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Log page index: User:ProteinBoxBot/PBB_Log_Index
[edit] Protein Status Quick Log - Date: 08:35, 19 November 2007 (UTC)
[edit] Proteins without matches (11)
[edit] Proteins with a High Potential Match (6)
[edit] Redirected Proteins (8)
[edit] Manual Inspection (Page not found) (17)
[edit] Updated (8)
[edit] Protein Status Grid - Date: 08:35, 19 November 2007 (UTC)
[edit] Vebose Log - Date: 08:35, 19 November 2007 (UTC)
- INFO: Beginning work on ATXN2... {November 19, 2007 12:25:15 AM PST}
- SEARCH REDIRECT: Control Box Found: ATXN2 {November 19, 2007 12:25:47 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:25:50 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:25:50 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:25:50 AM PST}
- UPDATED: Updated protein page: ATXN2 {November 19, 2007 12:25:56 AM PST}
- INFO: Beginning work on BGLAP... {November 19, 2007 12:15:27 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:15:48 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_BGLAP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1q3m.
| PDB = {{PDB2|1q3m}}, {{PDB2|1q8h}}
| Name = Bone gamma-carboxyglutamate (gla) protein (osteocalcin)
| HGNCid = 1043
| Symbol = BGLAP
| AltSymbols =; BGP; PMF1
| OMIM = 112260
| ECnumber =
| Homologene = 86974
| MGIid =
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008147 |text = structural constituent of bone}} {{GNF_GO|id=GO:0046848 |text = hydroxyapatite binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0030500 |text = regulation of bone mineralization}} {{GNF_GO|id=GO:0042476 |text = odontogenesis}} {{GNF_GO|id=GO:0045124 |text = regulation of bone resorption}} {{GNF_GO|id=GO:0045670 |text = regulation of osteoclast differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 632
| Hs_Ensembl =
| Hs_RefseqProtein = NP_954642
| Hs_RefseqmRNA = NM_199173
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Bone gamma-carboxyglutamate (gla) protein (osteocalcin)''', also known as '''BGLAP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BGLAP bone gamma-carboxyglutamate (gla) protein (osteocalcin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=632| 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=Desbois C, Karsenty G |title=Osteocalcin cluster: implications for functional studies. |journal=J. Cell. Biochem. |volume=57 |issue= 3 |pages= 379-83 |year= 1995 |pmid= 7768973 |doi= 10.1002/jcb.240570302 }}
*{{cite journal | author=Fujisawa R |title=[Recent advances in research on bone matrix proteins] |journal=Nippon Rinsho |volume=60 Suppl 3 |issue= |pages= 72-8 |year= 2002 |pmid= 11979972 |doi= }}
*{{cite journal | author=Kiefer MC, Saphire AC, Bauer DM, Barr PJ |title=The cDNA and derived amino acid sequences of human and bovine bone Gla protein. |journal=Nucleic Acids Res. |volume=18 |issue= 7 |pages= 1909 |year= 1990 |pmid= 2336375 |doi= }}
*{{cite journal | author=Cancela L, Hsieh CL, Francke U, Price PA |title=Molecular structure, chromosome assignment, and promoter organization of the human matrix Gla protein gene. |journal=J. Biol. Chem. |volume=265 |issue= 25 |pages= 15040-8 |year= 1990 |pmid= 2394711 |doi= }}
*{{cite journal | author=Puchacz E, Lian JB, Stein GS, ''et al.'' |title=Chromosomal localization of the human osteocalcin gene. |journal=Endocrinology |volume=124 |issue= 5 |pages= 2648-50 |year= 1989 |pmid= 2785029 |doi= }}
*{{cite journal | author=Celeste AJ, Rosen V, Buecker JL, ''et al.'' |title=Isolation of the human gene for bone gla protein utilizing mouse and rat cDNA clones. |journal=EMBO J. |volume=5 |issue= 8 |pages= 1885-90 |year= 1986 |pmid= 3019668 |doi= }}
*{{cite journal | author=Poser JW, Esch FS, Ling NC, Price PA |title=Isolation and sequence of the vitamin K-dependent protein from human bone. Undercarboxylation of the first glutamic acid residue. |journal=J. Biol. Chem. |volume=255 |issue= 18 |pages= 8685-91 |year= 1980 |pmid= 6967872 |doi= }}
*{{cite journal | author=Baumgrass R, Williamson MK, Price PA |title=Identification of peptide fragments generated by digestion of bovine and human osteocalcin with the lysosomal proteinases cathepsin B, D, L, H, and S. |journal=J. Bone Miner. Res. |volume=12 |issue= 3 |pages= 447-55 |year= 1997 |pmid= 9076588 |doi= }}
*{{cite journal | author=Houben RJ, Jin D, Stafford DW, ''et al.'' |title=Osteocalcin binds tightly to the gamma-glutamylcarboxylase at a site distinct from that of the other known vitamin K-dependent proteins. |journal=Biochem. J. |volume=341 ( Pt 2) |issue= |pages= 265-9 |year= 1999 |pmid= 10393081 |doi= }}
*{{cite journal | author=Wang Y, Devereux W, Stewart TM, Casero RA |title=Cloning and characterization of human polyamine-modulated factor-1, a transcriptional cofactor that regulates the transcription of the spermidine/spermine N(1)-acetyltransferase gene. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 22095-101 |year= 1999 |pmid= 10419538 |doi= }}
*{{cite journal | author=Raymond MH, Schutte BC, Torner JC, ''et al.'' |title=Osteocalcin: genetic and physical mapping of the human gene BGLAP and its potential role in postmenopausal osteoporosis. |journal=Genomics |volume=60 |issue= 2 |pages= 210-7 |year= 1999 |pmid= 10486212 |doi= 10.1006/geno.1999.5893 }}
*{{cite journal | author=Beaudreuil J, Taboulet J, Orcel P, ''et al.'' |title=Calcitonin receptor mRNA in mononuclear leucocytes from postmenopausal women: decrease during osteoporosis and link to bone markers with specific isoform involvement. |journal=Bone |volume=27 |issue= 1 |pages= 161-8 |year= 2000 |pmid= 10865224 |doi= }}
*{{cite journal | author=Papagerakis P, Berdal A, Mesbah M, ''et al.'' |title=Investigation of osteocalcin, osteonectin, and dentin sialophosphoprotein in developing human teeth. |journal=Bone |volume=30 |issue= 2 |pages= 377-85 |year= 2002 |pmid= 11856645 |doi= }}
*{{cite journal | author=Deng HW, Shen H, Xu FH, ''et al.'' |title=Tests of linkage and/or association of genes for vitamin D receptor, osteocalcin, and parathyroid hormone with bone mineral density. |journal=J. Bone Miner. Res. |volume=17 |issue= 4 |pages= 678-86 |year= 2002 |pmid= 11918225 |doi= }}
*{{cite journal | author=Viereck V, Siggelkow H, Tauber S, ''et al.'' |title=Differential regulation of Cbfa1/Runx2 and osteocalcin gene expression by vitamin-D3, dexamethasone, and local growth factors in primary human osteoblasts. |journal=J. Cell. Biochem. |volume=86 |issue= 2 |pages= 348-56 |year= 2002 |pmid= 12112004 |doi= 10.1002/jcb.10220 }}
*{{cite journal | author=Willis DM, Loewy AP, Charlton-Kachigian N, ''et al.'' |title=Regulation of osteocalcin gene expression by a novel Ku antigen transcription factor complex. |journal=J. Biol. Chem. |volume=277 |issue= 40 |pages= 37280-91 |year= 2002 |pmid= 12145306 |doi= 10.1074/jbc.M206482200 }}
*{{cite journal | author=Knepper-Nicolai B, Reinstorf A, Hofinger I, ''et al.'' |title=Influence of osteocalcin and collagen I on the mechanical and biological properties of Biocement D. |journal=Biomol. Eng. |volume=19 |issue= 2-6 |pages= 227-31 |year= 2003 |pmid= 12202187 |doi= }}
*{{cite journal | author=Yousfi M, Lasmoles F, Marie PJ |title=TWIST inactivation reduces CBFA1/RUNX2 expression and DNA binding to the osteocalcin promoter in osteoblasts. |journal=Biochem. Biophys. Res. Commun. |volume=297 |issue= 3 |pages= 641-4 |year= 2002 |pmid= 12270142 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BIK... {November 19, 2007 12:15:48 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:16:16 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 = BCL2-interacting killer (apoptosis-inducing)
| HGNCid = 1051
| Symbol = BIK
| AltSymbols =; BIP1; BP4; NBK
| OMIM = 603392
| ECnumber =
| Homologene = 924
| MGIid = 1206591
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005740 |text = mitochondrial envelope}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0008632 |text = apoptotic program}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 638
| Hs_Ensembl = ENSG00000100290
| Hs_RefseqProtein = NP_001188
| Hs_RefseqmRNA = NM_001197
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 41836701
| Hs_GenLoc_end = 41855661
| Hs_Uniprot = Q13323
| Mm_EntrezGene = 12124
| Mm_Ensembl = ENSMUSG00000016758
| Mm_RefseqmRNA = XM_001001652
| Mm_RefseqProtein = XP_001001652
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 83354629
| Mm_GenLoc_end = 83372401
| Mm_Uniprot =
}}
}}
'''BCL2-interacting killer (apoptosis-inducing)''', also known as '''BIK''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BIK BCL2-interacting killer (apoptosis-inducing)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=638| 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 known to interact with cellular and viral survival-promoting proteins, such as BCL2 and the Epstein-Barr virus in order to enhance programed cell death. Because its activity is suppressed in the presence of survival-promoting proteins, this protein is suggested as a likely target for antiapoptotic proteins. This protein shares a critical BH3 domain with other death-promoting proteins, BAX and BAK.<ref name="entrez">{{cite web | title = Entrez Gene: BIK BCL2-interacting killer (apoptosis-inducing)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=638| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Boyd JM, Gallo GJ, Elangovan B, ''et al.'' |title=Bik, a novel death-inducing protein shares a distinct sequence motif with Bcl-2 family proteins and interacts with viral and cellular survival-promoting proteins. |journal=Oncogene |volume=11 |issue= 9 |pages= 1921-8 |year= 1995 |pmid= 7478623 |doi= }}
*{{cite journal | author=Chittenden T, Flemington C, Houghton AB, ''et al.'' |title=A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions. |journal=EMBO J. |volume=14 |issue= 22 |pages= 5589-96 |year= 1996 |pmid= 8521816 |doi= }}
*{{cite journal | author=Han J, Sabbatini P, White E |title=Induction of apoptosis by human Nbk/Bik, a BH3-containing protein that interacts with E1B 19K. |journal=Mol. Cell. Biol. |volume=16 |issue= 10 |pages= 5857-64 |year= 1996 |pmid= 8816500 |doi= }}
*{{cite journal | author=Inohara N, Ding L, Chen S, Núñez G |title=harakiri, a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survival-promoting proteins Bcl-2 and Bcl-X(L). |journal=EMBO J. |volume=16 |issue= 7 |pages= 1686-94 |year= 1997 |pmid= 9130713 |doi= 10.1093/emboj/16.7.1686 }}
*{{cite journal | author=Huang DC, Adams JM, Cory S |title=The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4. |journal=EMBO J. |volume=17 |issue= 4 |pages= 1029-39 |year= 1998 |pmid= 9463381 |doi= 10.1093/emboj/17.4.1029 }}
*{{cite journal | author=Hegde R, Srinivasula SM, Ahmad M, ''et al.'' |title=Blk, a BH3-containing mouse protein that interacts with Bcl-2 and Bcl-xL, is a potent death agonist. |journal=J. Biol. Chem. |volume=273 |issue= 14 |pages= 7783-6 |year= 1998 |pmid= 9525867 |doi= }}
*{{cite journal | author=Ohi N, Tokunaga A, Tsunoda H, ''et al.'' |title=A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region. |journal=Cell Death Differ. |volume=6 |issue= 4 |pages= 314-25 |year= 1999 |pmid= 10381623 |doi= 10.1038/sj.cdd.4400493 }}
*{{cite journal | author=Holmgreen SP, Huang DC, Adams JM, Cory S |title=Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members. |journal=Cell Death Differ. |volume=6 |issue= 6 |pages= 525-32 |year= 1999 |pmid= 10381646 |doi= 10.1038/sj.cdd.4400519 }}
*{{cite journal | author=Castells A, Ino Y, Louis DN, ''et al.'' |title=Mapping of a target region of allelic loss to a 0.5-cM interval on chromosome 22q13 in human colorectal cancer. |journal=Gastroenterology |volume=117 |issue= 4 |pages= 831-7 |year= 1999 |pmid= 10500065 |doi= }}
*{{cite journal | author=Dunham I, Shimizu N, Roe BA, ''et al.'' |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489-95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031 }}
*{{cite journal | author=Verma S, Budarf ML, Emanuel BS, Chinnadurai G |title=Structural analysis of the human pro-apoptotic gene Bik: chromosomal localization, genomic organization and localization of promoter sequences. |journal=Gene |volume=254 |issue= 1-2 |pages= 157-62 |year= 2000 |pmid= 10974546 |doi= }}
*{{cite journal | author=Jiang A, Clark EA |title=Involvement of Bik, a proapoptotic member of the Bcl-2 family, in surface IgM-mediated B cell apoptosis. |journal=J. Immunol. |volume=166 |issue= 10 |pages= 6025-33 |year= 2001 |pmid= 11342619 |doi= }}
*{{cite journal | author=Federici M, Hribal M, Perego L, ''et al.'' |title=High glucose causes apoptosis in cultured human pancreatic islets of Langerhans: a potential role for regulation of specific Bcl family genes toward an apoptotic cell death program. |journal=Diabetes |volume=50 |issue= 6 |pages= 1290-301 |year= 2001 |pmid= 11375329 |doi= }}
*{{cite journal | author=Zou Y, Peng H, Zhou B, ''et al.'' |title=Systemic tumor suppression by the proapoptotic gene bik. |journal=Cancer Res. |volume=62 |issue= 1 |pages= 8-12 |year= 2002 |pmid= 11782349 |doi= }}
*{{cite journal | author=Germain M, Mathai JP, Shore GC |title=BH-3-only BIK functions at the endoplasmic reticulum to stimulate cytochrome c release from mitochondria. |journal=J. Biol. Chem. |volume=277 |issue= 20 |pages= 18053-60 |year= 2002 |pmid= 11884414 |doi= 10.1074/jbc.M201235200 }}
*{{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=Gillissen B, Essmann F, Graupner V, ''et al.'' |title=Induction of cell death by the BH3-only Bcl-2 homolog Nbk/Bik is mediated by an entirely Bax-dependent mitochondrial pathway. |journal=EMBO J. |volume=22 |issue= 14 |pages= 3580-90 |year= 2003 |pmid= 12853473 |doi= 10.1093/emboj/cdg343 }}
*{{cite journal | author=Arena V, Martini M, Luongo M, ''et al.'' |title=Mutations of the BIK gene in human peripheral B-cell lymphomas. |journal=Genes Chromosomes Cancer |volume=38 |issue= 1 |pages= 91-6 |year= 2003 |pmid= 12874789 |doi= 10.1002/gcc.10245 }}
*{{cite journal | author=Hur J, Chesnes J, Coser KR, ''et al.'' |title=The Bik BH3-only protein is induced in estrogen-starved and antiestrogen-exposed breast cancer cells and provokes apoptosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 8 |pages= 2351-6 |year= 2004 |pmid= 14983013 |doi= }}
*{{cite journal | author=Collins JE, Wright CL, Edwards CA, ''et al.'' |title=A genome annotation-driven approach to cloning the human ORFeome. |journal=Genome Biol. |volume=5 |issue= 10 |pages= R84 |year= 2005 |pmid= 15461802 |doi= 10.1186/gb-2004-5-10-r84 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NFYB... {November 19, 2007 12:16:16 AM PST}
- SEARCH REDIRECT: Control Box Found: NFYB {November 19, 2007 12:16:52 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:16:53 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:16:53 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:16:53 AM PST}
- UPDATED: Updated protein page: NFYB {November 19, 2007 12:17:00 AM PST}
- INFO: Beginning work on NSF... {November 19, 2007 12:17:00 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:17:19 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_NSF_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1d2n.
