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F1LM93 (YES_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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):
p61-Yes
Gene names
Name:Yes1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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. Ref.4

Catalytic activity

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

Subunit structure

Interacts with YAP1 and CSF1R By similarity. Interacts with FASLG By similarity. Interacts with CTNND1; this interaction allows YES1-mediated activation of FYN and FER and subsequent phosphorylation of CTNND1. Ref.3

Subcellular location

Cell membrane. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytosol. 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-424 maintains enzyme activity by blocking CSK-mediated inhibition By similarity.

Palmitoylation at Cys-3 promotes membrane localization By similarity.

Sequence similarities

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 Potential
Chain2 – 541540Tyrosine-protein kinase Yes
PRO_0000413800

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 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; by CSK By similarity
Lipidation21N-myristoyl glycine Potential
Lipidation31S-palmitoyl cysteine; in membrane form By similarity

Sequences

Sequence LengthMass (Da)Tools
F1LM93 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 3864A9ED1D3A3F2F

FASTA54160,614
        10         20         30         40         50         60 
MGCIKSKENK SPAIKYTPEN PTEPVNTSAG HYGVEHATAA TTSSTKGASA NFNSLSMTPF 

        70         80         90        100        110        120 
GGSSGVTPFG GASSSFSVVP SSYPTSLTGG VTIFVALYDY EARTTEDLSF KKGERFQIIN 

       130        140        150        160        170        180 
NTEGDWWEAR SIATGKNGYI PSNYVAPADS 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 KGILLDFLKE 

       370        380        390        400        410        420 
GDGKYLKLPQ LVDMAAQIAD GMAYIERMNY IHRDLRAANI LVGENLVCKI 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]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"Specific proto-oncogenic tyrosine kinases of src family are enriched in cell-to-cell adherens junctions where the level of tyrosine phosphorylation is elevated."
Tsukita S., Oishi K., Akiyama T., Yamanashi Y., Yamamoto T., Tsukita S.
J. Cell Biol. 113:867-879(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[3]"p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin Interaction."
Piedra J., Miravet S., Castano J., Palmer H.G., Heisterkamp N., Garcia de Herreros A., Dunach M.
Mol. Cell. Biol. 23:2287-2297(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTNND1.
[4]"c-Yes regulates cell adhesion at the blood-testis barrier and the apical ectoplasmic specialization in the seminiferous epithelium of rat testes."
Xiao X., Mruk D.D., Lee W.M., Cheng C.Y.
Int. J. Biochem. Cell Biol. 43:651-665(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03068393 Genomic DNA. No translation available.
AABR03068636 Genomic DNA. No translation available.
UniGeneRn.214217.
Rn.6816.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000056250; ENSRNOP00000053093; ENSRNOG00000037227.

Organism-specific databases

RGD3977. Yes1.

Phylogenomic databases

GeneTreeENSGT00620000087702.
OMAIKYRTEN.
OrthoDBEOG7GTT2V.
TreeFamTF351634.

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

PROF1LM93.

Entry information

Entry nameYES_RAT
AccessionPrimary (citable) accession number: F1LM93
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2011
Last sequence update: May 3, 2011
Last modified: April 16, 2014
This is version 25 of the entry and version 1 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