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UniProtKB - P02679 (FIBG_HUMAN)

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Protein

Fibrinogen gamma chain

Gene

FGG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways.By similarity

Miscellaneous

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi344CalciumCombined sources6 Publications1
Metal bindingi346CalciumCombined sources6 Publications1
Metal bindingi348Calcium; via carbonyl oxygenCombined sources6 Publications1
Metal bindingi350Calcium; via carbonyl oxygenCombined sources6 Publications1

GO - Molecular functioni

  • cell adhesion molecule binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • protein homodimerization activity Source: Ensembl
  • signaling receptor binding Source: BHF-UCL
  • structural molecule activity Source: BHF-UCL
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • blood coagulation Source: Reactome
  • blood coagulation, fibrin clot formation Source: UniProtKB
  • cell-matrix adhesion Source: BHF-UCL
  • cellular protein-containing complex assembly Source: BHF-UCL
  • cellular protein metabolic process Source: Reactome
  • cellular response to interleukin-1 Source: Ensembl
  • cellular response to interleukin-6 Source: Ensembl
  • extracellular matrix organization Source: Reactome
  • fibrinolysis Source: UniProtKB
  • negative regulation of endothelial cell apoptotic process Source: BHF-UCL
  • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
  • negative regulation of platelet aggregation Source: Ensembl
  • plasminogen activation Source: UniProtKB
  • platelet aggregation Source: BHF-UCL
  • platelet degranulation Source: Reactome
  • platelet maturation Source: Ensembl
  • positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  • positive regulation of exocytosis Source: BHF-UCL
  • positive regulation of heterotypic cell-cell adhesion Source: BHF-UCL
  • positive regulation of peptide hormone secretion Source: BHF-UCL
  • positive regulation of protein secretion Source: BHF-UCL
  • positive regulation of substrate adhesion-dependent cell spreading Source: BHF-UCL
  • positive regulation of vasoconstriction Source: BHF-UCL
  • post-translational protein modification Source: Reactome
  • protein polymerization Source: BHF-UCL
  • protein secretion Source: UniProtKB
  • response to calcium ion Source: BHF-UCL
  • toll-like receptor signaling pathway Source: Reactome
View the complete GO annotation on QuickGO ...

Keywordsi

Biological processBlood coagulation, Hemostasis
LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-140875 Common Pathway of Fibrin Clot Formation
R-HSA-216083 Integrin cell surface interactions
R-HSA-354192 Integrin alphaIIb beta3 signaling
R-HSA-354194 GRB2:SOS provides linkage to MAPK signaling for Integrins
R-HSA-372708 p130Cas linkage to MAPK signaling for integrins
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-5674135 MAP2K and MAPK activation
R-HSA-5686938 Regulation of TLR by endogenous ligand
R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants
R-HSA-6802948 Signaling by high-kinase activity BRAF mutants
R-HSA-6802949 Signaling by RAS mutants
R-HSA-6802952 Signaling by BRAF and RAF fusions
R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF
R-HSA-8957275 Post-translational protein phosphorylation
SIGNORiP02679

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrinogen gamma chain
Gene namesi
Name:FGG
ORF Names:PRO2061
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000171557.16
HGNCiHGNC:3694 FGG
MIMi134850 gene
neXtProtiNX_P02679

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Congenital afibrinogenemia (CAFBN)1 Publication
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.
Disease descriptionRare 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.
See also OMIM:202400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_072726303T → P in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; impaired fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_072727327D → H in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; no effect on fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_072728345N → D in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; decreased fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_072729401R → W in CAFBN; hypofibrinogenemia; heterozygous. 1 PublicationCorresponds to variant dbSNP:rs75848804EnsemblClinVar.1
Dysfibrinogenemia, congenital (DYSFIBRIN)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by qualitative abnormalities (dysfibrinogenemia) of the circulating fibrinogen. Affected individuals are frequently asymptomatic, but some patients have bleeding diathesis, thromboembolic complications, or both. In some cases, dysfibrinogenemia is associated with low circulating fibrinogen levels (hypodysfibrinogenemia).
See also OMIM:616004
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_002410301R → H in DYSFIBRIN; fibrinogen Bergamo-2/Essen/Haifa/Osaka-3/Perugia/Saga/Barcelona-3/Barcelona-4. 4 PublicationsCorresponds to variant dbSNP:rs121913088EnsemblClinVar.1
Natural variantiVAR_002411318G → V in DYSFIBRIN; fibrinogen Baltimore-1; impaired polymerization. 1 PublicationCorresponds to variant dbSNP:rs121913089EnsemblClinVar.1
Natural variantiVAR_002418356D → V in DYSFIBRIN; fibrinogen Milano-1; impaired polymerization. 1 PublicationCorresponds to variant dbSNP:rs121913094EnsemblClinVar.1
Natural variantiVAR_072621404S → P in DYSFIBRIN; fibrinogen Philadelphia. 1 PublicationCorresponds to variant dbSNP:rs587777720EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2266
MalaCardsiFGG
MIMi202400 phenotype
616004 phenotype
OpenTargetsiENSG00000171557
Orphaneti98880 Familial afibrinogenemia
98881 Familial dysfibrinogenemia
248408 Familial hypodysfibrinogenemia
101041 Familial hypofibrinogenemia
PharmGKBiPA430

