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Protein

Tyrosine-protein kinase Yes

Gene

Yes1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei303ATPPROSITE-ProRule annotation1
Active sitei394Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi281 – 289ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

  • cell differentiation Source: GO_Central
  • cellular response to platelet-derived growth factor stimulus Source: MGI
  • cellular response to retinoic acid Source: MGI
  • cellular response to transforming growth factor beta stimulus Source: MGI
  • glucose transport Source: MGI
  • innate immune response Source: GO_Central
  • peptidyl-tyrosine autophosphorylation Source: GO_Central
  • positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • regulation of cell proliferation Source: GO_Central
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
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.
ReactomeiR-MMU-1433557. Signaling by SCF-KIT.
R-MMU-1433559. Regulation of KIT signaling.
R-MMU-389356. CD28 co-stimulation.
R-MMU-389513. CTLA4 inhibitory signaling.
R-MMU-3928662. EPHB-mediated forward signaling.
R-MMU-3928663. EPHA-mediated growth cone collapse.
R-MMU-3928665. EPH-ephrin mediated repulsion of cells.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:99147. Yes1.

Subcellular locationi

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000881822 – 541Tyrosine-protein kinase YesAdd BLAST540

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycineBy similarity1
Lipidationi3S-palmitoyl cysteine; in membrane formBy similarity1
Modified residuei32Phosphotyrosine1 Publication1
Modified residuei334PhosphotyrosineBy similarity1
Modified residuei343PhosphotyrosineBy similarity1
Modified residuei424Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei535PhosphotyrosineCombined sources1

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

PaxDbiQ04736.
PeptideAtlasiQ04736.
PRIDEiQ04736.

PTM databases

iPTMnetiQ04736.
PhosphoSitePlusiQ04736.
SwissPalmiQ04736.

Expressioni

Gene expression databases

BgeeiENSMUSG00000014932.
ExpressionAtlasiQ04736. baseline and differential.
GenevisibleiQ04736. MM.

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204615. 6 interactors.
IntActiQ04736. 4 interactors.
STRINGi10090.ENSMUSP00000072154.

Structurei

Secondary structure

1541
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi93 – 98Combined sources6
Beta strandi115 – 120Combined sources6
Beta strandi127 – 134Combined sources8
Beta strandi137 – 140Combined sources4
Turni142 – 144Combined sources3
Beta strandi145 – 150Combined sources6
Turni152 – 154Combined sources3
Helixi155 – 159Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YT6NMR-A71-167[»]
ProteinModelPortaliQ04736.
SMRiQ04736.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04736.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini89 – 150SH3PROSITE-ProRule annotationAdd BLAST62
Domaini156 – 253SH2PROSITE-ProRule annotationAdd BLAST98
Domaini275 – 528Protein kinasePROSITE-ProRule annotationAdd BLAST254

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

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiQ04736.
KOiK05705.
OMAiIKYRTEN.
OrthoDBiEOG091G0D46.
PhylomeDBiQ04736.
TreeFamiTF351634.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR028459. FGR.
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]
PANTHERiPTHR24418:SF224. PTHR24418:SF224. 1 hit.
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.
ENSMUST00000202543; ENSMUSP00000144001; 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.
CCDSiCCDS39061.1.
PIRiI48318. S31645.
RefSeqiNP_001192061.1. NM_001205132.1.
NP_001192062.1. NM_001205133.1.
NP_033561.1. NM_009535.3.
UniGeneiMm.4558.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YT6NMR-A71-167[»]
ProteinModelPortaliQ04736.
SMRiQ04736.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204615. 6 interactors.
IntActiQ04736. 4 interactors.
STRINGi10090.ENSMUSP00000072154.

PTM databases

iPTMnetiQ04736.
PhosphoSitePlusiQ04736.
SwissPalmiQ04736.

Proteomic databases

PaxDbiQ04736.
PeptideAtlasiQ04736.
PRIDEiQ04736.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072311; ENSMUSP00000072154; ENSMUSG00000014932.
ENSMUST00000168707; ENSMUSP00000132161; ENSMUSG00000014932.
ENSMUST00000202543; ENSMUSP00000144001; ENSMUSG00000014932.
GeneIDi22612.
KEGGimmu:22612.
UCSCiuc008wzs.2. mouse.

Organism-specific databases

CTDi7525.
MGIiMGI:99147. Yes1.

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiQ04736.
KOiK05705.
OMAiIKYRTEN.
OrthoDBiEOG091G0D46.
PhylomeDBiQ04736.
TreeFamiTF351634.

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiR-MMU-1433557. Signaling by SCF-KIT.
R-MMU-1433559. Regulation of KIT signaling.
R-MMU-389356. CD28 co-stimulation.
R-MMU-389513. CTLA4 inhibitory signaling.
R-MMU-3928662. EPHB-mediated forward signaling.
R-MMU-3928663. EPHA-mediated growth cone collapse.
R-MMU-3928665. EPH-ephrin mediated repulsion of cells.

Miscellaneous databases

EvolutionaryTraceiQ04736.
PROiQ04736.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000014932.
ExpressionAtlasiQ04736. baseline and differential.
GenevisibleiQ04736. MM.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR028459. FGR.
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]
PANTHERiPTHR24418:SF224. PTHR24418:SF224. 1 hit.
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]
ProtoNetiSearch...

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 2, 2016
This is version 182 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.