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Log page index: User:ProteinBoxBot/PBB_Log_Index
[edit] Protein Status Quick Log - Date: 03:11, 16 November 2007 (UTC)
[edit] Conflict: Ambiguous Proteins (1)
[edit] Proteins without matches (4)
[edit] Proteins with a High Potential Match (14)
[edit] Redirected Proteins (6)
[edit] Manual Inspection (Page not found) (19)
[edit] Updated (6)
[edit] Protein Status Grid - Date: 03:11, 16 November 2007 (UTC)
[edit] Vebose Log - Date: 03:11, 16 November 2007 (UTC)
- INFO: Beginning work on AFP... {November 15, 2007 6:52:16 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:52:38 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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| 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 = Alpha-fetoprotein
| HGNCid = 317
| Symbol = AFP
| AltSymbols =; FETA; HPAFP
| OMIM = 104150
| ECnumber =
| Homologene = 36278
| MGIid = 87951
| GeneAtlas_image1 = PBB_GE_AFP_204694_at_tn.png
| Function = {{GNF_GO|id=GO:0005386 |text = transmembrane transporter activity}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0016151 |text = nickel ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0001542 |text = ovulation (sensu Mammalia)}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0019953 |text = sexual reproduction}} {{GNF_GO|id=GO:0042448 |text = progesterone metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 174
| Hs_Ensembl = ENSG00000081051
| Hs_RefseqProtein = NP_001125
| Hs_RefseqmRNA = NM_001134
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 74520797
| Hs_GenLoc_end = 74540356
| Hs_Uniprot = P02771
| Mm_EntrezGene = 11576
| Mm_Ensembl = ENSMUSG00000054932
| Mm_RefseqmRNA = NM_007423
| Mm_RefseqProtein = NP_031449
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 91565937
| Mm_GenLoc_end = 91584107
| Mm_Uniprot = Q3TGA3
}}
}}
'''Alpha-fetoprotein''', also known as '''AFP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AFP alpha-fetoprotein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=174| 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 alpha-fetoprotein, a major plasma protein produced by the yolk sac and the liver during fetal life. Alpha-fetoprotein expression in adults is often associated with hepatoma or teratoma. However, hereditary persistance of alpha-fetoprotein may also be found in individuals with no obvious pathology. The protein is thought to be the fetal counterpart of serum albumin, and the alpha-fetoprotein and albumin genes are present in tandem in the same transcriptional orientation on chromosome 4. Alpha-fetoprotein is found in monomeric as well as dimeric and trimeric forms, and binds copper, nickel, fatty acids and bilirubin. The level of alpha-fetoprotein in amniotic fluid is used to measure renal loss of protein to screen for spina bifida and anencephaly.<ref name="entrez">{{cite web | title = Entrez Gene: AFP alpha-fetoprotein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=174| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nahon JL |title=The regulation of albumin and alpha-fetoprotein gene expression in mammals. |journal=Biochimie |volume=69 |issue= 5 |pages= 445-59 |year= 1987 |pmid= 2445387 |doi= }}
*{{cite journal | author=Tilghman SM |title=The structure and regulation of the alpha-fetoprotein and albumin genes. |journal=Oxf. Surv. Eukaryot. Genes |volume=2 |issue= |pages= 160-206 |year= 1989 |pmid= 2474300 |doi= }}
*{{cite journal | author=Mizejewski GJ |title=Biological role of alpha-fetoprotein in cancer: prospects for anticancer therapy. |journal=Expert Rev Anticancer Ther |volume=2 |issue= 6 |pages= 709-35 |year= 2003 |pmid= 12503217 |doi= 10.1586/14737140.2.6.709 }}
*{{cite journal | author=Yachnin S, Hsu R, Heinrikson RL, Miller JB |title=Studies on human alpha-fetoprotein. Isolation and characterization of monomeric and polymeric forms and amino-terminal sequence analysis. |journal=Biochim. Biophys. Acta |volume=493 |issue= 2 |pages= 418-28 |year= 1977 |pmid= 70228 |doi= }}
*{{cite journal | author=Aoyagi Y, Ikenaka T, Ichida F |title=Comparative chemical structures of human alpha-fetoproteins from fetal serum and from ascites fluid of a patient with hepatoma. |journal=Cancer Res. |volume=37 |issue= 10 |pages= 3663-7 |year= 1977 |pmid= 71198 |doi= }}
*{{cite journal | author=Aoyagi Y, Ikenaka T, Ichida F |title=Copper(II)-binding ability of human alpha-fetoprotein. |journal=Cancer Res. |volume=38 |issue= 10 |pages= 3483-6 |year= 1978 |pmid= 80265 |doi= }}
*{{cite journal | author=Aoyagi Y, Ikenaka T, Ichida F |title=alpha-Fetoprotein as a carrier protein in plasma and its bilirubin-binding ability. |journal=Cancer Res. |volume=39 |issue= 9 |pages= 3571-4 |year= 1979 |pmid= 89900 |doi= }}
*{{cite journal | author=Torres JM, Anel A, Uriel J |title=Alpha-fetoprotein-mediated uptake of fatty acids by human T lymphocytes. |journal=J. Cell. Physiol. |volume=150 |issue= 3 |pages= 456-62 |year= 1992 |pmid= 1371512 |doi= 10.1002/jcp.1041500305 }}
*{{cite journal | author=Greenberg F, Faucett A, Rose E, ''et al.'' |title=Congenital deficiency of alpha-fetoprotein. |journal=Am. J. Obstet. Gynecol. |volume=167 |issue= 2 |pages= 509-11 |year= 1992 |pmid= 1379776 |doi= }}
*{{cite journal | author=Bansal V, Kumari K, Dixit A, Sahib MK |title=Interaction of human alpha fetoprotein with bilirubin. |journal=Indian J. Exp. Biol. |volume=28 |issue= 7 |pages= 697-8 |year= 1991 |pmid= 1703124 |doi= }}
*{{cite journal | author=Pucci P, Siciliano R, Malorni A, ''et al.'' |title=Human alpha-fetoprotein primary structure: a mass spectrometric study. |journal=Biochemistry |volume=30 |issue= 20 |pages= 5061-6 |year= 1991 |pmid= 1709810 |doi= }}
*{{cite journal | author=Liu MC, Yu S, Sy J, ''et al.'' |title=Tyrosine sulfation of proteins from the human hepatoma cell line HepG2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 21 |pages= 7160-4 |year= 1985 |pmid= 2414772 |doi= }}
*{{cite journal | author=Gibbs PE, Zielinski R, Boyd C, Dugaiczyk A |title=Structure, polymorphism, and novel repeated DNA elements revealed by a complete sequence of the human alpha-fetoprotein gene. |journal=Biochemistry |volume=26 |issue= 5 |pages= 1332-43 |year= 1987 |pmid= 2436661 |doi= }}
*{{cite journal | author=Sakai M, Morinaga T, Urano Y, ''et al.'' |title=The human alpha-fetoprotein gene. Sequence organization and the 5' flanking region. |journal=J. Biol. Chem. |volume=260 |issue= 8 |pages= 5055-60 |year= 1985 |pmid= 2580830 |doi= }}
*{{cite journal | author=Ruoslahti E, Pihko H, Vaheri A, ''et al.'' |title=Alpha fetoprotein: structure and expression in man and inbred mouse strains under normal conditions and liver injury. |journal=Johns Hopkins Med. J. Suppl. |volume=3 |issue= |pages= 249-55 |year= 1975 |pmid= 4138095 |doi= }}
*{{cite journal | author=Urano Y, Sakai M, Watanabe K, Tamaoki T |title=Tandem arrangement of the albumin and alpha-fetoprotein genes in the human genome. |journal=Gene |volume=32 |issue= 3 |pages= 255-61 |year= 1985 |pmid= 6085063 |doi= }}
*{{cite journal | author=Beattie WG, Dugaiczyk A |title=Structure and evolution of human alpha-fetoprotein deduced from partial sequence of cloned cDNA. |journal=Gene |volume=20 |issue= 3 |pages= 415-22 |year= 1983 |pmid= 6187626 |doi= }}
*{{cite journal | author=Morinaga T, Sakai M, Wegmann TG, Tamaoki T |title=Primary structures of human alpha-fetoprotein and its mRNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 15 |pages= 4604-8 |year= 1983 |pmid= 6192439 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BDKRB2... {November 15, 2007 6:52:38 PM PST}
- SEARCH REDIRECT: Control Box Found: BDKRB2 {November 15, 2007 6:53:14 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 6:53:17 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 6:53:17 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 6:53:17 PM PST}
- UPDATED: Updated protein page: BDKRB2 {November 15, 2007 6:53:24 PM PST}
- INFO: Beginning work on CD63... {November 15, 2007 6:53:24 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:53:52 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = CD63 molecule
| HGNCid = 1692
| Symbol = CD63
| AltSymbols =; LAMP-3; ME491; MLA1; OMA81H; TSPAN30
| OMIM = 155740
| ECnumber =
| Homologene = 37526
| MGIid =
| GeneAtlas_image1 = PBB_GE_CD63_200663_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005765 |text = lysosomal membrane}} {{GNF_GO|id=GO:0005770 |text = late endosome}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0010008 |text = endosome membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 967
| Hs_Ensembl = ENSG00000135404
| Hs_RefseqProtein = NP_001035123
| Hs_RefseqmRNA = NM_001040034
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 54405533
| Hs_GenLoc_end = 54409711
| Hs_Uniprot = P08962
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''CD63 molecule''', also known as '''CD63''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CD63 CD63 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=967| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. This encoded protein is a cell surface glycoprotein that is known to complex with integrins. It may function as a blood platelet activation marker. Deficiency of this protein is associated with Hermansky-Pudlak syndrome. Also this gene has been associated with tumor progression. The use of alternate polyadenylation sites has been found for this gene. Alternative splicing results in multiple transcript variants encoding different proteins.<ref name="entrez">{{cite web | title = Entrez Gene: CD63 CD63 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=967| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Horejsí V, Vlcek C |title=Novel structurally distinct family of leucocyte surface glycoproteins including CD9, CD37, CD53 and CD63. |journal=FEBS Lett. |volume=288 |issue= 1-2 |pages= 1-4 |year= 1991 |pmid= 1879540 |doi= }}
*{{cite journal | author=Berditchevski F |title=Complexes of tetraspanins with integrins: more than meets the eye. |journal=J. Cell. Sci. |volume=114 |issue= Pt 23 |pages= 4143-51 |year= 2002 |pmid= 11739647 |doi= }}
*{{cite journal | author=Wang MX, Earley JJ, Shields JA, Donoso LA |title=An ocular melanoma-associated antigen. Molecular characterization. |journal=Arch. Ophthalmol. |volume=110 |issue= 3 |pages= 399-404 |year= 1992 |pmid= 1339263 |doi= }}
*{{cite journal | author=Hotta H, Miyamoto H, Hara I, ''et al.'' |title=Genomic structure of the ME491/CD63 antigen gene and functional analysis of the 5'-flanking regulatory sequences. |journal=Biochem. Biophys. Res. Commun. |volume=185 |issue= 1 |pages= 436-42 |year= 1992 |pmid= 1599482 |doi= }}
*{{cite journal | author=Metzelaar MJ, Wijngaard PL, Peters PJ, ''et al.'' |title=CD63 antigen. A novel lysosomal membrane glycoprotein, cloned by a screening procedure for intracellular antigens in eukaryotic cells. |journal=J. Biol. Chem. |volume=266 |issue= 5 |pages= 3239-45 |year= 1991 |pmid= 1993697 |doi= }}
*{{cite journal | author=Rapp G, Freudenstein J, Klaudiny J, ''et al.'' |title=Characterization of three abundant mRNAs from human ovarian granulosa cells. |journal=DNA Cell Biol. |volume=9 |issue= 7 |pages= 479-85 |year= 1990 |pmid= 2171551 |doi= }}
*{{cite journal | author=Hotta H, Takahashi N, Homma M |title=Transcriptional enhancement of the human gene encoding for a melanoma-associated antigen (ME491) in association with malignant transformation. |journal=Jpn. J. Cancer Res. |volume=80 |issue= 12 |pages= 1186-91 |year= 1990 |pmid= 2516848 |doi= }}
*{{cite journal | author=Hotta H, Ross AH, Huebner K, ''et al.'' |title=Molecular cloning and characterization of an antigen associated with early stages of melanoma tumor progression. |journal=Cancer Res. |volume=48 |issue= 11 |pages= 2955-62 |year= 1988 |pmid= 3365686 |doi= }}
*{{cite journal | author=Ross AH, Dietzschold B, Jackson DM, ''et al.'' |title=Isolation and amino terminal sequencing of a novel melanoma-associated antigen. |journal=Arch. Biochem. Biophys. |volume=242 |issue= 2 |pages= 540-8 |year= 1985 |pmid= 4062294 |doi= }}
*{{cite journal | author=Berditchevski F, Bazzoni G, Hemler ME |title=Specific association of CD63 with the VLA-3 and VLA-6 integrins. |journal=J. Biol. Chem. |volume=270 |issue= 30 |pages= 17784-90 |year= 1995 |pmid= 7629079 |doi= }}
*{{cite journal | author=Nishibori M, Cham B, McNicol A, ''et al.'' |title=The protein CD63 is in platelet dense granules, is deficient in a patient with Hermansky-Pudlak syndrome, and appears identical to granulophysin. |journal=J. Clin. Invest. |volume=91 |issue= 4 |pages= 1775-82 |year= 1993 |pmid= 7682577 |doi= }}
*{{cite journal | author=Radford KJ, Thorne RF, Hersey P |title=CD63 associates with transmembrane 4 superfamily members, CD9 and CD81, and with beta 1 integrins in human melanoma. |journal=Biochem. Biophys. Res. Commun. |volume=222 |issue= 1 |pages= 13-8 |year= 1996 |pmid= 8630057 |doi= 10.1006/bbrc.1996.0690 }}
*{{cite journal | author=Gwynn B, Eicher EM, Peters LL |title=Genetic localization of Cd63, a member of the transmembrane 4 superfamily, reveals two distinct loci in the mouse genome. |journal=Genomics |volume=35 |issue= 2 |pages= 389-91 |year= 1996 |pmid= 8661157 |doi= 10.1006/geno.1996.0375 }}
*{{cite journal | author=Mannion BA, Berditchevski F, Kraeft SK, ''et al.'' |title=Transmembrane-4 superfamily proteins CD81 (TAPA-1), CD82, CD63, and CD53 specifically associated with integrin alpha 4 beta 1 (CD49d/CD29). |journal=J. Immunol. |volume=157 |issue= 5 |pages= 2039-47 |year= 1996 |pmid= 8757325 |doi= }}
*{{cite journal | author=Skubitz KM, Campbell KD, Iida J, Skubitz AP |title=CD63 associates with tyrosine kinase activity and CD11/CD18, and transmits an activation signal in neutrophils. |journal=J. Immunol. |volume=157 |issue= 8 |pages= 3617-26 |year= 1996 |pmid= 8871662 |doi= }}
*{{cite journal | author=Berditchevski F, Tolias KF, Wong K, ''et al.'' |title=A novel link between integrins, transmembrane-4 superfamily proteins (CD63 and CD81), and phosphatidylinositol 4-kinase. |journal=J. Biol. Chem. |volume=272 |issue= 5 |pages= 2595-8 |year= 1997 |pmid= 9006891 |doi= }}
*{{cite journal | author=Sincock PM, Mayrhofer G, Ashman LK |title=Localization of the transmembrane 4 superfamily (TM4SF) member PETA-3 (CD151) in normal human tissues: comparison with CD9, CD63, and alpha5beta1 integrin. |journal=J. Histochem. Cytochem. |volume=45 |issue= 4 |pages= 515-25 |year= 1997 |pmid= 9111230 |doi= }}
*{{cite journal | author=Berditchevski F, Chang S, Bodorova J, Hemler ME |title=Generation of monoclonal antibodies to integrin-associated proteins. Evidence that alpha3beta1 complexes with EMMPRIN/basigin/OX47/M6. |journal=J. Biol. Chem. |volume=272 |issue= 46 |pages= 29174-80 |year= 1997 |pmid= 9360995 |doi= }}
*{{cite journal | author=Tachibana I, Bodorova J, Berditchevski F, ''et al.'' |title=NAG-2, a novel transmembrane-4 superfamily (TM4SF) protein that complexes with integrins and other TM4SF proteins. |journal=J. Biol. Chem. |volume=272 |issue= 46 |pages= 29181-9 |year= 1997 |pmid= 9360996 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CDC25A... {November 15, 2007 6:53:52 PM PST}
- SEARCH REDIRECT: Control Box Found: CDC25A {November 15, 2007 6:54:18 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 6:54:19 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 6:54:19 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 6:54:19 PM PST}
- UPDATED: Updated protein page: CDC25A {November 15, 2007 6:54:25 PM PST}
- INFO: Beginning work on COX1... {November 15, 2007 6:57:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:57:45 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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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_COX1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1occ.
| PDB = {{PDB2|1occ}}, {{PDB2|1oco}}, {{PDB2|1ocr}}, {{PDB2|1ocz}}, {{PDB2|1v54}}, {{PDB2|1v55}}, {{PDB2|2dyr}}, {{PDB2|2dys}}, {{PDB2|2eij}}, {{PDB2|2eik}}, {{PDB2|2eil}}, {{PDB2|2eim}}, {{PDB2|2ein}}, {{PDB2|2occ}}
| Name = Cytochrome c oxidase subunit I
| HGNCid = 7419
| Symbol = COX1
| AltSymbols =; MTCO1
| OMIM =
| ECnumber =
| Homologene = 5016
| MGIid = 102504
| Function = {{GNF_GO|id=GO:0004129 |text = cytochrome-c oxidase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005746 |text = mitochondrial respiratory chain}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006123 |text = mitochondrial electron transport, cytochrome c to oxygen}} {{GNF_GO|id=GO:0006810 |text = transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4512
| Hs_Ensembl = ENSG00000198804
| Hs_RefseqProtein = NP_536845
| Hs_RefseqmRNA =
| Hs_GenLoc_db =
| Hs_GenLoc_chr = MT
| Hs_GenLoc_start = 5905
| Hs_GenLoc_end = 7446
| Hs_Uniprot = P00395
| Mm_EntrezGene = 17708
| Mm_Ensembl = ENSMUSG00000064351
| Mm_RefseqmRNA =
| Mm_RefseqProtein = NP_904330
| Mm_GenLoc_db =
| Mm_GenLoc_chr = MT
| Mm_GenLoc_start = 5328
| Mm_GenLoc_end = 6872
| Mm_Uniprot = Q35042
}}
}}
'''Cytochrome c oxidase subunit I''', also known as '''COX1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: COX1 cytochrome c oxidase subunit I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4512| 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=Torroni A, Achilli A, Macaulay V, ''et al.'' |title=Harvesting the fruit of the human mtDNA tree. |journal=Trends Genet. |volume=22 |issue= 6 |pages= 339-45 |year= 2006 |pmid= 16678300 |doi= 10.1016/j.tig.2006.04.001 }}
*{{cite journal | author=Bodenteich A, Mitchell LG, Polymeropoulos MH, Merril CR |title=Dinucleotide repeat in the human mitochondrial D-loop. |journal=Hum. Mol. Genet. |volume=1 |issue= 2 |pages= 140 |year= 1993 |pmid= 1301157 |doi= }}
*{{cite journal | author=Brown MD, Yang CC, Trounce I, ''et al.'' |title=A mitochondrial DNA variant, identified in Leber hereditary optic neuropathy patients, which extends the amino acid sequence of cytochrome c oxidase subunit I. |journal=Am. J. Hum. Genet. |volume=51 |issue= 2 |pages= 378-85 |year= 1992 |pmid= 1322638 |doi= }}
*{{cite journal | author=Lu X, Walker T, MacManus JP, Seligy VL |title=Differentiation of HT-29 human colonic adenocarcinoma cells correlates with increased expression of mitochondrial RNA: effects of trehalose on cell growth and maturation. |journal=Cancer Res. |volume=52 |issue= 13 |pages= 3718-25 |year= 1992 |pmid= 1377597 |doi= }}
*{{cite journal | author=Marzuki S, Noer AS, Lertrit P, ''et al.'' |title=Normal variants of human mitochondrial DNA and translation products: the building of a reference data base. |journal=Hum. Genet. |volume=88 |issue= 2 |pages= 139-45 |year= 1992 |pmid= 1757091 |doi= }}
*{{cite journal | author=Moraes CT, Andreetta F, Bonilla E, ''et al.'' |title=Replication-competent human mitochondrial DNA lacking the heavy-strand promoter region. |journal=Mol. Cell. Biol. |volume=11 |issue= 3 |pages= 1631-7 |year= 1991 |pmid= 1996112 |doi= }}
*{{cite journal | author=Attardi G, Chomyn A, Doolittle RF, ''et al.'' |title=Seven unidentified reading frames of human mitochondrial DNA encode subunits of the respiratory chain NADH dehydrogenase. |journal=Cold Spring Harb. Symp. Quant. Biol. |volume=51 Pt 1 |issue= |pages= 103-14 |year= 1987 |pmid= 3472707 |doi= }}
*{{cite journal | author=Chomyn A, Cleeter MW, Ragan CI, ''et al.'' |title=URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit. |journal=Science |volume=234 |issue= 4776 |pages= 614-8 |year= 1986 |pmid= 3764430 |doi= }}
*{{cite journal | author=Chomyn A, Mariottini P, Cleeter MW, ''et al.'' |title=Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. |journal=Nature |volume=314 |issue= 6012 |pages= 592-7 |year= 1985 |pmid= 3921850 |doi= }}
*{{cite journal | author=Sanger F, Coulson AR, Barrell BG, ''et al.'' |title=Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. |journal=J. Mol. Biol. |volume=143 |issue= 2 |pages= 161-78 |year= 1981 |pmid= 6260957 |doi= }}
*{{cite journal | author=Anderson S, Bankier AT, Barrell BG, ''et al.'' |title=Sequence and organization of the human mitochondrial genome. |journal=Nature |volume=290 |issue= 5806 |pages= 457-65 |year= 1981 |pmid= 7219534 |doi= }}
*{{cite journal | author=Montoya J, Ojala D, Attardi G |title=Distinctive features of the 5'-terminal sequences of the human mitochondrial mRNAs. |journal=Nature |volume=290 |issue= 5806 |pages= 465-70 |year= 1981 |pmid= 7219535 |doi= }}
*{{cite journal | author=Horai S, Hayasaka K, Kondo R, ''et al.'' |title=Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 2 |pages= 532-6 |year= 1995 |pmid= 7530363 |doi= }}
*{{cite journal | author=Gattermann N, Retzlaff S, Wang YL, ''et al.'' |title=Heteroplasmic point mutations of mitochondrial DNA affecting subunit I of cytochrome c oxidase in two patients with acquired idiopathic sideroblastic anemia. |journal=Blood |volume=90 |issue= 12 |pages= 4961-72 |year= 1997 |pmid= 9389715 |doi= }}
*{{cite journal | author=Bröker S, Meunier B, Rich P, ''et al.'' |title=MtDNA mutations associated with sideroblastic anaemia cause a defect of mitochondrial cytochrome c oxidase. |journal=Eur. J. Biochem. |volume=258 |issue= 1 |pages= 132-8 |year= 1998 |pmid= 9851701 |doi= }}
*{{cite journal | author=Andrews RM, Kubacka I, Chinnery PF, ''et al.'' |title=Reanalysis and revision of the Cambridge reference sequence for human mitochondrial DNA. |journal=Nat. Genet. |volume=23 |issue= 2 |pages= 147 |year= 1999 |pmid= 10508508 |doi= 10.1038/13779 }}
*{{cite journal | author=Karadimas CL, Greenstein P, Sue CM, ''et al.'' |title=Recurrent myoglobinuria due to a nonsense mutation in the COX I gene of mitochondrial DNA. |journal=Neurology |volume=55 |issue= 5 |pages= 644-9 |year= 2000 |pmid= 10980727 |doi= }}
*{{cite journal | author=Ingman M, Kaessmann H, Pääbo S, Gyllensten U |title=Mitochondrial genome variation and the origin of modern humans. |journal=Nature |volume=408 |issue= 6813 |pages= 708-13 |year= 2001 |pmid= 11130070 |doi= 10.1038/35047064 }}
*{{cite journal | author=Finnilä S, Lehtonen MS, Majamaa K |title=Phylogenetic network for European mtDNA. |journal=Am. J. Hum. Genet. |volume=68 |issue= 6 |pages= 1475-84 |year= 2001 |pmid= 11349229 |doi= }}
*{{cite journal | author=Maca-Meyer N, González AM, Larruga JM, ''et al.'' |title=Major genomic mitochondrial lineages delineate early human expansions. |journal=BMC Genet. |volume=2 |issue= |pages= 13 |year= 2003 |pmid= 11553319 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CR2... {November 15, 2007 6:54:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:54:48 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CR2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ghq.
| PDB = {{PDB2|1ghq}}, {{PDB2|1ly2}}, {{PDB2|1w2r}}, {{PDB2|1w2s}}, {{PDB2|2gsx}}
| Name = Complement component (3d/Epstein Barr virus) receptor 2
| HGNCid = 2336
| Symbol = CR2
| AltSymbols =; C3DR; CD21
| OMIM = 120650
| ECnumber =
| Homologene = 55611
| MGIid = 88489
| GeneAtlas_image1 = PBB_GE_CR2_205544_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004875 |text = complement receptor activity}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006958 |text = complement activation, classical pathway}} {{GNF_GO|id=GO:0045087 |text = innate immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1380
| Hs_Ensembl = ENSG00000117322
| Hs_RefseqProtein = NP_001006659
| Hs_RefseqmRNA = NM_001006658
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 205694198
| Hs_GenLoc_end = 205729863
| Hs_Uniprot = P20023
| Mm_EntrezGene = 12902
| Mm_Ensembl = ENSMUSG00000026616
| Mm_RefseqmRNA = NM_007758
| Mm_RefseqProtein = NP_031784
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 196841897
| Mm_GenLoc_end = 196877439
| Mm_Uniprot = Q6LAP4
}}
}}
'''Complement component (3d/Epstein Barr virus) receptor 2''', also known as '''CR2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CR2 complement component (3d/Epstein Barr virus) receptor 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1380| 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 = Complement component receptor-2 (CR2) is the membrane protein on B lymphocytes to which the Epstein-Barr virus (EBV) binds during infection of these cells. See also MIM 120620. Yefenof et al. (1976) found complete overlapping of EBV receptors and C3 (MIM 120700) receptors on human B lymphocytes.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: CR2 complement component (3d/Epstein Barr virus) receptor 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1380| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Cooper NR, Bradt BM, Rhim JS, Nemerow GR |title=CR2 complement receptor. |journal=J. Invest. Dermatol. |volume=94 |issue= 6 Suppl |pages= 112S-117S |year= 1990 |pmid= 2161885 |doi= }}
*{{cite journal | author=Yefenof E, Klein G, Jondal M, Oldstone MB |title=Surface markers on human B and T-lymphocytes. IX. Two-color immunofluorescence studies on the association between ebv receptors and complement receptors on the surface of lymphoid cell lines. |journal=Int. J. Cancer |volume=17 |issue= 6 |pages= 693-700 |year= 1976 |pmid= 181330 |doi= }}
*{{cite journal | author=Gauffre A, Viron A, Barel M, ''et al.'' |title=Nuclear localization of the Epstein-Barr virus/C3d receptor (CR2) in the human Burkitt B lymphoma cell, Raji. |journal=Mol. Immunol. |volume=29 |issue= 9 |pages= 1113-20 |year= 1992 |pmid= 1323059 |doi= }}
*{{cite journal | author=Bradbury LE, Kansas GS, Levy S, ''et al.'' |title=The CD19/CD21 signal transducing complex of human B lymphocytes includes the target of antiproliferative antibody-1 and Leu-13 molecules. |journal=J. Immunol. |volume=149 |issue= 9 |pages= 2841-50 |year= 1992 |pmid= 1383329 |doi= }}
*{{cite journal | author=Levy E, Ambrus J, Kahl L, ''et al.'' |title=T lymphocyte expression of complement receptor 2 (CR2/CD21): a role in adhesive cell-cell interactions and dysregulation in a patient with systemic lupus erythematosus (SLE). |journal=Clin. Exp. Immunol. |volume=90 |issue= 2 |pages= 235-44 |year= 1992 |pmid= 1424280 |doi= }}
*{{cite journal | author=Matsumoto AK, Kopicky-Burd J, Carter RH, ''et al.'' |title=Intersection of the complement and immune systems: a signal transduction complex of the B lymphocyte-containing complement receptor type 2 and CD19. |journal=J. Exp. Med. |volume=173 |issue= 1 |pages= 55-64 |year= 1991 |pmid= 1702139 |doi= }}
*{{cite journal | author=Tuveson DA, Ahearn JM, Matsumoto AK, Fearon DT |title=Molecular interactions of complement receptors on B lymphocytes: a CR1/CR2 complex distinct from the CR2/CD19 complex. |journal=J. Exp. Med. |volume=173 |issue= 5 |pages= 1083-9 |year= 1991 |pmid= 1708808 |doi= }}
*{{cite journal | author=Kalli KR, Ahearn JM, Fearon DT |title=Interaction of iC3b with recombinant isotypic and chimeric forms of CR2. |journal=J. Immunol. |volume=147 |issue= 2 |pages= 590-4 |year= 1991 |pmid= 1830068 |doi= }}
*{{cite journal | author=Barel M, Gauffre A, Lyamani F, ''et al.'' |title=Intracellular interaction of EBV/C3d receptor (CR2) with p68, a calcium-binding protein present in normal but not in transformed B lymphocytes. |journal=J. Immunol. |volume=147 |issue= 4 |pages= 1286-91 |year= 1991 |pmid= 1831222 |doi= }}
*{{cite journal | author=Delcayre AX, Salas F, Mathur S, ''et al.'' |title=Epstein Barr virus/complement C3d receptor is an interferon alpha receptor. |journal=EMBO J. |volume=10 |issue= 4 |pages= 919-26 |year= 1991 |pmid= 1849076 |doi= }}
*{{cite journal | author=Kurtz CB, Paul MS, Aegerter M, ''et al.'' |title=Murine complement receptor gene family. II. Identification and characterization of the murine homolog (Cr2) to human CR2 and its molecular linkage to Crry. |journal=J. Immunol. |volume=143 |issue= 6 |pages= 2058-67 |year= 1989 |pmid= 2528587 |doi= }}
*{{cite journal | author=Fujisaku A, Harley JB, Frank MB, ''et al.'' |title=Genomic organization and polymorphisms of the human C3d/Epstein-Barr virus receptor. |journal=J. Biol. Chem. |volume=264 |issue= 4 |pages= 2118-25 |year= 1989 |pmid= 2563370 |doi= }}
*{{cite journal | author=Moore MD, Cooper NR, Tack BF, Nemerow GR |title=Molecular cloning of the cDNA encoding the Epstein-Barr virus/C3d receptor (complement receptor type 2) of human B lymphocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 24 |pages= 9194-8 |year= 1988 |pmid= 2827171 |doi= }}
*{{cite journal | author=Weis JJ, Toothaker LE, Smith JA, ''et al.'' |title=Structure of the human B lymphocyte receptor for C3d and the Epstein-Barr virus and relatedness to other members of the family of C3/C4 binding proteins. |journal=J. Exp. Med. |volume=167 |issue= 3 |pages= 1047-66 |year= 1988 |pmid= 2832506 |doi= }}
*{{cite journal | author=Weis JJ, Fearon DT, Klickstein LB, ''et al.'' |title=Identification of a partial cDNA clone for the C3d/Epstein-Barr virus receptor of human B lymphocytes: homology with the receptor for fragments C3b and C4b of the third and fourth components of complement. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 15 |pages= 5639-43 |year= 1986 |pmid= 3016712 |doi= }}
*{{cite journal | author=Weis JH, Morton CC, Bruns GA, ''et al.'' |title=A complement receptor locus: genes encoding C3b/C4b receptor and C3d/Epstein-Barr virus receptor map to 1q32. |journal=J. Immunol. |volume=138 |issue= 1 |pages= 312-5 |year= 1987 |pmid= 3782802 |doi= }}
*{{cite journal | author=Aubry JP, Pochon S, Gauchat JF, ''et al.'' |title=CD23 interacts with a new functional extracytoplasmic domain involving N-linked oligosaccharides on CD21. |journal=J. Immunol. |volume=152 |issue= 12 |pages= 5806-13 |year= 1994 |pmid= 7515913 |doi= }}
*{{cite journal | author=Matsumoto AK, Martin DR, Carter RH, ''et al.'' |title=Functional dissection of the CD21/CD19/TAPA-1/Leu-13 complex of B lymphocytes. |journal=J. Exp. Med. |volume=178 |issue= 4 |pages= 1407-17 |year= 1993 |pmid= 7690834 |doi= }}
*{{cite journal | author=Barel M, Balbo M, Gauffre A, Frade R |title=Binding sites of the Epstein-Barr virus and C3d receptor (CR2, CD21) for its three intracellular ligands, the p53 anti-oncoprotein, the p68 calcium binding protein and the nuclear p120 ribonucleoprotein. |journal=Mol. Immunol. |volume=32 |issue= 6 |pages= 389-97 |year= 1995 |pmid= 7753047 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CRH... {November 15, 2007 6:54:48 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:55:09 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CRH_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1go9.
| PDB = {{PDB2|1go9}}, {{PDB2|1goe}}
| Name = Corticotropin releasing hormone
| HGNCid = 2355
| Symbol = CRH
| AltSymbols =; CRF
| OMIM = 122560
| ECnumber =
| Homologene = 599
| MGIid = 88496
| GeneAtlas_image1 = PBB_GE_CRH_205630_at_tn.png
| GeneAtlas_image2 = PBB_GE_CRH_205629_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005184 |text = neuropeptide hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007565 |text = female pregnancy}} {{GNF_GO|id=GO:0007567 |text = parturition}} {{GNF_GO|id=GO:0007611 |text = learning and/or memory}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1392
| Hs_Ensembl = ENSG00000147571
| Hs_RefseqProtein = NP_000747
| Hs_RefseqmRNA = NM_000756
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 67251166
| Hs_GenLoc_end = 67253380
| Hs_Uniprot = P06850
| Mm_EntrezGene = 12918
| Mm_Ensembl = ENSMUSG00000049796
| Mm_RefseqmRNA = NM_205769
| Mm_RefseqProtein = NP_991338
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 19885565
| Mm_GenLoc_end = 19887480
| Mm_Uniprot = Q14AA2
}}
}}
'''Corticotropin releasing hormone''', also known as '''CRH''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CRH corticotropin releasing hormone| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1392| 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 = Corticotropin-releasing hormone (CRH) is a 41-amino acid peptide derived from a 191-amino acid preprohormone. CRH is secreted by the paraventricular nucleus (PVN) of the hypothalamus in response to stress. Marked reduction in CRH has been observed in association with Alzheimer disease and autosomal recessive hypothalamic corticotropin dificiency has multiple and potentially fatal metabolic consequences including hypoglycemia and hepatitis. In addition to production in the hypothalamus, CRH is also synthesized in peripheral tissues, such as T lymphocytes and is highly expressed in the placenta. In the placenta CRH is a marker that determines the length of gestation and the timing of parturition and delivery. A rapid increase in circulating levels of CRH occurs at the onset of parturition, suggesting that, in addition to its metabolic functions, CRH may act as a trigger for parturition.<ref name="entrez">{{cite web | title = Entrez Gene: CRH corticotropin releasing hormone| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1392| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Florio P, Severi FM, Ciarmela P, ''et al.'' |title=Placental stress factors and maternal-fetal adaptive response: the corticotropin-releasing factor family. |journal=Endocrine |volume=19 |issue= 1 |pages= 91-102 |year= 2003 |pmid= 12583606 |doi= }}
*{{cite journal | author=Florio P, Rossi M, Sigurdardottir M, ''et al.'' |title=Paracrine regulation of endometrial function: interaction between progesterone and corticotropin-releasing factor (CRF) and activin A. |journal=Steroids |volume=68 |issue= 10-13 |pages= 801-7 |year= 2004 |pmid= 14667971 |doi= }}
*{{cite journal | author=Vamvakopoulos NC, Karl M, Mayol V, ''et al.'' |title=Structural analysis of the regulatory region of the human corticotropin releasing hormone gene. |journal=FEBS Lett. |volume=267 |issue= 1 |pages= 1-5 |year= 1990 |pmid= 2365075 |doi= }}
*{{cite journal | author=Robinson BG, D'Angio LA, Pasieka KB, Majzoub JA |title=Preprocorticotropin releasing hormone: cDNA sequence and in vitro processing. |journal=Mol. Cell. Endocrinol. |volume=61 |issue= 2 |pages= 175-80 |year= 1989 |pmid= 2783917 |doi= }}
*{{cite journal | author=Arbiser JL, Morton CC, Bruns GA, Majzoub JA |title=Human corticotropin releasing hormone gene is located on the long arm of chromosome 8. |journal=Cytogenet. Cell Genet. |volume=47 |issue= 3 |pages= 113-6 |year= 1988 |pmid= 3259914 |doi= }}
*{{cite journal | author=Sasaki A, Tempst P, Liotta AS, ''et al.'' |title=Isolation and characterization of a corticotropin-releasing hormone-like peptide from human placenta. |journal=J. Clin. Endocrinol. Metab. |volume=67 |issue= 4 |pages= 768-73 |year= 1988 |pmid= 3262120 |doi= }}
*{{cite journal | author=Shibahara S, Morimoto Y, Furutani Y, ''et al.'' |title=Isolation and sequence analysis of the human corticotropin-releasing factor precursor gene. |journal=EMBO J. |volume=2 |issue= 5 |pages= 775-9 |year= 1984 |pmid= 6605851 |doi= }}
*{{cite journal | author=Behan DP, Heinrichs SC, Troncoso JC, ''et al.'' |title=Displacement of corticotropin releasing factor from its binding protein as a possible treatment for Alzheimer's disease. |journal=Nature |volume=378 |issue= 6554 |pages= 284-7 |year= 1995 |pmid= 7477348 |doi= 10.1038/378284a0 }}
*{{cite journal | author=Kawahito Y, Sano H, Mukai S, ''et al.'' |title=Corticotropin releasing hormone in colonic mucosa in patients with ulcerative colitis. |journal=Gut |volume=37 |issue= 4 |pages= 544-51 |year= 1996 |pmid= 7489943 |doi= }}
*{{cite journal | author=McLean M, Bisits A, Davies J, ''et al.'' |title=A placental clock controlling the length of human pregnancy. |journal=Nat. Med. |volume=1 |issue= 5 |pages= 460-3 |year= 1995 |pmid= 7585095 |doi= }}
*{{cite journal | author=Slominski A, Ermak G, Hwang J, ''et al.'' |title=Proopiomelanocortin, corticotropin releasing hormone and corticotropin releasing hormone receptor genes are expressed in human skin. |journal=FEBS Lett. |volume=374 |issue= 1 |pages= 113-6 |year= 1995 |pmid= 7589495 |doi= }}
*{{cite journal | author=Sutton SW, Behan DP, Lahrichi SL, ''et al.'' |title=Ligand requirements of the human corticotropin-releasing factor-binding protein. |journal=Endocrinology |volume=136 |issue= 3 |pages= 1097-102 |year= 1995 |pmid= 7867564 |doi= }}
*{{cite journal | author=Vamvakopoulos NC, Chrousos GP |title=Structural organization of the 5' flanking region of the human corticotropin releasing hormone gene. |journal=DNA Seq. |volume=4 |issue= 3 |pages= 197-206 |year= 1994 |pmid= 8161822 |doi= }}
*{{cite journal | author=Perrin MH, Donaldson CJ, Chen R, ''et al.'' |title=Cloning and functional expression of a rat brain corticotropin releasing factor (CRF) receptor. |journal=Endocrinology |volume=133 |issue= 6 |pages= 3058-61 |year= 1994 |pmid= 8243338 |doi= }}
*{{cite journal | author=Romier C, Bernassau JM, Cambillau C, Darbon H |title=Solution structure of human corticotropin releasing factor by 1H NMR and distance geometry with restrained molecular dynamics. |journal=Protein Eng. |volume=6 |issue= 2 |pages= 149-56 |year= 1993 |pmid= 8386360 |doi= }}
*{{cite journal | author=Liaw CW, Grigoriadis DE, Lovenberg TW, ''et al.'' |title=Localization of ligand-binding domains of human corticotropin-releasing factor receptor: a chimeric receptor approach. |journal=Mol. Endocrinol. |volume=11 |issue= 7 |pages= 980-5 |year= 1997 |pmid= 9178757 |doi= }}
*{{cite journal | author=Timpl P, Spanagel R, Sillaber I, ''et al.'' |title=Impaired stress response and reduced anxiety in mice lacking a functional corticotropin-releasing hormone receptor 1. |journal=Nat. Genet. |volume=19 |issue= 2 |pages= 162-6 |year= 1998 |pmid= 9620773 |doi= 10.1038/520 }}
*{{cite journal | author=Perone MJ, Murray CA, Brown OA, ''et al.'' |title=Procorticotrophin-releasing hormone: endoproteolytic processing and differential release of its derived peptides within AtT20 cells. |journal=Mol. Cell. Endocrinol. |volume=142 |issue= 1-2 |pages= 191-202 |year= 1998 |pmid= 9783915 |doi= }}
*{{cite journal | author=Willenberg HS, Bornstein SR, Hiroi N, ''et al.'' |title=Effects of a novel corticotropin-releasing-hormone receptor type I antagonist on human adrenal function. |journal=Mol. Psychiatry |volume=5 |issue= 2 |pages= 137-41 |year= 2000 |pmid= 10822340 |doi= }}
*{{cite journal | author=Saeed B, Fawcett M, Self C |title=Corticotropin-releasing hormone binding to the syncytiotrophoblast membranes. |journal=Eur. J. Clin. Invest. |volume=31 |issue= 2 |pages= 125-30 |year= 2001 |pmid= 11168450 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYCS... {November 15, 2007 7:04:04 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:04:34 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CYCS_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1j3s.
| PDB = {{PDB2|1j3s}}, {{PDB2|2b4z}}
| Name = Cytochrome c, somatic
| HGNCid = 19986
| Symbol = CYCS
| AltSymbols =; HCS; CYC
| OMIM = 123970
| ECnumber =
| Homologene = 68675
| MGIid = 88578
| GeneAtlas_image1 = PBB_GE_CYCS_208905_at_tn.png
| Function = {{GNF_GO|id=GO:0000158 |text = protein phosphatase type 2A activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0045155 |text = electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0000159 |text = protein phosphatase type 2A complex}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005746 |text = mitochondrial respiratory chain}} {{GNF_GO|id=GO:0005758 |text = mitochondrial intermembrane space}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006309 |text = DNA fragmentation during apoptosis}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0008635 |text = caspase activation via cytochrome c}} {{GNF_GO|id=GO:0045333 |text = cellular respiration}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 54205
| Hs_Ensembl = ENSG00000172115
| Hs_RefseqProtein = NP_061820
| Hs_RefseqmRNA = NM_018947
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 25124802
| Hs_GenLoc_end = 25131480
| Hs_Uniprot = P99999
| Mm_EntrezGene = 13063
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_975140
| Mm_RefseqProtein = XP_980234
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Cytochrome c, somatic''', also known as '''CYCS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CYCS cytochrome c, somatic| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54205| 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 cytochrome c, a component of the electron transport chain in mitochondria. The heme group of cytochrome c accepts electrons from the b-c1 complex and transfers electrons to the cytochrome oxidase complex. Cytochrome c is also involved in initiation of apoptosis. Upon release of cytochrome c to the cytoplasm, the protein binds apoptotic protease activating factor which activates the apoptotic initiator procaspase 9. Many cytochrome c pseudogenes exist, scattered throughout the human genome.<ref name="entrez">{{cite web | title = Entrez Gene: CYCS cytochrome c, somatic| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54205| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Skulachev VP |title=Cytochrome c in the apoptotic and antioxidant cascades. |journal=FEBS Lett. |volume=423 |issue= 3 |pages= 275-80 |year= 1998 |pmid= 9515723 |doi= }}
*{{cite journal | author=Mannella CA |title=Conformational changes in the mitochondrial channel protein, VDAC, and their functional implications. |journal=J. Struct. Biol. |volume=121 |issue= 2 |pages= 207-18 |year= 1998 |pmid= 9615439 |doi= 10.1006/jsbi.1997.3954 }}
*{{cite journal | author=Ferri KF, Jacotot E, Blanco J, ''et al.'' |title=Mitochondrial control of cell death induced by HIV-1-encoded proteins. |journal=Ann. N. Y. Acad. Sci. |volume=926 |issue= |pages= 149-64 |year= 2001 |pmid= 11193032 |doi= }}
*{{cite journal | author=Britton RS, Leicester KL, Bacon BR |title=Iron toxicity and chelation therapy. |journal=Int. J. Hematol. |volume=76 |issue= 3 |pages= 219-28 |year= 2002 |pmid= 12416732 |doi= }}
*{{cite journal | author=Haider N, Narula N, Narula J |title=Apoptosis in heart failure represents programmed cell survival, not death, of cardiomyocytes and likelihood of reverse remodeling. |journal=J. Card. Fail. |volume=8 |issue= 6 Suppl |pages= S512-7 |year= 2003 |pmid= 12555167 |doi= 10.1054/jcaf.2002.130034 }}
*{{cite journal | author=Castedo M, Perfettini JL, Andreau K, ''et al.'' |title=Mitochondrial apoptosis induced by the HIV-1 envelope. |journal=Ann. N. Y. Acad. Sci. |volume=1010 |issue= |pages= 19-28 |year= 2004 |pmid= 15033690 |doi= }}
*{{cite journal | author=Ng S, Smith MB, Smith HT, Millett F |title=Effect of modification of individual cytochrome c lysines on the reaction with cytochrome b5. |journal=Biochemistry |volume=16 |issue= 23 |pages= 4975-8 |year= 1977 |pmid= 199233 |doi= }}
*{{cite journal | author=Lynch SR, Sherman D, Copeland RA |title=Cytochrome c binding affects the conformation of cytochrome a in cytochrome c oxidase. |journal=J. Biol. Chem. |volume=267 |issue= 1 |pages= 298-302 |year= 1992 |pmid= 1309738 |doi= }}
*{{cite journal | author=Garber EA, Margoliash E |title=Interaction of cytochrome c with cytochrome c oxidase: an understanding of the high- to low-affinity transition. |journal=Biochim. Biophys. Acta |volume=1015 |issue= 2 |pages= 279-87 |year= 1990 |pmid= 2153405 |doi= }}
*{{cite journal | author=Bedetti CD |title=Immunocytochemical demonstration of cytochrome c oxidase with an immunoperoxidase method: a specific stain for mitochondria in formalin-fixed and paraffin-embedded human tissues. |journal=J. Histochem. Cytochem. |volume=33 |issue= 5 |pages= 446-52 |year= 1985 |pmid= 2580882 |doi= }}
*{{cite journal | author=Tanaka Y, Ashikari T, Shibano Y, ''et al.'' |title=Construction of a human cytochrome c gene and its functional expression in Saccharomyces cerevisiae. |journal=J. Biochem. |volume=103 |issue= 6 |pages= 954-61 |year= 1988 |pmid= 2844747 |doi= }}
*{{cite journal | author=Evans MJ, Scarpulla RC |title=The human somatic cytochrome c gene: two classes of processed pseudogenes demarcate a period of rapid molecular evolution. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 24 |pages= 9625-9 |year= 1989 |pmid= 2849112 |doi= }}
*{{cite journal | author=Passon PG, Hultquist DE |title=Soluble cytochrome b 5 reductase from human erythrocytes. |journal=Biochim. Biophys. Acta |volume=275 |issue= 1 |pages= 62-73 |year= 1972 |pmid= 4403130 |doi= }}
*{{cite journal | author=Dowe RJ, Vitello LB, Erman JE |title=Sedimentation equilibrium studies on the interaction between cytochrome c and cytochrome c peroxidase. |journal=Arch. Biochem. Biophys. |volume=232 |issue= 2 |pages= 566-73 |year= 1984 |pmid= 6087732 |doi= }}
*{{cite journal | author=Michel B, Bosshard HR |title=Spectroscopic analysis of the interaction between cytochrome c and cytochrome c oxidase. |journal=J. Biol. Chem. |volume=259 |issue= 16 |pages= 10085-91 |year= 1984 |pmid= 6088481 |doi= }}
*{{cite journal | author=Broger C, Nałecz MJ, Azzi A |title=Interaction of cytochrome c with cytochrome bc1 complex of the mitochondrial respiratory chain. |journal=Biochim. Biophys. Acta |volume=592 |issue= 3 |pages= 519-27 |year= 1980 |pmid= 6251869 |doi= }}
*{{cite journal | author=Smith HT, Ahmed AJ, Millett F |title=Electrostatic interaction of cytochrome c with cytochrome c1 and cytochrome oxidase. |journal=J. Biol. Chem. |volume=256 |issue= 10 |pages= 4984-90 |year= 1981 |pmid= 6262312 |doi= }}
*{{cite journal | author=Geren LM, Millett F |title=Fluorescence energy transfer studies of the interaction between adrenodoxin and cytochrome c. |journal=J. Biol. Chem. |volume=256 |issue= 20 |pages= 10485-9 |year= 1981 |pmid= 6270113 |doi= }}
*{{cite journal | author=Favre B, Zolnierowicz S, Turowski P, Hemmings BA |title=The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo. |journal=J. Biol. Chem. |volume=269 |issue= 23 |pages= 16311-7 |year= 1994 |pmid= 8206937 |doi= }}
*{{cite journal | author=Gao B, Eisenberg E, Greene L |title=Effect of constitutive 70-kDa heat shock protein polymerization on its interaction with protein substrate. |journal=J. Biol. Chem. |volume=271 |issue= 28 |pages= 16792-7 |year= 1996 |pmid= 8663341 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EPAS1... {November 15, 2007 6:55:09 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:55:37 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_EPAS1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1p97.
| PDB = {{PDB2|1p97}}, {{PDB2|2a24}}
| Name = Endothelial PAS domain protein 1
| HGNCid = 3374
| Symbol = EPAS1
| AltSymbols =; HIF2A; HLF; MOP2; PASD2
| OMIM = 603349
| ECnumber =
| Homologene = 1095
| MGIid = 109169
| GeneAtlas_image1 = PBB_GE_EPAS1_200878_at_tn.png
| GeneAtlas_image2 = PBB_GE_EPAS1_200879_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003705 |text = RNA polymerase II transcription factor activity, enhancer binding}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0035035 |text = histone acetyltransferase binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0001666 |text = response to hypoxia}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2034
| Hs_Ensembl = ENSG00000116016
| Hs_RefseqProtein = NP_001421
| Hs_RefseqmRNA = NM_001430
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 46378045
| Hs_GenLoc_end = 46467340
| Hs_Uniprot = Q99814
| Mm_EntrezGene = 13819
| Mm_Ensembl = ENSMUSG00000024140
| Mm_RefseqmRNA = XM_986887
| Mm_RefseqProtein = XP_991981
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 86662228
| Mm_GenLoc_end = 86739907
| Mm_Uniprot = Q6PEU2
}}
}}
'''Endothelial PAS domain protein 1''', also known as '''EPAS1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EPAS1 endothelial PAS domain protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2034| 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=Brahimi-Horn MC, Pouysségur J |title=The hypoxia-inducible factor and tumor progression along the angiogenic pathway. |journal=Int. Rev. Cytol. |volume=242 |issue= |pages= 157-213 |year= 2005 |pmid= 15598469 |doi= 10.1016/S0074-7696(04)42004-X }}
*{{cite journal | author=Haase VH |title=Hypoxia-inducible factors in the kidney. |journal=Am. J. Physiol. Renal Physiol. |volume=291 |issue= 2 |pages= F271-81 |year= 2006 |pmid= 16554418 |doi= 10.1152/ajprenal.00071.2006 }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal | author=Tian H, McKnight SL, Russell DW |title=Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells. |journal=Genes Dev. |volume=11 |issue= 1 |pages= 72-82 |year= 1997 |pmid= 9000051 |doi= }}
*{{cite journal | author=Hogenesch JB, Chan WK, Jackiw VH, ''et al.'' |title=Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8581-93 |year= 1997 |pmid= 9079689 |doi= }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
*{{cite journal | author=Ema M, Taya S, Yokotani N, ''et al.'' |title=A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1alpha regulates the VEGF expression and is potentially involved in lung and vascular development. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 9 |pages= 4273-8 |year= 1997 |pmid= 9113979 |doi= }}
*{{cite journal | author=Hogenesch JB, Gu YZ, Jain S, Bradfield CA |title=The basic-helix-loop-helix-PAS orphan MOP3 forms transcriptionally active complexes with circadian and hypoxia factors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 10 |pages= 5474-9 |year= 1998 |pmid= 9576906 |doi= }}
*{{cite journal | author=Takahata S, Sogawa K, Kobayashi A, ''et al.'' |title=Transcriptionally active heterodimer formation of an Arnt-like PAS protein, Arnt3, with HIF-1a, HLF, and clock. |journal=Biochem. Biophys. Res. Commun. |volume=248 |issue= 3 |pages= 789-94 |year= 1998 |pmid= 9704006 |doi= 10.1006/bbrc.1998.9012 }}
*{{cite journal | author=Ema M, Hirota K, Mimura J, ''et al.'' |title=Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300. |journal=EMBO J. |volume=18 |issue= 7 |pages= 1905-14 |year= 1999 |pmid= 10202154 |doi= 10.1093/emboj/18.7.1905 }}
*{{cite journal | author=Cockman ME, Masson N, Mole DR, ''et al.'' |title=Hypoxia inducible factor-alpha binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein. |journal=J. Biol. Chem. |volume=275 |issue= 33 |pages= 25733-41 |year= 2000 |pmid= 10823831 |doi= 10.1074/jbc.M002740200 }}
*{{cite journal | author=Maemura K, de la Monte SM, Chin MT, ''et al.'' |title=CLIF, a novel cycle-like factor, regulates the circadian oscillation of plasminogen activator inhibitor-1 gene expression. |journal=J. Biol. Chem. |volume=275 |issue= 47 |pages= 36847-51 |year= 2001 |pmid= 11018023 |doi= 10.1074/jbc.C000629200 }}
*{{cite journal | author=Luo JC, Shibuya M |title=A variant of nuclear localization signal of bipartite-type is required for the nuclear translocation of hypoxia inducible factors (1alpha, 2alpha and 3alpha). |journal=Oncogene |volume=20 |issue= 12 |pages= 1435-44 |year= 2001 |pmid= 11313887 |doi= 10.1038/sj.onc.1204228 }}
*{{cite journal | author=Woods SL, Whitelaw ML |title=Differential activities of murine single minded 1 (SIM1) and SIM2 on a hypoxic response element. Cross-talk between basic helix-loop-helix/per-Arnt-Sim homology transcription factors. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 10236-43 |year= 2002 |pmid= 11782478 |doi= 10.1074/jbc.M110752200 }}
*{{cite journal | author=Lando D, Peet DJ, Whelan DA, ''et al.'' |title=Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch. |journal=Science |volume=295 |issue= 5556 |pages= 858-61 |year= 2002 |pmid= 11823643 |doi= 10.1126/science.1068592 }}
*{{cite journal | author=Mole DR, Pugh CW, Ratcliffe PJ, Maxwell PH |title=Regulation of the HIF pathway: enzymatic hydroxylation of a conserved prolyl residue in hypoxia-inducible factor alpha subunits governs capture by the pVHL E3 ubiquitin ligase complex. |journal=Adv. Enzyme Regul. |volume=42 |issue= |pages= 333-47 |year= 2002 |pmid= 12123724 |doi= }}
*{{cite journal | author=Sivridis E, Giatromanolaki A, Gatter KC, ''et al.'' |title=Association of hypoxia-inducible factors 1alpha and 2alpha with activated angiogenic pathways and prognosis in patients with endometrial carcinoma. |journal=Cancer |volume=95 |issue= 5 |pages= 1055-63 |year= 2002 |pmid= 12209691 |doi= 10.1002/cncr.10774 }}
*{{cite journal | author=Elvert G, Kappel A, Heidenreich R, ''et al.'' |title=Cooperative interaction of hypoxia-inducible factor-2alpha (HIF-2alpha ) and Ets-1 in the transcriptional activation of vascular endothelial growth factor receptor-2 (Flk-1). |journal=J. Biol. Chem. |volume=278 |issue= 9 |pages= 7520-30 |year= 2003 |pmid= 12464608 |doi= 10.1074/jbc.M211298200 }}
*{{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=Sang N, Stiehl DP, Bohensky J, ''et al.'' |title=MAPK signaling up-regulates the activity of hypoxia-inducible factors by its effects on p300. |journal=J. Biol. Chem. |volume=278 |issue= 16 |pages= 14013-9 |year= 2003 |pmid= 12588875 |doi= 10.1074/jbc.M209702200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FEN1... {November 15, 2007 6:55:37 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:56:04 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_FEN1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ul1.
| PDB = {{PDB2|1ul1}}
| Name = Flap structure-specific endonuclease 1
| HGNCid = 3650
| Symbol = FEN1
| AltSymbols =; FEN-1; MF1; RAD2
| OMIM = 600393
| ECnumber =
| Homologene = 3034
| MGIid = 102779
| GeneAtlas_image1 = PBB_GE_FEN1_204767_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FEN1_204768_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0003684 |text = damaged DNA binding}} {{GNF_GO|id=GO:0003690 |text = double-stranded DNA binding}} {{GNF_GO|id=GO:0004519 |text = endonuclease activity}} {{GNF_GO|id=GO:0004523 |text = ribonuclease H activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008309 |text = double-stranded DNA specific exodeoxyribonuclease activity}} {{GNF_GO|id=GO:0008409 |text = 5'-3' exonuclease activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0017108 |text = 5'-flap endonuclease activity}} {{GNF_GO|id=GO:0030145 |text = manganese ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006260 |text = DNA replication}} {{GNF_GO|id=GO:0006302 |text = double-strand break repair}} {{GNF_GO|id=GO:0009650 |text = UV protection}} {{GNF_GO|id=GO:0048015 |text = phosphoinositide-mediated signaling}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2237
| Hs_Ensembl = ENSG00000168496
| Hs_RefseqProtein = NP_004102
| Hs_RefseqmRNA = NM_004111
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 61316726
| Hs_GenLoc_end = 61321284
| Hs_Uniprot = P39748
| Mm_EntrezGene = 14156
| Mm_Ensembl = ENSMUSG00000024742
| Mm_RefseqmRNA = NM_007999
| Mm_RefseqProtein = NP_032025
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 10266184
| Mm_GenLoc_end = 10270988
| Mm_Uniprot = Q3TGH6
}}
}}
'''Flap structure-specific endonuclease 1''', also known as '''FEN1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FEN1 flap structure-specific endonuclease 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2237| 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 removes 5' overhanging flaps in DNA repair and processes the 5' ends of Okazaki fragments in lagging strand DNA synthesis. Direct physical interaction between this protein and AP endonuclease 1 during long-patch base excision repair provides coordinated loading of the proteins onto the substrate, thus passing the substrate from one enzyme to another. The protein is a member of the XPG/RAD2 endonuclease family and is one of ten proteins essential for cell-free DNA replication. DNA secondary structure can inhibit flap processing at certain trinucleotide repeats in a length-dependent manner by concealing the 5' end of the flap that is necessary for both binding and cleavage by the protein encoded by this gene. Therefore, secondary structure can deter the protective function of this protein, leading to site-specific trinucleotide expansions.<ref name="entrez">{{cite web | title = Entrez Gene: FEN1 flap structure-specific endonuclease 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2237| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kemeny MM, Alava G, Oliver JM |title=Improving responses in hepatomas with circadian-patterned hepatic artery infusions of recombinant interleukin-2. |journal=J. Immunother. |volume=12 |issue= 4 |pages= 219-23 |year= 1993 |pmid= 1477073 |doi= }}
*{{cite journal | author=Li X, Li J, Harrington J, ''et al.'' |title=Lagging strand DNA synthesis at the eukaryotic replication fork involves binding and stimulation of FEN-1 by proliferating cell nuclear antigen. |journal=J. Biol. Chem. |volume=270 |issue= 38 |pages= 22109-12 |year= 1995 |pmid= 7673186 |doi= }}
*{{cite journal | author=Hiraoka LR, Harrington JJ, Gerhard DS, ''et al.'' |title=Sequence of human FEN-1, a structure-specific endonuclease, and chromosomal localization of the gene (FEN1) in mouse and human. |journal=Genomics |volume=25 |issue= 1 |pages= 220-5 |year= 1995 |pmid= 7774922 |doi= }}
*{{cite journal | author=Robins P, Pappin DJ, Wood RD, Lindahl T |title=Structural and functional homology between mammalian DNase IV and the 5'-nuclease domain of Escherichia coli DNA polymerase I. |journal=J. Biol. Chem. |volume=269 |issue= 46 |pages= 28535-8 |year= 1994 |pmid= 7961795 |doi= }}
*{{cite journal | author=Murray JM, Tavassoli M, al-Harithy R, ''et al.'' |title=Structural and functional conservation of the human homolog of the Schizosaccharomyces pombe rad2 gene, which is required for chromosome segregation and recovery from DNA damage. |journal=Mol. Cell. Biol. |volume=14 |issue= 7 |pages= 4878-88 |year= 1994 |pmid= 8007985 |doi= }}
*{{cite journal | author=Harrington JJ, Lieber MR |title=The characterization of a mammalian DNA structure-specific endonuclease. |journal=EMBO J. |volume=13 |issue= 5 |pages= 1235-46 |year= 1994 |pmid= 8131753 |doi= }}
*{{cite journal | author=Shen B, Nolan JP, Sklar LA, Park MS |title=Essential amino acids for substrate binding and catalysis of human flap endonuclease 1. |journal=J. Biol. Chem. |volume=271 |issue= 16 |pages= 9173-6 |year= 1996 |pmid= 8621570 |doi= }}
*{{cite journal | author=Chen U, Chen S, Saha P, Dutta A |title=p21Cip1/Waf1 disrupts the recruitment of human Fen1 by proliferating-cell nuclear antigen into the DNA replication complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 21 |pages= 11597-602 |year= 1996 |pmid= 8876181 |doi= }}
*{{cite journal | author=Warbrick E, Lane DP, Glover DM, Cox LS |title=Homologous regions of Fen1 and p21Cip1 compete for binding to the same site on PCNA: a potential mechanism to co-ordinate DNA replication and repair. |journal=Oncogene |volume=14 |issue= 19 |pages= 2313-21 |year= 1997 |pmid= 9178907 |doi= 10.1038/sj.onc.1201072 }}
*{{cite journal | author=Klungland A, Lindahl T |title=Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1). |journal=EMBO J. |volume=16 |issue= 11 |pages= 3341-8 |year= 1997 |pmid= 9214649 |doi= 10.1093/emboj/16.11.3341 }}
*{{cite journal | author=Gary R, Ludwig DL, Cornelius HL, ''et al.'' |title=The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21. |journal=J. Biol. Chem. |volume=272 |issue= 39 |pages= 24522-9 |year= 1997 |pmid= 9305916 |doi= }}
*{{cite journal | author=Stöhr H, Marquardt A, Rivera A, ''et al.'' |title=A gene map of the Best's vitelliform macular dystrophy region in chromosome 11q12-q13.1. |journal=Genome Res. |volume=8 |issue= 1 |pages= 48-56 |year= 1998 |pmid= 9445487 |doi= }}
*{{cite journal | author=Jónsson ZO, Hindges R, Hübscher U |title=Regulation of DNA replication and repair proteins through interaction with the front side of proliferating cell nuclear antigen. |journal=EMBO J. |volume=17 |issue= 8 |pages= 2412-25 |year= 1998 |pmid= 9545252 |doi= 10.1093/emboj/17.8.2412 }}
*{{cite journal | author=Warbrick E, Heatherington W, Lane DP, Glover DM |title=PCNA binding proteins in Drosophila melanogaster : the analysis of a conserved PCNA binding domain. |journal=Nucleic Acids Res. |volume=26 |issue= 17 |pages= 3925-32 |year= 1998 |pmid= 9705499 |doi= }}
*{{cite journal | author=Hosfield DJ, Mol CD, Shen B, Tainer JA |title=Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity. |journal=Cell |volume=95 |issue= 1 |pages= 135-46 |year= 1998 |pmid= 9778254 |doi= }}
*{{cite journal | author=Dianov GL, Jensen BR, Kenny MK, Bohr VA |title=Replication protein A stimulates proliferating cell nuclear antigen-dependent repair of abasic sites in DNA by human cell extracts. |journal=Biochemistry |volume=38 |issue= 34 |pages= 11021-5 |year= 1999 |pmid= 10460157 |doi= 10.1021/bi9908890 }}
*{{cite journal | author=Greene AL, Snipe JR, Gordenin DA, Resnick MA |title=Functional analysis of human FEN1 in Saccharomyces cerevisiae and its role in genome stability. |journal=Hum. Mol. Genet. |volume=8 |issue= 12 |pages= 2263-73 |year= 1999 |pmid= 10545607 |doi= }}
*{{cite journal | author=Matsumoto Y, Kim K, Hurwitz J, ''et al.'' |title=Reconstitution of proliferating cell nuclear antigen-dependent repair of apurinic/apyrimidinic sites with purified human proteins. |journal=J. Biol. Chem. |volume=274 |issue= 47 |pages= 33703-8 |year= 1999 |pmid= 10559261 |doi= }}
*{{cite journal | author=Spiro C, Pelletier R, Rolfsmeier ML, ''et al.'' |title=Inhibition of FEN-1 processing by DNA secondary structure at trinucleotide repeats. |journal=Mol. Cell |volume=4 |issue= 6 |pages= 1079-85 |year= 2000 |pmid= 10635332 |doi= }}
*{{cite journal | author=Hasan S, Stucki M, Hassa PO, ''et al.'' |title=Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300. |journal=Mol. Cell |volume=7 |issue= 6 |pages= 1221-31 |year= 2001 |pmid= 11430825 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FTL... {November 15, 2007 6:56:04 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:56:26 PM 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_FTL_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ffx.
| PDB = {{PDB2|2ffx}}, {{PDB2|2fg4}}, {{PDB2|2fg8}}
| Name = Ferritin, light polypeptide
| HGNCid = 3999
| Symbol = FTL
| AltSymbols =; MGC71996
| OMIM = 134790
| ECnumber =
| Homologene = 79330
| MGIid = 95590
| GeneAtlas_image1 = PBB_GE_FTL_212788_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_FTL_213187_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005488 |text = binding}} {{GNF_GO|id=GO:0008199 |text = ferric iron binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0008043 |text = ferritin complex}}
| Process = {{GNF_GO|id=GO:0006826 |text = iron ion transport}} {{GNF_GO|id=GO:0006879 |text = cellular iron ion homeostasis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2512
| Hs_Ensembl = ENSG00000087086
| Hs_RefseqProtein = NP_000137
| Hs_RefseqmRNA = NM_000146
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 54160378
| Hs_GenLoc_end = 54161850
| Hs_Uniprot = P02792
| Mm_EntrezGene = 14337
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_008049
| Mm_RefseqProtein = NP_032075
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Ferritin, light polypeptide''', also known as '''FTL''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FTL ferritin, light polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2512| 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 light subunit of the ferritin protein. Ferritin is the major intracellular iron storage protein in prokaryotes and eukaryotes. It is composed of 24 subunits of the heavy and light ferritin chains. Variation in ferritin subunit composition may affect the rates of iron uptake and release in different tissues. A major function of ferritin is the storage of iron in a soluble and nontoxic state. Defects in this light chain ferritin gene are associated with several neurodegenerative diseases and hyperferritinemia-cataract syndrome. This gene has multiple pseudogenes.<ref name="entrez">{{cite web | title = Entrez Gene: FTL ferritin, light polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2512| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Munro HN, Aziz N, Leibold EA, ''et al.'' |title=The ferritin genes: structure, expression, and regulation. |journal=Ann. N. Y. Acad. Sci. |volume=526 |issue= |pages= 113-23 |year= 1988 |pmid= 3291676 |doi= }}
*{{cite journal | author=Cazzola M, Skoda RC |title=Translational pathophysiology: a novel molecular mechanism of human disease. |journal=Blood |volume=95 |issue= 11 |pages= 3280-8 |year= 2000 |pmid= 10828006 |doi= }}
*{{cite journal | author=Arosio P, Adelman TG, Drysdale JW |title=On ferritin heterogeneity. Further evidence for heteropolymers. |journal=J. Biol. Chem. |volume=253 |issue= 12 |pages= 4451-8 |year= 1978 |pmid= 659425 |doi= }}
*{{cite journal | author=Gatti RA, Shaked R, Mohandas TK, Salser W |title=Human ferritin genes: chromosomal assignments and polymorphisms. |journal=Am. J. Hum. Genet. |volume=41 |issue= 4 |pages= 654-67 |year= 1987 |pmid= 2821803 |doi= }}
*{{cite journal | author=Lebo RV, Kan YW, Cheung MC, ''et al.'' |title=Human ferritin light chain gene sequences mapped to several sorted chromosomes. |journal=Hum. Genet. |volume=71 |issue= 4 |pages= 325-8 |year= 1986 |pmid= 3000916 |doi= }}
*{{cite journal | author=Chou CC, Gatti RA, Fuller ML, ''et al.'' |title=Structure and expression of ferritin genes in a human promyelocytic cell line that differentiates in vitro. |journal=Mol. Cell. Biol. |volume=6 |issue= 2 |pages= 566-73 |year= 1987 |pmid= 3023856 |doi= }}
*{{cite journal | author=Santoro C, Marone M, Ferrone M, ''et al.'' |title=Cloning of the gene coding for human L apoferritin. |journal=Nucleic Acids Res. |volume=14 |issue= 7 |pages= 2863-76 |year= 1986 |pmid= 3754330 |doi= }}
*{{cite journal | author=Boyd D, Vecoli C, Belcher DM, ''et al.'' |title=Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones. |journal=J. Biol. Chem. |volume=260 |issue= 21 |pages= 11755-61 |year= 1985 |pmid= 3840162 |doi= }}
*{{cite journal | author=Worwood M, Brook JD, Cragg SJ, ''et al.'' |title=Assignment of human ferritin genes to chromosomes 11 and 19q13.3----19qter. |journal=Hum. Genet. |volume=69 |issue= 4 |pages= 371-4 |year= 1985 |pmid= 3857215 |doi= }}
*{{cite journal | author=Dörner MH, Salfeld J, Will H, ''et al.'' |title=Structure of human ferritin light subunit messenger RNA: comparison with heavy subunit message and functional implications. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 10 |pages= 3139-43 |year= 1985 |pmid= 3858810 |doi= }}
*{{cite journal | author=Caskey JH, Jones C, Miller YE, Seligman PA |title=Human ferritin gene is assigned to chromosome 19. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 2 |pages= 482-6 |year= 1983 |pmid= 6572903 |doi= }}
*{{cite journal | author=Addison JM, Fitton JE, Lewis WG, ''et al.'' |title=The amino acid sequence of human liver apoferritin. |journal=FEBS Lett. |volume=164 |issue= 1 |pages= 139-44 |year= 1984 |pmid= 6653779 |doi= }}
*{{cite journal | author=Girelli D, Corrocher R, Bisceglia L, ''et al.'' |title=Molecular basis for the recently described hereditary hyperferritinemia-cataract syndrome: a mutation in the iron-responsive element of ferritin L-subunit gene (the "Verona mutation") |journal=Blood |volume=86 |issue= 11 |pages= 4050-3 |year= 1996 |pmid= 7492760 |doi= }}
*{{cite journal | author=Beaumont C, Leneuve P, Devaux I, ''et al.'' |title=Mutation in the iron responsive element of the L ferritin mRNA in a family with dominant hyperferritinaemia and cataract. |journal=Nat. Genet. |volume=11 |issue= 4 |pages= 444-6 |year= 1996 |pmid= 7493028 |doi= 10.1038/ng1295-444 }}
*{{cite journal | author=D'Agostino P, Faniello MC, Quaresima B, ''et al.'' |title=Negative and positive elements in the promoter region of the human apoferritin L gene. |journal=Biochem. Biophys. Res. Commun. |volume=215 |issue= 1 |pages= 329-37 |year= 1995 |pmid= 7575610 |doi= }}
*{{cite journal | author=Rogers JT, Andriotakis JL, Lacroix L, ''et al.'' |title=Translational enhancement of H-ferritin mRNA by interleukin-1 beta acts through 5' leader sequences distinct from the iron responsive element. |journal=Nucleic Acids Res. |volume=22 |issue= 13 |pages= 2678-86 |year= 1994 |pmid= 8041631 |doi= }}
*{{cite journal | author=Spanner M, Weber K, Lanske B, ''et al.'' |title=The iron-binding protein ferritin is expressed in cells of the osteoblastic lineage in vitro and in vivo. |journal=Bone |volume=17 |issue= 2 |pages= 161-5 |year= 1996 |pmid= 8554925 |doi= }}
*{{cite journal | author=Rogers JT |title=Ferritin translation by interleukin-1and interleukin-6: the role of sequences upstream of the start codons of the heavy and light subunit genes. |journal=Blood |volume=87 |issue= 6 |pages= 2525-37 |year= 1996 |pmid= 8630420 |doi= }}
*{{cite journal | author=Pang JH, Jiang MJ, Chen YL, ''et al.'' |title=Increased ferritin gene expression in atherosclerotic lesions. |journal=J. Clin. Invest. |volume=97 |issue= 10 |pages= 2204-12 |year= 1996 |pmid= 8636399 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HSD11B2... {November 15, 2007 6:56:26 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:56:53 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Hydroxysteroid (11-beta) dehydrogenase 2
| HGNCid = 5209
| Symbol = HSD11B2
| AltSymbols =; AME; AME1; HSD11K; HSD2
| OMIM = 218030
| ECnumber =
| Homologene = 20088
| MGIid = 104720
| GeneAtlas_image1 = PBB_GE_HSD11B2_204130_at_tn.png
| Function = {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}}
| Process = {{GNF_GO|id=GO:0006704 |text = glucocorticoid biosynthetic process}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3291
| Hs_Ensembl = ENSG00000176387
| Hs_RefseqProtein = NP_000187
| Hs_RefseqmRNA = NM_000196
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 66022518
| Hs_GenLoc_end = 66028953
| Hs_Uniprot = P80365
| Mm_EntrezGene = 15484
| Mm_Ensembl = ENSMUSG00000031891
| Mm_RefseqmRNA = NM_008289
| Mm_RefseqProtein = NP_032315
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 108407884
| Mm_GenLoc_end = 108413115
| Mm_Uniprot = Q3U2R0
}}
}}
'''Hydroxysteroid (11-beta) dehydrogenase 2''', also known as '''HSD11B2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HSD11B2 hydroxysteroid (11-beta) dehydrogenase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3291| 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=White PC, Mune T, Agarwal AK |title=11 beta-Hydroxysteroid dehydrogenase and the syndrome of apparent mineralocorticoid excess. |journal=Endocr. Rev. |volume=18 |issue= 1 |pages= 135-56 |year= 1997 |pmid= 9034789 |doi= }}
*{{cite journal | author=Wilson RC, Dave-Sharma S, Wei JQ, ''et al.'' |title=A genetic defect resulting in mild low-renin hypertension. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 17 |pages= 10200-5 |year= 1998 |pmid= 9707624 |doi= }}
*{{cite journal | author=Quinkler M, Stewart PM |title=Hypertension and the cortisol-cortisone shuttle. |journal=J. Clin. Endocrinol. Metab. |volume=88 |issue= 6 |pages= 2384-92 |year= 2003 |pmid= 12788832 |doi= }}
*{{cite journal | author=Tomlinson JW, Walker EA, Bujalska IJ, ''et al.'' |title=11beta-hydroxysteroid dehydrogenase type 1: a tissue-specific regulator of glucocorticoid response. |journal=Endocr. Rev. |volume=25 |issue= 5 |pages= 831-66 |year= 2005 |pmid= 15466942 |doi= 10.1210/er.2003-0031 }}
*{{cite journal | author=Persu A |title=11beta-Hydroxysteroid deshydrogenase: a multi-faceted enzyme. |journal=J. Hypertens. |volume=23 |issue= 1 |pages= 29-31 |year= 2005 |pmid= 15643119 |doi= }}
*{{cite journal | author=Funder JW, Pearce PT, Smith R, Smith AI |title=Mineralocorticoid action: target tissue specificity is enzyme, not receptor, mediated. |journal=Science |volume=242 |issue= 4878 |pages= 583-5 |year= 1988 |pmid= 2845584 |doi= }}
*{{cite journal | author=Stewart PM, Wallace AM, Valentino R, ''et al.'' |title=Mineralocorticoid activity of liquorice: 11-beta-hydroxysteroid dehydrogenase deficiency comes of age. |journal=Lancet |volume=2 |issue= 8563 |pages= 821-4 |year= 1987 |pmid= 2889032 |doi= }}
*{{cite journal | author=Wilson RC, Harbison MD, Krozowski ZS, ''et al.'' |title=Several homozygous mutations in the gene for 11 beta-hydroxysteroid dehydrogenase type 2 in patients with apparent mineralocorticoid excess. |journal=J. Clin. Endocrinol. Metab. |volume=80 |issue= 11 |pages= 3145-50 |year= 1995 |pmid= 7593417 |doi= }}
*{{cite journal | author=Wilson RC, Krozowski ZS, Li K, ''et al.'' |title=A mutation in the HSD11B2 gene in a family with apparent mineralocorticoid excess. |journal=J. Clin. Endocrinol. Metab. |volume=80 |issue= 7 |pages= 2263-6 |year= 1995 |pmid= 7608290 |doi= }}
*{{cite journal | author=Krozowski Z, Baker E, Obeyesekere V, Callen DF |title=Localization of the gene for human 11 beta-hydroxysteroid dehydrogenase type 2 (HSD11B2) to chromosome band 16q22. |journal=Cytogenet. Cell Genet. |volume=71 |issue= 2 |pages= 124-5 |year= 1995 |pmid= 7656579 |doi= }}
