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Q28923 (YES_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length539 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. Interacts with CSF1R By similarity. Ref.2

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. Ref.2

Post-translational modification

Phosphorylation by CSK on the C-terminal tail maintains the enzyme in an inactive state. Autophosphorylation at Tyr-422 maintains enzyme activity by blocking CSK-mediated inhibition By similarity.

Palmitoylation at Cys-3 promotes membrane localization By similarity.

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 – 539538Tyrosine-protein kinase Yes
PRO_0000088180

Regions

Domain87 – 14862SH3
Domain154 – 25198SH2
Domain273 – 526254Protein kinase
Nucleotide binding279 – 2879ATP By similarity

Sites

Active site3921Proton acceptor By similarity
Binding site3011ATP By similarity

Amino acid modifications

Modified residue191Phosphothreonine By similarity
Modified residue281Phosphotyrosine By similarity
Modified residue1071Phosphoserine By similarity
Modified residue1901Phosphotyrosine By similarity
Modified residue1911Phosphoserine By similarity
Modified residue2181Phosphotyrosine By similarity
Modified residue2191Phosphotyrosine By similarity
Modified residue3321Phosphotyrosine By similarity
Modified residue3411Phosphotyrosine By similarity
Modified residue4221Phosphotyrosine; by autocatalysis By similarity
Modified residue4421Phosphotyrosine By similarity
Modified residue5331Phosphotyrosine; by CSK By similarity
Lipidation21N-myristoyl glycine By similarity
Lipidation31S-palmitoyl cysteine; in membrane form By similarity

Sequences

Sequence LengthMass (Da)Tools
Q28923 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CC4BEA38073CC106

FASTA53960,300
        10         20         30         40         50         60 
MGCIKSKEDK GPAIKYRNTP EPVSVSHYGA EPTQATPWPS SSGWGTAFNF SSLSMTGFGG 

        70         80         90        100        110        120 
SSGVTPFGGA SSSFSVVPSP YPAGLTGGVT IFVALYDYEA RTTEDLSFKG GERFQIINNT 

       130        140        150        160        170        180 
EGDWWEARSI ATGKNGYIPS NYVAPADSIA AEEWYFGKMG RKDAERLLLN PGNQRGIFLV 

       190        200        210        220        230        240 
RESETTKGAY SLSIRDWDEI RGDNVKHYKI RKLDNGGYYI TTRAQFDTLQ KLVKHSTEHA 

       250        260        270        280        290        300 
DGLCHKLTTV CPTVKPQTQG LAKDAWEIPR ESLRLEVKLG QGCFGEVWMG TWNGTTKVAI 

       310        320        330        340        350        360 
KTLKLGTMMP EAFLQEAQIM KKLRHDKLVP LYAVVSEEPI YIVTEFMSKG SLLDFLKEGD 

       370        380        390        400        410        420 
GKYLKLPQLV DMAAQIADGM AYIERMNYIH RDLRAANILV GENLVCKIAD FGLARLIEDN 

       430        440        450        460        470        480 
EYTARQGAKF PIKWTAPEAA LYGRFTIKSD VWSFGILQTE LTTKGRVPYP GMVNREVLEQ 

       490        500        510        520        530 
VERGYRMPCP QGCPESLHEL MNLCWKKDPD ERPTFEYIQS FLEDYFTAAE PQYQPGENL 

« Hide

References

[1]"Sequence of the canine c-yes proto-oncogene."
Zhao D.M., Tateyama S., Miyoshi N., Uchida K., Yamaguchi R., Yamagami T., Hayashi T.
Res. Vet. Sci. 59:230-233(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Spleen.
[2]"Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight junction formation in canine kidney epithelial cells."
Chen Y.H., Lu Q., Goodenough D.A., Jeansonne B.
Mol. Biol. Cell 13:1227-1237(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH OCLLUDIN/OCLN, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S81472 mRNA. Translation: AAB36132.1.
RefSeqNP_001003239.1. NM_001003239.1.
UniGeneCfa.3778.

3D structure databases

ProteinModelPortalQ28923.
SMRQ28923. Positions 89-539.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000027127.

Proteomic databases

PRIDEQ28923.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID403917.
KEGGcfa:403917.

Organism-specific databases

CTD7525.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233858.
HOVERGENHBG008761.
InParanoidQ28923.
KOK05705.

Enzyme and pathway databases

BRENDA2.7.10.2. 1154.

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

NextBio20817409.

Entry information

Entry nameYES_CANFA
AccessionPrimary (citable) accession number: Q28923
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 118 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