P14234 (FGR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase Fgr
EC=2.7.10.2

Alternative name(s):
Proto-oncogene c-Fgr
p55-Fgr

Gene names

Name:

Fgr

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	517 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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, FCER1G and FCGR2. 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 (Ref.10). Required for normal ITGB1 and ITGB2 signaling, normal cell spreading and adhesion in neutrophils and macrophages (Ref.7 and Ref.8). Functions as positive regulator of cell migration and regulates cytoskeleton reorganization via RAC1 activation (Ref.11). Phosphorylates SYK (in vitro) and promotes SYK-dependent activation of AKT1 and MAP kinase signaling (Ref.15). 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.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.11
Enzyme regulation	Activated by autophosphorylation. Prior phosphorylation at Tyr-511 by SRC inhibits ulterior autophosphorylation at Tyr-400. 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.
Subunit structure	Interacts with ITGB1, ITGB2, MS4A2/FCER1B, FCER1G and FCGR2. 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 By similarity. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15
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.11
Post-translational modification	Ubiquitinated. Becomes ubiquitinated in response to ITGB2 signaling; this does not lead to degradation By similarity. Phosphorylated. Autophosphorylated on tyrosine residues. Becomes phosphorylated in response to FCGR2 engagement, cell adhesion and signaling by ITGB2. Prior phosphorylation at Tyr-511 by SRC inhibits ulterior autophosphorylation at Tyr-400 By similarity.
Disruption phenotype	No visible phenotype. Mice lacking both Fgr and Hck are normal and fertile, but show increased susceptibility to infection with Listeria monocytogenes. In addition, their polymorphonuclear leukocytes show defects in cell spreading and adhesion. Ref.6 Ref.7
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
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	defense response to Gram-positive bacterium Inferred from mutant phenotype Ref.6. Source: UniProtKB innate immune response Inferred from electronic annotation. Source: UniProtKB-KW integrin-mediated signaling pathway Inferred from mutant phenotype Ref.10. Source: UniProtKB peptidyl-tyrosine phosphorylation Inferred from direct assay Ref.11. Source: UniProtKB positive regulation of cell migration Inferred from mutant phenotype Ref.11. Source: UniProtKB positive regulation of cytokine secretion Inferred from direct assay Ref.15. Source: UniProtKB positive regulation of mast cell degranulation Inferred from direct assay Ref.15. Source: UniProtKB positive regulation of phosphatidylinositol 3-kinase activity Inferred from electronic annotation. Source: Compara positive regulation of phosphatidylinositol 3-kinase cascade Inferred from electronic annotation. Source: Compara protein autophosphorylation Inferred from electronic annotation. Source: Compara regulation of actin cytoskeleton organization Traceable author statement Ref.11. Source: UniProtKB regulation of cell shape Inferred from mutant phenotype Ref.10. Source: UniProtKB regulation of innate immune response Inferred from mutant phenotype Ref.15. Source: UniProtKB regulation of phagocytosis Inferred from mutant phenotype Ref.10. Source: UniProtKB regulation of protein kinase activity Inferred from direct assay Ref.10. Source: UniProtKB
Cellular_component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay Ref.11Ref.15. Source: UniProtKB ruffle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW immunoglobulin receptor binding Inferred from direct assay Ref.15. Source: UniProtKB non-membrane spanning protein tyrosine kinase activity Inferred from direct assay Ref.11. Source: UniProtKB phosphotyrosine binding Inferred from direct assay Ref.10. Source: UniProtKB protein kinase binding Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Probable
	Chain	2 – 517	516	Tyrosine-protein kinase Fgr		PRO_0000088092
Regions
	Domain	65 – 126	62	SH3
	Domain	132 – 229	98	SH2
	Domain	251 – 504	254	Protein kinase
	Nucleotide binding	257 – 265	9	ATP By similarity
Sites
	Active site	370	1	Proton acceptor By similarity
	Binding site	279	1	ATP By similarity
Amino acid modifications
	Modified residue	13	1	Phosphoserine Ref.13
	Modified residue	25	1	Phosphoserine By similarity
	Modified residue	32	1	Phosphotyrosine By similarity
	Modified residue	196	1	Phosphotyrosine By similarity
	Modified residue	400	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	511	1	Phosphotyrosine; by SRC By similarity
	Modified residue	517	1	Phosphothreonine By similarity
	Lipidation	2	1	N-myristoyl glycine Probable
	Lipidation	3	1	S-palmitoyl cysteine Probable
	Lipidation	6	1	S-palmitoyl cysteine Probable
Experimental info
	Mutagenesis	1 – 7	7	Missing: Abolishes localization at the cell membrane. Ref.11
	Mutagenesis	279	1	K → R: Loss of kinase activity. Ref.9
	Sequence conflict	33	1	F → Y in CAA34463. Ref.1
	Sequence conflict	33	1	F → Y in CAA36437. Ref.2
	Sequence conflict	41	1	T → N in CAA34463. Ref.1
	Sequence conflict	212	1	R → Q in CAA34463. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P14234 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 87DF5B19BF3F4734	FASTA	517	58,867
	10 20 30 40 50 60 MGCVFCKKLE PASKEDVGLE GDFRSQTAEE RYFPDPTQGR TSSVFPQPTS PAFLNTGNMR 70 80 90 100 110 120 SISGTGVTIF VALYDYEART GDDLTFTKGE KFHILNNTEY DWWEARSLSS GHRGYVPSNY 130 140 150 160 170 180 VAPVDSIQAE EWYFGKISRK DAERQLLSSG NPQGAFLIRE SETTKGAYSL SIRDWDQNRG 190 200 210 220 230 240 DHIKHYKIRK LDTGGYYITT RAQFDSIQDL VRHYMEVNDG LCYLLTAPCT TTKPQTLGLA 250 260 270 280 290 300 KDAWEIDRNS IALERRLGTG CFGDVWLGTW NCSTKVAVKT LKPGTMSPKA FLEEAQIMKL 310 320 330 340 350 360 LRHDKLVQLY AVVSEEPIYI VTEFMCYGSL LDFLKDREGQ NLMLPHLVDM AAQVAEGMAY 370 380 390 400 410 420 MERMNYIHRD LRAANILVGE YLICKIADFG LARLIEDNEY NPQQGTKFPI KWTAPEAALF 430 440 450 460 470 480 GRFTVKSDVW SFGILLTELI TKGRVPYPGM NNREVLEQVE HGYHMPCPPG CPASLYEVME 490 500 510 QAWRLDPEER PTFEYLQSFL EDYFTSTEPQ YQPGDQT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the murine c-fgr proto-oncogene cDNA and induction of c-fgr expression by proliferation and activation factors in normal bone marrow-derived monocytic cells." Yi T.L., Willman C.L. Oncogene 4:1081-1087(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: DBA/2J.
[2]	"Molecular cloning and sequencing of the murine c-fgr gene." King F.J., Cole M.D. Oncogene 5:337-344(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Monocytic leukemia.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone and Thymus.
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"Functional overlap in the src gene family: inactivation of hck and fgr impairs natural immunity." Lowell C.A., Soriano P., Varmus H.E. Genes Dev. 8:387-398(1994) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION IN IMMUNITY TO LISTERIA INFECTION.
[7]	"Deficiency of Src family kinases p59/61hck and p58c-fgr results in defective adhesion-dependent neutrophil functions." Lowell C.A., Fumagalli L., Berton G. J. Cell Biol. 133:895-910(1996) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION IN CELL ADHESION AND INTEGRIN SIGNALING.
[8]	"A beta 1 integrin signaling pathway involving Src-family kinases, Cbl and PI-3 kinase is required for macrophage spreading and migration." Meng F., Lowell C.A. EMBO J. 17:4391-4403(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ITGB1 SIGNALING, FUNCTION IN PHOSPHORYLATION OF CBL, INTERACTION WITH CBL.
[9]	"Negative regulation of phagocytosis in murine macrophages by the Src kinase family member, Fgr." Gresham H.D., Dale B.M., Potter J.W., Chang P.W., Vines C.M., Lowell C.A., Lagenaur C.F., Willman C.L. J. Exp. Med. 191:515-528(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SIRPA AND PTPNS1, MUTAGENESIS OF LYS-279, FUNCTION AS NEGATIVE REGULATOR OF PHAGOCYTOSIS.
[10]	"Inhibition of beta 2 integrin receptor and Syk kinase signaling in monocytes by the Src family kinase Fgr." Vines C.M., Potter J.W., Xu Y., Geahlen R.L., Costello P.S., Tybulewicz V.L., Lowell C.A., Chang P.W., Gresham H.D., Willman C.L. Immunity 15:507-519(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS NEGATIVE REGULATOR OF SYK AND INTEGRIN SIGNALING, INTERACTION WITH SYK.
[11]	"The proto-oncogene Fgr regulates cell migration and this requires its plasma membrane localization." Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L., Lowell C.A., Berton G. Exp. Cell Res. 302:253-269(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF CELL MIGRATION; ACTIVATION OF RAC1 AND IN PHOSPHORYLATION OF PIK3R1; PTK2/FAK1; VAV2; PTK2B/PYK2 AND CTTN, CATALYTIC ACTIVITY, INTERACTION WITH PTK2/FAK1, MYRISTOYLATION, PALMITOYLATION, MUTAGENESIS OF 1-MET--LYS-7, SUBCELLULAR LOCATION.
[12]	"Identification of Y589 and Y599 in the juxtamembrane domain of Flt3 as ligand-induced autophosphorylation sites involved in binding of Src family kinases and the protein tyrosine phosphatase SHP2." Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S., Ronnstrand L. Blood 108:1542-1550(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FLT3.
[13]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND TYR-400, MASS SPECTROMETRY. Tissue: Macrophage.
[14]	"c-Abl and Src-family kinases cross-talk in regulation of myeloid cell migration." Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G., Berton G. FEBS Lett. 584:15-21(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF CELL MIGRATION, INTERACTION WITH ABL1; ITGB1 AND ITGB2.
[15]	"The Src family kinase Fgr is critical for activation of mast cells and IgE-mediated anaphylaxis in mice." Lee J.H., Kim J.W., Kim do K., Kim H.S., Park H.J., Park D.K., Kim A.R., Kim B., Beaven M.A., Park K.L., Kim Y.M., Choi W.S. J. Immunol. 187:1807-1815(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF SYK; MAST CELL DEGRANULATION AND RELEASE OF CYTOKINES, INTERACTION WITH FCER1G.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X16440 mRNA. Translation: CAA34463.1. X52191 mRNA. Translation: CAA36437.1. AK036438 mRNA. Translation: BAC29429.1. AK036476 mRNA. Translation: BAC29445.1. AK038141 mRNA. Translation: BAC29939.1. AK155902 mRNA. Translation: BAE33493.1. AL627184 Genomic DNA. Translation: CAM14378.1. CH466552 Genomic DNA. Translation: EDL30081.1. CH466552 Genomic DNA. Translation: EDL30082.1.
IPI	IPI00123708.
PIR	A43807.
RefSeq	NP_034338.3. NM_010208.4.
UniGene	Mm.271665.
3D structure databases
ProteinModelPortal	P14234.
SMR	P14234. Positions 37-515.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-85500.
STRING	10090.ENSMUSP00000030693.
PTM databases
PhosphoSite	P14234.
Proteomic databases
PaxDb	P14234.
PRIDE	P14234.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030693; ENSMUSP00000030693; ENSMUSG00000028874. ENSMUST00000171223; ENSMUSP00000128411; ENSMUSG00000028874.
GeneID	14191.
KEGG	mmu:14191.
Organism-specific databases
CTD	2268.
MGI	MGI:95527. Fgr.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00620000087702.
HOGENOM	HOG000233858.
HOVERGEN	HBG008761.
InParanoid	Q8BGM0.
KO	K08891.
OMA	RGDHVKH.
OrthoDB	EOG4GMTWM.
Enzyme and pathway databases
BRENDA	2.7.10.2. 3474.
Gene expression databases
Bgee	P14234.
Genevestigator	P14234.
GermOnline	ENSMUSG00000028874. Mus musculus.
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
NextBio	285410.
SOURCE	Search...

Entry information

Entry name

FGR_MOUSE

Accession

Primary (citable) accession number: P14234
Secondary accession number(s): Q61404, Q8BGM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program