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Protein

Fibrinogen beta chain

Gene

FGB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways.By similarity

GO - Molecular functioni

  • chaperone binding Source: BHF-UCL
  • structural molecule activity Source: BHF-UCL

GO - Biological processi

  • adaptive immune response Source: UniProtKB-KW
  • blood coagulation Source: Reactome
  • blood coagulation, fibrin clot formation Source: UniProtKB
  • cell-matrix adhesion Source: BHF-UCL
  • cellular protein complex assembly Source: BHF-UCL
  • cellular response to interleukin-1 Source: Ensembl
  • cellular response to leptin stimulus Source: Ensembl
  • extracellular matrix organization Source: Reactome
  • fibrinolysis Source: UniProtKB
  • induction of bacterial agglutination Source: CACAO
  • innate immune response Source: UniProtKB-KW
  • negative regulation of endothelial cell apoptotic process Source: BHF-UCL
  • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
  • plasminogen activation Source: UniProtKB
  • platelet aggregation Source: BHF-UCL
  • platelet degranulation Source: Reactome
  • positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  • positive regulation of exocytosis Source: BHF-UCL
  • positive regulation of heterotypic cell-cell adhesion Source: BHF-UCL
  • positive regulation of peptide hormone secretion Source: BHF-UCL
  • positive regulation of protein secretion Source: BHF-UCL
  • positive regulation of substrate adhesion-dependent cell spreading Source: BHF-UCL
  • positive regulation of vasoconstriction Source: BHF-UCL
  • protein polymerization Source: BHF-UCL
  • response to calcium ion Source: BHF-UCL
  • signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Blood coagulation, Hemostasis, Immunity, Innate immunity

Enzyme and pathway databases

BioCyciZFISH:ENSG00000171564-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-140875. Common Pathway of Fibrin Clot Formation.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-354192. Integrin alphaIIb beta3 signaling.
R-HSA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-HSA-372708. p130Cas linkage to MAPK signaling for integrins.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-5686938. Regulation of TLR by endogenous ligand.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrinogen beta chain
Cleaved into the following 2 chains:
Gene namesi
Name:FGB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:3662. FGB.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cell cortex Source: Ensembl
  • cell surface Source: BHF-UCL
  • external side of plasma membrane Source: BHF-UCL
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • extracellular vesicle Source: UniProtKB
  • fibrinogen complex Source: UniProtKB
  • plasma membrane Source: Reactome
  • platelet alpha granule Source: BHF-UCL
  • platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Congenital afibrinogenemia (CAFBN)3 Publications
The disease is caused by mutations affecting the gene represented in this entry. Patients with congenital fibrinogen abnormalities can manifest different clinical pictures. Some cases are clinically silent, some show a tendency toward bleeding and some show a predisposition for thrombosis with or without bleeding.
Disease descriptionRare autosomal recessive disorder is characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen.
See also OMIM:202400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07272495C → R in CAFBN; hypofibrinogenemia; heterozygous; decreased fibrinogen complex assembly; no effect on fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_016908196R → C in CAFBN; fibrinogen Longmont. 1 PublicationCorresponds to variant rs121909623dbSNPEnsembl.1
Natural variantiVAR_072620202L → Q in CAFBN. 1 PublicationCorresponds to variant rs121909624dbSNPEnsembl.1
Natural variantiVAR_016909383L → R in CAFBN; abolishes fibrinogen secretion. 1 PublicationCorresponds to variant rs121909621dbSNPEnsembl.1
Natural variantiVAR_072725407T → K in CAFBN; homozygous; heterozygous; no effect on fibrinogen complex assembly; impaired fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_016910430G → D in CAFBN; abolishes fibrinogen secretion. 1 PublicationCorresponds to variant rs121909622dbSNPEnsembl.1
Dysfibrinogenemia, congenital (DYSFIBRIN)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by qualitative abnormalities (dysfibrinogenemia) of the circulating fibrinogen. Affected individuals are frequently asymptomatic, but some patients have bleeding diathesis, thromboembolic complications, or both. In some cases, dysfibrinogenemia is associated with low circulating fibrinogen levels (hypodysfibrinogenemia).
See also OMIM:616004
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00240698A → T in DYSFIBRIN; fibrinogen Naples and Milano-2; associated with defective thrombin binding and thrombophilia. 1 PublicationCorresponds to variant rs121909620dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2244.
MalaCardsiFGB.
MIMi202400. phenotype.
616004. phenotype.
OpenTargetsiENSG00000171564.
Orphaneti98880. Familial afibrinogenemia.
98881. Familial dysfibrinogenemia.
248408. Familial hypodysfibrinogenemia.
101041. Familial hypofibrinogenemia.
PharmGKBiPA163.

