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 01-MAY-2013, entry version 103.
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).
CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC [protein]-L-tyrosine phosphate.
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).
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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC Cytoplasm, cytoskeleton (By similarity). Cell membrane; Peripheral
CC membrane protein; Cytoplasmic side (By similarity). Cytoplasmic
CC vesicle (By similarity). Golgi apparatus (By similarity). Cell
CC junction, focal adhesion (By similarity). Note=Distributed
CC throughout the cytosol when the kinase is not activated.
CC Association with microtubules requires activation of the kinase
CC activity. Shuttles between focal adhesions and cell-cell contacts
CC in epithelial cells. Recruited to the lateral cell membrane in
CC polarized epithelial cells by interaction with phosphorylated EZR.
CC Detected at tubular membrane structures in the cytoplasm and at
CC the cell periphery (By similarity).
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 -!- DOMAIN: The N-terminal region including the first coiled coil
CC domain mediates interaction with phosphoinositide-containing
CC membranes (By similarity).
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).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Fes/fps subfamily.
CC -!- SIMILARITY: Contains 1 FCH domain.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SIMILARITY: Contains 1 SH2 domain.
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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 eggNOG; COG0515; -.
DR HOVERGEN; HBG005655; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic to internal side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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: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: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_cat_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016250; Tyr_kinase_non-rcpt_Fes_subgr.
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; SSF56112; Kinase_like; 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; SH2 domain; Transferase;
KW Tumor suppressor; Tyrosine-protein kinase.
FT CHAIN 1 820 Tyrosine-protein kinase Fes/Fps.
FT /FTId=PRO_0000088085.
FT DOMAIN 1 94 FCH.
FT DOMAIN 458 547 SH2.
FT DOMAIN 559 820 Protein kinase.
FT NP_BIND 565 573 ATP (By similarity).
FT REGION 1 298 Important for interaction with membranes
FT containing phosphoinositides (By
FT similarity).
FT COILED 123 163 Potential.
FT COILED 318 389 Potential.
FT ACT_SITE 681 681 Proton acceptor (By similarity).
FT BINDING 588 588 ATP (By similarity).
FT MOD_RES 65 65 Phosphoserine (By similarity).
FT MOD_RES 259 259 Phosphotyrosine (By similarity).
FT MOD_RES 419 419 Phosphothreonine (By similarity).
FT MOD_RES 711 711 Phosphotyrosine; by autocatalysis (By
FT similarity).
FT MOD_RES 714 714 Phosphoserine (By similarity).
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
//
