YES_CANLF
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 03-AUG-2022, entry version 155.
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 EGRF, 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). {ECO:0000250}.
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}.
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DR EMBL; S81472; AAB36132.1; -; mRNA.
DR AlphaFoldDB; Q28923; -.
DR SMR; Q28923; -.
DR STRING; 9612.ENSCAFP00000027127; -.
DR eggNOG; KOG0197; Eukaryota.
DR InParanoid; Q28923; -.
DR BRENDA; 2.7.10.2; 1153.
DR Proteomes; UP000002254; Unplaced.
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:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
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:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd12007; SH3_Yes; 1.
DR Gene3D; 3.30.505.10; -; 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 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; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 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
