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P09769 (FGR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

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

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase Fgr

EC=2.7.10.2
Alternative name(s):
Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene homolog
Proto-oncogene c-Fgr
p55-Fgr
p58-Fgr
p58c-Fgr
Gene names
Name:FGR
Synonyms:SRC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length529 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors devoid of kinase activity and contributes to the regulation of immune responses, including neutrophil, monocyte, macrophage and mast cell functions, cytoskeleton remodeling in response to extracellular stimuli, phagocytosis, cell adhesion and migration. Promotes mast cell degranulation, release of inflammatory cytokines and IgE-mediated anaphylaxis. Acts downstream of receptors that bind the Fc region of immunoglobulins, such as MS4A2/FCER1B, FCGR2A and/or FCGR2B. Acts downstream of ITGB1 and ITGB2, and regulates actin cytoskeleton reorganization, cell spreading and adhesion. Depending on the context, activates or inhibits cellular responses. Functions as negative regulator of ITGB2 signaling, phagocytosis and SYK activity in monocytes. Required for normal ITGB1 and ITGB2 signaling, normal cell spreading and adhesion in neutrophils and macrophages. Functions as positive regulator of cell migration and regulates cytoskeleton reorganization via RAC1 activation. Phosphorylates SYK (in vitro) and promotes SYK-dependent activation of AKT1 and MAP kinase signaling. Phosphorylates PLD2 in antigen-stimulated mast cells, leading to PLD2 activation and the production of the signaling molecules lysophosphatidic acid and diacylglycerol. Promotes activation of PIK3R1. Phosphorylates FASLG, and thereby regulates its ubiquitination and subsequent internalization. Phosphorylates ABL1. Promotes phosphorylation of CBL, CTTN, PIK3R1, PTK2/FAK1, PTK2B/PYK2 and VAV2. Phosphorylates HCLS1 that has already been phosphorylated by SYK, but not unphosphorylated HCLS1. Ref.10 Ref.12 Ref.14 Ref.17

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.9 Ref.10 Ref.11

Enzyme regulation

Activated by autophosphorylation. Prior phosphorylation at Tyr-523 by SRC inhibits ulterior autophosphorylation at Tyr-412. Activated by phorbol myristate acetate, phosphatidic acid and poly-Lys. Binding (via SH2 domain) of HCLS1 that is already phosphorylated by SYK strongly increases kinase activity. Ref.11 Ref.13 Ref.15

Subunit structure

Interacts with ITGB1, ITGB2, MS4A2/FCER1B, FCER1G, FCGR2A and/or FCGR2B. Interacts (via SH2 domain) with SYK (tyrosine phosphorylated). Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with PTK2/FAK1. Interacts (via SH2 domain) with HCLS1 (tyrosine phosphorylated by SYK). Interacts with SIRPA and PTPNS1. Interacts (not phosphorylated on tyrosine residues) with CBL; FGR tyrosine phosphorylation promotes dissociation. Interacts with PIK3R1 and FASLG By similarity. Ref.11 Ref.14 Ref.16 Ref.17

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Probable. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionruffle membrane. Cytoplasmcytosol. Cytoplasmcytoskeleton. Mitochondrion inner membrane By similarity. Mitochondrion intermembrane space By similarity. Note: Detected in mitochondrial intermembrane space and at inner membranes By similarity. Colocalizes with actin fibers at membrane ruffles. Detected at plasma membrane lipid rafts. Ref.13 Ref.15

Tissue specificity

Detected in neutrophils, monocytes and natural killer cells (at protein level). Detected in monocytes and large lymphocytes. Ref.9 Ref.11 Ref.15

Post-translational modification

Ubiquitinated. Becomes ubiquitinated in response to ITGB2 signaling; this does not lead to degradation. Ref.16

Phosphorylated. Autophosphorylated on tyrosine residues. Becomes phosphorylated in response to FCGR2A and/or FCGR2B engagement, cell adhesion and signaling by ITGB2. Prior phosphorylation at Tyr-523 by SRC inhibits ulterior autophosphorylation at Tyr-412. Ref.9 Ref.11 Ref.12 Ref.14

Involvement in disease

Mutations that cause aberrant kinase activation can confer oncogene activity and promote aberrant cell proliferation. Ref.10

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processImmunity
Innate immunity
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityPolymorphism
   DiseaseProto-oncogene
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMLipoprotein
Myristate
Palmitate
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

defense response to Gram-positive bacterium

Inferred from sequence or structural similarity. Source: UniProtKB

immune response-regulating cell surface receptor signaling pathway

Traceable author statement Ref.11. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

integrin-mediated signaling pathway

Inferred from mutant phenotype Ref.14Ref.12. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.12Ref.11. Source: UniProtKB

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytokine secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mast cell degranulation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from mutant phenotype Ref.14. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from mutant phenotype Ref.14. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.9Ref.11. Source: UniProtKB

protein phosphorylation

Traceable author statement PubMed 2995972. Source: ProtInc

regulation of cell shape

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of innate immune response

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of phagocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

response to virus

Traceable author statement PubMed 3003578. Source: ProtInc

   Cellular_componentactin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

mitochondrial inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial intermembrane space

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

ruffle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Fc-gamma receptor I complex binding

Inferred from direct assay Ref.11. Source: UniProtKB

immunoglobulin receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

non-membrane spanning protein tyrosine kinase activity

Inferred from direct assay Ref.11. Source: UniProtKB

phosphotyrosine binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16273093PubMed 22939624PubMed 24728074. Source: IntAct

protein kinase binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein tyrosine kinase activity

Inferred from direct assay Ref.12. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 529528Tyrosine-protein kinase Fgr
PRO_0000088091

Regions

Domain77 – 13862SH3
Domain144 – 24198SH2
Domain263 – 516254Protein kinase
Nucleotide binding269 – 2779ATP By similarity

Sites

Active site3821Proton acceptor By similarity
Binding site2911ATP By similarity

Amino acid modifications

Modified residue341Phosphotyrosine Ref.18
Modified residue4121Phosphotyrosine Ref.18
Modified residue5231Phosphotyrosine; by SRC Ref.18
Lipidation21N-myristoyl glycine By similarity
Lipidation31S-palmitoyl cysteine By similarity
Lipidation61S-palmitoyl cysteine By similarity

Natural variations

Natural variant1101T → I. Ref.19
Corresponds to variant rs34597831 [ dbSNP | Ensembl ].
VAR_041700
Natural variant1301S → R. Ref.19
Corresponds to variant rs35334091 [ dbSNP | Ensembl ].
VAR_041701

Experimental info

Mutagenesis5231Y → F: Strongly increased catalytic activity. Functions as oncogene. Ref.10

Sequences

Sequence LengthMass (Da)Tools
P09769 [UniParc].

Last modified January 1, 1990. Version 2.
Checksum: 6B8C1E08414E0F9C

FASTA52959,479
        10         20         30         40         50         60 
MGCVFCKKLE PVATAKEDAG LEGDFRSYGA ADHYGPDPTK ARPASSFAHI PNYSNFSSQA 

        70         80         90        100        110        120 
INPGFLDSGT IRGVSGIGVT LFIALYDYEA RTEDDLTFTK GEKFHILNNT EGDWWEARSL 

       130        140        150        160        170        180 
SSGKTGCIPS NYVAPVDSIQ AEEWYFGKIG RKDAERQLLS PGNPQGAFLI RESETTKGAY 

       190        200        210        220        230        240 
SLSIRDWDQT RGDHVKHYKI RKLDMGGYYI TTRVQFNSVQ ELVQHYMEVN DGLCNLLIAP 

       250        260        270        280        290        300 
CTIMKPQTLG LAKDAWEISR SSITLERRLG TGCFGDVWLG TWNGSTKVAV KTLKPGTMSP 

       310        320        330        340        350        360 
KAFLEEAQVM KLLRHDKLVQ LYAVVSEEPI YIVTEFMCHG SLLDFLKNPE GQDLRLPQLV 

       370        380        390        400        410        420 
DMAAQVAEGM AYMERMNYIH RDLRAANILV GERLACKIAD FGLARLIKDD EYNPCQGSKF 

       430        440        450        460        470        480 
PIKWTAPEAA LFGRFTIKSD VWSFGILLTE LITKGRIPYP GMNKREVLEQ VEQGYHMPCP 

       490        500        510        520 
PGCPASLYEA MEQTWRLDPE ERPTFEYLQS FLEDYFTSAE PQYQPGDQT 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of the human fgr proto-oncogene product p55c-fgr."
Katamine S., Notario V., Rao C.D., Miki T., Cheah M.S.C., Tronick S.R., Robbins K.C.
Mol. Cell. Biol. 8:259-266(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Brain.
[5]"Structure and expression of c-fgr protooncogene mRNA in Epstein-Barr virus converted cell lines."
Brickell P.M., Patel M.
Br. J. Cancer 58:704-709(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-177 AND 524-529.
[6]"Isolation and sequencing of cDNA clones homologous to the v-fgr oncogene from a human B lymphocyte cell line, IM-9."
Inoue K., Ikawa S., Semba K., Sukegawa J., Yamamoto T., Toyoshima K.
Oncogene 1:301-304(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-143.
[7]"Structure of the complete human c-fgr proto-oncogene and identification of multiple transcriptional start sites."
Patel M., Leevers S.J., Brickell P.M.
Oncogene 5:201-206(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-142.
[8]"Structure, expression, and chromosomal location of the human c-fgr gene."
Nishizawa M., Semba K., Yoshida M.C., Yamamoto T., Sasaki M., Toyoshima K.
Mol. Cell. Biol. 6:511-517(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 111-416.
[9]"Specific expression of human c-fgr in natural immunity effector cells."
Inoue K., Yamamoto T., Toyoshima K.
Mol. Cell. Biol. 10:1789-1792(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
[10]"Diverse biologic properties imparted by the c-fgr proto-oncogene."
Sartor O., Moriuchi R., Sameshima J.H., Severino M., Gutkind J.S., Robbins K.C.
J. Biol. Chem. 267:3460-3465(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS PROTO-ONCOGENE, ROLE IN DISEASE, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-523.
[11]"Association of immunoglobulin G Fc receptor II with Src-like protein-tyrosine kinase Fgr in neutrophils."
Hamada F., Aoki M., Akiyama T., Toyoshima K.
Proc. Natl. Acad. Sci. U.S.A. 90:6305-6309(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCGR2A AND/OR FCGR2B, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
[12]"Beta 2 integrin-dependent protein tyrosine phosphorylation and activation of the FGR protein tyrosine kinase in human neutrophils."
Berton G., Fumagalli L., Laudanna C., Sorio C.
J. Cell Biol. 126:1111-1121(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, FUNCTION IN INTEGRIN SIGNALING.
[13]"Activation of SRC family kinases in human neutrophils. Evidence that p58C-FGR and p53/56LYN redistributed to a Triton X-100-insoluble cytoskeletal fraction, also enriched in the caveolar protein caveolin, display an enhanced kinase activity."
Yan S.R., Fumagalli L., Berton G.
FEBS Lett. 380:198-203(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION AT THE CYTOSKELETON, ENZYME REGULATION.
[14]"Clustering of beta(2)-integrins on human neutrophils activates dual signaling pathways to PtdIns 3-kinase."
Axelsson L., Hellberg C., Melander F., Smith D., Zheng L., Andersson T.
Exp. Cell Res. 256:257-263(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ACTIVATION OF PIK3R1, PHOSPHORYLATION, INTERACTION WITH ITGB2 AND PIK3R1.
[15]"Phosphatidic acid regulates tyrosine phosphorylating activity in human neutrophils: enhancement of Fgr activity."
Sergeant S., Waite K.A., Heravi J., McPhail L.C.
J. Biol. Chem. 276:4737-4746(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[16]"Fgr but not Syk tyrosine kinase is a target for beta 2 integrin-induced c-Cbl-mediated ubiquitination in adherent human neutrophils."
Melander F., Andersson T., Dib K.
Biochem. J. 370:687-694(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, INTERACTION WITH CBL.
[17]"Sorting of Fas ligand to secretory lysosomes is regulated by mono-ubiquitylation and phosphorylation."
Zuccato E., Blott E.J., Holt O., Sigismund S., Shaw M., Bossi G., Griffiths G.M.
J. Cell Sci. 120:191-199(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF FASLG, INTERACTION WITH FASLG.
[18]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-34; TYR-412 AND TYR-523, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-110 AND ARG-130.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19722 mRNA. Translation: AAA52451.1.
AL031729 Genomic DNA. Translation: CAB62998.1.
CH471059 Genomic DNA. Translation: EAX07748.1.
CH471059 Genomic DNA. Translation: EAX07749.1.
CH471059 Genomic DNA. Translation: EAX07750.1.
BC064382 mRNA. Translation: AAH64382.1.
X52207, X52208 Genomic DNA. Translation: CAA36457.2.
M12724 expand/collapse EMBL AC list , M12719, M12720, M12721, M12722, M12723 Genomic DNA. Translation: AAA52762.1.
CCDSCCDS305.1.
PIRTVHUFR. A27676.
RefSeqNP_001036194.1. NM_001042729.1.
NP_001036212.1. NM_001042747.1.
NP_005239.1. NM_005248.2.
XP_006710515.1. XM_006710452.1.
UniGeneHs.1422.

3D structure databases

ProteinModelPortalP09769.
SMRP09769. Positions 78-527.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108559. 20 interactions.
DIPDIP-1049N.
IntActP09769. 11 interactions.
MINTMINT-1209880.
STRING9606.ENSP00000363115.

Chemistry

BindingDBP09769.
ChEMBLCHEMBL4454.
GuidetoPHARMACOLOGY2024.

PTM databases

PhosphoSiteP09769.

Polymorphism databases

DMDM125358.

Proteomic databases

PaxDbP09769.
PRIDEP09769.

Protocols and materials databases

DNASU2268.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374003; ENSP00000363115; ENSG00000000938.
ENST00000374004; ENSP00000363116; ENSG00000000938.
ENST00000374005; ENSP00000363117; ENSG00000000938.
ENST00000399173; ENSP00000382126; ENSG00000000938.
GeneID2268.
KEGGhsa:2268.
UCSCuc001boj.3. human.

Organism-specific databases

CTD2268.
GeneCardsGC01M027938.
HGNCHGNC:3697. FGR.
HPACAB018959.
HPA002024.
MIM164940. gene.
neXtProtNX_P09769.
PharmGKBPA28135.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233858.
HOVERGENHBG008761.
InParanoidP09769.
KOK08891.
OMATWNGSTK.
OrthoDBEOG7GTT2V.
PhylomeDBP09769.
TreeFamTF351634.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP09769.

Gene expression databases

ArrayExpressP09769.
BgeeP09769.
CleanExHS_FGR.
GenevestigatorP09769.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR028459. FGR.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERPTHR24418:SF224. PTHR24418:SF224. 1 hit.
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFGR. human.
GeneWikiFGR_(gene).
GenomeRNAi2268.
NextBio9223.
PROP09769.
SOURCESearch...

Entry information

Entry nameFGR_HUMAN
AccessionPrimary (citable) accession number: P09769
Secondary accession number(s): D3DPL7, Q9UIQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 1, 1990
Last modified: July 9, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM