Gene FGA - ENSG00000171560 | NCBI Gene ID: 2243

Details for: FGA

Gene ID: 2243

Symbol: FGA

Ensembl ID: ENSG00000171560

Description: fibrinogen alpha chain

Associated with

Adaptive immune system
(R-HSA-1280218)
Amyloid fiber formation
(R-HSA-977225)
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)
Adaptive immune response
(GO:0002250)
Blood coagulation, common pathway
(GO:0072377)
Blood coagulation, fibrin clot formation
(GO:0072378)
Cell-matrix adhesion
(GO:0007160)
Cell adhesion molecule binding
(GO:0050839)
Cell surface
(GO:0009986)
Endoplasmic reticulum
(GO:0005783)
Endoplasmic reticulum lumen
(GO:0005788)
External side of plasma membrane
(GO:0009897)
Extracellular matrix structural constituent
(GO:0005201)
Extracellular region
(GO:0005576)
Extracellular space
(GO:0005615)
Fibrinogen complex
(GO:0005577)
Fibrinolysis
(GO:0042730)
Induction of bacterial agglutination
(GO:0043152)
Innate immune response
(GO:0045087)
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)
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)
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: 9.51
Marker Score: 31147
Cell Name: periportal region hepatocyte (CL0019026)
Fold Change: 3.95
Marker Score: 21240
Cell Name: enterocyte of colon (CL1000347)
Fold Change: 2.67
Marker Score: 4109
Cell Name: endothelial cell of pericentral hepatic sinusoid (CL0019022)
Fold Change: 2.53
Marker Score: 2707
Cell Name: centrilobular region hepatocyte (CL0019029)
Fold Change: 2.37
Marker Score: 15220
Cell Name: inflammatory macrophage (CL0000863)
Fold Change: 2.36
Marker Score: 733
Cell Name: midzonal region hepatocyte (CL0019028)
Fold Change: 2.35
Marker Score: 10160
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 2
Marker Score: 1997
Cell Name: erythroblast (CL0000765)
Fold Change: 1.92
Marker Score: 1201
Cell Name: endothelial cell of periportal hepatic sinusoid (CL0019021)
Fold Change: 1.65
Marker Score: 453.5
Cell Name: colon goblet cell (CL0009039)
Fold Change: 1.61
Marker Score: 1172
Cell Name: Kupffer cell (CL0000091)
Fold Change: 1.51
Marker Score: 1509
Cell Name: endothelial cell of hepatic sinusoid (CL1000398)
Fold Change: 1.37
Marker Score: 301
Cell Name: hepatocyte (CL0000182)
Fold Change: 1.34
Marker Score: 914
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 1.15
Marker Score: 4817
Cell Name: hepatic stellate cell (CL0000632)
Fold Change: 1.13
Marker Score: 427
Cell Name: goblet cell (CL0000160)
Fold Change: 1.07
Marker Score: 7139
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: 1
Marker Score: 678
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.99
Marker Score: 510
Cell Name: absorptive cell (CL0000212)
Fold Change: 0.98
Marker Score: 30408
Cell Name: BEST4+ intestinal epithelial cell, human (CL4030026)
Fold Change: 0.98
Marker Score: 463
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 0.95
Marker Score: 2412
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.94
Marker Score: 376
Cell Name: transit amplifying cell (CL0009010)
Fold Change: 0.94
Marker Score: 5349
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: 0.92
Marker Score: 423
Cell Name: abnormal cell (CL0001061)
Fold Change: 0.92
Marker Score: 2741
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.91
Marker Score: 328
Cell Name: transit amplifying cell of small intestine (CL0009012)
Fold Change: 0.9
Marker Score: 374.5
Cell Name: neoplastic cell (CL0001063)
Fold Change: 0.87
Marker Score: 5296
Cell Name: intestinal epithelial cell (CL0002563)
Fold Change: 0.78
Marker Score: 1269
Cell Name: brush cell (CL0002204)
Fold Change: 0.78
Marker Score: 710
Cell Name: alpha-beta T cell (CL0000789)
Fold Change: 0.62
Marker Score: 467
Cell Name: gut absorptive cell (CL0000677)
Fold Change: 0.61
Marker Score: 391
Cell Name: mucosal invariant T cell (CL0000940)
Fold Change: 0.59
Marker Score: 521
Cell Name: intestinal enteroendocrine cell (CL1001516)
Fold Change: 0.57
Marker Score: 457
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: 0.56
Marker Score: 176
Cell Name: malignant cell (CL0001064)
Fold Change: 0.52
Marker Score: 7039
Cell Name: cholangiocyte (CL1000488)
Fold Change: 0.48
Marker Score: 180
Cell Name: pneumocyte (CL0000322)
Fold Change: 0.44
Marker Score: 702
Cell Name: mature NK T cell (CL0000814)
Fold Change: 0.43
Marker Score: 197
Cell Name: B cell (CL0000236)
Fold Change: 0.4
Marker Score: 382
Cell Name: kidney proximal convoluted tubule epithelial cell (CL1000838)
Fold Change: 0.38
Marker Score: 778.5
Cell Name: erythrocyte (CL0000232)
Fold Change: 0.35
Marker Score: 194
Cell Name: pancreatic D cell (CL0000173)
Fold Change: 0.32
Marker Score: 137
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: 0.29
Marker Score: 303
Cell Name: type II pneumocyte (CL0002063)
Fold Change: 0.28
Marker Score: 1851
Cell Name: cardiac endothelial cell (CL0010008)
Fold Change: 0.25
Marker Score: 476
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: 0.25
Marker Score: 85
Cell Name: plasma cell (CL0000786)
Fold Change: 0.24
Marker Score: 270
Cell Name: gamma-delta T cell (CL0000798)
Fold Change: 0.24
Marker Score: 160
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: 0.23
Marker Score: 66
Cell Name: CD8-positive, alpha-beta T cell (CL0000625)
Fold Change: 0.23
Marker Score: 376
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.22
Marker Score: 76
Cell Name: ciliated epithelial cell (CL0000067)
Fold Change: 0.22
Marker Score: 102
Cell Name: macrophage (CL0000235)
Fold Change: 0.22
Marker Score: 243
Cell Name: immature innate lymphoid cell (CL0001082)
Fold Change: 0.21
Marker Score: 435
Cell Name: myeloid cell (CL0000763)
Fold Change: 0.21
Marker Score: 337
Cell Name: secretory cell (CL0000151)
Fold Change: 0.2
Marker Score: 374
Cell Name: regulatory T cell (CL0000815)
Fold Change: 0.2
Marker Score: 220
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: 0.18
Marker Score: 183
Cell Name: pancreatic A cell (CL0000171)
Fold Change: 0.18
Marker Score: 180
Cell Name: endothelial cell (CL0000115)
Fold Change: 0.18
Marker Score: 162
Cell Name: parietal epithelial cell (CL1000452)
Fold Change: 0.18
Marker Score: 65
Cell Name: innate lymphoid cell (CL0001065)
Fold Change: 0.18
Marker Score: 64
Cell Name: intestine goblet cell (CL0019031)
Fold Change: 0.18
Marker Score: 169
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.17
Marker Score: 43
Cell Name: mast cell (CL0000097)
Fold Change: 0.15
Marker Score: 88
Cell Name: endothelial cell of vascular tree (CL0002139)
Fold Change: 0.15
Marker Score: 213
Cell Name: epithelial cell (CL0000066)
Fold Change: 0.14
Marker Score: 228
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 0.14
Marker Score: 2233
Cell Name: progenitor cell of endocrine pancreas (CL0002351)
Fold Change: 0.14
Marker Score: 31
Cell Name: lymphoid lineage restricted progenitor cell (CL0000838)
Fold Change: 0.14
Marker Score: 85
Cell Name: vascular associated smooth muscle cell (CL0000359)
Fold Change: 0.14
Marker Score: 64.5
Cell Name: megakaryocyte (CL0000556)
Fold Change: 0.14
Marker Score: 79
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.14
Marker Score: 286
Cell Name: luminal epithelial cell of mammary gland (CL0002326)
Fold Change: 0.13
Marker Score: 237
Cell Name: progenitor cell (CL0011026)
Fold Change: 0.13
Marker Score: 853
Cell Name: fibroblast of cardiac tissue (CL0002548)
Fold Change: 0.13
Marker Score: 767
Cell Name: kidney distal convoluted tubule epithelial cell (CL1000849)
Fold Change: 0.13
Marker Score: 135
Cell Name: blood vessel endothelial cell (CL0000071)
Fold Change: 0.12
Marker Score: 125.5
Cell Name: Unknown (CL0000003)
Fold Change: 0.12
Marker Score: 378
Cell Name: parietal cell (CL0000162)
Fold Change: 0.12
Marker Score: 34
Cell Name: megakaryocyte-erythroid progenitor cell (CL0000050)
Fold Change: 0.12
Marker Score: 50
Cell Name: CD8-positive, alpha-beta memory T cell (CL0000909)
Fold Change: 0.12
Marker Score: 99
Cell Name: CD16-negative, CD56-bright natural killer cell, human (CL0000938)
Fold Change: 0.11
Marker Score: 94
Cell Name: astrocyte (CL0000127)
Fold Change: 0.11
Marker Score: 98
Cell Name: kidney proximal straight tubule epithelial cell (CL1000839)
Fold Change: 0.11
Marker Score: 260.5
Cell Name: CD4-positive, alpha-beta T cell (CL0000624)
Fold Change: 0.11
Marker Score: 241
Cell Name: enteroendocrine cell (CL0000164)
Fold Change: 0.1
Marker Score: 54
Cell Name: ciliated cell (CL0000064)
Fold Change: 0.1
Marker Score: 352.5
Cell Name: PP cell (CL0000696)
Fold Change: 0.1
Marker Score: 23
Cell Name: myofibroblast cell (CL0000186)
Fold Change: 0.1
Marker Score: 126
Cell Name: pericyte (CL0000669)
Fold Change: 0.1
Marker Score: 57
Cell Name: multi-ciliated epithelial cell (CL0005012)
Fold Change: 0.1
Marker Score: 185
Cell Name: smooth muscle myoblast (CL0000514)
Fold Change: 0.09
Marker Score: 45
Cell Name: fibroblast (CL0000057)
Fold Change: 0.09
Marker Score: 91
Cell Name: hematopoietic stem cell (CL0000037)
Fold Change: 0.09
Marker Score: 48
Cell Name: CD16-positive, CD56-dim natural killer cell, human (CL0000939)
Fold Change: 0.09
Marker Score: 69
Cell Name: mature B cell (CL0000785)
Fold Change: 0.08
Marker Score: 62
Cell Name: lung ciliated cell (CL1000271)
Fold Change: 0.08
Marker Score: 40

Hover over a box to see details here...

**Key characteristics:** * Protein type: Glycoprotein * Ensembl ID: ENSG00000171560 * Molecular weight: 125,000 Da * Expression: Highly expressed in the liver and other tissues * Functions: * Promotes blood clot formation * Regulates blood clotting * Plays a role in inflammation **Pathways and functions:** * The FGA gene encodes the fibrinogen alpha chain, which is a key component of fibrin. * Fibrinogen is synthesized in the liver and then secreted into the blood. * Once in the blood, fibrinogen is converted into fibrin by thrombin, an enzyme produced by activated platelets and activated endothelial cells. * Fibrin is responsible for the formation of blood clots by promoting the aggregation of fibrinogen monomers into fibrin polymers. * Fibrin also plays a role in inflammation by promoting the formation of blood clots in response to injury or infection. **Clinical significance:** Mutations in the FGA gene have been linked to a number of human diseases, including: * Thromboangiitis * Liver cirrhosis * Heart disease * Stroke * Cancer **Additional information:** * FGA is a highly important protein for blood clotting. * Mutations in the FGA gene can lead to the formation of abnormal blood clots, which can lead to serious health problems. * Fibrinogen is a very important protein for human health. It is involved in a variety of physiological processes, including blood clotting, inflammation, and tissue repair.

