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P02675 (FIBB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibrinogen beta chain

Cleaved into the following 2 chains:

  1. Fibrinopeptide B
  2. Fibrinogen beta chain
Gene names
Name:FGB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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. Ref.19

Subcellular location

Secreted.

Domain

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.

Post-translational modification

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.

Involvement in disease

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.
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.

Sequence similarities

Contains 1 fibrinogen C-terminal domain.

Ontologies

Keywords
   Biological processBlood coagulation
Hemostasis
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainCoiled coil
Signal
   PTMDisulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

cellular response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

cellular response to leptin stimulus

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

protein polymerization

Inferred from electronic annotation. Source: InterPro

response to calcium ion

Inferred from direct assay PubMed 6777381. Source: BHF-UCL

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cell cortex

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 6777381. Source: BHF-UCL

external side of plasma membrane

Inferred from direct assay PubMed 6777381. Source: BHF-UCL

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 19996109PubMed 6777381. Source: BHF-UCL

fibrinogen complex

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

platelet alpha granule

Inferred from direct assay PubMed 6777381. Source: BHF-UCL

platelet alpha granule lumen

Traceable author statement. Source: Reactome

   Molecular_functionchaperone binding

Inferred from physical interaction PubMed 19996109. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P279584EBI-1034445,EBI-6377335From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Ref.10 Ref.11 Ref.12 Ref.13
Peptide31 – 4414Fibrinopeptide B Ref.13
PRO_0000009070
Chain45 – 491447Fibrinogen beta chain
PRO_0000009071

Regions

Domain232 – 488257Fibrinogen C-terminal
Region45 – 473Beta-chain polymerization, binding distal domain of another fibrin
Coiled coil157 – 22266 Potential

Sites

Site44 – 452Cleavage; by thrombin; to release fibrinopeptide B
Site152 – 1532Cleavage; by plasmin; to break down fibrin clots
Site160 – 1612Cleavage; by hementin; to prevent blood coagulation
Site163 – 1642Cleavage; by plasmin; to break down fibrin clots

Amino acid modifications

Modified residue311Pyrrolidone carboxylic acid
Glycosylation3941N-linked (GlcNAc...) Ref.11 Ref.21 Ref.22 Ref.23
Disulfide bond95Interchain (with C-55 in alpha chain) Ref.12 Ref.16 Ref.17 Ref.18
Disulfide bond106Interchain (with C-68 in alpha chain) Ref.12 Ref.16 Ref.17 Ref.18
Disulfide bond110Interchain (with C-45 in gamma chain) Ref.12 Ref.16 Ref.17 Ref.18
Disulfide bond223Interchain (with C-184 in alpha chain) Ref.12 Ref.16 Ref.17 Ref.18
Disulfide bond227Interchain (with C-161 in gamma chain) Ref.12 Ref.16 Ref.17 Ref.18
Disulfide bond231 ↔ 316 Ref.12 Ref.16 Ref.17 Ref.18
Disulfide bond241 ↔ 270 Ref.12 Ref.16 Ref.17 Ref.18
Disulfide bond424 ↔ 437 Ref.12 Ref.16 Ref.17 Ref.18

Natural variations

Natural variant21K → E. Ref.34
Corresponds to variant rs6053 [ dbSNP | Ensembl ].
VAR_014169
Natural variant39 – 10264Missing in New York-1.
VAR_002402
Natural variant441R → C in Christchurch-2, Seattle-1 and Ijmuiden. Ref.32
VAR_002403
Natural variant451G → R in Ise. Ref.30
VAR_002404
Natural variant741R → C in Nijmegen. Ref.32
VAR_002405
Natural variant981A → T in Naples and Milano-2; associated with defective thrombin binding and thrombophilia. Ref.31
VAR_002406
Natural variant1001P → S. Ref.4
Corresponds to variant rs2227434 [ dbSNP | Ensembl ].
VAR_013091
Natural variant1701N → H. Ref.4
Corresponds to variant rs2227409 [ dbSNP | Ensembl ].
VAR_013092
Natural variant1961R → C in congenital afibrinogenemia; variant Longmont. Ref.37
VAR_016908
Natural variant2651P → L. Ref.4 Ref.34
Corresponds to variant rs6054 [ dbSNP | Ensembl ].
VAR_013093
Natural variant3651A → T in Pontoise-2.
VAR_002407
Natural variant3831L → R in congenital afibrinogenemia; abolishes fibrinogen secretion. Ref.36
VAR_016909
Natural variant4301G → D in congenital afibrinogenemia; abolishes fibrinogen secretion. Ref.36
VAR_016910
Natural variant4781R → K in Baltimore-2. Ref.4 Ref.29 Ref.34
Corresponds to variant rs4220 [ dbSNP | Ensembl ].
VAR_002408

Experimental info

Sequence conflict138 – 1392SQ → QS AA sequence Ref.11
Sequence conflict138 – 1392SQ → QS AA sequence Ref.12
Sequence conflict145 – 1462FQ → QF AA sequence Ref.10
Sequence conflict145 – 1462FQ → QF AA sequence Ref.11
Sequence conflict145 – 1462FQ → QF AA sequence Ref.12
Sequence conflict1921P → A in AAA52429. Ref.1

Secondary structure

................................................................................ 491
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02675 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: B92FFB9976AB53C5

FASTA49155,928
        10         20         30         40         50         60 
MKRMVSWSFH KLKTMKHLLL LLLCVFLVKS QGVNDNEEGF FSARGHRPLD KKREEAPSLR 

        70         80         90        100        110        120 
PAPPPISGGG YRARPAKAAA TQKKVERKAP DAGGCLHADP DLGVLCPTGC QLQEALLQQE 

       130        140        150        160        170        180 
RPIRNSVDEL NNNVEAVSQT SSSSFQYMYL LKDLWQKRQK QVKDNENVVN EYSSELEKHQ 

       190        200        210        220        230        240 
LYIDETVNSN IPTNLRVLRS ILENLRSKIQ KLESDVSAQM EYCRTPCTVS CNIPVVSGKE 

       250        260        270        280        290        300 
CEEIIRKGGE TSEMYLIQPD SSVKPYRVYC DMNTENGGWT VIQNRQDGSV DFGRKWDPYK 

       310        320        330        340        350        360 
QGFGNVATNT DGKNYCGLPG EYWLGNDKIS QLTRMGPTEL LIEMEDWKGD KVKAHYGGFT 

       370        380        390        400        410        420 
VQNEANKYQI SVNKYRGTAG NALMDGASQL MGENRTMTIH NGMFFSTYDR DNDGWLTSDP 

       430        440        450        460        470        480 
RKQCSKEDGG GWWYNRCHAA NPNGRYYWGG QYTWDMAKHG TDDGVVWMNW KGSWYSMRKM 

       490 
SMKIRPFFPQ Q 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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].
[8]"Cloning of fibrinogen genes and their cDNA."
Chung D.W., Rixon M.W., Que B.G., Davie E.W.
Ann. N. Y. Acad. Sci. 408:449-456(1983) [PubMed] [Europe PMC] [Abstract]
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]"Covalent structure of fibrinogen."
Henschen A., Lottspeich F., Kehl M., Southan C.
Ann. N. Y. Acad. Sci. 408:28-43(1983) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLU-2; LEU-265 AND LYS-478.
[35]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
[36]"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.
[37]"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.
+Additional computationally mapped references.

Web resources

GeneReviews
SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Fibrinogen entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
BC106760 mRNA. Translation: AAI06761.1.
AH002694 Genomic DNA. Translation: AAA52445.1.
X05018 Genomic DNA. Translation: CAA28674.1.
PIRFGHUB. B43568.
RefSeqNP_001171670.1. NM_001184741.1.
NP_005132.2. NM_005141.4.
UniGeneHs.300774.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
M/N/S/T45-48[»]
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[»]
ProteinModelPortalP02675.
SMRP02675. Positions 88-488.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108535. 17 interactions.
DIPDIP-385N.
IntActP02675. 14 interactions.
STRING9606.ENSP00000306099.

Chemistry

BindingDBP02675.
ChEMBLCHEMBL2364709.
DrugBankDB00364. Sucralfate.

PTM databases

PhosphoSiteP02675.

Polymorphism databases

DMDM399492.

2D gel databases

DOSAC-COBS-2DPAGEP02675.
OGPP02675.
REPRODUCTION-2DPAGEIPI00298497.
P02675.
SWISS-2DPAGEP02675.
UCD-2DPAGEP02675.

Proteomic databases

PaxDbP02675.
PeptideAtlasP02675.
PRIDEP02675.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302068; ENSP00000306099; ENSG00000171564.
GeneID2244.
KEGGhsa:2244.
UCSCuc003ioa.4. human.

Organism-specific databases

CTD2244.
GeneCardsGC04P155484.
HGNCHGNC:3662. FGB.
HPACAB008624.
HPA001900.
HPA001901.
MIM134830. gene.
202400. phenotype.
neXtProtNX_P02675.
Orphanet98880. Familial afibrinogenemia.
98881. Familial dysfibrinogenemia.
248408. Familial hypodysfibrinogenemia.
101041. Familial hypofibrinogenemia.
PharmGKBPA163.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG277105.
HOGENOMHOG000059561.
HOVERGENHBG005707.
InParanoidP02675.
KOK03904.
OMATIHNGMF.
OrthoDBEOG7X9G60.
PhylomeDBP02675.
TreeFamTF336658.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP02675.
BgeeP02675.
CleanExHS_FGB.
GenevestigatorP02675.

Family and domain databases

Gene3D3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProIPR014716. 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]
PfamPF08702. Fib_alpha. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMSSF56496. SSF56496. 1 hit.
PROSITEPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFGB. human.
EvolutionaryTraceP02675.
GeneWikiFibrinogen_beta_chain.
GenomeRNAi2244.
NextBio9079.
PMAP-CutDBP02675.
PROP02675.
SOURCESearch...

Entry information

Entry nameFIBB_HUMAN
AccessionPrimary (citable) accession number: P02675
Secondary accession number(s): B2R7G3, Q3KPF2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 174 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM