ID   YES_CANLF               Reviewed;         539 AA.
AC   Q28923;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Tyrosine-protein kinase Yes;
DE            EC=2.7.10.2;
DE   AltName: Full=Proto-oncogene c-Yes;
DE   AltName: Full=p61-Yes;
GN   Name=YES1; Synonyms=YES;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
RX   PubMed=8588097; DOI=10.1016/0034-5288(95)90008-x;
RA   Zhao D.M., Tateyama S., Miyoshi N., Uchida K., Yamaguchi R., Yamagami T.,
RA   Hayashi T.;
RT   "Sequence of the canine c-yes proto-oncogene.";
RL   Res. Vet. Sci. 59:230-233(1995).
RN   [2]
RP   INTERACTION WITH OCLLUDIN/OCLN, AND SUBCELLULAR LOCATION.
RX   PubMed=11950934; DOI=10.1091/mbc.01-08-0423;
RA   Chen Y.H., Lu Q., Goodenough D.A., Jeansonne B.;
RT   "Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight
RT   junction formation in canine kidney epithelial cells.";
RL   Mol. Biol. Cell 13:1227-1237(2002).
CC   -!- FUNCTION: Non-receptor protein tyrosine kinase that is involved in the
CC       regulation of cell growth and survival, apoptosis, cell-cell adhesion,
CC       cytoskeleton remodeling, and differentiation. Stimulation by receptor
CC       tyrosine kinases (RTKs) including EGFR, PDGFR, CSF1R and FGFR leads to
CC       recruitment of YES1 to the phosphorylated receptor, and activation and
CC       phosphorylation of downstream substrates. Upon EGFR activation,
CC       promotes the phosphorylation of PARD3 to favor epithelial tight
CC       junction assembly. Participates in the phosphorylation of specific
CC       junctional components such as CTNND1 by stimulating the FYN and FER
CC       tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by
CC       CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and
CC       induces T-cell migration. Participates in CD95L/FASLG signaling pathway
CC       and mediates AKT-mediated cell migration. Plays a role in cell cycle
CC       progression by phosphorylating the cyclin dependent kinase 4/CDK4 thus
CC       regulating the G1 phase. Also involved in G2/M progression and
CC       cytokinesis (By similarity). Catalyzes phosphorylation of organic
CC       cation transporter OCT2 which induces its transport activity (By
CC       similarity). {ECO:0000250, ECO:0000250|UniProtKB:P07947}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- SUBUNIT: Interacts with YAP1. Interacts with FASLG. Interacts with
CC       CTNND1; this interaction allows YES1-mediated activation of FYN and FER
CC       and subsequent phosphorylation of CTNND1. Interacts with CSF1R (By
CC       similarity). Interacts with IL6ST/gp130 (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P07947}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC       Cytoplasm, cytosol {ECO:0000250}. Note=Newly synthesized protein
CC       initially accumulates in the Golgi region and traffics to the plasma
CC       membrane through the exocytic pathway. {ECO:0000250}.
CC   -!- PTM: Phosphorylation by CSK on the C-terminal tail maintains the enzyme
CC       in an inactive state. Autophosphorylation at Tyr-422 maintains enzyme
CC       activity by blocking CSK-mediated inhibition (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Palmitoylation at Cys-3 promotes membrane localization.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; S81472; AAB36132.1; -; mRNA.
DR   AlphaFoldDB; Q28923; -.
DR   SMR; Q28923; -.
DR   STRING; 9615.ENSCAFP00000063973; -.
DR   SwissPalm; Q28923; -.
DR   PaxDb; 9612-ENSCAFP00000027127; -.
DR   eggNOG; KOG0197; Eukaryota.
DR   InParanoid; Q28923; -.
DR   BRENDA; 2.7.10.2; 1153.
DR   Proteomes; UP000002254; Unplaced.
DR   Proteomes; UP000694429; Unplaced.
DR   Proteomes; UP000694542; Unplaced.
DR   Proteomes; UP000805418; Unplaced.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   CDD; cd05069; PTKc_Yes; 1.
DR   CDD; cd09933; SH2_Src_family; 1.
DR   CDD; cd12007; SH3_Yes; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
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; IPR036860; SH2_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR035751; Yes_SH3.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24418:SF90; TYROSINE-PROTEIN KINASE YES; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 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.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Cytoplasm; Cytoskeleton; Kinase; Lipoprotein;
KW   Membrane; Myristate; Nucleotide-binding; Palmitate; Phosphoprotein;
KW   Proto-oncogene; Reference proteome; SH2 domain; SH3 domain; Transferase;
KW   Tyrosine-protein kinase.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..539
FT                   /note="Tyrosine-protein kinase Yes"
FT                   /id="PRO_0000088180"
FT   DOMAIN          87..148
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          154..251
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          273..526
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        392
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         279..287
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         301
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         19
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P07947"
FT   MOD_RES         28
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q04736"
FT   MOD_RES         332
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P07947"
FT   MOD_RES         341
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P07947"
FT   MOD_RES         422
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P07947"
FT   MOD_RES         533
FT                   /note="Phosphotyrosine; by CSK"
FT                   /evidence="ECO:0000250|UniProtKB:P07947"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine; in membrane form"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   539 AA;  60300 MW;  CC4BEA38073CC106 CRC64;
     MGCIKSKEDK GPAIKYRNTP EPVSVSHYGA EPTQATPWPS SSGWGTAFNF SSLSMTGFGG
     SSGVTPFGGA SSSFSVVPSP YPAGLTGGVT IFVALYDYEA RTTEDLSFKG GERFQIINNT
     EGDWWEARSI ATGKNGYIPS NYVAPADSIA AEEWYFGKMG RKDAERLLLN PGNQRGIFLV
     RESETTKGAY SLSIRDWDEI RGDNVKHYKI RKLDNGGYYI TTRAQFDTLQ KLVKHSTEHA
     DGLCHKLTTV CPTVKPQTQG LAKDAWEIPR ESLRLEVKLG QGCFGEVWMG TWNGTTKVAI
     KTLKLGTMMP EAFLQEAQIM KKLRHDKLVP LYAVVSEEPI YIVTEFMSKG SLLDFLKEGD
     GKYLKLPQLV DMAAQIADGM AYIERMNYIH RDLRAANILV GENLVCKIAD FGLARLIEDN
     EYTARQGAKF PIKWTAPEAA LYGRFTIKSD VWSFGILQTE LTTKGRVPYP GMVNREVLEQ
     VERGYRMPCP QGCPESLHEL MNLCWKKDPD ERPTFEYIQS FLEDYFTAAE PQYQPGENL
//