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Database: UniProt
Entry: P14238
LinkDB: P14238
Original site: P14238 
ID   FES_FELCA               Reviewed;         820 AA.
AC   P14238;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   29-OCT-2014, entry version 114.
DE   RecName: Full=Tyrosine-protein kinase Fes/Fps;
DE            EC=2.7.10.2;
DE   AltName: Full=Proto-oncogene c-Fes;
GN   Name=FES; Synonyms=FPS;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae;
OC   Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3553615;
RA   Roebroek A.J.M., Schalken J.A., Onnekink C., Bloemers H.P.J.,
RA   van de Ven W.J.M.;
RT   "Structure of the feline c-fes/fps proto-oncogene: genesis of a
RT   retroviral oncogene.";
RL   J. Virol. 61:2009-2016(1987).
CC   -!- FUNCTION: Tyrosine-protein kinase that acts downstream of cell
CC       surface receptors and plays a role in the regulation of the actin
CC       cytoskeleton, microtubule assembly, cell attachment and cell
CC       spreading. Plays a role in FCER1 (high affinity immunoglobulin
CC       epsilon receptor)-mediated signaling in mast cells. Acts down-
CC       stream of the activated FCER1 receptor and the mast/stem cell
CC       growth factor receptor KIT. Plays a role in the regulation of mast
CC       cell degranulation. Plays a role in the regulation of cell
CC       differentiation and promotes neurite outgrowth in response to NGF
CC       signaling. Plays a role in cell scattering and cell migration in
CC       response to HGF-induced activation of EZR. Phosphorylates BCR and
CC       down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1,
CC       PECAM1, STAT3 and TRIM28 (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
CC       ProRule:PRU10028}.
CC   -!- ENZYME REGULATION: Kinase activity is tightly regulated. Activated
CC       in response to signaling from a cell surface receptor. Activation
CC       probably requires binding of a substrate via the SH2 domain, plus
CC       autophosphorylation at Tyr-711. Present in an inactive form in the
CC       absence of activating stimuli (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homooligomer. Interacts with BCR. Interacts (when
CC       activated, via coiled coil domain) with TRIM28. Interacts (via SH2
CC       domain) with phosphorylated EZR, MS4A2/FCER1B and HCLS1/HS1.
CC       Interacts with phosphorylated KIT. Interacts with FLT3. Interacts
CC       (via FCH domain) with soluble tubulin. Interacts (via SH2 domain)
CC       with microtubules (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm,
CC       cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Golgi apparatus
CC       {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}.
CC       Note=Distributed throughout the cytosol when the kinase is not
CC       activated. Association with microtubules requires activation of
CC       the kinase activity. Shuttles between focal adhesions and cell-
CC       cell contacts in epithelial cells. Recruited to the lateral cell
CC       membrane in polarized epithelial cells by interaction with
CC       phosphorylated EZR. Detected at tubular membrane structures in the
CC       cytoplasm and at the cell periphery (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: The coiled coil domains are important for regulating the
CC       kinase activity. They mediate homooligomerization and probably
CC       also interaction with other proteins (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal region including the first coiled coil
CC       domain mediates interaction with phosphoinositide-containing
CC       membranes. {ECO:0000250}.
CC   -!- PTM: Autophosphorylated on Tyr-711 in response to FGF2.
CC       Phosphorylated by LYN in response to FCER1 activation.
CC       Phosphorylated by HCK (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Fes/fps subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
CC   -!- SIMILARITY: Contains 1 FCH domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00083}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SIMILARITY: Contains 1 SH2 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00191}.
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DR   EMBL; M16705; AAA30808.1; -; Genomic_DNA.
DR   EMBL; M16666; AAA30808.1; JOINED; Genomic_DNA.
DR   EMBL; M16667; AAA30808.1; JOINED; Genomic_DNA.
DR   EMBL; M16668; AAA30808.1; JOINED; Genomic_DNA.
DR   EMBL; M16669; AAA30808.1; JOINED; Genomic_DNA.
DR   EMBL; M16670; AAA30808.1; JOINED; Genomic_DNA.
DR   EMBL; M16671; AAA30808.1; JOINED; Genomic_DNA.
DR   EMBL; M16706; AAA30808.1; JOINED; Genomic_DNA.
DR   EMBL; M16672; AAA30808.1; JOINED; Genomic_DNA.
DR   EMBL; M16673; AAA30808.1; JOINED; Genomic_DNA.
DR   EMBL; M16674; AAA30808.1; JOINED; Genomic_DNA.
DR   EMBL; M16698; AAA30808.1; JOINED; Genomic_DNA.
DR   EMBL; M16700; AAA30808.1; JOINED; Genomic_DNA.
DR   EMBL; M16701; AAA30808.1; JOINED; Genomic_DNA.
DR   EMBL; M16702; AAA30808.1; JOINED; Genomic_DNA.
DR   EMBL; M16704; AAA30808.1; JOINED; Genomic_DNA.
DR   PIR; A27824; TVCTFF.
DR   ProteinModelPortal; P14238; -.
DR   SMR; P14238; 447-819.
DR   STRING; 9685.ENSFCAP00000005663; -.
DR   PRIDE; P14238; -.
DR   eggNOG; COG0515; -.
DR   HOVERGEN; HBG005655; -.
DR   InParanoid; P14238; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR   GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0034987; F:immunoglobulin receptor binding; ISS:UniProtKB.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISS:UniProtKB.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR   GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISS:UniProtKB.
DR   GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
DR   GO; GO:0045639; P:positive regulation of myeloid cell differentiation; ISS:UniProtKB.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR   GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
DR   GO; GO:0045595; P:regulation of cell differentiation; ISS:UniProtKB.
DR   GO; GO:2000145; P:regulation of cell motility; ISS:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell proliferation; ISS:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR   GO; GO:0043304; P:regulation of mast cell degranulation; ISS:UniProtKB.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR016250; Tyr-prot_kinase_Fes/Fps.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PIRSF; PIRSF000632; TyrPK_fps; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50133; FCH; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell junction; Cell membrane; Coiled coil;
KW   Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW   Golgi apparatus; Kinase; Lipid-binding; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Proto-oncogene; Reference proteome; SH2 domain;
KW   Transferase; Tumor suppressor; Tyrosine-protein kinase.
FT   CHAIN         1    820       Tyrosine-protein kinase Fes/Fps.
FT                                /FTId=PRO_0000088085.
FT   DOMAIN        1     94       FCH. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00083}.
FT   DOMAIN      458    547       SH2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00191}.
FT   DOMAIN      559    820       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     565    573       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION        1    298       Important for interaction with membranes
FT                                containing phosphoinositides.
FT                                {ECO:0000250}.
FT   COILED      123    163       {ECO:0000255}.
FT   COILED      318    389       {ECO:0000255}.
FT   ACT_SITE    681    681       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10028}.
FT   BINDING     588    588       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES      65     65       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     259    259       Phosphotyrosine. {ECO:0000250}.
FT   MOD_RES     419    419       Phosphothreonine. {ECO:0000250}.
FT   MOD_RES     711    711       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000250}.
FT   MOD_RES     714    714       Phosphoserine. {ECO:0000250}.
SQ   SEQUENCE   820 AA;  92975 MW;  F3A52B750236834E CRC64;
     MGFSSELCSP QGHGAVQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH MSLQDGGGRG
     TGPYSPISQS WAEITSQTEG LSRLLRQHAE DLNSGPLSKL GLLIRERQQL RKTYSEQWQQ
     LQQELTKTHN QDIEKLKSQY RALARDSAQA RRKYQEASKD KDRDKAKDKY VRSLWKLFAH
     HNRYVLGVRA AQLHHHHHHQ LMLPGLLQSL QDLHQEMACI LKEILQEYLE ISSLVQDEVV
     AIHLEMAAAV ARIQPEAEYQ GFLRQYGSTP DVPPCVTFDE SLLEEGEPLE PGELQLNELT
     VESVQHTLTS VTDELTVATQ TVLSRQEAVA QLQRELQNEE QNTHPRERVQ LLAKKQVLQE
     ALQALQVALC SQAKLQAQRE LLQAKLEQLG PGEPPPVLLL QDDRHSTSSS EQEREGGRTP
     TLEILKSHIS GIFRPKFSLP PPLQLVPEVQ KPLHEQLWYH GALPRAEVAE LLTHSGDFLV
     RESQGKQEYV LSVLWDGQPR HFIIESADNL YRLEGDGFAS IPLLVDHLLR SQQPLTKKSG
     IVLNRAVPKD KWVLNHEDLV LGEQIGRGNF GEVFSGRLRA DNTLVAVKSC RETLPPDIKA
     KFLQEAKILK QYSHPNIVRL IGVCTQKQPI YIVMELVQGG DFLTFLRTEG ARLRMKTLLQ
     MVGDAAAGME YLESKCCIHR DLAARNCLVT EKNVLKISDF GMSREEADGI YAASGGLRQV
     PVKWTAPEAL NYGRYSSESD VWSFGILLWE TFSLGASPYP NLSNQQTREF VEKGGRLPCP
     ELCPDAVFRL MEQCWAYEPG QRPSFSAIYQ ELQSIRKRHR
//
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