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 alpha chain

Genular Protein ID: 1664192174

Symbol: FIBA_HUMAN

Name: Fibrinogen alpha chain

UniProtKB Accession Codes:

P02671 A8K3E4 D3DP14 D3DP15 Q4QQH7 Q9BX62 Q9UCH2

Database IDs:

Citations:

PubMed ID: 1457396

Title: Carboxy-terminal-extended variant of the human fibrinogen alpha subunit: a novel exon conferring marked homology to beta and gamma subunits.

PubMed ID: 1457396

DOI: 10.1021/bi00163a002

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: 2102623

Title: Nucleotide sequences of the three genes coding for human fibrinogen.

PubMed ID: 2102623

DOI: 10.1007/978-1-4615-3806-6_3

PubMed ID: 6575389

Title: Partial mRNA sequences for human A alpha, B beta, and gamma fibrinogen chains: evolutionary and functional implications.

PubMed ID: 6575389

DOI: 10.1073/pnas.80.13.3953

PubMed ID: 6688355

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

PubMed ID: 6688355

DOI: 10.1021/bi00282a031

PubMed ID: 518846

Title: Amino acid sequence studies on the alpha chain of human fibrinogen. Overlapping sequences providing the complete sequence.

PubMed ID: 518846

DOI: 10.1021/bi00591a024

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: 6575700

Title: Cloning of fibrinogen genes and their cDNA.

PubMed ID: 6575700

DOI: 10.1111/j.1749-6632.1983.tb23265.x

PubMed ID: 741445

Title: The arrangement of disulfide bonds in fragment D from human fibrinogen.

PubMed ID: 741445

DOI: 10.1016/0049-3848(78)90142-1

PubMed ID: 518845

Title: Amino acid sequence studies on the alpha chain of human fibrinogen. Exact location of cross-linking acceptor sites.

PubMed ID: 518845

DOI: 10.1021/bi00591a023

PubMed ID: 632262

Title: Localization of the alpha-chain cross-link acceptor sites of human fibrin.

PubMed ID: 632262

DOI: 10.1016/s0021-9258(17)38057-2

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: 936108

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

PubMed ID: 936108

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

PubMed ID: 6383194

Title: Fibrinogen and fibrin.

PubMed ID: 6383194

DOI: 10.1146/annurev.bi.53.070184.001211

PubMed ID: 2877981

Title: Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor.

PubMed ID: 2877981

DOI: 10.1016/s0021-9258(18)66755-9

PubMed ID: 6318767

Title: Phosphorylation of fibrinogen by casein kinase 1.

PubMed ID: 6318767

DOI: 10.1016/0006-291x(83)91247-0

PubMed ID: 11418620

Title: Extracellular fibrinogen-binding protein, Efb, from Staphylococcus aureus blocks platelet aggregation due to its binding to the alpha-chain.

PubMed ID: 11418620

DOI: 10.1074/jbc.m104554200

PubMed ID: 16807684

Title: Phosphoproteomic analysis of the human pituitary.

PubMed ID: 16807684

DOI: 10.1007/s11102-006-8916-x

PubMed ID: 18088087

Title: Phosphoproteome of resting human platelets.

PubMed ID: 18088087

DOI: 10.1021/pr0704130

PubMed ID: 19696023

Title: Prolyl 4-hydroxylation of alpha-fibrinogen: a novel protein modification revealed by plasma proteomics.

PubMed ID: 19696023

DOI: 10.1074/jbc.m109.041749

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: 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: 23050552

Title: Glycoproteomic analysis of human fibrinogen reveals novel regions of O-glycosylation.

PubMed ID: 23050552

DOI: 10.1021/pr3005937

PubMed ID: 24348255

Title: Phagocytosis escape by a Staphylococcus aureus protein that connects complement and coagulation proteins at the bacterial surface.

PubMed ID: 24348255

DOI: 10.1371/journal.ppat.1003816

PubMed ID: 23151259

Title: Characterization of fibrinogen glycosylation and its importance for serum/plasma N-glycome analysis.

PubMed ID: 23151259

DOI: 10.1021/pr300813h

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: 1560020

Title: The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution.

PubMed ID: 1560020

DOI: 10.1016/s0021-9258(18)42599-9

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: 9689040

Title: Crystal structure of a recombinant alphaEC domain from human fibrinogen-420.

PubMed ID: 9689040

DOI: 10.1073/pnas.95.16.9099

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: 2070049

Title: Fibrinogen Kyoto II, a new congenitally abnormal molecule, characterized by the replacement of A alpha proline-18 by leucine.

PubMed ID: 2070049

PubMed ID: 1634621

Title: Fibrinogen Lima: a homozygous dysfibrinogen with an A alpha-arginine-141 to serine substitution associated with extra N-glycosylation at A alpha-asparagine-139. Impaired fibrin gel formation but normal fibrin-facilitated plasminogen activation catalyzed by tissue-type plasminogen activator.

PubMed ID: 1634621

DOI: 10.1172/jci115857

PubMed ID: 1675636

Title: An A alpha Ser-434 to N-glycosylated Asn substitution in a dysfibrinogen, fibrinogen Caracas II, characterized by impaired fibrin gel formation.

PubMed ID: 1675636

DOI: 10.1016/s0021-9258(18)98995-7

PubMed ID: 8473507

Title: Molecular basis for fibrinogen Dusart (A alpha 554 Arg-->Cys) and its association with abnormal fibrin polymerization and thrombophilia.

PubMed ID: 8473507

DOI: 10.1172/jci116371

PubMed ID: 8097946

Title: Hereditary renal amyloidosis associated with a mutant fibrinogen alpha-chain.

PubMed ID: 8097946

DOI: 10.1038/ng0393-252

PubMed ID: 8461606

Title: Fibrinogen Osaka IV: a congenital dysfibrinogenemia found in a patient originally reported in relation to surgery, now defined to have an A alpha arginine-16 to histidine substitution.

PubMed ID: 8461606

DOI: 10.1007/bf00308999

PubMed ID: 8675656

Title: Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (A-alpha 20 Val-to-Asp).

PubMed ID: 8675656

DOI: 10.1172/jci118356

PubMed ID: 10391209

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

PubMed ID: 10391209

DOI: 10.1038/10290

PubMed ID: 16846481

Title: The fibrinogen Aalpha R16C mutation results in fibrinolytic resistance.

PubMed ID: 16846481

DOI: 10.1111/j.1365-2141.2006.06129.x

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: 866
Mass: 94973
Checksum: EA73A81204D8AEC4
Sequence:

MFSMRIVCLV LSVVGTAWTA DSGEGDFLAE GGGVRGPRVV ERHQSACKDS DWPFCSDEDW 
NYKCPSGCRM KGLIDEVNQD FTNRINKLKN SLFEYQKNNK DSHSLTTNIM EILRGDFSSA 
NNRDNTYNRV SEDLRSRIEV LKRKVIEKVQ HIQLLQKNVR AQLVDMKRLE VDIDIKIRSC 
RGSCSRALAR EVDLKDYEDQ QKQLEQVIAK DLLPSRDRQH LPLIKMKPVP DLVPGNFKSQ 
LQKVPPEWKA LTDMPQMRME LERPGGNEIT RGGSTSYGTG SETESPRNPS SAGSWNSGSS 
GPGSTGNRNP GSSGTGGTAT WKPGSSGPGS TGSWNSGSSG TGSTGNQNPG SPRPGSTGTW 
NPGSSERGSA GHWTSESSVS GSTGQWHSES GSFRPDSPGS GNARPNNPDW GTFEEVSGNV 
SPGTRREYHT EKLVTSKGDK ELRTGKEKVT SGSTTTTRRS CSKTVTKTVI GPDGHKEVTK 
EVVTSEDGSD CPEAMDLGTL SGIGTLDGFR HRHPDEAAFF DTASTGKTFP GFFSPMLGEF 
VSETESRGSE SGIFTNTKES SSHHPGIAEF PSRGKSSSYS KQFTSSTSYN RGDSTFESKS 
YKMADEAGSE ADHEGTHSTK RGHAKSRPVR DCDDVLQTHP SGTQSGIFNI KLPGSSKIFS 
VYCDQETSLG GWLLIQQRMD GSLNFNRTWQ DYKRGFGSLN DEGEGEFWLG NDYLHLLTQR 
GSVLRVELED WAGNEAYAEY HFRVGSEAEG YALQVSSYEG TAGDALIEGS VEEGAEYTSH 
NNMQFSTFDR DADQWEENCA EVYGGGWWYN NCQAANLNGI YYPGGSYDPR NNSPYEIENG 
VVWVSFRGAD YSLRAVRMKI RPLVTQ

