Search Results
Overview
| Uniprot ID | P02679 |
|---|---|
| Protein Name | Fibrinogen gamma chain |
| Gene Name | FGG |
| Organism | Homo 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
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.