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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

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti95 – 951C → R in CAFBN; hypofibrinogenemia; heterozygous; decreased fibrinogen complex assembly; no effect on fibrinogen complex secretion. 1 Publication
VAR_072724
Natural varianti196 – 1961R → C in CAFBN; fibrinogen Longmont. 1 Publication
Corresponds to variant rs121909623 [ dbSNP | Ensembl ].
VAR_016908
Natural varianti202 – 2021L → Q in CAFBN. 1 Publication
Corresponds to variant rs121909624 [ dbSNP | Ensembl ].
VAR_072620
Natural varianti383 – 3831L → R in CAFBN; abolishes fibrinogen secretion. 1 Publication
Corresponds to variant rs121909621 [ dbSNP | Ensembl ].
VAR_016909
Natural varianti407 – 4071T → K in CAFBN; homozygous; heterozygous; no effect on fibrinogen complex assembly; impaired fibrinogen complex secretion. 1 Publication
VAR_072725
Natural varianti430 – 4301G → D in CAFBN; abolishes fibrinogen secretion. 1 Publication
Corresponds to variant rs121909622 [ dbSNP | Ensembl ].
VAR_016910
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti98 – 981A → T in DYSFIBRIN; fibrinogen Naples and Milano-2; associated with defective thrombin binding and thrombophilia. 1 Publication
Corresponds to variant rs121909620 [ dbSNP | Ensembl ].
VAR_002406

Keywords - Diseasei

Disease mutation

Organism-specific databases

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

Chemistry

ChEMBLiCHEMBL2364709.
DrugBankiDB00364. Sucralfate.

Polymorphism and mutation databases

BioMutaiFGB.
DMDMi399492.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 30304 PublicationsAdd
BLAST
Peptidei31 – 4414Fibrinopeptide B1 PublicationPRO_0000009070Add
BLAST
Chaini45 – 491447Fibrinogen beta chainPRO_0000009071Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311Pyrrolidone carboxylic acid1 Publication
Disulfide bondi95 – 95Interchain (with C-55 in alpha chain)1 Publication
Disulfide bondi106 – 106Interchain (with C-68 in alpha chain)1 Publication
Disulfide bondi110 – 110Interchain (with C-45 in gamma chain)1 Publication
Disulfide bondi223 – 223Interchain (with C-184 in alpha chain)Combined sources4 Publications
Disulfide bondi227 – 227Interchain (with C-161 in gamma chain)
Disulfide bondi231 ↔ 316Combined sources4 Publications
Disulfide bondi241 ↔ 270Combined sources4 Publications
Glycosylationi394 – 3941N-linked (GlcNAc...)6 Publications
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)LengthDescriptionGraphical viewFeature identifierActions
Sitei44 – 452Cleavage; by thrombin; to release fibrinopeptide B
Sitei152 – 1532Cleavage; by plasmin; to break down fibrin clots
Sitei160 – 1612Cleavage; by hementin; to prevent blood coagulation
Sitei163 – 1642Cleavage; by plasmin; to break down fibrin clots

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.
PhosphoSiteiP02675.
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 interactions.
DIPiDIP-385N.
IntActiP02675. 16 interactions.
STRINGi9606.ENSP00000306099.

Structurei

Secondary structure

1
491
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni100 – 1023Combined sources
Helixi109 – 14537Combined sources
Helixi147 – 16721Combined sources
Helixi172 – 1809Combined sources
Turni182 – 1898Combined sources
Helixi190 – 22233Combined sources
Beta strandi224 – 2263Combined sources
Beta strandi233 – 2353Combined sources
Beta strandi238 – 2403Combined sources
Helixi241 – 2466Combined sources
Beta strandi253 – 2575Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi266 – 2716Combined sources
Helixi274 – 2763Combined sources
Beta strandi279 – 28810Combined sources
Helixi296 – 3016Combined sources
Beta strandi302 – 3043Combined sources
Beta strandi306 – 3083Combined sources
Beta strandi311 – 3155Combined sources
Beta strandi321 – 3233Combined sources
Helixi326 – 3349Combined sources
Beta strandi335 – 3373Combined sources
Beta strandi339 – 3457Combined sources
Beta strandi347 – 3493Combined sources
Beta strandi351 – 36111Combined sources
Helixi364 – 3663Combined sources
Beta strandi370 – 37910Combined sources
Helixi382 – 3854Combined sources
Beta strandi388 – 3903Combined sources
Helixi392 – 3965Combined sources
Beta strandi404 – 4074Combined sources
Beta strandi408 – 4103Combined sources
Helixi420 – 4223Combined sources
Turni424 – 4285Combined sources
Beta strandi435 – 4373Combined sources
Beta strandi439 – 4413Combined sources
Beta strandi448 – 4514Combined sources
Turni454 – 4563Combined sources
Beta strandi457 – 4615Combined sources
Beta strandi464 – 4674Combined sources
Helixi468 – 4714Combined sources
Beta strandi473 – 4753Combined sources
Beta strandi478 – 4858Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 88-488.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02675.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini232 – 488257Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 473Beta-chain polymerization, binding distal domain of another fibrin

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili157 – 222663 PublicationsAdd
BLAST

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

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1392SQ → QS AA sequence (Ref. 11) Curated
Sequence conflicti138 – 1392SQ → QS AA sequence (PubMed:936108).Curated
Sequence conflicti145 – 1462FQ → QF AA sequence (PubMed:420779).Curated
Sequence conflicti145 – 1462FQ → QF AA sequence (Ref. 11) Curated
Sequence conflicti145 – 1462FQ → QF AA sequence (PubMed:936108).Curated
Sequence conflicti192 – 1921P → A in AAA52429 (PubMed:6688356).Curated
Sequence conflicti245 – 2451I → T in AAI07767 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21K → E.1 Publication
Corresponds to variant rs6053 [ dbSNP | Ensembl ].
VAR_014169
Natural varianti39 – 10264Missing in New York-1. 1 Publication
VAR_002402Add
BLAST
Natural varianti44 – 441R → C in Christchurch-2, Seattle-1 and Ijmuiden. 1 Publication
Corresponds to variant rs121909616 [ dbSNP | Ensembl ].
VAR_002403
Natural varianti45 – 451G → R in Ise. 1 Publication
VAR_002404
Natural varianti74 – 741R → C in Nijmegen. 1 Publication
Corresponds to variant rs121909619 [ dbSNP | Ensembl ].
VAR_002405
Natural varianti95 – 951C → R in CAFBN; hypofibrinogenemia; heterozygous; decreased fibrinogen complex assembly; no effect on fibrinogen complex secretion. 1 Publication
VAR_072724
Natural varianti98 – 981A → T in DYSFIBRIN; fibrinogen Naples and Milano-2; associated with defective thrombin binding and thrombophilia. 1 Publication
Corresponds to variant rs121909620 [ dbSNP | Ensembl ].
VAR_002406
Natural varianti100 – 1001P → S.1 Publication
Corresponds to variant rs2227434 [ dbSNP | Ensembl ].
VAR_013091
Natural varianti170 – 1701N → H.1 Publication
Corresponds to variant rs2227409 [ dbSNP | Ensembl ].
VAR_013092
Natural varianti196 – 1961R → C in CAFBN; fibrinogen Longmont. 1 Publication
Corresponds to variant rs121909623 [ dbSNP | Ensembl ].
VAR_016908
Natural varianti202 – 2021L → Q in CAFBN. 1 Publication
Corresponds to variant rs121909624 [ dbSNP | Ensembl ].
VAR_072620
Natural varianti265 – 2651P → L.2 Publications
Corresponds to variant rs6054 [ dbSNP | Ensembl ].
VAR_013093
Natural varianti365 – 3651A → T in Pontoise-2.
Corresponds to variant rs121909617 [ dbSNP | Ensembl ].
VAR_002407
Natural varianti383 – 3831L → R in CAFBN; abolishes fibrinogen secretion. 1 Publication
Corresponds to variant rs121909621 [ dbSNP | Ensembl ].
VAR_016909
Natural varianti407 – 4071T → K in CAFBN; homozygous; heterozygous; no effect on fibrinogen complex assembly; impaired fibrinogen complex secretion. 1 Publication
VAR_072725
Natural varianti430 – 4301G → D in CAFBN; abolishes fibrinogen secretion. 1 Publication
Corresponds to variant rs121909622 [ dbSNP | Ensembl ].
VAR_016910
Natural varianti478 – 4781R → K in Baltimore-2. 3 Publications
Corresponds to variant rs4220 [ dbSNP | Ensembl ].
VAR_002408

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
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. Positions 88-488.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL2364709.
DrugBankiDB00364. Sucralfate.

PTM databases

iPTMnetiP02675.
PhosphoSiteiP02675.
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.
GeneCardsiFGB.
HGNCiHGNC:3662. FGB.
HPAiCAB008624.
HPA001900.
HPA001901.
MalaCardsiFGB.
MIMi134830. gene.
202400. phenotype.
616004. phenotype.
neXtProtiNX_P02675.
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

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.

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

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: September 7, 2016
This is version 200 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.