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UniProtKB/Swiss-Prot entry P07947


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name YES_HUMAN
Primary accession number P07947
Secondary accession number A6NLB3
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 105)
Name and origin of the protein
Protein name Proto-oncogene tyrosine-protein kinase Yes
Synonyms EC 2.7.10.2
p61-Yes
c-Yes
Gene name
Name: YES1
Synonyms: YES
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2436037 [NCBI, ExPASy, EBI, Israel, Japan]
Sukegawa J., Semba K., Yamanashi Y., Nishizawa M., Miyajima N., Yamamoto T., Toyoshima K.;
"Characterization of cDNA clones for the human c-yes gene.";
Mol. Cell. Biol. 7:41-47(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03983; PubMed=16177791 [NCBI, ExPASy, EBI, Israel, Japan]
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
SUBCELLULAR LOCATION, PHOSPHORYLATION, AND FUNCTION.
DOI=10.1083/jcb.200109005; PubMed=11901164 [NCBI, ExPASy, EBI, Israel, Japan]
Lee S.W., Bonnah R.A., Higashi D.L., Atkinson J.P., Milgram S.L., So M.;
"CD46 is phosphorylated at tyrosine 354 upon infection of epithelial cells by Neisseria gonorrhoeae.";
J. Cell Biol. 156:951-957(2002).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-426, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1074/mcp.M500089-MCP200; PubMed=15951569 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.;
"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.";
Mol. Cell. Proteomics 4:1240-1250(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-537, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-426, AND MASS SPECTROMETRY.
TISSUE=T-cell;
DOI=10.1038/nmeth776; PubMed=16094384 [NCBI, ExPASy, EBI, Israel, Japan]
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry.";
Nat. Methods 2:591-598(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-426, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-32; TYR-222; TYR-223; TYR-426; TYR-446 AND TYR-537, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-426, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.;
"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.";
Mol. Cell. Proteomics 6:537-547(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-426, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[13]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 91-152.
DOI=10.1016/j.febslet.2007.03.059; PubMed=17418139 [NCBI, ExPASy, EBI, Israel, Japan]
Martin-Garcia J.M., Luque I., Mateo P.L., Ruiz-Sanz J., Camara-Artigas A.;
"Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: loop flexibility and amyloid aggregation.";
FEBS Lett. 581:1701-1706(2007).
[14]
VARIANTS [LARGE SCALE ANALYSIS] VAL-198 AND ARG-282.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M15990; AAA35735.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP001178; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
CH471113; EAX01709.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC048960; AAH48960.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A26714; TVHUYS.
RefSeq NP_005424.1; -.
UniGene Hs.194148
3D structure databases
PDB
2HDA; X-ray; 1.90 A; A=91-152.[ExPASy / RCSB / EBI]
PDBsum 2HDA; -.
SMR P07947; 93-542, 94-543.
ModBase P07947.
Protein-protein interaction databases
IntAct P07947; -.
PTM databases
PhosphoSite P07947; -.
Organism-specific databases
HGNC HGNC:12841; YES1.
GenAtlas YES1.
HPA CAB004370; -.
MIM 164880; gene. [NCBI / EBI]
PharmGKB PA37432; -.
GeneCards P07947.
Gene expression databases
ArrayExpress P07947; -.
CleanEx HS_YES1; -.
GermOnline ENSG00000176105; Homo sapiens.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004713; Molecular function: protein tyrosine kinase activity (traceable author statement from ProtInc).
GO:0006464; Biological process: protein modification process (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR000980; SH2.
IPR001452; SH3.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
Graphical view of domain structure.
Gene3D G3DSA:3.30.505.10; SH2; 1.
Pfam PF07714; Pkinase_Tyr; 1.
PF00017; SH2; 1.
PF00018; SH3_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00401; SH2DOMAIN.
PR00452; SH3DOMAIN.
PR00109; TYRKINASE.
ProDom PD000001; Prot_kinase; 1.
PD000093; SH2; 1.
PD000066; SH3; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00252; SH2; 1.
SM00326; SH3; 1.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PS50001; SH2; 1.
PS50002; SH3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P07947.
Genome annotation databases
Ensembl ENSG00000176105; Homo sapiens. [Contig view]
GeneID 7525; -.
KEGG hsa:7525; -.
Phylogenomic databases
HOGENOM P07947; -.
HOVERGEN P07947; -.
Other
DrugBank DB01254; Dasatinib.
LinkHub P07947; -.
SOURCE YES1; Homo sapiens.
ProtoNet P07947.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Cytoplasm; Kinase; Lipoprotein; Myristate; Nucleotide-binding; Phosphoprotein; Polymorphism; Proto-oncogene; SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   543  542     Proto-oncogene tyrosine-protein kinase Yes. PRO_0000088181
DOMAIN   91   152  62     SH3. 
DOMAIN   158   255  98     SH2. 
DOMAIN   277   530  254     Protein kinase. 
NP_BIND   283   291  9     ATP (By similarity). 
ACT_SITE   396   396        Proton acceptor (By similarity). 
BINDING   305   305        ATP (By similarity). 
MOD_RES   32    32        Phosphotyrosine. 
MOD_RES   194   194        Phosphotyrosine (By similarity). 
MOD_RES   222   222        Phosphotyrosine. 
MOD_RES   223   223        Phosphotyrosine. 
MOD_RES   426   426        Phosphotyrosine; by autocatalysis. 
MOD_RES   446   446        Phosphotyrosine. 
MOD_RES   537   537        Phosphotyrosine. 
LIPID   2     2        N-myristoyl glycine (By similarity). 
VARIANT   198   198  1     I -> V. VAR_041879 
VARIANT   282   282  1     K -> R. VAR_041880 [3D]
STRAND   93   100  8      
STRAND   117   121  5      
STRAND   126   133  8      
TURN   134   136  3      
STRAND   139   143  5      
HELIX   144   146  3      
STRAND   147   149  3      
Sequence information
Length: 543 AA [This is the length of the unprocessed precursor] Molecular weight: 60801 Da [This is the MW of the unprocessed precursor] CRC64: A2B376084686BBCD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGCIKSKENK SPAIKYRPEN TPEPVSTSVS HYGAEPTTVS PCPSSSAKGT AVNFSSLSMT 

        70         80         90        100        110        120 
PFGGSSGVTP FGGASSSFSV VPSSYPAGLT GGVTIFVALY DYEARTTEDL SFKKGERFQI 

       130        140        150        160        170        180 
INNTEGDWWE ARSIATGKNG YIPSNYVAPA DSIQAEEWYF GKMGRKDAER LLLNPGNQRG 

       190        200        210        220        230        240 
IFLVRESETT KGAYSLSIRD WDEIRGDNVK HYKIRKLDNG GYYITTRAQF DTLQKLVKHY 

       250        260        270        280        290        300 
TEHADGLCHK LTTVCPTVKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT 

       310        320        330        340        350        360 
KVAIKTLKPG TMMPEAFLQE AQIMKKLRHD KLVPLYAVVS EEPIYIVTEF MSKGSLLDFL 

       370        380        390        400        410        420 
KEGDGKYLKL PQLVDMAAQI ADGMAYIERM NYIHRDLRAA NILVGENLVC KIADFGLARL 

       430        440        450        460        470        480 
IEDNEYTARQ GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LQTELVTKGR VPYPGMVNRE 

       490        500        510        520        530        540 
VLEQVERGYR MPCPQGCPES LHELMNLCWK KDPDERPTFE YIQSFLEDYF TATEPQYQPG 


ENL 

P07947 in FASTA format

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