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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: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation By similarity.

Sites

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

GO - Biological processi

  1. cellular response to interleukin-1 Source: Ensembl
  2. cellular response to leptin stimulus Source: Ensembl
  3. platelet activation Source: InterPro
  4. protein polymerization Source: InterPro
  5. response to calcium ion Source: Ensembl
  6. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

Enzyme and pathway databases

ReactomeiREACT_216309. Integrin cell surface interactions.

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. fibrinogen complex Source: InterPro
  5. platelet alpha granule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi213 – 213Interchain (with alpha chain) By similarity
Disulfide bondi217 – 217Interchain (with gamma chain) By similarity
Disulfide bondi221 ↔ 306 By similarity
Disulfide bondi231 ↔ 260 By similarity
Glycosylationi384 – 3841N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi414 ↔ 427 By similarity

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.
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.

Protein-protein interaction databases

IntActiQ8K0E8. 5 interactions.
MINTiMINT-1863241.

Structurei

3D structure databases

ProteinModelPortaliQ8K0E8.
SMRiQ8K0E8. Positions 78-479.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini222 – 478257Fibrinogen C-terminalAdd
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili149 – 21365 Reviewed predictionAdd
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.

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiNOG277105.
GeneTreeiENSGT00750000117251.
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

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MRHLWLLLLL CVFSVQTQAA DDDYDEPTDS LDARGHRPVD RRKEEPPSLR    50
PAPPPISGGG YRARPAKATA NQKKVERRPP DAGGCLHADT DMGVLCPTGC 100
TLQQTLLNQE RPIKSSIAEL NNNIQSVSDT SSVTFQYLTL LKDMWKKKQA 150
QVKENENVIN EYSSILEDQR LYIDETVNDN IPLNLRVLRS ILEDLRSKIQ 200
KLESDISAQM EYCRTPCTVS CNIPVVSGKE CEEIIRKGGE TSEMYLIQPD 250
TSIKPYRVYC DMKTENGGWT VIQNRQDGSV DFGRKWDPYK KGFGNIATNE 300
DAKKYCGLPG EYWLGNDKIS QLTRMGPTEL LIEMEDWKGD KVKAHYGGFT 350
VQNEASKYQV SVNKYKGTAG NALMDGASQL VGENRTMTIH NGMFFSTYDR 400
DNDGWVTTDP RKQCSKEDGG GWWYNRCHAA NPNGRYYWGG LYSWDMSKHG 450
TDDGVVWMNW KGSWYSMRRM SMKIRPFFPQ Q 481
Length:481
Mass (Da):54,753
Last modified:October 1, 2002 - v1
Checksum:i9902830CF708A155
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 ENSGT00750000117251.
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.

Miscellaneous databases

ChiTaRSi FGB. mouse.
NextBioi 363391.
PROi Q8K0E8.
SOURCEi Search...

Gene expression databases

Bgeei Q8K0E8.
CleanExi MM_FGB.
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: September 3, 2014
This is version 91 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

Similar proteinsi