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Tyrosine-protein kinase Fes/Fps (EC 2.7.10.2) (Proto-oncogene c-Fes)

 FES_FELCA               Reviewed;         820 AA.
P14238;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
28-FEB-2018, entry version 135.
RecName: Full=Tyrosine-protein kinase Fes/Fps;
EC=2.7.10.2;
AltName: Full=Proto-oncogene c-Fes;
Name=FES; Synonyms=FPS;
Felis catus (Cat) (Felis silvestris catus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae;
Felinae; Felis.
NCBI_TaxID=9685;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3553615;
Roebroek A.J.M., Schalken J.A., Onnekink C., Bloemers H.P.J.,
van de Ven W.J.M.;
"Structure of the feline c-fes/fps proto-oncogene: genesis of a
retroviral oncogene.";
J. Virol. 61:2009-2016(1987).
-!- FUNCTION: Tyrosine-protein kinase that acts downstream of cell
surface receptors and plays a role in the regulation of the actin
cytoskeleton, microtubule assembly, cell attachment and cell
spreading. Plays a role in FCER1 (high affinity immunoglobulin
epsilon receptor)-mediated signaling in mast cells. Acts down-
stream of the activated FCER1 receptor and the mast/stem cell
growth factor receptor KIT. Plays a role in the regulation of mast
cell degranulation. Plays a role in the regulation of cell
differentiation and promotes neurite outgrowth in response to NGF
signaling. Plays a role in cell scattering and cell migration in
response to HGF-induced activation of EZR. Phosphorylates BCR and
down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1,
PECAM1, STAT3 and TRIM28 (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Kinase activity is tightly regulated. Activated
in response to signaling from a cell surface receptor. Activation
probably requires binding of a substrate via the SH2 domain, plus
autophosphorylation at Tyr-711. Present in an inactive form in the
absence of activating stimuli (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homooligomer. Interacts with BCR. Interacts (when
activated, via coiled coil domain) with TRIM28. Interacts (via SH2
domain) with phosphorylated EZR, MS4A2/FCER1B and HCLS1/HS1.
Interacts with phosphorylated KIT. Interacts with FLT3. Interacts
(via F-BAR domain) with soluble tubulin. Interacts (via SH2
domain) with microtubules (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm,
cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Golgi apparatus
{ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}.
Note=Distributed throughout the cytosol when the kinase is not
activated. Association with microtubules requires activation of
the kinase activity. Shuttles between focal adhesions and cell-
cell contacts in epithelial cells. Recruited to the lateral cell
membrane in polarized epithelial cells by interaction with
phosphorylated EZR. Detected at tubular membrane structures in the
cytoplasm and at the cell periphery (By similarity).
{ECO:0000250}.
-!- DOMAIN: The coiled coil domains are important for regulating the
kinase activity. They mediate homooligomerization and probably
also interaction with other proteins (By similarity).
{ECO:0000250}.
-!- DOMAIN: The N-terminal region including the first coiled coil
domain mediates interaction with phosphoinositide-containing
membranes. {ECO:0000250}.
-!- PTM: Autophosphorylated on Tyr-711 in response to FGF2.
Phosphorylated by LYN in response to FCER1 activation.
Phosphorylated by HCK (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Fes/fps subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; M16705; AAA30808.1; -; Genomic_DNA.
EMBL; M16666; AAA30808.1; JOINED; Genomic_DNA.
EMBL; M16667; AAA30808.1; JOINED; Genomic_DNA.
EMBL; M16668; AAA30808.1; JOINED; Genomic_DNA.
EMBL; M16669; AAA30808.1; JOINED; Genomic_DNA.
EMBL; M16670; AAA30808.1; JOINED; Genomic_DNA.
EMBL; M16671; AAA30808.1; JOINED; Genomic_DNA.
EMBL; M16706; AAA30808.1; JOINED; Genomic_DNA.
EMBL; M16672; AAA30808.1; JOINED; Genomic_DNA.
EMBL; M16673; AAA30808.1; JOINED; Genomic_DNA.
EMBL; M16674; AAA30808.1; JOINED; Genomic_DNA.
EMBL; M16698; AAA30808.1; JOINED; Genomic_DNA.
EMBL; M16700; AAA30808.1; JOINED; Genomic_DNA.
EMBL; M16701; AAA30808.1; JOINED; Genomic_DNA.
EMBL; M16702; AAA30808.1; JOINED; Genomic_DNA.
EMBL; M16704; AAA30808.1; JOINED; Genomic_DNA.
PIR; A27824; TVCTFF.
ProteinModelPortal; P14238; -.
SMR; P14238; -.
STRING; 9685.ENSFCAP00000005663; -.
PRIDE; P14238; -.
eggNOG; KOG0194; Eukaryota.
eggNOG; ENOG410Y6RP; LUCA.
HOVERGEN; HBG005655; -.
InParanoid; P14238; -.
Proteomes; UP000011712; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0034987; F:immunoglobulin receptor binding; ISS:UniProtKB.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0005102; F:receptor binding; IBA:GO_Central.
GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
GO; GO:0045639; P:positive regulation of myeloid cell differentiation; ISS:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
GO; GO:0045595; P:regulation of cell differentiation; ISS:UniProtKB.
GO; GO:2000145; P:regulation of cell motility; ISS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
GO; GO:0043304; P:regulation of mast cell degranulation; ISS:UniProtKB.
CDD; cd10361; SH2_Fps_family; 1.
Gene3D; 1.20.1270.60; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR031160; F_BAR.
InterPro; IPR001060; FCH_dom.
InterPro; IPR035849; Fes/Fps/Fer_SH2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR016250; Tyr-prot_kinase_Fes/Fps.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
PIRSF; PIRSF000632; TyrPK_fps; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00055; FCH; 1.
SMART; SM00252; SH2; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF103657; SSF103657; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51741; F_BAR; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
3: Inferred from homology;
ATP-binding; Cell junction; Cell membrane; Coiled coil;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
Golgi apparatus; Kinase; Lipid-binding; Membrane; Nucleotide-binding;
Phosphoprotein; Proto-oncogene; Reference proteome; SH2 domain;
Transferase; Tumor suppressor; Tyrosine-protein kinase.
CHAIN 1 820 Tyrosine-protein kinase Fes/Fps.
/FTId=PRO_0000088085.
DOMAIN 1 258 F-BAR. {ECO:0000255|PROSITE-
ProRule:PRU01077}.
DOMAIN 458 547 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 559 820 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 565 573 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 298 Important for interaction with membranes
containing phosphoinositides.
{ECO:0000250}.
COILED 123 163 {ECO:0000255}.
COILED 318 389 {ECO:0000255}.
ACT_SITE 681 681 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 588 588 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 65 65 Phosphoserine.
{ECO:0000250|UniProtKB:P07332}.
MOD_RES 259 259 Phosphotyrosine.
{ECO:0000250|UniProtKB:P07332}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000250|UniProtKB:P07332}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000250|UniProtKB:P07332}.
MOD_RES 419 419 Phosphothreonine.
{ECO:0000250|UniProtKB:P07332}.
MOD_RES 711 711 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P07332}.
MOD_RES 714 714 Phosphoserine.
{ECO:0000250|UniProtKB:P07332}.
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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