Reviewed, UniProtKB/Swiss-Prot P02679 (FIBG_HUMAN)

Names and origin

Protein names

Recommended name:
    Fibrinogen gamma chain

Gene names

Name:	FGG
ORF Names:	PRO2061

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	453 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.
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. Sulfation of C-terminal tyrosines increases affinity for thrombin.
Involvement in disease	Defects in FGG are a cause of thrombophilia. Defects in FGG are a cause of congenital afibrinogenemia [MIM:202400]. It is a rare autosomal recessive disorder characterized by complete absence of detectable fibrinogen.
Miscellaneous	The gamma-chain carries the main binding site for the platelet receptor.
Sequence similarities	Contains 1 fibrinogen C-terminal domain.

Ontologies

Keywords
Biological process	Blood coagulation
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Coiled coil Signal
Ligand	Calcium
PTM	Disulfide bond Glycoprotein Isopeptide bond Sulfation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	platelet activation Inferred from electronic annotation. Source: InterPro protein polymerization Inferred from electronic annotation. Source: InterPro response to calcium ion Inferred from direct assay. Source: UniProtKB signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	external side of plasma membrane Inferred from direct assay. Source: UniProtKB fibrinogen complex Ref.53 Traceable author statement. Source: ProtInc platelet alpha granule lumen Inferred from Experiment. Source: Reactome
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW eukaryotic cell surface binding Inferred from direct assay. Source: UniProtKB protein binding, bridging Inferred from electronic annotation. Source: InterPro receptor binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Gamma-B (identifier: P02679-1)

Also known as: Gamma';

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Present in about 10% of the fibrinogen molecules in plasma but absent from those in the platelets.

Isoform Gamma-A (identifier: P02679-2)

The sequence of this isoform differs from the canonical sequence as follows:
     434-453: VRPEHPAETEYDSLYPEDDL → AGDV

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Ref.6

Chain

27 – 453

427

Fibrinogen gamma chain

PRO_0000009099

Regions

Domain

170 – 416

247

Fibrinogen C-terminal

Calcium binding

341 – 355

15

Ref.27

Region

400 – 422

23

Gamma-chain polymerization, binding amino end of another fibrin alpha chain

Region

423 – 437

15

Platelet aggregation and Staphylococcus clumping

Amino acid modifications

Modified residue

444

1

Sulfotyrosine

Modified residue

448

1

Sulfotyrosine

Glycosylation

78

1

N-linked (GlcNAc...) Ref.29 Ref.30 Ref.31 Ref.32

Glycosylation

334

1

N-linked (GlcNAc...); in variant Asahi

Disulfide bond

34

Interchain (with C-35) Ref.16 Ref.12 Ref.18 Ref.19

Disulfide bond

35

Interchain (with C-34) Ref.16 Ref.12 Ref.18 Ref.19

Disulfide bond

45

Interchain (with C-110 in beta chain) Ref.16 Ref.12 Ref.18 Ref.19

Disulfide bond

49

Interchain (with C-64 in alpha chain) Ref.16 Ref.12 Ref.18 Ref.19

Disulfide bond

161

Interchain (with C-227 in beta chain) Ref.16 Ref.12 Ref.18 Ref.19

Disulfide bond

165

Interchain (with C-180 in alpha chain) Ref.16 Ref.12 Ref.18 Ref.19

Disulfide bond

179 ↔ 208

Ref.16 Ref.12 Ref.18 Ref.19

Disulfide bond

352 ↔ 365

Ref.16 Ref.12 Ref.18 Ref.19

Cross-link

424

Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-432)

Cross-link

432

Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424)

Natural variations

Alternative sequence

434 – 453

20

VRPEH…PEDDL → AGDV in isoform Gamma-A.

VSP_001537

Natural variant

77

1

E → G: dbSNP rs11551835.

VAR_049066

Natural variant

140

1

Y → H: dbSNP rs2066870. Ref.4

VAR_033930

Natural variant

191

1

G → R in Milano-12. dbSNP rs6063.

VAR_014170

Natural variant

301

1

R → C in Tochigi/Osaka-2/Milano-5/Villajoyosa.

VAR_002409

Natural variant

301

1

R → H in Bergamo-2/Essen/Haifa/Osaka-3/Perugia/Saga/Barcelona-3/Barcelona-4.

VAR_002410

Natural variant

318

1

G → V in Baltimore-1; impaired polymerization.

VAR_002411

Natural variant

334

1

N → I in Baltimore-3; impaired polymerization.

VAR_002413

Natural variant

334

1

N → K in Kyoto-1; causes accelerated cleavage by plasmin.

VAR_002412

Natural variant

335

1

G → D in Hillsborough; prolonged thrombin clotting time.

VAR_015853

Natural variant

336

1

M → T in Asahi; impaired polymerization.

VAR_002414

Natural variant

345 – 346

2

Missing in Vlissingen; defective calcium binding and impaired polymerization.

VAR_002415

Natural variant

355

1

Q → R in Nagoya-1; impaired polymerization.

VAR_002416

Natural variant

356

1

D → V in Milano-1; impaired polymerization.

VAR_002418

Natural variant

356

1

D → Y in Kyoto-3; impaired polymerization.

VAR_002417

Natural variant

363

1

N → K in Bern-1; impaired polymerization.

VAR_002419

Natural variant

377

1

G → VMCGEALPMLKDPCYS in Paris-1; impaired polymerization.

VAR_002420

Natural variant

384

1

S → C in Milano-7; impaired polymerization.

VAR_002421

Natural variant

401

1

R → G in Osaka-5.

VAR_002422

Natural variant

410

1

M → V: dbSNP rs6061. Ref.59

VAR_014171

Experimental info

Sequence conflict

114

1

K → I in AAB59530. Ref.2

Sequence conflict

114

1

K → I in AAB59531. Ref.2

Sequence conflict

435

1

R → Y AA sequence Ref.15

Sequence conflict

448

1

Y → R AA sequence Ref.15

Secondary structure

1

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453

Helix Strand Turn

Details...

