Reviewed, UniProtKB/Swiss-Prot P09769 (FGR_HUMAN)

Names and origin

Protein names

Recommended name:
    Proto-oncogene tyrosine-protein kinase Fgr
    EC=2.7.10.2
Alternative name(s):
    Proto-oncogene c-Fgr
    p55-Fgr

Gene names

Name:	FGR
Synonyms:	SRC2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	529 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	Binds PTPNS1 By similarity.
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
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	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Traceable author statement. Source: ProtInc response to virus Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 529	529	Proto-oncogene 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	27	1	Phosphoserine
	Modified residue	28	1	Phosphotyrosine Ref.8
	Modified residue	34	1	Phosphotyrosine Ref.8
	Modified residue	208	1	Phosphotyrosine Ref.8
	Modified residue	412	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	523	1	Phosphotyrosine
	Modified residue	529	1	Phosphothreonine
Natural variations
	Natural variant	110	1	T → I: dbSNP rs34597831. Ref.10		VAR_041700
	Natural variant	130	1	S → R: dbSNP rs35334091. Ref.10		VAR_041701

Sequences

	Sequence		Length	Mass (Da)
	P09769-1 [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: 3275868] [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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"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: 2852026] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-177 AND 524-529.
[5]	"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: 3330776] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-143.
[6]	"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: 1690869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-142.
[7]	"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: 3023853] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 111-416.
[8]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-28; TYR-34; TYR-208 AND TYR-412, MASS SPECTROMETRY.
[9]	"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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; TYR-34; TYR-412; TYR-523 AND THR-529, MASS SPECTROMETRY.
[10]	"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: 17344846] [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. 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. NP_001036212.1. NP_005239.1.
UniGene	Hs.1422
3D structure databases
SMR	P09769. Positions 79-527.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1049N.
STRING	P09769.
PTM databases
PhosphoSite	P09769.
Proteomic databases
PRIDE	P09769.
Genome annotation databases
Ensembl	ENST00000374003; ENSP00000363115; ENSG00000000938; Homo sapiens. [Genome view] ENST00000374004; ENSP00000363116; ENSG00000000938; Homo sapiens. [Genome view] ENST00000374005; ENSP00000363117; ENSG00000000938; Homo sapiens. [Genome view] ENST00000399173; ENSP00000382126; ENSG00000000938; Homo sapiens. [Genome view]
GeneID	2268.
KEGG	hsa:2268.
UCSC	uc001boj.1. human.
Organism-specific databases
CTD	2268.
GeneCards	GC01M027811.
H-InvDB	HIX0023582.
HGNC	HGNC:3697. FGR.
HPA	CAB018959. HPA002024.
MIM	164940. gene.
PharmGKB	PA28135.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18978.
HOGENOM	HBG755340.
HOVERGEN	P09769.
InParanoid	P09769.
OMA	RGDHVKH.
OrthoDB	EOG9PP12J.
PhylomeDB	P09769.
Enzyme and pathway databases
BRENDA	2.7.10.2. 247.
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.
Gene expression databases
ArrayExpress	P09769.
Bgee	P09769.
CleanEx	HS_FGR.
Genevestigator	P09769.
GermOnline	ENSG00000000938. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR000980. SH2. IPR001452. SH3_domain. IPR020473. SH3_region. IPR020635. Tyr_Pkinase_cat_dom. IPR020685. Tyr_prot_kinase. IPR008266. Tyr_prot_kinase_AS. IPR020746. Tyr_prot_kinase_non-rcpt_Fgr. [Graphical view]
Gene3D	G3DSA:3.30.505.10. SH2. 1 hit.
PANTHER	PTHR23256. Tyr_prot_kinase. 1 hit. PTHR23256:SF257. Tyr_prot_kinase_non-rcpt_Fgr. 1 hit.
Pfam	PF00017. SH2. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00452. SH3DOMAIN.
SMART	SM00252. SH2. 1 hit. SM00326. SH3. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
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 Resources
NextBio	9223.
SOURCE	Search...

Entry information

Entry name

FGR_HUMAN

Accession

Primary (citable) accession number: P09769
Secondary accession number(s): Q9UIQ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 1, 1990
Last modified:	February 9, 2010
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.