelope}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}} {{GNF_GO|id=GO:0005658 |text = alpha DNA polymerase:primase complex}} {{GNF_GO|id=GO:0005730 |text = nucleolus}} {{GNF_GO|id=GO:0016363 |text = nuclear matrix}}
| Process = {{GNF_GO|id=GO:0000084 |text = S phase of mitotic cell cycle}} {{GNF_GO|id=GO:0000731 |text = DNA synthesis during DNA repair}} {{GNF_GO|id=GO:0006270 |text = DNA replication initiation}} {{GNF_GO|id=GO:0006272 |text = leading strand elongation}} {{GNF_GO|id=GO:0006273 |text = lagging strand elongation}} {{GNF_GO|id=GO:0006303 |text = double-strand break repair via nonhomologous end joining}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0009268 |text = response to pH}} {{GNF_GO|id=GO:0009615 |text = response to virus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5422
| Hs_Ensembl = ENSG00000101868
| Hs_RefseqProtein = NP_058633
| Hs_RefseqmRNA = NM_016937
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 24621957
| Hs_GenLoc_end = 24925024
| Hs_Uniprot = P09884
| Mm_EntrezGene = 18968
| Mm_Ensembl = ENSMUSG00000006678
| Mm_RefseqmRNA = NM_008892
| Mm_RefseqProtein = NP_032918
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 89557486
| Mm_GenLoc_end = 89884874
| Mm_Uniprot = Q8CAT7
}}
}}
'''Polymerase (DNA directed), alpha 1''', also known as '''POLA1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: POLA1 polymerase (DNA directed), alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5422| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Pollok S, Stoepel J, Bauerschmidt C, ''et al.'' |title=Regulation of eukaryotic DNA replication at the initiation step. |journal=Biochem. Soc. Trans. |volume=31 |issue= Pt 1 |pages= 266-9 |year= 2003 |pmid= 12546699 |doi= 10.1042/ }}
*{{cite journal | author=Fisher PA, Korn D |title=DNA polymerase-alpha. Purification and structural characterization of the near homogeneous enzyme from human KB cells. |journal=J. Biol. Chem. |volume=252 |issue= 18 |pages= 6528-35 |year= 1977 |pmid= 893425 |doi= }}
*{{cite journal | author=Dornreiter I, Erdile LF, Gilbert IU, ''et al.'' |title=Interaction of DNA polymerase alpha-primase with cellular replication protein A and SV40 T antigen. |journal=EMBO J. |volume=11 |issue= 2 |pages= 769-76 |year= 1992 |pmid= 1311258 |doi= }}
*{{cite journal | author=Coverley D, Kenny MK, Lane DP, Wood RD |title=A role for the human single-stranded DNA binding protein HSSB/RPA in an early stage of nucleotide excision repair. |journal=Nucleic Acids Res. |volume=20 |issue= 15 |pages= 3873-80 |year= 1992 |pmid= 1508673 |doi= }}
*{{cite journal | author=Popanda O, Thielmann HW |title=The function of DNA polymerases in DNA repair synthesis of ultraviolet-irradiated human fibroblasts. |journal=Biochim. Biophys. Acta |volume=1129 |issue= 2 |pages= 155-60 |year= 1992 |pmid= 1730053 |doi= }}
*{{cite journal | author=Collins KL, Kelly TJ |title=Effects of T antigen and replication protein A on the initiation of DNA synthesis by DNA polymerase alpha-primase. |journal=Mol. Cell. Biol. |volume=11 |issue= 4 |pages= 2108-15 |year= 1991 |pmid= 1848671 |doi= }}
*{{cite journal | author=Martelli AM, Cocco L, Manzoli FA |title=On the association of DNA polymerase alpha activity with the nuclear matrix in HeLa cells. |journal=Cell Biol. Int. Rep. |volume=15 |issue= 2 |pages= 131-40 |year= 1991 |pmid= 1903085 |doi= }}
*{{cite journal | author=Pearson BE, Nasheuer HP, Wang TS |title=Human DNA polymerase alpha gene: sequences controlling expression in cycling and serum-stimulated cells. |journal=Mol. Cell. Biol. |volume=11 |issue= 4 |pages= 2081-95 |year= 1991 |pmid= 2005899 |doi= }}
*{{cite journal | author=Matsumoto T, Eki T, Hurwitz J |title=Studies on the initiation and elongation reactions in the simian virus 40 DNA replication system. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 24 |pages= 9712-6 |year= 1991 |pmid= 2175912 |doi= }}
*{{cite journal | author=Hsi KL, Copeland WC, Wang TS |title=Human DNA polymerase alpha catalytic polypeptide binds ConA and RCA and contains a specific labile site in the N-terminus. |journal=Nucleic Acids Res. |volume=18 |issue= 21 |pages= 6231-7 |year= 1991 |pmid= 2243771 |doi= }}
*{{cite journal | author=Wang TS, Pearson BE, Suomalainen HA, ''et al.'' |title=Assignment of the gene for human DNA polymerase alpha to the X chromosome. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 16 |pages= 5270-4 |year= 1985 |pmid= 2410918 |doi= }}
*{{cite journal | author=Knorre DG, Lavrik OI, Nevinsky GA |title=Protein-nucleic acid interaction in reactions catalyzed with DNA polymerases. |journal=Biochimie |volume=70 |issue= 5 |pages= 655-61 |year= 1988 |pmid= 3139084 |doi= }}
*{{cite journal | author=Nishida C, Reinhard P, Linn S |title=DNA repair synthesis in human fibroblasts requires DNA polymerase delta. |journal=J. Biol. Chem. |volume=263 |issue= 1 |pages= 501-10 |year= 1988 |pmid= 3335506 |doi= }}
*{{cite journal | author=Wong SW, Wahl AF, Yuan PM, ''et al.'' |title=Human DNA polymerase alpha gene expression is cell proliferation dependent and its primary structure is similar to both prokaryotic and eukaryotic replicative DNA polymerases. |journal=EMBO J. |volume=7 |issue= 1 |pages= 37-47 |year= 1988 |pmid= 3359994 |doi= }}
*{{cite journal | author=Tsuda M, Masuyama M, Katsunuma T |title=Inhibition of human DNA polymerase alpha by alpha 1-antichymotrypsin. |journal=Cancer Res. |volume=46 |issue= 12 Pt 1 |pages= 6139-42 |year= 1986 |pmid= 3490907 |doi= }}
*{{cite journal | author=Jackson DA, Cook PR |title=Different populations of DNA polymerase alpha in HeLa cells. |journal=J. Mol. Biol. |volume=192 |issue= 1 |pages= 77-86 |year= 1987 |pmid= 3820307 |doi= }}
*{{cite journal | author=Miller MR, Seighman C, Ulrich RG |title=Inhibition of DNA replication and DNA polymerase alpha activity by monoclonal anti-(DNA polymerase alpha) immunoglobulin G and F(ab) fragments. |journal=Biochemistry |volume=24 |issue= 25 |pages= 7440-5 |year= 1986 |pmid= 4084590 |doi= }}
*{{cite journal | author=Bensch KG, Tanaka S, Hu SZ, ''et al.'' |title=Intracellular localization of human DNA polymerase alpha with monoclonal antibodies. |journal=J. Biol. Chem. |volume=257 |issue= 14 |pages= 8391-6 |year= 1982 |pmid= 7045121 |doi= }}
*{{cite journal | author=Tanaka S, Hu SZ, Wang TS, Korn D |title=Preparation and preliminary characterization of monoclonal antibodies against human DNA polymerase alpha. |journal=J. Biol. Chem. |volume=257 |issue= 14 |pages= 8386-90 |year= 1982 |pmid= 7085672 |doi= }}
*{{cite journal | author=Eckert KA, Kunkel TA |title=Fidelity of DNA synthesis catalyzed by human DNA polymerase alpha and HIV-1 reverse transcriptase: effect of reaction pH. |journal=Nucleic Acids Res. |volume=21 |issue= 22 |pages= 5212-20 |year= 1994 |pmid= 7504813 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on POU5F1... {November 17, 2007 11:56:44 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:57:26 AM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = POU domain, class 5, transcription factor 1
| HGNCid = 9221
| Symbol = POU5F1
| AltSymbols =; MGC22487; OCT3; OCT4; OTF3; OTF4
| OMIM = 164177
| ECnumber =
| Homologene = 8422
| MGIid = 101893
| GeneAtlas_image1 = PBB_GE_POU5F1_210265_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_POU5F1_208286_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_POU5F1_210905_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5460
| Hs_Ensembl = ENSG00000204531
| Hs_RefseqProtein = NP_002692
| Hs_RefseqmRNA = NM_002701
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 31240099
| Hs_GenLoc_end = 31246422
| Hs_Uniprot = Q01860
| Mm_EntrezGene = 18999
| Mm_Ensembl = ENSMUSG00000024406
| Mm_RefseqmRNA = NM_013633
| Mm_RefseqProtein = NP_038661
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 35114104
| Mm_GenLoc_end = 35118822
| Mm_Uniprot =
}}
}}
'''POU domain, class 5, transcription factor 1''', also known as '''POU5F1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: POU5F1 POU domain, class 5, transcription factor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5460| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Takeda J, Seino S, Bell GI |title=Human Oct3 gene family: cDNA sequences, alternative splicing, gene organization, chromosomal location, and expression at low levels in adult tissues. |journal=Nucleic Acids Res. |volume=20 |issue= 17 |pages= 4613-20 |year= 1992 |pmid= 1408763 |doi= }}
*{{cite journal | author=Schoorlemmer J, Kruijer W |title=Octamer-dependent regulation of the kFGF gene in embryonal carcinoma and embryonic stem cells. |journal=Mech. Dev. |volume=36 |issue= 1-2 |pages= 75-86 |year= 1992 |pmid= 1723621 |doi= }}
*{{cite journal | author=Wey E, Lyons GE, Schäfer BW |title=A human POU domain gene, mPOU, is expressed in developing brain and specific adult tissues. |journal=Eur. J. Biochem. |volume=220 |issue= 3 |pages= 753-62 |year= 1994 |pmid= 7908264 |doi= }}
*{{cite journal | author=Crouau-Roy B, Amadou C, Bouissou C, ''et al.'' |title=Localization of the OTF3 gene within the human MHC class I region by physical and meiotic mapping. |journal=Genomics |volume=21 |issue= 1 |pages= 241-3 |year= 1994 |pmid= 8088794 |doi= 10.1006/geno.1994.1249 }}
*{{cite journal | author=Guillaudeux T, Mattei MG, Depetris D, ''et al.'' |title=In situ hybridization localizes the human OTF3 to chromosome 6p21.3-->p22 and OTF3L to 12p13. |journal=Cytogenet. Cell Genet. |volume=63 |issue= 4 |pages= 212-4 |year= 1993 |pmid= 8500351 |doi= }}
*{{cite journal | author=Abdel-Rahman B, Fiddler M, Rappolee D, Pergament E |title=Expression of transcription regulating genes in human preimplantation embryos. |journal=Hum. Reprod. |volume=10 |issue= 10 |pages= 2787-92 |year= 1996 |pmid= 8567814 |doi= }}
*{{cite journal | author=Hillier LD, Lennon G, Becker M, ''et al.'' |title=Generation and analysis of 280,000 human expressed sequence tags. |journal=Genome Res. |volume=6 |issue= 9 |pages= 807-28 |year= 1997 |pmid= 8889549 |doi= }}
*{{cite journal | author=Inamoto S, Segil N, Pan ZQ, ''et al.'' |title=The cyclin-dependent kinase-activating kinase (CAK) assembly factor, MAT1, targets and enhances CAK activity on the POU domains of octamer transcription factors. |journal=J. Biol. Chem. |volume=272 |issue= 47 |pages= 29852-8 |year= 1997 |pmid= 9368058 |doi= }}
*{{cite journal | author=Nichols J, Zevnik B, Anastassiadis K, ''et al.'' |title=Formation of pluripotent stem cells in the mammalian embryo depends on the POU transcription factor Oct4. |journal=Cell |volume=95 |issue= 3 |pages= 379-91 |year= 1998 |pmid= 9814708 |doi= }}
*{{cite journal | author=Gonzalez MI, Robins DM |title=Oct-1 preferentially interacts with androgen receptor in a DNA-dependent manner that facilitates recruitment of SRC-1. |journal=J. Biol. Chem. |volume=276 |issue= 9 |pages= 6420-8 |year= 2001 |pmid= 11096094 |doi= 10.1074/jbc.M008689200 }}
*{{cite journal | author=Butteroni C, De Felici M, Schöler HR, Pesce M |title=Phage display screening reveals an association between germline-specific transcription factor Oct-4 and multiple cellular proteins. |journal=J. Mol. Biol. |volume=304 |issue= 4 |pages= 529-40 |year= 2001 |pmid= 11099378 |doi= 10.1006/jmbi.2000.4238 }}
*{{cite journal | author=Ezashi T, Ghosh D, Roberts RM |title=Repression of Ets-2-induced transactivation of the tau interferon promoter by Oct-4. |journal=Mol. Cell. Biol. |volume=21 |issue= 23 |pages= 7883-91 |year= 2001 |pmid= 11689681 |doi= 10.1128/MCB.21.23.7883-7891.2001 }}
*{{cite journal | author=Guo Y, Costa R, Ramsey H, ''et al.'' |title=The embryonic stem cell transcription factors Oct-4 and FoxD3 interact to regulate endodermal-specific promoter expression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 6 |pages= 3663-7 |year= 2002 |pmid= 11891324 |doi= 10.1073/pnas.062041099 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Looijenga LH, Stoop H, de Leeuw HP, ''et al.'' |title=POU5F1 (OCT3/4) identifies cells with pluripotent potential in human germ cell tumors. |journal=Cancer Res. |volume=63 |issue= 9 |pages= 2244-50 |year= 2003 |pmid= 12727846 |doi= }}
*{{cite journal | author=Wang P, Branch DR, Bali M, ''et al.'' |title=The POU homeodomain protein OCT3 as a potential transcriptional activator for fibroblast growth factor-4 (FGF-4) in human breast cancer cells. |journal=Biochem. J. |volume=375 |issue= Pt 1 |pages= 199-205 |year= 2003 |pmid= 12841847 |doi= 10.1042/BJ20030579 }}
*{{cite journal | author=Reményi A, Lins K, Nissen LJ, ''et al.'' |title=Crystal structure of a POU/HMG/DNA ternary complex suggests differential assembly of Oct4 and Sox2 on two enhancers. |journal=Genes Dev. |volume=17 |issue= 16 |pages= 2048-59 |year= 2003 |pmid= 12923055 |doi= 10.1101/gad.269303 }}
*{{cite journal | author=Rajpert-De Meyts E, Hanstein R, Jørgensen N, ''et al.'' |title=Developmental expression of POU5F1 (OCT-3/4) in normal and dysgenetic human gonads. |journal=Hum. Reprod. |volume=19 |issue= 6 |pages= 1338-44 |year= 2004 |pmid= 15105401 |doi= 10.1093/humrep/deh265 }}
*{{cite journal | author=Matin MM, Walsh JR, Gokhale PJ, ''et al.'' |title=Specific knockdown of Oct4 and beta2-microglobulin expression by RNA interference in human embryonic stem cells and embryonic carcinoma cells. |journal=Stem Cells |volume=22 |issue= 5 |pages= 659-68 |year= 2005 |pmid= 15342930 |doi= 10.1634/stemcells.22-5-659 }}
*{{cite journal | author=Baal N, Reisinger K, Jahr H, ''et al.'' |title=Expression of transcription factor Oct-4 and other embryonic genes in CD133 positive cells from human umbilical cord blood. |journal=Thromb. Haemost. |volume=92 |issue= 4 |pages= 767-75 |year= 2005 |pmid= 15467907 |doi= 10.1267/THRO04040767 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PPP3CA... {November 17, 2007 11:57:26 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:58:08 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PPP3CA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aui.
| PDB = {{PDB2|1aui}}, {{PDB2|1m63}}, {{PDB2|1mf8}}, {{PDB2|1tco}}, {{PDB2|2jog}}, {{PDB2|2p6b}}
| Name = Protein phosphatase 3 (formerly 2B), catalytic subunit, alpha isoform
| HGNCid = 9314
| Symbol = PPP3CA
| AltSymbols =; CCN1; CNA1; CALN; CALNA; CALNA1; PPP2B
| OMIM = 114105
| ECnumber =
| Homologene = 55497
| MGIid = 107164
| GeneAtlas_image1 = PBB_GE_PPP3CA_202429_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PPP3CA_202425_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_PPP3CA_202457_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004722 |text = protein serine/threonine phosphatase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005955 |text = calcineurin complex}} {{GNF_GO|id=GO:0030018 |text = Z disc}}
| Process = {{GNF_GO|id=GO:0000082 |text = G1/S transition of mitotic cell cycle}} {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}} {{GNF_GO|id=GO:0006606 |text = protein import into nucleus}} {{GNF_GO|id=GO:0006816 |text = calcium ion transport}} {{GNF_GO|id=GO:0006950 |text = response to stress}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5530
| Hs_Ensembl = ENSG00000138814
| Hs_RefseqProtein = NP_000935
| Hs_RefseqmRNA = NM_000944
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 102163610
| Hs_GenLoc_end = 102487376
| Hs_Uniprot = Q08209
| Mm_EntrezGene = 19055
| Mm_Ensembl = ENSMUSG00000028161
| Mm_RefseqmRNA = NM_008913
| Mm_RefseqProtein = NP_032939
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 136608220
| Mm_GenLoc_end = 136874773
| Mm_Uniprot = P63328
}}
}}
'''Protein phosphatase 3 (formerly 2B), catalytic subunit, alpha isoform''', also known as '''PPP3CA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PPP3CA protein phosphatase 3 (formerly 2B), catalytic subunit, alpha isoform| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5530| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Crabtree GR |title=Generic signals and specific outcomes: signaling through Ca2+, calcineurin, and NF-AT. |journal=Cell |volume=96 |issue= 5 |pages= 611-4 |year= 1999 |pmid= 10089876 |doi= }}
*{{cite journal | author=Giri PR, Higuchi S, Kincaid RL |title=Chromosomal mapping of the human genes for the calmodulin-dependent protein phosphatase (calcineurin) catalytic subunit. |journal=Biochem. Biophys. Res. Commun. |volume=181 |issue= 1 |pages= 252-8 |year= 1992 |pmid= 1659808 |doi= }}
*{{cite journal | author=Kincaid RL, Giri PR, Higuchi S, ''et al.'' |title=Cloning and characterization of molecular isoforms of the catalytic subunit of calcineurin using nonisotopic methods. |journal=J. Biol. Chem. |volume=265 |issue= 19 |pages= 11312-9 |year= 1990 |pmid= 2162844 |doi= }}
*{{cite journal | author=Guerini D, Klee CB |title=Cloning of human calcineurin A: evidence for two isozymes and identification of a polyproline structural domain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 23 |pages= 9183-7 |year= 1990 |pmid= 2556704 |doi= }}
*{{cite journal | author=Kincaid RL, Nightingale MS, Martin BM |title=Characterization of a cDNA clone encoding the calmodulin-binding domain of mouse brain calcineurin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 23 |pages= 8983-7 |year= 1988 |pmid= 2848250 |doi= }}
*{{cite journal | author=Coghlan VM, Perrino BA, Howard M, ''et al.'' |title=Association of protein kinase A and protein phosphatase 2B with a common anchoring protein. |journal=Science |volume=267 |issue= 5194 |pages= 108-11 |year= 1995 |pmid= 7528941 |doi= }}
*{{cite journal | author=Griffith JP, Kim JL, Kim EE, ''et al.'' |title=X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex. |journal=Cell |volume=82 |issue= 3 |pages= 507-22 |year= 1995 |pmid= 7543369 |doi= }}
*{{cite journal | author=Shibasaki F, McKeon F |title=Calcineurin functions in Ca(2+)-activated cell death in mammalian cells. |journal=J. Cell Biol. |volume=131 |issue= 3 |pages= 735-43 |year= 1995 |pmid= 7593193 |doi= }}
*{{cite journal | author=Muramatsu T, Kincaid RL |title=Molecular cloning of a full-length cDNA encoding the catalytic subunit of human calmodulin-dependent protein phosphatase (calcineurin A alpha). |journal=Biochim. Biophys. Acta |volume=1178 |issue= 1 |pages= 117-20 |year= 1993 |pmid= 8392375 |doi= }}
*{{cite journal | author=Cameron AM, Steiner JP, Roskams AJ, ''et al.'' |title=Calcineurin associated with the inositol 1,4,5-trisphosphate receptor-FKBP12 complex modulates Ca2+ flux. |journal=Cell |volume=83 |issue= 3 |pages= 463-72 |year= 1996 |pmid= 8521476 |doi= }}
*{{cite journal | author=Kissinger CR, Parge HE, Knighton DR, ''et al.'' |title=Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. |journal=Nature |volume=378 |issue= 6557 |pages= 641-4 |year= 1996 |pmid= 8524402 |doi= 10.1038/378641a0 }}
*{{cite journal | author=Wang MG, Yi H, Guerini D, ''et al.'' |title=Calcineurin A alpha (PPP3CA), calcineurin A beta (PPP3CB) and calcineurin B (PPP3R1) are located on human chromosomes 4, 10q21-->q22 and 2p16-->p15 respectively. |journal=Cytogenet. Cell Genet. |volume=72 |issue= 2-3 |pages= 236-41 |year= 1997 |pmid= 8978785 |doi= }}
*{{cite journal | author=Shibasaki F, Kondo E, Akagi T, McKeon F |title=Suppression of signalling through transcription factor NF-AT by interactions between calcineurin and Bcl-2. |journal=Nature |volume=386 |issue= 6626 |pages= 728-31 |year= 1997 |pmid= 9109491 |doi= 10.1038/386728a0 }}
*{{cite journal | author=Kashishian A, Howard M, Loh C, ''et al.'' |title=AKAP79 inhibits calcineurin through a site distinct from the immunophilin-binding region. |journal=J. Biol. Chem. |volume=273 |issue= 42 |pages= 27412-9 |year= 1998 |pmid= 9765270 |doi= }}
*{{cite journal | author=Wang HG, Pathan N, Ethell IM, ''et al.'' |title=Ca2+-induced apoptosis through calcineurin dephosphorylation of BAD. |journal=Science |volume=284 |issue= 5412 |pages= 339-43 |year= 1999 |pmid= 10195903 |doi= }}
*{{cite journal | author=Fuentes JJ, Genescà L, Kingsbury TJ, ''et al.'' |title=DSCR1, overexpressed in Down syndrome, is an inhibitor of calcineurin-mediated signaling pathways. |journal=Hum. Mol. Genet. |volume=9 |issue= 11 |pages= 1681-90 |year= 2000 |pmid= 10861295 |doi= }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Frey N, Richardson JA, Olson EN |title=Calsarcins, a novel family of sarcomeric calcineurin-binding proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 26 |pages= 14632-7 |year= 2001 |pmid= 11114196 |doi= 10.1073/pnas.260501097 }}
*{{cite journal | author=Siddiq A, Miyazaki T, Takagishi Y, ''et al.'' |title=Expression of ZAKI-4 messenger ribonucleic acid in the brain during rat development and the effect of hypothyroidism. |journal=Endocrinology |volume=142 |issue= 5 |pages= 1752-9 |year= 2001 |pmid= 11316738 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSME1... {November 17, 2007 11:58:08 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:58:48 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PSME1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1avo.
| PDB = {{PDB2|1avo}}
| Name = Proteasome (prosome, macropain) activator subunit 1 (PA28 alpha)
| HGNCid = 9568
| Symbol = PSME1
| AltSymbols =; IFI5111; MGC8628; PA28A; PA28alpha; REGalpha
| OMIM = 600654
| ECnumber =
| Homologene = 4560
| MGIid = 1096367
| GeneAtlas_image1 = PBB_GE_PSME1_200814_at_tn.png
| Function = {{GNF_GO|id=GO:0008538 |text = proteasome activator activity}}
| Component = {{GNF_GO|id=GO:0000502 |text = proteasome complex (sensu Eukaryota)}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0008537 |text = proteasome activator complex}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5720
| Hs_Ensembl = ENSG00000092010
| Hs_RefseqProtein = NP_006254
| Hs_RefseqmRNA = NM_006263
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 23661207
| Hs_GenLoc_end = 23678015
| Hs_Uniprot = Q06323
| Mm_EntrezGene = 19186
| Mm_Ensembl = ENSMUSG00000022216
| Mm_RefseqmRNA = NM_011189
| Mm_RefseqProtein = NP_035319
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 54532646
| Mm_GenLoc_end = 54535608
| Mm_Uniprot = Q5HZK3
}}
}}
'''Proteasome (prosome, macropain) activator subunit 1 (PA28 alpha)''', also known as '''PSME1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSME1 proteasome (prosome, macropain) activator subunit 1 (PA28 alpha)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5720| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the alpha subunit of the 11S regulator, one of the two 11S subunits that is induced by gamma-interferon. Three alpha and three beta subunits combine to form a heterohexameric ring. Two transcripts encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: PSME1 proteasome (prosome, macropain) activator subunit 1 (PA28 alpha)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5720| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Coux O, Tanaka K, Goldberg AL |title=Structure and functions of the 20S and 26S proteasomes. |journal=Annu. Rev. Biochem. |volume=65 |issue= |pages= 801-47 |year= 1996 |pmid= 8811196 |doi= 10.1146/annurev.bi.65.070196.004101 }}
*{{cite journal | author=Sijts A, Sun Y, Janek K, ''et al.'' |title=The role of the proteasome activator PA28 in MHC class I antigen processing. |journal=Mol. Immunol. |volume=39 |issue= 3-4 |pages= 165-9 |year= 2002 |pmid= 12200048 |doi= }}
*{{cite journal | author=Goff SP |title=Death by deamination: a novel host restriction system for HIV-1. |journal=Cell |volume=114 |issue= 3 |pages= 281-3 |year= 2003 |pmid= 12914693 |doi= }}
*{{cite journal | author=Rasmussen HH, van Damme J, Puype M, ''et al.'' |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960-9 |year= 1993 |pmid= 1286667 |doi= }}
*{{cite journal | author=Ahn JY, Tanahashi N, Akiyama K, ''et al.'' |title=Primary structures of two homologous subunits of PA28, a gamma-interferon-inducible protein activator of the 20S proteasome. |journal=FEBS Lett. |volume=366 |issue= 1 |pages= 37-42 |year= 1995 |pmid= 7789512 |doi= }}
*{{cite journal | author=Realini C, Dubiel W, Pratt G, ''et al.'' |title=Molecular cloning and expression of a gamma-interferon-inducible activator of the multicatalytic protease. |journal=J. Biol. Chem. |volume=269 |issue= 32 |pages= 20727-32 |year= 1994 |pmid= 8051173 |doi= }}
*{{cite journal | author=Honoré B, Leffers H, Madsen P, Celis JE |title=Interferon-gamma up-regulates a unique set of proteins in human keratinocytes. Molecular cloning and expression of the cDNA encoding the RGD-sequence-containing protein IGUP I-5111. |journal=Eur. J. Biochem. |volume=218 |issue= 2 |pages= 421-30 |year= 1994 |pmid= 8269930 |doi= }}
*{{cite journal | author=Ahn K, Erlander M, Leturcq D, ''et al.'' |title=In vivo characterization of the proteasome regulator PA28. |journal=J. Biol. Chem. |volume=271 |issue= 30 |pages= 18237-42 |year= 1996 |pmid= 8663520 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Seeger M, Ferrell K, Frank R, Dubiel W |title=HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8145-8 |year= 1997 |pmid= 9079628 |doi= }}
*{{cite journal | author=Soza A, Knuehl C, Groettrup M, ''et al.'' |title=Expression and subcellular localization of mouse 20S proteasome activator complex PA28. |journal=FEBS Lett. |volume=413 |issue= 1 |pages= 27-34 |year= 1997 |pmid= 9287111 |doi= }}
*{{cite journal | author=McCusker D, Jones T, Sheer D, Trowsdale J |title=Genetic relationships of the genes encoding the human proteasome beta subunits and the proteasome PA28 complex. |journal=Genomics |volume=45 |issue= 2 |pages= 362-7 |year= 1998 |pmid= 9344661 |doi= 10.1006/geno.1997.4948 }}
*{{cite journal | author=Johnston SC, Whitby FG, Realini C, ''et al.'' |title=The proteasome 11S regulator subunit REG alpha (PA28 alpha) is a heptamer. |journal=Protein Sci. |volume=6 |issue= 11 |pages= 2469-73 |year= 1998 |pmid= 9385652 |doi= }}
*{{cite journal | author=Wang X, Omura S, Szweda LI, ''et al.'' |title=Rapamycin inhibits proteasome activator expression and proteasome activity. |journal=Eur. J. Immunol. |volume=27 |issue= 11 |pages= 2781-6 |year= 1998 |pmid= 9394799 |doi= }}
*{{cite journal | author=Knowlton JR, Johnston SC, Whitby FG, ''et al.'' |title=Structure of the proteasome activator REGalpha (PA28alpha). |journal=Nature |volume=390 |issue= 6660 |pages= 639-43 |year= 1998 |pmid= 9403698 |doi= 10.1038/37670 }}
*{{cite journal | author=Kohda K, Ishibashi T, Shimbara N, ''et al.'' |title=Characterization of the mouse PA28 activator complex gene family: complete organizations of the three member genes and a physical map of the approximately 150-kb region containing the alpha- and beta-subunit genes. |journal=J. Immunol. |volume=160 |issue= 10 |pages= 4923-35 |year= 1998 |pmid= 9590240 |doi= }}
*{{cite journal | author=Madani N, Kabat D |title=An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. |journal=J. Virol. |volume=72 |issue= 12 |pages= 10251-5 |year= 1998 |pmid= 9811770 |doi= }}
*{{cite journal | author=Simon JH, Gaddis NC, Fouchier RA, Malim MH |title=Evidence for a newly discovered cellular anti-HIV-1 phenotype. |journal=Nat. Med. |volume=4 |issue= 12 |pages= 1397-400 |year= 1998 |pmid= 9846577 |doi= 10.1038/3987 }}
*{{cite journal | author=McCusker D, Wilson M, Trowsdale J |title=Organization of the genes encoding the human proteasome activators PA28alpha and beta. |journal=Immunogenetics |volume=49 |issue= 5 |pages= 438-45 |year= 1999 |pmid= 10199920 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RHOB... {November 17, 2007 11:48:18 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:48:49 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_RHOB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2fv8.
| PDB = {{PDB2|2fv8}}
| Name = Ras homolog gene family, member B
| HGNCid = 668
| Symbol = RHOB
| AltSymbols =; ARH6; ARHB; MST081; MSTP081; RHOH6
| OMIM = 165370
| ECnumber =
| Homologene = 68377
| MGIid = 107949
| GeneAtlas_image1 = PBB_GE_RHOB_212099_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0010008 |text = endosome membrane}}
| Process = {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0006927 |text = transformed cell apoptosis}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0007266 |text = Rho protein signal transduction}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008333 |text = endosome to lysosome transport}} {{GNF_GO|id=GO:0015031 |text = protein transport}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0045766 |text = positive regulation of angiogenesis}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 388
| Hs_Ensembl = ENSG00000143878
| Hs_RefseqProtein = NP_004031
| Hs_RefseqmRNA = NM_004040
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 20510316
| Hs_GenLoc_end = 20512687
| Hs_Uniprot = P62745
| Mm_EntrezGene = 11852
| Mm_Ensembl = ENSMUSG00000054364
| Mm_RefseqmRNA = NM_007483
| Mm_RefseqProtein = NP_031509
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 8525050
| Mm_GenLoc_end = 8525640
| Mm_Uniprot = Q3TIC2
}}
}}
'''Ras homolog gene family, member B''', also known as '''RHOB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RHOB ras homolog gene family, member B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=388| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Casey PJ, Seabra MC |title=Protein prenyltransferases. |journal=J. Biol. Chem. |volume=271 |issue= 10 |pages= 5289-92 |year= 1996 |pmid= 8621375 |doi= }}
*{{cite journal | author=Adamson P, Marshall CJ, Hall A, Tilbrook PA |title=Post-translational modifications of p21rho proteins. |journal=J. Biol. Chem. |volume=267 |issue= 28 |pages= 20033-8 |year= 1992 |pmid= 1400319 |doi= }}
*{{cite journal | author=Cannizzaro LA, Madaule P, Hecht F, ''et al.'' |title=Chromosome localization of human ARH genes, a ras-related gene family. |journal=Genomics |volume=6 |issue= 2 |pages= 197-203 |year= 1990 |pmid= 2407642 |doi= }}
*{{cite journal | author=Chardin P, Madaule P, Tavitian A |title=Coding sequence of human rho cDNAs clone 6 and clone 9. |journal=Nucleic Acids Res. |volume=16 |issue= 6 |pages= 2717 |year= 1988 |pmid= 3283705 |doi= }}
*{{cite journal | author=Madaule P, Axel R |title=A novel ras-related gene family. |journal=Cell |volume=41 |issue= 1 |pages= 31-40 |year= 1985 |pmid= 3888408 |doi= }}
*{{cite journal | author=Robertson D, Paterson HF, Adamson P, ''et al.'' |title=Ultrastructural localization of ras-related proteins using epitope-tagged plasmids. |journal=J. Histochem. Cytochem. |volume=43 |issue= 5 |pages= 471-80 |year= 1995 |pmid= 7537292 |doi= }}
*{{cite journal | author=Armstrong SA, Hannah VC, Goldstein JL, Brown MS |title=CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB. |journal=J. Biol. Chem. |volume=270 |issue= 14 |pages= 7864-8 |year= 1995 |pmid= 7713879 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Zalcman G, Closson V, Camonis J, ''et al.'' |title=RhoGDI-3 is a new GDP dissociation inhibitor (GDI). Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG. |journal=J. Biol. Chem. |volume=271 |issue= 48 |pages= 30366-74 |year= 1997 |pmid= 8939998 |doi= }}
*{{cite journal | author=Mellor H, Flynn P, Nobes CD, ''et al.'' |title=PRK1 is targeted to endosomes by the small GTPase, RhoB. |journal=J. Biol. Chem. |volume=273 |issue= 9 |pages= 4811-4 |year= 1998 |pmid= 9478917 |doi= }}
*{{cite journal | author=Ishikawa K, Nagase T, Suyama M, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. |journal=DNA Res. |volume=5 |issue= 3 |pages= 169-76 |year= 1998 |pmid= 9734811 |doi= }}
*{{cite journal | author=Liu JP, Jessell TM |title=A role for rhoB in the delamination of neural crest cells from the dorsal neural tube. |journal=Development |volume=125 |issue= 24 |pages= 5055-67 |year= 1999 |pmid= 9811589 |doi= }}
*{{cite journal | author=Gampel A, Parker PJ, Mellor H |title=Regulation of epidermal growth factor receptor traffic by the small GTPase rhoB. |journal=Curr. Biol. |volume=9 |issue= 17 |pages= 955-8 |year= 2000 |pmid= 10508588 |doi= }}
*{{cite journal | author=Matarrese P, Conti L, Varano B, ''et al.'' |title=The HIV-1 vpr protein induces anoikis-resistance by modulating cell adhesion process and microfilament system assembly. |journal=Cell Death Differ. |volume=7 |issue= 1 |pages= 25-36 |year= 2000 |pmid= 10713718 |doi= 10.1038/sj.cdd.4400616 }}
*{{cite journal | author=Liu A, Du W, Liu JP, ''et al.'' |title=RhoB alteration is necessary for apoptotic and antineoplastic responses to farnesyltransferase inhibitors. |journal=Mol. Cell. Biol. |volume=20 |issue= 16 |pages= 6105-13 |year= 2000 |pmid= 10913192 |doi= }}
*{{cite journal | author=Michaelson D, Silletti J, Murphy G, ''et al.'' |title=Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding. |journal=J. Cell Biol. |volume=152 |issue= 1 |pages= 111-26 |year= 2001 |pmid= 11149925 |doi= }}
*{{cite journal | author=Liu Ax , Cerniglia GJ, Bernhard EJ, Prendergast GC |title=RhoB is required to mediate apoptosis in neoplastically transformed cells after DNA damage. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 11 |pages= 6192-7 |year= 2001 |pmid= 11353846 |doi= 10.1073/pnas.111137198 }}
*{{cite journal | author=Diviani D, Soderling J, Scott JD |title=AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation. |journal=J. Biol. Chem. |volume=276 |issue= 47 |pages= 44247-57 |year= 2001 |pmid= 11546812 |doi= 10.1074/jbc.M106629200 }}
*{{cite journal | author=Adnane J, Seijo E, Chen Z, ''et al.'' |title=RhoB, not RhoA, represses the transcription of the transforming growth factor beta type II receptor by a mechanism involving activator protein 1. |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 8500-7 |year= 2002 |pmid= 11741970 |doi= 10.1074/jbc.M104367200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SCN4A... {November 17, 2007 11:58:48 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:59:21 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SCN4A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1byy.
| PDB = {{PDB2|1byy}}
| Name = Sodium channel, voltage-gated, type IV, alpha subunit
| HGNCid = 10591
| Symbol = SCN4A
| AltSymbols =; HYKPP; HYPP; NAC1A; Na(V)1.4; Nav1.4; SkM1
| OMIM = 603967
| ECnumber =
| Homologene = 283
| MGIid = 98250
| GeneAtlas_image1 = PBB_GE_SCN4A_206981_at_tn.png
| Function = {{GNF_GO|id=GO:0005248 |text = voltage-gated sodium channel activity}} {{GNF_GO|id=GO:0031402 |text = sodium ion binding}}
| Component = {{GNF_GO|id=GO:0001518 |text = voltage-gated sodium channel complex}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006814 |text = sodium ion transport}} {{GNF_GO|id=GO:0006936 |text = muscle contraction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6329
| Hs_Ensembl = ENSG00000007314
| Hs_RefseqProtein = NP_000325
| Hs_RefseqmRNA = NM_000334
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 59369646
| Hs_GenLoc_end = 59404010
| Hs_Uniprot = P35499
| Mm_EntrezGene = 110880
| Mm_Ensembl = ENSMUSG00000001027
| Mm_RefseqmRNA = NM_133199
| Mm_RefseqProtein = NP_573462
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 106135394
| Mm_GenLoc_end = 106165480
| Mm_Uniprot =
}}
}}
'''Sodium channel, voltage-gated, type IV, alpha subunit''', also known as '''SCN4A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SCN4A sodium channel, voltage-gated, type IV, alpha subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6329| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Voltage-gated sodium channels are transmembrane glycoprotein complexes composed of a large alpha subunit with 24 transmembrane domains and one or more regulatory beta subunits. They are responsible for the generation and propagation of action potentials in neurons and muscle. This gene encodes one member of the sodium channel alpha subunit gene family. It is expressed in skeletal muscle, and mutations in this gene have been linked to several myotonia and periodic paralysis disorders.<ref name="entrez">{{cite web | title = Entrez Gene: SCN4A sodium channel, voltage-gated, type IV, alpha subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6329| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ackerman MJ, Clapham DE |title=Ion channels--basic science and clinical disease. |journal=N. Engl. J. Med. |volume=336 |issue= 22 |pages= 1575-86 |year= 1997 |pmid= 9164815 |doi= }}