| PDB = {{PDB2|1d2n}}, {{PDB2|1nsf}}, {{PDB2|1qcs}}, {{PDB2|1qdn}}
| Name = N-ethylmaleimide-sensitive factor
| HGNCid = 8016
| Symbol = NSF
| AltSymbols =; SKD2
| OMIM = 601633
| ECnumber =
| Homologene = 4502
| MGIid = 104560
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0017111 |text = nucleoside-triphosphatase activity}} {{GNF_GO|id=GO:0019905 |text = syntaxin binding}} {{GNF_GO|id=GO:0042623 |text = ATPase activity, coupled}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}}
| Process = {{GNF_GO|id=GO:0015031 |text = protein transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4905
| Hs_Ensembl =
| Hs_RefseqProtein = XP_001128468
| Hs_RefseqmRNA = XM_001128468
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 18195
| Mm_Ensembl = ENSMUSG00000034187
| Mm_RefseqmRNA = NM_008740
| Mm_RefseqProtein = NP_032766
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 103637872
| Mm_GenLoc_end = 103770146
| Mm_Uniprot = Q8BQ65
}}
}}
'''N-ethylmaleimide-sensitive factor''', also known as '''NSF''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NSF N-ethylmaleimide-sensitive factor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4905| 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=Wilson DW, Whiteheart SW, Wiedmann M, ''et al.'' |title=A multisubunit particle implicated in membrane fusion. |journal=J. Cell Biol. |volume=117 |issue= 3 |pages= 531-8 |year= 1992 |pmid= 1315316 |doi= }}
*{{cite journal | author=Hanson PI, Otto H, Barton N, Jahn R |title=The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin. |journal=J. Biol. Chem. |volume=270 |issue= 28 |pages= 16955-61 |year= 1995 |pmid= 7622514 |doi= }}
*{{cite journal | author=Püschel AW, O'Connor V, Betz H |title=The N-ethylmaleimide-sensitive fusion protein (NSF) is preferentially expressed in the nervous system. |journal=FEBS Lett. |volume=347 |issue= 1 |pages= 55-8 |year= 1994 |pmid= 8013662 |doi= }}
*{{cite journal | author=Whiteheart SW, Rossnagel K, Buhrow SA, ''et al.'' |title=N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. |journal=J. Cell Biol. |volume=126 |issue= 4 |pages= 945-54 |year= 1994 |pmid= 8051214 |doi= }}
*{{cite journal | author=Nagahama M, Orci L, Ravazzola M, ''et al.'' |title=A v-SNARE implicated in intra-Golgi transport. |journal=J. Cell Biol. |volume=133 |issue= 3 |pages= 507-16 |year= 1996 |pmid= 8636227 |doi= }}
*{{cite journal | author=Hoyle J, Phelan JP, Bermingham N, Fisher EM |title=Localization of human and mouse N-ethylmaleimide-sensitive factor (NSF) gene: a two-domain member of the AAA family that is involved in membrane fusion. |journal=Mamm. Genome |volume=7 |issue= 11 |pages= 850-2 |year= 1997 |pmid= 8875895 |doi= }}
*{{cite journal | author=Jacobsson G, Meister B |title=Molecular components of the exocytotic machinery in the rat pituitary gland. |journal=Endocrinology |volume=137 |issue= 12 |pages= 5344-56 |year= 1997 |pmid= 8940356 |doi= }}
*{{cite journal | author=Timmers KI, Clark AE, Omatsu-Kanbe M, ''et al.'' |title=Identification of SNAP receptors in rat adipose cell membrane fractions and in SNARE complexes co-immunoprecipitated with epitope-tagged N-ethylmaleimide-sensitive fusion protein. |journal=Biochem. J. |volume=320 ( Pt 2) |issue= |pages= 429-36 |year= 1997 |pmid= 8973549 |doi= }}
*{{cite journal | author=Germain-Lee EL, Obie C, Valle D |title=NVL: a new member of the AAA family of ATPases localized to the nucleus. |journal=Genomics |volume=44 |issue= 1 |pages= 22-34 |year= 1997 |pmid= 9286697 |doi= 10.1006/geno.1997.4856 }}
*{{cite journal | author=Subramaniam VN, Loh E, Hong W |title=N-Ethylmaleimide-sensitive factor (NSF) and alpha-soluble NSF attachment proteins (SNAP) mediate dissociation of GS28-syntaxin 5 Golgi SNAP receptors (SNARE) complex. |journal=J. Biol. Chem. |volume=272 |issue= 41 |pages= 25441-4 |year= 1997 |pmid= 9325254 |doi= }}
*{{cite journal | author=Lowe SL, Peter F, Subramaniam VN, ''et al.'' |title=A SNARE involved in protein transport through the Golgi apparatus. |journal=Nature |volume=389 |issue= 6653 |pages= 881-4 |year= 1997 |pmid= 9349823 |doi= 10.1038/39923 }}
*{{cite journal | author=Barnard RJ, Morgan A, Burgoyne RD |title=Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis. |journal=J. Cell Biol. |volume=139 |issue= 4 |pages= 875-83 |year= 1997 |pmid= 9362506 |doi= }}
*{{cite journal | author=Osten P, Srivastava S, Inman GJ, ''et al.'' |title=The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and alpha- and beta-SNAPs. |journal=Neuron |volume=21 |issue= 1 |pages= 99-110 |year= 1998 |pmid= 9697855 |doi= }}
*{{cite journal | author=McDonald PH, Cote NL, Lin FT, ''et al.'' |title=Identification of NSF as a beta-arrestin1-binding protein. Implications for beta2-adrenergic receptor regulation. |journal=J. Biol. Chem. |volume=274 |issue= 16 |pages= 10677-80 |year= 1999 |pmid= 10196135 |doi= }}
*{{cite journal | author=Subramaniam VN, Loh E, Horstmann H, ''et al.'' |title=Preferential association of syntaxin 8 with the early endosome. |journal=J. Cell. Sci. |volume=113 ( Pt 6) |issue= |pages= 997-1008 |year= 2000 |pmid= 10683148 |doi= }}
*{{cite journal | author=Sagiv Y, Legesse-Miller A, Porat A, Elazar Z |title=GATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28. |journal=EMBO J. |volume=19 |issue= 7 |pages= 1494-504 |year= 2000 |pmid= 10747018 |doi= 10.1093/emboj/19.7.1494 }}
*{{cite journal | author=Allan BB, Moyer BD, Balch WE |title=Rab1 recruitment of p115 into a cis-SNARE complex: programming budding COPII vesicles for fusion. |journal=Science |volume=289 |issue= 5478 |pages= 444-8 |year= 2000 |pmid= 10903204 |doi= }}
*{{cite journal | author=Michaut M, Tomes CN, De Blas G, ''et al.'' |title=Calcium-triggered acrosomal exocytosis in human spermatozoa requires the coordinated activation of Rab3A and N-ethylmaleimide-sensitive factor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 18 |pages= 9996-10001 |year= 2000 |pmid= 10954749 |doi= 10.1073/pnas.180206197 }}
*{{cite journal | author=Imai C, Sugai T, Iritani S, ''et al.'' |title=A quantitative study on the expression of synapsin II and N-ethylmaleimide-sensitive fusion protein in schizophrenic patients. |journal=Neurosci. Lett. |volume=305 |issue= 3 |pages= 185-8 |year= 2001 |pmid= 11403936 |doi= }}
*{{cite journal | author=Kittler JT, Rostaing P, Schiavo G, ''et al.'' |title=The subcellular distribution of GABARAP and its ability to interact with NSF suggest a role for this protein in the intracellular transport of GABA(A) receptors. |journal=Mol. Cell. Neurosci. |volume=18 |issue= 1 |pages= 13-25 |year= 2001 |pmid= 11461150 |doi= 10.1006/mcne.2001.1005 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on OXT... {November 19, 2007 12:17:19 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:17:49 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 =
| image_source =
| PDB =
| Name = Oxytocin, prepro- (neurophysin I)
| HGNCid = 8528
| Symbol = OXT
| AltSymbols =; MGC126890; MGC126892; OT; OT-NPI
| OMIM = 167050
| ECnumber =
| Homologene = 55494
| MGIid = 97453
| GeneAtlas_image1 = PBB_GE_OXT_207576_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}} {{GNF_GO|id=GO:0005185 |text = neurohypophyseal hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007567 |text = parturition}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5020
| Hs_Ensembl = ENSG00000101405
| Hs_RefseqProtein = NP_000906
| Hs_RefseqmRNA = NM_000915
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 3000266
| Hs_GenLoc_end = 3001162
| Hs_Uniprot = P01178
| Mm_EntrezGene = 18429
| Mm_Ensembl = ENSMUSG00000027301
| Mm_RefseqmRNA = NM_011025
| Mm_RefseqProtein = NP_035155
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 130267614
| Mm_GenLoc_end = 130268429
| Mm_Uniprot = Q545V4
}}
}}
'''Oxytocin, prepro- (neurophysin I)''', also known as '''OXT''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: OXT oxytocin, prepro- (neurophysin I)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5020| 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 = There are two proteins encoded by this gene, oxytocin and neurophysin I. Oxytocin is posterior pituitary hormone which is synthesized as an inactive precursor in the hypothalamus along with its carrier protein neurophysin I. Together with neurophysin, it is packaged into neurosecretory vesicles and transported axonally to the nerve endings in the neurohypophysis, where it is either stored or secreted into the bloodstream. The precursor seems to be activated while it is being transported along the axon to the posterior pituitary. This hormone contracts smooth muscle during parturition and lactation. It is also involved in cognition, tolerance, adaptation and complex sexual and maternal behaviour, as well as in the regulation of water excretion and cardiovascular functions.<ref name="entrez">{{cite web | title = Entrez Gene: OXT oxytocin, prepro- (neurophysin I)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5020| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Gutkowska J, Jankowski M, Mukaddam-Daher S, McCann SM |title=Oxytocin is a cardiovascular hormone. |journal=Braz. J. Med. Biol. Res. |volume=33 |issue= 6 |pages= 625-33 |year= 2000 |pmid= 10829090 |doi= }}
*{{cite journal | author=Filippi S, Vignozzi L, Vannelli GB, ''et al.'' |title=Role of oxytocin in the ejaculatory process. |journal=J. Endocrinol. Invest. |volume=26 |issue= 3 Suppl |pages= 82-6 |year= 2004 |pmid= 12834028 |doi= }}
*{{cite journal | author=Cassoni P, Sapino A, Marrocco T, ''et al.'' |title=Oxytocin and oxytocin receptors in cancer cells and proliferation. |journal=J. Neuroendocrinol. |volume=16 |issue= 4 |pages= 362-4 |year= 2004 |pmid= 15089975 |doi= 10.1111/j.0953-8194.2004.01165.x }}
*{{cite journal | author=Koida M, Walter R |title=Post-proline cleaving enzyme. Purification of this endopeptidase by affinity chromatography. |journal=J. Biol. Chem. |volume=251 |issue= 23 |pages= 7593-9 |year= 1977 |pmid= 12173 |doi= }}
*{{cite journal | author=Rao VV, Löffler C, Battey J, Hansmann I |title=The human gene for oxytocin-neurophysin I (OXT) is physically mapped to chromosome 20p13 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=61 |issue= 4 |pages= 271-3 |year= 1993 |pmid= 1486803 |doi= }}
*{{cite journal | author=Ivell R, Furuya K, Brackmann B, ''et al.'' |title=Expression of the oxytocin and vasopressin genes in human and baboon gonadal tissues. |journal=Endocrinology |volume=127 |issue= 6 |pages= 2990-6 |year= 1991 |pmid= 2249637 |doi= }}
*{{cite journal | author=Sausville E, Carney D, Battey J |title=The human vasopressin gene is linked to the oxytocin gene and is selectively expressed in a cultured lung cancer cell line. |journal=J. Biol. Chem. |volume=260 |issue= 18 |pages= 10236-41 |year= 1985 |pmid= 2991279 |doi= }}
*{{cite journal | author=Wood SP, Tickle IJ, Treharne AM, ''et al.'' |title=Crystal structure analysis of deamino-oxytocin: conformational flexibility and receptor binding. |journal=Science |volume=232 |issue= 4750 |pages= 633-6 |year= 1986 |pmid= 3008332 |doi= }}
*{{cite journal | author=Rehbein M, Hillers M, Mohr E, ''et al.'' |title=The neurohypophyseal hormones vasopressin and oxytocin. Precursor structure, synthesis and regulation. |journal=Biol. Chem. Hoppe-Seyler |volume=367 |issue= 8 |pages= 695-704 |year= 1986 |pmid= 3768139 |doi= }}
*{{cite journal | author=Mohr E, Hillers M, Ivell R, ''et al.'' |title=Expression of the vasopressin and oxytocin genes in human hypothalami. |journal=FEBS Lett. |volume=193 |issue= 1 |pages= 12-6 |year= 1986 |pmid= 4065330 |doi= }}
*{{cite journal | author=Brownstein MJ, Russell JT, Gainer H |title=Synthesis, transport, and release of posterior pituitary hormones. |journal=Science |volume=207 |issue= 4429 |pages= 373-8 |year= 1980 |pmid= 6153132 |doi= }}
*{{cite journal | author=Chauvet MT, Hurpet D, Chauvet J, Acher R |title=Identification of human neurophysins: complete amino acid sequences of MSEL- and VLDV-neurophysins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 10 |pages= 2839-43 |year= 1983 |pmid= 6574452 |doi= }}
*{{cite journal | author=Schlesinger DH, Audhya TK |title=A comparative study of mammalian neurophysin protein sequences. |journal=FEBS Lett. |volume=128 |issue= 2 |pages= 325-8 |year= 1981 |pmid= 7262323 |doi= }}
*{{cite journal | author=Alves SE, Lopez V, McEwen BS, Weiland NG |title=Differential colocalization of estrogen receptor beta (ERbeta) with oxytocin and vasopressin in the paraventricular and supraoptic nuclei of the female rat brain: an immunocytochemical study. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 6 |pages= 3281-6 |year= 1998 |pmid= 9501254 |doi= }}
*{{cite journal | author=Frayne J, Nicholson HD |title=Localization of oxytocin receptors in the human and macaque monkey male reproductive tracts: evidence for a physiological role of oxytocin in the male. |journal=Mol. Hum. Reprod. |volume=4 |issue= 6 |pages= 527-32 |year= 1998 |pmid= 9665335 |doi= }}
*{{cite journal | author=Copland JA, Jeng YJ, Strakova Z, ''et al.'' |title=Demonstration of functional oxytocin receptors in human breast Hs578T cells and their up-regulation through a protein kinase C-dependent pathway. |journal=Endocrinology |volume=140 |issue= 5 |pages= 2258-67 |year= 1999 |pmid= 10218979 |doi= }}
*{{cite journal | author=Politowska E, Czaplewski C, Ciarkowski J |title=Molecular modeling of the oxytocin receptor/bioligand interactions. |journal=Acta Biochim. Pol. |volume=46 |issue= 3 |pages= 581-90 |year= 2000 |pmid= 10698266 |doi= }}
*{{cite journal | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{cite journal | author=Petersson M, Lagumdzija A, Stark A, Bucht E |title=Oxytocin stimulates proliferation of human osteoblast-like cells. |journal=Peptides |volume=23 |issue= 6 |pages= 1121-6 |year= 2003 |pmid= 12126740 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PAWR... {November 19, 2007 12:17:49 AM PST}
- SEARCH REDIRECT: Control Box Found: PAWR {November 19, 2007 12:18:22 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:18:25 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:18:25 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:18:25 AM PST}
- UPDATED: Updated protein page: PAWR {November 19, 2007 12:18:33 AM PST}
- INFO: Beginning work on PIK3CB... {November 19, 2007 12:18:33 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:19:13 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 = Phosphoinositide-3-kinase, catalytic, beta polypeptide
| HGNCid = 8976
| Symbol = PIK3CB
| AltSymbols =; PI3K; DKFZp779K1237; MGC133043; PI3Kbeta; PIK3C1; p110-BETA
| OMIM = 602925
| ECnumber =
| Homologene = 21250
| MGIid = 1922019
| GeneAtlas_image1 = PBB_GE_PIK3CB_212688_at_tn.png
| GeneAtlas_image2 = PBB_GE_PIK3CB_217620_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004428 |text = inositol or phosphatidylinositol kinase activity}} {{GNF_GO|id=GO:0016303 |text = 1-phosphatidylinositol-3-kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0043560 |text = insulin receptor substrate binding}} {{GNF_GO|id=GO:0046934 |text = phosphatidylinositol-4,5-bisphosphate 3-kinase activity}}
| Component = {{GNF_GO|id=GO:0005942 |text = phosphoinositide 3-kinase complex}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0000187 |text = activation of MAPK activity}} {{GNF_GO|id=GO:0001952 |text = regulation of cell-matrix adhesion}} {{GNF_GO|id=GO:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0007156 |text = homophilic cell adhesion}} {{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:0030168 |text = platelet activation}} {{GNF_GO|id=GO:0040016 |text = embryonic cleavage}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5291
| Hs_Ensembl = ENSG00000051382
| Hs_RefseqProtein = NP_006210
| Hs_RefseqmRNA = NM_006219
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 139856921
| Hs_GenLoc_end = 139960875
| Hs_Uniprot = P42338
| Mm_EntrezGene = 74769
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_029094
| Mm_RefseqProtein = NP_083370
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Phosphoinositide-3-kinase, catalytic, beta polypeptide''', also known as '''PIK3CB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PIK3CB phosphoinositide-3-kinase, catalytic, beta polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5291| 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 = Phosphoinositide 3-kinases (PI3Ks) phosphorylate the 3-prime OH position of the inositol ring of inositol lipids. They have been implicated as participants in signaling pathways regulating cell growth by virtue of their activation in response to various mitogenic stimuli. PI3Ks are composed of a 110-kD catalytic subunit, such as PIK3CB, and an 85-kD adaptor subunit (Hu et al., 1993).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: PIK3CB phosphoinositide-3-kinase, catalytic, beta polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5291| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Katada T, Kurosu H, Okada T, ''et al.'' |title=Synergistic activation of a family of phosphoinositide 3-kinase via G-protein coupled and tyrosine kinase-related receptors. |journal=Chem. Phys. Lipids |volume=98 |issue= 1-2 |pages= 79-86 |year= 1999 |pmid= 10358930 |doi= }}
*{{cite journal | author=Lee C, Liu QH, Tomkowicz B, ''et al.'' |title=Macrophage activation through CCR5- and CXCR4-mediated gp120-elicited signaling pathways. |journal=J. Leukoc. Biol. |volume=74 |issue= 5 |pages= 676-82 |year= 2004 |pmid= 12960231 |doi= 10.1189/jlb.0503206 }}
*{{cite journal | author=Carpenter CL, Duckworth BC, Auger KR, ''et al.'' |title=Purification and characterization of phosphoinositide 3-kinase from rat liver. |journal=J. Biol. Chem. |volume=265 |issue= 32 |pages= 19704-11 |year= 1991 |pmid= 2174051 |doi= }}
*{{cite journal | author=Bonnefoy-Bérard N, Liu YC, von Willebrand M, ''et al.'' |title=Inhibition of phosphatidylinositol 3-kinase activity by association with 14-3-3 proteins in T cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 22 |pages= 10142-6 |year= 1995 |pmid= 7479742 |doi= }}
*{{cite journal | author=Hu P, Schlessinger J |title=Direct association of p110 beta phosphatidylinositol 3-kinase with p85 is mediated by an N-terminal fragment of p110 beta. |journal=Mol. Cell. Biol. |volume=14 |issue= 4 |pages= 2577-83 |year= 1994 |pmid= 8139559 |doi= }}
*{{cite journal | author=Hu P, Mondino A, Skolnik EY, Schlessinger J |title=Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85. |journal=Mol. Cell. Biol. |volume=13 |issue= 12 |pages= 7677-88 |year= 1994 |pmid= 8246984 |doi= }}
*{{cite journal | author=Milani D, Mazzoni M, Borgatti P, ''et al.'' |title=Extracellular human immunodeficiency virus type-1 Tat protein activates phosphatidylinositol 3-kinase in PC12 neuronal cells. |journal=J. Biol. Chem. |volume=271 |issue= 38 |pages= 22961-4 |year= 1996 |pmid= 8798481 |doi= }}
*{{cite journal | author=Mazerolles F, Barbat C, Fischer A |title=Down-regulation of LFA-1-mediated T cell adhesion induced by the HIV envelope glycoprotein gp160 requires phosphatidylinositol-3-kinase activity. |journal=Eur. J. Immunol. |volume=27 |issue= 9 |pages= 2457-65 |year= 1997 |pmid= 9341793 |doi= }}
*{{cite journal | author=Borgatti P, Zauli G, Colamussi ML, ''et al.'' |title=Extracellular HIV-1 Tat protein activates phosphatidylinositol 3- and Akt/PKB kinases in CD4+ T lymphoblastoid Jurkat cells. |journal=Eur. J. Immunol. |volume=27 |issue= 11 |pages= 2805-11 |year= 1998 |pmid= 9394803 |doi= }}
*{{cite journal | author=Borgatti P, Zauli G, Cantley LC, Capitani S |title=Extracellular HIV-1 Tat protein induces a rapid and selective activation of protein kinase C (PKC)-alpha, and -epsilon and -zeta isoforms in PC12 cells. |journal=Biochem. Biophys. Res. Commun. |volume=242 |issue= 2 |pages= 332-7 |year= 1998 |pmid= 9446795 |doi= }}
*{{cite journal | author=Milani D, Mazzoni M, Zauli G, ''et al.'' |title=HIV-1 Tat induces tyrosine phosphorylation of p125FAK and its association with phosphoinositide 3-kinase in PC12 cells. |journal=AIDS |volume=12 |issue= 11 |pages= 1275-84 |year= 1998 |pmid= 9708406 |doi= }}
*{{cite journal | author=Jauliac S, Mazerolles F, Jabado N, ''et al.'' |title=Ligands of CD4 inhibit the association of phospholipase Cgamma1 with phosphoinositide 3 kinase in T cells: regulation of this association by the phosphoinositide 3 kinase activity. |journal=Eur. J. Immunol. |volume=28 |issue= 10 |pages= 3183-91 |year= 1998 |pmid= 9808187 |doi= }}
*{{cite journal | author=Graness A, Adomeit A, Heinze R, ''et al.'' |title=A novel mitogenic signaling pathway of bradykinin in the human colon carcinoma cell line SW-480 involves sequential activation of a Gq/11 protein, phosphatidylinositol 3-kinase beta, and protein kinase Cepsilon. |journal=J. Biol. Chem. |volume=273 |issue= 48 |pages= 32016-22 |year= 1998 |pmid= 9822674 |doi= }}
*{{cite journal | author=Sotsios Y, Whittaker GC, Westwick J, Ward SG |title=The CXC chemokine stromal cell-derived factor activates a Gi-coupled phosphoinositide 3-kinase in T lymphocytes. |journal=J. Immunol. |volume=163 |issue= 11 |pages= 5954-63 |year= 1999 |pmid= 10570282 |doi= }}
*{{cite journal | author=Park IW, Wang JF, Groopman JE |title=HIV-1 Tat promotes monocyte chemoattractant protein-1 secretion followed by transmigration of monocytes. |journal=Blood |volume=97 |issue= 2 |pages= 352-8 |year= 2001 |pmid= 11154208 |doi= }}
*{{cite journal | author=Zauli G, Milani D, Mirandola P, ''et al.'' |title=HIV-1 Tat protein down-regulates CREB transcription factor expression in PC12 neuronal cells through a phosphatidylinositol 3-kinase/AKT/cyclic nucleoside phosphodiesterase pathway. |journal=FASEB J. |volume=15 |issue= 2 |pages= 483-91 |year= 2001 |pmid= 11156964 |doi= 10.1096/fj.00-0354com }}
*{{cite journal | author=Yang H, Wang X, Raizada MK |title=Characterization of signal transduction pathway in neurotropic action of angiotensin II in brain neurons. |journal=Endocrinology |volume=142 |issue= 8 |pages= 3502-11 |year= 2001 |pmid= 11459796 |doi= }}
*{{cite journal | author=Steták A, Csermely P, Ullrich A, Kéri G |title=Physical and functional interactions between protein tyrosine phosphatase alpha, PI 3-kinase, and PKCdelta. |journal=Biochem. Biophys. Res. Commun. |volume=288 |issue= 3 |pages= 564-72 |year= 2001 |pmid= 11676480 |doi= 10.1006/bbrc.2001.5811 }}
*{{cite journal | author=Ueki K, Yballe CM, Brachmann SM, ''et al.'' |title=Increased insulin sensitivity in mice lacking p85beta subunit of phosphoinositide 3-kinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 1 |pages= 419-24 |year= 2002 |pmid= 11752399 |doi= 10.1073/pnas.012581799 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PPIB... {November 19, 2007 12:19:13 AM PST}
- SEARCH REDIRECT: Control Box Found: PPIB {November 19, 2007 12:19:49 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:19:50 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:19:50 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:19:50 AM PST}
- UPDATED: Updated protein page: PPIB {November 19, 2007 12:19:56 AM PST}
- INFO: Beginning work on PPT1... {November 19, 2007 12:19:56 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:20:21 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_PPT1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1eh5.
| PDB = {{PDB2|1eh5}}, {{PDB2|1ei9}}, {{PDB2|1exw}}
| Name = Palmitoyl-protein thioesterase 1 (ceroid-lipofuscinosis, neuronal 1, infantile)
| HGNCid = 9325
| Symbol = PPT1
| AltSymbols =; CLN1; INCL; PPT
| OMIM = 600722
| ECnumber =
| Homologene = 7488
| MGIid = 1298204
| GeneAtlas_image1 = PBB_GE_PPT1_200975_at_tn.png
| Function = {{GNF_GO|id=GO:0008474 |text = palmitoyl-(protein) hydrolase activity}} {{GNF_GO|id=GO:0016290 |text = palmitoyl-CoA hydrolase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0008021 |text = synaptic vesicle}} {{GNF_GO|id=GO:0030424 |text = axon}} {{GNF_GO|id=GO:0045121 |text = lipid raft}}
| Process = {{GNF_GO|id=GO:0002084 |text = protein depalmitoylation}} {{GNF_GO|id=GO:0006309 |text = DNA fragmentation during apoptosis}} {{GNF_GO|id=GO:0006464 |text = protein modification process}} {{GNF_GO|id=GO:0006898 |text = receptor-mediated endocytosis}} {{GNF_GO|id=GO:0006907 |text = pinocytosis}} {{GNF_GO|id=GO:0007042 |text = lysosomal lumen acidification}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0007420 |text = brain development}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0015031 |text = protein transport}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}} {{GNF_GO|id=GO:0030149 |text = sphingolipid catabolic process}} {{GNF_GO|id=GO:0030163 |text = protein catabolic process}} {{GNF_GO|id=GO:0030308 |text = negative regulation of cell growth}} {{GNF_GO|id=GO:0031579 |text = lipid raft organization and biogenesis}} {{GNF_GO|id=GO:0043524 |text = negative regulation of neuron apoptosis}} {{GNF_GO|id=GO:0048260 |text = positive regulation of receptor mediated endocytosis}} {{GNF_GO|id=GO:0048549 |text = positive regulation of pinocytosis}} {{GNF_GO|id=GO:0048666 |text = neuron development}} {{GNF_GO|id=GO:0050803 |text = regulation of synapse structure and activity}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}} {{GNF_GO|id=GO:0051181 |text = cofactor transport}} {{GNF_GO|id=GO:0051186 |text = cofactor metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5538
| Hs_Ensembl = ENSG00000131238
| Hs_RefseqProtein = NP_000301
| Hs_RefseqmRNA = NM_000310
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 40310964
| Hs_GenLoc_end = 40335962
| Hs_Uniprot = P50897
| Mm_EntrezGene = 19063
| Mm_Ensembl = ENSMUSG00000028657
| Mm_RefseqmRNA = NM_008917
| Mm_RefseqProtein = NP_032943
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 122338549
| Mm_GenLoc_end = 122361381
| Mm_Uniprot = Q3TAR8
}}
}}
'''Palmitoyl-protein thioesterase 1 (ceroid-lipofuscinosis, neuronal 1, infantile)''', also known as '''PPT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PPT1 palmitoyl-protein thioesterase 1 (ceroid-lipofuscinosis, neuronal 1, infantile)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5538| 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 = Palmitoyl-protein thioesterase (PPT) is a small glycoprotein that removes palmitate groups from cysteine residues in lipid-modified proteins. PPT is thought to be involved in the catabolism of lipid-modified proteins (Camp et al., 1994).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: PPT1 palmitoyl-protein thioesterase 1 (ceroid-lipofuscinosis, neuronal 1, infantile)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5538| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Dawson G, Cho S |title=Batten's disease: clues to neuronal protein catabolism in lysosomes. |journal=J. Neurosci. Res. |volume=60 |issue= 2 |pages= 133-40 |year= 2000 |pmid= 10740217 |doi= }}
*{{cite journal | author=Weimer JM, Kriscenski-Perry E, Elshatory Y, Pearce DA |title=The neuronal ceroid lipofuscinoses: mutations in different proteins result in similar disease. |journal=Neuromolecular Med. |volume=1 |issue= 2 |pages= 111-24 |year= 2002 |pmid= 12025857 |doi= }}
*{{cite journal | author=Hofmann SL, Atashband A, Cho SK, ''et al.'' |title=Neuronal ceroid lipofuscinoses caused by defects in soluble lysosomal enzymes (CLN1 and CLN2). |journal=Curr. Mol. Med. |volume=2 |issue= 5 |pages= 423-37 |year= 2003 |pmid= 12125808 |doi= }}
*{{cite journal | author=Vesa J, Hellsten E, Verkruyse LA, ''et al.'' |title=Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis. |journal=Nature |volume=376 |issue= 6541 |pages= 584-7 |year= 1995 |pmid= 7637805 |doi= 10.1038/376584a0 }}
*{{cite journal | author=Camp LA, Verkruyse LA, Afendis SJ, ''et al.'' |title=Molecular cloning and expression of palmitoyl-protein thioesterase. |journal=J. Biol. Chem. |volume=269 |issue= 37 |pages= 23212-9 |year= 1994 |pmid= 7916016 |doi= }}
*{{cite journal | author=Hellsten E, Vesa J, Speer MC, ''et al.'' |title=Refined assignment of the infantile neuronal ceroid lipofuscinosis (INCL, CLN1) locus at 1p32: incorporation of linkage disequilibrium in multipoint analysis. |journal=Genomics |volume=16 |issue= 3 |pages= 720-5 |year= 1993 |pmid= 8325646 |doi= 10.1006/geno.1993.1253 }}
*{{cite journal | author=Crews CM, Lane WS, Schreiber SL |title=Didemnin binds to the protein palmitoyl thioesterase responsible for infantile neuronal ceroid lipofuscinosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 9 |pages= 4316-9 |year= 1996 |pmid= 8633062 |doi= }}
*{{cite journal | author=Schriner JE, Yi W, Hofmann SL |title=cDNA and genomic cloning of human palmitoyl-protein thioesterase (PPT), the enzyme defective in infantile neuronal ceroid lipofuscinosis. |journal=Genomics |volume=34 |issue= 3 |pages= 317-22 |year= 1996 |pmid= 8786130 |doi= 10.1006/geno.1996.0292 }}
*{{cite journal | author=Lu JY, Verkruyse LA, Hofmann SL |title=Lipid thioesters derived from acylated proteins accumulate in infantile neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by recombinant palmitoyl-protein thioesterase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 19 |pages= 10046-50 |year= 1996 |pmid= 8816748 |doi= }}
*{{cite journal | author=Hellsten E, Vesa J, Olkkonen VM, ''et al.'' |title=Human palmitoyl protein thioesterase: evidence for lysosomal targeting of the enzyme and disturbed cellular routing in infantile neuronal ceroid lipofuscinosis. |journal=EMBO J. |volume=15 |issue= 19 |pages= 5240-5 |year= 1996 |pmid= 8895569 |doi= }}
*{{cite journal | author=Mitchison HM, Hofmann SL, Becerra CH, ''et al.'' |title=Mutations in the palmitoyl-protein thioesterase gene (PPT; CLN1) causing juvenile neuronal ceroid lipofuscinosis with granular osmiophilic deposits. |journal=Hum. Mol. Genet. |volume=7 |issue= 2 |pages= 291-7 |year= 1998 |pmid= 9425237 |doi= }}
*{{cite journal | author=Santorelli FM, Bertini E, Petruzzella V, ''et al.'' |title=A novel insertion mutation (A169i) in the CLN1 gene is associated with infantile neuronal ceroid lipofuscinosis in an Italian patient. |journal=Biochem. Biophys. Res. Commun. |volume=245 |issue= 2 |pages= 519-22 |year= 1998 |pmid= 9571187 |doi= }}
*{{cite journal | author=Das AK, Becerra CH, Yi W, ''et al.'' |title=Molecular genetics of palmitoyl-protein thioesterase deficiency in the U.S. |journal=J. Clin. Invest. |volume=102 |issue= 2 |pages= 361-70 |year= 1998 |pmid= 9664077 |doi= }}
*{{cite journal | author=de Vries BB, Kleijer WJ, Keulemans JL, ''et al.'' |title=First-trimester diagnosis of infantile neuronal ceroid lipofuscinosis (INCL) using PPT enzyme assay and CLN1 mutation analysis. |journal=Prenat. Diagn. |volume=19 |issue= 6 |pages= 559-62 |year= 1999 |pmid= 10416973 |doi= }}
*{{cite journal | author=Cho S, Dawson PE, Dawson G |title=In vitro depalmitoylation of neurospecific peptides: implication for infantile neuronal ceroid lipofuscinosis. |journal=J. Neurosci. Res. |volume=59 |issue= 1 |pages= 32-8 |year= 2000 |pmid= 10658183 |doi= }}
*{{cite journal | author=Cho S, Dawson G |title=Palmitoyl protein thioesterase 1 protects against apoptosis mediated by Ras-Akt-caspase pathway in neuroblastoma cells. |journal=J. Neurochem. |volume=74 |issue= 4 |pages= 1478-88 |year= 2000 |pmid= 10737604 |doi= }}
*{{cite journal | author=Heinonen O, Salonen T, Jalanko A, ''et al.'' |title=CLN-1 and CLN-5, genes for infantile and variant late infantile neuronal ceroid lipofuscinoses, are expressed in the embryonic human brain. |journal=J. Comp. Neurol. |volume=426 |issue= 3 |pages= 406-12 |year= 2000 |pmid= 10992246 |doi= }}
*{{cite journal | author=Cho S, Dawson PE, Dawson G |title=Antisense palmitoyl protein thioesterase 1 (PPT1) treatment inhibits PPT1 activity and increases cell death in LA-N-5 neuroblastoma cells. |journal=J. Neurosci. Res. |volume=62 |issue= 2 |pages= 234-40 |year= 2000 |pmid= 11020216 |doi= }}
*{{cite journal | author=Lehtovirta M, Kyttälä A, Eskelinen EL, ''et al.'' |title=Palmitoyl protein thioesterase (PPT) localizes into synaptosomes and synaptic vesicles in neurons: implications for infantile neuronal ceroid lipofuscinosis (INCL). |journal=Hum. Mol. Genet. |volume=10 |issue= 1 |pages= 69-75 |year= 2001 |pmid= 11136716 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSMB6... {November 19, 2007 12:20:21 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:20:49 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_PSMB6_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1iru.
| PDB = {{PDB2|1iru}}
| Name = Proteasome (prosome, macropain) subunit, beta type, 6
| HGNCid = 9543
| Symbol = PSMB6
| AltSymbols =; Y; DELTA; LMPY; MGC5169
| OMIM = 600307
| ECnumber =
| Homologene = 2092
| MGIid = 104880
| GeneAtlas_image1 = PBB_GE_PSMB6_208827_at_tn.png
| Function = {{GNF_GO|id=GO:0004298 |text = threonine endopeptidase activity}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005839 |text = proteasome core complex (sensu Eukaryota)}}
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5694
| Hs_Ensembl = ENSG00000142507
| Hs_RefseqProtein = NP_002789
| Hs_RefseqmRNA = NM_002798
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 4646397
| Hs_GenLoc_end = 4648756
| Hs_Uniprot = P28072
| Mm_EntrezGene = 19175
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_008946
| Mm_RefseqProtein = NP_032972
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Proteasome (prosome, macropain) subunit, beta type, 6''', also known as '''PSMB6''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMB6 proteasome (prosome, macropain) subunit, beta type, 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5694| 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 proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure 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. 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. This gene encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit in the proteasome. This catalytic subunit is not present in the immunoproteasome and is replaced by catalytic subunit 1i (proteasome beta 9 subunit).<ref name="entrez">{{cite web | title = Entrez Gene: PSMB6 proteasome (prosome, macropain) subunit, beta type, 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5694| 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=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=DeMartino GN, Orth K, McCullough ML, ''et al.'' |title=The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous. |journal=Biochim. Biophys. Acta |volume=1079 |issue= 1 |pages= 29-38 |year= 1991 |pmid= 1888762 |doi= }}
*{{cite journal | author=Lee LW, Moomaw CR, Orth K, ''et al.'' |title=Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome). |journal=Biochim. Biophys. Acta |volume=1037 |issue= 2 |pages= 178-85 |year= 1990 |pmid= 2306472 |doi= }}
*{{cite journal | author=Kristensen P, Johnsen AH, Uerkvitz W, ''et al.'' |title=Human proteasome subunits from 2-dimensional gels identified by partial sequencing. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 3 |pages= 1785-9 |year= 1995 |pmid= 7811265 |doi= }}
*{{cite journal | author=Akiyama K, Yokota K, Kagawa S, ''et al.'' |title=cDNA cloning and interferon gamma down-regulation of proteasomal subunits X and Y. |journal=Science |volume=265 |issue= 5176 |pages= 1231-4 |year= 1994 |pmid= 8066462 |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=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=Elenich LA, Nandi D, Kent AE, ''et al.'' |title=The complete primary structure of mouse 20S proteasomes. |journal=Immunogenetics |volume=49 |issue= 10 |pages= 835-42 |year= 1999 |pmid= 10436176 |doi= }}
*{{cite journal | author=Mulder LC, Muesing MA |title=Degradation of HIV-1 integrase by the N-end rule pathway. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29749-53 |year= 2000 |pmid= 10893419 |doi= 10.1074/jbc.M004670200 }}
*{{cite journal | author=Feng Y, Longo DL, Ferris DK |title=Polo-like kinase interacts with proteasomes and regulates their activity. |journal=Cell Growth Differ. |volume=12 |issue= 1 |pages= 29-37 |year= 2001 |pmid= 11205743 |doi= }}
*{{cite journal | author=Sheehy AM, Gaddis NC, Choi JD, Malim MH |title=Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. |journal=Nature |volume=418 |issue= 6898 |pages= 646-50 |year= 2002 |pmid= 12167863 |doi= 10.1038/nature00939 }}
*{{cite journal | author=Chen M, Rockel T, Steinweger G, ''et al.'' |title=Subcellular recruitment of fibrillarin to nucleoplasmic proteasomes: implications for processing of a nucleolar autoantigen. |journal=Mol. Biol. Cell |volume=13 |issue= 10 |pages= 3576-87 |year= 2003 |pmid= 12388758 |doi= 10.1091/mbc.02-05-0083 }}
*{{cite journal | author=Huang X, Seifert U, Salzmann U, ''et al.'' |title=The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing. |journal=J. Mol. Biol. |volume=323 |issue= 4 |pages= 771-82 |year= 2002 |pmid= 12419264 |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=Gaddis NC, Chertova E, Sheehy AM, ''et al.'' |title=Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions. |journal=J. Virol. |volume=77 |issue= 10 |pages= 5810-20 |year= 2003 |pmid= 12719574 |doi= }}
*{{cite journal | author=Lecossier D, Bouchonnet F, Clavel F, Hance AJ |title=Hypermutation of HIV-1 DNA in the absence of the Vif protein. |journal=Science |volume=300 |issue= 5622 |pages= 1112 |year= 2003 |pmid= 12750511 |doi= 10.1126/science.1083338 }}
*{{cite journal | author=Zhang H, Yang B, Pomerantz RJ, ''et al.'' |title=The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. |journal=Nature |volume=424 |issue= 6944 |pages= 94-8 |year= 2003 |pmid= 12808465 |doi= 10.1038/nature01707 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSMD9... {November 19, 2007 12:20:49 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:21:11 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 = Proteasome (prosome, macropain) 26S subunit, non-ATPase, 9
| HGNCid = 9567
| Symbol = PSMD9
| AltSymbols =; MGC8644; p27
| OMIM = 603146
| ECnumber =
| Homologene = 2106
| MGIid = 1914401
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005838 |text = proteasome regulatory particle (sensu Eukaryota)}}
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5715
| Hs_Ensembl = ENSG00000110801
| Hs_RefseqProtein = NP_002804
| Hs_RefseqmRNA = NM_002813
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 120811029
| Hs_GenLoc_end = 120840153
| Hs_Uniprot = O00233
| Mm_EntrezGene = 67151
| Mm_Ensembl = ENSMUSG00000029440
| Mm_RefseqmRNA = NM_026000
| Mm_RefseqProtein = NP_080276
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 123488864
| Mm_GenLoc_end = 123510734
| Mm_Uniprot = Q3THC1
}}
}}
'''Proteasome (prosome, macropain) 26S subunit, non-ATPase, 9''', also known as '''PSMD9''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMD9 proteasome (prosome, macropain) 26S subunit, non-ATPase, 9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5715| 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. This gene encodes a non-ATPase subunit of the 19S regulator.<ref name="entrez">{{cite web | title = Entrez Gene: PSMD9 proteasome (prosome, macropain) 26S subunit, non-ATPase, 9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5715| 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=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=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=Watanabe TK, Saito A, Suzuki M, ''et al.'' |title=cDNA cloning and characterization of a human proteasomal modulator subunit, p27 (PSMD9). |journal=Genomics |volume=50 |issue= 2 |pages= 241-50 |year= 1998 |pmid= 9653651 |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=Thomas MK, Yao KM, Tenser MS, ''et al.'' |title=Bridge-1, a novel PDZ-domain coactivator of E2A-mediated regulation of insulin gene transcription. |journal=Mol. Cell. Biol. |volume=19 |issue= 12 |pages= 8492-504 |year= 2000 |pmid= 10567574 |doi= }}
*{{cite journal | author=Tanahashi N, Murakami Y, Minami Y, ''et al.'' |title=Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis. |journal=J. Biol. Chem. |volume=275 |issue= 19 |pages= 14336-45 |year= 2000 |pmid= 10799514 |doi= }}
*{{cite journal | author=Mulder LC, Muesing MA |title=Degradation of HIV-1 integrase by the N-end rule pathway. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29749-53 |year= 2000 |pmid= 10893419 |doi= 10.1074/jbc.M004670200 }}
*{{cite journal | author=Ciarallo S, Subramaniam V, Hung W, ''et al.'' |title=Altered p27(Kip1) phosphorylation, localization, and function in human epithelial cells resistant to transforming growth factor beta-mediated G(1) arrest. |journal=Mol. Cell. Biol. |volume=22 |issue= 9 |pages= 2993-3002 |year= 2002 |pmid= 11940657 |doi= }}
*{{cite journal | author=Sheehy AM, Gaddis NC, Choi JD, Malim MH |title=Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. |journal=Nature |volume=418 |issue= 6898 |pages= 646-50 |year= 2002 |pmid= 12167863 |doi= 10.1038/nature00939 }}
*{{cite journal | author=Huang X, Seifert U, Salzmann U, ''et al.'' |title=The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing. |journal=J. Mol. Biol. |volume=323 |issue= 4 |pages= 771-82 |year= 2002 |pmid= 12419264 |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=Gaddis NC, Chertova E, Sheehy AM, ''et al.'' |title=Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions. |journal=J. Virol. |volume=77 |issue= 10 |pages= 5810-20 |year= 2003 |pmid= 12719574 |doi= }}
*{{cite journal | author=Lecossier D, Bouchonnet F, Clavel F, Hance AJ |title=Hypermutation of HIV-1 DNA in the absence of the Vif protein. |journal=Science |volume=300 |issue= 5622 |pages= 1112 |year= 2003 |pmid= 12750511 |doi= 10.1126/science.1083338 }}
*{{cite journal | author=Hedberg Y, Ljungberg B, Roos G, Landberg G |title=Expression of cyclin D1, D3, E, and p27 in human renal cell carcinoma analysed by tissue microarray. |journal=Br. J. Cancer |volume=88 |issue= 9 |pages= 1417-23 |year= 2003 |pmid= 12778072 |doi= 10.1038/sj.bjc.6600922 }}
*{{cite journal | author=Zhang H, Yang B, Pomerantz RJ, ''et al.'' |title=The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. |journal=Nature |volume=424 |issue= 6944 |pages= 94-8 |year= 2003 |pmid= 12808465 |doi= 10.1038/nature01707 }}
*{{cite journal | author=Mangeat B, Turelli P, Caron G, ''et al.'' |title=Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. |journal=Nature |volume=424 |issue= 6944 |pages= 99-103 |year= 2003 |pmid= 12808466 |doi= 10.1038/nature01709 }}
*{{cite journal | author=Harris RS, Bishop KN, Sheehy AM, ''et al.'' |title=DNA deamination mediates innate immunity to retroviral infection. |journal=Cell |volume=113 |issue= 6 |pages= 803-9 |year= 2003 |pmid= 12809610 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PTS... {November 19, 2007 12:21:11 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:21:33 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 =
| image_source =
| PDB =
| Name = 6-pyruvoyltetrahydropterin synthase
| HGNCid = 9689
| Symbol = PTS
| AltSymbols =; PTPS
| OMIM = 261640
| ECnumber =
| Homologene = 268
| MGIid = 1338783
| GeneAtlas_image1 = PBB_GE_PTS_209694_at_tn.png
| Function = {{GNF_GO|id=GO:0003874 |text = 6-pyruvoyltetrahydropterin synthase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016829 |text = lyase activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0006520 |text = amino acid metabolic process}} {{GNF_GO|id=GO:0006559 |text = L-phenylalanine catabolic process}} {{GNF_GO|id=GO:0006729 |text = tetrahydrobiopterin biosynthetic process}} {{GNF_GO|id=GO:0007417 |text = central nervous system development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5805
| Hs_Ensembl = ENSG00000150787
| Hs_RefseqProtein = NP_000308
| Hs_RefseqmRNA = NM_000317
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 111602309
| Hs_GenLoc_end = 111609903
| Hs_Uniprot = Q03393
| Mm_EntrezGene = 19286
| Mm_Ensembl = ENSMUSG00000032067
| Mm_RefseqmRNA = NM_011220
| Mm_RefseqProtein = NP_035350
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 50273848
| Mm_GenLoc_end = 50280880
| Mm_Uniprot = Q9R1Z7
}}
}}
'''6-pyruvoyltetrahydropterin synthase''', also known as '''PTS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTS 6-pyruvoyltetrahydropterin synthase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5805| 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=Werner ER, Werner-Felmayer G, Fuchs D, ''et al.'' |title=Biochemistry and function of pteridine synthesis in human and murine macrophages. |journal=Pathobiology |volume=59 |issue= 4 |pages= 276-9 |year= 1991 |pmid= 1883524 |doi= }}
*{{cite journal | author=Thöny B, Blau N |title=Mutations in the GTP cyclohydrolase I and 6-pyruvoyl-tetrahydropterin synthase genes. |journal=Hum. Mutat. |volume=10 |issue= 1 |pages= 11-20 |year= 1997 |pmid= 9222755 |doi= 10.1002/(SICI)1098-1004(1997)10:1<11::AID-HUMU2>3.0.CO;2-P }}
*{{cite journal | author=Thöny B, Auerbach G, Blau N |title=Tetrahydrobiopterin biosynthesis, regeneration and functions. |journal=Biochem. J. |volume=347 Pt 1 |issue= |pages= 1-16 |year= 2000 |pmid= 10727395 |doi= }}
*{{cite journal | author=Thöny B, Leimbacher W, Bürgisser D, Heizmann CW |title=Human 6-pyruvoyltetrahydropterin synthase: cDNA cloning and heterologous expression of the recombinant enzyme. |journal=Biochem. Biophys. Res. Commun. |volume=189 |issue= 3 |pages= 1437-43 |year= 1993 |pmid= 1282802 |doi= }}
*{{cite journal | author=Scriver CR, Clow CL, Kaplan P, Niederwieser A |title=Hyperphenylalaninemia due to deficiency of 6-pyruvoyl tetrahydropterin synthase. Unusual gene dosage effect in heterozygotes. |journal=Hum. Genet. |volume=77 |issue= 2 |pages= 168-71 |year= 1987 |pmid= 3308682 |doi= }}
*{{cite journal | author=Oppliger T, Thöny B, Nar H, ''et al.'' |title=Structural and functional consequences of mutations in 6-pyruvoyltetrahydropterin synthase causing hyperphenylalaninemia in humans. Phosphorylation is a requirement for in vivo activity. |journal=J. Biol. Chem. |volume=270 |issue= 49 |pages= 29498-506 |year= 1996 |pmid= 7493990 |doi= }}
*{{cite journal | author=Ashida A, Owada M, Hatakeyama K |title=A missense mutation (A to G) of 6-pyruvoyltetrahydropterin synthase in tetrahydrobiopterin-deficient form of hyperphenylalaninemia. |journal=Genomics |volume=24 |issue= 2 |pages= 408-10 |year= 1995 |pmid= 7698774 |doi= 10.1006/geno.1994.1642 }}
*{{cite journal | author=Thöny B, Leimbacher W, Blau N, ''et al.'' |title=Hyperphenylalaninemia due to defects in tetrahydrobiopterin metabolism: molecular characterization of mutations in 6-pyruvoyl-tetrahydropterin synthase. |journal=Am. J. Hum. Genet. |volume=54 |issue= 5 |pages= 782-92 |year= 1994 |pmid= 8178819 |doi= }}
*{{cite journal | author=Thöny B, Heizmann CW, Mattei MG |title=Chromosomal location of two human genes encoding tetrahydrobiopterin-metabolizing enzymes: 6-pyruvoyl-tetrahydropterin synthase maps to 11q22.3-q23.3, and pterin-4 alpha-carbinolamine dehydratase maps to 10q22. |journal=Genomics |volume=19 |issue= 2 |pages= 365-8 |year= 1994 |pmid= 8188266 |doi= 10.1006/geno.1994.1071 }}
*{{cite journal | author=Ashida A, Hatakeyama K, Kagamiyama H |title=cDNA cloning, expression in Escherichia coli and purification of human 6-pyruvoyl-tetrahydropterin synthase. |journal=Biochem. Biophys. Res. Commun. |volume=195 |issue= 3 |pages= 1386-93 |year= 1993 |pmid= 8216273 |doi= 10.1006/bbrc.1993.2197 }}
*{{cite journal | author=Liu TT, Hsiao KJ |title=Identification of a common 6-pyruvoyl-tetrahydropterin synthase mutation at codon 87 in Chinese phenylketonuria caused by tetrahydrobiopterin synthesis deficiency. |journal=Hum. Genet. |volume=98 |issue= 3 |pages= 313-6 |year= 1996 |pmid= 8707300 |doi= }}
*{{cite journal | author=Kluge C, Brecevic L, Heizmann CW, ''et al.'' |title=Chromosomal localization, genomic structure and characterization of the human gene and a retropseudogene for 6-pyruvoyltetrahydropterin synthase. |journal=Eur. J. Biochem. |volume=240 |issue= 2 |pages= 477-84 |year= 1996 |pmid= 8841415 |doi= }}
*{{cite journal | author=Hanihara T, Inoue K, Kawanishi C, ''et al.'' |title=6-Pyruvoyl-tetrahydropterin synthase deficiency with generalized dystonia and diurnal fluctuation of symptoms: a clinical and molecular study. |journal=Mov. Disord. |volume=12 |issue= 3 |pages= 408-11 |year= 1997 |pmid= 9159737 |doi= 10.1002/mds.870120321 }}
*{{cite journal | author=Oppliger T, Thöny B, Kluge C, ''et al.'' |title=Identification of mutations causing 6-pyruvoyl-tetrahydropterin synthase deficiency in four Italian families. |journal=Hum. Mutat. |volume=10 |issue= 1 |pages= 25-35 |year= 1997 |pmid= 9222757 |doi= 10.1002/(SICI)1098-1004(1997)10:1<25::AID-HUMU4>3.0.CO;2-L }}
*{{cite journal | author=Liu TT, Hsiao KJ, Lu SF, ''et al.'' |title=Mutation analysis of the 6-pyruvoyl-tetrahydropterin synthase gene in Chinese hyperphenylalaninemia caused by tetrahydrobiopterin synthesis deficiency. |journal=Hum. Mutat. |volume=11 |issue= 1 |pages= 76-83 |year= 1998 |pmid= 9450907 |doi= 10.1002/(SICI)1098-1004(1998)11:1<76::AID-HUMU12>3.0.CO;2-W }}
*{{cite journal | author=Scherer-Oppliger T, Matasovic A, Laufs S, ''et al.'' |title=Dominant negative allele (N47D) in a compound heterozygote for a variant of 6-pyruvoyltetrahydropterin synthase deficiency causing transient hyperphenylalaninemia. |journal=Hum. Mutat. |volume=13 |issue= 4 |pages= 286-9 |year= 1999 |pmid= 10220141 |doi= 10.1002/(SICI)1098-1004(1999)13:4<286::AID-HUMU4>3.0.CO;2-C }}
*{{cite journal | author=Scherer-Oppliger T, Leimbacher W, Blau N, Thöny B |title=Serine 19 of human 6-pyruvoyltetrahydropterin synthase is phosphorylated by cGMP protein kinase II. |journal=J. Biol. Chem. |volume=274 |issue= 44 |pages= 31341-8 |year= 1999 |pmid= 10531334 |doi= }}
*{{cite journal | author=Kim ST, Lim DS, Canman CE, Kastan MB |title=Substrate specificities and identification of putative substrates of ATM kinase family members. |journal=J. Biol. Chem. |volume=274 |issue= 53 |pages= 37538-43 |year= 2000 |pmid= 10608806 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RAG1... {November 19, 2007 12:21:33 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:21:59 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_RAG1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1rmd.
| PDB = {{PDB2|1rmd}}
| Name = Recombination activating gene 1
| HGNCid = 9831
| Symbol = RAG1
| AltSymbols =; MGC43321; RNF74
| OMIM = 179615
| ECnumber =
| Homologene = 387
| MGIid = 97848
| GeneAtlas_image1 = PBB_GE_RAG1_206591_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004519 |text = endonuclease activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006310 |text = DNA recombination}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007516 |text = hemocyte development}} {{GNF_GO|id=GO:0030183 |text = B cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5896
| Hs_Ensembl = ENSG00000166349
| Hs_RefseqProtein = NP_000439
| Hs_RefseqmRNA = NM_000448
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 36546139
| Hs_GenLoc_end = 36557862
| Hs_Uniprot = P15918
| Mm_EntrezGene = 19373
| Mm_Ensembl = ENSMUSG00000061311
| Mm_RefseqmRNA = NM_009019
| Mm_RefseqProtein = NP_033045
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 101442512
| Mm_GenLoc_end = 101445634
| Mm_Uniprot = Q3TR87
}}
}}
'''Recombination activating gene 1''', also known as '''RAG1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RAG1 recombination activating gene 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5896| 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 linked genes RAG1 and RAG2 act together to activate immunoglobulin V-D-J recombination. RAG1 is involved in recognition of the DNA substrate.<ref name="entrez">{{cite web | title = Entrez Gene: RAG1 recombination activating gene 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5896| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kato M, Kimura H, Seki M, ''et al.'' |title=Omenn syndrome--review of several phenotypes of Omenn syndrome and RAG1/RAG2 mutations in Japan. |journal=Allergology international : official journal of the Japanese Society of Allergology |volume=55 |issue= 2 |pages= 115-9 |year= 2006 |pmid= 17075247 |doi= 10.2332/allergolint.55.115 }}
*{{cite journal | author=Sherrington PD, Forster A, Seawright A, ''et al.'' |title=Human RAG2, like RAG1, is on chromosome 11 band p13 and therefore not linked to ataxia telangiectasia complementation groups. |journal=Genes Chromosomes Cancer |volume=5 |issue= 4 |pages= 404-6 |year= 1993 |pmid= 1283330 |doi= }}
*{{cite journal | author=Blanquet V, Turleau C, Goossens M, Besmond C |title=Assignment of the human recombination activating gene 1 (RAG1) to the 14q21.3-q22.2 region. |journal=Genomics |volume=13 |issue= 2 |pages= 488-9 |year= 1992 |pmid= 1612612 |doi= }}
*{{cite journal | author=Schatz DG, Oettinger MA, Baltimore D |title=The V(D)J recombination activating gene, RAG-1. |journal=Cell |volume=59 |issue= 6 |pages= 1035-48 |year= 1990 |pmid= 2598259 |doi= }}
*{{cite journal | author=Cuomo CA, Kirch SA, Gyuris J, ''et al.'' |title=Rch1, a protein that specifically interacts with the RAG-1 recombination-activating protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 13 |pages= 6156-60 |year= 1994 |pmid= 8016130 |doi= }}
*{{cite journal | author=Cortes P, Ye ZS, Baltimore D |title=RAG-1 interacts with the repeated amino acid motif of the human homologue of the yeast protein SRP1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 16 |pages= 7633-7 |year= 1994 |pmid= 8052633 |doi= }}
*{{cite journal | author=Spanopoulou E, Cortes P, Shih C, ''et al.'' |title=Localization, interaction, and RNA binding properties of the V(D)J recombination-activating proteins RAG1 and RAG2. |journal=Immunity |volume=3 |issue= 6 |pages= 715-26 |year= 1996 |pmid= 8777717 |doi= }}
*{{cite journal | author=Schwarz K, Gauss GH, Ludwig L, ''et al.'' |title=RAG mutations in human B cell-negative SCID. |journal=Science |volume=274 |issue= 5284 |pages= 97-9 |year= 1996 |pmid= 8810255 |doi= }}
*{{cite journal | author=Nomdedéu JF, Lasa A, Seminago R, ''et al.'' |title=Two new variants of RAG-1 protein predicted by SSCP. |journal=Hum. Mutat. |volume=8 |issue= 2 |pages= 191-2 |year= 1996 |pmid= 8844221 |doi= 10.1002/(SICI)1098-1004(1996)8:2<191::AID-HUMU15>3.0.CO;2-Y }}
*{{cite journal | author=McMahan CJ, Sadofsky MJ, Schatz DG |title=Definition of a large region of RAG1 that is important for coimmunoprecipitation of RAG2. |journal=J. Immunol. |volume=158 |issue= 5 |pages= 2202-10 |year= 1997 |pmid= 9036966 |doi= }}
*{{cite journal | author=Zarrin AA, Fong I, Malkin L, ''et al.'' |title=Cloning and characterization of the human recombination activating gene 1 (RAG1) and RAG2 promoter regions. |journal=J. Immunol. |volume=159 |issue= 9 |pages= 4382-94 |year= 1997 |pmid= 9379036 |doi= }}
*{{cite journal | author=Villa A, Santagata S, Bozzi F, ''et al.'' |title=Partial V(D)J recombination activity leads to Omenn syndrome. |journal=Cell |volume=93 |issue= 5 |pages= 885-96 |year= 1998 |pmid= 9630231 |doi= }}
*{{cite journal | author=Aidinis V, Bonaldi T, Beltrame M, ''et al.'' |title=The RAG1 homeodomain recruits HMG1 and HMG2 to facilitate recombination signal sequence binding and to enhance the intrinsic DNA-bending activity of RAG1-RAG2. |journal=Mol. Cell. Biol. |volume=19 |issue= 10 |pages= 6532-42 |year= 2000 |pmid= 10490593 |doi= }}
*{{cite journal | author=Wada T, Takei K, Kudo M, ''et al.'' |title=Characterization of immune function and analysis of RAG gene mutations in Omenn syndrome and related disorders. |journal=Clin. Exp. Immunol. |volume=119 |issue= 1 |pages= 148-55 |year= 2000 |pmid= 10606976 |doi= }}
*{{cite journal | author=Villa A, Sobacchi C, Notarangelo LD, ''et al.'' |title=V(D)J recombination defects in lymphocytes due to RAG mutations: severe immunodeficiency with a spectrum of clinical presentations. |journal=Blood |volume=97 |issue= 1 |pages= 81-8 |year= 2001 |pmid= 11133745 |doi= }}
*{{cite journal | author=Murphy WJ, Eizirik E, Johnson WE, ''et al.'' |title=Molecular phylogenetics and the origins of placental mammals. |journal=Nature |volume=409 |issue= 6820 |pages= 614-8 |year= 2001 |pmid= 11214319 |doi= 10.1038/35054550 }}
*{{cite journal | author=Girschick HJ, Grammer AC, Nanki T, ''et al.'' |title=Expression of recombination activating genes 1 and 2 in peripheral B cells of patients with systemic lupus erythematosus. |journal=Arthritis Rheum. |volume=46 |issue= 5 |pages= 1255-63 |year= 2002 |pmid= 12115231 |doi= 10.1002/art.10264 }}
*{{cite journal | author=Mulero MC, Estivill C, Corral J, ''et al.'' |title=Sequence conservation of RAG-1 and RAG-2 genes in hematologic malignancies. |journal=Leukemia |volume=16 |issue= 8 |pages= 1571 |year= 2002 |pmid= 12145704 |doi= 10.1038/sj.leu.2402518 }}
*{{cite journal | author=Noordzij JG, de Bruin-Versteeg S, Verkaik NS, ''et al.'' |title=The immunophenotypic and immunogenotypic B-cell differentiation arrest in bone marrow of RAG-deficient SCID patients corresponds to residual recombination activities of mutated RAG proteins. |journal=Blood |volume=100 |issue= 6 |pages= 2145-52 |year= 2002 |pmid= 12200379 |doi= }}
*{{cite journal | author=Jin ZX, Kishi H, Wei XC, ''et al.'' |title=Lymphoid enhancer-binding factor-1 binds and activates the recombination-activating gene-2 promoter together with c-Myb and Pax-5 in immature B cells. |journal=J. Immunol. |volume=169 |issue= 7 |pages= 3783-92 |year= 2002 |pmid= 12244173 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RAG2... {November 19, 2007 12:21:59 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:22:20 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_RAG2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2a23.
| PDB = {{PDB2|2a23}}
| Name = Recombination activating gene 2
| HGNCid = 9832
| Symbol = RAG2
| AltSymbols =;
| OMIM = 179616
| ECnumber =
| Homologene = 7507
| MGIid = 97849
| GeneAtlas_image1 = PBB_GE_RAG2_215117_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004519 |text = endonuclease activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006310 |text = DNA recombination}} {{GNF_GO|id=GO:0016445 |text = somatic diversification of immunoglobulins}} {{GNF_GO|id=GO:0030183 |text = B cell differentiation}} {{GNF_GO|id=GO:0030217 |text = T cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5897
| Hs_Ensembl = ENSG00000175097
| Hs_RefseqProtein = NP_000527
| Hs_RefseqmRNA = NM_000536
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 36570071
| Hs_GenLoc_end = 36576362
| Hs_Uniprot = P55895
| Mm_EntrezGene = 19374
| Mm_Ensembl = ENSMUSG00000032864
| Mm_RefseqmRNA = NM_009020
| Mm_RefseqProtein = NP_033046
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 101425587
| Mm_GenLoc_end = 101433367
| Mm_Uniprot = Q542D1
}}
}}
'''Recombination activating gene 2''', also known as '''RAG2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RAG2 recombination activating gene 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5897| 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=Kato M, Kimura H, Seki M, ''et al.'' |title=Omenn syndrome--review of several phenotypes of Omenn syndrome and RAG1/RAG2 mutations in Japan. |journal=Allergology international : official journal of the Japanese Society of Allergology |volume=55 |issue= 2 |pages= 115-9 |year= 2006 |pmid= 17075247 |doi= 10.2332/allergolint.55.115 }}
*{{cite journal | author=Sherrington PD, Forster A, Seawright A, ''et al.'' |title=Human RAG2, like RAG1, is on chromosome 11 band p13 and therefore not linked to ataxia telangiectasia complementation groups. |journal=Genes Chromosomes Cancer |volume=5 |issue= 4 |pages= 404-6 |year= 1993 |pmid= 1283330 |doi= }}
*{{cite journal | author=Ichihara Y, Hirai M, Kurosawa Y |title=Sequence and chromosome assignment to 11p13-p12 of human RAG genes. |journal=Immunol. Lett. |volume=33 |issue= 3 |pages= 277-84 |year= 1992 |pmid= 1428003 |doi= }}
*{{cite journal | author=Bories JC, Cayuela JM, Loiseau P, Sigaux F |title=Expression of human recombination activating genes (RAG1 and RAG2) in neoplastic lymphoid cells: correlation with cell differentiation and antigen receptor expression. |journal=Blood |volume=78 |issue= 8 |pages= 2053-61 |year= 1991 |pmid= 1832998 |doi= }}
*{{cite journal | author=Lynch S, Kelleher D, McManus R, O'Farrelly C |title=RAG1 and RAG2 expression in human intestinal epithelium: evidence of extrathymic T cell differentiation. |journal=Eur. J. Immunol. |volume=25 |issue= 5 |pages= 1143-7 |year= 1995 |pmid= 7774617 |doi= }}
*{{cite journal | author=Hayakawa S, Saito S, Nemoto N, ''et al.'' |title=Expression of recombinase-activating genes (RAG-1 and 2) in human decidual mononuclear cells. |journal=J. Immunol. |volume=153 |issue= 11 |pages= 4934-9 |year= 1994 |pmid= 7963556 |doi= }}
*{{cite journal | author=Schwarz K, Gauss GH, Ludwig L, ''et al.'' |title=RAG mutations in human B cell-negative SCID. |journal=Science |volume=274 |issue= 5284 |pages= 97-9 |year= 1996 |pmid= 8810255 |doi= }}
*{{cite journal | author=McMahan CJ, Sadofsky MJ, Schatz DG |title=Definition of a large region of RAG1 that is important for coimmunoprecipitation of RAG2. |journal=J. Immunol. |volume=158 |issue= 5 |pages= 2202-10 |year= 1997 |pmid= 9036966 |doi= }}
*{{cite journal | author=Villa A, Santagata S, Bozzi F, ''et al.'' |title=Partial V(D)J recombination activity leads to Omenn syndrome. |journal=Cell |volume=93 |issue= 5 |pages= 885-96 |year= 1998 |pmid= 9630231 |doi= }}
*{{cite journal | author=Besmer E, Mansilla-Soto J, Cassard S, ''et al.'' |title=Hairpin coding end opening is mediated by RAG1 and RAG2 proteins. |journal=Mol. Cell |volume=2 |issue= 6 |pages= 817-28 |year= 1999 |pmid= 9885569 |doi= }}
*{{cite journal | author=Shockett PE, Schatz DG |title=DNA hairpin opening mediated by the RAG1 and RAG2 proteins. |journal=Mol. Cell. Biol. |volume=19 |issue= 6 |pages= 4159-66 |year= 1999 |pmid= 10330156 |doi= }}
*{{cite journal | author=Gomez CA, Ptaszek LM, Villa A, ''et al.'' |title=Mutations in conserved regions of the predicted RAG2 kelch repeats block initiation of V(D)J recombination and result in primary immunodeficiencies. |journal=Mol. Cell. Biol. |volume=20 |issue= 15 |pages= 5653-64 |year= 2000 |pmid= 10891502 |doi= }}
*{{cite journal | author=Girschick HJ, Grammer AC, Nanki T, ''et al.'' |title=RAG1 and RAG2 expression by B cell subsets from human tonsil and peripheral blood. |journal=J. Immunol. |volume=166 |issue= 1 |pages= 377-86 |year= 2001 |pmid= 11123315 |doi= }}
*{{cite journal | author=Williams CJ, Grandal I, Vesprini DJ, ''et al.'' |title=Irradiation promotes V(D)J joining and RAG-dependent neoplastic transformation in SCID T-cell precursors. |journal=Mol. Cell. Biol. |volume=21 |issue= 2 |pages= 400-13 |year= 2001 |pmid= 11134329 |doi= 10.1128/MCB.21.2.400-413.2001 }}
*{{cite journal | author=Murphy WJ, Eizirik E, Johnson WE, ''et al.'' |title=Molecular phylogenetics and the origins of placental mammals. |journal=Nature |volume=409 |issue= 6820 |pages= 614-8 |year= 2001 |pmid= 11214319 |doi= 10.1038/35054550 }}
*{{cite journal | author=Girschick HJ, Grammer AC, Nanki T, ''et al.'' |title=Expression of recombination activating genes 1 and 2 in peripheral B cells of patients with systemic lupus erythematosus. |journal=Arthritis Rheum. |volume=46 |issue= 5 |pages= 1255-63 |year= 2002 |pmid= 12115231 |doi= 10.1002/art.10264 }}
*{{cite journal | author=Mulero MC, Estivill C, Corral J, ''et al.'' |title=Sequence conservation of RAG-1 and RAG-2 genes in hematologic malignancies. |journal=Leukemia |volume=16 |issue= 8 |pages= 1571 |year= 2002 |pmid= 12145704 |doi= 10.1038/sj.leu.2402518 }}
*{{cite journal | author=Noordzij JG, de Bruin-Versteeg S, Verkaik NS, ''et al.'' |title=The immunophenotypic and immunogenotypic B-cell differentiation arrest in bone marrow of RAG-deficient SCID patients corresponds to residual recombination activities of mutated RAG proteins. |journal=Blood |volume=100 |issue= 6 |pages= 2145-52 |year= 2002 |pmid= 12200379 |doi= }}
*{{cite journal | author=Li TT, Han S, Cubbage M, Zheng B |title=Continued expression of recombination-activating genes and TCR gene recombination in human peripheral T cells. |journal=Eur. J. Immunol. |volume=32 |issue= 10 |pages= 2792-9 |year= 2002 |pmid= 12355431 |doi= 10.1002/1521-4141(2002010)32:10<2792::AID-IMMU2792>3.0.CO;2-I }}
*{{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 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RBBP7... {November 19, 2007 12:22:20 AM PST}
- SEARCH REDIRECT: Control Box Found: RBBP7 {November 19, 2007 12:22:49 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:22:51 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:22:51 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:22:51 AM PST}
- UPDATED: Updated protein page: RBBP7 {November 19, 2007 12:22:56 AM PST}
- INFO: Beginning work on RLN2... {November 19, 2007 12:22:57 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:23:26 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
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| 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 = PBB_Protein_RLN2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 6rlx.
| PDB = {{PDB2|6rlx}}
| Name = Relaxin 2
| HGNCid = 10027
| Symbol = RLN2
| AltSymbols =; H2; RLXH2; bA12D24.1.1; bA12D24.1.2
| OMIM = 179740
| ECnumber =
| Homologene = 55524
| MGIid = 97931
| GeneAtlas_image1 = PBB_GE_RLN2_214519_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0007565 |text = female pregnancy}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6019
| Hs_Ensembl = ENSG00000107014
| Hs_RefseqProtein = NP_005050
| Hs_RefseqmRNA = NM_005059
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 5289868
| Hs_GenLoc_end = 5294969
| Hs_Uniprot = P04090
| Mm_EntrezGene = 19773
| Mm_Ensembl = ENSMUSG00000039097
| Mm_RefseqmRNA = NM_011272
| Mm_RefseqProtein = NP_035402
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 29397695
| Mm_GenLoc_end = 29400593
| Mm_Uniprot = Q2M2Q1
}}
}}
'''Relaxin 2''', also known as '''RLN2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RLN2 relaxin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6019| 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 = Relaxins are known endocrine and autocrine/paracrine hormones, belonging to the insulin gene superfamily. In the human there are three non-allelic relaxin genes, RLN1, RLN2 and RLN3. RLN1 and RLN2 share high sequence homology. The active form of the encoded protein consists of an A chain and a B chain but their cleavage sites are not definitely described yet. Relaxin is produced by the ovary, and targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may have additional roles in enhancing sperm motility, regulating blood pressure, controlling heart rate and releasing oxytocin and vasopressin. There are two alternatively spliced transcript variants encoding different isoforms described for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: RLN2 relaxin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6019| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schwabe C, Büllesbach EE |title=Relaxin: structures, functions, promises, and nonevolution. |journal=FASEB J. |volume=8 |issue= 14 |pages= 1152-60 |year= 1994 |pmid= 7958621 |doi= }}
*{{cite journal | author=Winslow JW, Shih A, Bourell JH, ''et al.'' |title=Human seminal relaxin is a product of the same gene as human luteal relaxin. |journal=Endocrinology |volume=130 |issue= 5 |pages= 2660-8 |year= 1992 |pmid= 1572287 |doi= }}
*{{cite journal | author=Eigenbrot C, Randal M, Quan C, ''et al.'' |title=X-ray structure of human relaxin at 1.5 A. Comparison to insulin and implications for receptor binding determinants. |journal=J. Mol. Biol. |volume=221 |issue= 1 |pages= 15-21 |year= 1991 |pmid= 1656049 |doi= }}
*{{cite journal | author=Hansell DJ, Bryant-Greenwood GD, Greenwood FC |title=Expression of the human relaxin H1 gene in the decidua, trophoblast, and prostate. |journal=J. Clin. Endocrinol. Metab. |volume=72 |issue= 4 |pages= 899-904 |year= 1991 |pmid= 2005217 |doi= }}
*{{cite journal | author=Büllesbach EE, Schwabe C |title=Total synthesis of human relaxin and human relaxin derivatives by solid-phase peptide synthesis and site-directed chain combination. |journal=J. Biol. Chem. |volume=266 |issue= 17 |pages= 10754-61 |year= 1991 |pmid= 2040595 |doi= }}
*{{cite journal | author=Stults JT, Bourell JH, Canova-Davis E, ''et al.'' |title=Structural characterization by mass spectrometry of native and recombinant human relaxin. |journal=Biomed. Environ. Mass Spectrom. |volume=19 |issue= 11 |pages= 655-64 |year= 1991 |pmid= 2076464 |doi= }}
*{{cite journal | author=Hudson P, John M, Crawford R, ''et al.'' |title=Relaxin gene expression in human ovaries and the predicted structure of a human preprorelaxin by analysis of cDNA clones. |journal=EMBO J. |volume=3 |issue= 10 |pages= 2333-9 |year= 1985 |pmid= 6548702 |doi= }}
*{{cite journal | author=Crawford RJ, Hudson P, Shine J, ''et al.'' |title=Two human relaxin genes are on chromosome 9. |journal=EMBO J. |volume=3 |issue= 10 |pages= 2341-5 |year= 1985 |pmid= 6548703 |doi= }}
*{{cite journal | author=Bogic LV, Mandel M, Bryant-Greenwood GD |title=Relaxin gene expression in human reproductive tissues by in situ hybridization. |journal=J. Clin. Endocrinol. Metab. |volume=80 |issue= 1 |pages= 130-7 |year= 1995 |pmid= 7829601 |doi= }}
*{{cite journal | author=Tashima LS, Mazoujian G, Bryant-Greenwood GD |title=Human relaxins in normal, benign and neoplastic breast tissue. |journal=J. Mol. Endocrinol. |volume=12 |issue= 3 |pages= 351-64 |year= 1994 |pmid= 7916973 |doi= }}
*{{cite journal | author=Gunnersen JM, Fu P, Roche PJ, Tregear GW |title=Expression of human relaxin genes: characterization of a novel alternatively-spliced human relaxin mRNA species. |journal=Mol. Cell. Endocrinol. |volume=118 |issue= 1-2 |pages= 85-94 |year= 1996 |pmid= 8735594 |doi= }}
*{{cite journal | author=Veitia R, Laurent A, Quintana-Murci L, ''et al.'' |title=The INSL4 gene maps close to WI-5527 at 9p24.1-->p23.3 clustered with two relaxin genes and outside the critical region for the monosomy 9p syndrome. |journal=Cytogenet. Cell Genet. |volume=81 |issue= 3-4 |pages= 275-7 |year= 1998 |pmid= 9730618 |doi= }}
*{{cite journal | author=Garibay-Tupas JL, Csiszár K, Fox M, ''et al.'' |title=Analysis of the 5'-upstream regions of the human relaxin H1 and H2 genes and their chromosomal localization on chromosome 9p24.1 by radiation hybrid and breakpoint mapping. |journal=J. Mol. Endocrinol. |volume=23 |issue= 3 |pages= 355-65 |year= 2000 |pmid= 10601981 |doi= }}
*{{cite journal | author=Garibay-Tupas JL, Bao S, Kim MT, ''et al.'' |title=Isolation and analysis of the 3'-untranslated regions of the human relaxin H1 and H2 genes. |journal=J. Mol. Endocrinol. |volume=24 |issue= 2 |pages= 241-52 |year= 2000 |pmid= 10750025 |doi= }}
*{{cite journal | author=Armbruster FP, Grön HJ, Maier I, ''et al.'' |title=A sensitive homologous radioimmunoassay for human relaxin-2 (h-RLX-2) based on antibodies characterized by epitope mapping studies. |journal=Eur. J. Med. Res. |volume=6 |issue= 1 |pages= 1-9 |year= 2001 |pmid= 11313185 |doi= }}
*{{cite journal | author=Chen LM, Yang XW, Tang JG |title=[Expression, purification and characterization of human prorelaxin-like-protein H2 in Escherichia coli] |journal=Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao |volume=34 |issue= 5 |pages= 595-600 |year= 2002 |pmid= 12198562 |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=Sudo S, Kumagai J, Nishi S, ''et al.'' |title=H3 relaxin is a specific ligand for LGR7 and activates the receptor by interacting with both the ectodomain and the exoloop 2. |journal=J. Biol. Chem. |volume=278 |issue= 10 |pages= 7855-62 |year= 2003 |pmid= 12506116 |doi= 10.1074/jbc.M212457200 }}
*{{cite journal | author=Samuel CS, Sakai LY, Amento EP |title=Relaxin regulates fibrillin 2, but not fibrillin 1, mRNA and protein expression by human dermal fibroblasts and murine fetal skin. |journal=Arch. Biochem. Biophys. |volume=411 |issue= 1 |pages= 47-55 |year= 2003 |pmid= 12590922 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RNASE3... {November 19, 2007 12:23:26 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:23:51 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_RNASE3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dyt.
| PDB = {{PDB2|1dyt}}, {{PDB2|1h1h}}, {{PDB2|1qmt}}
| Name = Ribonuclease, RNase A family, 3 (eosinophil cationic protein)
| HGNCid = 10046
| Symbol = RNASE3
| AltSymbols =; ECP; RNS3
| OMIM = 131398
| ECnumber =
| Homologene = 48149
| MGIid = 1890465
| GeneAtlas_image1 = PBB_GE_RNASE3_206851_at_tn.png
| Function = {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0004519 |text = endonuclease activity}} {{GNF_GO|id=GO:0004522 |text = pancreatic ribonuclease activity}} {{GNF_GO|id=GO:0004540 |text = ribonuclease activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0006401 |text = RNA catabolic process}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6037
| Hs_Ensembl = ENSG00000169397
| Hs_RefseqProtein = NP_002926
| Hs_RefseqmRNA = NM_002935
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 20429402
| Hs_GenLoc_end = 20430347
| Hs_Uniprot = P12724
| Mm_EntrezGene = 93726
| Mm_Ensembl = ENSMUSG00000047222
| Mm_RefseqmRNA = NM_053113
| Mm_RefseqProtein = NP_444343
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 50177212
| Mm_GenLoc_end = 50178063
| Mm_Uniprot =
}}
}}
'''Ribonuclease, RNase A family, 3 (eosinophil cationic protein)''', also known as '''RNASE3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RNASE3 ribonuclease, RNase A family, 3 (eosinophil cationic protein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6037| 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=Abu-Ghazaleh RI, Dunnette SL, Loegering DA, ''et al.'' |title=Eosinophil granule proteins in peripheral blood granulocytes. |journal=J. Leukoc. Biol. |volume=52 |issue= 6 |pages= 611-8 |year= 1993 |pmid= 1464733 |doi= }}
*{{cite journal | author=Mastrianni DM, Eddy RL, Rosenberg HF, ''et al.'' |title=Localization of the human eosinophil Charcot-Leyden crystal protein (lysophospholipase) gene (CLC) to chromosome 19 and the human ribonuclease 2 (eosinophil-derived neurotoxin) and ribonuclease 3 (eosinophil cationic protein) genes (RNS2 and RNS3) to chromosome 14. |journal=Genomics |volume=13 |issue= 1 |pages= 240-2 |year= 1992 |pmid= 1577491 |doi= }}
*{{cite journal | author=Hamann KJ, Ten RM, Loegering DA, ''et al.'' |title=Structure and chromosome localization of the human eosinophil-derived neurotoxin and eosinophil cationic protein genes: evidence for intronless coding sequences in the ribonuclease gene superfamily. |journal=Genomics |volume=7 |issue= 4 |pages= 535-46 |year= 1990 |pmid= 2387583 |doi= }}
*{{cite journal | author=Rosenberg HF, Ackerman SJ, Tenen DG |title=Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity. |journal=J. Exp. Med. |volume=170 |issue= 1 |pages= 163-76 |year= 1989 |pmid= 2473157 |doi= }}
*{{cite journal | author=Gabay JE, Scott RW, Campanelli D, ''et al.'' |title=Antibiotic proteins of human polymorphonuclear leukocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 14 |pages= 5610-4 |year= 1989 |pmid= 2501794 |doi= }}
*{{cite journal | author=Barker RL, Loegering DA, Ten RM, ''et al.'' |title=Eosinophil cationic protein cDNA. Comparison with other toxic cationic proteins and ribonucleases. |journal=J. Immunol. |volume=143 |issue= 3 |pages= 952-5 |year= 1989 |pmid= 2745977 |doi= }}
*{{cite journal | author=Gleich GJ, Loegering DA, Bell MP, ''et al.'' |title=Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 10 |pages= 3146-50 |year= 1986 |pmid= 3458170 |doi= }}
*{{cite journal | author=Peters MS, Rodriguez M, Gleich GJ |title=Localization of human eosinophil granule major basic protein, eosinophil cationic protein, and eosinophil-derived neurotoxin by immunoelectron microscopy. |journal=Lab. Invest. |volume=54 |issue= 6 |pages= 656-62 |year= 1986 |pmid= 3520144 |doi= }}
*{{cite journal | author=Boix E, Nikolovski Z, Moiseyev GP, ''et al.'' |title=Kinetic and product distribution analysis of human eosinophil cationic protein indicates a subsite arrangement that favors exonuclease-type activity. |journal=J. Biol. Chem. |volume=274 |issue= 22 |pages= 15605-14 |year= 1999 |pmid= 10336457 |doi= }}
*{{cite journal | author=Boix E, Leonidas DD, Nikolovski Z, ''et al.'' |title=Crystal structure of eosinophil cationic protein at 2.4 A resolution. |journal=Biochemistry |volume=38 |issue= 51 |pages= 16794-801 |year= 2000 |pmid= 10606511 |doi= }}
*{{cite journal | author=Kampen GT, Stafford S, Adachi T, ''et al.'' |title=Eotaxin induces degranulation and chemotaxis of eosinophils through the activation of ERK2 and p38 mitogen-activated protein kinases. |journal=Blood |volume=95 |issue= 6 |pages= 1911-7 |year= 2000 |pmid= 10706854 |doi= }}
*{{cite journal | author=Mallorquí-Fernández G, Pous J, Peracaula R, ''et al.'' |title=Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 A resolution. |journal=J. Mol. Biol. |volume=300 |issue= 5 |pages= 1297-307 |year= 2000 |pmid= 10903870 |doi= 10.1006/jmbi.2000.3939 }}
*{{cite journal | author=Simon HU, Weber M, Becker E, ''et al.'' |title=Eosinophils maintain their capacity to signal and release eosinophil cationic protein upon repetitive stimulation with the same agonist. |journal=J. Immunol. |volume=165 |issue= 7 |pages= 4069-75 |year= 2000 |pmid= 11034418 |doi= }}
*{{cite journal | author=Zhang J, Rosenberg HF |title=Sequence variation at two eosinophil-associated ribonuclease loci in humans. |journal=Genetics |volume=156 |issue= 4 |pages= 1949-58 |year= 2001 |pmid= 11102386 |doi= }}
*{{cite journal | author=Boix E, Carreras E, Nikolovski Z, ''et al.'' |title=Identification and characterization of human eosinophil cationic protein by an epitope-specific antibody. |journal=J. Leukoc. Biol. |volume=69 |issue= 6 |pages= 1027-35 |year= 2001 |pmid= 11404391 |doi= }}
*{{cite journal | author=Byström J, Tenno T, Håkansson L, ''et al.'' |title=Monocytes, but not macrophages, produce the eosinophil cationic protein. |journal=APMIS |volume=109 |issue= 7-8 |pages= 507-16 |year= 2001 |pmid= 11552948 |doi= }}
*{{cite journal | author=Benner SA |title=The past as the key to the present: resurrection of ancient proteins from eosinophils. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 8 |pages= 4760-1 |year= 2002 |pmid= 11959927 |doi= 10.1073/pnas.092143699 }}
*{{cite journal | author=Jönsson UB, Byström J, Stålenheim G, Venge P |title=Polymorphism of the eosinophil cationic protein-gene is related to the expression of allergic symptoms. |journal=Clin. Exp. Allergy |volume=32 |issue= 7 |pages= 1092-5 |year= 2003 |pmid= 12100059 |doi= }}
*{{cite journal | author=Mohan CG, Boix E, Evans HR, ''et al.'' |title=The crystal structure of eosinophil cationic protein in complex with 2',5'-ADP at 2.0 A resolution reveals the details of the ribonucleolytic active site. |journal=Biochemistry |volume=41 |issue= 40 |pages= 12100-6 |year= 2002 |pmid= 12356310 |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 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RPS19... {November 19, 2007 12:23:51 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:24:13 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 = Ribosomal protein S19
| HGNCid = 10402
| Symbol = RPS19
| AltSymbols =; DBA
| OMIM = 603474
| ECnumber =
| Homologene = 37416
| MGIid = 1333780
| Function = {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0003735 |text = structural constituent of ribosome}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005730 |text = nucleolus}} {{GNF_GO|id=GO:0005840 |text = ribosome}} {{GNF_GO|id=GO:0005843 |text = cytosolic small ribosomal subunit (sensu Eukaryota)}}
| Process = {{GNF_GO|id=GO:0006412 |text = translation}} {{GNF_GO|id=GO:0007516 |text = hemocyte development}} {{GNF_GO|id=GO:0009991 |text = response to extracellular stimulus}} {{GNF_GO|id=GO:0030218 |text = erythrocyte differentiation}} {{GNF_GO|id=GO:0051272 |text = positive regulation of cell motility}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6223
| Hs_Ensembl =
| Hs_RefseqProtein = NP_001013
| Hs_RefseqmRNA = NM_001022
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 20085
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_023133
| Mm_RefseqProtein = NP_075622
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Ribosomal protein S19''', also known as '''RPS19''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RPS19 ribosomal protein S19| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6223| 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 = Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S19E family of ribosomal proteins. It is located in the cytoplasm. Mutations in this gene cause Diamond-Blackfan anemia (DBA), a constitutional erythroblastopenia characterized by absent or decreased erythroid precursors, in a subset of patients. This suggests a possible extra-ribosomal function for this gene in erythropoietic differentiation and proliferation, in addition to its ribosomal function. Higher expression levels of this gene in some primary colon carcinomas compared to matched normal colon tissues has been observed. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.<ref name="entrez">{{cite web | title = Entrez Gene: RPS19 ribosomal protein S19| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6223| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wool IG, Chan YL, Glück A |title=Structure and evolution of mammalian ribosomal proteins. |journal=Biochem. Cell Biol. |volume=73 |issue= 11-12 |pages= 933-47 |year= 1996 |pmid= 8722009 |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=Kondoh N, Schweinfest CW, Henderson KW, Papas TS |title=Differential expression of S19 ribosomal protein, laminin-binding protein, and human lymphocyte antigen class I messenger RNAs associated with colon carcinoma progression and differentiation. |journal=Cancer Res. |volume=52 |issue= 4 |pages= 791-6 |year= 1992 |pmid= 1339304 |doi= }}
*{{cite journal | author=Vladimirov SN, Ivanov AV, Karpova GG, ''et al.'' |title=Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry. |journal=Eur. J. Biochem. |volume=239 |issue= 1 |pages= 144-9 |year= 1996 |pmid= 8706699 |doi= }}
*{{cite journal | author=Kenmochi N, Kawaguchi T, Rozen S, ''et al.'' |title=A map of 75 human ribosomal protein genes. |journal=Genome Res. |volume=8 |issue= 5 |pages= 509-23 |year= 1998 |pmid= 9582194 |doi= }}
*{{cite journal | author=Draptchinskaia N, Gustavsson P, Andersson B, ''et al.'' |title=The gene encoding ribosomal protein S19 is mutated in Diamond-Blackfan anaemia. |journal=Nat. Genet. |volume=21 |issue= 2 |pages= 169-75 |year= 1999 |pmid= 9988267 |doi= 10.1038/5951 }}
*{{cite journal | author=Willig TN, Draptchinskaia N, Dianzani I, ''et al.'' |title=Mutations in ribosomal protein S19 gene and diamond blackfan anemia: wide variations in phenotypic expression. |journal=Blood |volume=94 |issue= 12 |pages= 4294-306 |year= 2000 |pmid= 10590074 |doi= }}
*{{cite journal | author=Matsson H, Klar J, Draptchinskaia N, ''et al.'' |title=Truncating ribosomal protein S19 mutations and variable clinical expression in Diamond-Blackfan anemia. |journal=Hum. Genet. |volume=105 |issue= 5 |pages= 496-500 |year= 2000 |pmid= 10598818 |doi= }}
*{{cite journal | author=Tentler D, Gustavsson P, Elinder G, ''et al.'' |title=A microdeletion in 19q13.2 associated with mental retardation, skeletal malformations, and Diamond-Blackfan anaemia suggests a novel contiguous gene syndrome. |journal=J. Med. Genet. |volume=37 |issue= 2 |pages= 128-31 |year= 2000 |pmid= 10662814 |doi= }}
*{{cite journal | author=Ramenghi U, Campagnoli MF, Garelli E, ''et al.'' |title=Diamond-Blackfan anemia: report of seven further mutations in the RPS19 gene and evidence of mutation heterogeneity in the Italian population. |journal=Blood Cells Mol. Dis. |volume=26 |issue= 5 |pages= 417-22 |year= 2001 |pmid= 11112378 |doi= 10.1006/bcmd.2000.0324 }}
*{{cite journal | author=Nishimura T, Horino K, Nishiura H, ''et al.'' |title=Apoptotic cells of an epithelial cell line, AsPC-1, release monocyte chemotactic S19 ribosomal protein dimer. |journal=J. Biochem. |volume=129 |issue= 3 |pages= 445-54 |year= 2001 |pmid= 11226885 |doi= }}
*{{cite journal | author=Soulet F, Al Saati T, Roga S, ''et al.'' |title=Fibroblast growth factor-2 interacts with free ribosomal protein S19. |journal=Biochem. Biophys. Res. Commun. |volume=289 |issue= 2 |pages= 591-6 |year= 2002 |pmid= 11716516 |doi= 10.1006/bbrc.2001.5960 }}
*{{cite journal | author=Shibuya Y, Shiokawa M, Nishiura H, ''et al.'' |title=Identification of receptor-binding sites of monocyte chemotactic S19 ribosomal protein dimer. |journal=Am. J. Pathol. |volume=159 |issue= 6 |pages= 2293-301 |year= 2001 |pmid= 11733378 |doi= }}
*{{cite journal | author=Li B, Sun M, He B, ''et al.'' |title=Identification of differentially expressed genes in human uterine leiomyomas using differential display. |journal=Cell Res. |volume=12 |issue= 1 |pages= 39-45 |year= 2004 |pmid= 11942409 |doi= 10.1038/sj.cr.7290108 }}
*{{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=Da Costa L, Tchernia G, Gascard P, ''et al.'' |title=Nucleolar localization of RPS19 protein in normal cells and mislocalization due to mutations in the nucleolar localization signals in 2 Diamond-Blackfan anemia patients: potential insights into pathophysiology. |journal=Blood |volume=101 |issue= 12 |pages= 5039-45 |year= 2004 |pmid= 12586610 |doi= 10.1182/blood-2002-12-3878 }}
*{{cite journal | author=Shrestha A, Shiokawa M, Nishimura T, ''et al.'' |title=Switch moiety in agonist/antagonist dual effect of S19 ribosomal protein dimer on leukocyte chemotactic C5a receptor. |journal=Am. J. Pathol. |volume=162 |issue= 4 |pages= 1381-8 |year= 2003 |pmid= 12651630 |doi= }}
*{{cite journal | author=Proust A, Da Costa L, Rince P, ''et al.'' |title=Ten novel Diamond-Blackfan anemia mutations and three polymorphisms within the rps19 gene. |journal=Hematol. J. |volume=4 |issue= 2 |pages= 132-6 |year= 2003 |pmid= 12750732 |doi= 10.1038/sj.thj.6200230 }}
*{{cite journal | author=Campagnoli MF, Garelli E, Quarello P, ''et al.'' |title=Molecular basis of Diamond-Blackfan anemia: new findings from the Italian registry and a review of the literature. |journal=Haematologica |volume=89 |issue= 4 |pages= 480-9 |year= 2006 |pmid= 15075082 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RS1... {November 19, 2007 12:24:13 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:24:45 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
}}
<!-- 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 = Retinoschisis (X-linked, juvenile) 1
| HGNCid = 10457
| Symbol = RS1
| AltSymbols =; RS; XLRS1
| OMIM = 312700
| ECnumber =
| Homologene = 279
| MGIid = 1336189
| GeneAtlas_image1 = PBB_GE_RS1_207363_at_tn.png
| GeneAtlas_image2 = PBB_GE_RS1_216937_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6247
| Hs_Ensembl = ENSG00000102104
| Hs_RefseqProtein = NP_000321
| Hs_RefseqmRNA = NM_000330
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 18567733
| Hs_GenLoc_end = 18600150
| Hs_Uniprot = O15537
| Mm_EntrezGene = 20147
| Mm_Ensembl = ENSMUSG00000031293
| Mm_RefseqmRNA = NM_011302
| Mm_RefseqProtein = NP_035432
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 156112118
| Mm_GenLoc_end = 156143768
| Mm_Uniprot = Q9R1M6
}}
}}
'''Retinoschisis (X-linked, juvenile) 1''', also known as '''RS1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RS1 retinoschisis (X-linked, juvenile) 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6247| 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=Sikkink SK, Biswas S, Parry NR, ''et al.'' |title=X-linked retinoschisis: an update. |journal=J. Med. Genet. |volume=44 |issue= 4 |pages= 225-32 |year= 2007 |pmid= 17172462 |doi= 10.1136/jmg.2006.047340 }}
*{{cite journal | author=Alitalo T, Kruse TA, de la Chapelle A |title=Refined localization of the gene causing X-linked juvenile retinoschisis. |journal=Genomics |volume=9 |issue= 3 |pages= 505-10 |year= 1991 |pmid= 2032721 |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=Sauer CG, Gehrig A, Warneke-Wittstock R, ''et al.'' |title=Positional cloning of the gene associated with X-linked juvenile retinoschisis. |journal=Nat. Genet. |volume=17 |issue= 2 |pages= 164-70 |year= 1997 |pmid= 9326935 |doi= 10.1038/ng1097-164 }}
*{{cite journal | author=Hotta Y, Fujiki K, Hayakawa M, ''et al.'' |title=Japanese juvenile retinoschisis is caused by mutations of the XLRS1 gene. |journal=Hum. Genet. |volume=103 |issue= 2 |pages= 142-4 |year= 1998 |pmid= 9760195 |doi= }}
*{{cite journal | author=Shastry BS, Hejtmancik FJ, Trese MT |title=Recurrent missense (R197C) and nonsense (Y89X) mutations in the XLRS1 gene in families with X-linked retinoschisis. |journal=Biochem. Biophys. Res. Commun. |volume=256 |issue= 2 |pages= 317-9 |year= 1999 |pmid= 10079181 |doi= 10.1006/bbrc.1999.0323 }}
*{{cite journal | author=Mashima Y, Shinoda K, Ishida S, ''et al.'' |title=Identification of four novel mutations of the XLRS1 gene in Japanese patients with X-linked juvenile retinoschisis. Mutation in brief no. 234. Online. |journal=Hum. Mutat. |volume=13 |issue= 4 |pages= 338 |year= 1999 |pmid= 10220153 |doi= 10.1002/(SICI)1098-1004(1999)13:4<338::AID-HUMU16>3.0.CO;2-0 }}
*{{cite journal | author=Huopaniemi L, Rantala A, Forsius H, ''et al.'' |title=Three widespread founder mutations contribute to high incidence of X-linked juvenile retinoschisis in Finland. |journal=Eur. J. Hum. Genet. |volume=7 |issue= 3 |pages= 368-76 |year= 1999 |pmid= 10234514 |doi= 10.1038/sj.ejhg.5200300 }}
*{{cite journal | author=Gehrig A, White K, Lorenz B, ''et al.'' |title=Assessment of RS1 in X-linked juvenile retinoschisis and sporadic senile retinoschisis. |journal=Clin. Genet. |volume=55 |issue= 6 |pages= 461-5 |year= 1999 |pmid= 10450864 |doi= }}
*{{cite journal | author=Hiriyanna KT, Bingham EL, Yashar BM, ''et al.'' |title=Novel mutations in XLRS1 causing retinoschisis, including first evidence of putative leader sequence change. |journal=Hum. Mutat. |volume=14 |issue= 5 |pages= 423-7 |year= 2000 |pmid= 10533068 |doi= 10.1002/(SICI)1098-1004(199911)14:5<423::AID-HUMU8>3.0.CO;2-D }}
*{{cite journal | author=Grayson C, Reid SN, Ellis JA, ''et al.'' |title=Retinoschisin, the X-linked retinoschisis protein, is a secreted photoreceptor protein, and is expressed and released by Weri-Rb1 cells. |journal=Hum. Mol. Genet. |volume=9 |issue= 12 |pages= 1873-9 |year= 2000 |pmid= 10915776 |doi= }}
*{{cite journal | author=Weber BH, Schrewe H, Molday LL, ''et al.'' |title=Inactivation of the murine X-linked juvenile retinoschisis gene, Rs1h, suggests a role of retinoschisin in retinal cell layer organization and synaptic structure. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 9 |pages= 6222-7 |year= 2002 |pmid= 11983912 |doi= 10.1073/pnas.092528599 }}
*{{cite journal | author=Tuvdendorj D, Isashiki Y, Ohba N, ''et al.'' |title=Two Japanese patients with mutations in the XLRS1 gene. |journal=Retina (Philadelphia, Pa.) |volume=22 |issue= 3 |pages= 354-7 |year= 2002 |pmid= 12055472 |doi= }}
*{{cite journal | author=Wistow G, Bernstein SL, Wyatt MK, ''et al.'' |title=Expressed sequence tag analysis of human retina for the NEIBank Project: retbindin, an abundant, novel retinal cDNA and alternative splicing of other retina-preferred gene transcripts. |journal=Mol. Vis. |volume=8 |issue= |pages= 196-204 |year= 2002 |pmid= 12107411 |doi= }}
*{{cite journal | author=Inoue Y, Yamamoto S, Inoue T, ''et al.'' |title=Two novel point mutations of the XLRS1 gene in patients with X-linked juvenile retinoschisis. |journal=Am. J. Ophthalmol. |volume=134 |issue= 4 |pages= 622-4 |year= 2002 |pmid= 12383832 |doi= }}
*{{cite journal | author=Wang T, Waters CT, Rothman AM, ''et al.'' |title=Intracellular retention of mutant retinoschisin is the pathological mechanism underlying X-linked retinoschisis. |journal=Hum. Mol. Genet. |volume=11 |issue= 24 |pages= 3097-105 |year= 2003 |pmid= 12417531 |doi= }}
*{{cite journal | author=Tanimoto N, Usui T, Takagi M, ''et al.'' |title=Electroretinographic findings in three family members with X-linked juvenile retinoschisis associated with a novel Pro192Thr mutation of the XLRS1 gene. |journal=Jpn. J. Ophthalmol. |volume=46 |issue= 5 |pages= 568-76 |year= 2003 |pmid= 12457918 |doi= }}
*{{cite journal | author=Wu WW, Molday RS |title=Defective discoidin domain structure, subunit assembly, and endoplasmic reticulum processing of retinoschisin are primary mechanisms responsible for X-linked retinoschisis. |journal=J. Biol. Chem. |volume=278 |issue= 30 |pages= 28139-46 |year= 2003 |pmid= 12746437 |doi= 10.1074/jbc.M302464200 }}
*{{cite journal | author=Fraternali F, Cavallo L, Musco G |title=Effects of pathological mutations on the stability of a conserved amino acid triad in retinoschisin. |journal=FEBS Lett. |volume=544 |issue= 1-3 |pages= 21-6 |year= 2003 |pmid= 12782284 |doi= }}
*{{cite journal | author=Sato M, Oshika T, Kaji Y, Nose H |title=Three novel mutations in the X-linked juvenile retinoschisis (XLRS1) gene in 6 Japanese patients, 1 of whom had Turner's syndrome. |journal=Ophthalmic Res. |volume=35 |issue= 5 |pages= 295-300 |year= 2003 |pmid= 12920343 |doi= 10.1159/000072151 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RTN4R... {November 19, 2007 12:27:37 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:28:02 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_RTN4R_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ozn.
| PDB = {{PDB2|1ozn}}, {{PDB2|1p8t}}
| Name = Reticulon 4 receptor
| HGNCid = 18601
| Symbol = RTN4R
| AltSymbols =; NGR; NOGOR
| OMIM = 605566
| ECnumber =
| Homologene = 11299
| MGIid = 2136886
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0007409 |text = axonogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 65078
| Hs_Ensembl = ENSG00000040608
| Hs_RefseqProtein = NP_075380
| Hs_RefseqmRNA = NM_023004
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 18608940
| Hs_GenLoc_end = 18635816
| Hs_Uniprot = Q9BZR6
| Mm_EntrezGene = 65079
| Mm_Ensembl = ENSMUSG00000043811
| Mm_RefseqmRNA = NM_022982
| Mm_RefseqProtein = NP_075358
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 18064294
| Mm_GenLoc_end = 18065694
| Mm_Uniprot = Q99PI8
}}
}}
'''Reticulon 4 receptor''', also known as '''RTN4R''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RTN4R reticulon 4 receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=65078| 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 the receptor for reticulon 4, oligodendrocyte myelin glycoprotein and myelin-associated glycoprotein. This receptor mediates axonal growth inhibition and may play a role in regulating axonal regeneration and plasticity in the adult central nervous system.<ref name="entrez">{{cite web | title = Entrez Gene: RTN4R reticulon 4 receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=65078| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ng CE, Tang BL |title=Nogos and the Nogo-66 receptor: factors inhibiting CNS neuron regeneration. |journal=J. Neurosci. Res. |volume=67 |issue= 5 |pages= 559-65 |year= 2002 |pmid= 11891768 |doi= }}
*{{cite journal | author=Ferraro GB |title=Refining our understanding of NgR1 function during myelin inhibition. |journal=J. Neurosci. |volume=27 |issue= 43 |pages= 11451-2 |year= 2007 |pmid= 17959786 |doi= 10.1523/JNEUROSCI.3419-07.2007 }}
*{{cite journal | author=Dunham I, Shimizu N, Roe BA, ''et al.'' |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489-95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031 }}
*{{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=Fournier AE, GrandPre T, Strittmatter SM |title=Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration. |journal=Nature |volume=409 |issue= 6818 |pages= 341-6 |year= 2001 |pmid= 11201742 |doi= 10.1038/35053072 }}
*{{cite journal | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
*{{cite journal | author=GrandPré T, Li S, Strittmatter SM |title=Nogo-66 receptor antagonist peptide promotes axonal regeneration. |journal=Nature |volume=417 |issue= 6888 |pages= 547-51 |year= 2002 |pmid= 12037567 |doi= 10.1038/417547a }}
*{{cite journal | author=Wang KC, Koprivica V, Kim JA, ''et al.'' |title=Oligodendrocyte-myelin glycoprotein is a Nogo receptor ligand that inhibits neurite outgrowth. |journal=Nature |volume=417 |issue= 6892 |pages= 941-4 |year= 2002 |pmid= 12068310 |doi= 10.1038/nature00867 }}
*{{cite journal | author=Liu BP, Fournier A, GrandPré T, Strittmatter SM |title=Myelin-associated glycoprotein as a functional ligand for the Nogo-66 receptor. |journal=Science |volume=297 |issue= 5584 |pages= 1190-3 |year= 2002 |pmid= 12089450 |doi= 10.1126/science.1073031 }}
*{{cite journal | author=Domeniconi M, Cao Z, Spencer T, ''et al.'' |title=Myelin-associated glycoprotein interacts with the Nogo66 receptor to inhibit neurite outgrowth. |journal=Neuron |volume=35 |issue= 2 |pages= 283-90 |year= 2002 |pmid= 12160746 |doi= }}
*{{cite journal | author=Woolf CJ, Bloechlinger S |title=Neuroscience. It takes more than two to Nogo. |journal=Science |volume=297 |issue= 5584 |pages= 1132-4 |year= 2002 |pmid= 12183616 |doi= 10.1126/science.1076247 }}
*{{cite journal | author=Josephson A, Trifunovski A, Widmer HR, ''et al.'' |title=Nogo-receptor gene activity: cellular localization and developmental regulation of mRNA in mice and humans. |journal=J. Comp. Neurol. |volume=453 |issue= 3 |pages= 292-304 |year= 2002 |pmid= 12378589 |doi= 10.1002/cne.10408 }}
*{{cite journal | author=Wang KC, Kim JA, Sivasankaran R, ''et al.'' |title=P75 interacts with the Nogo receptor as a co-receptor for Nogo, MAG and OMgp. |journal=Nature |volume=420 |issue= 6911 |pages= 74-8 |year= 2002 |pmid= 12422217 |doi= 10.1038/nature01176 }}
*{{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=He XL, Bazan JF, McDermott G, ''et al.'' |title=Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition. |journal=Neuron |volume=38 |issue= 2 |pages= 177-85 |year= 2003 |pmid= 12718853 |doi= }}
*{{cite journal | author=Barton WA, Liu BP, Tzvetkova D, ''et al.'' |title=Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins. |journal=EMBO J. |volume=22 |issue= 13 |pages= 3291-302 |year= 2003 |pmid= 12839991 |doi= 10.1093/emboj/cdg325 }}
*{{cite journal | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SAA2... {November 19, 2007 12:24:45 AM PST}
- SEARCH REDIRECT: Control Box Found: SAA2 {November 19, 2007 12:25:06 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:25:08 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:25:08 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:25:08 AM PST}
- UPDATED: Updated protein page: SAA2 {November 19, 2007 12:25:14 AM PST}
- INFO: Beginning work on SDHD... {November 19, 2007 12:25:56 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:26:25 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_SDHD_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1zoy.
| PDB = {{PDB2|1zoy}}, {{PDB2|1zp0}}
| Name = Succinate dehydrogenase complex, subunit D, integral membrane protein
| HGNCid = 10683
| Symbol = SDHD
| AltSymbols =; CBT1; PGL; PGL1; SDH4
| OMIM = 602690
| ECnumber =
| Homologene = 37718
| MGIid = 1914175
| Function = {{GNF_GO|id=GO:0000104 |text = succinate dehydrogenase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005740 |text = mitochondrial envelope}} {{GNF_GO|id=GO:0005743 |text = mitochondrial inner membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006099 |text = tricarboxylic acid cycle}} {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006810 |text = transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6392
| Hs_Ensembl =
| Hs_RefseqProtein = NP_002993
| Hs_RefseqmRNA = NM_003002
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 66925
| Mm_Ensembl = ENSMUSG00000000171
| Mm_RefseqmRNA = NM_025848
| Mm_RefseqProtein = NP_080124
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 50348576
| Mm_GenLoc_end = 50356047
| Mm_Uniprot = Q9D6J9
}}
}}
'''Succinate dehydrogenase complex, subunit D, integral membrane protein''', also known as '''SDHD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SDHD succinate dehydrogenase complex, subunit D, integral membrane protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6392| 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 = Complex II of the respiratory chain, which is specifically involved in the oxidation of succinate, carries electrons from FADH to CoQ. The complex is composed of four nuclear-encoded subunits and is localized in the mitochondrial inner membrane. The subunit D protein is one of two integral membrane proteins anchoring the complex to the matrix side of the membrane. Mutations in SDHD have been linked to hereditary paraganglioma.<ref name="entrez">{{cite web | title = Entrez Gene: SDHD succinate dehydrogenase complex, subunit D, integral membrane protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6392| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Eng C, Kiuru M, Fernandez MJ, Aaltonen LA |title=A role for mitochondrial enzymes in inherited neoplasia and beyond. |journal=Nat. Rev. Cancer |volume=3 |issue= 3 |pages= 193-202 |year= 2003 |pmid= 12612654 |doi= 10.1038/nrc1013 }}
*{{cite journal | author=Martin TP, Irving RM, Maher ER |title=The genetics of paragangliomas: a review. |journal=Clinical otolaryngology : official journal of ENT-UK ; official journal of Netherlands Society for Oto-Rhino-Laryngology & Cervico-Facial Surgery |volume=32 |issue= 1 |pages= 7-11 |year= 2007 |pmid= 17298303 |doi= 10.1111/j.1365-2273.2007.01378.x }}
*{{cite journal | author=Heutink P, van der Mey AG, Sandkuijl LA, ''et al.'' |title=A gene subject to genomic imprinting and responsible for hereditary paragangliomas maps to chromosome 11q23-qter. |journal=Hum. Mol. Genet. |volume=1 |issue= 1 |pages= 7-10 |year= 1993 |pmid= 1301144 |doi= }}
*{{cite journal | author=Kita K, Oya H, Gennis RB, ''et al.'' |title=Human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of iron sulfur (Ip) subunit of liver mitochondria. |journal=Biochem. Biophys. Res. Commun. |volume=166 |issue= 1 |pages= 101-8 |year= 1990 |pmid= 2302193 |doi= }}
*{{cite journal | author=Mariman EC, van Beersum SE, Cremers CW, ''et al.'' |title=Fine mapping of a putatively imprinted gene for familial non-chromaffin paragangliomas to chromosome 11q13.1: evidence for genetic heterogeneity. |journal=Hum. Genet. |volume=95 |issue= 1 |pages= 56-62 |year= 1995 |pmid= 7814027 |doi= }}
*{{cite journal | author=Hirawake H, Taniwaki M, Tamura A, ''et al.'' |title=Cytochrome b in human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of the components in liver mitochondria and chromosome assignment of the genes for the large (SDHC) and small (SDHD) subunits to 1q21 and 11q23. |journal=Cytogenet. Cell Genet. |volume=79 |issue= 1-2 |pages= 132-8 |year= 1998 |pmid= 9533030 |doi= }}
*{{cite journal | author=Hirawake H, Taniwaki M, Tamura A, ''et al.'' |title=Characterization of the human SDHD gene encoding the small subunit of cytochrome b (cybS) in mitochondrial succinate-ubiquinone oxidoreductase. |journal=Biochim. Biophys. Acta |volume=1412 |issue= 3 |pages= 295-300 |year= 1999 |pmid= 10482792 |doi= }}
*{{cite journal | author=Baysal BE, Ferrell RE, Willett-Brozick JE, ''et al.'' |title=Mutations in SDHD, a mitochondrial complex II gene, in hereditary paraganglioma. |journal=Science |volume=287 |issue= 5454 |pages= 848-51 |year= 2000 |pmid= 10657297 |doi= }}
*{{cite journal | author=Gimm O, Armanios M, Dziema H, ''et al.'' |title=Somatic and occult germ-line mutations in SDHD, a mitochondrial complex II gene, in nonfamilial pheochromocytoma. |journal=Cancer Res. |volume=60 |issue= 24 |pages= 6822-5 |year= 2001 |pmid= 11156372 |doi= }}
*{{cite journal | author=Astuti D, Douglas F, Lennard TW, ''et al.'' |title=Germline SDHD mutation in familial phaeochromocytoma. |journal=Lancet |volume=357 |issue= 9263 |pages= 1181-2 |year= 2001 |pmid= 11323050 |doi= }}
*{{cite journal | author=Milunsky JM, Maher TA, Michels VV, Milunsky A |title=Novel mutations and the emergence of a common mutation in the SDHD gene causing familial paraganglioma. |journal=Am. J. Med. Genet. |volume=100 |issue= 4 |pages= 311-4 |year= 2001 |pmid= 11343322 |doi= }}
*{{cite journal | author=Badenhop RF, Cherian S, Lord RS, ''et al.'' |title=Novel mutations in the SDHD gene in pedigrees with familial carotid body paraganglioma and sensorineural hearing loss. |journal=Genes Chromosomes Cancer |volume=31 |issue= 3 |pages= 255-63 |year= 2001 |pmid= 11391796 |doi= 10.1002/gcc.1142 }}
*{{cite journal | author=Taschner PE, Jansen JC, Baysal BE, ''et al.'' |title=Nearly all hereditary paragangliomas in the Netherlands are caused by two founder mutations in the SDHD gene. |journal=Genes Chromosomes Cancer |volume=31 |issue= 3 |pages= 274-81 |year= 2001 |pmid= 11391798 |doi= 10.1002/gcc.1144 }}
*{{cite journal | author=Masuoka J, Brandner S, Paulus W, ''et al.'' |title=Germline SDHD mutation in paraganglioma of the spinal cord. |journal=Oncogene |volume=20 |issue= 36 |pages= 5084-6 |year= 2001 |pmid= 11526495 |doi= 10.1038/sj.onc.1204579 }}
*{{cite journal | author=Gimenez-Roqueplo AP, Favier J, Rustin P, ''et al.'' |title=The R22X mutation of the SDHD gene in hereditary paraganglioma abolishes the enzymatic activity of complex II in the mitochondrial respiratory chain and activates the hypoxia pathway. |journal=Am. J. Hum. Genet. |volume=69 |issue= 6 |pages= 1186-97 |year= 2002 |pmid= 11605159 |doi= }}
*{{cite journal | author=Baysal BE, Willett-Brozick JE, Lawrence EC, ''et al.'' |title=Prevalence of SDHB, SDHC, and SDHD germline mutations in clinic patients with head and neck paragangliomas. |journal=J. Med. Genet. |volume=39 |issue= 3 |pages= 178-83 |year= 2002 |pmid= 11897817 |doi= }}
*{{cite journal | author=Kytölä S, Nord B, Elder EE, ''et al.'' |title=Alterations of the SDHD gene locus in midgut carcinoids, Merkel cell carcinomas, pheochromocytomas, and abdominal paragangliomas. |journal=Genes Chromosomes Cancer |volume=34 |issue= 3 |pages= 325-32 |year= 2002 |pmid= 12007193 |doi= 10.1002/gcc.10081 }}
*{{cite journal | author=Cascon A, Ruiz-Llorente S, Cebrian A, ''et al.'' |title=Identification of novel SDHD mutations in patients with phaeochromocytoma and/or paraganglioma. |journal=Eur. J. Hum. Genet. |volume=10 |issue= 8 |pages= 457-61 |year= 2003 |pmid= 12111639 |doi= 10.1038/sj.ejhg.5200829 }}
*{{cite journal | author=Dannenberg H, Dinjens WN, Abbou M, ''et al.'' |title=Frequent germ-line succinate dehydrogenase subunit D gene mutations in patients with apparently sporadic parasympathetic paraganglioma. |journal=Clin. Cancer Res. |volume=8 |issue= 7 |pages= 2061-6 |year= 2003 |pmid= 12114404 |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 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SLC9A3... {November 19, 2007 12:26:25 AM PST}
- SEARCH REDIRECT: Control Box Found: SLC9A3 {November 19, 2007 12:26:52 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:26:55 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:26:55 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:26:55 AM PST}
- UPDATED: Updated protein page: SLC9A3 {November 19, 2007 12:27:05 AM PST}
- INFO: Beginning work on SNRPD1... {November 19, 2007 12:27:05 AM PST}
- SEARCH REDIRECT: Control Box Found: SNRPD1 {November 19, 2007 12:27:30 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:27:32 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:27:32 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:27:32 AM PST}
- UPDATED: Updated protein page: SNRPD1 {November 19, 2007 12:27:37 AM PST}
end log.
