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YES_MOUSE
ID   YES_MOUSE               Reviewed;         541 AA.
AC   Q04736;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 217.
DE   RecName: Full=Tyrosine-protein kinase Yes;
DE            EC=2.7.10.2;
DE   AltName: Full=Proto-oncogene c-Yes;
DE   AltName: Full=p61-Yes;
GN   Name=Yes1; Synonyms=Yes;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=8437854;
RA   Klages S., Adam D., Eiseman E., Fargnoli J., Dymecki S.M., Desiderio S.V.,
RA   Bolen J.B.;
RT   "Molecular cloning and analysis of cDNA encoding the murine c-yes tyrosine
RT   protein kinase.";
RL   Oncogene 8:713-719(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 391-458.
RX   PubMed=8206383; DOI=10.1016/0378-1119(94)90106-6;
RA   Hebert B., Bergeron J., Tijssen P., Potworowski E.F.;
RT   "Protein tyrosine kinases transcribed in a murine thymic medullary
RT   epithelial cell line.";
RL   Gene 143:257-260(1994).
RN   [4]
RP   INTERACTION WITH CSF1R.
RX   PubMed=7681396; DOI=10.1002/j.1460-2075.1993.tb05735.x;
RA   Courtneidge S.A., Dhand R., Pilat D., Twamley G.M., Waterfield M.D.,
RA   Roussel M.F.;
RT   "Activation of Src family kinases by colony stimulating factor-1, and their
RT   association with its receptor.";
RL   EMBO J. 12:943-950(1993).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=7958873; DOI=10.1101/gad.8.17.1999;
RA   Stein P.L., Vogel H., Soriano P.;
RT   "Combined deficiencies of Src, Fyn, and Yes tyrosine kinases in mutant
RT   mice.";
RL   Genes Dev. 8:1999-2007(1994).
RN   [6]
RP   PHOSPHORYLATION AT TYR-32.
RX   PubMed=9058199; DOI=10.1093/oxfordjournals.jbchem.a021551;
RA   Ariki M., Tanabe O., Usui H., Hayashi H., Inoue R., Nishito Y.,
RA   Kagamiyama H., Takeda M.;
RT   "Identification of autophosphorylation sites in c-Yes purified from rat
RT   liver plasma membranes.";
RL   J. Biochem. 121:104-111(1997).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-535, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   STRUCTURE BY NMR OF 62-167.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the SH3_1 domain of Yamaguchi sarcoma viral (v-Yes)
RT   oncogene homolog 1.";
RL   Submitted (APR-2008) to the PDB data bank.
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   -!- 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. Interacts with FASLG. Interacts with
CC       CTNND1; this interaction allows YES1-mediated activation of FYN and FER
CC       and subsequent phosphorylation of CTNND1 (By similarity). Interacts
CC       with CSF1R. Interacts with IL6ST/gp130 (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P07947, ECO:0000269|PubMed:7681396}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC       Cytoplasm, cytosol {ECO:0000250}. Note=Newly synthesized protein
CC       initially accumulates in the Golgi region and traffics to the plasma
CC       membrane through the exocytic 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}.
CC   -!- DISRUPTION PHENOTYPE: Mice are viable, fertile, and display no apparent
CC       phenotypes. This lack of phenotype may be attributable to compensatory
CC       roles of the other SRC-family members. {ECO:0000269|PubMed:7958873}.
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; X67677; CAA47909.1; -; mRNA.
DR   EMBL; BC010594; AAH10594.1; -; mRNA.
DR   EMBL; L25762; AAA40020.1; -; mRNA.
DR   CCDS; CCDS39061.1; -.
DR   PIR; I48318; S31645.
DR   RefSeq; NP_001192061.1; NM_001205132.1.
DR   RefSeq; NP_001192062.1; NM_001205133.1.
DR   RefSeq; NP_033561.1; NM_009535.3.
DR   PDB; 2YT6; NMR; -; A=71-167.
DR   PDB; 5MTJ; X-ray; 1.95 A; A=147-260.
DR   PDBsum; 2YT6; -.
DR   PDBsum; 5MTJ; -.
DR   AlphaFoldDB; Q04736; -.
DR   SMR; Q04736; -.
DR   BioGRID; 204615; 7.
DR   IntAct; Q04736; 4.
DR   MINT; Q04736; -.
DR   STRING; 10090.ENSMUSP00000072154; -.
DR   iPTMnet; Q04736; -.
DR   PhosphoSitePlus; Q04736; -.
DR   SwissPalm; Q04736; -.
DR   jPOST; Q04736; -.
DR   PaxDb; Q04736; -.
DR   PeptideAtlas; Q04736; -.
DR   PRIDE; Q04736; -.
DR   ProteomicsDB; 299631; -.
DR   Antibodypedia; 3819; 503 antibodies from 37 providers.
DR   DNASU; 22612; -.
DR   Ensembl; ENSMUST00000072311; ENSMUSP00000072154; ENSMUSG00000014932.
DR   Ensembl; ENSMUST00000168707; ENSMUSP00000132161; ENSMUSG00000014932.
DR   Ensembl; ENSMUST00000202543; ENSMUSP00000144001; ENSMUSG00000014932.
DR   GeneID; 22612; -.
DR   KEGG; mmu:22612; -.
DR   UCSC; uc008wzs.2; mouse.
DR   CTD; 7525; -.
DR   MGI; MGI:99147; Yes1.
DR   VEuPathDB; HostDB:ENSMUSG00000014932; -.
DR   eggNOG; KOG0197; Eukaryota.
DR   GeneTree; ENSGT00940000154920; -.
DR   InParanoid; Q04736; -.
DR   OMA; HSDGLCY; -.
DR   OrthoDB; 539311at2759; -.
DR   PhylomeDB; Q04736; -.
DR   TreeFam; TF351634; -.
DR   BRENDA; 2.7.10.2; 3474.
DR   Reactome; R-MMU-1227986; Signaling by ERBB2.
DR   Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR   Reactome; R-MMU-1433559; Regulation of KIT signaling.
DR   Reactome; R-MMU-2029481; FCGR activation.
DR   Reactome; R-MMU-210990; PECAM1 interactions.
DR   Reactome; R-MMU-389356; CD28 co-stimulation.
DR   Reactome; R-MMU-389513; CTLA4 inhibitory signaling.
DR   Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-MMU-3928663; EPHA-mediated growth cone collapse.
DR   Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
DR   Reactome; R-MMU-912631; Regulation of signaling by CBL.
DR   BioGRID-ORCS; 22612; 3 hits in 75 CRISPR screens.
DR   ChiTaRS; Yes1; mouse.
DR   EvolutionaryTrace; Q04736; -.
DR   PRO; PR:Q04736; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q04736; protein.
DR   Bgee; ENSMUSG00000014932; Expressed in lumbar dorsal root ganglion and 244 other tissues.
DR   ExpressionAtlas; Q04736; baseline and differential.
DR   Genevisible; Q04736; MM.
DR   GO; GO:0005884; C:actin filament; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0099091; C:postsynaptic specialization, intracellular component; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0005154; F:epidermal growth factor receptor binding; ISO:MGI.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IDA:MGI.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IDA:MGI.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IGI:MGI.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR   GO; GO:0010827; P:regulation of glucose transmembrane transport; IDA:MGI.
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   3D-structure; ATP-binding; Cell membrane; Cytoplasm; Cytoskeleton; Kinase;
KW   Lipoprotein; Membrane; Myristate; Nucleotide-binding; Palmitate;
KW   Phosphoprotein; Proto-oncogene; Reference proteome; SH2 domain; SH3 domain;
KW   Transferase; Tyrosine-protein kinase.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..541
FT                   /note="Tyrosine-protein kinase Yes"
FT                   /id="PRO_0000088182"
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   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:0000269|PubMed:9058199"
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:18034455"
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"
FT   STRAND          93..98
FT                   /evidence="ECO:0007829|PDB:2YT6"
FT   STRAND          115..120
FT                   /evidence="ECO:0007829|PDB:2YT6"
FT   STRAND          127..134
FT                   /evidence="ECO:0007829|PDB:2YT6"
FT   STRAND          137..140
FT                   /evidence="ECO:0007829|PDB:2YT6"
FT   TURN            142..144
FT                   /evidence="ECO:0007829|PDB:2YT6"
FT   STRAND          145..150
FT                   /evidence="ECO:0007829|PDB:2YT6"
FT   TURN            152..154
FT                   /evidence="ECO:0007829|PDB:2YT6"
FT   STRAND          157..160
FT                   /evidence="ECO:0007829|PDB:5MTJ"
FT   HELIX           163..170
FT                   /evidence="ECO:0007829|PDB:5MTJ"
FT   STRAND          180..184
FT                   /evidence="ECO:0007829|PDB:5MTJ"
FT   STRAND          186..188
FT                   /evidence="ECO:0007829|PDB:5MTJ"
FT   STRAND          192..200
FT                   /evidence="ECO:0007829|PDB:5MTJ"
FT   TURN            201..203
FT                   /evidence="ECO:0007829|PDB:5MTJ"
FT   STRAND          204..214
FT                   /evidence="ECO:0007829|PDB:5MTJ"
FT   STRAND          216..218
FT                   /evidence="ECO:0007829|PDB:5MTJ"
FT   STRAND          220..223
FT                   /evidence="ECO:0007829|PDB:5MTJ"
FT   STRAND          226..230
FT                   /evidence="ECO:0007829|PDB:5MTJ"
FT   HELIX           231..240
FT                   /evidence="ECO:0007829|PDB:5MTJ"
FT   STRAND          245..247
FT                   /evidence="ECO:0007829|PDB:5MTJ"
SQ   SEQUENCE   541 AA;  60630 MW;  9A773C39D2119EA6 CRC64;
     MGCIKSKENK SPAIKYTPEN LTEPVSPSAS HYGVEHATVA PTSSTKGASV NFNSLSMTPF
     GGSSGVTPFG GASSSFSVVS SSYPTGLTGG VTIFVALYDY EARTTEDLSF KKGERFQIIN
     NTEGDWWEAR SIATGKSGYI PSNYVVPADS IQAEEWYFGK MGRKDAERLL LNPGNQRGIF
     LVRESETTKG AYSLSIRDWD EVRGDNVKHY KIRKLDNGGY YITTRAQFDT LQKLVKHYTE
     HADGLCHKLT TVCPTVKPQT QGLAKDAWEI PRESLRLEVK LGQGCFGEVW MGTWNGTTKV
     AIKTLKPGTM MPEAFLQEAQ IMKKLRHDKL VPLYAVVSEE PIYIVTEFMS KGSLLDFLKE
     GDGKYLKLPQ LVDMAAQIAD GMAYIERMNY IHRDLRAANI LVGENLICKI ADFGLARLIE
     DNEYTARQGA KFPIKWTAPE AALYGRFTIK SDVWSFGILQ TELVTKGRVP YPGMVNREVL
     EQVERGYRMP CPQGCPESLH ELMNLCWKKD PDERPTFEYI QSFLEDYFTA TEPQYQPGEN
     L
 
 
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