dbPTM

YES_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	YES_MOUSE
UniProt AC	Q04736
Protein Name	Tyrosine-protein kinase Yes
Gene Name	Yes1
Organism	Mus musculus (Mouse).
Sequence Length	541
Subcellular Localization	Cell membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytosol. Newly synthesized protein initially accumulates in the Golgi region and traffics to the plasma membrane through the exocytic pathway..
Protein Description	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)..
Protein Sequence	MGCIKSKENKSPAIKYTPENLTEPVSPSASHYGVEHATVAPTSSTKGASVNFNSLSMTPFGGSSGVTPFGGASSSFSVVSSSYPTGLTGGVTIFVALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKSGYIPSNYVVPADSIQAEEWYFGKMGRKDAERLLLNPGNQRGIFLVRESETTKGAYSLSIRDWDEVRGDNVKHYKIRKLDNGGYYITTRAQFDTLQKLVKHYTEHADGLCHKLTTVCPTVKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEFMSKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGENLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILQTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHELMNLCWKKDPDERPTFEYIQSFLEDYFTATEPQYQPGENL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Myristoylation	------MGCIKSKEN ------CCCCCCCCC	23.12	-
3	S-palmitoylation	-----MGCIKSKENK -----CCCCCCCCCC	3.23	-
11	Phosphorylation	IKSKENKSPAIKYTP CCCCCCCCCCCCCCC	31.01	-
15	Ubiquitination	ENKSPAIKYTPENLT CCCCCCCCCCCCCCC	45.22	22790023
16	Phosphorylation	NKSPAIKYTPENLTE CCCCCCCCCCCCCCC	22.78	27087446
17	Phosphorylation	KSPAIKYTPENLTEP CCCCCCCCCCCCCCC	21.08	26643407
22	Phosphorylation	KYTPENLTEPVSPSA CCCCCCCCCCCCCCC	50.23	26643407
26	Phosphorylation	ENLTEPVSPSASHYG CCCCCCCCCCCCCCC	24.69	27087446
28	Phosphorylation	LTEPVSPSASHYGVE CCCCCCCCCCCCCCC	34.59	27087446
30	Phosphorylation	EPVSPSASHYGVEHA CCCCCCCCCCCCCEE	22.91	27087446
32	Phosphorylation	VSPSASHYGVEHATV CCCCCCCCCCCEEEE	21.99	9058199
38	Phosphorylation	HYGVEHATVAPTSST CCCCCEEEECCCCCC	21.07	26643407
42	Phosphorylation	EHATVAPTSSTKGAS CEEEECCCCCCCCCE	26.10	26643407
43	Phosphorylation	HATVAPTSSTKGASV EEEECCCCCCCCCEE	34.64	26643407
44	Phosphorylation	ATVAPTSSTKGASVN EEECCCCCCCCCEEE	36.29	26643407
45	Phosphorylation	TVAPTSSTKGASVNF EECCCCCCCCCEEEC	33.01	26643407
67	Phosphorylation	FGGSSGVTPFGGASS CCCCCCCCCCCCCCC	19.20	-
74	Phosphorylation	TPFGGASSSFSVVSS CCCCCCCCCEEEEEC	34.56	-
75	Phosphorylation	PFGGASSSFSVVSSS CCCCCCCCEEEEECC	21.03	-
98	Phosphorylation	VTIFVALYDYEARTT EEEEEEEEECCCCCC	13.52	-
157	Phosphorylation	SIQAEEWYFGKMGRK HCCCHHHHCCCCCHH	13.01	-
189	Ubiquitination	VRESETTKGAYSLSI EEECCCCCCEEEEEE	49.30	22790023
192	Phosphorylation	SETTKGAYSLSIRDW CCCCCCEEEEEEECH	20.86	25521595
193	Phosphorylation	ETTKGAYSLSIRDWD CCCCCEEEEEEECHH	18.33	23737553
195	Phosphorylation	TKGAYSLSIRDWDEV CCCEEEEEEECHHHH	15.05	25367039
220	Phosphorylation	RKLDNGGYYITTRAQ EECCCCCEEEEEHHH	7.97	25521595
221	Phosphorylation	KLDNGGYYITTRAQF ECCCCCEEEEEHHHH	8.61	20116462
223	Phosphorylation	DNGGYYITTRAQFDT CCCCEEEEEHHHHHH	8.29	21183079
224	Phosphorylation	NGGYYITTRAQFDTL CCCEEEEEHHHHHHH	17.91	20415495
233	Ubiquitination	AQFDTLQKLVKHYTE HHHHHHHHHHHHHHH	59.36	22790023
255	Phosphorylation	KLTTVCPTVKPQTQG HCHHCCCCCCCCCCC	35.71	23140645
260	Phosphorylation	CPTVKPQTQGLAKDA CCCCCCCCCCCCCCH	32.88	23140645
306	Ubiquitination	KVAIKTLKPGTMMPE EEEEEECCCCCCCCH	46.78	-
324	Ubiquitination	QEAQIMKKLRHDKLV HHHHHHHHHCCCCCE	33.11	-
334	Phosphorylation	HDKLVPLYAVVSEEP CCCCEEEEEEECCCC	7.41	-
343	Phosphorylation	VVSEEPIYIVTEFMS EECCCCEEEEEEECC	10.47	25263469
424	Phosphorylation	RLIEDNEYTARQGAK HHHCCCCCCCCCCCC	16.38	18515860
425	Phosphorylation	LIEDNEYTARQGAKF HHCCCCCCCCCCCCC	14.80	27566939
444	Phosphorylation	TAPEAALYGRFTIKS CCCCHHHHCCEEECC	11.09	20116462
527	Phosphorylation	IQSFLEDYFTATEPQ HHHHHHHHHCCCCCC	8.08	20415495
529	Phosphorylation	SFLEDYFTATEPQYQ HHHHHHHCCCCCCCC	26.83	20415495
531	Phosphorylation	LEDYFTATEPQYQPG HHHHHCCCCCCCCCC	45.18	26643407
535	Phosphorylation	FTATEPQYQPGENL- HCCCCCCCCCCCCC-	27.65	27180971

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
32	Y	Phosphorylation	Kinase	YES1	Q04736	GPS
424	Y	Phosphorylation	Kinase	YES1	Q04736	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
3	C	Palmitoylation		-
Palmitoylation at Cys-3 promotes membrane localization.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of YES_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KHDR1_MOUSE	Khdrbs1	physical	10844001
DIAP1_MOUSE	Diap1	physical	18194650
JAK2_MOUSE	Jak2	physical	8702385

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of YES_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-192; TYR-220; TYR-424AND TYR-535, AND MASS SPECTROMETRY.	18034455 [Abstract]

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