Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P02675

- FIBB_HUMAN

UniProt

P02675 - FIBB_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Fibrinogen beta chain

Gene

FGB

Organism
Homo sapiens (Human)
Status
Reviewed - 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

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

GO - Molecular functioni

  1. chaperone binding Source: BHF-UCL
  2. structural molecule activity Source: BHF-UCL

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. cell-matrix adhesion Source: BHF-UCL
  3. cellular protein complex assembly Source: BHF-UCL
  4. cellular response to interleukin-1 Source: Ensembl
  5. cellular response to leptin stimulus Source: Ensembl
  6. extracellular matrix organization Source: Reactome
  7. negative regulation of endothelial cell apoptotic process Source: BHF-UCL
  8. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
  9. platelet activation Source: Reactome
  10. platelet aggregation Source: BHF-UCL
  11. platelet degranulation Source: Reactome
  12. positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  13. positive regulation of exocytosis Source: BHF-UCL
  14. positive regulation of heterotypic cell-cell adhesion Source: BHF-UCL
  15. positive regulation of peptide hormone secretion Source: BHF-UCL
  16. positive regulation of protein secretion Source: BHF-UCL
  17. positive regulation of substrate adhesion-dependent cell spreading Source: BHF-UCL
  18. positive regulation of vasoconstriction Source: BHF-UCL
  19. protein polymerization Source: BHF-UCL
  20. response to calcium ion Source: BHF-UCL
  21. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiREACT_13552. Integrin cell surface interactions.
REACT_1439. Common Pathway.
REACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_15523. Integrin alphaIIb beta3 signaling.

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
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:3662. FGB.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. cell cortex Source: Ensembl
  3. cell surface Source: BHF-UCL
  4. external side of plasma membrane Source: BHF-UCL
  5. extracellular region Source: UniProtKB
  6. extracellular space Source: BHF-UCL
  7. extracellular vesicular exosome Source: UniProtKB
  8. fibrinogen complex Source: BHF-UCL
  9. plasma membrane Source: Reactome
  10. platelet alpha granule Source: BHF-UCL
  11. platelet alpha granule lumen Source: Reactome
  12. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Congenital afibrinogenemia (CAFBN) [MIM:202400]: Rare 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.2 Publications
Note: 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.

Keywords - Diseasei

Disease mutation

Organism-specific databases

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

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)
Disulfide bondi106 – 106Interchain (with C-68 in alpha chain)
Disulfide bondi110 – 110Interchain (with C-45 in gamma chain)
Disulfide bondi223 – 223Interchain (with C-184 in alpha chain)
Disulfide bondi227 – 227Interchain (with C-161 in gamma chain)
Disulfide bondi231 ↔ 316
Disulfide bondi241 ↔ 270
Glycosylationi394 – 3941N-linked (GlcNAc...)4 Publications
Disulfide bondi424 ↔ 437

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP02675.
PaxDbiP02675.
PeptideAtlasiP02675.
PRIDEiP02675.

2D gel databases

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

PTM databases

PhosphoSiteiP02675.

Miscellaneous databases

PMAP-CutDBP02675.

Expressioni

Gene expression databases

BgeeiP02675.
CleanExiHS_FGB.
ExpressionAtlasiP02675. baseline and differential.
GenevestigatoriP02675.

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 By similarity.By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi108535. 24 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 – 1023
Helixi109 – 14537
Helixi147 – 16721
Helixi172 – 1809
Turni182 – 1898
Helixi190 – 22233
Beta strandi224 – 2263
Beta strandi233 – 2353
Beta strandi238 – 2403
Helixi241 – 2466
Beta strandi253 – 2575
Beta strandi261 – 2633
Beta strandi266 – 2716
Helixi274 – 2763
Beta strandi279 – 28810
Helixi296 – 3016
Beta strandi302 – 3043
Beta strandi306 – 3083
Beta strandi311 – 3155
Beta strandi321 – 3233
Helixi326 – 3349
Beta strandi335 – 3373
Beta strandi339 – 3457
Beta strandi347 – 3493
Beta strandi351 – 36111
Helixi364 – 3663
Beta strandi370 – 37910
Helixi382 – 3854
Beta strandi388 – 3903
Helixi392 – 3965
Beta strandi404 – 4074
Beta strandi408 – 4103
Helixi420 – 4223
Turni424 – 4285
Beta strandi435 – 4373
Beta strandi439 – 4413
Beta strandi448 – 4514
Turni454 – 4563
Beta strandi457 – 4615
Beta strandi464 – 4674
Helixi468 – 4714
Beta strandi473 – 4753
Beta strandi478 – 4858

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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 – 22266Sequence 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.

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiNOG277105.
HOGENOMiHOG000059561.
HOVERGENiHBG005707.
InParanoidiP02675.
KOiK03904.
OMAiTIHNGMF.
OrthoDBiEOG7X9G60.
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.
[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 AAH07030.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1392SQ → QS AA sequence 1 PublicationCurated
Sequence conflicti138 – 1392SQ → QS AA sequence (PubMed:936108)Curated
Sequence conflicti145 – 1462FQ → QF AA sequence (PubMed:420779)Curated
Sequence conflicti145 – 1462FQ → QF AA sequence 1 PublicationCurated
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
VAR_002403
Natural varianti45 – 451G → R in Ise. 1 Publication
VAR_002404
Natural varianti74 – 741R → C in Nijmegen. 1 Publication
VAR_002405
Natural varianti98 – 981A → T in Naples and Milano-2; associated with defective thrombin binding and thrombophilia. 1 Publication
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 congenital afibrinogenemia; variant Longmont. 1 Publication
VAR_016908
Natural varianti265 – 2651P → L.2 Publications
Corresponds to variant rs6054 [ dbSNP | Ensembl ].
VAR_013093
Natural varianti365 – 3651A → T in Pontoise-2.
VAR_002407
Natural varianti383 – 3831L → R in congenital afibrinogenemia; abolishes fibrinogen secretion. 1 Publication
VAR_016909
Natural varianti430 – 4301G → D in congenital afibrinogenemia; abolishes fibrinogen secretion. 1 Publication
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:
EMBL
GenBank
DDBJ
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.
UCSCiuc003ioa.4. human.

Polymorphism databases

DMDMi399492.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS3786.1.
PIRi B43568. FGHUB.
RefSeqi NP_001171670.1. NM_001184741.1.
NP_005132.2. NM_005141.4.
UniGenei Hs.300774.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FZA X-ray 2.90 B/E 164-491 [» ]
1FZB X-ray 2.90 B/E 164-491 [» ]
1FZC X-ray 2.30 B/E 164-491 [» ]
1FZE X-ray 3.00 B/E 164-491 [» ]
1FZF X-ray 2.70 B/E 164-491 [» ]
M/N/S/T 45-48 [» ]
1FZG X-ray 2.50 B/E 164-491 [» ]
1LT9 X-ray 2.80 B/E 179-491 [» ]
1LTJ X-ray 2.80 B/E 179-491 [» ]
1N86 X-ray 3.20 B/E 164-491 [» ]
I/J 45-51 [» ]
1N8E X-ray 4.50 B/E 164-491 [» ]
1RE3 X-ray 2.45 B/E 179-491 [» ]
1RE4 X-ray 2.70 B/E 179-491 [» ]
1RF0 X-ray 2.81 B/E 179-491 [» ]
1RF1 X-ray 2.53 B/E 179-491 [» ]
2A45 X-ray 3.65 H/K 45-135 [» ]
2FFD X-ray 2.89 B/E 179-491 [» ]
2H43 X-ray 2.70 B/E 164-491 [» ]
2HLO X-ray 2.60 B/E 164-491 [» ]
2HOD X-ray 2.90 B/E/H/K 164-491 [» ]
2HPC X-ray 2.90 B/E/H/K 164-491 [» ]
2OYH X-ray 2.40 B/E 179-491 [» ]
2OYI X-ray 2.70 B/E 179-491 [» ]
2Q9I X-ray 2.80 B/E 164-491 [» ]
2XNX X-ray 3.30 B/E/H/K 164-491 [» ]
2XNY X-ray 7.50 B/E 164-491 [» ]
2Z4E X-ray 2.70 B/E 164-489 [» ]
3BVH X-ray 2.60 B/E 191-488 [» ]
3E1I X-ray 2.30 B/E 164-491 [» ]
3GHG X-ray 2.90 B/E/H/K 31-491 [» ]
3H32 X-ray 3.60 B/E 31-488 [» ]
3HUS X-ray 3.04 B/E 179-491 [» ]
ProteinModelPortali P02675.
SMRi P02675. Positions 88-488.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108535. 24 interactions.
DIPi DIP-385N.
IntActi P02675. 16 interactions.
STRINGi 9606.ENSP00000306099.

Chemistry

BindingDBi P02675.
ChEMBLi CHEMBL2364709.
DrugBanki DB00364. Sucralfate.

PTM databases

PhosphoSitei P02675.

Polymorphism databases

DMDMi 399492.

2D gel databases

DOSAC-COBS-2DPAGE P02675.
OGPi P02675.
REPRODUCTION-2DPAGE IPI00298497.
P02675.
SWISS-2DPAGE P02675.
UCD-2DPAGE P02675.

Proteomic databases

MaxQBi P02675.
PaxDbi P02675.
PeptideAtlasi P02675.
PRIDEi P02675.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000302068 ; ENSP00000306099 ; ENSG00000171564 .
GeneIDi 2244.
KEGGi hsa:2244.
UCSCi uc003ioa.4. human.

Organism-specific databases

CTDi 2244.
GeneCardsi GC04P155484.
HGNCi HGNC:3662. FGB.
HPAi CAB008624.
HPA001900.
HPA001901.
MIMi 134830. gene.
202400. phenotype.
neXtProti NX_P02675.
Orphaneti 98880. Familial afibrinogenemia.
98881. Familial dysfibrinogenemia.
248408. Familial hypodysfibrinogenemia.
101041. Familial hypofibrinogenemia.
PharmGKBi PA163.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG277105.
HOGENOMi HOG000059561.
HOVERGENi HBG005707.
InParanoidi P02675.
KOi K03904.
OMAi TIHNGMF.
OrthoDBi EOG7X9G60.
PhylomeDBi P02675.
TreeFami TF336658.

Enzyme and pathway databases

Reactomei REACT_13552. Integrin cell surface interactions.
REACT_1439. Common Pathway.
REACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_15523. Integrin alphaIIb beta3 signaling.

Miscellaneous databases

ChiTaRSi FGB. human.
EvolutionaryTracei P02675.
GeneWikii Fibrinogen_beta_chain.
GenomeRNAii 2244.
NextBioi 35459926.
PMAP-CutDB P02675.
PROi P02675.
SOURCEi Search...

Gene expression databases

Bgeei P02675.
CleanExi HS_FGB.
ExpressionAtlasi P02675. baseline and differential.
Genevestigatori P02675.

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. "Characterization of complementary deoxyribonucleic acid and genomic deoxyribonucleic acid for the beta chain of human fibrinogen."
    Chung D.W., Que B.G., Rixon M.W., Mace M. Jr., Davie E.W.
    Biochemistry 22:3244-3250(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. "Nucleotide sequences of the three genes coding for human fibrinogen."
    Chung D.W., Harris J.E., Davie E.W.
    Adv. Exp. Med. Biol. 281:39-48(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Nucleotide sequences of the three genes coding for human fibrinogen."
    Chung D.W., Harris J.E., Davie E.W.
    (In) Liu C.Y., Chien S. (eds.); Fibrinogen, thrombosis, coagulation and fibrinolysis, pp.39-48, Plenum Press, New York (1991)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. SeattleSNPs variation discovery resource
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-100; HIS-170; LEU-265 AND LYS-478.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary gland.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Liver.
  8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-60.
  9. "Characterization of the 5'-flanking region for the human fibrinogen beta gene."
    Huber P., Dalmon J., Courtois G., Laurent M., Assouline Z., Marguerie G.
    Nucleic Acids Res. 15:1615-1625(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38.
  10. "Amino acid sequence of the beta chain of human fibrinogen."
    Watt K.W.K., Takagi T., Doolittle R.F.
    Biochemistry 18:68-76(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-491, PYROGLUTAMATE FORMATION AT GLN-31.
  11. "Human fibrinogen: sequence, sulfur bridges, glycosylation and some structural variants."
    Henschen A., Lottspeich F., Southan C., Topfer-Petersen E.
    (In) Peeters H. (eds.); Protides of the biological fluids, Proc. 28th colloquium, pp.51-56, Pergamon Press, Oxford (1980)
    Cited for: PROTEIN SEQUENCE OF 31-491, GLYCOSYLATION AT ASN-394.
  12. "Disulfide bridges in NH2-terminal part of human fibrinogen."
    Blombaeck B., Hessel B., Hogg D.
    Thromb. Res. 8:639-658(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-148, DISULFIDE BONDS.
  13. "Studies on fibrinopeptides from primates."
    Blombaeck B., Blombaeck M., Grondahl N.J., Guthrie C., Hinton M.
    Acta Chem. Scand. 19:1788-1789(1965)
    Cited for: PROTEIN SEQUENCE OF 31-44.
  14. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 45-53.
    Tissue: Platelet.
  15. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 54-72; 164-178 AND 225-239, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  16. Cited for: REVIEW, DISULFIDE BONDS.
  17. "Primary structure of human fibrinogen. Characterization of disulfide-containing cyanogen-bromide fragments."
    Gaardlund B., Hessel B., Marguerie G., Murano G., Blombaeck B.
    Eur. J. Biochem. 77:595-610(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  18. "The structures of fibrinogen and fibrin."
    Doolittle R.F., Takagi T., Watt K.W.K., Bouma H. III, Cottrell B.A., Cassman K.G., Goldbaum D.M., Doolittle L.R., Friezner S.J.
    (In) Magnusson S., Ottesen M., Foltmann B., Dano K., Neurath H. (eds.); Regulatory proteolytic enzymes and their inhibitors, pp.163-172, Pergamon Press, New York (1978)
    Cited for: DISULFIDE BONDS.
  19. "Fibrinogen and fibrin."
    Doolittle R.F.
    Annu. Rev. Biochem. 53:195-229(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, ELECTRON MICROSCOPY, POLYMERIZATION, LIGANDS.
  20. "The interaction of fibulin-1 with fibrinogen. A potential role in hemostasis and thrombosis."
    Tran H., Tanaka A., Litvinovich S.V., Medved L.V., Haudenschild C.C., Argraves W.S.
    J. Biol. Chem. 270:19458-19464(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FBLN1.
  21. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-394.
    Tissue: Plasma.
  22. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
    Lewandrowski U., Moebius J., Walter U., Sickmann A.
    Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-394.
    Tissue: Platelet.
  23. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-394.
    Tissue: Liver.
  24. "A unique proteolytic fragment of human fibrinogen containing the A alpha COOH-terminal domain of the native molecule."
    Kirschbaum N.E., Budzynski A.Z.
    J. Biol. Chem. 265:13669-13676(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY HEMENTIN AND PLASMIN.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin."
    Spraggon G., Everse S.J., Doolittle R.F.
    Nature 389:455-462(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 164-491.
  27. "Crystal structure of fragment double-D from human fibrin with two different bound ligands."
    Everse S.J., Spraggon G., Veerapandian L., Riley M., Doolittle R.F.
    Biochemistry 37:8637-8642(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 164-491.
  28. "Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide."
    Everse S.J., Spraggon G., Veerapandian L., Doolittle R.F.
    Biochemistry 38:2941-2946(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 164-491.
  29. "A polymorphism at B beta 448 of fibrinogen identified during structural studies of fibrinogen Baltimore II."
    Schmelzer C.H., Ebert R.F., Bell W.R.
    Thromb. Res. 52:173-177(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT BALTIMORE-2 LYS-478.
  30. "A new congenital abnormal fibrinogen Ise characterized by the replacement of B beta glycine-15 by cysteine."
    Yoshida N., Wada H., Morita K., Hirata H., Matsuda M., Yamazumi K., Asakura S., Shirakawa S.
    Blood 77:1958-1963(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ISE ARG-45.
  31. "Molecular basis of fibrinogen Naples associated with defective thrombin binding and thrombophilia. Homozygous substitution of B beta 68 Ala-->Thr."
    Koopman J., Haverkate F., Lord S.T., Grimbergen J., Mannucci P.M.
    J. Clin. Invest. 90:238-244(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT NAPLES THR-98.
  32. "Abnormal fibrinogens IJmuiden (B beta Arg14-->Cys) and Nijmegen (B beta Arg44-->Cys) form disulfide-linked fibrinogen-albumin complexes."
    Koopman J., Haverkate F., Grimbergen J., Engesser L., Novakova I., Kerst A.F.J.A., Lord S.T.
    Proc. Natl. Acad. Sci. U.S.A. 89:3478-3482(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS IJMUIDEN CYS-44 AND NIJMEGEN CYS-74.
  33. "Characterization of fibrinogen New York 1. A dysfunctional fibrinogen with a deletion of B beta(9-72) corresponding exactly to exon 2 of the gene."
    Liu C.Y., Koehn J.A., Morgan F.J.
    J. Biol. Chem. 260:4390-4396(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT NEW YORK-1 39-GLY--LEU-102 DEL.
  34. Cited for: VARIANTS GLU-2; LEU-265 AND LYS-478.
  35. "Missense mutations in the human beta fibrinogen gene cause congenital afibrinogenemia by impairing fibrinogen secretion."
    Duga S., Asselta R., Santagostino E., Zeinali S., Simonic T., Malcovati M., Mannucci P.M., Tenchini M.L.
    Blood 95:1336-1341(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CONGENITAL AFIBRINOGENEMIA ARG-383 AND ASP-430.
  36. "The impaired polymerization of fibrinogen Longmont (Bbeta166Arg-->Cys) is not improved by removal of disulfide-linked dimers from a mixture of dimers and cysteine-linked monomers."
    Lounes K.C., Lefkowitz J.B., Henschen-Edman A.H., Coates A.I., Hantgan R.R., Lord S.T.
    Blood 98:661-666(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CONGENITAL AFIBRINOGENEMIA CYS-196.

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: October 29, 2014
This is version 180 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

External Data

Dasty 3