Gene FGG - ENSG00000171557 | NCBI Gene ID: 2266

Details for: FGG

Gene ID: 2266

Symbol: FGG

Ensembl ID: ENSG00000171557

Description: fibrinogen gamma chain

Associated with

Adaptive immune system
(R-HSA-1280218)
Antigen processing-cross presentation
(R-HSA-1236975)
Class i mhc mediated antigen processing & presentation
(R-HSA-983169)
Common pathway of fibrin clot formation
(R-HSA-140875)
Disease
(R-HSA-1643685)
Diseases associated with the tlr signaling cascade
(R-HSA-5602358)
Diseases of immune system
(R-HSA-5260271)
Diseases of signal transduction by growth factor receptors and second messengers
(R-HSA-5663202)
Er-phagosome pathway
(R-HSA-1236974)
Extracellular matrix organization
(R-HSA-1474244)
Formation of fibrin clot (clotting cascade)
(R-HSA-140877)
Grb2:sos provides linkage to mapk signaling for integrins
(R-HSA-354194)
Hemostasis
(R-HSA-109582)
Immune system
(R-HSA-168256)
Innate immune system
(R-HSA-168249)
Integrin cell surface interactions
(R-HSA-216083)
Integrin signaling
(R-HSA-354192)
Irak4 deficiency (tlr2/4)
(R-HSA-5603041)
Map2k and mapk activation
(R-HSA-5674135)
Mapk1/mapk3 signaling
(R-HSA-5684996)
Mapk family signaling cascades
(R-HSA-5683057)
Metabolism of proteins
(R-HSA-392499)
Myd88 deficiency (tlr2/4)
(R-HSA-5602498)
Myd88:mal(tirap) cascade initiated on plasma membrane
(R-HSA-166058)
Oncogenic mapk signaling
(R-HSA-6802957)
P130cas linkage to mapk signaling for integrins
(R-HSA-372708)
Paradoxical activation of raf signaling by kinase inactive braf
(R-HSA-6802955)
Platelet activation, signaling and aggregation
(R-HSA-76002)
Platelet aggregation (plug formation)
(R-HSA-76009)
Platelet degranulation
(R-HSA-114608)
Post-translational protein modification
(R-HSA-597592)
Post-translational protein phosphorylation
(R-HSA-8957275)
Raf/map kinase cascade
(R-HSA-5673001)
Regulation of insulin-like growth factor (igf) transport and uptake by insulin-like growth factor binding proteins (igfbps)
(R-HSA-381426)
Regulation of tlr by endogenous ligand
(R-HSA-5686938)
Response to elevated platelet cytosolic ca2+
(R-HSA-76005)
Signaling by braf and raf1 fusions
(R-HSA-6802952)
Signaling by high-kinase activity braf mutants
(R-HSA-6802948)
Signaling by moderate kinase activity braf mutants
(R-HSA-6802946)
Signaling by raf1 mutants
(R-HSA-9656223)
Signaling by ras mutants
(R-HSA-6802949)
Signaling downstream of ras mutants
(R-HSA-9649948)
Signal transduction
(R-HSA-162582)
Toll-like receptor cascades
(R-HSA-168898)
Toll like receptor 2 (tlr2) cascade
(R-HSA-181438)
Toll like receptor 4 (tlr4) cascade
(R-HSA-166016)
Toll like receptor tlr1:tlr2 cascade
(R-HSA-168179)
Toll like receptor tlr6:tlr2 cascade
(R-HSA-168188)
Blood coagulation, fibrin clot formation
(GO:0072378)
Blood microparticle
(GO:0072562)
Cell-matrix adhesion
(GO:0007160)
Cell adhesion molecule binding
(GO:0050839)
Cell surface
(GO:0009986)
Cellular response to interleukin-1
(GO:0071347)
Cellular response to interleukin-6
(GO:0071354)
Collagen-containing extracellular matrix
(GO:0062023)
Endoplasmic reticulum lumen
(GO:0005788)
External side of plasma membrane
(GO:0009897)
Extracellular exosome
(GO:0070062)
Extracellular matrix structural constituent
(GO:0005201)
Extracellular region
(GO:0005576)
Extracellular space
(GO:0005615)
Fibrinogen complex
(GO:0005577)
Fibrinolysis
(GO:0042730)
Identical protein binding
(GO:0042802)
Metal ion binding
(GO:0046872)
Negative regulation of endothelial cell apoptotic process
(GO:2000352)
Negative regulation of extrinsic apoptotic signaling pathway via death domain receptors
(GO:1902042)
Plasma membrane
(GO:0005886)
Plasminogen activation
(GO:0031639)
Platelet aggregation
(GO:0070527)
Platelet alpha granule
(GO:0031091)
Platelet alpha granule lumen
(GO:0031093)
Platelet maturation
(GO:0036345)
Positive regulation of erk1 and erk2 cascade
(GO:0070374)
Positive regulation of exocytosis
(GO:0045921)
Positive regulation of heterotypic cell-cell adhesion
(GO:0034116)
Positive regulation of peptide hormone secretion
(GO:0090277)
Positive regulation of protein secretion
(GO:0050714)
Positive regulation of substrate adhesion-dependent cell spreading
(GO:1900026)
Positive regulation of vasoconstriction
(GO:0045907)
Protein-containing complex assembly
(GO:0065003)
Protein binding
(GO:0005515)
Protein polymerization
(GO:0051258)
Protein secretion
(GO:0009306)
Response to calcium ion
(GO:0051592)
Signaling receptor binding
(GO:0005102)
Structural molecule activity
(GO:0005198)

Cells (max top 100)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: hepatoblast (CL0005026)
Fold Change: 7.34
Marker Score: 24033
Cell Name: enterocyte of colon (CL1000347)
Fold Change: 5.21
Marker Score: 8024
Cell Name: periportal region hepatocyte (CL0019026)
Fold Change: 3.89
Marker Score: 20898
Cell Name: endothelial cell of pericentral hepatic sinusoid (CL0019022)
Fold Change: 2.61
Marker Score: 2798.5
Cell Name: midzonal region hepatocyte (CL0019028)
Fold Change: 2.36
Marker Score: 10190
Cell Name: centrilobular region hepatocyte (CL0019029)
Fold Change: 2.36
Marker Score: 15152
Cell Name: inflammatory macrophage (CL0000863)
Fold Change: 2.28
Marker Score: 708
Cell Name: hepatocyte (CL0000182)
Fold Change: 1.53
Marker Score: 1043
Cell Name: endothelial cell of periportal hepatic sinusoid (CL0019021)
Fold Change: 1.5
Marker Score: 414
Cell Name: Kupffer cell (CL0000091)
Fold Change: 1.48
Marker Score: 1478
Cell Name: transit amplifying cell of small intestine (CL0009012)
Fold Change: 1.47
Marker Score: 609
Cell Name: endothelial cell of hepatic sinusoid (CL1000398)
Fold Change: 1.2
Marker Score: 262
Cell Name: hepatic stellate cell (CL0000632)
Fold Change: 1.1
Marker Score: 416
Cell Name: neoplastic cell (CL0001063)
Fold Change: 1.1
Marker Score: 6638
Cell Name: goblet cell (CL0000160)
Fold Change: 1.09
Marker Score: 7243
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 0.99
Marker Score: 2526
Cell Name: absorptive cell (CL0000212)
Fold Change: 0.98
Marker Score: 30406
Cell Name: transit amplifying cell (CL0009010)
Fold Change: 0.94
Marker Score: 5345
Cell Name: abnormal cell (CL0001061)
Fold Change: 0.91
Marker Score: 2740
Cell Name: intestinal epithelial cell (CL0002563)
Fold Change: 0.87
Marker Score: 1410
Cell Name: stem cell (CL0000034)
Fold Change: 0.81
Marker Score: 1927
Cell Name: brush cell (CL0002204)
Fold Change: 0.77
Marker Score: 705
Cell Name: type II pneumocyte (CL0002063)
Fold Change: 0.76
Marker Score: 4924
Cell Name: pneumocyte (CL0000322)
Fold Change: 0.72
Marker Score: 1150
Cell Name: erythroblast (CL0000765)
Fold Change: 0.67
Marker Score: 419
Cell Name: malignant cell (CL0001064)
Fold Change: 0.65
Marker Score: 8753
Cell Name: alpha-beta T cell (CL0000789)
Fold Change: 0.58
Marker Score: 438
Cell Name: intestinal enteroendocrine cell (CL1001516)
Fold Change: 0.58
Marker Score: 460
Cell Name: mucosal invariant T cell (CL0000940)
Fold Change: 0.49
Marker Score: 438
Cell Name: macrophage (CL0000235)
Fold Change: 0.44
Marker Score: 491
Cell Name: intestine goblet cell (CL0019031)
Fold Change: 0.44
Marker Score: 420
Cell Name: mature NK T cell (CL0000814)
Fold Change: 0.4
Marker Score: 186
Cell Name: progenitor cell of endocrine pancreas (CL0002351)
Fold Change: 0.38
Marker Score: 83
Cell Name: cholangiocyte (CL1000488)
Fold Change: 0.35
Marker Score: 131
Cell Name: enterocyte (CL0000584)
Fold Change: 0.34
Marker Score: 1622
Cell Name: progenitor cell (CL0011026)
Fold Change: 0.33
Marker Score: 2130
Cell Name: vascular associated smooth muscle cell (CL0000359)
Fold Change: 0.29
Marker Score: 133.5
Cell Name: erythrocyte (CL0000232)
Fold Change: 0.28
Marker Score: 157
Cell Name: epithelial cell of exocrine pancreas (CL1001433)
Fold Change: 0.28
Marker Score: 158
Cell Name: regulatory T cell (CL0000815)
Fold Change: 0.27
Marker Score: 301
Cell Name: enteroendocrine cell (CL0000164)
Fold Change: 0.27
Marker Score: 140
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: 0.26
Marker Score: 270
Cell Name: lactocyte (CL0002325)
Fold Change: 0.26
Marker Score: 4165
Cell Name: pancreatic D cell (CL0000173)
Fold Change: 0.25
Marker Score: 108
Cell Name: kidney proximal convoluted tubule epithelial cell (CL1000838)
Fold Change: 0.25
Marker Score: 509.5
Cell Name: epithelial cell of alveolus of lung (CL0010003)
Fold Change: 0.24
Marker Score: 109
Cell Name: epithelial cell (CL0000066)
Fold Change: 0.23
Marker Score: 364
Cell Name: luminal epithelial cell of mammary gland (CL0002326)
Fold Change: 0.22
Marker Score: 398.5
Cell Name: gamma-delta T cell (CL0000798)
Fold Change: 0.22
Marker Score: 150
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: 0.22
Marker Score: 76
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.21
Marker Score: 443
Cell Name: ionocyte (CL0005006)
Fold Change: 0.21
Marker Score: 63
Cell Name: CD4-positive, alpha-beta T cell (CL0000624)
Fold Change: 0.19
Marker Score: 438
Cell Name: cardiac endothelial cell (CL0010008)
Fold Change: 0.19
Marker Score: 360
Cell Name: immature innate lymphoid cell (CL0001082)
Fold Change: 0.19
Marker Score: 386
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: 0.18
Marker Score: 84
Cell Name: pancreatic A cell (CL0000171)
Fold Change: 0.18
Marker Score: 177
Cell Name: endothelial cell (CL0000115)
Fold Change: 0.17
Marker Score: 151
Cell Name: CD8-positive, alpha-beta T cell (CL0000625)
Fold Change: 0.16
Marker Score: 257
Cell Name: M cell of gut (CL0000682)
Fold Change: 0.15
Marker Score: 40
Cell Name: type I enteroendocrine cell (CL0002277)
Fold Change: 0.15
Marker Score: 37
Cell Name: epithelial cell of lung (CL0000082)
Fold Change: 0.14
Marker Score: 762
Cell Name: innate lymphoid cell (CL0001065)
Fold Change: 0.14
Marker Score: 52
Cell Name: monocyte (CL0000576)
Fold Change: 0.14
Marker Score: 186
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: 0.13
Marker Score: 132
Cell Name: kidney distal convoluted tubule epithelial cell (CL1000849)
Fold Change: 0.13
Marker Score: 141
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 0.13
Marker Score: 2028
Cell Name: vein endothelial cell (CL0002543)
Fold Change: 0.13
Marker Score: 117
Cell Name: NKp44-negative group 3 innate lymphoid cell, human (CL0001080)
Fold Change: 0.13
Marker Score: 28
Cell Name: enteric neuron (CL0007011)
Fold Change: 0.13
Marker Score: 67
Cell Name: common myeloid progenitor (CL0000049)
Fold Change: 0.12
Marker Score: 33
Cell Name: neural crest cell (CL0011012)
Fold Change: 0.12
Marker Score: 133
Cell Name: CD16-negative, CD56-bright natural killer cell, human (CL0000938)
Fold Change: 0.12
Marker Score: 101
Cell Name: connective tissue cell (CL0002320)
Fold Change: 0.12
Marker Score: 31.5
Cell Name: cardiac mesenchymal cell (CL0000569)
Fold Change: 0.12
Marker Score: 29
Cell Name: B cell (CL0000236)
Fold Change: 0.12
Marker Score: 112
Cell Name: bronchial epithelial cell (CL0002328)
Fold Change: 0.12
Marker Score: 31
Cell Name: stromal cell (CL0000499)
Fold Change: 0.11
Marker Score: 133
Cell Name: fibroblast of cardiac tissue (CL0002548)
Fold Change: 0.11
Marker Score: 644
Cell Name: megakaryocyte (CL0000556)
Fold Change: 0.1
Marker Score: 58
Cell Name: lymphoid lineage restricted progenitor cell (CL0000838)
Fold Change: 0.1
Marker Score: 61
Cell Name: type L enteroendocrine cell (CL0002279)
Fold Change: 0.1
Marker Score: 27
Cell Name: muscle cell (CL0000187)
Fold Change: 0.1
Marker Score: 28
Cell Name: myeloid lineage restricted progenitor cell (CL0000839)
Fold Change: 0.1
Marker Score: 34
Cell Name: megakaryocyte-erythroid progenitor cell (CL0000050)
Fold Change: 0.1
Marker Score: 41
Cell Name: CD8-positive, alpha-beta memory T cell (CL0000909)
Fold Change: 0.1
Marker Score: 83
Cell Name: sympathetic neuron (CL0011103)
Fold Change: 0.1
Marker Score: 32
Cell Name: intestinal crypt stem cell of large intestine (CL0009016)
Fold Change: 0.1
Marker Score: 29
Cell Name: Schwann cell (CL0002573)
Fold Change: 0.1
Marker Score: 33
Cell Name: plasma cell (CL0000786)
Fold Change: 0.09
Marker Score: 106
Cell Name: mononuclear cell (CL0000842)
Fold Change: 0.09
Marker Score: 30
Cell Name: kidney capillary endothelial cell (CL1000892)
Fold Change: 0.09
Marker Score: 29
Cell Name: interstitial cell of Cajal (CL0002088)
Fold Change: 0.09
Marker Score: 32
Cell Name: mammary gland epithelial cell (CL0002327)
Fold Change: 0.09
Marker Score: 32
Cell Name: CD16-positive, CD56-dim natural killer cell, human (CL0000939)
Fold Change: 0.09
Marker Score: 69
Cell Name: PP cell (CL0000696)
Fold Change: 0.09
Marker Score: 20
Cell Name: common dendritic progenitor (CL0001029)
Fold Change: 0.09
Marker Score: 30
Cell Name: male germ cell (CL0000015)
Fold Change: 0.09
Marker Score: 25
Cell Name: mucus secreting cell (CL0000319)
Fold Change: 0.09
Marker Score: 22
Cell Name: natural killer cell (CL0000623)
Fold Change: 0.08
Marker Score: 110

