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Overview

Uniprot IDP02679
Protein NameFibrinogen gamma chain
Gene NameFGG
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
146 IYNSNNQKIVNLKEK
151 NQKIVNLKEKVAQLE
153 KIVNLKEKVAQLEAQ
166 AQCQEPCKDTVQIHD
177 QIHDITGKDCQDIAN
185 DCQDIANKGAKQSGL
188 DIANKGAKQSGLYFI
196 QSGLYFIKPLKANQQ
231 LDGSVDFKKNWIQYK
232 DGSVDFKKNWIQYKE
299 KVGPEADKYRLTYAY
84 ENKTSEVKQLIKAIQ

Function

Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. 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 antibacterial immune response via both innate and T-cell mediated pathways

Protein Sequence

10 MSWSLHPRNL 20 ILYFYALLFL 30 SSTCVAYVAT 40 RDNCCILDER 50 FGSYCPTTCG 60 IADFLSTYQT 70 KVDKDLQSLE 80 DILHQVENKT 90 SEVKQLIKAI 100 QLTYNPDESS 110 KPNMIDAATL 120 KSRKMLEEIM 130 KYEASILTHD 140 SSIRYLQEIY 150 NSNNQKIVNL 160 KEKVAQLEAQ 170 CQEPCKDTVQ 180 IHDITGKDCQ 190 DIANKGAKQS 200 GLYFIKPLKA 210 NQQFLVYCEI 220 DGSGNGWTVF 230 QKRLDGSVDF 240 KKNWIQYKEG 250 FGHLSPTGTT 260 EFWLGNEKIH 270 LISTQSAIPY 280 ALRVELEDWN 290 GRTSTADYAM 300 FKVGPEADKY 310 RLTYAYFAGG 320 DAGDAFDGFD 330 FGDDPSDKFF 340 TSHNGMQFST 350 WDNDNDKFEG 360 NCAEQDGSGW 370 WMNKCHAGHL 380 NGVYYQGGTY 390 SKASTPNGYD 400 NGIIWATWKT 410 RWYSMKKTTM 420 KIIPFNRLTI 430 GEGQQHHLGG 440 AKQVRPEHPA 450 ETEYDSLYPE DDL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0072562 blood microparticle
Cellular Component GO:0009986 cell surface
Cellular Component GO:0005788 endoplasmic reticulum lumen
Cellular Component GO:0009897 external side of plasma membrane
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0031012 extracellular matrix
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0005577 fibrinogen complex
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0031091 platelet alpha granule
Cellular Component GO:0031093 platelet alpha granule lumen
Molecular Function GO:0050839 cell adhesion molecule binding
Molecular Function GO:0005201 extracellular matrix structural constituent
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0005102 signaling receptor binding
Molecular Function GO:0005198 structural molecule activity
Biological Process GO:0072378 blood coagulation, fibrin clot formation
Biological Process GO:0007160 cell-matrix adhesion
Biological Process GO:0042730 fibrinolysis
Biological Process GO:2000352 negative regulation of endothelial cell apoptotic process
Biological Process GO:1902042 negative regulation of extrinsic apoptotic signaling pathway via death domain receptors
Biological Process GO:0031639 plasminogen activation
Biological Process GO:0070527 platelet aggregation
Biological Process GO:0070374 positive regulation of ERK1 and ERK2 cascade
Biological Process GO:0045921 positive regulation of exocytosis
Biological Process GO:0034116 positive regulation of heterotypic cell-cell adhesion
Biological Process GO:0090277 positive regulation of peptide hormone secretion
Biological Process GO:0050714 positive regulation of protein secretion
Biological Process GO:1900026 positive regulation of substrate adhesion-dependent cell spreading
Biological Process GO:0045907 positive regulation of vasoconstriction
Biological Process GO:0051258 protein polymerization
Biological Process GO:0009306 protein secretion
Biological Process GO:0065003 protein-containing complex assembly
Biological Process GO:0051592 response to calcium ion

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.