FGA | ENSG00000171560 | NCBI 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)
Collagen-containing extracellular matrix
(GO:0062023)
Endoplasmic reticulum
(GO:0005783)
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)
Induction of bacterial agglutination
(GO:0043152)
Innate immune response
(GO:0045087)
Metal ion binding
(GO:0046872)
Negative regulation of blood coagulation, common pathway
(GO:2000261)
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)
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-macromolecule adaptor activity
(GO:0030674)
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)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: centrilobular region hepatocyte (CL0019029)
Fold Change: 15.4303
Cell Significance Index: 259.9200
Cell Name: intrahepatic cholangiocyte (CL0002538)
Fold Change: 4.9426
Cell Significance Index: 18.6200
Cell Name: hepatic pit cell (CL2000054)
Fold Change: 4.9274
Cell Significance Index: 13.2000
Cell Name: endothelial cell of periportal hepatic sinusoid (CL0019021)
Fold Change: 4.3116
Cell Significance Index: 15.0000
Cell Name: midzonal region hepatocyte (CL0019028)
Fold Change: 4.0035
Cell Significance Index: 23.0600
Cell Name: hepatoblast (CL0005026)
Fold Change: 3.8813
Cell Significance Index: 65.2800
Cell Name: neoplastic cell (CL0001063)
Fold Change: 3.6455
Cell Significance Index: 723.4700
Cell Name: periportal region hepatocyte (CL0019026)
Fold Change: 2.2941
Cell Significance Index: 33.8600
Cell Name: endothelial cell of pericentral hepatic sinusoid (CL0019022)
Fold Change: 1.9735
Cell Significance Index: 15.5800
Cell Name: liver dendritic cell (CL2000055)
Fold Change: 1.7817
Cell Significance Index: 4.7000
Cell Name: cholangiocyte (CL1000488)
Fold Change: 1.5680
Cell Significance Index: 15.4700
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: 0.9109
Cell Significance Index: 29.1800
Cell Name: abnormal cell (CL0001061)
Fold Change: 0.8901
Cell Significance Index: 90.9200
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.7997
Cell Significance Index: 28.1000
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.7272
Cell Significance Index: 15.7600
Cell Name: endothelial cell of hepatic sinusoid (CL1000398)
Fold Change: 0.4145
Cell Significance Index: 3.9400
Cell Name: mature B cell (CL0000785)
Fold Change: 0.4083
Cell Significance Index: 2.6600
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: 0.3791
Cell Significance Index: 23.2500
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.2159
Cell Significance Index: 41.0900
Cell Name: gut absorptive cell (CL0000677)
Fold Change: 0.1248
Cell Significance Index: 7.4900
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: 0.0935
Cell Significance Index: 58.4000
Cell Name: hepatic stellate cell (CL0000632)
Fold Change: 0.0751
Cell Significance Index: 0.7800
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: 0.0487
Cell Significance Index: 36.8600
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 0.0479
Cell Significance Index: 5.2100
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: 0.0405
Cell Significance Index: 4.7200
Cell Name: Kupffer cell (CL0000091)
Fold Change: 0.0404
Cell Significance Index: 0.3700
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: 0.0285
Cell Significance Index: 3.2600
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.0239
Cell Significance Index: 21.5500
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.0081
Cell Significance Index: 1.3800
Cell Name: hepatocyte (CL0000182)
Fold Change: 0.0076
Cell Significance Index: 0.1100
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.0023
Cell Significance Index: 0.3800
Cell Name: neuron associated cell (CL0000095)
Fold Change: 0.0016
Cell Significance Index: 0.0600
Cell Name: pancreatic A cell (CL0000171)
Fold Change: 0.0009
Cell Significance Index: 0.6900
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 0.0007
Cell Significance Index: 0.0500
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0018
Cell Significance Index: -1.0000
Cell Name: near-projecting glutamatergic cortical neuron (CL4023012)
Fold Change: -0.0027
Cell Significance Index: -0.0700
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.0079
Cell Significance Index: -1.6700
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: -0.0111
Cell Significance Index: -0.3200
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: -0.0136
Cell Significance Index: -0.3400
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0194
Cell Significance Index: -14.2300
Cell Name: colon goblet cell (CL0009039)
Fold Change: -0.0212
Cell Significance Index: -2.1000
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.0240
Cell Significance Index: -2.7400
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: -0.0261
Cell Significance Index: -0.7000
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: -0.0286
Cell Significance Index: -3.9300
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: -0.0309
Cell Significance Index: -6.1900
Cell Name: inflammatory macrophage (CL0000863)
Fold Change: -0.0469
Cell Significance Index: -0.3600
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: -0.0534
Cell Significance Index: -2.4200
Cell Name: transit amplifying cell of small intestine (CL0009012)
Fold Change: -0.0550
Cell Significance Index: -1.1400
Cell Name: intestinal epithelial cell (CL0002563)
Fold Change: -0.0565
Cell Significance Index: -0.5900
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: -0.0694
Cell Significance Index: -3.2400
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: -0.0836
Cell Significance Index: -3.9300
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.0930
Cell Significance Index: -1.9800
Cell Name: plasmablast (CL0000980)
Fold Change: -0.1013
Cell Significance Index: -0.9400
Cell Name: peg cell (CL4033014)
Fold Change: -0.1162
Cell Significance Index: -2.6900
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: -0.1272
Cell Significance Index: -3.6500
Cell Name: keratinocyte (CL0000312)
Fold Change: -0.1289
Cell Significance Index: -3.2200
Cell Name: lymphocyte (CL0000542)
Fold Change: -0.1307
Cell Significance Index: -1.7800
Cell Name: erythroid progenitor cell (CL0000038)
Fold Change: -0.1338
Cell Significance Index: -1.7500
Cell Name: cytotoxic T cell (CL0000910)
Fold Change: -0.1396
Cell Significance Index: -2.0400
Cell Name: L6b glutamatergic cortical neuron (CL4023038)
Fold Change: -0.1607
Cell Significance Index: -5.2600
Cell Name: proerythroblast (CL0000547)
Fold Change: -0.1619
Cell Significance Index: -2.3200
Cell Name: epithelial cell of pancreas (CL0000083)
Fold Change: -0.1669
Cell Significance Index: -2.7500
Cell Name: epithelial cell (CL0000066)
Fold Change: -0.1844
Cell Significance Index: -1.9500
Cell Name: alpha-beta T cell (CL0000789)
Fold Change: -0.1972
Cell Significance Index: -1.6800
Cell Name: BEST4+ enteroycte (CL4030026)
Fold Change: -0.2054
Cell Significance Index: -3.1000
Cell Name: fallopian tube secretory epithelial cell (CL4030006)
Fold Change: -0.2133
Cell Significance Index: -3.3000
Cell Name: erythrocyte (CL0000232)
Fold Change: -0.2345
Cell Significance Index: -5.9800
Cell Name: luminal epithelial cell of mammary gland (CL0002326)
Fold Change: -0.2388
Cell Significance Index: -3.0800
Cell Name: stratified epithelial cell (CL0000079)
Fold Change: -0.2397
Cell Significance Index: -8.8000
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: -0.2412
Cell Significance Index: -6.4400
Cell Name: lamp5 GABAergic cortical interneuron (CL4023011)
Fold Change: -0.2462
Cell Significance Index: -5.3200
Cell Name: granulosa cell (CL0000501)
Fold Change: -0.2464
Cell Significance Index: -6.4800
Cell Name: thymocyte (CL0000893)
Fold Change: -0.2497
Cell Significance Index: -3.1600
Cell Name: hematopoietic multipotent progenitor cell (CL0000837)
Fold Change: -0.2609
Cell Significance Index: -3.1500
Cell Name: Purkinje cell (CL0000121)
Fold Change: -0.2667
Cell Significance Index: -5.8400
Cell Name: caudal ganglionic eminence derived cortical interneuron (CL4023064)
Fold Change: -0.2713
Cell Significance Index: -5.4100
Cell Name: endothelial cell of artery (CL1000413)
Fold Change: -0.2761
Cell Significance Index: -2.9100
Cell Name: cardiac muscle cell (CL0000746)
Fold Change: -0.2784
Cell Significance Index: -4.1100
Cell Name: myoepithelial cell (CL0000185)
Fold Change: -0.2856
Cell Significance Index: -3.2400
Cell Name: luminal cell of prostate epithelium (CL0002340)
Fold Change: -0.2899
Cell Significance Index: -3.0000
Cell Name: naive B cell (CL0000788)
Fold Change: -0.2958
Cell Significance Index: -3.1200
Cell Name: mesenchymal cell (CL0008019)
Fold Change: -0.3026
Cell Significance Index: -5.0700
Cell Name: astrocyte of the cerebral cortex (CL0002605)
Fold Change: -0.3060
Cell Significance Index: -5.2900
Cell Name: myeloid lineage restricted progenitor cell (CL0000839)
Fold Change: -0.3135
Cell Significance Index: -4.4000
Cell Name: monocyte (CL0000576)
Fold Change: -0.3181
Cell Significance Index: -3.6600
Cell Name: oligodendrocyte precursor cell (CL0002453)
Fold Change: -0.3210
Cell Significance Index: -4.1900
Cell Name: decidual cell (CL2000002)
Fold Change: -0.3219
Cell Significance Index: -5.1700
Cell Name: erythroblast (CL0000765)
Fold Change: -0.3271
Cell Significance Index: -3.9000
Cell Name: lymphoid lineage restricted progenitor cell (CL0000838)
Fold Change: -0.3283
Cell Significance Index: -4.1600
Cell Name: vascular associated smooth muscle cell (CL0000359)
Fold Change: -0.3493
Cell Significance Index: -3.7100
Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
Fold Change: -0.3510
Cell Significance Index: -7.4500
Cell Name: medial ganglionic eminence derived interneuron (CL4023063)
Fold Change: -0.3568
Cell Significance Index: -5.1100
Cell Name: CD14-low, CD16-positive monocyte (CL0002396)
Fold Change: -0.3582
Cell Significance Index: -8.6800
Cell Name: CD14-positive monocyte (CL0001054)
Fold Change: -0.3775
Cell Significance Index: -7.3800
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: -0.3791
Cell Significance Index: -11.1700
Cell Name: PP cell (CL0000696)
Fold Change: -0.3826
Cell Significance Index: -3.8900
Cell Name: hematopoietic stem cell (CL0000037)
Fold Change: -0.3879
Cell Significance Index: -6.6300
Cell Name: adipocyte (CL0000136)
Fold Change: -0.3923
Cell Significance Index: -5.2300
Cell Name: myelocyte (CL0002193)
Fold Change: -0.3959
Cell Significance Index: -4.2300
Cell Name: nasal mucosa goblet cell (CL0002480)
Fold Change: -0.4034
Cell Significance Index: -4.1200

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics** 1. **Structure**: Fibrinogen is a tetrameric glycoprotein composed of three polypeptide chains: alpha, beta, and gamma. 2. **Function**: Fibrinogen plays a central role in blood coagulation, regulating the conversion of soluble fibrinogen to insoluble fibrin. 3. **Synthesis**: Fibrinogen is synthesized in the liver and released into the bloodstream. 4. **Expression**: Fibrinogen is expressed in various cells, including hepatoblasts, endothelial cells, and inflammatory macrophages. 5. **Binding**: Fibrinogen binds to other proteins, including thrombin, factor XIII, and integrins, to regulate coagulation and cellular processes. **Pathways and Functions** 1. **Blood Coagulation**: Fibrinogen is converted into fibrin by thrombin, forming a fibrin clot that helps to stop bleeding. 2. **Cell-Matrix Adhesion**: Fibrinogen interacts with integrins and other proteins to regulate cell-matrix adhesion and signaling. 3. **Adaptive Immune Response**: Fibrinogen is involved in the adaptive immune response, regulating the activation of immune cells and the production of cytokines. 4. **Amyloid Fiber Formation**: Fibrinogen can form amyloid fibers, which are associated with various diseases, including Alzheimer's and Parkinson's. 5. **Signaling Pathways**: Fibrinogen interacts with various signaling pathways, including MAPK, PI3K, and JAK/STAT, to regulate cellular processes. **Clinical Significance** 1. **Thrombotic Disorders**: Fibrinogen dysregulation is associated with thrombotic disorders, including deep vein thrombosis and pulmonary embolism. 2. **Hemostasis**: Fibrinogen plays a critical role in hemostasis, regulating the formation of fibrin clots that help to stop bleeding. 3. **Inflammatory Diseases**: Fibrinogen is involved in the regulation of inflammatory responses, including the activation of immune cells and the production of cytokines. 4. **Cancer**: Fibrinogen is overexpressed in various cancers, including breast, lung, and colon cancer, and is associated with poor prognosis. 5. **Infectious Diseases**: Fibrinogen is involved in the regulation of the innate immune response, including the activation of immune cells and the production of cytokines. In conclusion, fibrinogen alpha chain is a multifunctional protein that plays a critical role in blood coagulation, cellular processes, and the regulation of the immune response. Its dysregulation is associated with various diseases, including thrombotic disorders, hemostasis, inflammatory diseases, cancer, and infectious diseases.

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. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. 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