Hover over a box to see details here...

**Key characteristics:** - Fibrinogen is a glycoprotein that is synthesized in the liver and secreted into the plasma. - It is a central protein in the blood clotting cascade, where it helps to form fibrin strands that cross-link to form a stable clot. - Fibrinogen is a multi-functional protein that also plays a role in cell adhesion, migration, and signaling. **Pathways and functions:** - Fibrinogen is produced by hepatocytes and is transported to the site of clot formation. - It binds to tissue factor, which is another protein that is involved in the clotting cascade. - The complex of fibrinogen and tissue factor is then converted into fibrinogen alpha, which is the active form of the protein. - Fibrinogen alpha polymerizes with fibrinogen beta to form fibrin strands. - These fibrin strands cross-link to form a stable clot. **Clinical significance:** - Mutations in the FGG gene can lead to a genetic disorder called von Willebrand disease. - In von Willebrand disease, the absence of fibrinogen leads to a deficiency of fibrinogen, which results in impaired blood clotting and an increased risk of bleeding. - Fibrinogen is also involved in other medical conditions, including liver disease, stroke, and cancer. **Additional information:** - The FGG gene is located on chromosome 15q26. - It is a highly conserved protein, with a similar sequence found in humans, mice, and rats. - Fibrinogen is a very important protein in blood clotting, and its dysfunction can lead to serious medical complications.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Fibrinogen gamma chain
A0A140VJJ6_HUMAN

Genular Protein ID: 84210600

Symbol: FIBG_HUMAN

Name: Fibrinogen gamma chain

UniProtKB Accession Codes:

P02679 A8K057 P04469 P04470 Q53Y18 Q96A14 Q96KJ3 Q9UC62 Q9UC63 Q9UCF3

Database IDs:

Citations:

PubMed ID: 6688357

Title: Characterization of a complementary deoxyribonucleic acid coding for the gamma chain of human fibrinogen.

PubMed ID: 6688357

DOI: 10.1021/bi00282a033

PubMed ID: 2990550

Title: Nucleotide sequence of the gene for the gamma chain of human fibrinogen.

PubMed ID: 2990550

DOI: 10.1021/bi00329a041

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8509453

Title: Evidence for the selective association of a subpopulation of GPIIb-IIIa with the actin cytoskeletons of thrombin-activated platelets.

PubMed ID: 8509453

DOI: 10.1083/jcb.121.6.1329

PubMed ID: 1685103

Title: Polymorphism of the human gamma chain fibrinogen gene.

PubMed ID: 1685103

DOI: 10.3109/10425179109020801

PubMed ID: 6689067

Title: Isolation and characterisation of cDNA clones for the A alpha- and gamma-chains of human fibrinogen.

PubMed ID: 6689067

DOI: 10.1093/nar/11.21.7427

PubMed ID: 6092346

Title: Structure of the human gamma-fibrinogen gene. Alternate mRNA splicing near the 3' end of the gene produces gamma A and gamma B forms of gamma-fibrinogen.

PubMed ID: 6092346

DOI: 10.1016/s0021-9258(18)90821-5

PubMed ID: 7654933

Title: Abnormal polymerization and normal binding of plasminogen and t-PA in three new dysfibrinogenaemias: Barcelona III and IV (gamma Arg 275-->His) and Villajoyosa (gamma Arg 275-->Cys).

PubMed ID: 7654933

DOI: 10.1097/00001721-199505000-00002

PubMed ID: 7306501

Title: Carboxy-terminal amino acid sequence of a human fibrinogen gamma-chain variant (gamma').

PubMed ID: 7306501

DOI: 10.1021/bi00524a036

PubMed ID: 6575689

Title: Covalent structure of fibrinogen.

