P09769 (FGR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	529 AA.
Sequence status	Complete.
Protein existence	Evidence 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 projection › ruffle membrane. Cytoplasm › cytosol. Cytoplasm › cytoskeleton. 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 process	Immunity Innate immunity
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Polymorphism
Disease	Proto-oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 Inferred from electronic annotation. Source: UniProtKB-KW 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 cascade Inferred from mutant phenotype Ref.14. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.9Ref.11. Source: UniProtKB 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_component	actin cytoskeleton Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome 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_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW Fc-gamma receptor I complex binding Inferred from direct assay Ref.11. 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 kinase binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSP90AB1	P08238	2	EBI-1383732,EBI-352572

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 529	529	Tyrosine-protein kinase Fgr		PRO_0000088091
Regions
	Domain	77 – 138	62	SH3
	Domain	144 – 241	98	SH2
	Domain	263 – 516	254	Protein kinase
	Nucleotide binding	269 – 277	9	ATP By similarity
Sites
	Active site	382	1	Proton acceptor By similarity
	Binding site	291	1	ATP By similarity
Amino acid modifications
	Modified residue	34	1	Phosphotyrosine Ref.18
	Modified residue	412	1	Phosphotyrosine Ref.18
	Modified residue	523	1	Phosphotyrosine; by SRC Ref.18
	Lipidation	2	1	N-myristoyl glycine By similarity
	Lipidation	3	1	S-palmitoyl cysteine By similarity
	Lipidation	6	1	S-palmitoyl cysteine By similarity
Natural variations
	Natural variant	110	1	T → I. Ref.19 Corresponds to variant rs34597831 [ dbSNP | Ensembl ].		VAR_041700
	Natural variant	130	1	S → R. Ref.19 Corresponds to variant rs35334091 [ dbSNP | Ensembl ].		VAR_041701
Experimental info
	Mutagenesis	523	1	Y → F: Strongly increased catalytic activity. Functions as oncogene. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	P09769 [UniParc]. Last modified January 1, 1990. Version 2. Checksum: 6B8C1E08414E0F9C	FASTA	529	59,479
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY.
[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. , 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 , M12719, M12720, M12721, M12722, M12723 Genomic DNA. Translation: AAA52762.1.
IPI	IPI00016871.
PIR	TVHUFR. A27676.
RefSeq	NP_001036194.1. NM_001042729.1. NP_001036212.1. NM_001042747.1. NP_005239.1. NM_005248.2.
UniGene	Hs.1422.
3D structure databases
ProteinModelPortal	P09769.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1049N.
IntAct	P09769. 4 interactions.
MINT	MINT-1209880.
STRING	9606.ENSP00000363115.
PTM databases
PhosphoSite	P09769.
Polymorphism databases
DMDM	125358.
Proteomic databases
PaxDb	P09769.
PRIDE	P09769.
Protocols and materials databases
DNASU	2268.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000374003; ENSP00000363115; ENSG00000000938. ENST00000374004; ENSP00000363116; ENSG00000000938. ENST00000374005; ENSP00000363117; ENSG00000000938. ENST00000399173; ENSP00000382126; ENSG00000000938.
GeneID	2268.
KEGG	hsa:2268.
UCSC	uc001boj.3. human.
Organism-specific databases
CTD	2268.
GeneCards	GC01M027938.
HGNC	HGNC:3697. FGR.
HPA	CAB018959. HPA002024.
MIM	164940. gene.
neXtProt	NX_P09769.
PharmGKB	PA28135.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233858.
HOVERGEN	HBG008761.
InParanoid	P09769.
KO	K08891.
OMA	RGDHVKH.
OrthoDB	EOG4GMTWM.
PhylomeDB	P09769.
Enzyme and pathway databases
Pathway_Interaction_DB	alphasynuclein_pathway. Alpha-synuclein signaling. amb2_neutrophils_pathway. amb2 Integrin signaling. pi3kcipathway. Class I PI3K signaling events. epha_fwdpathway. EPHA forward signaling. ephrinbrevpathway. Ephrin B reverse signaling. glypican_1pathway. Glypican 1 network. pdgfrbpathway. PDGFR-beta signaling pathway. p38alphabetapathway. Regulation of p38-alpha and p38-beta. ptp1bpathway. Signaling events mediated by PTP1B. txa2pathway. Thromboxane A2 receptor signaling.
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P09769.
Bgee	P09769.
CleanEx	HS_FGR.
Genevestigator	P09769.
GermOnline	ENSG00000000938. Homo sapiens.
Family and domain databases
Gene3D	3.30.505.10. 1 hit.
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_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]
Pfam	PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00452. SH3DOMAIN. PR00109. TYRKINASE.
SMART	SM00252. SH2. 1 hit. SM00326. SH3. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF50044. SH3. 1 hit.
PROSITE	PS00107. 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]
ProtoNet	Search...
Other
BindingDB	P09769.
ChEMBL	CHEMBL4454.
ChiTaRS	FGR. human.
GenomeRNAi	2268.
NextBio	9223.
SOURCE	Search...

Entry information

Entry name

FGR_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 148 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.