Tyrosine-protein kinase Yes - Mus musculus (Mouse)

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Q04736 (YES_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 143. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	541 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity. Interacts with CSF1R. Ref.4
Subcellular location	Cell membrane By similarity. Cytoplasm › cytoskeleton › centrosome By similarity. Cytoplasm › cytosol By similarity. Note: Newly synthesized protein initially accumulates in the Golgi region and traffics to the plasma membrane through the exocytic pathway By similarity.
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.
Disruption phenotype	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. Ref.5
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.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Disease	Proto-oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glucose transport Inferred from direct assay PubMed 11546805. Source: MGI protein autophosphorylation Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 541

541

Tyrosine-protein kinase Yes

PRO_0000088182

Regions

Domain

89 – 150

SH3

Domain

156 – 253

SH2

Domain

275 – 528

254

Protein kinase

Nucleotide binding

281 – 289

ATP By similarity

Sites

Active site

394

Proton acceptor By similarity

Binding site

303

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphotyrosine By similarity

Modified residue

109

Phosphoserine By similarity

Modified residue

192

Phosphotyrosine Ref.8

Modified residue

193

Phosphoserine By similarity

Modified residue

220

Phosphotyrosine Ref.8

Modified residue

221

Phosphotyrosine By similarity

Modified residue

334

Phosphotyrosine By similarity

Modified residue

343

Phosphotyrosine By similarity

Modified residue

424

Phosphotyrosine; by autocatalysis By similarity

Modified residue

444

Phosphotyrosine By similarity

Modified residue

535

Phosphotyrosine; by CSK By similarity

Lipidation

N-myristoyl glycine By similarity

Lipidation

S-palmitoyl cysteine; in membrane form By similarity

Secondary structure

541

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q04736 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9A773C39D2119EA6
Show »

FASTA

541

60,630

        10         20         30         40         50         60 
MGCIKSKENK SPAIKYTPEN LTEPVSPSAS HYGVEHATVA PTSSTKGASV NFNSLSMTPF 

        70         80         90        100        110        120 
GGSSGVTPFG GASSSFSVVS SSYPTGLTGG VTIFVALYDY EARTTEDLSF KKGERFQIIN 

       130        140        150        160        170        180 
NTEGDWWEAR SIATGKSGYI PSNYVVPADS 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 KGSLLDFLKE 

       370        380        390        400        410        420 
GDGKYLKLPQ LVDMAAQIAD GMAYIERMNY IHRDLRAANI LVGENLICKI 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' referencesShow 'large scale' references »
[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: AUTOPHOSPHORYLATION.
[7]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-424, MASS SPECTROMETRY. Tissue: Mast cell.
[8]	"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-192; TYR-220; TYR-424 AND TYR-535, MASS SPECTROMETRY. Tissue: Brain.
[9]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X67677 mRNA. Translation: CAA47909.1.
BC010594 mRNA. Translation: AAH10594.1.
L25762 mRNA. Translation: AAA40020.1.

IPI

IPI00109672.

PIR

S31645. I48318.

RefSeq

NP_001192061.1. NM_001205132.1.
NP_001192062.1. NM_001205133.1.
NP_033561.1. NM_009535.3.

UniGene

Mm.4558.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YT6	NMR	-	A	71-167	[»]

ProteinModelPortal

Q04736.

SMR

Q04736. Positions 83-541.

ModBase

Search...

PTM databases

PhosphoSite

Q04736.

Proteomic databases

PaxDb

Q04736.

PRIDE

Q04736.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000072311; ENSMUSP00000072154; ENSMUSG00000014932.
ENSMUST00000168707; ENSMUSP00000132161; ENSMUSG00000014932.

GeneID

22612.

KEGG

mmu:22612.

Organism-specific databases

CTD

7525.

MGI

MGI:99147. Yes1.

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233858.

HOVERGEN

HBG008761.

InParanoid

Q04736.

K05705.

OMA

IKYRTEN.

OrthoDB

EOG4KKZ2S.

Enzyme and pathway databases

BRENDA

2.7.10.2. 3474.

Gene expression databases

ArrayExpress

Q04736.

Bgee

Q04736.

Genevestigator

Q04736.

GermOnline

ENSMUSG00000014932. Mus musculus.

Family and domain databases

Gene3D

3.30.505.10. 1 hit.

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_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]

Pfam

PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.

SMART

SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other

EvolutionaryTrace

Q04736.

NextBio

302969.

SOURCE

Search...

Entry information

Entry name

YES_MOUSE

Accession

Primary (citable) accession number: Q04736

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 143 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents