ID   YES_RAT                 Reviewed;         541 AA.
AC   F1LM93;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=Tyrosine-protein kinase Yes;
DE            EC=2.7.10.2;
DE   AltName: Full=p61-Yes;
GN   Name=Yes1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=1709169; DOI=10.1083/jcb.113.4.867;
RA   Tsukita S., Oishi K., Akiyama T., Yamanashi Y., Yamamoto T., Tsukita S.;
RT   "Specific proto-oncogenic tyrosine kinases of src family are enriched in
RT   cell-to-cell adherens junctions where the level of tyrosine phosphorylation
RT   is elevated.";
RL   J. Cell Biol. 113:867-879(1991).
RN   [3]
RP   INTERACTION WITH CTNND1.
RX   PubMed=12640114; DOI=10.1128/mcb.23.7.2287-2297.2003;
RA   Piedra J., Miravet S., Castano J., Palmer H.G., Heisterkamp N.,
RA   Garcia de Herreros A., Dunach M.;
RT   "p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin
RT   Tyr-142 phosphorylation and beta-catenin-alpha-catenin Interaction.";
RL   Mol. Cell. Biol. 23:2287-2297(2003).
RN   [4]
RP   FUNCTION.
RX   PubMed=21256972; DOI=10.1016/j.biocel.2011.01.008;
RA   Xiao X., Mruk D.D., Lee W.M., Cheng C.Y.;
RT   "c-Yes regulates cell adhesion at the blood-testis barrier and the apical
RT   ectoplasmic specialization in the seminiferous epithelium of rat testes.";
RL   Int. J. Biochem. Cell Biol. 43:651-665(2011).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-535, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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, and differentiation. Stimulation by receptor
CC       tyrosine kinases (RTKs) including EGFR, PDGFR, CSF1R and FGFR leads to
CC       recruitment of YES1 to the phosphorylated receptor, and activation and
CC       phosphorylation of downstream substrates. Upon EGFR activation,
CC       promotes the phosphorylation of PARD3 to favor epithelial tight
CC       junction assembly. Participates in the phosphorylation of specific
CC       junctional components such as CTNND1 by stimulating the FYN and FER
CC       tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by
CC       CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and
CC       induces T-cell migration. Participates in CD95L/FASLG signaling pathway
CC       and mediates AKT-mediated cell migration. Plays a role in cell cycle
CC       progression by phosphorylating the cyclin dependent kinase 4/CDK4 thus
CC       regulating the G1 phase. Also involved in G2/M progression and
CC       cytokinesis (By similarity). Catalyzes phosphorylation of organic
CC       cation transporter OCT2 which induces its transport activity (By
CC       similarity). {ECO:0000250, ECO:0000250|UniProtKB:P07947,
CC       ECO:0000269|PubMed:21256972}.
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   -!- SUBUNIT: Interacts with YAP1 and CSF1R (By similarity). Interacts with
CC       FASLG (By similarity). Interacts with CTNND1; this interaction allows
CC       YES1-mediated activation of FYN and FER and subsequent phosphorylation
CC       of CTNND1. Interacts with IL6ST/gp130 (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P07947, ECO:0000269|PubMed:12640114}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1709169}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250}. Cytoplasm, cytosol {ECO:0000269|PubMed:1709169}.
CC       Note=Newly synthesized protein initially accumulates in the Golgi
CC       region and traffics to the plasma membrane through the exocytic
CC       pathway. {ECO:0000250}.
CC   -!- PTM: Phosphorylation by CSK on the C-terminal tail maintains the enzyme
CC       in an inactive state. Autophosphorylation at Tyr-424 maintains enzyme
CC       activity by blocking CSK-mediated inhibition (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Palmitoylation at Cys-3 promotes membrane localization.
CC       {ECO:0000250}.
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DR   EMBL; AABR03068393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03068636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F1LM93; -.
DR   SMR; F1LM93; -.
DR   IntAct; F1LM93; 24.
