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[edit] Protein Status Quick Log - Date: 16:56, 2 April 2008 (UTC)
[edit] Proteins without matches (1)
[edit] Redirected Proteins (1)
[edit] Unresolved Status (1)
[edit] Manual Inspection (Page not found) (1)
[edit] Protein Status Grid - Date: 16:56, 2 April 2008 (UTC)
[edit] Vebose Log - Date: 16:56, 2 April 2008 (UTC)
- INFO: Beginning work on SERPIND1... {April 2, 2008 9:56:01 AM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {April 2, 2008 9:56:23 AM PDT}
<!-- 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_SERPIND1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jmj.
| PDB = {{PDB2|1jmj}}, {{PDB2|1jmo}}
| Name = Serpin peptidase inhibitor, clade D (heparin cofactor), member 1
| HGNCid = 4838
| Symbol = SERPIND1
| AltSymbols =; D22S673; HC2; HCF2; HCII; HLS2; LS2
| OMIM = 142360
| ECnumber =
| Homologene = 36018
| MGIid = 96051
| GeneAtlas_image1 = PBB_GE_SERPIND1_205576_at_tn.png
| GeneAtlas_image2 = PBB_GE_SERPIND1_31825_at_tn.png
| Function = {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}}{{GNF_GO|id=GO:0008201 |text = heparin binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3053
| Hs_Ensembl = ENSG00000099937
| Hs_RefseqProtein = NP_000176
| Hs_RefseqmRNA = NM_000185
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 19458383
| Hs_GenLoc_end = 19472008
| Hs_Uniprot = P05546
| Mm_EntrezGene = 15160
| Mm_Ensembl = ENSMUSG00000022766
| Mm_RefseqmRNA = NM_008223
| Mm_RefseqProtein = NP_032249
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 17244978
| Mm_GenLoc_end = 17257137
| Mm_Uniprot = Q5FW62
}}
}}
'''Serpin peptidase inhibitor, clade D (heparin cofactor), member 1''', also known as '''SERPIND1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SERPIND1 serpin peptidase inhibitor, clade D (heparin cofactor), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3053| 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 encoded by this gene is a serine proteinase inhibitor which rapidly inhibits thrombin in the presence of dermatan sulfate or heparin. The gene contains five exons and four introns. This protein shares homology with antithrombin III and other members of the alpha 1-antitrypsin superfamily. Mutations in this gene are associated with heparin cofactor II deficiency.<ref name="entrez">{{cite web | title = Entrez Gene: SERPIND1 serpin peptidase inhibitor, clade D (heparin cofactor), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3053| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Pizzo SV |title=Serpin receptor 1: a hepatic receptor that mediates the clearance of antithrombin III-proteinase complexes. |journal=Am. J. Med. |volume=87 |issue= 3B |pages= 10S-14S |year= 1989 |pmid= 2552799 |doi= }}
*{{cite journal | author=Uszyński M |title=Tissue anticoagulants in the human placenta: preliminary study with a heparin-like anticoagulant and review of the literature. |journal=Gynecol. Obstet. Invest. |volume=32 |issue= 3 |pages= 129-33 |year= 1992 |pmid= 1836773 |doi= }}
*{{cite journal | author=Sutherland JS, Bhakta V, Filion ML, Sheffield WP |title=The transferable tail: fusion of the N-terminal acidic extension of heparin cofactor II to alpha1-proteinase inhibitor M358R specifically increases the rate of thrombin inhibition. |journal=Biochemistry |volume=45 |issue= 38 |pages= 11444-52 |year= 2006 |pmid= 16981704 |doi= 10.1021/bi0609624 }}
*{{cite journal | author=Giri TK, Tollefsen DM |title=Placental dermatan sulfate: isolation, anticoagulant activity, and association with heparin cofactor II. |journal=Blood |volume=107 |issue= 7 |pages= 2753-8 |year= 2006 |pmid= 16339402 |doi= 10.1182/blood-2005-09-3755 }}
*{{cite journal | author=Liu T, Qian WJ, Gritsenko MA, ''et al.'' |title=Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. |journal=J. Proteome Res. |volume=4 |issue= 6 |pages= 2070-80 |year= 2006 |pmid= 16335952 |doi= 10.1021/pr0502065 }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal | author=Schillinger M, Exner M, Sabeti S, ''et al.'' |title=High plasma heparin cofactor II activity protects from restenosis after femoropopliteal stenting. |journal=Thromb. Haemost. |volume=92 |issue= 5 |pages= 1108-13 |year= 2005 |pmid= 15543340 |doi= 10.1267/THRO04051108 }}
*{{cite journal | author=Collins JE, Wright CL, Edwards CA, ''et al.'' |title=A genome annotation-driven approach to cloning the human ORFeome. |journal=Genome Biol. |volume=5 |issue= 10 |pages= R84 |year= 2005 |pmid= 15461802 |doi= 10.1186/gb-2004-5-10-r84 }}
*{{cite journal | author=Suzuki Y, Yamashita R, Shirota M, ''et al.'' |title=Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions. |journal=Genome Res. |volume=14 |issue= 9 |pages= 1711-8 |year= 2004 |pmid= 15342556 |doi= 10.1101/gr.2435604 }}
*{{cite journal | author=Corral J, Aznar J, Gonzalez-Conejero R, ''et al.'' |title=Homozygous deficiency of heparin cofactor II: relevance of P17 glutamate residue in serpins, relationship with conformational diseases, and role in thrombosis. |journal=Circulation |volume=110 |issue= 10 |pages= 1303-7 |year= 2006 |pmid= 15337701 |doi= 10.1161/01.CIR.0000140763.51679.D9 }}
*{{cite journal | author=Fortenberry YM, Whinna HC, Gentry HR, ''et al.'' |title=Molecular mapping of the thrombin-heparin cofactor II complex. |journal=J. Biol. Chem. |volume=279 |issue= 41 |pages= 43237-44 |year= 2004 |pmid= 15292227 |doi= 10.1074/jbc.M406716200 }}
*{{cite journal | author=Zhang F, Wu Y, Ma Q, ''et al.'' |title=Studies on the effect of calcium in interactions between heparin and heparin cofactor II using surface plasmon resonance. |journal=Clin. Appl. Thromb. Hemost. |volume=10 |issue= 3 |pages= 249-57 |year= 2004 |pmid= 15247982 |doi= }}
*{{cite journal | author=Anderson NL, Polanski M, Pieper R, ''et al.'' |title=The human plasma proteome: a nonredundant list developed by combination of four separate sources. |journal=Mol. Cell Proteomics |volume=3 |issue= 4 |pages= 311-26 |year= 2004 |pmid= 14718574 |doi= 10.1074/mcp.M300127-MCP200 }}
*{{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=Noda A, Wada H, Kusiya F, ''et al.'' |title=Plasma levels of heparin cofactor II (HCII) and thrombin-HCII complex in patients with disseminated intravascular coagulation. |journal=Clin. Appl. Thromb. Hemost. |volume=8 |issue= 3 |pages= 265-71 |year= 2003 |pmid= 12361205 |doi= }}
*{{cite journal | author=Baglin TP, Carrell RW, Church FC, ''et al.'' |title=Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 17 |pages= 11079-84 |year= 2002 |pmid= 12169660 |doi= 10.1073/pnas.162232399 }}
*{{cite journal | author=Cunningham MA, Bhakta V, Sheffield WP |title=Altering heparin cofactor II at VAL439 (P6) either impairs inhibition of thrombin or confers elastase resistance. |journal=Thromb. Haemost. |volume=88 |issue= 1 |pages= 89-97 |year= 2003 |pmid= 12152684 |doi= }}
*{{cite journal | author=Hayakawa Y, Hirashima Y, Kurimoto M, ''et al.'' |title=Contribution of basic residues of the A helix of heparin cofactor II to heparin- or dermatan sulfate-mediated thrombin inhibition. |journal=FEBS Lett. |volume=522 |issue= 1-3 |pages= 147-50 |year= 2002 |pmid= 12095635 |doi= }}
*{{cite journal | author=Mitchell JW, Church FC |title=Aspartic acid residues 72 and 75 and tyrosine-sulfate 73 of heparin cofactor II promote intramolecular interactions during glycosaminoglycan binding and thrombin inhibition. |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 19823-30 |year= 2002 |pmid= 11856753 |doi= 10.1074/jbc.M200630200 }}
*{{cite journal | author=Böhme C, Nimtz M, Grabenhorst E, ''et al.'' |title=Tyrosine sulfation and N-glycosylation of human heparin cofactor II from plasma and recombinant Chinese hamster ovary cells and their effects on heparin binding. |journal=Eur. J. Biochem. |volume=269 |issue= 3 |pages= 977-88 |year= 2002 |pmid= 11846800 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SERPINF2... {April 2, 2008 9:56:23 AM PDT}
- SEARCH REDIRECT: Control Box Found: SERPINF2 {April 2, 2008 9:56:55 AM PDT}
end log.
