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Protein

Tyrosine-protein kinase Yes

Gene

YES1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis.5 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei305 – 3051ATPPROSITE-ProRule annotation
Active sitei396 – 3961Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi283 – 2919ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. enzyme binding Source: UniProtKB
  3. ion channel binding Source: BHF-UCL
  4. non-membrane spanning protein tyrosine kinase activity Source: BHF-UCL
  5. protein tyrosine kinase activity Source: Reactome
  6. receptor binding Source: GO_Central

GO - Biological processi

  1. axon guidance Source: Reactome
  2. blood coagulation Source: Reactome
  3. cell differentiation Source: GO_Central
  4. cellular protein modification process Source: ProtInc
  5. cellular response to peptide hormone stimulus Source: GO_Central
  6. cellular response to platelet-derived growth factor stimulus Source: Ensembl
  7. ephrin receptor signaling pathway Source: Reactome
  8. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  9. glucose transport Source: Ensembl
  10. innate immune response Source: GO_Central
  11. leukocyte migration Source: Reactome
  12. peptidyl-tyrosine autophosphorylation Source: GO_Central
  13. regulation of cell proliferation Source: GO_Central
  14. regulation of vascular permeability Source: BHF-UCL
  15. T cell costimulation Source: Reactome
  16. transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_111040. Signaling by SCF-KIT.
REACT_111225. Regulation of KIT signaling.
REACT_115755. Signaling by ERBB2.
REACT_12519. PECAM1 interactions.
REACT_160274. FCGR activation.
REACT_19183. CD28 co-stimulation.
REACT_19405. CTLA4 inhibitory signaling.
REACT_23787. Regulation of signaling by CBL.
REACT_263952. EPHB-mediated forward signaling.
REACT_264068. EPH-Ephrin signaling.
REACT_264198. EPH-ephrin mediated repulsion of cells.
REACT_264548. EPHA-mediated growth cone collapse.
SignaLinkiP07947.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Yes (EC:2.7.10.2)
Alternative name(s):
Proto-oncogene c-Yes
p61-Yes
Gene namesi
Name:YES1
Synonyms:YES
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:12841. YES1.

Subcellular locationi

Cell membrane. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytosol
Note: Newly synthesized protein initially accumulates in the Golgi region and traffics to the plasma membrane through the exocytic pathway.

GO - Cellular componenti

  1. actin filament Source: Ensembl
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProtKB
  5. extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
  6. focal adhesion Source: UniProtKB
  7. Golgi apparatus Source: UniProtKB
  8. microtubule organizing center Source: UniProtKB-SubCell
  9. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi426 – 4261Y → F: About 50% loss of CSK-mediated inhibition. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA37432.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 543542Tyrosine-protein kinase YesPRO_0000088181Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Lipidationi3 – 31S-palmitoyl cysteine; in membrane formBy similarity
Modified residuei11 – 111Phosphoserine
Modified residuei21 – 211Phosphothreonine1 Publication
Modified residuei26 – 261Phosphoserine
Modified residuei32 – 321Phosphotyrosine
Modified residuei40 – 401Phosphoserine1 Publication
Modified residuei111 – 1111Phosphoserine
Modified residuei194 – 1941Phosphotyrosine
Modified residuei195 – 1951Phosphoserine
Modified residuei222 – 2221Phosphotyrosine
Modified residuei223 – 2231Phosphotyrosine
Modified residuei336 – 3361Phosphotyrosine1 Publication
Modified residuei345 – 3451Phosphotyrosine1 Publication
Modified residuei426 – 4261Phosphotyrosine; by autocatalysis1 Publication
Modified residuei446 – 4461PhosphotyrosineCurated
Modified residuei537 – 5371Phosphotyrosine; by CSK2 Publications

Post-translational modificationi

Phosphorylation by CSK on the C-terminal tail maintains the enzyme in an inactive state. Autophosphorylation at Tyr-426 maintains enzyme activity by blocking CSK-mediated inhibition.3 Publications
Palmitoylation at Cys-3 promotes membrane localization.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP07947.
PaxDbiP07947.
PRIDEiP07947.

PTM databases

PhosphoSiteiP07947.

Expressioni

Tissue specificityi

Expressed in the epithelial cells of renal proximal tubules and stomach as well as hematopoietic cells in the bone marrow and spleen in the fetal tissues. In adult, expressed in epithelial cells of the renal proximal tubules and present in keratinocytes in the basal epidermal layer of epidermis.2 Publications

Gene expression databases

BgeeiP07947.
CleanExiHS_YES1.
ExpressionAtlasiP07947. baseline and differential.
GenevestigatoriP07947.

Organism-specific databases

HPAiCAB004370.
HPA026480.

Interactioni

Subunit structurei

Interacts with YAP1 and CSF1R (By similarity). Interacts with CTNND1; this interaction allows YES1-mediated activation of FYN and FER and subsequent phosphorylation of CTNND1 (By similarity). Interacts with FASLG.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ALOX5P099172EBI-515331,EBI-79934
ARP102755EBI-515331,EBI-608057
EGFRP005333EBI-515331,EBI-297353
GAB1Q134807EBI-515331,EBI-517684
KITP107217EBI-515331,EBI-1379503
MED28Q9H2042EBI-515331,EBI-514199
METP085813EBI-515331,EBI-1039152

Protein-protein interaction databases

BioGridi113357. 78 interactions.
DIPiDIP-33849N.
IntActiP07947. 30 interactions.
MINTiMINT-93566.
STRINGi9606.ENSP00000324740.

Structurei

Secondary structure

1
543
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi93 – 1008Combined sources
Beta strandi117 – 1215Combined sources
Beta strandi126 – 1338Combined sources
Turni134 – 1363Combined sources
Beta strandi139 – 1435Combined sources
Helixi144 – 1463Combined sources
Beta strandi147 – 1493Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HDAX-ray1.90A91-152[»]
ProteinModelPortaliP07947.
SMRiP07947. Positions 92-543.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07947.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini91 – 15262SH3PROSITE-ProRule annotationAdd
BLAST
Domaini158 – 25598SH2PROSITE-ProRule annotationAdd
BLAST
Domaini277 – 530254Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP07947.
KOiK05705.
PhylomeDBiP07947.
TreeFamiTF351634.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07947-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGCIKSKENK SPAIKYRPEN TPEPVSTSVS HYGAEPTTVS PCPSSSAKGT
60 70 80 90 100
AVNFSSLSMT PFGGSSGVTP FGGASSSFSV VPSSYPAGLT GGVTIFVALY
110 120 130 140 150
DYEARTTEDL SFKKGERFQI INNTEGDWWE ARSIATGKNG YIPSNYVAPA
160 170 180 190 200
DSIQAEEWYF GKMGRKDAER LLLNPGNQRG IFLVRESETT KGAYSLSIRD
210 220 230 240 250
WDEIRGDNVK HYKIRKLDNG GYYITTRAQF DTLQKLVKHY TEHADGLCHK
260 270 280 290 300
LTTVCPTVKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT
310 320 330 340 350
KVAIKTLKPG TMMPEAFLQE AQIMKKLRHD KLVPLYAVVS EEPIYIVTEF
360 370 380 390 400
MSKGSLLDFL KEGDGKYLKL PQLVDMAAQI ADGMAYIERM NYIHRDLRAA
410 420 430 440 450
NILVGENLVC KIADFGLARL IEDNEYTARQ GAKFPIKWTA PEAALYGRFT
460 470 480 490 500
IKSDVWSFGI LQTELVTKGR VPYPGMVNRE VLEQVERGYR MPCPQGCPES
510 520 530 540
LHELMNLCWK KDPDERPTFE YIQSFLEDYF TATEPQYQPG ENL
Length:543
Mass (Da):60,801
Last modified:January 23, 2007 - v3
Checksum:iA2B376084686BBCD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti198 – 1981I → V.1 Publication
Corresponds to variant rs34580680 [ dbSNP | Ensembl ].
VAR_041879
Natural varianti282 – 2821K → R.1 Publication
Corresponds to variant rs35126906 [ dbSNP | Ensembl ].
VAR_041880

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15990 mRNA. Translation: AAA35735.1.
AP001178 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01709.1.
CH471113 Genomic DNA. Translation: EAX01710.1.
BC048960 mRNA. Translation: AAH48960.1.
CCDSiCCDS11824.1.
PIRiA26714. TVHUYS.
RefSeqiNP_005424.1. NM_005433.3.
UniGeneiHs.194148.

Genome annotation databases

EnsembliENST00000314574; ENSP00000324740; ENSG00000176105.
ENST00000584307; ENSP00000462468; ENSG00000176105.
GeneIDi7525.
KEGGihsa:7525.
UCSCiuc002kky.3. human.

Polymorphism databases

DMDMi125870.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15990 mRNA. Translation: AAA35735.1.
AP001178 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01709.1.
CH471113 Genomic DNA. Translation: EAX01710.1.
BC048960 mRNA. Translation: AAH48960.1.
CCDSiCCDS11824.1.
PIRiA26714. TVHUYS.
RefSeqiNP_005424.1. NM_005433.3.
UniGeneiHs.194148.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HDAX-ray1.90A91-152[»]
ProteinModelPortaliP07947.
SMRiP07947. Positions 92-543.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113357. 78 interactions.
DIPiDIP-33849N.
IntActiP07947. 30 interactions.
MINTiMINT-93566.
STRINGi9606.ENSP00000324740.

Chemistry

BindingDBiP07947.
ChEMBLiCHEMBL2073.
DrugBankiDB01254. Dasatinib.
GuidetoPHARMACOLOGYi2284.

PTM databases

PhosphoSiteiP07947.

Polymorphism databases

DMDMi125870.

Proteomic databases

MaxQBiP07947.
PaxDbiP07947.
PRIDEiP07947.

Protocols and materials databases

DNASUi7525.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000314574; ENSP00000324740; ENSG00000176105.
ENST00000584307; ENSP00000462468; ENSG00000176105.
GeneIDi7525.
KEGGihsa:7525.
UCSCiuc002kky.3. human.

