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UniProtKB - P02675 (FIBB_HUMAN)

Protein

Fibrinogen beta chain

Gene

FGB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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
  • signaling receptor binding Source: InterPro
  • structural molecule activity Source: BHF-UCL
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Biological processAdaptive 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
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
SIGNORiP02675

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrinogen beta chain
Cleaved into the following 2 chains:
Fibrinopeptide B
Fibrinogen beta chain
Gene namesi
Name:FGB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000171564.11
HGNCiHGNC:3662 FGB
MIMi134830 gene
neXtProtiNX_P02675

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Congenital afibrinogenemia (CAFBN)4 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 dbSNP:rs121909623EnsemblClinVar.1
Natural variantiVAR_072620202L → Q in CAFBN. 1 PublicationCorresponds to variant dbSNP:rs121909624EnsemblClinVar.1
Natural variantiVAR_016909383L → R in CAFBN; abolishes fibrinogen secretion. 1 PublicationCorresponds to variant dbSNP:rs121909621EnsemblClinVar.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 dbSNP:rs121909622EnsemblClinVar.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 dbSNP:rs121909620EnsemblClinVar.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
DrugBankiDB04919 Alfimeprase
DB00364 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...) asparagine6 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

EPDiP02675
PaxDbiP02675
PeptideAtlasiP02675
PRIDEiP02675
ProteomicsDBi51544

2D gel databases

DOSAC-COBS-2DPAGEiP02675
OGPiP02675
REPRODUCTION-2DPAGEiIPI00298497
P02675
SWISS-2DPAGEiP02675
UCD-2DPAGEiP02675

PTM databases

CarbonylDBiP02675
GlyConnecti157
159
iPTMnetiP02675
PhosphoSitePlusiP02675
SwissPalmiP02675
UniCarbKBiP02675

Miscellaneous databases

PMAP-CutDBiP02675

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000171564 Expressed in 108 organ(s), highest expression level in liver
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 Hepatitis C virus genotype 1a (isolate H).

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi108535, 129 interactors
ComplexPortaliCPX-1922 Fibrinogen
CORUMiP02675
DIPiDIP-385N
IntActiP02675, 16 interactors
MINTiP02675
STRINGi9606.ENSP00000306099

Structurei

Secondary structure

1491
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiKOG2579 Eukaryota
ENOG410ZYS4 LUCA
GeneTreeiENSGT00920000148942
HOGENOMiHOG000059561
HOVERGENiHBG005707
InParanoidiP02675
KOiK03904
OMAiTIHNGMF
OrthoDBiEOG091G03M1
PhylomeDBiP02675
TreeFamiTF336658

Family and domain databases

CDDicd00087 FReD, 1 hit
InterProiView protein in InterPro
IPR036056 Fibrinogen-like_C
IPR002181 Fibrinogen_a/b/g_C_dom
IPR012290 Fibrinogen_a/b/g_coil_dom
IPR037580 Fibrinogen_beta
IPR020837 Fibrinogen_CS
PANTHERiPTHR19143:SF332 PTHR19143:SF332, 1 hit
PfamiView protein in Pfam
PF08702 Fib_alpha, 1 hit
PF00147 Fibrinogen_C, 1 hit
SMARTiView protein in SMART
SM00186 FBG, 1 hit
SM01212 Fib_alpha, 1 hit
SUPFAMiSSF56496 SSF56496, 1 hit
PROSITEiView protein in PROSITE
PS00514 FIBRINOGEN_C_1, 1 hit
PS51406 FIBRINOGEN_C_2, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.iShow all

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

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D6REL8D6REL8_HUMAN
Fibrinogen beta chain
FGB
272Annotation score:
F8W6P4F8W6P4_HUMAN
Fibrinogen beta chain
FGB
45Annotation score:

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 → E1 PublicationCorresponds to variant dbSNP:rs6053EnsemblClinVar.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 dbSNP:rs121909616EnsemblClinVar.1
Natural variantiVAR_00240445G → R in Ise. 1 Publication1
Natural variantiVAR_00240574R → C in Nijmegen. 1 PublicationCorresponds to variant dbSNP:rs121909619EnsemblClinVar.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 dbSNP:rs121909620EnsemblClinVar.1
Natural variantiVAR_013091100P → S1 PublicationCorresponds to variant dbSNP:rs2227434Ensembl.1
Natural variantiVAR_013092170N → H1 PublicationCorresponds to variant dbSNP:rs2227409Ensembl.1
Natural variantiVAR_016908196R → C in CAFBN; fibrinogen Longmont. 1 PublicationCorresponds to variant dbSNP:rs121909623EnsemblClinVar.1
Natural variantiVAR_072620202L → Q in CAFBN. 1 PublicationCorresponds to variant dbSNP:rs121909624EnsemblClinVar.1
Natural variantiVAR_013093265P → L2 PublicationsCorresponds to variant dbSNP:rs6054EnsemblClinVar.1
Natural variantiVAR_002407365A → T in Pontoise-2. Corresponds to variant dbSNP:rs121909617EnsemblClinVar.1
Natural variantiVAR_016909383L → R in CAFBN; abolishes fibrinogen secretion. 1 PublicationCorresponds to variant dbSNP:rs121909621EnsemblClinVar.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 dbSNP:rs121909622EnsemblClinVar.1
Natural variantiVAR_002408478R → K in Baltimore-2. 3 PublicationsCorresponds to variant dbSNP:rs4220EnsemblClinVar.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

Similar proteinsi

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[»]
6ATZX-ray2.70E/F69-79[»]
6BIJX-ray2.10C69-81[»]
6BILX-ray2.40C69-81[»]
ProteinModelPortaliP02675
SMRiP02675
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108535, 129 interactors
ComplexPortaliCPX-1922 Fibrinogen
CORUMiP02675
DIPiDIP-385N
IntActiP02675, 16 interactors
MINTiP02675
STRINGi9606.ENSP00000306099

Chemistry databases

ChEMBLiCHEMBL2048
DrugBankiDB04919 Alfimeprase
DB00364 Sucralfate

PTM databases

CarbonylDBiP02675
GlyConnecti157
159
iPTMnetiP02675
PhosphoSitePlusiP02675
SwissPalmiP02675
UniCarbKBiP02675

Polymorphism and mutation databases

BioMutaiFGB
DMDMi399492

2D gel databases

DOSAC-COBS-2DPAGEiP02675
OGPiP02675
REPRODUCTION-2DPAGEiIPI00298497
P02675
SWISS-2DPAGEiP02675
UCD-2DPAGEiP02675

Proteomic databases

EPDiP02675
PaxDbiP02675
PeptideAtlasiP02675
PRIDEiP02675
ProteomicsDBi51544

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302068; ENSP00000306099; ENSG00000171564
GeneIDi2244
KEGGihsa:2244

Organism-specific databases

CTDi2244
DisGeNETi2244
EuPathDBiHostDB:ENSG00000171564.11
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
GeneTreeiENSGT00920000148942
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
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
SIGNORiP02675

Miscellaneous databases

ChiTaRSiFGB human
EvolutionaryTraceiP02675
GeneWikiiFibrinogen_beta_chain
GenomeRNAii2244
PMAP-CutDBiP02675
PROiPR:P02675
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000171564 Expressed in 108 organ(s), highest expression level in liver
CleanExiHS_FGB
ExpressionAtlasiP02675 baseline and differential
GenevisibleiP02675 HS

Family and domain databases

CDDicd00087 FReD, 1 hit
InterProiView protein in InterPro
IPR036056 Fibrinogen-like_C
IPR002181 Fibrinogen_a/b/g_C_dom
IPR012290 Fibrinogen_a/b/g_coil_dom
IPR037580 Fibrinogen_beta
IPR020837 Fibrinogen_CS
PANTHERiPTHR19143:SF332 PTHR19143:SF332, 1 hit
PfamiView protein in Pfam
PF08702 Fib_alpha, 1 hit
PF00147 Fibrinogen_C, 1 hit
SMARTiView protein in SMART
SM00186 FBG, 1 hit
SM01212 Fib_alpha, 1 hit
SUPFAMiSSF56496 SSF56496, 1 hit
PROSITEiView protein in PROSITE
PS00514 FIBRINOGEN_C_1, 1 hit
PS51406 FIBRINOGEN_C_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiFIBB_HUMAN
AccessioniPrimary (citable) accession number: P02675
Secondary accession number(s): A0JLR9
, B2R7G3, Q32Q65, Q3KPF2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1993
Last modified: September 12, 2018
This is version 218 of the entry and version 2 of the sequence. See 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
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