Chemistry databases

ChEMBLiCHEMBL2364709
DrugBankiDB00364 Sucralfate

Polymorphism and mutation databases

BioMutaiFGG
DMDMi20178280

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 262 PublicationsAdd BLAST26
ChainiPRO_000000909927 – 453Fibrinogen gamma chainAdd BLAST427

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi34Interchain (with C-35)Combined sources1 Publication
Disulfide bondi35Interchain (with C-34)Combined sources1 Publication
Disulfide bondi45Interchain (with C-110 in beta chain)1 Publication
Disulfide bondi49Interchain (with C-64 in alpha chain)1 Publication
Modified residuei68Phosphoserine; by FAM20C1 Publication1
Glycosylationi78N-linked (GlcNAc...) (complex) asparagine6 Publications1
Disulfide bondi161Interchain (with C-227 in beta chain)1 Publication
Disulfide bondi165Interchain (with C-180 in alpha chain)1 Publication
Disulfide bondi179 ↔ 208Combined sources6 Publications
Glycosylationi334N-linked (GlcNAc...) asparagine; in variant Asahi1
Disulfide bondi352 ↔ 365Combined sources6 Publications
Cross-linki424Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-432)
Cross-linki432Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424)
Modified residuei444Sulfotyrosine1 Publication1
Modified residuei448Sulfotyrosine1 Publication1

Post-translational modificationi

Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.1 Publication
Sulfation of C-terminal tyrosines increases affinity for thrombin.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei84 – 85Cleavage; by plasmin; to break down fibrin clots2
Sitei88 – 89Cleavage; by plasmin; to break down fibrin clots2
Sitei102 – 103Cleavage; by hementin; to prevent blood coagulation2

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Sulfation

Proteomic databases

MaxQBiP02679
PaxDbiP02679
PeptideAtlasiP02679
PRIDEiP02679
ProteomicsDBi51545
51546 [P02679-2]

2D gel databases

DOSAC-COBS-2DPAGEiP02679
OGPiP02679
REPRODUCTION-2DPAGEiIPI00219713
P02679
SWISS-2DPAGEiP02679

PTM databases

CarbonylDBiP02679
GlyConnecti157
160
iPTMnetiP02679
PhosphoSitePlusiP02679
UniCarbKBiP02679

Miscellaneous databases

PMAP-CutDBiP02679

Expressioni

Tissue specificityi

Detected in blood plasma (at protein level).3 Publications

Gene expression databases

BgeeiENSG00000171557
CleanExiHS_FGG
ExpressionAtlasiP02679 baseline and differential
GenevisibleiP02679 HS

Organism-specific databases

HPAiCAB033120
HPA027529

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.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
gapAP753582EBI-1034422,EBI-2259469From Mycoplasma pneumoniae (strain ATCC 29342 / M129).

GO - Molecular functioni

  • cell adhesion molecule binding Source: BHF-UCL
  • protein homodimerization activity Source: Ensembl
  • signaling receptor binding Source: BHF-UCL
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi108557, 28 interactors
ComplexPortaliCPX-1922 Fibrinogen
CORUMiP02679
DIPiDIP-29644N
IntActiP02679, 14 interactors
STRINGi9606.ENSP00000336829

Structurei

Secondary structure

1453
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi31 – 33Combined sources3
Beta strandi34 – 36Combined sources3
Beta strandi44 – 46Combined sources3
Helixi49 – 94Combined sources46
Turni96 – 98Combined sources3
Turni115 – 118Combined sources4
Turni119 – 122Combined sources4
Turni124 – 128Combined sources5
Helixi129 – 160Combined sources32
Beta strandi161 – 163Combined sources3
Beta strandi166 – 168Combined sources3
Beta strandi171 – 178Combined sources8
Helixi179 – 184Combined sources6
Beta strandi191 – 195Combined sources5
Turni198 – 200Combined sources3
Beta strandi204 – 210Combined sources7
Beta strandi212 – 214Combined sources3
Beta strandi216 – 226Combined sources11
Helixi234 – 239Combined sources6
Beta strandi241 – 244Combined sources4
Beta strandi246 – 248Combined sources3
Beta strandi252 – 254Combined sources3
Helixi256 – 263Combined sources8
Helixi265 – 267Combined sources3
Beta strandi270 – 277Combined sources8
Beta strandi279 – 281Combined sources3
Beta strandi283 – 290Combined sources8
Helixi296 – 298Combined sources3
Beta strandi301 – 303Combined sources3
Beta strandi305 – 309Combined sources5
Helixi315 – 317Combined sources3
Beta strandi322 – 324Combined sources3
Helixi327 – 331Combined sources5
Beta strandi341 – 343Combined sources3
Beta strandi346 – 350Combined sources5
Helixi352 – 356Combined sources5
Beta strandi358 – 360Combined sources3
Beta strandi363 – 365Combined sources3
Beta strandi367 – 369Combined sources3
Beta strandi370 – 373Combined sources4
Beta strandi376 – 379Combined sources4
Helixi382 – 384Combined sources3
Beta strandi385 – 387Combined sources3
Beta strandi392 – 395Combined sources4
Turni396 – 398Combined sources3
Beta strandi406 – 414Combined sources9
Helixi415 – 417Combined sources3
Beta strandi420 – 424Combined sources5
Beta strandi426 – 433Combined sources8

3D structure databases

ProteinModelPortaliP02679
SMRiP02679
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02679

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini170 – 416Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST247

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni400 – 422Gamma-chain polymerization, binding amino end of another fibrin alpha chainAdd BLAST23
Regioni423 – 437Platelet aggregation and Staphylococcus clumpingAdd BLAST15

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.2 Publications

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiKOG2579 Eukaryota
ENOG410ZYS4 LUCA
GeneTreeiENSGT00920000148942
HOVERGENiHBG099783
InParanoidiP02679
KOiK03905
PhylomeDBiP02679
TreeFamiTF336658

Family and domain databases

CDDicd00087 FReD, 1 hit
Gene3Di3.90.215.10, 1 hit
4.10.530.10, 1 hit
InterProiView protein in InterPro
IPR036056 Fibrinogen-like_C
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
IPR037581 Fibrinogen_gamma
PANTHERiPTHR19143:SF338 PTHR19143:SF338, 1 hit
PfamiView protein in Pfam
PF08702 Fib_alpha, 1 hit
PF00147 Fibrinogen_C, 1 hit
SMARTiView protein in SMART
SM00186 FBG, 1 hit
SM01212 Fib_alpha, 1 hit
SUPFAMiSSF56496 SSF56496, 1 hit
PROSITEiView protein in PROSITE
PS00514 FIBRINOGEN_C_1, 1 hit
PS51406 FIBRINOGEN_C_2, 1 hit

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. AlignAdd to basket

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

        10         20         30         40         50
MSWSLHPRNL ILYFYALLFL SSTCVAYVAT RDNCCILDER FGSYCPTTCG 
        60         70         80         90        100
IADFLSTYQT KVDKDLQSLE DILHQVENKT SEVKQLIKAI QLTYNPDESS 
       110        120        130        140        150
KPNMIDAATL KSRKMLEEIM KYEASILTHD SSIRYLQEIY NSNNQKIVNL 
       160        170        180        190        200
KEKVAQLEAQ CQEPCKDTVQ IHDITGKDCQ DIANKGAKQS GLYFIKPLKA 
       210        220        230        240        250
NQQFLVYCEI DGSGNGWTVF QKRLDGSVDF KKNWIQYKEG FGHLSPTGTT 
       260        270        280        290        300
EFWLGNEKIH LISTQSAIPY ALRVELEDWN GRTSTADYAM FKVGPEADKY 
       310        320        330        340        350
RLTYAYFAGG DAGDAFDGFD FGDDPSDKFF TSHNGMQFST WDNDNDKFEG 
       360        370        380        390        400
NCAEQDGSGW WMNKCHAGHL NGVYYQGGTY SKASTPNGYD NGIIWATWKT 
       410        420        430        440        450
RWYSMKKTTM KIIPFNRLTI GEGQQHHLGG AKQVRPEHPA ETEYDSLYPE 

DDL
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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti114K → I in AAB59530 (PubMed:2990550).Curated1
Sequence conflicti114K → I in AAB59531 (PubMed:2990550).Curated1
Sequence conflicti435R → Y AA sequence (PubMed:7306501).Curated1
Sequence conflicti448Y → R AA sequence (PubMed:7306501).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04906677E → G. Corresponds to variant dbSNP:rs11551835Ensembl.1
Natural variantiVAR_033930140Y → H1 PublicationCorresponds to variant dbSNP:rs2066870EnsemblClinVar.1
Natural variantiVAR_014170191G → R in Milano-12. 3 PublicationsCorresponds to variant dbSNP:rs6063EnsemblClinVar.1
Natural variantiVAR_002409301R → C in Tochigi/Osaka-2/Milano-5/Villajoyosa. 5 PublicationsCorresponds to variant dbSNP:rs121913087EnsemblClinVar.1
Natural variantiVAR_002410301R → H in DYSFIBRIN; fibrinogen Bergamo-2/Essen/Haifa/Osaka-3/Perugia/Saga/Barcelona-3/Barcelona-4. 4 PublicationsCorresponds to variant dbSNP:rs121913088EnsemblClinVar.1
Natural variantiVAR_072726303T → P in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; impaired fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_002411318G → V in DYSFIBRIN; fibrinogen Baltimore-1; impaired polymerization. 1 PublicationCorresponds to variant dbSNP:rs121913089EnsemblClinVar.1
Natural variantiVAR_072727327D → H in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; no effect on fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_002413334N → I in Baltimore-3; impaired polymerization. 1 PublicationCorresponds to variant dbSNP:rs121913090EnsemblClinVar.1
Natural variantiVAR_002412334N → K in Kyoto-1; causes accelerated cleavage by plasmin. 2 Publications1
Natural variantiVAR_015853335G → D in Hillsborough; prolonged thrombin clotting time. 1 Publication1
Natural variantiVAR_002414336M → T in Asahi; impaired polymerization. 2 PublicationsCorresponds to variant dbSNP:rs121913091EnsemblClinVar.1
Natural variantiVAR_002415345 – 346Missing in Vlissingen; defective calcium binding and impaired polymerization. 1 Publication2
Natural variantiVAR_072728345N → D in CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; decreased fibrinogen complex secretion. 1 Publication1
Natural variantiVAR_002416355Q → R in Nagoya-1; impaired polymerization. 1 PublicationCorresponds to variant dbSNP:rs121913092EnsemblClinVar.1
Natural variantiVAR_002418356D → V in DYSFIBRIN; fibrinogen Milano-1; impaired polymerization. 1 PublicationCorresponds to variant dbSNP:rs121913094EnsemblClinVar.1
Natural variantiVAR_002417356D → Y in Kyoto-3; impaired polymerization. 2 PublicationsCorresponds to variant dbSNP:rs121913093EnsemblClinVar.1
Natural variantiVAR_002419363N → K in Bern-1; impaired polymerization. 1 Publication1
Natural variantiVAR_002420377G → VMCGEALPMLKDPCYS in Paris-1; impaired polymerization. 1 Publication1
Natural variantiVAR_002421384S → C in Milano-7; impaired polymerization. 1 Publication1
Natural variantiVAR_002422401R → G in Osaka-5. 1 PublicationCorresponds to variant dbSNP:rs75848804EnsemblClinVar.1
Natural variantiVAR_072729401R → W in CAFBN; hypofibrinogenemia; heterozygous. 1 PublicationCorresponds to variant dbSNP:rs75848804EnsemblClinVar.1
Natural variantiVAR_072621404S → P in DYSFIBRIN; fibrinogen Philadelphia. 1 PublicationCorresponds to variant dbSNP:rs587777720EnsemblClinVar.1
Natural variantiVAR_014171410M → V1 PublicationCorresponds to variant dbSNP:rs6061Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001537434 – 453VRPEH…PEDDL → AGDV in isoform Gamma-A. 5 PublicationsAdd BLAST20

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_000509.5 [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.4 human [P02679-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiFIBG_HUMAN
AccessioniPrimary (citable) accession number: P02679
Secondary accession number(s): A8K057
, P04469, P04470, Q53Y18, Q96A14, Q96KJ3, Q9UC62, Q9UC63, Q9UCF3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 16, 2002
Last modified: July 18, 2018
This is version 230 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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