Turn

115 – 118

4

Turn

124 – 128

5

Helix

129 – 160

32

Beta strand

166 – 168

3

Beta strand

171 – 178

8

Helix

179 – 184

6

Beta strand

191 – 195

5

Beta strand

204 – 210

7

Beta strand

216 – 226

11

Helix

234 – 239

6

Helix

256 – 264

9

Helix

265 – 267

3

Beta strand

270 – 277

8

Beta strand

283 – 290

8

Helix

296 – 298

3

Beta strand

305 – 309

5

Helix

315 – 317

3

Beta strand

322 – 324

3

Helix

327 – 331

5

Beta strand

346 – 350

5

Helix

352 – 356

5

Beta strand

363 – 365

3

Beta strand

367 – 369

3

Turn

382 – 384

3

Beta strand

385 – 387

3

Beta strand

392 – 395

4

Turn

396 – 398

3

Beta strand

406 – 414

9

Beta strand

420 – 424

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform Gamma-B (Gamma') [UniParc]. Last modified April 16, 2002. Version 3. Checksum: 1787204904E0D4BB	FASTA	453	51,512
	10 20 30 40 50 60 MSWSLHPRNL ILYFYALLFL SSTCVAYVAT RDNCCILDER FGSYCPTTCG IADFLSTYQT 70 80 90 100 110 120 KVDKDLQSLE DILHQVENKT SEVKQLIKAI QLTYNPDESS KPNMIDAATL KSRKMLEEIM 130 140 150 160 170 180 KYEASILTHD SSIRYLQEIY NSNNQKIVNL KEKVAQLEAQ CQEPCKDTVQ IHDITGKDCQ 190 200 210 220 230 240 DIANKGAKQS GLYFIKPLKA NQQFLVYCEI DGSGNGWTVF QKRLDGSVDF KKNWIQYKEG 250 260 270 280 290 300 FGHLSPTGTT EFWLGNEKIH LISTQSAIPY ALRVELEDWN GRTSTADYAM FKVGPEADKY 310 320 330 340 350 360 RLTYAYFAGG DAGDAFDGFD FGDDPSDKFF TSHNGMQFST WDNDNDKFEG NCAEQDGSGW 370 380 390 400 410 420 WMNKCHAGHL NGVYYQGGTY SKASTPNGYD NGIIWATWKT RWYSMKKTTM KIIPFNRLTI 430 440 450 GEGQQHHLGG AKQVRPEHPA ETEYDSLYPE DDL
	Isoform Gamma-A. Checksum: 3D73A7BC1E71381B	FASTA	437	49,497
	10 20 30 40 50 60 MSWSLHPRNL ILYFYALLFL SSTCVAYVAT RDNCCILDER FGSYCPTTCG IADFLSTYQT 70 80 90 100 110 120 KVDKDLQSLE DILHQVENKT SEVKQLIKAI QLTYNPDESS KPNMIDAATL KSRKMLEEIM 130 140 150 160 170 180 KYEASILTHD SSIRYLQEIY NSNNQKIVNL KEKVAQLEAQ CQEPCKDTVQ IHDITGKDCQ 190 200 210 220 230 240 DIANKGAKQS GLYFIKPLKA NQQFLVYCEI DGSGNGWTVF QKRLDGSVDF KKNWIQYKEG 250 260 270 280 290 300 FGHLSPTGTT EFWLGNEKIH LISTQSAIPY ALRVELEDWN GRTSTADYAM FKVGPEADKY 310 320 330 340 350 360 RLTYAYFAGG DAGDAFDGFD FGDDPSDKFF TSHNGMQFST WDNDNDKFEG NCAEQDGSGW 370 380 390 400 410 420 WMNKCHAGHL NGVYYQGGTY SKASTPNGYD NGIIWATWKT RWYSMKKTTM KIIPFNRLTI 430 GEGQQHHLGG AKQAGDV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a complementary deoxyribonucleic acid coding for the gamma chain of human fibrinogen." Chung D.W., Chan W.-Y., Davie E.W. Biochemistry 22:3250-3256(1983) [PubMed: 6688357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]	"Nucleotide sequence of the gene for the gamma chain of human fibrinogen." Rixon M.W., Chung D.W., Davie E.W. Biochemistry 24:2077-2086(1985) [PubMed: 2990550] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS GAMMA-A AND GAMMA-B).
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GAMMA-A AND GAMMA-B). Tissue: Liver.
[4]	"Functional prediction of the coding sequences of 33 new genes deduced by analysis of cDNA clones from human fetal liver." Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Bi J., Zhang Y., Liu M., He F. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-A). Tissue: Fetal liver.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-A).
[6]	SeattleSNPs variation discovery resource Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-140 AND ARG-191.
[7]	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].
[8]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-A). Tissue: Skeletal muscle.
[9]	"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 27-437.
[10]	"Evidence for the selective association of a subpopulation of GPIIb-IIIa with the actin cytoskeletons of thrombin-activated platelets." Bertagnolli M.E., Beckerle M.C. J. Cell Biol. 121:1329-1342(1993) [PubMed: 8509453] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-41. Tissue: Platelet.
[11]	"Polymorphism of the human gamma chain fibrinogen gene." Marchetti L., Zanelli T., Malcovati M., Tenchini M.L. DNA Seq. 1:419-422(1991) [PubMed: 1685103] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 75-286. Tissue: Liver.
[12]	"Isolation and characterisation of cDNA clones for the A alpha- and gamma-chains of human fibrinogen." Imam A.M.A., Eaton M.A.W., Williamson R., Humphries S. Nucleic Acids Res. 11:7427-7434(1983) [PubMed: 6689067] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 209-270.
[13]	"Structure of the human gamma-fibrinogen gene. Alternate mRNA splicing near the 3' end of the gene produces gamma A and gamma B forms of gamma-fibrinogen." Fornace A.J. Jr., Cummings D.E., Comeau C.M., Kant J.A., Crabtree G.R. J. Biol. Chem. 259:12826-12830(1984) [PubMed: 6092346] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 285-437 (ISOFORMS GAMMA-A AND GAMMA-B).
[14]	"Abnormal polymerization and normal binding of plasminogen and t-PA in three new dysfibrinogenaemias: Barcelona III and IV (gamma Arg 275-->His) and Villajoyosa (gamma Arg 275-->Cys)." Borrell M., Gari M., Coll I., Vallve C., Tirado I., Soria J.M., Sala N., Munoz C., Oliver A., Garcia A. Blood Coagul. Fibrinolysis 6:198-206(1995) [PubMed: 7654933] [Abstract] Cited for: PROTEIN SEQUENCE OF 291-310, VARIANTS BARCELONA-3/BARCELONA-4 HIS-301 AND VILLAJOYOSA CYS-301. Tissue: Blood.
[15]	"Carboxy-terminal amino acid sequence of a human fibrinogen gamma-chain variant (gamma')." Wolfenstein-Todel C., Mosesson M.W. Biochemistry 20:6146-6149(1981) [PubMed: 7306501] [Abstract] Cited for: PROTEIN SEQUENCE OF 411-453 (ISOFORM GAMMA-B).
[16]	"Covalent structure of fibrinogen." Henschen A., Lottspeich F., Kehl M., Southan C. Ann. N. Y. Acad. Sci. 408:28-43(1983) [PubMed: 6575689] [Abstract] Cited for: REVIEW, DISULFIDE BONDS.
[17]	"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.
[18]	"Disulfide bridges in NH2-terminal part of human fibrinogen." Blombaeck B., Hessel B., Hogg D. Thromb. Res. 8:639-658(1976) [PubMed: 936108] [Abstract] Cited for: DISULFIDE BONDS.
[19]	"Dimeric half-molecules of human fibrinogen are joined through disulfide bonds in an antiparallel orientation." Hoeprich P.D., Doolittle R.F. Biochemistry 22:2049-2055(1983) [PubMed: 6860649] [Abstract] Cited for: QUATERNARY STRUCTURE, DISULFIDE BONDS.
[20]	"Recombinant human fibrinogen and sulfation of the gamma' chain." Farrel D.H., Mulvihill E.R., Huang S., Chung D.W., Davie E.W. Biochemistry 30:9414-9420(1991) [PubMed: 1892842] [Abstract] Cited for: SULFATION.
[21]	"The amino acid sequence in fibrin responsible for high affinity thrombin binding." Meh D.A., Siebenlist K.R., Brennan S.O., Holyst T., Mosesson M.W. Thromb. Haemost. 85:470-474(2001) [PubMed: 11307817] [Abstract] Cited for: SULFATION AT TYR-444 AND TYR-448.
[22]	"Fibrinogen and fibrin." Doolittle R.F. Annu. Rev. Biochem. 53:195-229(1984) [PubMed: 6383194] [Abstract] Cited for: REVIEW, ELECTRON MICROSCOPY, POLYMERIZATION, LIGANDS.
[23]	"Localization of a fibrin gamma-chain polymerization site within segment Thr-374 to Glu-396 of human fibrinogen." Horwitz B.H., Varadi A., Scheraga H.A. Proc. Natl. Acad. Sci. U.S.A. 81:5980-5984(1984) [PubMed: 6592597] [Abstract] Cited for: POLYMERIZATION SITE.
[24]	"Localization of a fibrin polymerization site." Olexa S.A., Budzynski A.Z. J. Biol. Chem. 256:3544-3549(1981) [PubMed: 6451630] [Abstract] Cited for: POLYMERIZATION SITE.
[25]	"Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the gamma chain." Kloczewiak M., Timmons S., Lukas T.J., Hawiger J. Biochemistry 23:1767-1774(1984) [PubMed: 6326808] [Abstract] Cited for: PLATELET AGGREGATION SITE.
[26]	"Evidence that three adhesive proteins interact with a common recognition site on activated platelets." Plow E.F., Srouji A.H., Meyer D., Marguerie G., Ginsberg M.H. J. Biol. Chem. 259:5388-5391(1984) [PubMed: 6325435] [Abstract] Cited for: PLATELET AGGREGATION SITE.
[27]	"Localization of a fibrinogen calcium binding site between gamma-subunit positions 311 and 336 by terbium fluorescence." Dang C.V., Ebert R.F., Bell W.R. J. Biol. Chem. 260:9713-9719(1985) [PubMed: 3160702] [Abstract] Cited for: CALCIUM-BINDING SITE.
[28]	"Human plasma fibrinogen heterogeneity: evidence for an extended carboxyl-terminal sequence in a normal gamma chain variant (gamma')." Wolfenstein-Todel C., Mosesson M.W. Proc. Natl. Acad. Sci. U.S.A. 77:5069-5073(1980) [PubMed: 6933547] [Abstract] Cited for: CHROMATOGRAPHIC COMPARISON OF GAMMA-A AND GAMMA-B CHAINS.
[29]	"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry." Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R. Proteomics 4:454-465(2004) [PubMed: 14760718] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78, MASS SPECTROMETRY. Tissue: Plasma.
[30]	"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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78, MASS SPECTROMETRY. Tissue: Plasma.
[31]	"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: 16263699] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78, MASS SPECTROMETRY. Tissue: Platelet.
[32]	"Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry." Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F. Proteomics 8:3833-3847(2008) [PubMed: 18780401] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78, MASS SPECTROMETRY. Tissue: Milk.
[33]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78, MASS SPECTROMETRY. Tissue: Liver.
[34]	"Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen." Yee V.C., Pratt K.P., Cote H.C.F., le Trong I., Chung D.W., Davie E.W., Stenkamp R.E., Teller D.C. Structure 5:125-138(1997) [PubMed: 9016719] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 169-437.
[35]	"The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro." Pratt K.P., Cote H.C.F., Chung D.W., Stenkamp R.E., Davie E.W. Proc. Natl. Acad. Sci. U.S.A. 94:7176-7181(1997) [PubMed: 9207064] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 169-437.
[36]	"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: 9333233] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 114-432.
[37]	"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: 9628725] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 114-432.
[38]	"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: 10074346] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 114-432.
[39]	"A gamma methionine-310 to threonine substitution and consequent N-glycosylation at gamma asparagine-308 identified in a congenital dysfibrinogenemia associated with posttraumatic bleeding, fibrinogen Asahi." Yamazumi K., Shimura K., Terukina S., Takahashi N., Matsuda M. J. Clin. Invest. 83:1590-1597(1989) [PubMed: 2496144] [Abstract] Cited for: VARIANT ASAHI THR-336.
[40]	"Gene analyses of abnormal fibrinogens with a mutation in the gamma chain." Mimuro J., Muramatsu S., Maekawa H., Sakata Y., Kaneko M., Yoshitake S., Okuma M., Ito Y., Takeda Y., Matsuda M. Int. J. Hematol. 56:129-134(1992) [PubMed: 1421174] [Abstract] Cited for: VARIANTS OSAKA-2 CYS-301; KYOTO-1 LYS-334; ASAHI THR-336 AND KYOTO-3 TYR-356.
[41]	"Fibrinogen Baltimore I: polymerization defect associated with a gamma 292Gly-->Val (GGC-->GTC) mutation." Bantia S., Mane S.M., Bell W.R., Dang C.V. Blood 76:2279-2283(1990) [PubMed: 2257302] [Abstract] Cited for: VARIANT BALTIMORE-1 VAL-318.
[42]	"Polymerization defect of fibrinogen Baltimore III due to a gamma Asn308-->Ile mutation." Bantia S., Bell W.R., Dang C.V. Blood 75:1659-1663(1990) [PubMed: 2328317] [Abstract] Cited for: VARIANT BALTIMORE-3 ILE-334.
[43]	"Fibrinogen Bern I: substitution gamma 337 Asn-->Lys is responsible for defective fibrin monomer polymerization." Steinmann C., Reber P., Jungo M., Laemmle B., Heinemann G., Wermuth B., Furlan M. Blood 82:2104-2108(1993) [PubMed: 8400260] [Abstract] Cited for: VARIANT BERN-1 LYS-363.
[44]	"Characterization of an apparently lower molecular weight gamma-chain variant in fibrinogen Kyoto I. The replacement of gamma-asparagine 308 by lysine which causes accelerated cleavage of fragment D1 by plasmin and the generation of a new plasmin cleavage site." Yoshida N., Terukina S., Okuma M., Moroi M., Aoki N., Matsuda M. J. Biol. Chem. 263:13848-13856(1988) [PubMed: 2971046] [Abstract] Cited for: VARIANT KYOTO-1 LYS-334.
[45]	"Fibrinogen Kyoto III: a congenital dysfibrinogen with a gamma aspartic acid-330 to tyrosine substitution manifesting impaired fibrin monomer polymerization." Terukina S., Yamazumi K., Okamoto K., Yamashita H., Ito Y., Matsuda M. Blood 74:2681-2687(1989) [PubMed: 2819242] [Abstract] Cited for: VARIANT KYOTO-3 TYR-356.
[46]	"Characterization of fibrinogen Milano I: amino acid exchange gamma 330 Asp-->Val impairs fibrin polymerization." Reber P., Furlan M., Rupp C., Kehl M., Henschen A., Mannucci P.M., Beck E.A. Blood 67:1751-1756(1986) [PubMed: 3708159] [Abstract] Cited for: VARIANT MILANO-1 VAL-356.
[47]	"Fibrinogen Milano V: a congenital dysfibrinogenaemia with a gamma 275 Arg-->Cys substitution." Steinmann C., Boegli C., Jungo M., Laemmle B., Heinemann G., Wermuth B., Redaelli R., Baudo F., Furlan M. Blood Coagul. Fibrinolysis 5:463-471(1994) [PubMed: 7841300] [Abstract] Cited for: VARIANT MILANO-5 CYS-301.
[48]	"A new substitution, gamma 358 Ser-->Cys, in fibrinogen Milano VII causes defective fibrin polymerization." Steinmann C., Boegli C., Jungo M., Laemmle B., Heinemann G., Wermuth B., Redaelli R., Baudo F., Furlan M. Blood 84:1874-1880(1994) [PubMed: 8080993] [Abstract] Cited for: VARIANT MILANO-7 CYS-384.
[49]	"Fibrinogen Nagoya, a replacement of glutamine-329 by arginine in the gamma-chain that impairs the polymerization of fibrin monomer." Miyata T., Furukawa K., Iwanaga S., Takamatsu J., Saito H. J. Biochem. 105:10-14(1989) [PubMed: 2738036] [Abstract] Cited for: VARIANT NAGOYA-1 ARG-355.
[50]	"Substitution of gamma Arg-275 by Cys in an abnormal fibrinogen, 'fibrinogen Osaka II'. Evidence for a unique solitary cystine structure at the mutation site." Terukina S., Matsuda M., Hirata H., Takeda Y., Miyata T., Takao T., Shimonishi Y. J. Biol. Chem. 263:13579-13587(1988) [PubMed: 2971042] [Abstract] Cited for: VARIANT OSAKA-2 CYS-301.
[51]	"Heterozygous abnormal fibrinogen Osaka III with the replacement of gamma arginine-275 by histidine has an apparently higher molecular weight gamma-chain variant." Yoshida N., Imoka S., Hirata H., Matsuda M., Asakura S. Thromb. Haemost. 68:534-538(1992) [PubMed: 1455400] [Abstract] Cited for: VARIANT OSAKA-3 HIS-301.
[52]	"Characterization of an abnormal fibrinogen Osaka V with the replacement of gamma-arginine 375 by glycine. The lack of high affinity calcium binding to D-domains and the lack of protective effect of calcium on fibrinolysis." Yoshida N., Hirata H., Morigami Y., Imaoka S., Matsuda M., Yamazumi K., Asakura S. J. Biol. Chem. 267:2753-2759(1992) [PubMed: 1733971] [Abstract] Cited for: VARIANT OSAKA-5 GLY-401.
[53]	"Paris I dysfibrinogenemia: a point mutation in intron 8 results in insertion of a 15 amino acid sequence in the fibrinogen gamma-chain." Rosenberg J.B., Newman P.J., Mosesson M.W., Guillin M.-C., Amrani D.L. Thromb. Haemost. 69:217-220(1993) [PubMed: 8470043] [Abstract] Cited for: VARIANT PARIS-1 GLY-377 DELINS VAL-MET-CYS-GLY-GLU-ALA-LEU-PRO-MET-LEU-LYS-ASP-PRO-CYS-TYR-SER.
[54]	"An apparently higher molecular weight gamma-chain variant in a new congenital abnormal fibrinogen Tochigi characterized by the replacement of gamma arginine-275 by cysteine." Yoshida N., Ota K., Moroi M., Matsuda M. Blood 71:480-487(1988) [PubMed: 3337908] [Abstract] Cited for: VARIANT TOCHIGI CYS-301.
[55]	"A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the gamma-chain gene, causing defective calcium binding and impaired fibrin polymerization." Koopman J., Haverkate F., Briet E., Lord S.T. J. Biol. Chem. 266:13456-13461(1991) [PubMed: 2071611] [Abstract] Cited for: VARIANT VLISSINGEN 345-ASN-ASP-346 DEL.
[56]	"Three abnormal fibrinogen variants with the same amino acid substitution (gamma 275 Arg-->His): fibrinogens Bergamo II, Essen and Perugia." Reber P., Furlan M., Henschen A., Kaudewitz H., Barbui T., Hilgard P., Nenci G.G., Berrettini M., Beck E.A. Thromb. Haemost. 56:401-406(1986) [PubMed: 3563970] [Abstract] Cited for: VARIANT BERGAMO-2/ESSEN/HAIFA/PERUGIA HIS-301.
[57]	"Normal plasmic cleavage of the gamma-chain variant of 'fibrinogen Saga' with an Arg-275 to His substitution." Yamazumi K., Terukina S., Onohara S., Matsuda M. Thromb. Haemost. 60:476-480(1988) [PubMed: 2976995] [Abstract] Cited for: VARIANT SAGA HIS-301.
[58]	"Fibrinogen Milano XII: a dysfunctional variant containing 2 amino acid substitutions, A-alpha R16C and gamma G165R." Bolliger-Stucki B., Lord S.T., Furlan M. Blood 98:351-357(2001) [PubMed: 11435303] [Abstract] Cited for: VARIANT MILANO-12 ARG-191.
[59]	"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: 10391209] [Abstract] Cited for: VARIANTS ARG-191 AND VAL-410.
[60]	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)
[61]	"Fibrinogen Hillsborough: a novel gamma-gly309asp dysfibrinogen with impaired clotting." Mullin J.L., Brennan S.O., Ganly P.S., George P.M. Blood 99:3597-3601(2002) [PubMed: 11986213] [Abstract] Cited for: VARIANT HILLSBOROUGH ASP-335.
+	Additional computationally mapped references.

Web resources

GeneReviews

Wikipedia

Fibrinogen entry

SeattleSNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

M10014 Genomic DNA. Translation: AAB59530.1.
M10014 Genomic DNA. Translation: AAB59531.1.
AF118092 mRNA. Translation: AAF22036.1.
AF350254 Genomic DNA. Translation: AAK19751.2.
AF350254 Genomic DNA. Translation: AAK19752.2.
AK289422 mRNA. Translation: BAF82111.1.
AK290824 mRNA. Translation: BAF83513.1.
BT007081 mRNA. Translation: AAP35744.1.
CH471056 Genomic DNA. Translation: EAX04917.1.
CH471056 Genomic DNA. Translation: EAX04919.1.
BC007044 mRNA. Translation: AAH07044.1.
BC021674 mRNA. Translation: AAH21674.1.
X51473 mRNA. Translation: CAA35837.1.
X00086 mRNA. Translation: CAA24944.1.
K02569 Genomic DNA. Translation: AAA52430.1.
K02569 Genomic DNA. Translation: AAA52431.1.

IPI

IPI00021891.
IPI00219713.

PIR

FGHUG. A90470.
FGHUGB. A90494.

RefSeq

NP_000500.2.
NP_068656.2.

UniGene

Hs.546255

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DUG	X-ray	1.80	A/B	424-433	[»]
1FIB	X-ray	2.10	A	169-433	[»]
1FIC	X-ray	2.50	A/B	169-433	[»]
1FID	X-ray	2.10	A	169-433	[»]
1FZA	X-ray	2.90	C/F	114-432	[»]
1FZB	X-ray	2.90	C/F	114-432	[»]
1FZC	X-ray	2.30	C/F	114-432	[»]
1FZE	X-ray	3.00	C/F	114-432	[»]
1FZF	X-ray	2.70	C/F	114-432	[»]
1FZG	X-ray	2.50	C/F	114-432	[»]
1LT9	X-ray	2.80	C/F	122-432	[»]
1LTJ	X-ray	2.80	C/F	122-432	[»]
1N86	X-ray	3.20	C/F	114-433	[»]
1N8E	X-ray	4.50	C/F	114-433	[»]
1RE3	X-ray	2.45	C/F	122-432	[»]
1RE4	X-ray	2.70	C/F	122-432	[»]
1RF0	X-ray	2.81	C/F	122-432	[»]
1RF1	X-ray	2.53	C/F	122-432	[»]
2A45	X-ray	3.65	I/L	27-71	[»]
2FFD	X-ray	2.89	C/F	122-432	[»]
2FIB	X-ray	2.01	A	169-433	[»]
2H43	X-ray	2.70	C/F	115-433	[»]
2HLO	X-ray	2.60	C/F	114-437	[»]
2HOD	X-ray	2.90	C/F/I/L	115-437	[»]
2HPC	X-ray	2.90	C/F/I/L	115-437	[»]
2HWL	X-ray	2.40	P	439-452	[»]
2OYH	X-ray	2.40	C/F	122-432	[»]
2OYI	X-ray	2.70	C/F	122-432	[»]
2Q9I	X-ray	2.80	C/F	114-433	[»]
2VDO	X-ray	2.51	C	426-437	[»]
2VDP	X-ray	2.80	C	428-437	[»]
2VDQ	X-ray	2.59	C	426-437	[»]
2VDR	X-ray	2.40	C	428-437	[»]
2Z4E	X-ray	2.70	C/F	114-437	[»]
3BVH	X-ray	2.60	C/F	128-420	[»]
3E1I	X-ray	2.30	C/F	114-432	[»]
3FIB	X-ray	2.10	A	170-418	[»]

ModBase

Search...

2-D gel databases

SWISS-2DPAGE

P02679.

Cornea-2DPAGE

P02679.

DOSAC-COBS-2DPAGE

P02679.

OGP

P02679.

REPRODUCTION-2DPAGE

IPI00219713.
P02679.

Siena-2DPAGE

P02679.

Proteomic databases

PeptideAtlas

P02679.

PRIDE

P02679.

Genome annotation databases

Ensembl

ENSG00000171557. Homo sapiens. [Contig view]

GeneID

2266.

KEGG

hsa:2266.

UCSC

uc003ioj.1. human.

Organism-specific databases

GeneCards

GC04M155744.

H-InvDB

HIX0004586.

HGNC

HGNC:3694. FGG.

MIM

134850. gene.
202400. phenotype.

Orphanet

335. Congenital fibrinogen deficiency.

PharmGKB

PA430.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P02679.

HOVERGEN

P02679.

Enzyme and pathway databases

Pathway_Interaction_DB

il6_7pathway. IL6-mediated signaling events.

Reactome

REACT_13552. Integrin cell surface interactions.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P02679.

Bgee

P02679.

CleanEx

HS_FGG.

GermOnline

ENSG00000171557. Homo sapiens.

Family and domain databases

InterPro

IPR002181. Fibrinogen_a/b/g_C.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR012290. Fibrinogen_a/b/g_coil.
IPR018991. Fibrinogen_gsu_coiled-coil.
[Graphical view]

Gene3D

G3DSA:3.90.215.10. Fibrinogen_a/b/g_C_1. 1 hit.
G3DSA:4.10.530.10. Fibrinogen_a/b/g_C_2. 1 hit.
G3DSA:1.20.5.50. Fibrinogen_a/b/g_coil. 1 hit.

Pfam

PF09395. Fib_gamma. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]

SMART

SM00186. FBG. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other Resources

DrugBank

DB00364. Sucralfate.

NextBio

9205.

PMAP-CutDB

P02679.

SOURCE

Search...

Entry information

Entry name

FIBG_HUMAN

Accession

Primary (citable) accession number: P02679
Secondary accession number(s): A8K057 , P04469, P04470, Q53Y18, Q96A14, Q96KJ3, Q9UC62, Q9UC63, Q9UCF3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 16, 2002
Last modified:	July 7, 2009
This is version 135 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)