Chemistry databases

ChEMBLiCHEMBL2048.
DrugBankiDB00364. Sucralfate.

Polymorphism and mutation databases

BioMutaiFGB.
DMDMi399492.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 304 PublicationsAdd BLAST30
PeptideiPRO_000000907031 – 44Fibrinopeptide B1 PublicationAdd BLAST14
ChainiPRO_000000907145 – 491Fibrinogen beta chainAdd BLAST447

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei31Pyrrolidone carboxylic acid1 Publication1
Disulfide bondi95Interchain (with C-55 in alpha chain)1 Publication
Disulfide bondi106Interchain (with C-68 in alpha chain)1 Publication
Disulfide bondi110Interchain (with C-45 in gamma chain)1 Publication
Disulfide bondi223Interchain (with C-184 in alpha chain)Combined sources4 Publications
Disulfide bondi227Interchain (with C-161 in gamma chain)
Disulfide bondi231 ↔ 316Combined sources4 Publications
Disulfide bondi241 ↔ 270Combined sources4 Publications
Glycosylationi394N-linked (GlcNAc...)6 Publications1
Disulfide bondi424 ↔ 437Combined sources4 Publications

Post-translational modificationi

Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei44 – 45Cleavage; by thrombin; to release fibrinopeptide B2
Sitei152 – 153Cleavage; by plasmin; to break down fibrin clots2
Sitei160 – 161Cleavage; by hementin; to prevent blood coagulation2
Sitei163 – 164Cleavage; by plasmin; to break down fibrin clots2

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP02675.
PeptideAtlasiP02675.
PRIDEiP02675.

2D gel databases

DOSAC-COBS-2DPAGEP02675.
OGPiP02675.
REPRODUCTION-2DPAGEIPI00298497.
P02675.
SWISS-2DPAGEP02675.
UCD-2DPAGEP02675.

PTM databases

iPTMnetiP02675.
PhosphoSitePlusiP02675.
SwissPalmiP02675.
UniCarbKBiP02675.

Miscellaneous databases

PMAP-CutDBP02675.

Expressioni

Tissue specificityi

Detected in blood plasma (at protein level).3 Publications

Gene expression databases

BgeeiENSG00000171564.
CleanExiHS_FGB.
ExpressionAtlasiP02675. baseline and differential.
GenevisibleiP02675. HS.

Organism-specific databases

HPAiCAB008624.
HPA001900.
HPA001901.

Interactioni

Subunit structurei

Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P279584EBI-1034445,EBI-6377335From a different organism.

GO - Molecular functioni

  • chaperone binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108535. 111 interactors.
DIPiDIP-385N.
IntActiP02675. 16 interactors.
STRINGi9606.ENSP00000306099.

Structurei

Secondary structure

1491
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni100 – 102Combined sources3
Helixi109 – 145Combined sources37
Helixi147 – 167Combined sources21
Helixi172 – 180Combined sources9
Turni182 – 189Combined sources8
Helixi190 – 222Combined sources33
Beta strandi224 – 226Combined sources3
Beta strandi233 – 235Combined sources3
Beta strandi238 – 240Combined sources3
Helixi241 – 246Combined sources6
Beta strandi253 – 257Combined sources5
Beta strandi261 – 263Combined sources3
Beta strandi266 – 271Combined sources6
Helixi274 – 276Combined sources3
Beta strandi279 – 288Combined sources10
Helixi296 – 301Combined sources6
Beta strandi302 – 304Combined sources3
Beta strandi306 – 308Combined sources3
Beta strandi311 – 315Combined sources5
Beta strandi321 – 323Combined sources3
Helixi326 – 334Combined sources9
Beta strandi335 – 337Combined sources3
Beta strandi339 – 345Combined sources7
Beta strandi347 – 349Combined sources3
Beta strandi351 – 361Combined sources11
Helixi364 – 366Combined sources3
Beta strandi370 – 379Combined sources10
Helixi382 – 385Combined sources4
Beta strandi388 – 390Combined sources3
Helixi392 – 396Combined sources5
Beta strandi404 – 407Combined sources4
Beta strandi408 – 410Combined sources3
Helixi420 – 422Combined sources3
Turni424 – 428Combined sources5
Beta strandi435 – 437Combined sources3
Beta strandi439 – 441Combined sources3
Beta strandi448 – 451Combined sources4
Turni454 – 456Combined sources3
Beta strandi457 – 461Combined sources5
Beta strandi464 – 467Combined sources4
Helixi468 – 471Combined sources4
Beta strandi473 – 475Combined sources3
Beta strandi478 – 485Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FZAX-ray2.90B/E164-491[»]
1FZBX-ray2.90B/E164-491[»]
1FZCX-ray2.30B/E164-491[»]
1FZEX-ray3.00B/E164-491[»]
1FZFX-ray2.70B/E164-491[»]
M/N/S/T45-48[»]
1FZGX-ray2.50B/E164-491[»]
1LT9X-ray2.80B/E179-491[»]
1LTJX-ray2.80B/E179-491[»]
1N86X-ray3.20B/E164-491[»]
I/J45-51[»]
1N8EX-ray4.50B/E164-491[»]
1RE3X-ray2.45B/E179-491[»]
1RE4X-ray2.70B/E179-491[»]
1RF0X-ray2.81B/E179-491[»]
1RF1X-ray2.53B/E179-491[»]
2A45X-ray3.65H/K45-135[»]
2FFDX-ray2.89B/E179-491[»]
2H43X-ray2.70B/E164-491[»]
2HLOX-ray2.60B/E164-491[»]
2HODX-ray2.90B/E/H/K164-491[»]
2HPCX-ray2.90B/E/H/K164-491[»]
2OYHX-ray2.40B/E179-491[»]
2OYIX-ray2.70B/E179-491[»]
2Q9IX-ray2.80B/E164-491[»]
2XNXX-ray3.30B/E/H/K164-491[»]
2XNYX-ray7.50B/E164-491[»]
2Z4EX-ray2.70B/E164-489[»]
3BVHX-ray2.60B/E191-488[»]
3E1IX-ray2.30B/E164-491[»]
3GHGX-ray2.90B/E/H/K31-491[»]
3H32X-ray3.60B/E31-488[»]
3HUSX-ray3.04B/E179-491[»]
ProteinModelPortaliP02675.
SMRiP02675.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02675.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini232 – 488Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST257

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni45 – 47Beta-chain polymerization, binding distal domain of another fibrin3

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili157 – 2223 PublicationsAdd BLAST66

Domaini

A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.3 Publications

Sequence similaritiesi

Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00760000118809.
HOGENOMiHOG000059561.
HOVERGENiHBG005707.
InParanoidiP02675.
KOiK03904.
OMAiTIHNGMF.
OrthoDBiEOG091G03M1.
PhylomeDBiP02675.
TreeFamiTF336658.

Family and domain databases

CDDicd00087. FReD. 1 hit.
Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR012290. Fibrinogen_a/b/g_coil_dom.
IPR020837. Fibrinogen_CS.
[Graphical view]
PfamiPF08702. Fib_alpha. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
SM01212. Fib_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02675-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRMVSWSFH KLKTMKHLLL LLLCVFLVKS QGVNDNEEGF FSARGHRPLD
60 70 80 90 100
KKREEAPSLR PAPPPISGGG YRARPAKAAA TQKKVERKAP DAGGCLHADP
110 120 130 140 150
DLGVLCPTGC QLQEALLQQE RPIRNSVDEL NNNVEAVSQT SSSSFQYMYL
160 170 180 190 200
LKDLWQKRQK QVKDNENVVN EYSSELEKHQ LYIDETVNSN IPTNLRVLRS
210 220 230 240 250
ILENLRSKIQ KLESDVSAQM EYCRTPCTVS CNIPVVSGKE CEEIIRKGGE
260 270 280 290 300
TSEMYLIQPD SSVKPYRVYC DMNTENGGWT VIQNRQDGSV DFGRKWDPYK
310 320 330 340 350
QGFGNVATNT DGKNYCGLPG EYWLGNDKIS QLTRMGPTEL LIEMEDWKGD
360 370 380 390 400
KVKAHYGGFT VQNEANKYQI SVNKYRGTAG NALMDGASQL MGENRTMTIH
410 420 430 440 450
NGMFFSTYDR DNDGWLTSDP RKQCSKEDGG GWWYNRCHAA NPNGRYYWGG
460 470 480 490
QYTWDMAKHG TDDGVVWMNW KGSWYSMRKM SMKIRPFFPQ Q
Length:491
Mass (Da):55,928
Last modified:July 1, 1993 - v2
Checksum:iB92FFB9976AB53C5
GO

Sequence cautioni

The sequence AAH07030 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti138 – 139SQ → QS AA sequence (Ref. 11) Curated2
Sequence conflicti138 – 139SQ → QS AA sequence (PubMed:936108).Curated2
Sequence conflicti145 – 146FQ → QF AA sequence (PubMed:420779).Curated2
Sequence conflicti145 – 146FQ → QF AA sequence (Ref. 11) Curated2
Sequence conflicti145 – 146FQ → QF AA sequence (PubMed:936108).Curated2
Sequence conflicti192P → A in AAA52429 (PubMed:6688356).Curated1
Sequence conflicti245I → T in AAI07767 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0141692K → E.1 PublicationCorresponds to variant rs6053dbSNPEnsembl.1
Natural variantiVAR_00240239 – 102Missing in New York-1. 1 PublicationAdd BLAST64
Natural variantiVAR_00240344R → C in Christchurch-2, Seattle-1 and Ijmuiden. 1 PublicationCorresponds to variant rs121909616dbSNPEnsembl.1
Natural variantiVAR_00240445G → R in Ise. 1 Publication1
Natural variantiVAR_00240574R → C in Nijmegen. 1 PublicationCorresponds to variant rs121909619dbSNPEnsembl.1
Natural variantiVAR_07272495C → R in CAFBN; hypofibrinogenemia; heterozygous; decreased fibrinogen complex assembly; no effect on fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_00240698A → T in DYSFIBRIN; fibrinogen Naples and Milano-2; associated with defective thrombin binding and thrombophilia. 1 PublicationCorresponds to variant rs121909620dbSNPEnsembl.1
Natural variantiVAR_013091100P → S.1 PublicationCorresponds to variant rs2227434dbSNPEnsembl.1
Natural variantiVAR_013092170N → H.1 PublicationCorresponds to variant rs2227409dbSNPEnsembl.1
Natural variantiVAR_016908196R → C in CAFBN; fibrinogen Longmont. 1 PublicationCorresponds to variant rs121909623dbSNPEnsembl.1
Natural variantiVAR_072620202L → Q in CAFBN. 1 PublicationCorresponds to variant rs121909624dbSNPEnsembl.1
Natural variantiVAR_013093265P → L.2 PublicationsCorresponds to variant rs6054dbSNPEnsembl.1
Natural variantiVAR_002407365A → T in Pontoise-2. Corresponds to variant rs121909617dbSNPEnsembl.1
Natural variantiVAR_016909383L → R in CAFBN; abolishes fibrinogen secretion. 1 PublicationCorresponds to variant rs121909621dbSNPEnsembl.1
Natural variantiVAR_072725407T → K in CAFBN; homozygous; heterozygous; no effect on fibrinogen complex assembly; impaired fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_016910430G → D in CAFBN; abolishes fibrinogen secretion. 1 PublicationCorresponds to variant rs121909622dbSNPEnsembl.1
Natural variantiVAR_002408478R → K in Baltimore-2. 3 PublicationsCorresponds to variant rs4220dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00129 mRNA. Translation: AAA52429.1.
J00131, J00130 Genomic DNA. Translation: AAA98115.1.
J00132 Genomic DNA. Translation: AAA98116.1.
J00133 mRNA. No translation available.
M64983 Genomic DNA. Translation: AAA18024.2.
AF388026 Genomic DNA. Translation: AAK62470.1.
AK312972 mRNA. Translation: BAG35810.1.
CH471056 Genomic DNA. Translation: EAX04932.1.
BC007030 mRNA. Translation: AAH07030.1. Sequence problems.
BC106760 mRNA. Translation: AAI06761.1.
BC107766 mRNA. Translation: AAI07767.1.
AH002694 Genomic DNA. Translation: AAA52445.1.
X05018 Genomic DNA. Translation: CAA28674.1.
CCDSiCCDS3786.1.
PIRiB43568. FGHUB.
RefSeqiNP_001171670.1. NM_001184741.1.
NP_005132.2. NM_005141.4.
UniGeneiHs.300774.

Genome annotation databases

EnsembliENST00000302068; ENSP00000306099; ENSG00000171564.
GeneIDi2244.
KEGGihsa:2244.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Fibrinogen entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00129 mRNA. Translation: AAA52429.1.
J00131, J00130 Genomic DNA. Translation: AAA98115.1.
J00132 Genomic DNA. Translation: AAA98116.1.
J00133 mRNA. No translation available.
M64983 Genomic DNA. Translation: AAA18024.2.
AF388026 Genomic DNA. Translation: AAK62470.1.
AK312972 mRNA. Translation: BAG35810.1.
CH471056 Genomic DNA. Translation: EAX04932.1.
BC007030 mRNA. Translation: AAH07030.1. Sequence problems.
BC106760 mRNA. Translation: AAI06761.1.
BC107766 mRNA. Translation: AAI07767.1.
AH002694 Genomic DNA. Translation: AAA52445.1.
X05018 Genomic DNA. Translation: CAA28674.1.
CCDSiCCDS3786.1.
PIRiB43568. FGHUB.
RefSeqiNP_001171670.1. NM_001184741.1.
NP_005132.2. NM_005141.4.
UniGeneiHs.300774.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FZAX-ray2.90B/E164-491[»]
1FZBX-ray2.90B/E164-491[»]
1FZCX-ray2.30B/E164-491[»]
1FZEX-ray3.00B/E164-491[»]
1FZFX-ray2.70B/E164-491[»]
M/N/S/T45-48[»]
1FZGX-ray2.50B/E164-491[»]
1LT9X-ray2.80B/E179-491[»]
1LTJX-ray2.80B/E179-491[»]
1N86X-ray3.20B/E164-491[»]
I/J45-51[»]
1N8EX-ray4.50B/E164-491[»]
1RE3X-ray2.45B/E179-491[»]
1RE4X-ray2.70B/E179-491[»]
1RF0X-ray2.81B/E179-491[»]
1RF1X-ray2.53B/E179-491[»]
2A45X-ray3.65H/K45-135[»]
2FFDX-ray2.89B/E179-491[»]
2H43X-ray2.70B/E164-491[»]
2HLOX-ray2.60B/E164-491[»]
2HODX-ray2.90B/E/H/K164-491[»]
2HPCX-ray2.90B/E/H/K164-491[»]
2OYHX-ray2.40B/E179-491[»]
2OYIX-ray2.70B/E179-491[»]
2Q9IX-ray2.80B/E164-491[»]
2XNXX-ray3.30B/E/H/K164-491[»]
2XNYX-ray7.50B/E164-491[»]
2Z4EX-ray2.70B/E164-489[»]
3BVHX-ray2.60B/E191-488[»]
3E1IX-ray2.30B/E164-491[»]
3GHGX-ray2.90B/E/H/K31-491[»]
3H32X-ray3.60B/E31-488[»]
3HUSX-ray3.04B/E179-491[»]
ProteinModelPortaliP02675.
SMRiP02675.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108535. 111 interactors.
DIPiDIP-385N.
IntActiP02675. 16 interactors.
STRINGi9606.ENSP00000306099.

Chemistry databases

ChEMBLiCHEMBL2048.
DrugBankiDB00364. Sucralfate.

PTM databases

iPTMnetiP02675.
PhosphoSitePlusiP02675.
SwissPalmiP02675.
UniCarbKBiP02675.

Polymorphism and mutation databases

BioMutaiFGB.
DMDMi399492.

2D gel databases

DOSAC-COBS-2DPAGEP02675.
OGPiP02675.
REPRODUCTION-2DPAGEIPI00298497.
P02675.
SWISS-2DPAGEP02675.
UCD-2DPAGEP02675.

Proteomic databases

PaxDbiP02675.
PeptideAtlasiP02675.
PRIDEiP02675.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302068; ENSP00000306099; ENSG00000171564.
GeneIDi2244.
KEGGihsa:2244.

Organism-specific databases

CTDi2244.
DisGeNETi2244.
GeneCardsiFGB.
HGNCiHGNC:3662. FGB.
HPAiCAB008624.
HPA001900.
HPA001901.
MalaCardsiFGB.
MIMi134830. gene.
202400. phenotype.
616004. phenotype.
neXtProtiNX_P02675.
OpenTargetsiENSG00000171564.
Orphaneti98880. Familial afibrinogenemia.
98881. Familial dysfibrinogenemia.
248408. Familial hypodysfibrinogenemia.
101041. Familial hypofibrinogenemia.
PharmGKBiPA163.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00760000118809.
HOGENOMiHOG000059561.
HOVERGENiHBG005707.
InParanoidiP02675.
KOiK03904.
OMAiTIHNGMF.
OrthoDBiEOG091G03M1.
PhylomeDBiP02675.
TreeFamiTF336658.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000171564-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-140875. Common Pathway of Fibrin Clot Formation.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-354192. Integrin alphaIIb beta3 signaling.
R-HSA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-HSA-372708. p130Cas linkage to MAPK signaling for integrins.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-5686938. Regulation of TLR by endogenous ligand.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.

Miscellaneous databases

ChiTaRSiFGB. human.
EvolutionaryTraceiP02675.
GeneWikiiFibrinogen_beta_chain.
GenomeRNAii2244.
PMAP-CutDBP02675.
PROiP02675.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000171564.
CleanExiHS_FGB.
ExpressionAtlasiP02675. baseline and differential.
GenevisibleiP02675. HS.

Family and domain databases

CDDicd00087. FReD. 1 hit.
Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR012290. Fibrinogen_a/b/g_coil_dom.
IPR020837. Fibrinogen_CS.
[Graphical view]
PfamiPF08702. Fib_alpha. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
SM01212. Fib_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFIBB_HUMAN
AccessioniPrimary (citable) accession number: P02675
Secondary accession number(s): A0JLR9
, B2R7G3, Q32Q65, Q3KPF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1993
Last modified: November 30, 2016
This is version 203 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.