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Protein

Tyrosine-protein kinase Yes

Gene

Yes1

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei303 – 3031ATPPROSITE-ProRule annotation
Active sitei394 – 3941Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi281 – 2899ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. cell differentiation Source: GO_Central
  2. cellular response to peptide hormone stimulus Source: GO_Central
  3. cellular response to platelet-derived growth factor stimulus Source: MGI
  4. cellular response to retinoic acid Source: MGI
  5. cellular response to transforming growth factor beta stimulus Source: MGI
  6. glucose transport Source: MGI
  7. innate immune response Source: GO_Central
  8. peptidyl-tyrosine autophosphorylation Source: GO_Central
  9. positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  10. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  11. regulation of cell proliferation Source: GO_Central
  12. 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. 3474.
ReactomeiREACT_280640. EPHA-mediated growth cone collapse.
REACT_292566. EPH-Ephrin signaling.
REACT_311393. CTLA4 inhibitory signaling.
REACT_313804. EPHB-mediated forward signaling.
REACT_314615. EPH-ephrin mediated repulsion of cells.
REACT_327841. Signaling by SCF-KIT.
REACT_333749. FCGR activation.
REACT_334921. CD28 co-stimulation.
REACT_354765. Regulation of KIT signaling.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:99147. Yes1.

Subcellular locationi

  1. Cell membrane By similarity
  2. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
  3. Cytoplasmcytosol By similarity

  4. Note: Newly synthesized protein initially accumulates in the Golgi region and traffics to the plasma membrane through the exocytic pathway.By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are viable, fertile, and display no apparent phenotypes. This lack of phenotype may be attributable to compensatory roles of the other SRC-family members.1 Publication

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 541540Tyrosine-protein kinase YesPRO_0000088182Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Lipidationi3 – 31S-palmitoyl cysteine; in membrane formBy similarity
Modified residuei32 – 321Phosphotyrosine1 Publication
Modified residuei334 – 3341PhosphotyrosineBy similarity
Modified residuei343 – 3431PhosphotyrosineBy similarity
Modified residuei424 – 4241Phosphotyrosine; by autocatalysisBy similarity
Modified residuei535 – 5351Phosphotyrosine; alternate1 Publication
Modified residuei535 – 5351Phosphotyrosine; by CSK; alternateBy similarity

Post-translational modificationi

Phosphorylation by CSK on the C-terminal tail maintains the enzyme in an inactive state. Autophosphorylation at Tyr-424 maintains enzyme activity by blocking CSK-mediated inhibition (By similarity).By similarity
Palmitoylation at Cys-3 promotes membrane localization.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiQ04736.
PaxDbiQ04736.
PRIDEiQ04736.

PTM databases

PhosphoSiteiQ04736.

Expressioni

Gene expression databases

BgeeiQ04736.
ExpressionAtlasiQ04736. baseline and differential.
GenevestigatoriQ04736.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi204615. 5 interactions.
IntActiQ04736. 3 interactions.

Structurei

Secondary structure

1
541
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi93 – 986Combined sources
Beta strandi115 – 1206Combined sources
Beta strandi127 – 1348Combined sources
Beta strandi137 – 1404Combined sources
Turni142 – 1443Combined sources
Beta strandi145 – 1506Combined sources
Turni152 – 1543Combined sources
Helixi155 – 1595Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YT6NMR-A71-167[»]
ProteinModelPortaliQ04736.
SMRiQ04736. Positions 83-541.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04736.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini89 – 15062SH3PROSITE-ProRule annotationAdd
BLAST
Domaini156 – 25398SH2PROSITE-ProRule annotationAdd
BLAST
Domaini275 – 528254Protein 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.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiQ04736.
KOiK05705.
OMAiIKYRTEN.
OrthoDBiEOG7GTT2V.
PhylomeDBiQ04736.
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.

Q04736-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGCIKSKENK SPAIKYTPEN LTEPVSPSAS HYGVEHATVA PTSSTKGASV
60 70 80 90 100
NFNSLSMTPF GGSSGVTPFG GASSSFSVVS SSYPTGLTGG VTIFVALYDY
110 120 130 140 150
EARTTEDLSF KKGERFQIIN NTEGDWWEAR SIATGKSGYI PSNYVVPADS
160 170 180 190 200
IQAEEWYFGK MGRKDAERLL LNPGNQRGIF LVRESETTKG AYSLSIRDWD
210 220 230 240 250
EVRGDNVKHY KIRKLDNGGY YITTRAQFDT LQKLVKHYTE HADGLCHKLT
260 270 280 290 300
TVCPTVKPQT QGLAKDAWEI PRESLRLEVK LGQGCFGEVW MGTWNGTTKV
310 320 330 340 350
AIKTLKPGTM MPEAFLQEAQ IMKKLRHDKL VPLYAVVSEE PIYIVTEFMS
360 370 380 390 400
KGSLLDFLKE GDGKYLKLPQ LVDMAAQIAD GMAYIERMNY IHRDLRAANI
410 420 430 440 450
LVGENLICKI ADFGLARLIE DNEYTARQGA KFPIKWTAPE AALYGRFTIK
460 470 480 490 500
SDVWSFGILQ TELVTKGRVP YPGMVNREVL EQVERGYRMP CPQGCPESLH
510 520 530 540
ELMNLCWKKD PDERPTFEYI QSFLEDYFTA TEPQYQPGEN L
Length:541
Mass (Da):60,630
Last modified:January 23, 2007 - v3
Checksum:i9A773C39D2119EA6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67677 mRNA. Translation: CAA47909.1.
BC010594 mRNA. Translation: AAH10594.1.
L25762 mRNA. Translation: AAA40020.1.
CCDSiCCDS39061.1.
PIRiI48318. S31645.
RefSeqiNP_001192061.1. NM_001205132.1.
NP_001192062.1. NM_001205133.1.
NP_033561.1. NM_009535.3.
UniGeneiMm.4558.