Organism-specific databases

CTDi7525.
GeneCardsiGC18M000721.
HGNCiHGNC:12841. YES1.
HPAiCAB004370.
HPA026480.
MIMi164880. gene.
neXtProtiNX_P07947.
PharmGKBiPA37432.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP07947.
KOiK05705.
PhylomeDBiP07947.
TreeFamiTF351634.

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_111040. Signaling by SCF-KIT.
REACT_111225. Regulation of KIT signaling.
REACT_115755. Signaling by ERBB2.
REACT_12519. PECAM1 interactions.
REACT_160274. FCGR activation.
REACT_19183. CD28 co-stimulation.
REACT_19405. CTLA4 inhibitory signaling.
REACT_23787. Regulation of signaling by CBL.
REACT_263952. EPHB-mediated forward signaling.
REACT_264068. EPH-Ephrin signaling.
REACT_264198. EPH-ephrin mediated repulsion of cells.
REACT_264548. EPHA-mediated growth cone collapse.
SignaLinkiP07947.

Miscellaneous databases

ChiTaRSiYES1. human.
EvolutionaryTraceiP07947.
GeneWikiiYES1.
GenomeRNAii7525.
NextBioi29441.
PROiP07947.
SOURCEiSearch...

Gene expression databases

BgeeiP07947.
CleanExiHS_YES1.
ExpressionAtlasiP07947. baseline and differential.
GenevestigatoriP07947.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of cDNA clones for the human c-yes gene."
    Sukegawa J., Semba K., Yamanashi Y., Nishizawa M., Miyajima N., Yamamoto T., Toyoshima K.
    Mol. Cell. Biol. 7:41-47(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. Cited for: TISSUE SPECIFICITY.
  6. "Differential expression of p62c-yes in normal, hyperplastic and neoplastic human epidermis."
    Krueger J., Zhao Y.H., Murphy D., Sudol M.
    Oncogene 6:933-940(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Palmitoylation of multiple Src-family kinases at a homologous N-terminal motif."
    Koegl M., Zlatkine P., Ley S.C., Courtneidge S.A., Magee A.I.
    Biochem. J. 303:749-753(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION.
  8. "Expression, purification, and initial characterization of human Yes protein tyrosine kinase from a bacterial expression system."
    Sun G., Budde R.J.
    Arch. Biochem. Biophys. 345:135-142(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CSK.
  9. "Autophosphorylation of Src and Yes blocks their inactivation by Csk phosphorylation."
    Sun G., Sharma A.K., Budde R.J.
    Oncogene 17:1587-1595(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-426, MUTAGENESIS OF TYR-426.
  10. "CD46 is phosphorylated at tyrosine 354 upon infection of epithelial cells by Neisseria gonorrhoeae."
    Lee S.W., Bonnah R.A., Higashi D.L., Atkinson J.P., Milgram S.L., So M.
    J. Cell Biol. 156:951-957(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, FUNCTION.
  11. Cited for: REVIEW ON FUNCTION.
  12. "Phosphorylation of cyclin dependent kinase 4 on tyrosine 17 is mediated by Src family kinases."
    Martin N.G., McAndrew P.C., Eve P.D., Garrett M.D.
    FEBS J. 275:3099-3109(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CDK4.
  13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21 AND SER-40, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
    Voss M., Lettau M., Janssen O.
    BMC Immunol. 10:53-53(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FASLG.
  16. "Phosphorylation of collapsin response mediator protein 2 on Tyr-479 regulates CXCL12-induced T lymphocyte migration."
    Varrin-Doyer M., Vincent P., Cavagna S., Auvergnon N., Noraz N., Rogemond V., Honnorat J., Moradi-Ameli M., Giraudon P.
    J. Biol. Chem. 284:13265-13276(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF DPYSL2.
  17. "Differential trafficking of Src, Lyn, Yes and Fyn is specified by the state of palmitoylation in the SH4 domain."
    Sato I., Obata Y., Kasahara K., Nakayama Y., Fukumoto Y., Yamasaki T., Yokoyama K.K., Saito T., Yamaguchi N.
    J. Cell Sci. 122:965-975(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-336; TYR-345 AND TYR-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Clues for c-Yes involvement in the cell cycle and cytokinesis."
    Jung J., Lee M.K., Jin Y., Fu S.B., Rosales J.L., Lee K.Y.
    Cell Cycle 10:1502-1503(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  20. Cited for: FUNCTION.
  21. "Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: loop flexibility and amyloid aggregation."
    Martin-Garcia J.M., Luque I., Mateo P.L., Ruiz-Sanz J., Camara-Artigas A.
    FEBS Lett. 581:1701-1706(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 91-152.
  22. "Patterns of somatic mutation in human cancer genomes."
    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.
    Nature 446:153-158(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-198 AND ARG-282.

Entry informationi

Entry nameiYES_HUMAN
AccessioniPrimary (citable) accession number: P07947
Secondary accession number(s): A6NLB3, D3DUH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 182 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.