ID   YES_CHICK               Reviewed;         541 AA.
AC   P09324;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 194.
DE   RecName: Full=Tyrosine-protein kinase Yes;
DE            EC=2.7.10.2;
DE   AltName: Full=p61-Yes;
GN   Name=YES1; Synonyms=YES;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3054816; DOI=10.1093/nar/16.20.9876;
RA   Sudol M., Kieswetter C., Zhao Y.H., Dorai T., Wang L.H., Hanafusa H.;
RT   "Nucleotide sequence of a cDNA for the chick yes proto-oncogene: comparison
RT   with the viral yes gene.";
RL   Nucleic Acids Res. 16:9876-9876(1988).
RN   [2]
RP   SEQUENCE REVISION TO 233.
RA   Sudol M.;
RL   Submitted (NOV-1988) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain, and Kidney;
RX   PubMed=2464785;
RA   Zheng X., Podell S., Sefton B.M., Kaplan P.L.;
RT   "The sequence of chicken c-yes and p61c-yes.";
RL   Oncogene 4:99-104(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 396-451.
RX   PubMed=1281306;
RA   Marcelle C., Eichmann A.;
RT   "Molecular cloning of a family of protein kinase genes expressed in the
RT   avian embryo.";
RL   Oncogene 7:2479-2487(1992).
RN   [5]
RP   INTERACTION WITH YAP1.
RX   PubMed=8035999;
RA   Sudol M.;
RT   "Yes-associated protein (YAP65) is a proline-rich phosphoprotein that binds
RT   to the SH3 domain of the Yes proto-oncogene product.";
RL   Oncogene 9:2145-2152(1994).
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, differentiation, G2/M progression and
CC       cytokinesis. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC       Cytoplasm, cytosol {ECO:0000250}. Cell junction
CC       {ECO:0000250|UniProtKB:Q28923}.
CC   -!- PTM: Autophosphorylation at Tyr-424 maintains enzyme activity.
CC       {ECO:0000250|UniProtKB:P07947}.
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; X12461; CAA31002.1; -; mRNA.
DR   EMBL; X13207; CAA31595.1; -; mRNA.
DR   EMBL; X69695; CAA49365.1; -; mRNA.
DR   PIR; S03324; TVCHYS.
DR   RefSeq; NP_990632.1; NM_205301.2.
DR   AlphaFoldDB; P09324; -.
DR   SMR; P09324; -.
DR   FunCoup; P09324; 272.
DR   STRING; 9031.ENSGALP00000050000; -.
DR   PaxDb; 9031-ENSGALP00000050000; -.
DR   Ensembl; ENSGALT00010008965.1; ENSGALP00010005290.1; ENSGALG00010003874.1.
DR   GeneID; 396238; -.
DR   KEGG; gga:396238; -.
DR   CTD; 7525; -.
DR   VEuPathDB; HostDB:geneid_396238; -.
DR   eggNOG; KOG0197; Eukaryota.
DR   GeneTree; ENSGT00940000154920; -.
DR   HOGENOM; CLU_000288_7_2_1; -.
DR   InParanoid; P09324; -.
DR   OMA; RTENTPD; -.
DR   OrthoDB; 4062651at2759; -.
DR   PhylomeDB; P09324; -.
DR   BRENDA; 2.7.10.2; 1306.
DR   Reactome; R-GGA-1227986; Signaling by ERBB2.
DR   Reactome; R-GGA-1433557; Signaling by SCF-KIT.
DR   Reactome; R-GGA-1433559; Regulation of KIT signaling.
DR   Reactome; R-GGA-210990; PECAM1 interactions.
DR   Reactome; R-GGA-389356; Co-stimulation by CD28.
DR   Reactome; R-GGA-389513; Co-inhibition by CTLA4.
DR   Reactome; R-GGA-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-GGA-3928663; EPHA-mediated growth cone collapse.
DR   Reactome; R-GGA-3928665; EPH-ephrin mediated repulsion of cells.
DR   Reactome; R-GGA-912631; Regulation of signaling by CBL.
DR   PRO; PR:P09324; -.
DR   Proteomes; UP000000539; Chromosome 2.
DR   Bgee; ENSGALG00000014860; Expressed in kidney and 12 other cell types or tissues.
DR   GO; GO:0070161; C:anchoring junction; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; IEA:Ensembl.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0007169; P:cell surface 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   FunFam; 1.10.510.10:FF:000553; Tyrosine-protein kinase; 1.
DR   FunFam; 2.30.30.40:FF:000022; Tyrosine-protein kinase; 1.
DR   FunFam; 3.30.200.20:FF:000016; Tyrosine-protein kinase; 1.
DR   FunFam; 3.30.505.10:FF:000001; Tyrosine-protein kinase; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 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; IPR050198; Non-receptor_tyrosine_kinases.
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   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 junction; Cell membrane; Cytoplasm; Cytoskeleton; Kinase;
KW   Lipoprotein; Membrane; Myristate; Nucleotide-binding; Palmitate;
KW   Phosphoprotein; Reference proteome; SH2 domain; SH3 domain; Transferase;
KW   Tyrosine-protein kinase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..541
FT                   /note="Tyrosine-protein kinase Yes"
FT                   /id="PRO_0000088183"
FT   DOMAIN          89..150
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          156..253
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          275..528
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..37
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        394
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         281..289
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         303
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         424
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P07947"
FT   MOD_RES         535
FT                   /note="Phosphotyrosine; by CSK"
FT                   /evidence="ECO:0000250"
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"
FT   CONFLICT        67..71
FT                   /note="TPFGG -> IHPLR (in Ref. 3; CAA31595)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82
FT                   /note="P -> Q (in Ref. 3; CAA31595)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   541 AA;  60792 MW;  BEA849CC7D1755AF CRC64;
     MGCIKSKEDK GPAMKYRTDN TPEPISSHVS HYGSDSSQAT QSPAIKGSAV NFNSHSMTPF
     GGPSGMTPFG GASSSFSAVP SPYPSTLTGG VTVFVALYDY EARTTDDLSF KKGERFQIIN
     NTEGDWWEAR SIATGKTGYI PSNYVAPADS IQAEEWYFGK MGRKDAERLL LNPGNQRGIF
     LVRESETTKG AYSLSIRDWD EVRGDNVKHY KIRKLDNGGY YITTRAQFES LQKLVKHYRE
     HADGLCHKLT TVCPTVKPQT QGLAKDAWEI PRESLRLEVK LGQGCFGEVW MGTWNGTTKV
     AIKTLKPGTM MPEAFLQEAQ IMKKLRHDKL VPLYAVVSEE PIYIVTEFMT KGSLLDFLKE
     GEGKFLKLPQ LVDMAAQIAD GMAYIERMNY IHRDLRAANI LVGDNLVCKI ADFGLARLIE
     DNEYTARQGA KFPIKWTAPE AALYGRFTIK SDVWSFGILL TELVTKGRVP YPGMVNREVL
     EQVERGYRMP CPQGCPESLH ELMKLCWKKD PDERPTFEYI QSFLEDYFTA TEPQYQPGDN
     L
//