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: FGA

Associated with

Cells (max top 100)

Other Information

Carboxy-terminal-extended variant of the human fibrinogen alpha subunit: a novel exon conferring marked homology to beta and gamma subunits. PubMed ID: 1457396

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

Nucleotide sequences of the three genes coding for human fibrinogen. PubMed ID: 2102623

Partial mRNA sequences for human A alpha, B beta, and gamma fibrinogen chains: evolutionary and functional implications. PubMed ID: 6575389

Characterization of a complementary deoxyribonucleic acid coding for the alpha chain of human fibrinogen. PubMed ID: 6688355

Amino acid sequence studies on the alpha chain of human fibrinogen. Overlapping sequences providing the complete sequence. PubMed ID: 518846

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

Cloning of fibrinogen genes and their cDNA. PubMed ID: 6575700

The arrangement of disulfide bonds in fragment D from human fibrinogen. PubMed ID: 741445

Amino acid sequence studies on the alpha chain of human fibrinogen. Exact location of cross-linking acceptor sites. PubMed ID: 518845

Localization of the alpha-chain cross-link acceptor sites of human fibrin. PubMed ID: 632262

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

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

Fibrinogen and fibrin. PubMed ID: 6383194

Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor. PubMed ID: 2877981

Phosphorylation of fibrinogen by casein kinase 1. PubMed ID: 6318767

Extracellular fibrinogen-binding protein, Efb, from Staphylococcus aureus blocks platelet aggregation due to its binding to the alpha-chain. PubMed ID: 11418620

Phosphoproteomic analysis of the human pituitary. PubMed ID: 16807684

Phosphoproteome of resting human platelets. PubMed ID: 18088087

Prolyl 4-hydroxylation of alpha-fibrinogen: a novel protein modification revealed by plasma proteomics. PubMed ID: 19696023

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

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

Glycoproteomic analysis of human fibrinogen reveals novel regions of O-glycosylation. PubMed ID: 23050552

Phagocytosis escape by a Staphylococcus aureus protein that connects complement and coagulation proteins at the bacterial surface. PubMed ID: 24348255

Characterization of fibrinogen glycosylation and its importance for serum/plasma N-glycome analysis. PubMed ID: 23151259

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

The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution. PubMed ID: 1560020

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

Crystal structure of a recombinant alphaEC domain from human fibrinogen-420. PubMed ID: 9689040

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

Fibrinogen Kyoto II, a new congenitally abnormal molecule, characterized by the replacement of A alpha proline-18 by leucine. PubMed ID: 2070049

An A alpha Ser-434 to N-glycosylated Asn substitution in a dysfibrinogen, fibrinogen Caracas II, characterized by impaired fibrin gel formation. PubMed ID: 1675636

Molecular basis for fibrinogen Dusart (A alpha 554 Arg--&gt;Cys) and its association with abnormal fibrin polymerization and thrombophilia. PubMed ID: 8473507

Hereditary renal amyloidosis associated with a mutant fibrinogen alpha-chain. PubMed ID: 8097946

Fibrinogen Osaka IV: a congenital dysfibrinogenemia found in a patient originally reported in relation to surgery, now defined to have an A alpha arginine-16 to histidine substitution. PubMed ID: 8461606

Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (A-alpha 20 Val-to-Asp). PubMed ID: 8675656

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

The fibrinogen Aalpha R16C mutation results in fibrinolytic resistance. PubMed ID: 16846481

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