*{{cite journal | author=Mune T, Rogerson FM, Nikkilä H, ''et al.'' |title=Human hypertension caused by mutations in the kidney isozyme of 11 beta-hydroxysteroid dehydrogenase. |journal=Nat. Genet. |volume=10 |issue= 4 |pages= 394-9 |year= 1995 |pmid= 7670488 |doi= 10.1038/ng0895-394 }}
*{{cite journal | author=Albiston AL, Obeyesekere VR, Smith RE, Krozowski ZS |title=Cloning and tissue distribution of the human 11 beta-hydroxysteroid dehydrogenase type 2 enzyme. |journal=Mol. Cell. Endocrinol. |volume=105 |issue= 2 |pages= R11-7 |year= 1995 |pmid= 7859916 |doi= }}
*{{cite journal | author=Agarwal AK, Rogerson FM, Mune T, White PC |title=Gene structure and chromosomal localization of the human HSD11K gene encoding the kidney (type 2) isozyme of 11 beta-hydroxysteroid dehydrogenase. |journal=Genomics |volume=29 |issue= 1 |pages= 195-9 |year= 1996 |pmid= 8530071 |doi= 10.1006/geno.1995.1231 }}
*{{cite journal | author=Krozowski Z, Albiston AL, Obeyesekere VR, ''et al.'' |title=The human 11 beta-hydroxysteroid dehydrogenase type II enzyme: comparisons with other species and localization to the distal nephron. |journal=J. Steroid Biochem. Mol. Biol. |volume=55 |issue= 5-6 |pages= 457-64 |year= 1996 |pmid= 8547170 |doi= }}
*{{cite journal | author=Brown RW, Chapman KE, Kotelevtsev Y, ''et al.'' |title=Cloning and production of antisera to human placental 11 beta-hydroxysteroid dehydrogenase type 2. |journal=Biochem. J. |volume=313 ( Pt 3) |issue= |pages= 1007-17 |year= 1996 |pmid= 8611140 |doi= }}
*{{cite journal | author=Brown RW, Chapman KE, Murad P, ''et al.'' |title=Purification of 11 beta-hydroxysteroid dehydrogenase type 2 from human placenta utilizing a novel affinity labelling technique. |journal=Biochem. J. |volume=313 ( Pt 3) |issue= |pages= 997-1005 |year= 1996 |pmid= 8611186 |doi= }}
*{{cite journal | author=Kitanaka S, Katsumata N, Tanae A, ''et al.'' |title=A new compound heterozygous mutation in the 11 beta-hydroxysteroid dehydrogenase type 2 gene in a case of apparent mineralocorticoid excess. |journal=J. Clin. Endocrinol. Metab. |volume=82 |issue= 12 |pages= 4054-8 |year= 1998 |pmid= 9398712 |doi= }}
*{{cite journal | author=Dave-Sharma S, Wilson RC, Harbison MD, ''et al.'' |title=Examination of genotype and phenotype relationships in 14 patients with apparent mineralocorticoid excess. |journal=J. Clin. Endocrinol. Metab. |volume=83 |issue= 7 |pages= 2244-54 |year= 1998 |pmid= 9661590 |doi= }}
*{{cite journal | author=Li A, Tedde R, Krozowski ZS, ''et al.'' |title=Molecular basis for hypertension in the "type II variant" of apparent mineralocorticoid excess. |journal=Am. J. Hum. Genet. |volume=63 |issue= 2 |pages= 370-9 |year= 1998 |pmid= 9683587 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LCP2... {November 15, 2007 6:56:53 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:57:21 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Lymphocyte cytosolic protein 2 (SH2 domain containing leukocyte protein of 76kDa)
| HGNCid = 6529
| Symbol = LCP2
| AltSymbols =; SLP-76; SLP76
| OMIM = 601603
| ECnumber =
| Homologene = 4065
| MGIid = 1321402
| GeneAtlas_image1 = PBB_GE_LCP2_205269_at_tn.png
| GeneAtlas_image2 = PBB_GE_LCP2_205270_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component =
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0045576 |text = mast cell activation}} {{GNF_GO|id=GO:0050663 |text = cytokine secretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3937
| Hs_Ensembl = ENSG00000043462
| Hs_RefseqProtein = NP_005556
| Hs_RefseqmRNA = NM_005565
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 169607667
| Hs_GenLoc_end = 169657400
| Hs_Uniprot = Q13094
| Mm_EntrezGene = 16822
| Mm_Ensembl = ENSMUSG00000002699
| Mm_RefseqmRNA = NM_010696
| Mm_RefseqProtein = NP_034826
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 33947144
| Mm_GenLoc_end = 33992281
| Mm_Uniprot = Q3U5Y3
}}
}}
'''Lymphocyte cytosolic protein 2 (SH2 domain containing leukocyte protein of 76kDa)''', also known as '''LCP2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LCP2 lymphocyte cytosolic protein 2 (SH2 domain containing leukocyte protein of 76kDa)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3937| 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 = SLP-76 was originally identified as a substrate of the ZAP-70 protein tyrosine kinase following T cell receptor (TCR) ligation in the leukemic T cell line Jurkat. The SLP-76 locus has been localized to human chromosome 5q33 and the gene structure has been partially characterized in mice. The human and murine cDNAs both encode 533 amino acid proteins that are 72% identical and comprised of three modular domains. The NH2-terminus contains an acidic region that includes a PEST domain and several tyrosine residues which are phosphorylated following TCR ligation. SLP-76 also contains a central proline-rich domain and a COOH-terminal SH2 domain. A number of additional proteins have been identified that associate with SLP-76 both constitutively and inducibly following receptor ligation, supporting the notion that SLP-76 functions as an adaptor or scaffold protein. Studies using SLP-76 deficient T cell lines or mice have provided strong evidence that SLP-76 plays a positive role in promoting T cell development and activation as well as mast cell and platelet function.<ref name="entrez">{{cite web | title = Entrez Gene: LCP2 lymphocyte cytosolic protein 2 (SH2 domain containing leukocyte protein of 76kDa)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3937| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Jackman JK, Motto DG, Sun Q, ''et al.'' |title=Molecular cloning of SLP-76, a 76-kDa tyrosine phosphoprotein associated with Grb2 in T cells. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7029-32 |year= 1995 |pmid= 7706237 |doi= }}
*{{cite journal | author=Sunden SL, Carr LL, Clements JL, ''et al.'' |title=Polymorphism in and localization of the gene LCP2 (SLP-76) to chromosome 5q33.1-qter. |journal=Genomics |volume=35 |issue= 1 |pages= 269-70 |year= 1996 |pmid= 8661136 |doi= 10.1006/geno.1996.0354 }}
*{{cite journal | author=Motto DG, Ross SE, Wu J, ''et al.'' |title=Implication of the GRB2-associated phosphoprotein SLP-76 in T cell receptor-mediated interleukin 2 production. |journal=J. Exp. Med. |volume=183 |issue= 4 |pages= 1937-43 |year= 1996 |pmid= 8666952 |doi= }}
*{{cite journal | author=Wardenburg JB, Fu C, Jackman JK, ''et al.'' |title=Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function. |journal=J. Biol. Chem. |volume=271 |issue= 33 |pages= 19641-4 |year= 1996 |pmid= 8702662 |doi= }}
*{{cite journal | author=Onodera H, Motto DG, Koretzky GA, Rothstein DM |title=Differential regulation of activation-induced tyrosine phosphorylation and recruitment of SLP-76 to Vav by distinct isoforms of the CD45 protein-tyrosine phosphatase. |journal=J. Biol. Chem. |volume=271 |issue= 36 |pages= 22225-30 |year= 1996 |pmid= 8703037 |doi= }}
*{{cite journal | author=Mizuno K, Katagiri T, Hasegawa K, ''et al.'' |title=Hematopoietic cell phosphatase, SHP-1, is constitutively associated with the SH2 domain-containing leukocyte protein, SLP-76, in B cells. |journal=J. Exp. Med. |volume=184 |issue= 2 |pages= 457-63 |year= 1996 |pmid= 8760799 |doi= }}
*{{cite journal | author=Raab M, da Silva AJ, Findell PR, Rudd CE |title=Regulation of Vav-SLP-76 binding by ZAP-70 and its relevance to TCR zeta/CD3 induction of interleukin-2. |journal=Immunity |volume=6 |issue= 2 |pages= 155-64 |year= 1997 |pmid= 9047237 |doi= }}
*{{cite journal | author=Musci MA, Hendricks-Taylor LR, Motto DG, ''et al.'' |title=Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T cell antigen receptor-stimulated protein tyrosine kinases. |journal=J. Biol. Chem. |volume=272 |issue= 18 |pages= 11674-7 |year= 1997 |pmid= 9115214 |doi= }}
*{{cite journal | author=da Silva AJ, Li Z, de Vera C, ''et al.'' |title=Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-containing leukocyte protein 76 and modulates interleukin 2 production. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 14 |pages= 7493-8 |year= 1997 |pmid= 9207119 |doi= }}
*{{cite journal | author=Fu C, Chan AC |title=Identification of two tyrosine phosphoproteins, pp70 and pp68, which interact with phospholipase Cgamma, Grb2, and Vav after B cell antigen receptor activation. |journal=J. Biol. Chem. |volume=272 |issue= 43 |pages= 27362-8 |year= 1997 |pmid= 9341187 |doi= }}
*{{cite journal | author=Zhang W, Sloan-Lancaster J, Kitchen J, ''et al.'' |title=LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. |journal=Cell |volume=92 |issue= 1 |pages= 83-92 |year= 1998 |pmid= 9489702 |doi= }}
*{{cite journal | author=Fu C, Turck CW, Kurosaki T, Chan AC |title=BLNK: a central linker protein in B cell activation. |journal=Immunity |volume=9 |issue= 1 |pages= 93-103 |year= 1998 |pmid= 9697839 |doi= }}
*{{cite journal | author=Chu J, Liu Y, Koretzky GA, Durden DL |title=SLP-76-Cbl-Grb2-Shc interactions in FcgammaRI signaling. |journal=Blood |volume=92 |issue= 5 |pages= 1697-706 |year= 1998 |pmid= 9716598 |doi= }}
*{{cite journal | author=Binstadt BA, Billadeau DD, Jevremović D, ''et al.'' |title=SLP-76 is a direct substrate of SHP-1 recruited to killer cell inhibitory receptors. |journal=J. Biol. Chem. |volume=273 |issue= 42 |pages= 27518-23 |year= 1998 |pmid= 9765283 |doi= }}
*{{cite journal | author=Liu SK, Fang N, Koretzky GA, McGlade CJ |title=The hematopoietic-specific adaptor protein gads functions in T-cell signaling via interactions with the SLP-76 and LAT adaptors. |journal=Curr. Biol. |volume=9 |issue= 2 |pages= 67-75 |year= 1999 |pmid= 10021361 |doi= }}
*{{cite journal | author=Gross BS, Lee JR, Clements JL, ''et al.'' |title=Tyrosine phosphorylation of SLP-76 is downstream of Syk following stimulation of the collagen receptor in platelets. |journal=J. Biol. Chem. |volume=274 |issue= 9 |pages= 5963-71 |year= 1999 |pmid= 10026222 |doi= }}
*{{cite journal | author=Erdreich-Epstein A, Liu M, Kant AM, ''et al.'' |title=Cbl functions downstream of Src kinases in Fc gamma RI signaling in primary human macrophages. |journal=J. Leukoc. Biol. |volume=65 |issue= 4 |pages= 523-34 |year= 1999 |pmid= 10204582 |doi= }}
*{{cite journal | author=Asada H, Ishii N, Sasaki Y, ''et al.'' |title=Grf40, A novel Grb2 family member, is involved in T cell signaling through interaction with SLP-76 and LAT. |journal=J. Exp. Med. |volume=189 |issue= 9 |pages= 1383-90 |year= 1999 |pmid= 10224278 |doi= }}
*{{cite journal | author=Wunderlich L, Faragó A, Downward J, Buday L |title=Association of Nck with tyrosine-phosphorylated SLP-76 in activated T lymphocytes. |journal=Eur. J. Immunol. |volume=29 |issue= 4 |pages= 1068-75 |year= 1999 |pmid= 10229072 |doi= }}
*{{cite journal | author=Gross BS, Melford SK, Watson SP |title=Evidence that phospholipase C-gamma2 interacts with SLP-76, Syk, Lyn, LAT and the Fc receptor gamma-chain after stimulation of the collagen receptor glycoprotein VI in human platelets. |journal=Eur. J. Biochem. |volume=263 |issue= 3 |pages= 612-23 |year= 1999 |pmid= 10469124 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LEF1... {November 15, 2007 7:03:28 PM PST}
- SEARCH REDIRECT: Control Box Found: LEF1 {November 15, 2007 7:03:57 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 7:03:58 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 7:03:58 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 7:03:58 PM PST}
- UPDATED: Updated protein page: LEF1 {November 15, 2007 7:04:04 PM PST}
- INFO: Beginning work on NFATC1... {November 15, 2007 6:57:45 PM PST}
- SEARCH REDIRECT: Control Box Found: NFATC1 {November 15, 2007 6:58:09 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 6:58:10 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 6:58:10 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 6:58:10 PM PST}
- UPDATED: Updated protein page: NFATC1 {November 15, 2007 6:58:16 PM PST}
- INFO: Beginning work on NRAS... {November 15, 2007 6:58:16 PM PST}
- SEARCH REDIRECT: Control Box Found: NRAS {November 15, 2007 6:58:35 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 6:58:36 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 6:58:36 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 6:58:36 PM PST}
- UPDATED: Updated protein page: NRAS {November 15, 2007 6:58:43 PM PST}
- INFO: Beginning work on NRP1... {November 15, 2007 7:02:07 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:02:51 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_NRP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1kex.
| PDB = {{PDB2|1kex}}, {{PDB2|2orx}}, {{PDB2|2orz}}
| Name = Neuropilin 1
| HGNCid = 8004
| Symbol = NRP1
| AltSymbols =; NRP; CD304; DKFZp686A03134; DKFZp781F1414; VEGF165R
| OMIM = 602069
| ECnumber =
| Homologene = 2876
| MGIid = 106206
| GeneAtlas_image1 = PBB_GE_NRP1_212298_at_tn.png
| GeneAtlas_image2 = PBB_GE_NRP1_210510_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_NRP1_210615_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005021 |text = vascular endothelial growth factor receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0017154 |text = semaphorin receptor activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0007411 |text = axon guidance}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0016358 |text = dendrite development}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0030517 |text = negative regulation of axon extension}} {{GNF_GO|id=GO:0048010 |text = vascular endothelial growth factor receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8829
| Hs_Ensembl = ENSG00000099250
| Hs_RefseqProtein = NP_001019799
| Hs_RefseqmRNA = NM_001024628
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 33506426
| Hs_GenLoc_end = 33665196
| Hs_Uniprot = O14786
| Mm_EntrezGene = 18186
| Mm_Ensembl = ENSMUSG00000025810
| Mm_RefseqmRNA = NM_008737
| Mm_RefseqProtein = NP_032763
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 131245328
| Mm_GenLoc_end = 131389437
| Mm_Uniprot = Q3UFP7
}}
}}
'''Neuropilin 1''', also known as '''NRP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NRP1 neuropilin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8829| 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 = NRP1 is a membrane-bound coreceptor to a tyrosine kinase receptor for both vascular endothelial growth factor (VEGF; MIM 192240) and semaphorin (see SEMA3A; MIM 603961) family members. NRP1 plays versatile roles in angiogenesis, axon guidance, cell survival, migration, and invasion.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: NRP1 neuropilin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8829| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Zachary I, Gliki G |title=Signaling transduction mechanisms mediating biological actions of the vascular endothelial growth factor family. |journal=Cardiovasc. Res. |volume=49 |issue= 3 |pages= 568-81 |year= 2001 |pmid= 11166270 |doi= }}
*{{cite journal | author=He Z, Tessier-Lavigne M |title=Neuropilin is a receptor for the axonal chemorepellent Semaphorin III. |journal=Cell |volume=90 |issue= 4 |pages= 739-51 |year= 1997 |pmid= 9288753 |doi= }}
*{{cite journal | author=Chen H, Chédotal A, He Z, ''et al.'' |title=Neuropilin-2, a novel member of the neuropilin family, is a high affinity receptor for the semaphorins Sema E and Sema IV but not Sema III. |journal=Neuron |volume=19 |issue= 3 |pages= 547-59 |year= 1997 |pmid= 9331348 |doi= }}
*{{cite journal | author=Soker S, Takashima S, Miao HQ, ''et al.'' |title=Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor. |journal=Cell |volume=92 |issue= 6 |pages= 735-45 |year= 1998 |pmid= 9529250 |doi= }}
*{{cite journal | author=Giger RJ, Urquhart ER, Gillespie SK, ''et al.'' |title=Neuropilin-2 is a receptor for semaphorin IV: insight into the structural basis of receptor function and specificity. |journal=Neuron |volume=21 |issue= 5 |pages= 1079-92 |year= 1999 |pmid= 9856463 |doi= }}
*{{cite journal | author=Chen H, He Z, Bagri A, Tessier-Lavigne M |title=Semaphorin-neuropilin interactions underlying sympathetic axon responses to class III semaphorins. |journal=Neuron |volume=21 |issue= 6 |pages= 1283-90 |year= 1999 |pmid= 9883722 |doi= }}
*{{cite journal | author=Takahashi T, Nakamura F, Jin Z, ''et al.'' |title=Semaphorins A and E act as antagonists of neuropilin-1 and agonists of neuropilin-2 receptors. |journal=Nat. Neurosci. |volume=1 |issue= 6 |pages= 487-93 |year= 1999 |pmid= 10196546 |doi= 10.1038/2203 }}
*{{cite journal | author=Rossignol M, Beggs AH, Pierce EA, Klagsbrun M |title=Human neuropilin-1 and neuropilin-2 map to 10p12 and 2q34, respectively. |journal=Genomics |volume=57 |issue= 3 |pages= 459-60 |year= 1999 |pmid= 10329017 |doi= 10.1006/geno.1999.5790 }}
*{{cite journal | author=Makinen T, Olofsson B, Karpanen T, ''et al.'' |title=Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1. |journal=J. Biol. Chem. |volume=274 |issue= 30 |pages= 21217-22 |year= 1999 |pmid= 10409677 |doi= }}
*{{cite journal | author=Cai H, Reed RR |title=Cloning and characterization of neuropilin-1-interacting protein: a PSD-95/Dlg/ZO-1 domain-containing protein that interacts with the cytoplasmic domain of neuropilin-1. |journal=J. Neurosci. |volume=19 |issue= 15 |pages= 6519-27 |year= 1999 |pmid= 10414980 |doi= }}
*{{cite journal | author=Takahashi T, Fournier A, Nakamura F, ''et al.'' |title=Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors. |journal=Cell |volume=99 |issue= 1 |pages= 59-69 |year= 1999 |pmid= 10520994 |doi= }}
*{{cite journal | author=Tamagnone L, Artigiani S, Chen H, ''et al.'' |title=Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates. |journal=Cell |volume=99 |issue= 1 |pages= 71-80 |year= 1999 |pmid= 10520995 |doi= }}
*{{cite journal | author=Gagnon ML, Bielenberg DR, Gechtman Z, ''et al.'' |title=Identification of a natural soluble neuropilin-1 that binds vascular endothelial growth factor: In vivo expression and antitumor activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 6 |pages= 2573-8 |year= 2000 |pmid= 10688880 |doi= 10.1073/pnas.040337597 }}
*{{cite journal | author=Gluzman-Poltorak Z, Cohen T, Herzog Y, Neufeld G |title=Neuropilin-2 is a receptor for the vascular endothelial growth factor (VEGF) forms VEGF-145 and VEGF-165 [corrected]. |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18040-5 |year= 2000 |pmid= 10748121 |doi= 10.1074/jbc.M909259199 }}
*{{cite journal | author=Fuh G, Garcia KC, de Vos AM |title=The interaction of neuropilin-1 with vascular endothelial growth factor and its receptor flt-1. |journal=J. Biol. Chem. |volume=275 |issue= 35 |pages= 26690-5 |year= 2000 |pmid= 10842181 |doi= 10.1074/jbc.M003955200 }}
*{{cite journal | author=Rossignol M, Gagnon ML, Klagsbrun M |title=Genomic organization of human neuropilin-1 and neuropilin-2 genes: identification and distribution of splice variants and soluble isoforms. |journal=Genomics |volume=70 |issue= 2 |pages= 211-22 |year= 2001 |pmid= 11112349 |doi= 10.1006/geno.2000.6381 }}
*{{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=Whitaker GB, Limberg BJ, Rosenbaum JS |title=Vascular endothelial growth factor receptor-2 and neuropilin-1 form a receptor complex that is responsible for the differential signaling potency of VEGF(165) and VEGF(121). |journal=J. Biol. Chem. |volume=276 |issue= 27 |pages= 25520-31 |year= 2001 |pmid= 11333271 |doi= 10.1074/jbc.M102315200 }}
*{{cite journal | author=Walter JW, North PE, Waner M, ''et al.'' |title=Somatic mutation of vascular endothelial growth factor receptors in juvenile hemangioma. |journal=Genes Chromosomes Cancer |volume=33 |issue= 3 |pages= 295-303 |year= 2002 |pmid= 11807987 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PTPN22... {November 15, 2007 7:02:51 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:03:28 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PTPN22_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2p6x.
| PDB = {{PDB2|2p6x}}
| Name = Protein tyrosine phosphatase, non-receptor type 22 (lymphoid)
| HGNCid = 9652
| Symbol = PTPN22
| AltSymbols =; LYP; PEP; Lyp1; Lyp2; PTPN8
| OMIM = 600716
| ECnumber =
| Homologene = 7498
| MGIid = 107170
| GeneAtlas_image1 = PBB_GE_PTPN22_206060_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PTPN22_208010_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PTPN22_208011_at_tn.png
| Function = {{GNF_GO|id=GO:0004725 |text = protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0030217 |text = T cell differentiation}} {{GNF_GO|id=GO:0050852 |text = T cell receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 26191
| Hs_Ensembl = ENSG00000134242
| Hs_RefseqProtein = NP_036543
| Hs_RefseqmRNA = NM_012411
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 114092981
| Hs_GenLoc_end = 114215904
| Hs_Uniprot = Q9Y2R2
| Mm_EntrezGene = 19260
| Mm_Ensembl = ENSMUSG00000027843
| Mm_RefseqmRNA = NM_008979
| Mm_RefseqProtein = NP_033005
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 103989353
| Mm_GenLoc_end = 104041308
| Mm_Uniprot = Q3TEL9
}}
}}
'''Protein tyrosine phosphatase, non-receptor type 22 (lymphoid)''', also known as '''PTPN22''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTPN22 protein tyrosine phosphatase, non-receptor type 22 (lymphoid)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26191| 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 a protein tyrosine phosphatase which is expressed primarily in lymphoid tissues. This enzyme associates with the molecular adapter protein CBL and may be involved in regulating CBL function in the T-cell receptor signaling pathway. Alternative splicing of this gene results in two transcript variants encoding distinct isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: PTPN22 protein tyrosine phosphatase, non-receptor type 22 (lymphoid)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26191| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Gregersen PK |title=Pathways to gene identification in rheumatoid arthritis: PTPN22 and beyond. |journal=Immunol. Rev. |volume=204 |issue= |pages= 74-86 |year= 2005 |pmid= 15790351 |doi= 10.1111/j.0105-2896.2005.00243.x }}
*{{cite journal | author=Brand O, Gough S, Heward J |title=HLA , CTLA-4 and PTPN22 : the shared genetic master-key to autoimmunity? |journal=Expert reviews in molecular medicine |volume=7 |issue= 23 |pages= 1-15 |year= 2007 |pmid= 16229750 |doi= 10.1017/S1462399405009981 }}
*{{cite journal | author=Bottini N, Vang T, Cucca F, Mustelin T |title=Role of PTPN22 in type 1 diabetes and other autoimmune diseases. |journal=Semin. Immunol. |volume=18 |issue= 4 |pages= 207-13 |year= 2007 |pmid= 16697661 |doi= 10.1016/j.smim.2006.03.008 }}
*{{cite journal | author=Matthews RJ, Bowne DB, Flores E, Thomas ML |title=Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences. |journal=Mol. Cell. Biol. |volume=12 |issue= 5 |pages= 2396-405 |year= 1992 |pmid= 1373816 |doi= }}
*{{cite journal | author=Gregorieff A, Cloutier JF, Veillette A |title=Sequence requirements for association of protein-tyrosine phosphatase PEP with the Src homology 3 domain of inhibitory tyrosine protein kinase p50(csk). |journal=J. Biol. Chem. |volume=273 |issue= 21 |pages= 13217-22 |year= 1998 |pmid= 9582365 |doi= }}
*{{cite journal | author=Cohen S, Dadi H, Shaoul E, ''et al.'' |title=Cloning and characterization of a lymphoid-specific, inducible human protein tyrosine phosphatase, Lyp. |journal=Blood |volume=93 |issue= 6 |pages= 2013-24 |year= 1999 |pmid= 10068674 |doi= }}
*{{cite journal | author=Gjörloff-Wingren A, Saxena M, Han S, ''et al.'' |title=Subcellular localization of intracellular protein tyrosine phosphatases in T cells. |journal=Eur. J. Immunol. |volume=30 |issue= 8 |pages= 2412-21 |year= 2000 |pmid= 10940933 |doi= }}
*{{cite journal | author=Hill RJ, Zozulya S, Lu YL, ''et al.'' |title=The lymphoid protein tyrosine phosphatase Lyp interacts with the adaptor molecule Grb2 and functions as a negative regulator of T-cell activation. |journal=Exp. Hematol. |volume=30 |issue= 3 |pages= 237-44 |year= 2002 |pmid= 11882361 |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=Chien W, Tidow N, Williamson EA, ''et al.'' |title=Characterization of a myeloid tyrosine phosphatase, Lyp, and its role in the Bcr-Abl signal transduction pathway. |journal=J. Biol. Chem. |volume=278 |issue= 30 |pages= 27413-20 |year= 2003 |pmid= 12764153 |doi= 10.1074/jbc.M304575200 }}
*{{cite journal | author=Bottini N, Musumeci L, Alonso A, ''et al.'' |title=A functional variant of lymphoid tyrosine phosphatase is associated with type I diabetes. |journal=Nat. Genet. |volume=36 |issue= 4 |pages= 337-8 |year= 2004 |pmid= 15004560 |doi= 10.1038/ng1323 }}
*{{cite journal | author=Begovich AB, Carlton VE, Honigberg LA, ''et al.'' |title=A missense single-nucleotide polymorphism in a gene encoding a protein tyrosine phosphatase (PTPN22) is associated with rheumatoid arthritis. |journal=Am. J. Hum. Genet. |volume=75 |issue= 2 |pages= 330-7 |year= 2004 |pmid= 15208781 |doi= 10.1086/422827 }}
*{{cite journal | author=Kyogoku C, Langefeld CD, Ortmann WA, ''et al.'' |title=Genetic association of the R620W polymorphism of protein tyrosine phosphatase PTPN22 with human SLE. |journal=Am. J. Hum. Genet. |volume=75 |issue= 3 |pages= 504-7 |year= 2004 |pmid= 15273934 |doi= 10.1086/423790 }}
*{{cite journal | author=Smyth D, Cooper JD, Collins JE, ''et al.'' |title=Replication of an association between the lymphoid tyrosine phosphatase locus (LYP/PTPN22) with type 1 diabetes, and evidence for its role as a general autoimmunity locus. |journal=Diabetes |volume=53 |issue= 11 |pages= 3020-3 |year= 2005 |pmid= 15504986 |doi= }}
*{{cite journal | author=Ladner MB, Bottini N, Valdes AM, Noble JA |title=Association of the single nucleotide polymorphism C1858T of the PTPN22 gene with type 1 diabetes. |journal=Hum. Immunol. |volume=66 |issue= 1 |pages= 60-4 |year= 2005 |pmid= 15620463 |doi= 10.1016/j.humimm.2004.09.016 }}
*{{cite journal | author=Orozco G, Sánchez E, González-Gay MA, ''et al.'' |title=Association of a functional single-nucleotide polymorphism of PTPN22, encoding lymphoid protein phosphatase, with rheumatoid arthritis and systemic lupus erythematosus. |journal=Arthritis Rheum. |volume=52 |issue= 1 |pages= 219-24 |year= 2005 |pmid= 15641066 |doi= 10.1002/art.20771 }}
*{{cite journal | author=Steer S, Lad B, Grumley JA, ''et al.'' |title=Association of R602W in a protein tyrosine phosphatase gene with a high risk of rheumatoid arthritis in a British population: evidence for an early onset/disease severity effect. |journal=Arthritis Rheum. |volume=52 |issue= 1 |pages= 358-60 |year= 2005 |pmid= 15641088 |doi= 10.1002/art.20737 }}
*{{cite journal | author=Zheng W, She JX |title=Genetic association between a lymphoid tyrosine phosphatase (PTPN22) and type 1 diabetes. |journal=Diabetes |volume=54 |issue= 3 |pages= 906-8 |year= 2005 |pmid= 15734872 |doi= }}
*{{cite journal | author=Zhernakova A, Eerligh P, Wijmenga C, ''et al.'' |title=Differential association of the PTPN22 coding variant with autoimmune diseases in a Dutch population. |journal=Genes Immun. |volume=6 |issue= 6 |pages= 459-61 |year= 2005 |pmid= 15875058 |doi= 10.1038/sj.gene.6364220 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RAP1A... {November 15, 2007 6:58:43 PM PST}
- SEARCH: Multiple Conflicting Pages. Need Resolution. {November 15, 2007 6:59:12 PM PST}
- AMBIGUITY: More than one potential page found for updating, RAP1A RAP1A {November 15, 2007 6:59:12 PM PST}
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| 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_RAP1A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1c1y.
| PDB = {{PDB2|1c1y}}, {{PDB2|1gua}}
| Name = RAP1A, member of RAS oncogene family
| HGNCid = 9855
| Symbol = RAP1A
| AltSymbols =; KREV-1; KREV1; RAP1; SMGP21
| OMIM = 179520
| ECnumber =
| Homologene = 2162
| MGIid = 97852
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5906
| Hs_Ensembl = ENSG00000116473
| Hs_RefseqProtein = NP_001010935
| Hs_RefseqmRNA = NM_001010935
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 111886363
| Hs_GenLoc_end = 112060836
| Hs_Uniprot = P62834
| Mm_EntrezGene = 109905
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_145541
| Mm_RefseqProtein = NP_663516
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''RAP1A, member of RAS oncogene family''', also known as '''RAP1A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RAP1A RAP1A, member of RAS oncogene family| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5906| 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 product of this gene belongs to the family of RAS-related proteins. These proteins share approximately 50% amino acid identity with the classical RAS proteins and have numerous structural features in common. The most striking difference between RAP proteins and RAS proteins resides in their 61st amino acid: glutamine in RAS is replaced by threonine in RAP proteins. The product of this gene counteracts the mitogenic function of RAS because it can interact with RAS GAPs and RAF in a competitive manner. Two transcript variants encoding the same protein have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: RAP1A RAP1A, member of RAS oncogene family| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5906| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Quinn MT, Mullen ML, Jesaitis AJ, Linner JG |title=Subcellular distribution of the Rap1A protein in human neutrophils: colocalization and cotranslocation with cytochrome b559. |journal=Blood |volume=79 |issue= 6 |pages= 1563-73 |year= 1992 |pmid= 1312373 |doi= }}
*{{cite journal | author=Buss JE, Quilliam LA, Kato K, ''et al.'' |title=The COOH-terminal domain of the Rap1A (Krev-1) protein is isoprenylated and supports transformation by an H-Ras:Rap1A chimeric protein. |journal=Mol. Cell. Biol. |volume=11 |issue= 3 |pages= 1523-30 |year= 1991 |pmid= 1899909 |doi= }}
*{{cite journal | author=Rousseau-Merck MF, Pizon V, Tavitian A, Berger R |title=Chromosome mapping of the human RAS-related RAP1A, RAP1B, and RAP2 genes to chromosomes 1p12----p13, 12q14, and 13q34, respectively. |journal=Cytogenet. Cell Genet. |volume=53 |issue= 1 |pages= 2-4 |year= 1990 |pmid= 2108841 |doi= }}
*{{cite journal | author=Hata Y, Kikuchi A, Sasaki T, ''et al.'' |title=Inhibition of the ras p21 GTPase-activating protein-stimulated GTPase activity of c-Ha-ras p21 by smg p21 having the same putative effector domain as ras p21s. |journal=J. Biol. Chem. |volume=265 |issue= 13 |pages= 7104-7 |year= 1990 |pmid= 2158984 |doi= }}
*{{cite journal | author=Frech M, John J, Pizon V, ''et al.'' |title=Inhibition of GTPase activating protein stimulation of Ras-p21 GTPase by the Krev-1 gene product. |journal=Science |volume=249 |issue= 4965 |pages= 169-71 |year= 1990 |pmid= 2164710 |doi= }}
*{{cite journal | author=Nagata K, Itoh H, Katada T, ''et al.'' |title=Purification, identification, and characterization of two GTP-binding proteins with molecular weights of 25,000 and 21,000 in human platelet cytosol. One is the rap1/smg21/Krev-1 protein and the other is a novel GTP-binding protein. |journal=J. Biol. Chem. |volume=264 |issue= 29 |pages= 17000-5 |year= 1989 |pmid= 2507536 |doi= }}
*{{cite journal | author=Kitayama H, Sugimoto Y, Matsuzaki T, ''et al.'' |title=A ras-related gene with transformation suppressor activity. |journal=Cell |volume=56 |issue= 1 |pages= 77-84 |year= 1989 |pmid= 2642744 |doi= }}
*{{cite journal | author=Pizon V, Chardin P, Lerosey I, ''et al.'' |title=Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related to ras in the 'effector' region. |journal=Oncogene |volume=3 |issue= 2 |pages= 201-4 |year= 1988 |pmid= 3045729 |doi= }}
*{{cite journal | author=Bokoch GM, Parkos CA, Mumby SM |title=Purification and characterization of the 22,000-dalton GTP-binding protein substrate for ADP-ribosylation by botulinum toxin, G22K. |journal=J. Biol. Chem. |volume=263 |issue= 32 |pages= 16744-9 |year= 1988 |pmid= 3141412 |doi= }}
*{{cite journal | author=Kawata M, Matsui Y, Kondo J, ''et al.'' |title=A novel small molecular weight GTP-binding protein with the same putative effector domain as the ras proteins in bovine brain membranes. Purification, determination of primary structure, and characterization. |journal=J. Biol. Chem. |volume=263 |issue= 35 |pages= 18965-71 |year= 1989 |pmid= 3143720 |doi= }}
*{{cite journal | author=Ohmori T, Kikuchi A, Yamamoto K, ''et al.'' |title=Identification of a platelet Mr 22,000 GTP-binding protein as the novel smg-21 gene product having the same putative effector domain as the ras gene products. |journal=Biochem. Biophys. Res. Commun. |volume=157 |issue= 2 |pages= 670-6 |year= 1989 |pmid= 3144274 |doi= }}
*{{cite journal | author=Nassar N, Horn G, Herrmann C, ''et al.'' |title=The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. |journal=Nature |volume=375 |issue= 6532 |pages= 554-60 |year= 1995 |pmid= 7791872 |doi= 10.1038/375554a0 }}
*{{cite journal | author=Takai S, Nishino N, Kitayama H, ''et al.'' |title=Mapping of the KREV1 transformation suppressor gene and its pseudogene (KREV1P) to human chromosome 1p13.3 and 14q24.3, respectively, by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=63 |issue= 1 |pages= 59-61 |year= 1993 |pmid= 8449039 |doi= }}
*{{cite journal | author=Nassar N, Horn G, Herrmann C, ''et al.'' |title=Ras/Rap effector specificity determined by charge reversal. |journal=Nat. Struct. Biol. |volume=3 |issue= 8 |pages= 723-9 |year= 1996 |pmid= 8756332 |doi= }}
*{{cite journal | author=Serebriiskii I, Estojak J, Sonoda G, ''et al.'' |title=Association of Krev-1/rap1a with Krit1, a novel ankyrin repeat-containing protein encoded by a gene mapping to 7q21-22. |journal=Oncogene |volume=15 |issue= 9 |pages= 1043-9 |year= 1997 |pmid= 9285558 |doi= 10.1038/sj.onc.1201268 }}
*{{cite journal | author=Hu CD, Kariya K, Okada T, ''et al.'' |title=Effect of phosphorylation on activities of Rap1A to interact with Raf-1 and to suppress Ras-dependent Raf-1 activation. |journal=J. Biol. Chem. |volume=274 |issue= 1 |pages= 48-51 |year= 1999 |pmid= 9867809 |doi= }}
*{{cite journal | author=Pizon V, Méchali F, Baldacci G |title=RAP1A GTP/GDP cycles determine the intracellular location of the late endocytic compartments and contribute to myogenic differentiation. |journal=Exp. Cell Res. |volume=246 |issue= 1 |pages= 56-68 |year= 1999 |pmid= 9882515 |doi= 10.1006/excr.1998.4284 }}
*{{cite journal | author=Nancy V, Wolthuis RM, de Tand MF, ''et al.'' |title=Identification and characterization of potential effector molecules of the Ras-related GTPase Rap2. |journal=J. Biol. Chem. |volume=274 |issue= 13 |pages= 8737-45 |year= 1999 |pmid= 10085114 |doi= }}
*{{cite journal | author=Linnemann T, Geyer M, Jaitner BK, ''et al.'' |title=Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily. |journal=J. Biol. Chem. |volume=274 |issue= 19 |pages= 13556-62 |year= 1999 |pmid= 10224125 |doi= }}
*{{cite journal | author=Okada T, Hu CD, Jin TG, ''et al.'' |title=The strength of interaction at the Raf cysteine-rich domain is a critical determinant of response of Raf to Ras family small GTPases. |journal=Mol. Cell. Biol. |volume=19 |issue= 9 |pages= 6057-64 |year= 1999 |pmid= 10454553 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SFTPD... {November 15, 2007 6:59:12 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:59:37 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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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_SFTPD_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1b08.
| PDB = {{PDB2|1b08}}, {{PDB2|1m7l}}, {{PDB2|1pw9}}, {{PDB2|1pwb}}, {{PDB2|2ggu}}, {{PDB2|2ggx}}, {{PDB2|2orj}}, {{PDB2|2ork}}, {{PDB2|2os9}}
| Name = Surfactant, pulmonary-associated protein D
| HGNCid = 10803
| Symbol = SFTPD
| AltSymbols =; COLEC7; PSP-D; SFTP4; SP-D
| OMIM = 178635
| ECnumber =
| Homologene = 2272
| MGIid = 109515
| GeneAtlas_image1 = PBB_GE_SFTPD_214199_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}} {{GNF_GO|id=GO:0008367 |text = bacterial binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0030139 |text = endocytic vesicle}}
| Process = {{GNF_GO|id=GO:0001817 |text = regulation of cytokine production}} {{GNF_GO|id=GO:0006800 |text = oxygen and reactive oxygen species metabolic process}} {{GNF_GO|id=GO:0006817 |text = phosphate transport}} {{GNF_GO|id=GO:0006898 |text = receptor-mediated endocytosis}} {{GNF_GO|id=GO:0007585 |text = respiratory gaseous exchange}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}} {{GNF_GO|id=GO:0042130 |text = negative regulation of T cell proliferation}} {{GNF_GO|id=GO:0043129 |text = surfactant homeostasis}} {{GNF_GO|id=GO:0045085 |text = negative regulation of interleukin-2 biosynthetic process}} {{GNF_GO|id=GO:0045087 |text = innate immune response}} {{GNF_GO|id=GO:0048246 |text = macrophage chemotaxis}} {{GNF_GO|id=GO:0048286 |text = alveolus development}} {{GNF_GO|id=GO:0050766 |text = positive regulation of phagocytosis}} {{GNF_GO|id=GO:0050828 |text = regulation of liquid surface tension}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6441
| Hs_Ensembl = ENSG00000133661
| Hs_RefseqProtein = NP_003010
| Hs_RefseqmRNA = NM_003019
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 81687476
| Hs_GenLoc_end = 81698839
| Hs_Uniprot = P35247
| Mm_EntrezGene = 20390
| Mm_Ensembl = ENSMUSG00000021795
| Mm_RefseqmRNA = NM_009160
| Mm_RefseqProtein = NP_033186
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 40080927
| Mm_GenLoc_end = 40093876
| Mm_Uniprot = P50404
}}
}}
'''Surfactant, pulmonary-associated protein D''', also known as '''SFTPD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SFTPD surfactant, pulmonary-associated protein D| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6441| 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=Hansen S, Holmskov U |title=Structural aspects of collectins and receptors for collectins. |journal=Immunobiology |volume=199 |issue= 2 |pages= 165-89 |year= 1999 |pmid= 9777404 |doi= }}
*{{cite journal | author=Lu J, Willis AC, Reid KB |title=Purification, characterization and cDNA cloning of human lung surfactant protein D. |journal=Biochem. J. |volume=284 ( Pt 3) |issue= |pages= 795-802 |year= 1992 |pmid= 1339284 |doi= }}
*{{cite journal | author=Ogasawara Y, Kuroki Y, Akino T |title=Pulmonary surfactant protein D specifically binds to phosphatidylinositol. |journal=J. Biol. Chem. |volume=267 |issue= 29 |pages= 21244-9 |year= 1992 |pmid= 1400434 |doi= }}
*{{cite journal | author=Rust K, Grosso L, Zhang V, ''et al.'' |title=Human surfactant protein D: SP-D contains a C-type lectin carbohydrate recognition domain. |journal=Arch. Biochem. Biophys. |volume=290 |issue= 1 |pages= 116-26 |year= 1991 |pmid= 1898081 |doi= }}
*{{cite journal | author=Kuroki Y, Shiratori M, Ogasawara Y, ''et al.'' |title=Characterization of pulmonary surfactant protein D: its copurification with lipids. |journal=Biochim. Biophys. Acta |volume=1086 |issue= 2 |pages= 185-90 |year= 1991 |pmid= 1932100 |doi= }}
*{{cite journal | author=Crouch E, Persson A, Chang D, Heuser J |title=Molecular structure of pulmonary surfactant protein D (SP-D). |journal=J. Biol. Chem. |volume=269 |issue= 25 |pages= 17311-9 |year= 1994 |pmid= 8006040 |doi= }}
*{{cite journal | author=Schaeffer E, Guillou F, Part D, Zakin MM |title=A different combination of transcription factors modulates the expression of the human transferrin promoter in liver and Sertoli cells. |journal=J. Biol. Chem. |volume=268 |issue= 31 |pages= 23399-408 |year= 1993 |pmid= 8226864 |doi= }}
*{{cite journal | author=Kölble K, Lu J, Mole SE, ''et al.'' |title=Assignment of the human pulmonary surfactant protein D gene (SFTP4) to 10q22-q23 close to the surfactant protein A gene cluster. |journal=Genomics |volume=17 |issue= 2 |pages= 294-8 |year= 1993 |pmid= 8406480 |doi= 10.1006/geno.1993.1324 }}
*{{cite journal | author=Crouch E, Persson A, Chang D |title=Accumulation of surfactant protein D in human pulmonary alveolar proteinosis. |journal=Am. J. Pathol. |volume=142 |issue= 1 |pages= 241-8 |year= 1993 |pmid= 8424457 |doi= }}
*{{cite journal | author=Crouch E, Rust K, Veile R, ''et al.'' |title=Genomic organization of human surfactant protein D (SP-D). SP-D is encoded on chromosome 10q22.2-23.1. |journal=J. Biol. Chem. |volume=268 |issue= 4 |pages= 2976-83 |year= 1993 |pmid= 8428971 |doi= }}
*{{cite journal | author=Rust K, Bingle L, Mariencheck W, ''et al.'' |title=Characterization of the human surfactant protein D promoter: transcriptional regulation of SP-D gene expression by glucocorticoids. |journal=Am. J. Respir. Cell Mol. Biol. |volume=14 |issue= 2 |pages= 121-30 |year= 1996 |pmid= 8630261 |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=Holmskov U, Lawson P, Teisner B, ''et al.'' |title=Isolation and characterization of a new member of the scavenger receptor superfamily, glycoprotein-340 (gp-340), as a lung surfactant protein-D binding molecule. |journal=J. Biol. Chem. |volume=272 |issue= 21 |pages= 13743-9 |year= 1997 |pmid= 9153228 |doi= }}
*{{cite journal | author=Botas C, Poulain F, Akiyama J, ''et al.'' |title=Altered surfactant homeostasis and alveolar type II cell morphology in mice lacking surfactant protein D. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 20 |pages= 11869-74 |year= 1998 |pmid= 9751757 |doi= }}
*{{cite journal | author=Håkansson K, Lim NK, Hoppe HJ, Reid KB |title=Crystal structure of the trimeric alpha-helical coiled-coil and the three lectin domains of human lung surfactant protein D. |journal=Structure |volume=7 |issue= 3 |pages= 255-64 |year= 1999 |pmid= 10368295 |doi= }}
*{{cite journal | author=Holmskov U, Mollenhauer J, Madsen J, ''et al.'' |title=Cloning of gp-340, a putative opsonin receptor for lung surfactant protein D. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 19 |pages= 10794-9 |year= 1999 |pmid= 10485905 |doi= }}
*{{cite journal | author=Lausen M, Lynch N, Schlosser A, ''et al.'' |title=Microfibril-associated protein 4 is present in lung washings and binds to the collagen region of lung surfactant protein D. |journal=J. Biol. Chem. |volume=274 |issue= 45 |pages= 32234-40 |year= 1999 |pmid= 10542261 |doi= }}
*{{cite journal | author=Madsen J, Kliem A, Tornoe I, ''et al.'' |title=Localization of lung surfactant protein D on mucosal surfaces in human tissues. |journal=J. Immunol. |volume=164 |issue= 11 |pages= 5866-70 |year= 2000 |pmid= 10820266 |doi= }}
*{{cite journal | author=Zhang L, Ikegami M, Crouch EC, ''et al.'' |title=Activity of pulmonary surfactant protein-D (SP-D) in vivo is dependent on oligomeric structure. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19214-9 |year= 2001 |pmid= 11278637 |doi= 10.1074/jbc.M010191200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TH... {November 15, 2007 6:59:37 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:59:57 PM 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_TH_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1toh.
| PDB = {{PDB2|1toh}}, {{PDB2|2toh}}
| Name = Tyrosine hydroxylase
| HGNCid = 11782
| Symbol = TH
| AltSymbols =; TYH
| OMIM = 191290
| ECnumber =
| Homologene = 307
| MGIid = 98735
| GeneAtlas_image1 = PBB_GE_TH_208291_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0004511 |text = tyrosine 3-monooxygenase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0001963 |text = synaptic transmission, dopaminergic}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0007612 |text = learning}} {{GNF_GO|id=GO:0007613 |text = memory}} {{GNF_GO|id=GO:0007617 |text = mating behavior}} {{GNF_GO|id=GO:0007626 |text = locomotory behavior}} {{GNF_GO|id=GO:0008016 |text = regulation of heart contraction}} {{GNF_GO|id=GO:0009072 |text = aromatic amino acid family metabolic process}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0042136 |text = neurotransmitter biosynthetic process}} {{GNF_GO|id=GO:0042423 |text = catecholamine biosynthetic process}} {{GNF_GO|id=GO:0042755 |text = eating behavior}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7054
| Hs_Ensembl = ENSG00000180176
| Hs_RefseqProtein = NP_000351
| Hs_RefseqmRNA = NM_000360
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 2141735
| Hs_GenLoc_end = 2149612
| Hs_Uniprot = P07101
| Mm_EntrezGene = 21823
| Mm_Ensembl = ENSMUSG00000000214
| Mm_RefseqmRNA = NM_009377
| Mm_RefseqProtein = NP_033403
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 142702166
| Mm_GenLoc_end = 142709356
| Mm_Uniprot = Q3UTB3
}}
}}
'''Tyrosine hydroxylase''', also known as '''TH''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TH tyrosine hydroxylase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7054| 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 = Tyrosine hydroxylase is involved in the conversion of tyrosine to dopamine. As the rate-limiting enzyme in the synthesis of catecholamines, tyrosine hydroxylase has a key role in the physiology of adrenergic neurons.<ref name="entrez">{{cite web | title = Entrez Gene: TH tyrosine hydroxylase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7054| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Masserano JM, Weiner N |title=Tyrosine hydroxylase regulation in the central nervous system. |journal=Mol. Cell. Biochem. |volume=53-54 |issue= 1-2 |pages= 129-52 |year= 1983 |pmid= 6137760 |doi= }}
*{{cite journal | author=Meloni R, Biguet NF, Mallet J |title=Post-genomic era and gene discovery for psychiatric diseases: there is a new art of the trade? The example of the HUMTH01 microsatellite in the Tyrosine Hydroxylase gene. |journal=Mol. Neurobiol. |volume=26 |issue= 2-3 |pages= 389-403 |year= 2002 |pmid= 12428766 |doi= }}
*{{cite journal | author=Joh TH, Park DH, Reis DJ |title=Direct phosphorylation of brain tyrosine hydroxylase by cyclic AMP-dependent protein kinase: mechanism of enzyme activation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=75 |issue= 10 |pages= 4744-8 |year= 1979 |pmid= 33381 |doi= }}
*{{cite journal | author=Haycock JW, Ahn NG, Cobb MH, Krebs EG |title=ERK1 and ERK2, two microtubule-associated protein 2 kinases, mediate the phosphorylation of tyrosine hydroxylase at serine-31 in situ. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 6 |pages= 2365-9 |year= 1992 |pmid= 1347949 |doi= }}
*{{cite journal | author=Haycock JW |title=Phosphorylation of tyrosine hydroxylase in situ at serine 8, 19, 31, and 40. |journal=J. Biol. Chem. |volume=265 |issue= 20 |pages= 11682-91 |year= 1990 |pmid= 1973163 |doi= }}
*{{cite journal | author=Craig SP, Buckle VJ, Lamouroux A, ''et al.'' |title=Localization of the human tyrosine hydroxylase gene to 11p15: gene duplication and evolution of metabolic pathways. |journal=Cytogenet. Cell Genet. |volume=42 |issue= 1-2 |pages= 29-32 |year= 1986 |pmid= 2872999 |doi= }}
*{{cite journal | author=Grima B, Lamouroux A, Boni C, ''et al.'' |title=A single human gene encoding multiple tyrosine hydroxylases with different predicted functional characteristics. |journal=Nature |volume=326 |issue= 6114 |pages= 707-11 |year= 1987 |pmid= 2882428 |doi= 10.1038/326707a0 }}
*{{cite journal | author=Kaneda N, Kobayashi K, Ichinose H, ''et al.'' |title=Isolation of a novel cDNA clone for human tyrosine hydroxylase: alternative RNA splicing produces four kinds of mRNA from a single gene. |journal=Biochem. Biophys. Res. Commun. |volume=146 |issue= 3 |pages= 971-5 |year= 1987 |pmid= 2887169 |doi= }}
*{{cite journal | author=Kobayashi K, Kaneda N, Ichinose H, ''et al.'' |title=Isolation of a full-length cDNA clone encoding human tyrosine hydroxylase type 3. |journal=Nucleic Acids Res. |volume=15 |issue= 16 |pages= 6733 |year= 1987 |pmid= 2888085 |doi= }}
*{{cite journal | author=O'Malley KL, Anhalt MJ, Martin BM, ''et al.'' |title=Isolation and characterization of the human tyrosine hydroxylase gene: identification of 5' alternative splice sites responsible for multiple mRNAs. |journal=Biochemistry |volume=26 |issue= 22 |pages= 6910-4 |year= 1988 |pmid= 2892528 |doi= }}
*{{cite journal | author=Le Bourdellès B, Boularand S, Boni C, ''et al.'' |title=Analysis of the 5' region of the human tyrosine hydroxylase gene: combinatorial patterns of exon splicing generate multiple regulated tyrosine hydroxylase isoforms. |journal=J. Neurochem. |volume=50 |issue= 3 |pages= 988-91 |year= 1988 |pmid= 2892893 |doi= }}
*{{cite journal | author=Ginns EI, Rehavi M, Martin BM, ''et al.'' |title=Expression of human tyrosine hydroxylase cDNA in invertebrate cells using a baculovirus vector. |journal=J. Biol. Chem. |volume=263 |issue= 15 |pages= 7406-10 |year= 1988 |pmid= 2896667 |doi= }}
*{{cite journal | author=Kobayashi K, Kaneda N, Ichinose H, ''et al.'' |title=Structure of the human tyrosine hydroxylase gene: alternative splicing from a single gene accounts for generation of four mRNA types. |journal=J. Biochem. |volume=103 |issue= 6 |pages= 907-12 |year= 1988 |pmid= 2902075 |doi= }}
*{{cite journal | author=Coker GT, Vinnedge L, O'Malley KL |title=Characterization of rat and human tyrosine hydroxylase genes: functional expression of both promoters in neuronal and non-neuronal cell types. |journal=Biochem. Biophys. Res. Commun. |volume=157 |issue= 3 |pages= 1341-7 |year= 1989 |pmid= 2905129 |doi= }}
*{{cite journal | author=Vulliet PR, Woodgett JR, Cohen P |title=Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase. |journal=J. Biol. Chem. |volume=259 |issue= 22 |pages= 13680-3 |year= 1984 |pmid= 6150037 |doi= }}
*{{cite journal | author=Zhou QY, Quaife CJ, Palmiter RD |title=Targeted disruption of the tyrosine hydroxylase gene reveals that catecholamines are required for mouse fetal development. |journal=Nature |volume=374 |issue= 6523 |pages= 640-3 |year= 1995 |pmid= 7715703 |doi= 10.1038/374640a0 }}
*{{cite journal | author=Lüdecke B, Bartholomé K |title=Frequent sequence variant in the human tyrosine hydroxylase gene. |journal=Hum. Genet. |volume=95 |issue= 6 |pages= 716 |year= 1995 |pmid= 7789962 |doi= }}
*{{cite journal | author=Lüdecke B, Dworniczak B, Bartholomé K |title=A point mutation in the tyrosine hydroxylase gene associated with Segawa's syndrome. |journal=Hum. Genet. |volume=95 |issue= 1 |pages= 123-5 |year= 1995 |pmid= 7814018 |doi= }}
*{{cite journal | author=Knappskog PM, Flatmark T, Mallet J, ''et al.'' |title=Recessively inherited L-DOPA-responsive dystonia caused by a point mutation (Q381K) in the tyrosine hydroxylase gene. |journal=Hum. Mol. Genet. |volume=4 |issue= 7 |pages= 1209-12 |year= 1996 |pmid= 8528210 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on THPO... {November 15, 2007 6:59:57 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:00:34 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_THPO_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1v7m.
| PDB = {{PDB2|1v7m}}, {{PDB2|1v7n}}
| Name = Thrombopoietin (myeloproliferative leukemia virus oncogene ligand, megakaryocyte growth and development factor)
| HGNCid = 11795
| Symbol = THPO
| AltSymbols =; MGC163194; MGDF; MKCSF; ML; MPLLG; TPO
| OMIM = 600044
| ECnumber =
| Homologene = 398
| MGIid = 101875
| GeneAtlas_image1 = PBB_GE_THPO_211155_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_THPO_211154_at_tn.png
| GeneAtlas_image3 = PBB_GE_THPO_211831_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005179 |text = hormone activity}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0030099 |text = myeloid cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7066
| Hs_Ensembl = ENSG00000090534
| Hs_RefseqProtein = NP_954698
| Hs_RefseqmRNA = NM_199228
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 185572995
| Hs_GenLoc_end = 185578626
| Hs_Uniprot = P40225
| Mm_EntrezGene = 21832
| Mm_Ensembl = ENSMUSG00000022847
| Mm_RefseqmRNA = NM_009379
| Mm_RefseqProtein = NP_033405
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 20638951
| Mm_GenLoc_end = 20642402
| Mm_Uniprot = Q543R9
}}
}}
'''Thrombopoietin (myeloproliferative leukemia virus oncogene ligand, megakaryocyte growth and development factor)''', also known as '''THPO''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: THPO thrombopoietin (myeloproliferative leukemia virus oncogene ligand, megakaryocyte growth and development factor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7066| 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 = Megakaryocytopoiesis is the cellular development process that leads to platelet production. The protein encoded by this gene is a humoral growth factor that is necessary for megakaryocyte proliferation and maturation, as well as for thrombopoiesis. This protein is the ligand for MLP/C_MPL, the product of myeloproliferative leukemia virus oncogene.<ref name="entrez">{{cite web | title = Entrez Gene: THPO thrombopoietin (myeloproliferative leukemia virus oncogene ligand, megakaryocyte growth and development factor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7066| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kato T, Matsumoto A, Ogami K, ''et al.'' |title=Native thrombopoietin: structure and function. |journal=Stem Cells |volume=16 |issue= 5 |pages= 322-8 |year= 1999 |pmid= 9766811 |doi= }}
*{{cite journal | author=Kato T |title=Protein characteristics of thrombopoietin. |journal=Stem Cells |volume=14 Suppl 1 |issue= |pages= 139-47 |year= 2000 |pmid= 11012214 |doi= }}
*{{cite journal | author=Geddis AE, Linden HM, Kaushansky K |title=Thrombopoietin: a pan-hematopoietic cytokine. |journal=Cytokine Growth Factor Rev. |volume=13 |issue= 1 |pages= 61-73 |year= 2002 |pmid= 11750880 |doi= }}
*{{cite journal | author=von dem Borne A, Folman C, van den Oudenrijn S, ''et al.'' |title=The potential role of thrombopoietin in idiopathic thrombocytopenic purpura. |journal=Blood Rev. |volume=16 |issue= 1 |pages= 57-9 |year= 2002 |pmid= 11913997 |doi= 10.1054/blre.2001.0184 }}
*{{cite journal | author=Kaushansky K |title=Thrombopoietin: from theory to reality. |journal=Int. J. Hematol. |volume=76 Suppl 1 |issue= |pages= 343-5 |year= 2003 |pmid= 12430879 |doi= }}
*{{cite journal | author=Kralovics R, Skoda RC |title=Molecular pathogenesis of Philadelphia chromosome negative myeloproliferative disorders. |journal=Blood Rev. |volume=19 |issue= 1 |pages= 1-13 |year= 2005 |pmid= 15572213 |doi= 10.1016/j.blre.2004.02.002 }}
*{{cite journal | author=Migliaccio AR, Rana RA, Vannucchi AM, Manzoli FA |title=Role of thrombopoietin in mast cell differentiation. |journal=Ann. N. Y. Acad. Sci. |volume=1106 |issue= |pages= 152-74 |year= 2007 |pmid= 17468237 |doi= 10.1196/annals.1392.024 }}
*{{cite journal | author=Foster DC, Sprecher CA, Grant FJ, ''et al.'' |title=Human thrombopoietin: gene structure, cDNA sequence, expression, and chromosomal localization. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 26 |pages= 13023-7 |year= 1995 |pmid= 7809166 |doi= }}
*{{cite journal | author=Chang MS, McNinch J, Basu R, ''et al.'' |title=Cloning and characterization of the human megakaryocyte growth and development factor (MGDF) gene. |journal=J. Biol. Chem. |volume=270 |issue= 2 |pages= 511-4 |year= 1995 |pmid= 7822271 |doi= }}
*{{cite journal | author=Gurney AL, Kuang WJ, Xie MH, ''et al.'' |title=Genomic structure, chromosomal localization, and conserved alternative splice forms of thrombopoietin. |journal=Blood |volume=85 |issue= 4 |pages= 981-8 |year= 1995 |pmid= 7849319 |doi= }}
*{{cite journal | author=Sohma Y, Akahori H, Seki N, ''et al.'' |title=Molecular cloning and chromosomal localization of the human thrombopoietin gene. |journal=FEBS Lett. |volume=353 |issue= 1 |pages= 57-61 |year= 1994 |pmid= 7926023 |doi= }}
*{{cite journal | author=Bartley TD, Bogenberger J, Hunt P, ''et al.'' |title=Identification and cloning of a megakaryocyte growth and development factor that is a ligand for the cytokine receptor Mpl. |journal=Cell |volume=77 |issue= 7 |pages= 1117-24 |year= 1994 |pmid= 8020099 |doi= }}
*{{cite journal | author=de Sauvage FJ, Hass PE, Spencer SD, ''et al.'' |title=Stimulation of megakaryocytopoiesis and thrombopoiesis by the c-Mpl ligand. |journal=Nature |volume=369 |issue= 6481 |pages= 533-8 |year= 1994 |pmid= 8202154 |doi= 10.1038/369533a0 }}
*{{cite journal | author=Kaushansky K, Lok S, Holly RD, ''et al.'' |title=Promotion of megakaryocyte progenitor expansion and differentiation by the c-Mpl ligand thrombopoietin. |journal=Nature |volume=369 |issue= 6481 |pages= 568-71 |year= 1994 |pmid= 8202159 |doi= 10.1038/369568a0 }}
*{{cite journal | author=Wendling F, Maraskovsky E, Debili N, ''et al.'' |title=cMpl ligand is a humoral regulator of megakaryocytopoiesis. |journal=Nature |volume=369 |issue= 6481 |pages= 571-4 |year= 1994 |pmid= 8202160 |doi= 10.1038/369571a0 }}
*{{cite journal | author=Kato T, Ogami K, Shimada Y, ''et al.'' |title=Purification and characterization of thrombopoietin. |journal=J. Biochem. |volume=118 |issue= 1 |pages= 229-36 |year= 1996 |pmid= 8537317 |doi= }}
*{{cite journal | author=Hoffman RC, Andersen H, Walker K, ''et al.'' |title=Peptide, disulfide, and glycosylation mapping of recombinant human thrombopoietin from ser1 to Arg246. |journal=Biochemistry |volume=35 |issue= 47 |pages= 14849-61 |year= 1997 |pmid= 8942648 |doi= 10.1021/bi961075b }}
*{{cite journal | author=Wiestner A, Schlemper RJ, van der Maas AP, Skoda RC |title=An activating splice donor mutation in the thrombopoietin gene causes hereditary thrombocythaemia. |journal=Nat. Genet. |volume=18 |issue= 1 |pages= 49-52 |year= 1998 |pmid= 9425899 |doi= 10.1038/ng0198-49 }}
*{{cite journal | author=Kondo T, Okabe M, Sanada M, ''et al.'' |title=Familial essential thrombocythemia associated with one-base deletion in the 5'-untranslated region of the thrombopoietin gene. |journal=Blood |volume=92 |issue= 4 |pages= 1091-6 |year= 1998 |pmid= 9694695 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TNFRSF10A... {November 15, 2007 7:01:22 PM PST}
- SEARCH REDIRECT: Control Box Found: TNFRSF10A {November 15, 2007 7:01:58 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 7:02:00 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 7:02:00 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 7:02:00 PM PST}
- UPDATED: Updated protein page: TNFRSF10A {November 15, 2007 7:02:07 PM PST}
- INFO: Beginning work on TSC1... {November 15, 2007 7:00:34 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:01:01 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Tuberous sclerosis 1
| HGNCid = 12362
| Symbol = TSC1
| AltSymbols =; TSC; KIAA0243; LAM; MGC86987
| OMIM = 605284
| ECnumber =
| Homologene = 314
| MGIid = 1929183
| GeneAtlas_image1 = PBB_GE_TSC1_209390_at_tn.png
| Function =
| Component =
| Process = {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007266 |text = Rho protein signal transduction}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7248
| Hs_Ensembl = ENSG00000165699
| Hs_RefseqProtein = NP_000359
| Hs_RefseqmRNA = NM_000368
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 134756557
| Hs_GenLoc_end = 134809841
| Hs_Uniprot = Q92574
| Mm_EntrezGene = 64930
| Mm_Ensembl = ENSMUSG00000026812
| Mm_RefseqmRNA = NM_022887
| Mm_RefseqProtein = NP_075025
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 28463246
| Mm_GenLoc_end = 28513176
| Mm_Uniprot =
}}
}}
'''Tuberous sclerosis 1''', also known as '''TSC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TSC1 tuberous sclerosis 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7248| 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=Hengstschläger M |title=Tuberous sclerosis complex genes: from flies to human genetics. |journal=Arch. Dermatol. Res. |volume=293 |issue= 8 |pages= 383-6 |year= 2002 |pmid= 11686512 |doi= }}
*{{cite journal | author=Ramesh V |title=Aspects of tuberous sclerosis complex (TSC) protein function in the brain. |journal=Biochem. Soc. Trans. |volume=31 |issue= Pt 3 |pages= 579-83 |year= 2004 |pmid= 12773159 |doi= 10.1042/ }}
*{{cite journal | author=Knowles MA, Hornigold N, Pitt E |title=Tuberous sclerosis complex (TSC) gene involvement in sporadic tumours. |journal=Biochem. Soc. Trans. |volume=31 |issue= Pt 3 |pages= 597-602 |year= 2004 |pmid= 12773163 |doi= 10.1042/ }}
*{{cite journal | author=Ellisen LW |title=Growth control under stress: mTOR regulation through the REDD1-TSC pathway. |journal=Cell Cycle |volume=4 |issue= 11 |pages= 1500-02 |year= 2007 |pmid= 16258273 |doi= }}
*{{cite journal | author=Jozwiak J, Jozwiak S |title=Giant cells: contradiction to two-hit model of tuber formation? |journal=Cell. Mol. Neurobiol. |volume=27 |issue= 2 |pages= 251-61 |year= 2007 |pmid= 16897363 |doi= 10.1007/s10571-006-9106-0 }}
*{{cite journal | author=Nagase T, Seki N, Ishikawa K, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. |journal=DNA Res. |volume=3 |issue= 5 |pages= 321-9, 341-54 |year= 1997 |pmid= 9039502 |doi= }}
*{{cite journal | author=van Slegtenhorst M, de Hoogt R, Hermans C, ''et al.'' |title=Identification of the tuberous sclerosis gene TSC1 on chromosome 9q34. |journal=Science |volume=277 |issue= 5327 |pages= 805-8 |year= 1997 |pmid= 9242607 |doi= }}
*{{cite journal | author=Jones AC, Daniells CE, Snell RG, ''et al.'' |title=Molecular genetic and phenotypic analysis reveals differences between TSC1 and TSC2 associated familial and sporadic tuberous sclerosis. |journal=Hum. Mol. Genet. |volume=6 |issue= 12 |pages= 2155-61 |year= 1997 |pmid= 9328481 |doi= }}
*{{cite journal | author=van Slegtenhorst M, Nellist M, Nagelkerken B, ''et al.'' |title=Interaction between hamartin and tuberin, the TSC1 and TSC2 gene products. |journal=Hum. Mol. Genet. |volume=7 |issue= 6 |pages= 1053-7 |year= 1998 |pmid= 9580671 |doi= }}
*{{cite journal | author=Plank TL, Yeung RS, Henske EP |title=Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene, interacts with tuberin and appears to be localized to cytoplasmic vesicles. |journal=Cancer Res. |volume=58 |issue= 21 |pages= 4766-70 |year= 1998 |pmid= 9809973 |doi= }}
*{{cite journal | author=Kwiatkowska J, Jozwiak S, Hall F, ''et al.'' |title=Comprehensive mutational analysis of the TSC1 gene: observations on frequency of mutation, associated features, and nonpenetrance. |journal=Ann. Hum. Genet. |volume=62 |issue= Pt 4 |pages= 277-85 |year= 1999 |pmid= 9924605 |doi= 10.1046/j.1469-1809.1998.6240277.x }}
*{{cite journal | author=van Slegtenhorst M, Verhoef S, Tempelaars A, ''et al.'' |title=Mutational spectrum of the TSC1 gene in a cohort of 225 tuberous sclerosis complex patients: no evidence for genotype-phenotype correlation. |journal=J. Med. Genet. |volume=36 |issue= 4 |pages= 285-9 |year= 1999 |pmid= 10227394 |doi= }}
*{{cite journal | author=Niida Y, Lawrence-Smith N, Banwell A, ''et al.'' |title=Analysis of both TSC1 and TSC2 for germline mutations in 126 unrelated patients with tuberous sclerosis. |journal=Hum. Mutat. |volume=14 |issue= 5 |pages= 412-22 |year= 2000 |pmid= 10533067 |doi= 10.1002/(SICI)1098-1004(199911)14:5<412::AID-HUMU7>3.0.CO;2-K }}
*{{cite journal | author=Zhang H, Nanba E, Yamamoto T, ''et al.'' |title=Mutational analysis of TSC1 and TSC2 genes in Japanese patients with tuberous sclerosis complex. |journal=J. Hum. Genet. |volume=44 |issue= 6 |pages= 391-6 |year= 2000 |pmid= 10570911 |doi= }}
*{{cite journal | author=Nellist M, van Slegtenhorst MA, Goedbloed M, ''et al.'' |title=Characterization of the cytosolic tuberin-hamartin complex. Tuberin is a cytosolic chaperone for hamartin. |journal=J. Biol. Chem. |volume=274 |issue= 50 |pages= 35647-52 |year= 2000 |pmid= 10585443 |doi= }}
*{{cite journal | author=Yamashita Y, Ono J, Okada S, ''et al.'' |title=Analysis of all exons of TSC1 and TSC2 genes for germline mutations in Japanese patients with tuberous sclerosis: report of 10 mutations. |journal=Am. J. Med. Genet. |volume=90 |issue= 2 |pages= 123-6 |year= 2000 |pmid= 10607950 |doi= }}
*{{cite journal | author=Lamb RF, Roy C, Diefenbach TJ, ''et al.'' |title=The TSC1 tumour suppressor hamartin regulates cell adhesion through ERM proteins and the GTPase Rho. |journal=Nat. Cell Biol. |volume=2 |issue= 5 |pages= 281-7 |year= 2000 |pmid= 10806479 |doi= 10.1038/35010550 }}
*{{cite journal | author=Miloloza A, Rosner M, Nellist M, ''et al.'' |title=The TSC1 gene product, hamartin, negatively regulates cell proliferation. |journal=Hum. Mol. Genet. |volume=9 |issue= 12 |pages= 1721-7 |year= 2000 |pmid= 10915759 |doi= }}
*{{cite journal | author=Murthy V, Stemmer-Rachamimov AO, Haddad LA, ''et al.'' |title=Developmental expression of the tuberous sclerosis proteins tuberin and hamartin. |journal=Acta Neuropathol. |volume=101 |issue= 3 |pages= 202-10 |year= 2001 |pmid= 11307618 |doi= }}
*{{cite journal | author=Catania MG, Mischel PS, Vinters HV |title=Hamartin and tuberin interaction with the G2/M cyclin-dependent kinase CDK1 and its regulatory cyclins A and B. |journal=J. Neuropathol. Exp. Neurol. |volume=60 |issue= 7 |pages= 711-23 |year= 2001 |pmid= 11444800 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on VCL... {November 15, 2007 7:01:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:01:22 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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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_VCL_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1qkr.
| PDB = {{PDB2|1qkr}}, {{PDB2|1rkc}}, {{PDB2|1rke}}, {{PDB2|1st6}}, {{PDB2|1syq}}, {{PDB2|1t01}}, {{PDB2|1tr2}}, {{PDB2|1u6h}}, {{PDB2|1xwj}}, {{PDB2|1ydi}}, {{PDB2|1zvz}}, {{PDB2|1zw2}}, {{PDB2|1zw3}}, {{PDB2|2gdc}}, {{PDB2|2gww}}, {{PDB2|2hsq}}
| Name = Vinculin
| HGNCid = 12665
| Symbol = VCL
| AltSymbols =; MVCL
| OMIM = 193065
| ECnumber =
| Homologene = 7594
| MGIid = 98927
| GeneAtlas_image1 = PBB_GE_VCL_200931_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_VCL_200930_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0045294 |text = alpha-catenin binding}}
| Component = {{GNF_GO|id=GO:0005911 |text = intercellular junction}} {{GNF_GO|id=GO:0005912 |text = adherens junction}} {{GNF_GO|id=GO:0005925 |text = focal adhesion}} {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}} {{GNF_GO|id=GO:0030055 |text = cell-matrix junction}} {{GNF_GO|id=GO:0043034 |text = costamere}} {{GNF_GO|id=GO:0043234 |text = protein complex}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0030032 |text = lamellipodium biogenesis}} {{GNF_GO|id=GO:0030336 |text = negative regulation of cell migration}} {{GNF_GO|id=GO:0043297 |text = apical junction assembly}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7414
| Hs_Ensembl = ENSG00000035403
| Hs_RefseqProtein = NP_003364
| Hs_RefseqmRNA = NM_003373
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 75427878
| Hs_GenLoc_end = 75549924
| Hs_Uniprot = P18206
| Mm_EntrezGene = 22330
| Mm_Ensembl = ENSMUSG00000021823
| Mm_RefseqmRNA = NM_009502
| Mm_RefseqProtein = NP_033528
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 19717950
| Mm_GenLoc_end = 19822228
| Mm_Uniprot = Q64727
}}
}}
'''Vinculin''', also known as '''VCL''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: VCL vinculin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7414| 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 = Vinculin is a cytoskeletal protein associated with cell-cell and cell-matrix junctions, where it is thought to function as one of several interacting proteins involved in anchoring F-actin to the membrane. Multiple alternatively spliced transcript variants have been found for this gene, but the biological validity of some variants has not been determined. Human vinculin protein exhibits a greater than 95% sequence identity to the chicken vinculin protein.<ref name="entrez">{{cite web | title = Entrez Gene: VCL vinculin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7414| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Critchley DR |title=Cytoskeletal proteins talin and vinculin in integrin-mediated adhesion. |journal=Biochem. Soc. Trans. |volume=32 |issue= Pt 5 |pages= 831-6 |year= 2005 |pmid= 15494027 |doi= 10.1042/BST0320831 }}
*{{cite journal | author=Koteliansky VE, Ogryzko EP, Zhidkova NI, ''et al.'' |title=An additional exon in the human vinculin gene specifically encodes meta-vinculin-specific difference peptide. Cross-species comparison reveals variable and conserved motifs in the meta-vinculin insert. |journal=Eur. J. Biochem. |volume=204 |issue= 2 |pages= 767-72 |year= 1992 |pmid= 1339348 |doi= }}
*{{cite journal | author=Mulligan LM, Gardner E, Telenius H, Ponder BA |title=Complementary physical and genetic techniques map the vinculin (VCL) gene on chromosome 10q. |journal=Genomics |volume=13 |issue= 4 |pages= 1347-9 |year= 1992 |pmid= 1505973 |doi= }}
*{{cite journal | author=Weller PA, Ogryzko EP, Corben EB, ''et al.'' |title=Complete sequence of human vinculin and assignment of the gene to chromosome 10. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 15 |pages= 5667-71 |year= 1990 |pmid= 2116004 |doi= }}
*{{cite journal | author=Turner CE, Burridge K |title=Detection of metavinculin in human platelets using a modified talin overlay assay. |journal=Eur. J. Cell Biol. |volume=49 |issue= 1 |pages= 202-6 |year= 1989 |pmid= 2503380 |doi= }}
*{{cite journal | author=Turner CE, Miller JT |title=Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: identification of a vinculin and pp125Fak-binding region. |journal=J. Cell. Sci. |volume=107 ( Pt 6) |issue= |pages= 1583-91 |year= 1994 |pmid= 7525621 |doi= }}
*{{cite journal | author=Salgia R, Li JL, Lo SH, ''et al.'' |title=Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL. |journal=J. Biol. Chem. |volume=270 |issue= 10 |pages= 5039-47 |year= 1995 |pmid= 7534286 |doi= }}
*{{cite journal | author=Adams MD, Kerlavage AR, Fleischmann RD, ''et al.'' |title=Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. |journal=Nature |volume=377 |issue= 6547 Suppl |pages= 3-174 |year= 1995 |pmid= 7566098 |doi= }}
*{{cite journal | author=Hagmann J |title=Pattern formation and handedness in the cytoskeleton of human platelets. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 8 |pages= 3280-3 |year= 1993 |pmid= 7682697 |doi= }}
*{{cite journal | author=Johnson RP, Craig SW |title=F-actin binding site masked by the intramolecular association of vinculin head and tail domains. |journal=Nature |volume=373 |issue= 6511 |pages= 261-4 |year= 1995 |pmid= 7816144 |doi= 10.1038/373261a0 }}
*{{cite journal | author=Hirsch MS, Law LY, Trinkaus-Randall V, Svoboda KK |title=The intracellular distribution of vinculin and alpha 2 integrin in epithelial cells and chondrocytes. |journal=Scanning |volume=16 |issue= 5 |pages= 275-84 |year= 1995 |pmid= 7994488 |doi= }}
*{{cite journal | author=Fausser JL, Ungewickell E, Ruch JV, Lesot H |title=Interaction of vinculin with the clathrin heavy chain. |journal=J. Biochem. |volume=114 |issue= 4 |pages= 498-503 |year= 1994 |pmid= 8276759 |doi= }}
*{{cite journal | author=Moiseyeva EP, Weller PA, Zhidkova NI, ''et al.'' |title=Organization of the human gene encoding the cytoskeletal protein vinculin and the sequence of the vinculin promoter. |journal=J. Biol. Chem. |volume=268 |issue= 6 |pages= 4318-25 |year= 1993 |pmid= 8440716 |doi= }}
*{{cite journal | author=Yoshida M, Westlin WF, Wang N, ''et al.'' |title=Leukocyte adhesion to vascular endothelium induces E-selectin linkage to the actin cytoskeleton. |journal=J. Cell Biol. |volume=133 |issue= 2 |pages= 445-55 |year= 1996 |pmid= 8609175 |doi= }}
*{{cite journal | author=Scott GA, Liang H, Cassidy LL |title=Developmental regulation of focal contact protein expression in human melanocytes. |journal=Pigment Cell Res. |volume=8 |issue= 4 |pages= 221-8 |year= 1996 |pmid= 8610074 |doi= }}
*{{cite journal | author=Deroanne CF, Colige AC, Nusgens BV, Lapiere CM |title=Modulation of expression and assembly of vinculin during in vitro fibrillar collagen-induced angiogenesis and its reversal. |journal=Exp. Cell Res. |volume=224 |issue= 2 |pages= 215-23 |year= 1996 |pmid= 8612698 |doi= 10.1006/excr.1996.0131 }}
*{{cite journal | author=Maeda M, Holder E, Lowes B, ''et al.'' |title=Dilated cardiomyopathy associated with deficiency of the cytoskeletal protein metavinculin. |journal=Circulation |volume=95 |issue= 1 |pages= 17-20 |year= 1997 |pmid= 8994410 |doi= }}
*{{cite journal | author=Mazaki Y, Hashimoto S, Sabe H |title=Monocyte cells and cancer cells express novel paxillin isoforms with different binding properties to focal adhesion proteins. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 7437-44 |year= 1997 |pmid= 9054445 |doi= }}
*{{cite journal | author=Hazan RB, Kang L, Roe S, ''et al.'' |title=Vinculin is associated with the E-cadherin adhesion complex. |journal=J. Biol. Chem. |volume=272 |issue= 51 |pages= 32448-53 |year= 1998 |pmid= 9405455 |doi= }}
*{{cite journal | author=Hazan RB, Norton L |title=The epidermal growth factor receptor modulates the interaction of E-cadherin with the actin cytoskeleton. |journal=J. Biol. Chem. |volume=273 |issue= 15 |pages= 9078-84 |year= 1998 |pmid= 9535896 |doi= }}
}}
{{refend}}
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