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Q8K0E8

- FIBB_MOUSE

UniProt

Q8K0E8 - FIBB_MOUSE

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Protein

Fibrinogen beta chain

Gene

Fgb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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 via an ITGB3-dependent pathway. 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 immune response via both innate and T-cell mediated pathways.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei34 – 352Cleavage; by thrombin; to release fibrinopeptide BBy similarity

GO - Molecular functioni

  1. structural molecule activity Source: Ensembl

GO - Biological processi

  1. cell-matrix adhesion Source: Ensembl
  2. cellular response to interleukin-1 Source: Ensembl
  3. cellular response to leptin stimulus Source: Ensembl
  4. negative regulation of endothelial cell apoptotic process Source: Ensembl
  5. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  6. platelet aggregation Source: Ensembl
  7. positive regulation of ERK1 and ERK2 cascade Source: Ensembl
  8. positive regulation of exocytosis Source: Ensembl
  9. positive regulation of heterotypic cell-cell adhesion Source: Ensembl
  10. positive regulation of peptide hormone secretion Source: Ensembl
  11. positive regulation of protein secretion Source: Ensembl
  12. positive regulation of vasoconstriction Source: Ensembl
  13. protein polymerization Source: Ensembl
  14. response to calcium ion Source: Ensembl
  15. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiREACT_216309. Integrin cell surface interactions.
REACT_240371. p130Cas linkage to MAPK signaling for integrins.
REACT_246176. Integrin alphaIIb beta3 signaling.
REACT_259461. Common Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrinogen beta chain
Cleaved into the following 2 chains:
Gene namesi
Name:Fgb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:99501. Fgb.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: Ensembl
  2. cell cortex Source: MGI
  3. external side of plasma membrane Source: Ensembl
  4. extracellular vesicular exosome Source: Ensembl
  5. fibrinogen complex Source: Ensembl
  6. platelet alpha granule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Peptidei20 – 3415Fibrinopeptide BBy similarityPRO_0000009078Add
BLAST
Chaini35 – 481447Fibrinogen beta chainPRO_0000009077Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi213 – 213Interchain (with alpha chain)PROSITE-ProRule annotation
Disulfide bondi217 – 217Interchain (with gamma chain)PROSITE-ProRule annotation
Disulfide bondi221 ↔ 306PROSITE-ProRule annotation
Disulfide bondi231 ↔ 260PROSITE-ProRule annotation
Glycosylationi384 – 3841N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi414 ↔ 427PROSITE-ProRule annotation

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.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ8K0E8.
PaxDbiQ8K0E8.
PRIDEiQ8K0E8.

2D gel databases

REPRODUCTION-2DPAGEIPI00279079.
Q8K0E8.

PTM databases

PhosphoSiteiQ8K0E8.

Expressioni

Gene expression databases

BgeeiQ8K0E8.
CleanExiMM_FGB.
ExpressionAtlasiQ8K0E8. baseline and differential.
GenevestigatoriQ8K0E8.

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 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ8K0E8. 5 interactions.
MINTiMINT-1863241.

Structurei

3D structure databases

ProteinModelPortaliQ8K0E8.
SMRiQ8K0E8. Positions 78-479.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini222 – 478257Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 373Beta-chain polymerization, binding distal domain of another fibrinBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili149 – 21365Sequence AnalysisAdd
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 (By similarity).By similarity

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiNOG277105.
GeneTreeiENSGT00760000118809.
HOGENOMiHOG000059561.
HOVERGENiHBG005707.
InParanoidiQ8K0E8.
KOiK03904.
OMAiTIHNGMF.
OrthoDBiEOG7X9G60.
PhylomeDBiQ8K0E8.
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.
[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.

Q8K0E8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRHLWLLLLL CVFSVQTQAA DDDYDEPTDS LDARGHRPVD RRKEEPPSLR
60 70 80 90 100
PAPPPISGGG YRARPAKATA NQKKVERRPP DAGGCLHADT DMGVLCPTGC
110 120 130 140 150
TLQQTLLNQE RPIKSSIAEL NNNIQSVSDT SSVTFQYLTL LKDMWKKKQA
160 170 180 190 200
QVKENENVIN EYSSILEDQR LYIDETVNDN IPLNLRVLRS ILEDLRSKIQ
210 220 230 240 250
KLESDISAQM EYCRTPCTVS CNIPVVSGKE CEEIIRKGGE TSEMYLIQPD
260 270 280 290 300
TSIKPYRVYC DMKTENGGWT VIQNRQDGSV DFGRKWDPYK KGFGNIATNE
310 320 330 340 350
DAKKYCGLPG EYWLGNDKIS QLTRMGPTEL LIEMEDWKGD KVKAHYGGFT
360 370 380 390 400
VQNEASKYQV SVNKYKGTAG NALMDGASQL VGENRTMTIH NGMFFSTYDR
410 420 430 440 450
DNDGWVTTDP RKQCSKEDGG GWWYNRCHAA NPNGRYYWGG LYSWDMSKHG
460 470 480
TDDGVVWMNW KGSWYSMRRM SMKIRPFFPQ Q
Length:481
Mass (Da):54,753
Last modified:October 1, 2002 - v1
Checksum:i9902830CF708A155
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC031715 mRNA. Translation: AAH31715.1.
AF413205 mRNA. Translation: AAL02225.1.
CCDSiCCDS17432.1.
RefSeqiNP_862897.1. NM_181849.2.
UniGeneiMm.30063.

Genome annotation databases

EnsembliENSMUST00000048246; ENSMUSP00000039472; ENSMUSG00000033831.
GeneIDi110135.
KEGGimmu:110135.
UCSCiuc008pph.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC031715 mRNA. Translation: AAH31715.1 .
AF413205 mRNA. Translation: AAL02225.1 .
CCDSi CCDS17432.1.
RefSeqi NP_862897.1. NM_181849.2.
UniGenei Mm.30063.

3D structure databases

ProteinModelPortali Q8K0E8.
SMRi Q8K0E8. Positions 78-479.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8K0E8. 5 interactions.
MINTi MINT-1863241.

PTM databases

PhosphoSitei Q8K0E8.

2D gel databases

REPRODUCTION-2DPAGE IPI00279079.
Q8K0E8.

Proteomic databases

MaxQBi Q8K0E8.
PaxDbi Q8K0E8.
PRIDEi Q8K0E8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000048246 ; ENSMUSP00000039472 ; ENSMUSG00000033831 .
GeneIDi 110135.
KEGGi mmu:110135.
UCSCi uc008pph.1. mouse.

Organism-specific databases

CTDi 2244.
MGIi MGI:99501. Fgb.

Phylogenomic databases

eggNOGi NOG277105.
GeneTreei ENSGT00760000118809.
HOGENOMi HOG000059561.
HOVERGENi HBG005707.
InParanoidi Q8K0E8.
KOi K03904.
OMAi TIHNGMF.
OrthoDBi EOG7X9G60.
PhylomeDBi Q8K0E8.
TreeFami TF336658.

Enzyme and pathway databases

Reactomei REACT_216309. Integrin cell surface interactions.
REACT_240371. p130Cas linkage to MAPK signaling for integrins.
REACT_246176. Integrin alphaIIb beta3 signaling.
REACT_259461. Common Pathway.

Miscellaneous databases

NextBioi 363391.
PROi Q8K0E8.
SOURCEi Search...

Gene expression databases

Bgeei Q8K0E8.
CleanExi MM_FGB.
ExpressionAtlasi Q8K0E8. baseline and differential.
Genevestigatori Q8K0E8.

Family and domain databases

Gene3Di 3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProi IPR014716. 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 ]
Pfami PF08702. Fib_alpha. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view ]
SMARTi SM00186. FBG. 1 hit.
[Graphical view ]
SUPFAMi SSF56496. SSF56496. 1 hit.
PROSITEi PS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver.
  2. "Mouse fibrinogen B-beta-chain."
    Murakawa M., Freeman M.W.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 234-469.

Entry informationi

Entry nameiFIBB_MOUSE
AccessioniPrimary (citable) accession number: Q8K0E8
Secondary accession number(s): Q91ZP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 1, 2002
Last modified: November 26, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3