Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q04736

- YES_MOUSE

UniProt

Q04736 - YES_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Tyrosine-protein kinase Yes

Gene

Yes1

Organism
Mus musculus (Mouse)
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).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. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular response to platelet-derived growth factor stimulus Source: MGI
  2. glucose transport Source: MGI
  3. protein autophosphorylation Source: Ensembl
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_188578. Signaling by SCF-KIT.
REACT_196487. FCGR activation.
REACT_204081. CD28 co-stimulation.
REACT_227425. Regulation of KIT signaling.
REACT_243590. EPH-ephrin mediated repulsion of cells.
REACT_243939. EPHA-mediated growth cone collapse.
REACT_257656. EPHB-mediated forward signaling.
REACT_258158. EPH-Ephrin signaling.
REACT_261568. CTLA4 inhibitory 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: Chromosome 5

Organism-specific databases

MGIiMGI:99147. Yes1.

Subcellular locationi

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

GO - Cellular componenti

  1. actin filament Source: MGI
  2. extracellular vesicular exosome Source: Ensembl
  3. Golgi apparatus Source: Ensembl
  4. 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 – 11RemovedBy similarity
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 residuei11 – 111PhosphoserineBy similarity
Modified residuei26 – 261PhosphoserineBy similarity
Modified residuei32 – 321PhosphotyrosineBy similarity
Modified residuei109 – 1091PhosphoserineBy similarity
Modified residuei192 – 1921PhosphotyrosineBy similarity
Modified residuei193 – 1931PhosphoserineBy similarity
Modified residuei220 – 2201PhosphotyrosineBy similarity
Modified residuei221 – 2211PhosphotyrosineBy similarity
Modified residuei334 – 3341PhosphotyrosineBy similarity
Modified residuei343 – 3431PhosphotyrosineBy similarity
Modified residuei424 – 4241Phosphotyrosine; by autocatalysisBy similarity
Modified residuei444 – 4441PhosphotyrosineBy 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 .
CCDSi CCDS39061.1.
PIRi I48318. S31645.
RefSeqi NP_001192061.1. NM_001205132.1.
NP_001192062.1. NM_001205133.1.
NP_033561.1. NM_009535.3.
UniGenei Mm.4558.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YT6 NMR - A 71-167 [» ]
ProteinModelPortali Q04736.
SMRi Q04736. Positions 83-541.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204615. 5 interactions.
IntActi Q04736. 3 interactions.

PTM databases

PhosphoSitei Q04736.

Proteomic databases

MaxQBi Q04736.
PaxDbi Q04736.
PRIDEi Q04736.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000072311 ; ENSMUSP00000072154 ; ENSMUSG00000014932 .
ENSMUST00000168707 ; ENSMUSP00000132161 ; ENSMUSG00000014932 .
GeneIDi 22612.
KEGGi mmu:22612.
UCSCi uc008wzs.2. mouse.

Organism-specific databases

CTDi 7525.
MGIi MGI:99147. Yes1.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233858.
HOVERGENi HBG008761.
InParanoidi Q04736.
KOi K05705.
OMAi IKYRTEN.
OrthoDBi EOG7GTT2V.
PhylomeDBi Q04736.
TreeFami TF351634.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 3474.
Reactomei REACT_188578. Signaling by SCF-KIT.
REACT_196487. FCGR activation.
REACT_204081. CD28 co-stimulation.
REACT_227425. Regulation of KIT signaling.
REACT_243590. EPH-ephrin mediated repulsion of cells.
REACT_243939. EPHA-mediated growth cone collapse.
REACT_257656. EPHB-mediated forward signaling.
REACT_258158. EPH-Ephrin signaling.
REACT_261568. CTLA4 inhibitory signaling.

Miscellaneous databases

EvolutionaryTracei Q04736.
NextBioi 302969.
PROi Q04736.
SOURCEi Search...

Gene expression databases

Bgeei Q04736.
ExpressionAtlasi Q04736. baseline and differential.
Genevestigatori Q04736.

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. "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: November 26, 2014
This is version 161 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