Genome annotation databases

EnsembliENSMUST00000072311; ENSMUSP00000072154; ENSMUSG00000014932.
ENSMUST00000168707; ENSMUSP00000132161; ENSMUSG00000014932.
GeneIDi22612.
KEGGimmu:22612.
UCSCiuc008wzs.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67677 mRNA. Translation: CAA47909.1.
BC010594 mRNA. Translation: AAH10594.1.
L25762 mRNA. Translation: AAA40020.1.
CCDSiCCDS39061.1.
PIRiI48318. S31645.
RefSeqiNP_001192061.1. NM_001205132.1.
NP_001192062.1. NM_001205133.1.
NP_033561.1. NM_009535.3.
UniGeneiMm.4558.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YT6NMR-A71-167[»]
ProteinModelPortaliQ04736.
SMRiQ04736. Positions 83-541.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204615. 5 interactions.
IntActiQ04736. 3 interactions.

PTM databases

PhosphoSiteiQ04736.

Proteomic databases

MaxQBiQ04736.
PaxDbiQ04736.
PRIDEiQ04736.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072311; ENSMUSP00000072154; ENSMUSG00000014932.
ENSMUST00000168707; ENSMUSP00000132161; ENSMUSG00000014932.
GeneIDi22612.
KEGGimmu:22612.
UCSCiuc008wzs.2. mouse.

Organism-specific databases

CTDi7525.
MGIiMGI:99147. Yes1.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiQ04736.
KOiK05705.
OMAiIKYRTEN.
OrthoDBiEOG7GTT2V.
PhylomeDBiQ04736.
TreeFamiTF351634.

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_280640. EPHA-mediated growth cone collapse.
REACT_292566. EPH-Ephrin signaling.
REACT_311393. CTLA4 inhibitory signaling.
REACT_313804. EPHB-mediated forward signaling.
REACT_314615. EPH-ephrin mediated repulsion of cells.
REACT_327841. Signaling by SCF-KIT.
REACT_333749. FCGR activation.
REACT_334921. CD28 co-stimulation.
REACT_354765. Regulation of KIT signaling.

Miscellaneous databases

EvolutionaryTraceiQ04736.
NextBioi302969.
PROiQ04736.
SOURCEiSearch...

Gene expression databases

BgeeiQ04736.
ExpressionAtlasiQ04736. baseline and differential.
GenevestigatoriQ04736.

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. "Molecular cloning and analysis of cDNA encoding the murine c-yes tyrosine protein kinase."
    Klages S., Adam D., Eiseman E., Fargnoli J., Dymecki S.M., Desiderio S.V., Bolen J.B.
    Oncogene 8:713-719(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary gland.
  3. "Protein tyrosine kinases transcribed in a murine thymic medullary epithelial cell line."
    Hebert B., Bergeron J., Tijssen P., Potworowski E.F.
    Gene 143:257-260(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 391-458.
  4. "Activation of Src family kinases by colony stimulating factor-1, and their association with its receptor."
    Courtneidge S.A., Dhand R., Pilat D., Twamley G.M., Waterfield M.D., Roussel M.F.
    EMBO J. 12:943-950(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSF1R.
  5. "Combined deficiencies of Src, Fyn, and Yes tyrosine kinases in mutant mice."
    Stein P.L., Vogel H., Soriano P.
    Genes Dev. 8:1999-2007(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  6. "Identification of autophosphorylation sites in c-Yes purified from rat liver plasma membranes."
    Ariki M., Tanabe O., Usui H., Hayashi H., Inoue R., Nishito Y., Kagamiyama H., Takeda M.
    J. Biochem. 121:104-111(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-32.
  7. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-535, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  8. "Solution structure of the SH3_1 domain of Yamaguchi sarcoma viral (v-Yes) oncogene homolog 1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 62-167.

Entry informationi

Entry nameiYES_MOUSE
AccessioniPrimary (citable) accession number: Q04736
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. 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.