*{{cite journal | author=Catterall WA, Goldin AL, Waxman SG |title=International Union of Pharmacology. XLVII. Nomenclature and structure-function relationships of voltage-gated sodium channels. |journal=Pharmacol. Rev. |volume=57 |issue= 4 |pages= 397-409 |year= 2006 |pmid= 16382098 |doi= 10.1124/pr.57.4.4 }}
*{{cite journal | author=Wang JZ, Rojas CV, Zhou JH, ''et al.'' |title=Sequence and genomic structure of the human adult skeletal muscle sodium channel alpha subunit gene on 17q. |journal=Biochem. Biophys. Res. Commun. |volume=182 |issue= 2 |pages= 794-801 |year= 1992 |pmid= 1310396 |doi= }}
*{{cite journal | author=Ptacek LJ, Tawil R, Griggs RC, ''et al.'' |title=Linkage of atypical myotonia congenita to a sodium channel locus. |journal=Neurology |volume=42 |issue= 2 |pages= 431-3 |year= 1992 |pmid= 1310531 |doi= }}
*{{cite journal | author=McClatchey AI, Van den Bergh P, Pericak-Vance MA, ''et al.'' |title=Temperature-sensitive mutations in the III-IV cytoplasmic loop region of the skeletal muscle sodium channel gene in paramyotonia congenita. |journal=Cell |volume=68 |issue= 4 |pages= 769-74 |year= 1992 |pmid= 1310898 |doi= }}
*{{cite journal | author=George AL, Komisarof J, Kallen RG, Barchi RL |title=Primary structure of the adult human skeletal muscle voltage-dependent sodium channel. |journal=Ann. Neurol. |volume=31 |issue= 2 |pages= 131-7 |year= 1992 |pmid= 1315496 |doi= 10.1002/ana.410310203 }}
*{{cite journal | author=Ptácek LJ, George AL, Barchi RL, ''et al.'' |title=Mutations in an S4 segment of the adult skeletal muscle sodium channel cause paramyotonia congenita. |journal=Neuron |volume=8 |issue= 5 |pages= 891-7 |year= 1992 |pmid= 1316765 |doi= }}
*{{cite journal | author=McClatchey AI, McKenna-Yasek D, Cros D, ''et al.'' |title=Novel mutations in families with unusual and variable disorders of the skeletal muscle sodium channel. |journal=Nat. Genet. |volume=2 |issue= 2 |pages= 148-52 |year= 1993 |pmid= 1338909 |doi= 10.1038/ng1092-148 }}
*{{cite journal | author=McClatchey AI, Lin CS, Wang J, ''et al.'' |title=The genomic structure of the human skeletal muscle sodium channel gene. |journal=Hum. Mol. Genet. |volume=1 |issue= 7 |pages= 521-7 |year= 1993 |pmid= 1339144 |doi= }}
*{{cite journal | author=Ptacek LJ, Trimmer JS, Agnew WS, ''et al.'' |title=Paramyotonia congenita and hyperkalemic periodic paralysis map to the same sodium-channel gene locus. |journal=Am. J. Hum. Genet. |volume=49 |issue= 4 |pages= 851-4 |year= 1991 |pmid= 1654742 |doi= }}
*{{cite journal | author=Rojas CV, Wang JZ, Schwartz LS, ''et al.'' |title=A Met-to-Val mutation in the skeletal muscle Na+ channel alpha-subunit in hyperkalaemic periodic paralysis. |journal=Nature |volume=354 |issue= 6352 |pages= 387-9 |year= 1992 |pmid= 1659668 |doi= 10.1038/354387a0 }}
*{{cite journal | author=Ptácek LJ, George AL, Griggs RC, ''et al.'' |title=Identification of a mutation in the gene causing hyperkalemic periodic paralysis. |journal=Cell |volume=67 |issue= 5 |pages= 1021-7 |year= 1992 |pmid= 1659948 |doi= }}
*{{cite journal | author=George AL, Ledbetter DH, Kallen RG, Barchi RL |title=Assignment of a human skeletal muscle sodium channel alpha-subunit gene (SCN4A) to 17q23.1-25.3. |journal=Genomics |volume=9 |issue= 3 |pages= 555-6 |year= 1991 |pmid= 1851726 |doi= }}
*{{cite journal | author=Fontaine B, Khurana TS, Hoffman EP, ''et al.'' |title=Hyperkalemic periodic paralysis and the adult muscle sodium channel alpha-subunit gene. |journal=Science |volume=250 |issue= 4983 |pages= 1000-2 |year= 1990 |pmid= 2173143 |doi= }}
*{{cite journal | author=Plassart E, Reboul J, Rime CS, ''et al.'' |title=Mutations in the muscle sodium channel gene (SCN4A) in 13 French families with hyperkalemic periodic paralysis and paramyotonia congenita: phenotype to genotype correlations and demonstration of the predominance of two mutations. |journal=Eur. J. Hum. Genet. |volume=2 |issue= 2 |pages= 110-24 |year= 1994 |pmid= 8044656 |doi= }}
*{{cite journal | author=Ptáĉek LJ, Tawil R, Griggs RC, ''et al.'' |title=Sodium channel mutations in acetazolamide-responsive myotonia congenita, paramyotonia congenita, and hyperkalemic periodic paralysis. |journal=Neurology |volume=44 |issue= 8 |pages= 1500-3 |year= 1994 |pmid= 8058156 |doi= }}
*{{cite journal | author=Heine R, Pika U, Lehmann-Horn F |title=A novel SCN4A mutation causing myotonia aggravated by cold and potassium. |journal=Hum. Mol. Genet. |volume=2 |issue= 9 |pages= 1349-53 |year= 1993 |pmid= 8242056 |doi= }}
*{{cite journal | author=Lerche H, Heine R, Pika U, ''et al.'' |title=Human sodium channel myotonia: slowed channel inactivation due to substitutions for a glycine within the III-IV linker. |journal=J. Physiol. (Lond.) |volume=470 |issue= |pages= 13-22 |year= 1994 |pmid= 8308722 |doi= }}
*{{cite journal | author=George AL, Iyer GS, Kleinfield R, ''et al.'' |title=Genomic organization of the human skeletal muscle sodium channel gene. |journal=Genomics |volume=15 |issue= 3 |pages= 598-606 |year= 1993 |pmid= 8385647 |doi= 10.1006/geno.1993.1113 }}
*{{cite journal | author=Ptacek LJ, Gouw L, Kwieciński H, ''et al.'' |title=Sodium channel mutations in paramyotonia congenita and hyperkalemic periodic paralysis. |journal=Ann. Neurol. |volume=33 |issue= 3 |pages= 300-7 |year= 1993 |pmid= 8388676 |doi= 10.1002/ana.410330312 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SERPINF2... {November 17, 2007 11:54:58 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:55:37 AM PST}
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{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2
| HGNCid = 9075
| Symbol = SERPINF2
| AltSymbols =; A2AP; AAP; ALPHA-2-PI; API; PLI
| OMIM = 262850
| ECnumber =
| Homologene = 719
| MGIid = 107173
| GeneAtlas_image1 = PBB_GE_SERPINF2_205075_at_tn.png
| Function = {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}}
| Process = {{GNF_GO|id=GO:0006953 |text = acute-phase response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5345
| Hs_Ensembl = ENSG00000167711
| Hs_RefseqProtein = NP_000925
| Hs_RefseqmRNA = NM_000934
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 1593070
| Hs_GenLoc_end = 1605310
| Hs_Uniprot = P08697
| Mm_EntrezGene = 18816
| Mm_Ensembl = ENSMUSG00000038224
| Mm_RefseqmRNA = NM_008878
| Mm_RefseqProtein = NP_032904
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 75247932
| Mm_GenLoc_end = 75255698
| Mm_Uniprot = Q5ND35
}}
}}
'''Serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2''', also known as '''SERPINF2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SERPINF2 serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5345| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wiman B, Collen D |title=Purification and characterization of human antiplasmin, the fast-acting plasmin inhibitor in plasma. |journal=Eur. J. Biochem. |volume=78 |issue= 1 |pages= 19-26 |year= 1977 |pmid= 21075 |doi= }}
*{{cite journal | author=Moroi M, Aoki N |title=Isolation and characterization of alpha2-plasmin inhibitor from human plasma. A novel proteinase inhibitor which inhibits activator-induced clot lysis. |journal=J. Biol. Chem. |volume=251 |issue= 19 |pages= 5956-65 |year= 1976 |pmid= 134998 |doi= }}
*{{cite journal | author=Wiman B, Collen D |title=On the mechanism of the reaction between human alpha 2-antiplasmin and plasmin. |journal=J. Biol. Chem. |volume=254 |issue= 18 |pages= 9291-7 |year= 1979 |pmid= 158022 |doi= }}
*{{cite journal | author=Christensen S, Sottrup-Jensen L |title=Bovine alpha 2-antiplasmin. N-terminal and reactive site sequence. |journal=FEBS Lett. |volume=312 |issue= 1 |pages= 100-4 |year= 1992 |pmid= 1385210 |doi= }}
*{{cite journal | author=Welch SK, Francke U |title=Assignment of the human alpha 2-plasmin inhibitor gene (PLI) to chromosome 17, region pter-p12, by PCR analysis of somatic cell hybrids. |journal=Genomics |volume=13 |issue= 1 |pages= 213-4 |year= 1992 |pmid= 1577485 |doi= }}
*{{cite journal | author=Holmes WE, Nelles L, Lijnen HR, Collen D |title=Primary structure of human alpha 2-antiplasmin, a serine protease inhibitor (serpin). |journal=J. Biol. Chem. |volume=262 |issue= 4 |pages= 1659-64 |year= 1987 |pmid= 2433286 |doi= }}
*{{cite journal | author=Hortin G, Fok KF, Toren PC, Strauss AW |title=Sulfation of a tyrosine residue in the plasmin-binding domain of alpha 2-antiplasmin. |journal=J. Biol. Chem. |volume=262 |issue= 7 |pages= 3082-5 |year= 1987 |pmid= 2434496 |doi= }}
*{{cite journal | author=Shieh BH, Travis J |title=The reactive site of human alpha 2-antiplasmin. |journal=J. Biol. Chem. |volume=262 |issue= 13 |pages= 6055-9 |year= 1987 |pmid= 2437112 |doi= }}
*{{cite journal | author=Lijnen HR, Holmes WE, van Hoef B, ''et al.'' |title=Amino-acid sequence of human alpha 2-antiplasmin. |journal=Eur. J. Biochem. |volume=166 |issue= 3 |pages= 565-74 |year= 1987 |pmid= 2440681 |doi= }}
*{{cite journal | author=Potempa J, Shieh BH, Travis J |title=Alpha-2-antiplasmin: a serpin with two separate but overlapping reactive sites. |journal=Science |volume=241 |issue= 4866 |pages= 699-700 |year= 1988 |pmid= 2456616 |doi= }}
*{{cite journal | author=Miura O, Sugahara Y, Aoki N |title=Hereditary alpha 2-plasmin inhibitor deficiency caused by a transport-deficient mutation (alpha 2-PI-Okinawa). Deletion of Glu137 by a trinucleotide deletion blocks intracellular transport. |journal=J. Biol. Chem. |volume=264 |issue= 30 |pages= 18213-9 |year= 1989 |pmid= 2572590 |doi= }}
*{{cite journal | author=Tone M, Kikuno R, Kume-Iwaki A, Hashimoto-Gotoh T |title=Structure of human alpha 2-plasmin inhibitor deduced from the cDNA sequence. |journal=J. Biochem. |volume=102 |issue= 5 |pages= 1033-41 |year= 1988 |pmid= 2830248 |doi= }}
*{{cite journal | author=Holmes WE, Lijnen HR, Nelles L, ''et al.'' |title=Alpha 2-antiplasmin Enschede: alanine insertion and abolition of plasmin inhibitory activity. |journal=Science |volume=238 |issue= 4824 |pages= 209-11 |year= 1987 |pmid= 2958938 |doi= }}
*{{cite journal | author=Hirosawa S, Nakamura Y, Miura O, ''et al.'' |title=Organization of the human alpha 2-plasmin inhibitor gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 18 |pages= 6836-40 |year= 1988 |pmid= 3166140 |doi= }}
*{{cite journal | author=Sugiyama N, Sasaki T, Iwamoto M, Abiko Y |title=Binding site of alpha 2-plasmin inhibitor to plasminogen. |journal=Biochim. Biophys. Acta |volume=952 |issue= 1 |pages= 1-7 |year= 1988 |pmid= 3334852 |doi= }}
*{{cite journal | author=Kato A, Nakamura Y, Miura O, ''et al.'' |title=Assignment of the human alpha 2-plasmin inhibitor gene (PLI) to chromosome region 18p11.1----q11.2 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=47 |issue= 4 |pages= 209-11 |year= 1988 |pmid= 3416655 |doi= }}
*{{cite journal | author=Sumi Y, Nakamura Y, Aoki N, ''et al.'' |title=Structure of the carboxyl-terminal half of human alpha 2-plasmin inhibitor deduced from that of cDNA. |journal=J. Biochem. |volume=100 |issue= 5 |pages= 1399-402 |year= 1987 |pmid= 3818581 |doi= }}
*{{cite journal | author=Brower MS, Harpel PC |title=Proteolytic cleavage and inactivation of alpha 2-plasmin inhibitor and C1 inactivator by human polymorphonuclear leukocyte elastase. |journal=J. Biol. Chem. |volume=257 |issue= 16 |pages= 9849-54 |year= 1982 |pmid= 6980881 |doi= }}
*{{cite journal | author=Yoshioka A, Kamitsuji H, Takase T, ''et al.'' |title=Congenital deficiency of alpha 2-plasmin inhibitor in three sisters. |journal=Haemostasis |volume=11 |issue= 3 |pages= 176-84 |year= 1982 |pmid= 7095605 |doi= }}
*{{cite journal | author=Panyutich AV, Hiemstra PS, van Wetering S, Ganz T |title=Human neutrophil defensin and serpins form complexes and inactivate each other. |journal=Am. J. Respir. Cell Mol. Biol. |volume=12 |issue= 3 |pages= 351-7 |year= 1995 |pmid= 7873202 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SKP1A... {November 17, 2007 11:59:21 AM PST}
- SEARCH REDIRECT: Control Box Found: SKP1A {November 17, 2007 12:00:03 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:00:05 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:00:05 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:00:05 PM PST}
- UPDATED: Updated protein page: SKP1A {November 17, 2007 12:00:11 PM PST}
end log.
