P02675 (FIBB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fibrinogen beta chain

Cleaved into the following 2 chains:

1. Fibrinopeptide B
2. Fibrinogen beta chain

Gene names

Name:

FGB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	491 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Blood coagulation Hemostasis
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Coiled coil Signal
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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_component	blood microparticle Inferred from electronic annotation. Source: Compara cell cortex Inferred from electronic annotation. Source: Compara external side of plasma membrane Inferred from direct assay PubMed 6777381. Source: BHF-UCL fibrinogen complex Traceable author statement Ref.1. Source: ProtInc platelet alpha granule lumen Traceable author statement. Source: Reactome
Molecular_function	eukaryotic cell surface binding Inferred from direct assay PubMed 6777381. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

30

Ref.10 Ref.11 Ref.12 Ref.13

Peptide

31 – 44

14

Fibrinopeptide B Ref.13

PRO_0000009070

Chain

45 – 491

447

Fibrinogen beta chain

PRO_0000009071

Regions

Domain

232 – 488

257

Fibrinogen C-terminal

Region

45 – 47

3

Beta-chain polymerization, binding distal domain of another fibrin

Coiled coil

157 – 222

66

Potential

Sites

Site

44 – 45

2

Cleavage; by thrombin; to release fibrinopeptide B

Site

152 – 153

2

Cleavage; by plasmin; to break down fibrin clots

Site

160 – 161

2

Cleavage; by hementin; to prevent blood coagulation

Site

163 – 164

2

Cleavage; by plasmin; to break down fibrin clots

Amino acid modifications

Modified residue

31

1

Pyrrolidone carboxylic acid

Glycosylation

394

1

N-linked (GlcNAc...) Ref.11 Ref.21 Ref.22 Ref.23

Disulfide bond

95

Interchain (with C-55 in alpha chain) Ref.12 Ref.16 Ref.17 Ref.18

Disulfide bond

106

Interchain (with C-68 in alpha chain) Ref.12 Ref.16 Ref.17 Ref.18

Disulfide bond

110

Interchain (with C-45 in gamma chain) Ref.12 Ref.16 Ref.17 Ref.18

Disulfide bond

223

Interchain (with C-184 in alpha chain) Ref.12 Ref.16 Ref.17 Ref.18

Disulfide bond

227

Interchain (with C-161 in gamma chain) Ref.12 Ref.16 Ref.17 Ref.18

Disulfide bond

231 ↔ 316

Ref.12 Ref.16 Ref.17 Ref.18

Disulfide bond

241 ↔ 270

Ref.12 Ref.16 Ref.17 Ref.18

Disulfide bond

424 ↔ 437

Ref.12 Ref.16 Ref.17 Ref.18

Natural variations

Natural variant

2

1

K → E. Ref.34
Corresponds to variant rs6053 [ dbSNP | Ensembl ].

VAR_014169

Natural variant

39 – 102

64

Missing in New York-1.

VAR_002402

Natural variant

44

1

R → C in Christchurch-2, Seattle-1 and Ijmuiden. Ref.32

VAR_002403

Natural variant

45

1

G → R in Ise. Ref.30

VAR_002404

Natural variant

74

1

R → C in Nijmegen. Ref.32

VAR_002405

Natural variant

98

1

A → T in Naples and Milano-2; associated with defective thrombin binding and thrombophilia. Ref.31

VAR_002406

Natural variant

100

1

P → S. Ref.4
Corresponds to variant rs2227434 [ dbSNP | Ensembl ].

VAR_013091

Natural variant

170

1

N → H. Ref.4
Corresponds to variant rs2227409 [ dbSNP | Ensembl ].

VAR_013092

Natural variant

196

1

R → C in congenital afibrinogenemia; variant Longmont. Ref.37

VAR_016908

Natural variant

265

1

P → L. Ref.4 Ref.34
Corresponds to variant rs6054 [ dbSNP | Ensembl ].

VAR_013093

Natural variant

365

1

A → T in Pontoise-2.

VAR_002407

Natural variant

383

1

L → R in congenital afibrinogenemia; abolishes fibrinogen secretion. Ref.36

VAR_016909

Natural variant

430

1

G → D in congenital afibrinogenemia; abolishes fibrinogen secretion. Ref.36

VAR_016910

Natural variant

478

1

R → K in Baltimore-2. Ref.4 Ref.29 Ref.34
Corresponds to variant rs4220 [ dbSNP | Ensembl ].

VAR_002408

Experimental info

Sequence conflict

138 – 139

2

SQ → QS AA sequence Ref.11

Sequence conflict

138 – 139

2

SQ → QS AA sequence Ref.12

Sequence conflict

145 – 146

2

FQ → QF AA sequence Ref.10

Sequence conflict

145 – 146

2

FQ → QF AA sequence Ref.11

Sequence conflict

145 – 146

2

FQ → QF AA sequence Ref.12

Sequence conflict

192

1

P → A in AAA52429. Ref.1

Secondary structure

1

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491

Helix Strand Turn

Details...

Turn

100 – 102

3

Helix

109 – 145

37

Helix

147 – 167

21

Helix

172 – 180

9

Turn

182 – 189

8

Helix

190 – 222

33

Beta strand

224 – 226

3

Beta strand

233 – 235

3

Beta strand

238 – 240

3

Helix

241 – 246

6

Beta strand

253 – 257

5

Beta strand

261 – 263

3

Beta strand

266 – 271

6

Helix

274 – 276

3

Beta strand

279 – 288

10

Helix

296 – 301

6

Beta strand

302 – 304

3

Beta strand

306 – 308

3

Beta strand

311 – 315

5

Beta strand

321 – 323

3

Helix

326 – 334

9

Beta strand

335 – 337

3

Beta strand

339 – 345

7

Beta strand

347 – 349

3

Beta strand

351 – 361

11

Helix

364 – 366

3

Beta strand

370 – 379

10

Helix

382 – 385

4

Beta strand

388 – 390

3

Helix

392 – 396

5

Beta strand

404 – 407

4

Beta strand

408 – 410

3

Helix

420 – 422

3

Turn

424 – 428

5

Beta strand

435 – 437

3

Beta strand

439 – 441

3

Beta strand

448 – 451

4

Turn

454 – 456

3

Beta strand

457 – 461

5

Beta strand

464 – 467

4

Helix

468 – 471

4

Beta strand

473 – 475

3

Beta strand

478 – 485

8

Sequences

	Sequence		Length	Mass (Da)
	P02675 [UniParc]. Last modified July 1, 1993. Version 2. Checksum: B92FFB9976AB53C5	FASTA	491	55,928
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
[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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.

IPI

IPI00298497.

PIR

FGHUB. B43568.

RefSeq

NP_001171670.1. NM_001184741.1.
NP_005132.2. NM_005141.4.

UniGene

Hs.300774.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
			M/N/S/T	45-48	[»]
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	[»]

ProteinModelPortal

P02675.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-385N.

IntAct

P02675. 4 interactions.

STRING

9606.ENSP00000306099.

PTM databases

PhosphoSite

P02675.

Polymorphism databases

DMDM

399492.

2D gel databases

DOSAC-COBS-2DPAGE

P02675.

OGP

P02675.

REPRODUCTION-2DPAGE

IPI00298497.
P02675.

SWISS-2DPAGE

P02675.

UCD-2DPAGE

P02675.

Proteomic databases

PaxDb

P02675.

PeptideAtlas

P02675.

PRIDE

P02675.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000302068; ENSP00000306099; ENSG00000171564.

GeneID

2244.

KEGG

hsa:2244.

UCSC

uc003ioa.4. human.

Organism-specific databases

CTD

2244.

GeneCards

GC04P155484.

HGNC

HGNC:3662. FGB.

HPA

CAB008624.
HPA001900.
HPA001901.

MIM

134830. gene.
202400. phenotype.

neXtProt

NX_P02675.

Orphanet

98880. Familial afibrinogenemia.
98881. Familial dysfibrinogenemia.
248408. Familial hypodysfibrinogenemia.
101041. Familial hypofibrinogenemia.

PharmGKB

PA163.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG277105.

HOGENOM

HOG000059561.

HOVERGEN

HBG005707.

InParanoid

P02675.

KO

K03904.

OMA

TIHNGMF.

OrthoDB

EOG4WQ12K.

PhylomeDB

P02675.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P02675.

Bgee

P02675.

CleanEx

HS_FGB.

Genevestigator

P02675.

GermOnline

ENSG00000171564. Homo sapiens.

Family and domain databases

Gene3D

3.90.215.10. 1 hit.
4.10.530.10. 1 hit.

InterPro

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]

Pfam

PF08702. Fib_alpha. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]

SMART

SM00186. FBG. 1 hit.
[Graphical view]

SUPFAM

SSF56496. Fibrinogen_a/b/g_C. 1 hit.

PROSITE

PS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P02675.

ChEMBL

CHEMBL2048.

ChiTaRS

FGB. human.

DrugBank

DB00364. Sucralfate.

EvolutionaryTrace

P02675.

GenomeRNAi

2244.

NextBio

9079.

PMAP-CutDB

P02675.

SOURCE

Search...

Entry information

Entry name

FIBB_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 166 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.