YES_CHICK
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 03-AUG-2022, entry version 177.
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=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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC Cytoplasm, cytosol {ECO:0000250}.
CC -!- PTM: Autophosphorylation at Tyr-424 maintains enzyme activity.
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; 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_205301.1.
DR AlphaFoldDB; P09324; -.
DR SMR; P09324; -.
DR STRING; 9031.ENSGALP00000023934; -.
DR PaxDb; P09324; -.
DR Ensembl; ENSGALT00000023980; ENSGALP00000023934; ENSGALG00000014860.
DR Ensembl; ENSGALT00000064616; ENSGALP00000050000; ENSGALG00000014860.
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; HEMMMLC; -.
DR OrthoDB; 539311at2759; -.
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-2029481; FCGR activation.
DR Reactome; R-GGA-210990; PECAM1 interactions.
DR Reactome; R-GGA-389356; CD28 co-stimulation.
DR Reactome; R-GGA-389513; CTLA4 inhibitory signaling.
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 tissues.
DR ExpressionAtlas; P09324; baseline and differential.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
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: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 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..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..43
FT /note="Polar residues"
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"
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
