ID Q6PF70_XENLA Unreviewed; 537 AA.
AC Q6PF70;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN Name=yes1.L {ECO:0000313|RefSeq:NP_001079938.1,
GN ECO:0000313|Xenbase:XB-GENE-866413};
GN Synonyms=c-yes {ECO:0000313|RefSeq:NP_001079938.1}, yes
GN {ECO:0000313|EMBL:AAH57707.1, ECO:0000313|RefSeq:NP_001079938.1}, yes1
GN {ECO:0000313|RefSeq:NP_001079938.1,
GN ECO:0000313|Xenbase:XB-GENE-866413};
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 {ECO:0000313|EMBL:AAH57707.1};
RN [1] {ECO:0000313|RefSeq:NP_001079938.1}
RP NUCLEOTIDE SEQUENCE.
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).
RN [2] {ECO:0000313|RefSeq:NP_001079938.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [3] {ECO:0000313|EMBL:AAH57707.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000313|EMBL:AAH57707.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|RefSeq:NP_001079938.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001149,
CC ECO:0000256|RuleBase:RU362096};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000256|RuleBase:RU362096}.
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DR EMBL; BC057707; AAH57707.1; -; mRNA.
DR RefSeq; NP_001079938.1; NM_001086469.1.
DR STRING; 8355.Q6PF70; -.
DR PaxDb; 8355-Q6PF70; -.
DR DNASU; 379629; -.
DR GeneID; 379629; -.
DR KEGG; xla:379629; -.
DR AGR; Xenbase:XB-GENE-866413; -.
DR CTD; 379629; -.
DR Xenbase; XB-GENE-866413; yes1.L.
DR OMA; ESNEWHF; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 379629; Expressed in egg cell and 19 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 {ECO:0000256|PROSITE-ProRule:PRU10141,
KW ECO:0000256|RuleBase:RU362096};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022707};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362096};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|RuleBase:RU362096}.
FT DOMAIN 85..146
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 152..249
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 271..524
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
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 BINDING 299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 537 AA; 60304 MW; FA820445A10AC9DB 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 TVKPQTQGLA KDAWEIPRES LRLDVKLGQG CFGEVWIGTW NGTTKVAIKT
LKPGTMMPEA FLQEAQIMKK LRHDKLVPLY AVVSEEPIYI VTEYMIKGSL LDFLKEGDGK
YLKLPQLVDM AAQIADGMAY IERMNYIHRD LRAANILVGD NLVCKIADFG LARLIEDNEY
TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV TKGRVPYPGM VNREVLEQVE
RGYRMPCPQG CPESLHELMK LCWKKDPDER PTFEYIQSFL EDYFTATEPQ YQPGDNL
//