Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q04736 (YES_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase Yes

EC=2.7.10.2
Alternative name(s):
Proto-oncogene c-Yes
p61-Yes
Gene names
Name:Yes1
Synonyms:Yes
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length541 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Subunit structure

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. Ref.4

Subcellular location

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

Post-translational modification

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.

Palmitoylation at Cys-3 promotes membrane localization By similarity.

Disruption phenotype

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. Ref.5

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 541540Tyrosine-protein kinase Yes
PRO_0000088182

Regions

Domain89 – 15062SH3
Domain156 – 25398SH2
Domain275 – 528254Protein kinase
Nucleotide binding281 – 2899ATP By similarity

Sites

Active site3941Proton acceptor By similarity
Binding site3031ATP By similarity

Amino acid modifications

Modified residue111Phosphoserine By similarity
Modified residue261Phosphoserine By similarity
Modified residue321Phosphotyrosine By similarity
Modified residue1091Phosphoserine By similarity
Modified residue1921Phosphotyrosine By similarity
Modified residue1931Phosphoserine By similarity
Modified residue2201Phosphotyrosine By similarity
Modified residue2211Phosphotyrosine By similarity
Modified residue3341Phosphotyrosine By similarity
Modified residue3431Phosphotyrosine By similarity
Modified residue4241Phosphotyrosine; by autocatalysis By similarity
Modified residue4441Phosphotyrosine By similarity
Modified residue5351Phosphotyrosine; alternate Ref.7
Modified residue5351Phosphotyrosine; by CSK; alternate By similarity
Lipidation21N-myristoyl glycine By similarity
Lipidation31S-palmitoyl cysteine; in membrane form By similarity

Secondary structure

............... 541
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q04736 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9A773C39D2119EA6

FASTA54160,630
        10         20         30         40         50         60 
MGCIKSKENK SPAIKYTPEN LTEPVSPSAS HYGVEHATVA PTSSTKGASV NFNSLSMTPF 

        70         80         90        100        110        120 
GGSSGVTPFG GASSSFSVVS SSYPTGLTGG VTIFVALYDY EARTTEDLSF KKGERFQIIN 

       130        140        150        160        170        180 
NTEGDWWEAR SIATGKSGYI PSNYVVPADS IQAEEWYFGK MGRKDAERLL LNPGNQRGIF 

       190        200        210        220        230        240 
LVRESETTKG AYSLSIRDWD EVRGDNVKHY KIRKLDNGGY YITTRAQFDT LQKLVKHYTE 

       250        260        270        280        290        300 
HADGLCHKLT TVCPTVKPQT QGLAKDAWEI PRESLRLEVK LGQGCFGEVW MGTWNGTTKV 

       310        320        330        340        350        360 
AIKTLKPGTM MPEAFLQEAQ IMKKLRHDKL VPLYAVVSEE PIYIVTEFMS KGSLLDFLKE 

       370        380        390        400        410        420 
GDGKYLKLPQ LVDMAAQIAD GMAYIERMNY IHRDLRAANI LVGENLICKI ADFGLARLIE 

       430        440        450        460        470        480 
DNEYTARQGA KFPIKWTAPE AALYGRFTIK SDVWSFGILQ TELVTKGRVP YPGMVNREVL 

       490        500        510        520        530        540 
EQVERGYRMP CPQGCPESLH ELMNLCWKKD PDERPTFEYI QSFLEDYFTA TEPQYQPGEN 


L 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X67677 mRNA. Translation: CAA47909.1.
BC010594 mRNA. Translation: AAH10594.1.
L25762 mRNA. Translation: AAA40020.1.
CCDSCCDS39061.1.
PIRS31645. I48318.
RefSeqNP_001192061.1. NM_001205132.1.
NP_001192062.1. NM_001205133.1.
NP_033561.1. NM_009535.3.
UniGeneMm.4558.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YT6NMR-A71-167[»]
ProteinModelPortalQ04736.
SMRQ04736. Positions 83-541.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204615. 5 interactions.
IntActQ04736. 3 interactions.

PTM databases

PhosphoSiteQ04736.

Proteomic databases

MaxQBQ04736.
PaxDbQ04736.
PRIDEQ04736.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000072311; ENSMUSP00000072154; ENSMUSG00000014932.
ENSMUST00000168707; ENSMUSP00000132161; ENSMUSG00000014932.
GeneID22612.
KEGGmmu:22612.
UCSCuc008wzs.2. mouse.

Organism-specific databases

CTD7525.
MGIMGI:99147. Yes1.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233858.
HOVERGENHBG008761.
InParanoidQ04736.
KOK05705.
OMAIKYRTEN.
OrthoDBEOG7GTT2V.
PhylomeDBQ04736.
TreeFamTF351634.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.

Gene expression databases

ArrayExpressQ04736.
BgeeQ04736.
GenevestigatorQ04736.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR011009. 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]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. 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]
ProtoNetSearch...

Other

EvolutionaryTraceQ04736.
NextBio302969.
PROQ04736.
SOURCESearch...

Entry information

Entry nameYES_MOUSE
AccessionPrimary (citable) accession number: Q04736
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot