Result Untitled Document Fibrinogen beta chainSourceHomo sapiens (human) Taxonomy Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.Keywords3D-structure; Blood coagulation; Coiled coil; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Polymorphism; Pyrrolidone carboxylic acid; Secreted; Signal.DetailsFunction: Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. Post-translational modification: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers. Similarity: Contains 1 fibrinogen C-terminal domain. Subcellular location: Secreted. Subunit structure: Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain (By similarity). Disease: Defects in FGB are a cause of thrombophilia. Defects in FGB are a cause of congenital afibrinogenemia Interaction: Q92876:KLK6; NbExp=1; IntAct=EBI-1034445, EBI-2432309. Sequence length: 491 AA. SequenceMKRMVSWSFHKLKTMKHLLLLLLCVFLVKSQGVNDNEEGFFSARGHRPLDKKREEAPSLRPAPPPISGGGYRARPAKAAATQKKVERKAPDAGGCLHADPDLGVLCPTGCQLQEALLQQERPIRNSVDELNNNVEAVSQTSSSSFQYMYLLKDLWQKRQKQVKDNENVVNEYSSELEKHQLYIDETVNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVVSGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQDGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMGPTELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAGNALMDGASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKMSMKIRPFFPQQAccession NumberP02675 PubMed ID6688356, 2102623, 14702039, 15489334, 6575700, 3029722, 420779, 936108, 12665801, 6575689, 891553, 6383194, 7642629, 16335952, 16263699, 19159218, 9333233, 9628725, 10074346, 3194892, 2018836, 1634610, 1565641, 3156856, 10391209, 10666208, 11468164 CEX DBHS_FGBCTD DB2244DIP DBDIP-385NEnsembl DBENST00000302068CATHG3DSA:3.90.215.10, G3DSA:4.10.530.10, G3DSA:1.20.5.50Genecard DBGC04P155703GeneID DB2244GermOnline DBENSG00000171564GO DB0009897, 0005577, 0031093, 0005625, 0043499, 0030674, 0005102, 0030168, 0051258, 0051592, 0007165HGNC DB3662HOGENOM DBHBG717207HPA DBCAB008624, HPA001900, HPA001901InterPro DBIPR002181, IPR014716, IPR014715, IPR012290, IPR014814, IPR020837H-InvDBHIX0031426IPI DBIPI00298497, REPRODUCTION-2DPAGE:IPI00298497KEGGhsa:2244NCBIJ00129, AAA52429, J00131, AAA98115, J00130, J00132, AAA98116, J00133, M64983, AAA18024.2, AF388026, AAK62470, AK312972, BAG35810, CH471056.2, EAX04932, BC106760.2, AAI06761, M26877, AAA52445, M26876, X05018, CAA28674, NP_005132.2OMATIHNGMFOMIM105200, 134820, 202400, 134830, 202400Orphanet DB335, 98880, 98881, 101041OrthoDBEOG99CSSWPDB1FZA_B, 1FZA_E, 1FZB_B, 1FZB_E, 1FZC_B, 1FZC_E, 1FZE_B, 1FZE_E, 1FZF_B, 1FZF_E, 1FZF_M, 1FZF_N, 1FZF_S, 1FZF_T, 1FZG_B, 1FZG_E, 1FZG_M, 1FZG_N, 1FZG_S, 1FZG_T, 1LT9_B, 1LT9_E, 1LTJ_B, 1LTJ_E, 1N86_B, 1N86_E, 1N86_I, 1N86_J, 1N8E_B, 1N8E_E, 1RE3_B, 1RE3_E, 1RE4_B, 1RE4_E, 1RF0_B, 1RF0_E, 1RF1_B, 1RF1_E, 2A45_H, 2A45_K, 2FFD_B, 2FFD_E, 2H43_B, 2H43_E, 2HLO_B, 2HLO_E, 2HOD_B, 2HOD_E, 2HOD_H, 2HOD_K, 2HPC_B, 2HPC_E, 2HPC_H, 2HPC_K, 2OYH_B, 2OYH_E, 2OYI_B, 2OYI_E, 2Q9I_B, 2Q9I_E, 2Z4E_B, 2Z4E_E, 3BVH_B, 3BVH_E, 3E1I_B, 3E1I_E, 3GHG_B, 3GHG_E, 3GHG_H, 3GHG_K, 3H32_B, 3H32_E, 3HUS_B, 3HUS_EPfamPF08702, PF00147PharmaGKBPA163PROSITE DBPS00514, PS51406SMART DBSM00186UCSCuc003ioa.2UniGeneHs.300774
Result
Fibrinogen beta chain
Function: Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. Post-translational modification: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers. Similarity: Contains 1 fibrinogen C-terminal domain. Subcellular location: Secreted. Subunit structure: Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain (By similarity). Disease: Defects in FGB are a cause of thrombophilia. Defects in FGB are a cause of congenital afibrinogenemia Interaction: Q92876:KLK6; NbExp=1; IntAct=EBI-1034445, EBI-2432309. Sequence length: 491 AA.
MKRMVSWSFHKLKTMKHLLLLLLCVFLVKSQGVNDNEEGFFSARGHRPLDKKREEAPSLRPAPPPISGGGYRARPAKAAATQKKVERKAPDAGGCLHADPDLGVLCPTGCQLQEALLQQERPIRNSVDELNNNVEAVSQTSSSSFQYMYLLKDLWQKRQKQVKDNENVVNEYSSELEKHQLYIDETVNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVVSGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQDGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMGPTELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAGNALMDGASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKMSMKIRPFFPQQ
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