PubMed ID: 6575689

DOI: 10.1111/j.1749-6632.1983.tb23232.x

PubMed ID: 936108

Title: Disulfide bridges in NH2-terminal part of human fibrinogen.

PubMed ID: 936108

DOI: 10.1016/0049-3848(76)90245-0

PubMed ID: 6860649

Title: Dimeric half-molecules of human fibrinogen are joined through disulfide bonds in an antiparallel orientation.

PubMed ID: 6860649

DOI: 10.1021/bi00278a003

PubMed ID: 1892842

Title: Recombinant human fibrinogen and sulfation of the gamma' chain.

PubMed ID: 1892842

DOI: 10.1021/bi00103a004

PubMed ID: 11307817

Title: The amino acid sequence in fibrin responsible for high affinity thrombin binding.

PubMed ID: 11307817

PubMed ID: 6383194

Title: Fibrinogen and fibrin.

PubMed ID: 6383194

DOI: 10.1146/annurev.bi.53.070184.001211

PubMed ID: 6592597

Title: Localization of a fibrin gamma-chain polymerization site within segment Thr-374 to Glu-396 of human fibrinogen.

PubMed ID: 6592597

DOI: 10.1073/pnas.81.19.5980

PubMed ID: 6451630

Title: Localization of a fibrin polymerization site.

PubMed ID: 6451630

DOI: 10.1016/s0021-9258(19)69643-2

PubMed ID: 6326808

Title: Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the gamma chain.

PubMed ID: 6326808

DOI: 10.1021/bi00303a028

PubMed ID: 6325435

Title: Evidence that three adhesive proteins interact with a common recognition site on activated platelets.

PubMed ID: 6325435

DOI: 10.1016/s0021-9258(18)91019-7

PubMed ID: 3160702

Title: Localization of a fibrinogen calcium binding site between gamma-subunit positions 311 and 336 by terbium fluorescence.

PubMed ID: 3160702

DOI: 10.1016/s0021-9258(17)39297-9

PubMed ID: 6933547

Title: Human plasma fibrinogen heterogeneity: evidence for an extended carboxyl-terminal sequence in a normal gamma chain variant (gamma').

PubMed ID: 6933547

DOI: 10.1073/pnas.77.9.5069

PubMed ID: 14760718

Title: Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.

PubMed ID: 14760718

DOI: 10.1002/pmic.200300556

PubMed ID: 16335952

Title: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.

PubMed ID: 16335952

DOI: 10.1021/pr0502065

PubMed ID: 16263699

Title: Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.

PubMed ID: 16263699

DOI: 10.1074/mcp.m500324-mcp200

PubMed ID: 18780401

Title: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.

PubMed ID: 18780401

DOI: 10.1002/pmic.200701057

PubMed ID: 19159218

Title: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.

PubMed ID: 19159218

DOI: 10.1021/pr8008012

PubMed ID: 19139490

Title: A strategy for precise and large scale identification of core fucosylated glycoproteins.

PubMed ID: 19139490

DOI: 10.1074/mcp.m800504-mcp200

PubMed ID: 2143188

Title: A unique proteolytic fragment of human fibrinogen containing the A alpha COOH-terminal domain of the native molecule.

PubMed ID: 2143188

DOI: 10.1016/s0021-9258(18)77401-2

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 26091039

Title: A single kinase generates the majority of the secreted phosphoproteome.

PubMed ID: 26091039

DOI: 10.1016/j.cell.2015.05.028

PubMed ID: 9016719

Title: Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen.

PubMed ID: 9016719

DOI: 10.1016/s0969-2126(97)00171-8

PubMed ID: 9207064

Title: The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro.

PubMed ID: 9207064

DOI: 10.1073/pnas.94.14.7176

PubMed ID: 9333233

Title: Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin.

PubMed ID: 9333233

DOI: 10.1038/38947

PubMed ID: 9628725

Title: Crystal structure of fragment double-D from human fibrin with two different bound ligands.

PubMed ID: 9628725

DOI: 10.1021/bi9804129

PubMed ID: 10074346

Title: Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide.

PubMed ID: 10074346

DOI: 10.1021/bi982626w

PubMed ID: 19296670

Title: Crystal structure of human fibrinogen.

PubMed ID: 19296670

DOI: 10.1021/bi802205g

PubMed ID: 2496144

Title: A gamma methionine-310 to threonine substitution and consequent N-glycosylation at gamma asparagine-308 identified in a congenital dysfibrinogenemia associated with posttraumatic bleeding, fibrinogen Asahi.

PubMed ID: 2496144

DOI: 10.1172/jci114056

PubMed ID: 1421174

Title: Gene analyses of abnormal fibrinogens with a mutation in the gamma chain.

PubMed ID: 1421174

PubMed ID: 2257302

Title: Fibrinogen Baltimore I: polymerization defect associated with a gamma 292Gly-->Val (GGC-->GTC) mutation.

PubMed ID: 2257302

PubMed ID: 2328317

Title: Polymerization defect of fibrinogen Baltimore III due to a gamma Asn308-->Ile mutation.

