YES_RAT
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 03-AUG-2022, entry version 80.
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 EGRF, 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). {ECO:0000250,
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 jPOST; F1LM93; -.
DR PaxDb; F1LM93; -.
DR PRIDE; F1LM93; -.
DR RGD; 3977; Yes1.
DR eggNOG; KOG0197; Eukaryota.
DR HOGENOM; CLU_000288_7_2_1; -.
DR InParanoid; F1LM93; -.
DR OMA; HEMMMLC; -.
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 tissues.
DR ExpressionAtlas; F1LM93; baseline and differential.
DR GO; GO:0005884; C:actin filament; ISO:RGD.
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:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA: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: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:0046777; P:protein autophosphorylation; IDA: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; 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: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
