ID   YES_XENLA               Reviewed;         537 AA.
AC   P10936;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Tyrosine-protein kinase Yes;
DE            EC=2.7.10.2;
DE   AltName: Full=p61-Yes;
GN   Name=yes1; Synonyms=yes;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2472592;
RA   Steele R.E., Irwin M.Y., Knudsen C.L., Collett J.W., Fero J.B.;
RT   "The yes proto-oncogene is present in amphibians and contributes to the
RT   maternal RNA pool in the oocyte.";
RL   Oncogene Res. 4:223-233(1989).
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: Autophosphorylated at Tyr-420 inducing activation. {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; X14377; CAA32551.1; -; mRNA.
DR   PIR; A45501; A45501.
DR   AlphaFoldDB; P10936; -.
DR   SMR; P10936; -.
DR   AGR; Xenbase:XB-GENE-866413; -.
DR   Xenbase; XB-GENE-866413; yes1.L.
DR   BRENDA; 2.7.10.2; 6725.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; 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; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   2: Evidence at transcript 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..537
FT                   /note="Tyrosine-protein kinase Yes"
FT                   /id="PRO_0000088184"
FT   DOMAIN          85..146
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          152..249
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          271..524
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        390
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         277..285
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         299
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         420
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         531
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"
SQ   SEQUENCE   537 AA;  60358 MW;  FF26F615940AC31B CRC64;
     MGCIKSKEDK GPSIKYRTEP KPDPGSQYGA DPTQATQSPG IKGPAPNFNS HSMTPFGGSS
     GITPFGGASS IFSPTPVPYP GGLTGGVTVF VALYDYEART TEDLSFRKGE RFQIINNTEG
     DWWEARSIAT GKTGYIPSNY VAPADSIQAE EWYFGKMGRK DAERLLLNPG NQRGTFLVRE
     SETTKGAYSL SIRDWDEVRG DNVKHYKIRK LDNGGYYITT RAQFESLQKL VKHYSEHADG
     LCYRLTTVCP SVKPQTQGLA KDAWEIPRES LRLDVKLGQG CFGEVWIGTW NGTTKVAIKT
     LKPGTMMPEA FLQEAQIMKK LRHDKLVPLY AVVSEEPIYI VTEYMIKGSL LDFLKEGNGK
     YLKLPQLVDM AAQIADGMAY IERMNYIHRD LRAANILVGD NLVCKIADFG LARLIEDNEY
     TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV AKGRVPYPGM VNREVLEQVE
     RGYRMPCPQR CPESLHELMK LCWKKDPDER PTFEYIQSFL EDYFTATEPQ YQPGDNL
//