DR   STRING; 10116.ENSRNOP00000053093; -.
DR   iPTMnet; F1LM93; -.
DR   PhosphoSitePlus; F1LM93; -.
DR   SwissPalm; F1LM93; -.
DR   jPOST; F1LM93; -.
DR   PaxDb; 10116-ENSRNOP00000053093; -.
DR   AGR; RGD:3977; -.
DR   RGD; 3977; Yes1.
DR   eggNOG; KOG0197; Eukaryota.
DR   HOGENOM; CLU_000288_7_2_1; -.
DR   InParanoid; F1LM93; -.
DR   TreeFam; TF351634; -.
DR   Reactome; R-RNO-1227986; Signaling by ERBB2.
DR   Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR   Reactome; R-RNO-1433559; Regulation of KIT signaling.
DR   Reactome; R-RNO-2029481; FCGR activation.
DR   Reactome; R-RNO-210990; PECAM1 interactions.
DR   Reactome; R-RNO-389356; CD28 co-stimulation.
DR   Reactome; R-RNO-389513; CTLA4 inhibitory signaling.
DR   Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-RNO-3928663; EPHA-mediated growth cone collapse.
DR   Reactome; R-RNO-3928665; EPH-ephrin mediated repulsion of cells.
DR   Reactome; R-RNO-912631; Regulation of signaling by CBL.
DR   PRO; PR:F1LM93; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000037227; Expressed in duodenum and 18 other cell types or tissues.
DR   ExpressionAtlas; F1LM93; baseline and differential.
DR   GO; GO:0005884; C:actin filament; ISO:RGD.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0099091; C:postsynaptic specialization, intracellular component; IDA:SynGO.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR   GO; GO:0005154; F:epidermal growth factor receptor binding; IPI:RGD.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; ISO:RGD.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IDA:RGD.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISO:RGD.
DR   GO; GO:0071300; P:cellular response to retinoic acid; ISO:RGD.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:RGD.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0010827; P:regulation of glucose transmembrane transport; ISO:RGD.
DR   GO; GO:0007169; P:transmembrane 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   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   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:0000255"
FT   CHAIN           2..541
FT                   /note="Tyrosine-protein kinase Yes"
FT                   /id="PRO_0000413800"
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..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..27
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         32
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q04736"
FT   MOD_RES         334
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P07947"
FT   MOD_RES         343
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P07947"
FT   MOD_RES         424
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P07947"
FT   MOD_RES         535
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine; in membrane form"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   541 AA;  60614 MW;  3864A9ED1D3A3F2F CRC64;
     MGCIKSKENK SPAIKYTPEN PTEPVNTSAG HYGVEHATAA TTSSTKGASA NFNSLSMTPF
     GGSSGVTPFG GASSSFSVVP SSYPTSLTGG VTIFVALYDY EARTTEDLSF KKGERFQIIN
     NTEGDWWEAR SIATGKNGYI PSNYVAPADS IQAEEWYFGK MGRKDAERLL LNPGNQRGIF
     LVRESETTKG AYSLSIRDWD EVRGDNVKHY KIRKLDNGGY YITTRAQFDT LQKLVKHYTE
     HADGLCHKLT TVCPTVKPQT QGLAKDAWEI PRESLRLEVK LGQGCFGEVW MGTWNGTTKV
     AIKTLKPGTM MPEAFLQEAQ IMKKLRHDKL VPLYAVVSEE PIYIVTEFMS KGILLDFLKE
     GDGKYLKLPQ LVDMAAQIAD GMAYIERMNY IHRDLRAANI LVGENLVCKI ADFGLARLIE
     DNEYTARQGA KFPIKWTAPE AALYGRFTIK SDVWSFGILQ TELVTKGRVP YPGMVNREVL
     EQVERGYRMP CPQGCPESLH ELMNLCWKKD PDERPTFEYI QSFLEDYFTA TEPQYQPGEN
     L
//