Tyrosine-protein kinase Yes - Canis familiaris (Dog)

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Q28923 (YES_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 111. History...

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

Documents (1) |

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

Canis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis ›

Protein attributes

Sequence length	539 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. Interacts with CSF1R By similarity. Ref.2
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. Ref.2
Post-translational modification	Phosphorylation by CSK on the C-terminal tail maintains the enzyme in an inactive state. Autophosphorylation at Tyr-422 maintains enzyme activity by blocking CSK-mediated inhibition By similarity. Palmitoylation at Cys-3 promotes membrane localization By similarity.
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	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	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 – 539

539

Tyrosine-protein kinase Yes

PRO_0000088180

Regions

Domain

87 – 148

SH3

Domain

154 – 251

SH2

Domain

273 – 526

254

Protein kinase

Nucleotide binding

279 – 287

ATP By similarity

Sites

Active site

392

Proton acceptor By similarity

Binding site

301

ATP By similarity

Amino acid modifications

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphotyrosine By similarity

Modified residue

107

Phosphoserine By similarity

Modified residue

190

Phosphotyrosine By similarity

Modified residue

191

Phosphoserine By similarity

Modified residue

218

Phosphotyrosine By similarity

Modified residue

219

Phosphotyrosine By similarity

Modified residue

332

Phosphotyrosine By similarity

Modified residue

341

Phosphotyrosine By similarity

Modified residue

422

Phosphotyrosine; by autocatalysis By similarity

Modified residue

442

Phosphotyrosine By similarity

Modified residue

533

Phosphotyrosine; by CSK By similarity

Lipidation

N-myristoyl glycine By similarity

Lipidation

S-palmitoyl cysteine; in membrane form By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q28923 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CC4BEA38073CC106
Show »

FASTA

539

60,300

        10         20         30         40         50         60 
MGCIKSKEDK GPAIKYRNTP EPVSVSHYGA EPTQATPWPS SSGWGTAFNF SSLSMTGFGG 

        70         80         90        100        110        120 
SSGVTPFGGA SSSFSVVPSP YPAGLTGGVT IFVALYDYEA RTTEDLSFKG GERFQIINNT 

       130        140        150        160        170        180 
EGDWWEARSI ATGKNGYIPS NYVAPADSIA AEEWYFGKMG RKDAERLLLN PGNQRGIFLV 

       190        200        210        220        230        240 
RESETTKGAY SLSIRDWDEI RGDNVKHYKI RKLDNGGYYI TTRAQFDTLQ KLVKHSTEHA 

       250        260        270        280        290        300 
DGLCHKLTTV CPTVKPQTQG LAKDAWEIPR ESLRLEVKLG QGCFGEVWMG TWNGTTKVAI 

       310        320        330        340        350        360 
KTLKLGTMMP EAFLQEAQIM KKLRHDKLVP LYAVVSEEPI YIVTEFMSKG SLLDFLKEGD 

       370        380        390        400        410        420 
GKYLKLPQLV DMAAQIADGM AYIERMNYIH RDLRAANILV GENLVCKIAD FGLARLIEDN 

       430        440        450        460        470        480 
EYTARQGAKF PIKWTAPEAA LYGRFTIKSD VWSFGILQTE LTTKGRVPYP GMVNREVLEQ 

       490        500        510        520        530 
VERGYRMPCP QGCPESLHEL MNLCWKKDPD ERPTFEYIQS FLEDYFTAAE PQYQPGENL

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References

[1]	"Sequence of the canine c-yes proto-oncogene." Zhao D.M., Tateyama S., Miyoshi N., Uchida K., Yamaguchi R., Yamagami T., Hayashi T. Res. Vet. Sci. 59:230-233(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Spleen.
[2]	"Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight junction formation in canine kidney epithelial cells." Chen Y.H., Lu Q., Goodenough D.A., Jeansonne B. Mol. Biol. Cell 13:1227-1237(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH OCLLUDIN/OCLN, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S81472 mRNA. Translation: AAB36132.1.
RefSeq	NP_001003239.1. NM_001003239.1.
UniGene	Cfa.3778.
3D structure databases
ProteinModelPortal	Q28923.
SMR	Q28923. Positions 89-539.
ModBase	Search...
Protein-protein interaction databases
STRING	9615.ENSCAFP00000027127.
Proteomic databases
PRIDE	Q28923.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	403917.
KEGG	cfa:403917.
Organism-specific databases
CTD	7525.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233858.
HOVERGEN	HBG008761.
InParanoid	Q28923.
KO	K05705.
OrthoDB	EOG4KKZ2S.
Enzyme and pathway databases
BRENDA	2.7.10.2. 1154.
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
NextBio	20817409.

Entry information

Entry name

YES_CANFA

Accession

Primary (citable) accession number: Q28923

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 111 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

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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents