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P02679

- FIBG_HUMAN

UniProt

P02679 - FIBG_HUMAN

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Protein

Fibrinogen gamma chain

Gene
FGG, PRO2061
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei84 – 852Cleavage; by plasmin; to break down fibrin clots
Sitei88 – 892Cleavage; by plasmin; to break down fibrin clots
Sitei102 – 1032Cleavage; by hementin; to prevent blood coagulation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi341 – 355151 PublicationAdd
BLAST

GO - Molecular functioni

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

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Metal-binding

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 gamma chain
Gene namesi
Name:FGG
ORF Names:PRO2061
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:3694. FGG.

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: Reactome
  6. extracellular space Source: BHF-UCL
  7. extracellular vesicular exosome Source: UniProt
  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
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.
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.
PharmGKBiPA430.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26262 PublicationsAdd
BLAST
Chaini27 – 453427Fibrinogen gamma chainPRO_0000009099Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 – 34Interchain (with C-35)4 Publications
Disulfide bondi35 – 35Interchain (with C-34)4 Publications
Disulfide bondi45 – 45Interchain (with C-110 in beta chain)4 Publications
Disulfide bondi49 – 49Interchain (with C-64 in alpha chain)4 Publications
Glycosylationi78 – 781N-linked (GlcNAc...) (complex)6 Publications
Disulfide bondi161 – 161Interchain (with C-227 in beta chain)4 Publications
Disulfide bondi165 – 165Interchain (with C-180 in alpha chain)4 Publications
Disulfide bondi179 ↔ 2084 Publications
Glycosylationi334 – 3341N-linked (GlcNAc...); in variant Asahi
Disulfide bondi352 ↔ 3654 Publications
Cross-linki424 – 424Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-432)
Cross-linki432 – 432Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424)
Modified residuei444 – 4441Sulfotyrosine1 Publication
Modified residuei448 – 4481Sulfotyrosine1 Publication

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.
Sulfation of C-terminal tyrosines increases affinity for thrombin.

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Sulfation

Proteomic databases

MaxQBiP02679.
PaxDbiP02679.
PeptideAtlasiP02679.
PRIDEiP02679.

2D gel databases

DOSAC-COBS-2DPAGEP02679.
OGPiP02679.
REPRODUCTION-2DPAGEIPI00219713.
P02679.
SWISS-2DPAGEP02679.

PTM databases

PhosphoSiteiP02679.

Miscellaneous databases

PMAP-CutDBP02679.

Expressioni

Gene expression databases

ArrayExpressiP02679.
BgeeiP02679.
CleanExiHS_FGG.
GenevestigatoriP02679.

Organism-specific databases

HPAiHPA027529.

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.4 Publications

Protein-protein interaction databases

BioGridi108557. 10 interactions.
DIPiDIP-29644N.
IntActiP02679. 2 interactions.
MINTiMINT-5004002.

Structurei

Secondary structure

1
453
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 463
Helixi49 – 9446
Turni96 – 983
Turni115 – 1184
Turni119 – 1224
Turni124 – 1285
Helixi129 – 16032
Beta strandi161 – 1633
Beta strandi166 – 1683
Beta strandi171 – 1788
Helixi179 – 1846
Beta strandi191 – 1955
Turni198 – 2003
Beta strandi204 – 2107
Beta strandi212 – 2143
Beta strandi216 – 22611
Helixi234 – 2396
Beta strandi241 – 2444
Beta strandi246 – 2483
Beta strandi252 – 2543
Helixi256 – 2638
Helixi265 – 2673
Beta strandi270 – 2778
Beta strandi279 – 2813
Beta strandi283 – 2908
Helixi296 – 2983
Beta strandi301 – 3033
Beta strandi305 – 3095
Helixi315 – 3173
Beta strandi322 – 3243
Helixi327 – 3315
Beta strandi341 – 3433
Beta strandi346 – 3505
Helixi352 – 3565
Beta strandi358 – 3603
Beta strandi363 – 3653
Beta strandi367 – 3693
Beta strandi370 – 3734
Beta strandi376 – 3794
Helixi382 – 3843
Beta strandi385 – 3873
Beta strandi392 – 3954
Turni396 – 3983
Beta strandi406 – 4149
Helixi415 – 4173
Beta strandi420 – 4245
Beta strandi426 – 4338

