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F1LM93

- YES_RAT

UniProt

F1LM93 - YES_RAT

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Protein
Tyrosine-protein kinase Yes
Gene
Yes1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei303 – 3031ATP By similarity
Active sitei394 – 3941Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi281 – 2899ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. epidermal growth factor receptor binding Source: RGD
  3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  4. protein tyrosine kinase activity Source: RGD

GO - Biological processi

  1. glucose transport Source: Ensembl
  2. peptidyl-tyrosine phosphorylation Source: GOC
  3. protein autophosphorylation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_195025. Signaling by SCF-KIT.
REACT_197451. Regulation of KIT signaling.
REACT_198646. FCGR activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Yes (EC:2.7.10.2)
Alternative name(s):
p61-Yes
Gene namesi
Name:Yes1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 9

Organism-specific databases

RGDi3977. Yes1.

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. cytosol Source: UniProtKB-SubCell
  3. microtubule organizing center Source: UniProtKB-SubCell
  4. plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed Reviewed prediction
Chaini2 – 541540Tyrosine-protein kinase Yes
PRO_0000413800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine Reviewed prediction
Lipidationi3 – 31S-palmitoyl cysteine; in membrane form By similarity
Modified residuei11 – 111Phosphoserine By similarity
Modified residuei32 – 321Phosphotyrosine By similarity
Modified residuei109 – 1091Phosphoserine By similarity
Modified residuei192 – 1921Phosphotyrosine By similarity
Modified residuei193 – 1931Phosphoserine By similarity
Modified residuei220 – 2201Phosphotyrosine By similarity
Modified residuei221 – 2211Phosphotyrosine By similarity
Modified residuei334 – 3341Phosphotyrosine By similarity
Modified residuei343 – 3431Phosphotyrosine By similarity
Modified residuei424 – 4241Phosphotyrosine; by autocatalysis By similarity
Modified residuei444 – 4441Phosphotyrosine By similarity
Modified residuei535 – 5351Phosphotyrosine; by CSK By 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.
Palmitoylation at Cys-3 promotes membrane localization By similarity.

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Interactioni

Subunit structurei

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 CTNND1.1 Publication

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini89 – 15062SH3
Add
BLAST
Domaini156 – 25398SH2
Add
BLAST
Domaini275 – 528254Protein kinase
Add
BLAST

Sequence similaritiesi

Contains 1 SH2 domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

GeneTreeiENSGT00620000087702.
OMAiIKYRTEN.
OrthoDBiEOG7GTT2V.
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.

F1LM93-1 [UniParc]FASTAAdd to Basket

« Hide

MGCIKSKENK SPAIKYTPEN PTEPVNTSAG HYGVEHATAA TTSSTKGASA    50
NFNSLSMTPF GGSSGVTPFG GASSSFSVVP SSYPTSLTGG VTIFVALYDY 100
EARTTEDLSF KKGERFQIIN NTEGDWWEAR SIATGKNGYI PSNYVAPADS 150
IQAEEWYFGK MGRKDAERLL LNPGNQRGIF LVRESETTKG AYSLSIRDWD 200
EVRGDNVKHY KIRKLDNGGY YITTRAQFDT LQKLVKHYTE HADGLCHKLT 250
TVCPTVKPQT QGLAKDAWEI PRESLRLEVK LGQGCFGEVW MGTWNGTTKV 300
AIKTLKPGTM MPEAFLQEAQ IMKKLRHDKL VPLYAVVSEE PIYIVTEFMS 350
KGILLDFLKE GDGKYLKLPQ LVDMAAQIAD GMAYIERMNY IHRDLRAANI 400
LVGENLVCKI ADFGLARLIE DNEYTARQGA KFPIKWTAPE AALYGRFTIK 450
SDVWSFGILQ TELVTKGRVP YPGMVNREVL EQVERGYRMP CPQGCPESLH 500
ELMNLCWKKD PDERPTFEYI QSFLEDYFTA TEPQYQPGEN L 541
Length:541
Mass (Da):60,614
Last modified:May 3, 2011 - v1
Checksum:i3864A9ED1D3A3F2F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR03068393 Genomic DNA. No translation available.
AABR03068636 Genomic DNA. No translation available.
UniGeneiRn.214217.
Rn.6816.

Genome annotation databases

EnsembliENSRNOT00000056250; ENSRNOP00000053093; ENSRNOG00000037227.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR03068393 Genomic DNA. No translation available.
AABR03068636 Genomic DNA. No translation available.
UniGenei Rn.214217.
Rn.6816.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000056250 ; ENSRNOP00000053093 ; ENSRNOG00000037227 .

Organism-specific databases

RGDi 3977. Yes1.

Phylogenomic databases

GeneTreei ENSGT00620000087702.
OMAi IKYRTEN.
OrthoDBi EOG7GTT2V.
TreeFami TF351634.

Enzyme and pathway databases

Reactomei REACT_195025. Signaling by SCF-KIT.
REACT_197451. Regulation of KIT signaling.
REACT_198646. FCGR activation.

Miscellaneous databases

PROi F1LM93.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR011009. 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 ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiYES_RAT
AccessioniPrimary (citable) accession number: F1LM93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2011
Last sequence update: May 3, 2011
Last modified: September 3, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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