PubMed ID: 2328317

PubMed ID: 8400260

Title: Fibrinogen Bern I: substitution gamma 337 Asn-->Lys is responsible for defective fibrin monomer polymerization.

PubMed ID: 8400260

PubMed ID: 2971046

Title: Characterization of an apparently lower molecular weight gamma-chain variant in fibrinogen Kyoto I. The replacement of gamma-asparagine 308 by lysine which causes accelerated cleavage of fragment D1 by plasmin and the generation of a new plasmin cleavage site.

PubMed ID: 2971046

DOI: 10.1016/s0021-9258(18)68321-8

PubMed ID: 2819242

Title: Fibrinogen Kyoto III: a congenital dysfibrinogen with a gamma aspartic acid-330 to tyrosine substitution manifesting impaired fibrin monomer polymerization.

PubMed ID: 2819242

PubMed ID: 3708159

Title: Characterization of fibrinogen Milano I: amino acid exchange gamma 330 Asp-->Val impairs fibrin polymerization.

PubMed ID: 3708159

PubMed ID: 7841300

Title: Fibrinogen Milano V: a congenital dysfibrinogenaemia with a gamma 275 Arg-->Cys substitution.

PubMed ID: 7841300

PubMed ID: 8080993

Title: A new substitution, gamma 358 Ser-->Cys, in fibrinogen Milano VII causes defective fibrin polymerization.

PubMed ID: 8080993

PubMed ID: 2738036

Title: Fibrinogen Nagoya, a replacement of glutamine-329 by arginine in the gamma-chain that impairs the polymerization of fibrin monomer.

PubMed ID: 2738036

DOI: 10.1093/oxfordjournals.jbchem.a122601

PubMed ID: 2971042

Title: Substitution of gamma Arg-275 by Cys in an abnormal fibrinogen, 'fibrinogen Osaka II'. Evidence for a unique solitary cystine structure at the mutation site.

PubMed ID: 2971042

DOI: 10.1016/s0021-9258(18)68281-x

PubMed ID: 1455400

Title: Heterozygous abnormal fibrinogen Osaka III with the replacement of gamma arginine-275 by histidine has an apparently higher molecular weight gamma-chain variant.

PubMed ID: 1455400

PubMed ID: 1733971

Title: Characterization of an abnormal fibrinogen Osaka V with the replacement of gamma-arginine 375 by glycine. The lack of high affinity calcium binding to D-domains and the lack of protective effect of calcium on fibrinolysis.

PubMed ID: 1733971

DOI: 10.1016/s0021-9258(18)45943-1

PubMed ID: 8470043

Title: Paris I dysfibrinogenemia: a point mutation in intron 8 results in insertion of a 15 amino acid sequence in the fibrinogen gamma-chain.

PubMed ID: 8470043

PubMed ID: 3337908

Title: An apparently higher molecular weight gamma-chain variant in a new congenital abnormal fibrinogen Tochigi characterized by the replacement of gamma arginine-275 by cysteine.

PubMed ID: 3337908

PubMed ID: 2071611

Title: A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the gamma-chain gene, causing defective calcium binding and impaired fibrin polymerization.

PubMed ID: 2071611

DOI: 10.1016/s0021-9258(18)98861-7

PubMed ID: 3563970

Title: Three abnormal fibrinogen variants with the same amino acid substitution (gamma 275 Arg-->His): fibrinogens Bergamo II, Essen and Perugia.

PubMed ID: 3563970

PubMed ID: 2976995

Title: Normal plasmic cleavage of the gamma-chain variant of 'fibrinogen Saga' with an Arg-275 to His substitution.

PubMed ID: 2976995

PubMed ID: 11435303

Title: Fibrinogen Milano XII: a dysfunctional variant containing 2 amino acid substitutions, A-alpha R16C and gamma G165R.

PubMed ID: 11435303

DOI: 10.1182/blood.v98.2.351

PubMed ID: 10391209

Title: Characterization of single-nucleotide polymorphisms in coding regions of human genes.

PubMed ID: 10391209

DOI: 10.1038/10290

PubMed ID: 11986213

Title: Fibrinogen Hillsborough: a novel gamma-gly309asp dysfibrinogen with impaired clotting.

PubMed ID: 11986213

DOI: 10.1182/blood.v99.10.3597

PubMed ID: 15632207

Title: Fibrinogen Philadelphia, a hypodysfibrinogenemia characterized by abnormal polymerization and fibrinogen hypercatabolism due to gamma S378P mutation.

PubMed ID: 15632207

DOI: 10.1182/blood-2004-04-1621

PubMed ID: 25427968

Title: Clinical and molecular characterisation of 21 patients affected by quantitative fibrinogen deficiency.

PubMed ID: 25427968

DOI: 10.1160/th14-07-0629

Sequence Information:

Length: 453
Mass: 51512
Checksum: 1787204904E0D4BB
Sequence:

MSWSLHPRNL ILYFYALLFL SSTCVAYVAT RDNCCILDER FGSYCPTTCG IADFLSTYQT 
KVDKDLQSLE DILHQVENKT SEVKQLIKAI QLTYNPDESS KPNMIDAATL KSRKMLEEIM 
KYEASILTHD SSIRYLQEIY NSNNQKIVNL KEKVAQLEAQ CQEPCKDTVQ IHDITGKDCQ 
DIANKGAKQS GLYFIKPLKA NQQFLVYCEI DGSGNGWTVF QKRLDGSVDF KKNWIQYKEG 
FGHLSPTGTT EFWLGNEKIH LISTQSAIPY ALRVELEDWN GRTSTADYAM FKVGPEADKY 
RLTYAYFAGG DAGDAFDGFD FGDDPSDKFF TSHNGMQFST WDNDNDKFEG NCAEQDGSGW 
WMNKCHAGHL NGVYYQGGTY SKASTPNGYD NGIIWATWKT RWYSMKKTTM KIIPFNRLTI 
GEGQQHHLGG AKQVRPEHPA ETEYDSLYPE DDL

Genular Protein ID: 3010825293

Symbol: A0A140VJJ6_HUMAN

Name: N/A

UniProtKB Accession Codes:

A0A140VJJ6

Database IDs:

Sequence Information:

Length: 437
Mass: 49497
Checksum: 3D73A7BC1E71381B
Sequence:

MSWSLHPRNL ILYFYALLFL SSTCVAYVAT RDNCCILDER FGSYCPTTCG IADFLSTYQT 
KVDKDLQSLE DILHQVENKT SEVKQLIKAI QLTYNPDESS KPNMIDAATL KSRKMLEEIM 
KYEASILTHD SSIRYLQEIY NSNNQKIVNL KEKVAQLEAQ CQEPCKDTVQ IHDITGKDCQ 
DIANKGAKQS GLYFIKPLKA NQQFLVYCEI DGSGNGWTVF QKRLDGSVDF KKNWIQYKEG 
FGHLSPTGTT EFWLGNEKIH LISTQSAIPY ALRVELEDWN GRTSTADYAM FKVGPEADKY 
RLTYAYFAGG DAGDAFDGFD FGDDPSDKFF TSHNGMQFST WDNDNDKFEG NCAEQDGSGW 
WMNKCHAGHL NGVYYQGGTY SKASTPNGYD NGIIWATWKT RWYSMKKTTM KIIPFNRLTI 
GEGQQHHLGG AKQAGDV

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. For the full schema, download it here.

Details for: FGG

Associated with

Cells (max top 100)

Other Information

Characterization of a complementary deoxyribonucleic acid coding for the gamma chain of human fibrinogen. PubMed ID: 6688357

Nucleotide sequence of the gene for the gamma chain of human fibrinogen. PubMed ID: 2990550

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Evidence for the selective association of a subpopulation of GPIIb-IIIa with the actin cytoskeletons of thrombin-activated platelets. PubMed ID: 8509453

Polymorphism of the human gamma chain fibrinogen gene. PubMed ID: 1685103

Isolation and characterisation of cDNA clones for the A alpha- and gamma-chains of human fibrinogen. PubMed ID: 6689067

Structure of the human gamma-fibrinogen gene. Alternate mRNA splicing near the 3' end of the gene produces gamma A and gamma B forms of gamma-fibrinogen. PubMed ID: 6092346

Abnormal polymerization and normal binding of plasminogen and t-PA in three new dysfibrinogenaemias: Barcelona III and IV (gamma Arg 275--&gt;His) and Villajoyosa (gamma Arg 275--&gt;Cys). PubMed ID: 7654933

Carboxy-terminal amino acid sequence of a human fibrinogen gamma-chain variant (gamma'). PubMed ID: 7306501

Covalent structure of fibrinogen. PubMed ID: 6575689

Disulfide bridges in NH2-terminal part of human fibrinogen. PubMed ID: 936108

Dimeric half-molecules of human fibrinogen are joined through disulfide bonds in an antiparallel orientation. PubMed ID: 6860649

Recombinant human fibrinogen and sulfation of the gamma' chain. PubMed ID: 1892842

The amino acid sequence in fibrin responsible for high affinity thrombin binding. PubMed ID: 11307817

Fibrinogen and fibrin. PubMed ID: 6383194

Localization of a fibrin gamma-chain polymerization site within segment Thr-374 to Glu-396 of human fibrinogen. PubMed ID: 6592597

Localization of a fibrin polymerization site. PubMed ID: 6451630

Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the gamma chain. PubMed ID: 6326808

Evidence that three adhesive proteins interact with a common recognition site on activated platelets. PubMed ID: 6325435

Localization of a fibrinogen calcium binding site between gamma-subunit positions 311 and 336 by terbium fluorescence. PubMed ID: 3160702

Human plasma fibrinogen heterogeneity: evidence for an extended carboxyl-terminal sequence in a normal gamma chain variant (gamma'). PubMed ID: 6933547

Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. PubMed ID: 14760718

Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. PubMed ID: 16335952

Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. PubMed ID: 16263699

Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. PubMed ID: 18780401

Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. PubMed ID: 19159218

A strategy for precise and large scale identification of core fucosylated glycoproteins. PubMed ID: 19139490

A unique proteolytic fragment of human fibrinogen containing the A alpha COOH-terminal domain of the native molecule. PubMed ID: 2143188

Initial characterization of the human central proteome. PubMed ID: 21269460

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

A single kinase generates the majority of the secreted phosphoproteome. PubMed ID: 26091039

Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen. PubMed ID: 9016719

The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro. PubMed ID: 9207064

Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. PubMed ID: 9333233

Crystal structure of fragment double-D from human fibrin with two different bound ligands. PubMed ID: 9628725

Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide. PubMed ID: 10074346

Crystal structure of human fibrinogen. PubMed ID: 19296670

A gamma methionine-310 to threonine substitution and consequent N-glycosylation at gamma asparagine-308 identified in a congenital dysfibrinogenemia associated with posttraumatic bleeding, fibrinogen Asahi. PubMed ID: 2496144

Gene analyses of abnormal fibrinogens with a mutation in the gamma chain. PubMed ID: 1421174

Fibrinogen Baltimore I: polymerization defect associated with a gamma 292Gly--&gt;Val (GGC--&gt;GTC) mutation. PubMed ID: 2257302

Polymerization defect of fibrinogen Baltimore III due to a gamma Asn308--&gt;Ile mutation. PubMed ID: 2328317

Fibrinogen Bern I: substitution gamma 337 Asn--&gt;Lys is responsible for defective fibrin monomer polymerization. PubMed ID: 8400260

Characterization of an apparently lower molecular weight gamma-chain variant in fibrinogen Kyoto I. The replacement of gamma-asparagine 308 by lysine which causes accelerated cleavage of fragment D1 by plasmin and the generation of a new plasmin cleavage site. PubMed ID: 2971046

Fibrinogen Kyoto III: a congenital dysfibrinogen with a gamma aspartic acid-330 to tyrosine substitution manifesting impaired fibrin monomer polymerization. PubMed ID: 2819242

Characterization of fibrinogen Milano I: amino acid exchange gamma 330 Asp--&gt;Val impairs fibrin polymerization. PubMed ID: 3708159

Fibrinogen Milano V: a congenital dysfibrinogenaemia with a gamma 275 Arg--&gt;Cys substitution. PubMed ID: 7841300

A new substitution, gamma 358 Ser--&gt;Cys, in fibrinogen Milano VII causes defective fibrin polymerization. PubMed ID: 8080993

Fibrinogen Nagoya, a replacement of glutamine-329 by arginine in the gamma-chain that impairs the polymerization of fibrin monomer. PubMed ID: 2738036

Substitution of gamma Arg-275 by Cys in an abnormal fibrinogen, 'fibrinogen Osaka II'. Evidence for a unique solitary cystine structure at the mutation site. PubMed ID: 2971042

Heterozygous abnormal fibrinogen Osaka III with the replacement of gamma arginine-275 by histidine has an apparently higher molecular weight gamma-chain variant. PubMed ID: 1455400

Characterization of an abnormal fibrinogen Osaka V with the replacement of gamma-arginine 375 by glycine. The lack of high affinity calcium binding to D-domains and the lack of protective effect of calcium on fibrinolysis. PubMed ID: 1733971

Paris I dysfibrinogenemia: a point mutation in intron 8 results in insertion of a 15 amino acid sequence in the fibrinogen gamma-chain. PubMed ID: 8470043

An apparently higher molecular weight gamma-chain variant in a new congenital abnormal fibrinogen Tochigi characterized by the replacement of gamma arginine-275 by cysteine. PubMed ID: 3337908

A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the gamma-chain gene, causing defective calcium binding and impaired fibrin polymerization. PubMed ID: 2071611

Three abnormal fibrinogen variants with the same amino acid substitution (gamma 275 Arg--&gt;His): fibrinogens Bergamo II, Essen and Perugia. PubMed ID: 3563970

Normal plasmic cleavage of the gamma-chain variant of 'fibrinogen Saga' with an Arg-275 to His substitution. PubMed ID: 2976995

Fibrinogen Milano XII: a dysfunctional variant containing 2 amino acid substitutions, A-alpha R16C and gamma G165R. PubMed ID: 11435303

Characterization of single-nucleotide polymorphisms in coding regions of human genes. PubMed ID: 10391209

Fibrinogen Hillsborough: a novel gamma-gly309asp dysfibrinogen with impaired clotting. PubMed ID: 11986213

Fibrinogen Philadelphia, a hypodysfibrinogenemia characterized by abnormal polymerization and fibrinogen hypercatabolism due to gamma S378P mutation. PubMed ID: 15632207

Clinical and molecular characterisation of 21 patients affected by quantitative fibrinogen deficiency. PubMed ID: 25427968