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DUGX-ray1.80A/B424-433[»]
1FIBX-ray2.10A169-433[»]
1FICX-ray2.50A/B169-433[»]
1FIDX-ray2.10A169-433[»]
1FZAX-ray2.90C/F114-432[»]
1FZBX-ray2.90C/F114-432[»]
1FZCX-ray2.30C/F114-432[»]
1FZEX-ray3.00C/F114-432[»]
1FZFX-ray2.70C/F114-432[»]
1FZGX-ray2.50C/F114-432[»]
1LT9X-ray2.80C/F122-432[»]
1LTJX-ray2.80C/F122-432[»]
1N86X-ray3.20C/F114-433[»]
1N8EX-ray4.50C/F114-433[»]
1RE3X-ray2.45C/F122-432[»]
1RE4X-ray2.70C/F122-432[»]
1RF0X-ray2.81C/F122-432[»]
1RF1X-ray2.53C/F122-432[»]
2A45X-ray3.65I/L27-71[»]
2FFDX-ray2.89C/F122-432[»]
2FIBX-ray2.01A169-433[»]
2H43X-ray2.70C/F115-433[»]
2HLOX-ray2.60C/F114-433[»]
2HODX-ray2.90C/F/I/L115-433[»]
2HPCX-ray2.90C/F/I/L115-433[»]
2HWLX-ray2.40P439-452[»]
2OYHX-ray2.40C/F122-432[»]
2OYIX-ray2.70C/F122-432[»]
2Q9IX-ray2.80C/F114-433[»]
2VDOX-ray2.51C426-433[»]
2VDPX-ray2.80C428-433[»]
2VDQX-ray2.59C426-435[»]
2VDRX-ray2.40C428-452[»]
2VR3X-ray1.95C/D425-436[»]
2XNXX-ray3.30C/F/I/L114-432[»]
2XNYX-ray7.50C/F114-432[»]
2Y7LX-ray1.49B421-433[»]
2Z4EX-ray2.70C/F114-433[»]
3BVHX-ray2.60C/F128-420[»]
3E1IX-ray2.30C/F114-432[»]
3FIBX-ray2.10A170-418[»]
3GHGX-ray2.90C/F/I/L27-433[»]
3H32X-ray3.60C/F121-433[»]
3HUSX-ray3.04C/F122-432[»]
4B60X-ray1.83C/D421-433[»]
ProteinModelPortaliP02679.
SMRiP02679. Positions 28-421.

Miscellaneous databases

EvolutionaryTraceiP02679.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini170 – 416247Fibrinogen C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni400 – 42223Gamma-chain polymerization, binding amino end of another fibrin alpha chainAdd
BLAST
Regioni423 – 43715Platelet aggregation and Staphylococcus clumpingAdd
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

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiNOG269667.
HOVERGENiHBG099783.
KOiK03905.
OrthoDBiEOG7X9G60.
PhylomeDBiP02679.
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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Gamma-B (identifier: P02679-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSWSLHPRNL ILYFYALLFL SSTCVAYVAT RDNCCILDER FGSYCPTTCG    50
IADFLSTYQT KVDKDLQSLE DILHQVENKT SEVKQLIKAI QLTYNPDESS 100
KPNMIDAATL KSRKMLEEIM KYEASILTHD SSIRYLQEIY NSNNQKIVNL 150
KEKVAQLEAQ CQEPCKDTVQ IHDITGKDCQ DIANKGAKQS GLYFIKPLKA 200
NQQFLVYCEI DGSGNGWTVF QKRLDGSVDF KKNWIQYKEG FGHLSPTGTT 250
EFWLGNEKIH LISTQSAIPY ALRVELEDWN GRTSTADYAM FKVGPEADKY 300
RLTYAYFAGG DAGDAFDGFD FGDDPSDKFF TSHNGMQFST WDNDNDKFEG 350
NCAEQDGSGW WMNKCHAGHL NGVYYQGGTY SKASTPNGYD NGIIWATWKT 400
RWYSMKKTTM KIIPFNRLTI GEGQQHHLGG AKQVRPEHPA ETEYDSLYPE 450
DDL 453

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

Length:453
Mass (Da):51,512
Last modified:April 16, 2002 - v3
Checksum:i1787204904E0D4BB
GO
Isoform Gamma-A (identifier: P02679-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:437
Mass (Da):49,497
Checksum:i3D73A7BC1E71381B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti77 – 771E → G.
Corresponds to variant rs11551835 [ dbSNP | Ensembl ].
VAR_049066
Natural varianti140 – 1401Y → H.1 Publication
Corresponds to variant rs2066870 [ dbSNP | Ensembl ].
VAR_033930
Natural varianti191 – 1911G → R in Milano-12. 3 Publications
Corresponds to variant rs6063 [ dbSNP | Ensembl ].
VAR_014170
Natural varianti301 – 3011R → C in Tochigi/Osaka-2/Milano-5/Villajoyosa. 5 Publications
VAR_002409
Natural varianti301 – 3011R → H in Bergamo-2/Essen/Haifa/Osaka-3/Perugia/Saga/Barcelona-3/Barcelona-4. 4 Publications
VAR_002410
Natural varianti318 – 3181G → V in Baltimore-1; impaired polymerization. 1 Publication
VAR_002411
Natural varianti334 – 3341N → I in Baltimore-3; impaired polymerization. 1 Publication
Corresponds to variant rs121913090 [ dbSNP | Ensembl ].
VAR_002413
Natural varianti334 – 3341N → K in Kyoto-1; causes accelerated cleavage by plasmin. 2 Publications
VAR_002412
Natural varianti335 – 3351G → D in Hillsborough; prolonged thrombin clotting time. 1 Publication
VAR_015853
Natural varianti336 – 3361M → T in Asahi; impaired polymerization. 2 Publications
VAR_002414
Natural varianti345 – 3462Missing in Vlissingen; defective calcium binding and impaired polymerization.
VAR_002415
Natural varianti355 – 3551Q → R in Nagoya-1; impaired polymerization. 1 Publication
VAR_002416
Natural varianti356 – 3561D → V in Milano-1; impaired polymerization. 1 Publication
VAR_002418
Natural varianti356 – 3561D → Y in Kyoto-3; impaired polymerization. 2 Publications
VAR_002417
Natural varianti363 – 3631N → K in Bern-1; impaired polymerization. 1 Publication
VAR_002419
Natural varianti377 – 3771G → VMCGEALPMLKDPCYS in Paris-1; impaired polymerization.
VAR_002420
Natural varianti384 – 3841S → C in Milano-7; impaired polymerization. 1 Publication
VAR_002421
Natural varianti401 – 4011R → G in Osaka-5. 1 Publication
VAR_002422
Natural varianti410 – 4101M → V.1 Publication
Corresponds to variant rs6061 [ dbSNP | Ensembl ].
VAR_014171

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei434 – 45320VRPEH…PEDDL → AGDV in isoform Gamma-A. VSP_001537Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti114 – 1141K → I in AAB59530. 1 Publication
Sequence conflicti114 – 1141K → I in AAB59531. 1 Publication
Sequence conflicti435 – 4351R → Y AA sequence 1 Publication
Sequence conflicti448 – 4481Y → R AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3788.1. [P02679-1]
CCDS47153.1. [P02679-2]
PIRiA90470. FGHUG.
A90494. FGHUGB.
RefSeqiNP_000500.2. NM_000509.4. [P02679-2]
NP_068656.2. NM_021870.2. [P02679-1]
UniGeneiHs.727584.

Genome annotation databases

EnsembliENST00000336098; ENSP00000336829; ENSG00000171557. [P02679-1]
ENST00000404648; ENSP00000384860; ENSG00000171557. [P02679-2]
GeneIDi2266.
KEGGihsa:2266.
UCSCiuc003iog.3. human. [P02679-2]
uc003ioj.3. human. [P02679-1]

Polymorphism databases

DMDMi20178280.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Fibrinogen entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3788.1. [P02679-1 ]
CCDS47153.1. [P02679-2 ]
PIRi A90470. FGHUG.
A90494. FGHUGB.
RefSeqi NP_000500.2. NM_000509.4. [P02679-2 ]
NP_068656.2. NM_021870.2. [P02679-1 ]
UniGenei Hs.727584.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 114-433 [» ]
2HOD X-ray 2.90 C/F/I/L 115-433 [» ]
2HPC X-ray 2.90 C/F/I/L 115-433 [» ]
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 426-433 [» ]
2VDP X-ray 2.80 C 428-433 [» ]
2VDQ X-ray 2.59 C 426-435 [» ]
2VDR X-ray 2.40 C 428-452 [» ]
2VR3 X-ray 1.95 C/D 425-436 [» ]
2XNX X-ray 3.30 C/F/I/L 114-432 [» ]
2XNY X-ray 7.50 C/F 114-432 [» ]
2Y7L X-ray 1.49 B 421-433 [» ]
2Z4E X-ray 2.70 C/F 114-433 [» ]
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 [» ]
3GHG X-ray 2.90 C/F/I/L 27-433 [» ]
3H32 X-ray 3.60 C/F 121-433 [» ]
3HUS X-ray 3.04 C/F 122-432 [» ]
4B60 X-ray 1.83 C/D 421-433 [» ]
ProteinModelPortali P02679.
SMRi P02679. Positions 28-421.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108557. 10 interactions.
DIPi DIP-29644N.
IntActi P02679. 2 interactions.
MINTi MINT-5004002.

