ID   YES_XIPHE               Reviewed;         544 AA.
AC   P27447;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-NOV-2023, entry version 124.
DE   RecName: Full=Tyrosine-protein kinase Yes;
DE            EC=2.7.10.2;
DE   AltName: Full=p61-Yes;
GN   Name=yes;
OS   Xiphophorus hellerii (Green swordtail).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Rio Lancetilla;
RX   PubMed=1707152;
RA   Hannig G., Ottilie S., Schartl M.;
RT   "Conservation of structure and expression of the c-yes and fyn genes in
RT   lower vertebrates.";
RL   Oncogene 6:361-369(1991).
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   -!- 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; X54970; CAA38714.1; -; mRNA.
DR   PIR; I51593; I51593.
DR   AlphaFoldDB; P27447; -.
DR   SMR; P27447; -.
DR   BRENDA; 2.7.10.2; 6732.
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; 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   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Lipoprotein; Myristate; Nucleotide-binding;
KW   Phosphoprotein; SH2 domain; SH3 domain; Transferase;
KW   Tyrosine-protein kinase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..544
FT                   /note="Tyrosine-protein kinase Yes"
FT                   /id="PRO_0000088185"
FT   DOMAIN          92..153
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          159..256
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          278..531
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        397
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         284..292
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         306
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         427
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   544 AA;  61289 MW;  7D41818B3E7086EF CRC64;
     MGCVRSKEAK GPALKYQPDN SNVVPVSAHL GHYGPEPTIM GQSPAMKTQN NSHPTALSPF
     GGVSSPMTPF GGASTSFTSV TVNNPFPAVI TGGVTFFVAL YDYEARTSDD LSFRKGDRFQ
     IINNTEGDWW EARSINTGEN GYIPSNYVAP ADSIQSEEWY FGKLSRKDTE RLLLLPGNER
     GTFLIRESET TKGAYSLSLR DWDETKGDNC KHYKIRKLDN GGYYITTRTQ FMSLQMLVKH
     YTEHVDGLCY KLTTVCPQVK PQTQGIAKDA WEIPRESLRL DVRLGQGCFG EVWMGTWNGT
     TKVAIKTLKP GTMSPEAFLE EAQIMKKLRH DKLVPLYAVV SEEPIYIVTE FMGKGSLLDF
     LKEGDGKHLK LPQLVDMASQ IADGMAFIER MNYIHRDLRA ANILVADNLV CKIADFGLAR
     LIEDNEYTAR QGAKFPIKWT APEAALYGRF TIKSDVWSFG ILLTELVTKG RVPYPGMVNR
     EVLEQVDRGY RMPCPQGCPE SLHEMMRQCW KKEPDERPTF EYIQSFLEDY FTATEPQYQP
     GDNL
//