Tag | Content |
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UniProt Accession | FIBA_HUMAN; P02671; |
Entrez ID | 2243 |
GenBank Protein ID | NM_000508.4; NM_021871.3; |
GenBank Nucleotide ID | NP_000499.1; NP_068657.1; |
Protein Name | Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain] |
Gene Name | FGA |
Organism | Homo sapiens |
NCBI Taxa ID | 9606 |
Functional Description | Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways. |
Sequence (Fasta) | MFSMRIVCLV LSVVGTAWTA DSGEGDFLAE GGGVRGPRVV ERHQSACKDS DWPFCSDEDW 60 NYKCPSGCRM KGLIDEVNQD FTNRINKLKN SLFEYQKNNK DSHSLTTNIM EILRGDFSSA 120 NNRDNTYNRV SEDLRSRIEV LKRKVIEKVQ HIQLLQKNVR AQLVDMKRLE VDIDIKIRSC 180 RGSCSRALAR EVDLKDYEDQ QKQLEQVIAK DLLPSRDRQH LPLIKMKPVP DLVPGNFKSQ 240 LQKVPPEWKA LTDMPQMRME LERPGGNEIT RGGSTSYGTG SETESPRNPS SAGSWNSGSS 300 GPGSTGNRNP GSSGTGGTAT WKPGSSGPGS TGSWNSGSSG TGSTGNQNPG SPRPGSTGTW 360 NPGSSERGSA GHWTSESSVS GSTGQWHSES GSFRPDSPGS GNARPNNPDW GTFEEVSGNV 420 SPGTRREYHT EKLVTSKGDK ELRTGKEKVT SGSTTTTRRS CSKTVTKTVI GPDGHKEVTK 480 EVVTSEDGSD CPEAMDLGTL SGIGTLDGFR HRHPDEAAFF DTASTGKTFP GFFSPMLGEF 540 VSETESRGSE SGIFTNTKES SSHHPGIAEF PSRGKSSSYS KQFTSSTSYN RGDSTFESKS 600 YKMADEAGSE ADHEGTHSTK RGHAKSRPVR DCDDVLQTHP SGTQSGIFNI KLPGSSKIFS 660 VYCDQETSLG GWLLIQQRMD GSLNFNRTWQ DYKRGFGSLN DEGEGEFWLG NDYLHLLTQR 720 GSVLRVELED WAGNEAYAEY HFRVGSEAEG YALQVSSYEG TAGDALIEGS VEEGAEYTSH 780 NNMQFSTFDR DADQWEENCA EVYGGGWWYN NCQAANLNGI YYPGGSYDPR NNSPYEIENG 840 VVWVSFRGAD YSLRAVRMKI RPLVTQ 867 |
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Database | Annotation |
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CTD (Curated) (count: 14) (view all) | MESH:D000347
; Afibrinogenemia MESH:D028226 ; Amyloidosis, Familial MESH:C538249 ; Amyloidosis, familial visceral MESH:D056486 ; Chemical and Drug Induced Liver Injury MESH:D002779 ; Cholestasis MESH:D064420 ; Drug-Related Side Effects and Adverse Reactions |
DisGeNet (Curated) (count: 36) (view all) | C0000786; Spontaneous abortion
C0001733; Afibrinogenemia C0008370; Cholestasis C0013604; Edema C0014591; Epistaxis C0015230; Exanthema |
HGMD (count: 87) (view all) | CD011165; Afibrinogenaemia; Small deletions
CD072418; Afibrinogenaemia; Small deletions CD044976; Fibrinogen variant; Small deletions CD013642; Dysfibrinogenaemia; Small deletions CD035514; Fibrinogen variant; Small deletions CD001896; Afibrinogenaemia; Small deletions |
GWASdb (count: 4) | rs6050; Fibrinogen; cardiovascular system disease
rs6050; Venous thromboembolism; vein disease rs6050; Venous thrombosis; Null rs2070016; Fibrinogen; cardiovascular system disease |
PTM | Modification Sites |
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Phosphorylation (count: 55) (view all) | 126 SANNRDNTYNRVSED dbPAF
127 ANNRDNTYNRVSEDL dbPAF 179 DIDIKIRSCRGSCSR dbPAF 185 RSCRGSCSRALAREV dbPAF 22 GTAWTADSGEGDFLA dbPAF 274 NEITRGGSTSYGTGS dbPAF |
Acetylation (count: 10) (view all) | 148 LKRKVIEKVQHIQLL PLMD
167 RAQLVDMKRLEVDID PLMD 195 LAREVDLKDYEDQQK PLMD 210 QLEQVIAKDLLPSRD PLMD 227 HLPLIKMKPVPDLVP PLMD 243 NFKSQLQKVPPEWKA PLMD |
Glycation (count: 30) (view all) | 100 FEYQKNNKDSHSLTT PLMD
144 RIEVLKRKVIEKVQH PLMD 148 LKRKVIEKVQHIQLL PLMD 157 QHIQLLQKNVRAQLV PLMD 167 RAQLVDMKRLEVDID PLMD 176 LEVDIDIKIRSCRGS PLMD |
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