Chemistry

BindingDBi P02679.
ChEMBLi CHEMBL2364709.
DrugBanki DB00364. Sucralfate.

PTM databases

PhosphoSitei P02679.

Polymorphism databases

DMDMi 20178280.

2D gel databases

DOSAC-COBS-2DPAGE P02679.
OGPi P02679.
REPRODUCTION-2DPAGE IPI00219713.
P02679.
SWISS-2DPAGE P02679.

Proteomic databases

MaxQBi P02679.
PaxDbi P02679.
PeptideAtlasi P02679.
PRIDEi P02679.

Protocols and materials databases

DNASUi 2266.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000336098 ; ENSP00000336829 ; ENSG00000171557 . [P02679-1 ]
ENST00000404648 ; ENSP00000384860 ; ENSG00000171557 . [P02679-2 ]
GeneIDi 2266.
KEGGi hsa:2266.
UCSCi uc003iog.3. human. [P02679-2 ]
uc003ioj.3. human. [P02679-1 ]

Organism-specific databases

CTDi 2266.
GeneCardsi GC04M155525.
HGNCi HGNC:3694. FGG.
HPAi HPA027529.
MIMi 134850. gene.
202400. phenotype.
neXtProti NX_P02679.
Orphaneti 98880. Familial afibrinogenemia.
98881. Familial dysfibrinogenemia.
248408. Familial hypodysfibrinogenemia.
101041. Familial hypofibrinogenemia.
PharmGKBi PA430.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG269667.
HOVERGENi HBG099783.
KOi K03905.
OrthoDBi EOG7X9G60.
PhylomeDBi P02679.
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 FGG. human.
EvolutionaryTracei P02679.
GeneWikii FGG.
GenomeRNAii 2266.
NextBioi 9205.
PMAP-CutDB P02679.
PROi P02679.
SOURCEi Search...

Gene expression databases

ArrayExpressi P02679.
Bgeei P02679.
CleanExi HS_FGG.
Genevestigatori P02679.

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 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 411-453 (ISOFORM GAMMA-B).
  16. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
    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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
    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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
    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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
    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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
    Tissue: Liver.
  34. Cited for: GLYCOSYLATION AT ASN-78.
  35. "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.
  36. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 169-437.
  38. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 169-437.
  39. "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 114-432.
  40. "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 114-432.
  41. "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 114-432.
  42. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT ASAHI THR-336.
  43. "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] [Europe PMC] [Abstract]
    Cited for: VARIANTS OSAKA-2 CYS-301; KYOTO-1 LYS-334; ASAHI THR-336 AND KYOTO-3 TYR-356.
  44. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT BALTIMORE-1 VAL-318.
  45. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT BALTIMORE-3 ILE-334.
  46. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT BERN-1 LYS-363.
  47. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT KYOTO-1 LYS-334.
  48. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT KYOTO-3 TYR-356.
  49. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT MILANO-1 VAL-356.
  50. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT MILANO-5 CYS-301.
  51. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT MILANO-7 CYS-384.
  52. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT NAGOYA-1 ARG-355.
  53. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT OSAKA-2 CYS-301.
  54. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT OSAKA-3 HIS-301.
  55. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT OSAKA-5 GLY-401.
  56. "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] [Europe PMC] [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.
  57. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT TOCHIGI CYS-301.
  58. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT VLISSINGEN 345-ASN-ASP-346 DEL.
  59. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT BERGAMO-2/ESSEN/HAIFA/PERUGIA HIS-301.
  60. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT SAGA HIS-301.
  61. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT MILANO-12 ARG-191.
  62. Cited for: VARIANTS ARG-191 AND VAL-410.
  63. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT HILLSBOROUGH ASP-335.

Entry informationi

Entry nameiFIBG_HUMAN
AccessioniPrimary (citable) accession number: P02679
Secondary accession number(s): A8K057
, P04469, P04470, Q53Y18, Q96A14, Q96KJ3, Q9UC62, Q9UC63, Q9UCF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 16, 2002
Last modified: September 3, 2014
This is version 190 of the entry and version 3 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

Miscellaneous

The gamma-chain carries the main binding site for the platelet receptor.

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

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