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P14234 (FGR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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):
Proto-oncogene c-Fgr
p55-Fgr
Gene names
Name:Fgr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length517 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, 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 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.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 processImmunity
Innate immunity
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Mitochondrion
Mitochondrion inner membrane
   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_processdefense 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: Ensembl

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

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_componentcytoskeleton

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_functionATP 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...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ClnkQ9QZE23EBI-7587024,EBI-8040679

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Probable
Chain2 – 517516Tyrosine-protein kinase Fgr
PRO_0000088092

Regions

Domain65 – 12662SH3
Domain132 – 22998SH2
Domain251 – 504254Protein kinase
Nucleotide binding257 – 2659ATP By similarity

Sites

Active site3701Proton acceptor By similarity
Binding site2791ATP By similarity

Amino acid modifications

Modified residue131Phosphoserine Ref.13
Modified residue321Phosphotyrosine By similarity
Modified residue4001Phosphotyrosine; alternate Ref.13
Modified residue4001Phosphotyrosine; by autocatalysis; alternate By similarity
Modified residue5111Phosphotyrosine; by SRC By similarity
Lipidation21N-myristoyl glycine Probable
Lipidation31S-palmitoyl cysteine Probable
Lipidation61S-palmitoyl cysteine Probable

Experimental info

Mutagenesis1 – 77Missing: Abolishes localization at the cell membrane. Ref.11
Mutagenesis2791K → R: Loss of kinase activity. Ref.9
Sequence conflict331F → Y in CAA34463. Ref.1
Sequence conflict331F → Y in CAA36437. Ref.2
Sequence conflict411T → N in CAA34463. Ref.1
Sequence conflict2121R → Q in CAA34463. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P14234 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 87DF5B19BF3F4734

FASTA51758,867
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
PIRA43807.
RefSeqNP_034338.3. NM_010208.4.
XP_006538607.1. XM_006538544.1.
XP_006538608.1. XM_006538545.1.
UniGeneMm.271665.

3D structure databases

ProteinModelPortalP14234.
SMRP14234. Positions 37-515.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199663. 1 interaction.
IntActP14234. 3 interactions.
MINTMINT-85500.
STRING10090.ENSMUSP00000030693.

Chemistry

ChEMBLCHEMBL2034795.

PTM databases

PhosphoSiteP14234.

Proteomic databases

PaxDbP14234.
PRIDEP14234.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030693; ENSMUSP00000030693; ENSMUSG00000028874.
ENSMUST00000171223; ENSMUSP00000128411; ENSMUSG00000028874.
GeneID14191.
KEGGmmu:14191.
UCSCuc012dmj.1. mouse.

Organism-specific databases

CTD2268.
MGIMGI:95527. Fgr.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00620000087702.
HOGENOMHOG000233858.
HOVERGENHBG008761.
InParanoidQ8BGM0.
KOK08891.
OMATWNGSTK.
OrthoDBEOG7GTT2V.
TreeFamTF351634.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.

Gene expression databases

BgeeP14234.
GenevestigatorP14234.

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:SF45. PTHR24418:SF45. 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

NextBio285410.
PROP14234.
SOURCESearch...

Entry information

Entry nameFGR_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot