dbPTM

YES_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	YES_HUMAN
UniProt AC	P07947
Protein Name	Tyrosine-protein kinase Yes
Gene Name	YES1
Organism	Homo sapiens (Human).
Sequence Length	543
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..
Protein Sequence	MGCIKSKENKSPAIKYRPENTPEPVSTSVSHYGAEPTTVSPCPSSSAKGTAVNFSSLSMTPFGGSSGVTPFGGASSSFSVVPSSYPAGLTGGVTIFVALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKNGYIPSNYVAPADSIQAEEWYFGKMGRKDAERLLLNPGNQRGIFLVRESETTKGAYSLSIRDWDEIRGDNVKHYKIRKLDNGGYYITTRAQFDTLQKLVKHYTEHADGLCHKLTTVCPTVKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEFMSKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGENLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILQTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHELMNLCWKKDPDERPTFEYIQSFLEDYFTATEPQYQPGENL

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	-
6	Phosphorylation	--MGCIKSKENKSPA --CCCCCCCCCCCCC	25.87	28348404
10	Ubiquitination	CIKSKENKSPAIKYR CCCCCCCCCCCCCCC	59.93	33845483
11	Phosphorylation	IKSKENKSPAIKYRP CCCCCCCCCCCCCCC	31.01	26055452
15	Ubiquitination	ENKSPAIKYRPENTP CCCCCCCCCCCCCCC	37.00	21963094
16	Phosphorylation	NKSPAIKYRPENTPE CCCCCCCCCCCCCCC	25.86	21945579
21	Phosphorylation	IKYRPENTPEPVSTS CCCCCCCCCCCCCCC	27.63	21945579
26	Phosphorylation	ENTPEPVSTSVSHYG CCCCCCCCCCCCCCC	26.19	21945579
27	Phosphorylation	NTPEPVSTSVSHYGA CCCCCCCCCCCCCCC	33.12	21945579
28	Phosphorylation	TPEPVSTSVSHYGAE CCCCCCCCCCCCCCC	17.70	21945579
30	Phosphorylation	EPVSTSVSHYGAEPT CCCCCCCCCCCCCCC	15.68	21945579
32	Phosphorylation	VSTSVSHYGAEPTTV CCCCCCCCCCCCCEE	15.55	21945579
37	Phosphorylation	SHYGAEPTTVSPCPS CCCCCCCCEEECCCC	31.19	21945579
38	Phosphorylation	HYGAEPTTVSPCPSS CCCCCCCEEECCCCC	29.69	21945579
40	Phosphorylation	GAEPTTVSPCPSSSA CCCCCEEECCCCCCC	20.77	21945579
42	S-palmitoylation	EPTTVSPCPSSSAKG CCCEEECCCCCCCCC	3.88	19801377
44	Phosphorylation	TTVSPCPSSSAKGTA CEEECCCCCCCCCCE	43.58	21945579
45	Phosphorylation	TVSPCPSSSAKGTAV EEECCCCCCCCCCEE	21.32	21945579
46	Phosphorylation	VSPCPSSSAKGTAVN EECCCCCCCCCCEEE	38.03	21945579
100	Phosphorylation	VTIFVALYDYEARTT EEEEEEEEECCCCCC	13.52	25884760
107	Phosphorylation	YDYEARTTEDLSFKK EECCCCCCCCCCCCC	23.19	28060719
111	Phosphorylation	ARTTEDLSFKKGERF CCCCCCCCCCCCCCE	47.55	21082442
138	Ubiquitination	ARSIATGKNGYIPSN EEECCCCCCCEECCC	42.73	-
141	Phosphorylation	IATGKNGYIPSNYVA CCCCCCCEECCCCCC	21.03	19060867
144	Phosphorylation	GKNGYIPSNYVAPAD CCCCEECCCCCCCCH	31.10	-
146	Phosphorylation	NGYIPSNYVAPADSI CCEECCCCCCCCHHC	11.43	20736484
152	Phosphorylation	NYVAPADSIQAEEWY CCCCCCHHCCCHHHH	20.78	28442448
159	Phosphorylation	SIQAEEWYFGKMGRK HCCCHHHHCCCCCHH	13.01	28442448
187	Phosphorylation	GIFLVRESETTKGAY EEEEEEECCCCCCEE	29.67	28152594
189	Phosphorylation	FLVRESETTKGAYSL EEEEECCCCCCEEEE	42.99	28152594
190	Phosphorylation	LVRESETTKGAYSLS EEEECCCCCCEEEEE	24.35	28152594
191	Ubiquitination	VRESETTKGAYSLSI EEECCCCCCEEEEEE	49.30	23000965
194	Phosphorylation	SETTKGAYSLSIRDW CCCCCCEEEEEEECH	20.86	30266825
195	Phosphorylation	ETTKGAYSLSIRDWD CCCCCEEEEEEECHH	18.33	30266825
197	Phosphorylation	TKGAYSLSIRDWDEI CCCEEEEEEECHHHH	15.05	28152594
222	Phosphorylation	RKLDNGGYYITTRAQ EECCCCCEEEEEHHH	7.97	21945579
223	Phosphorylation	KLDNGGYYITTRAQF ECCCCCEEEEEHHHH	8.61	21945579
225	Phosphorylation	DNGGYYITTRAQFDT CCCCEEEEEHHHHHH	8.29	21945579
226	Phosphorylation	NGGYYITTRAQFDTL CCCEEEEEHHHHHHH	17.91	21945579
232	Phosphorylation	TTRAQFDTLQKLVKH EEHHHHHHHHHHHHH	32.17	29978859
235	Ubiquitination	AQFDTLQKLVKHYTE HHHHHHHHHHHHHHH	59.36	23000965
235	Acetylation	AQFDTLQKLVKHYTE HHHHHHHHHHHHHHH	59.36	26051181
238	Ubiquitination	DTLQKLVKHYTEHAD HHHHHHHHHHHHHCC	41.13	23000965
250	Acetylation	HADGLCHKLTTVCPT HCCCHHHHCHHCCCC	46.67	26051181
250	Ubiquitination	HADGLCHKLTTVCPT HCCCHHHHCHHCCCC	46.67	29967540
259	Ubiquitination	TTVCPTVKPQTQGLA HHCCCCCCCCCCCCC	33.61	33845483
259	Acetylation	TTVCPTVKPQTQGLA HHCCCCCCCCCCCCC	33.61	26051181
262	Phosphorylation	CPTVKPQTQGLAKDA CCCCCCCCCCCCCCH	32.88	20860994
267	Ubiquitination	PQTQGLAKDAWEIPR CCCCCCCCCHHHCCH	53.69	33845483
276	Phosphorylation	AWEIPRESLRLEVKL HHHCCHHHHHEEEEE	21.77	30266825
301	Ubiquitination	GTWNGTTKVAIKTLK EECCCCEEEEEEECC	29.52	32015554
325	Ubiquitination	LQEAQIMKKLRHDKL HHHHHHHHHHCCCCC	50.73	29967540
336	Phosphorylation	HDKLVPLYAVVSEEP CCCCEEEEEEECCCC	7.41	26356563
345	Phosphorylation	VVSEEPIYIVTEFMS EECCCCEEEEEEECC	10.47	24927040
355	Phosphorylation	TEFMSKGSLLDFLKE EEECCCCCHHHHHHH	29.51	27251275
361	Ubiquitination	GSLLDFLKEGDGKYL CCHHHHHHHCCCCEE	60.69	32015554
361	2-Hydroxyisobutyrylation	GSLLDFLKEGDGKYL CCHHHHHHHCCCCEE	60.69	-
367	Phosphorylation	LKEGDGKYLKLPQLV HHHCCCCEECHHHHH	18.01	27067055
386	Phosphorylation	QIADGMAYIERMNYI HHHHHHHHHHHHHHH	8.40	27067055
411	Ubiquitination	VGENLVCKIADFGLA ECCCEEEEEHHHHHH	33.19	30230243
426	Phosphorylation	RLIEDNEYTARQGAK HHHCCCCCCCCCCCC	16.38	19664994
427	Phosphorylation	LIEDNEYTARQGAKF HHCCCCCCCCCCCCC	14.80	29255136
433	Ubiquitination	YTARQGAKFPIKWTA CCCCCCCCCCCEECC	59.50	22817900
437	Ubiquitination	QGAKFPIKWTAPEAA CCCCCCCEECCCCHH	38.44	21890473
446	Phosphorylation	TAPEAALYGRFTIKS CCCCHHHHCCEEECC	11.09	27273156
468	Ubiquitination	LQTELVTKGRVPYPG EEEEEECCCCCCCCC	36.92	-
489	Phosphorylation	LEQVERGYRMPCPQG HHHHHHHCCCCCCCC	15.23	-
510	Ubiquitination	ELMNLCWKKDPDERP HHHHHHCCCCCCCCC	46.42	32015554
531	Phosphorylation	SFLEDYFTATEPQYQ HHHHHHHCCCCCCCC	26.83	26356563
533	Phosphorylation	LEDYFTATEPQYQPG HHHHHCCCCCCCCCC	45.18	26356563
537	Phosphorylation	FTATEPQYQPGENL- HCCCCCCCCCCCCC-	27.65	27273156

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
426	Y	Phosphorylation	Kinase	AXL	P30530	PSP
426	Y	Phosphorylation	Kinase	YES1	P07947	GPS
537	Y	Phosphorylation	Kinase	CSK	P41240	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:21596750

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CTND1_HUMAN	CTNND1	physical	12640114
FYN_HUMAN	FYN	physical	12640114
OCLN_HUMAN	OCLN	physical	11950934
PECA1_HUMAN	PECAM1	physical	10858437
RL10_HUMAN	RPL10	physical	12138090
KHDR1_HUMAN	KHDRBS1	physical	22745667
PDC6I_HUMAN	PDCD6IP	physical	15557335
CBL_HUMAN	CBL	physical	10829062
KHDR1_HUMAN	KHDRBS1	physical	15190072
SPR2A_HUMAN	SPRR2A	physical	18155796
SOCS3_HUMAN	SOCS3	physical	25416956
FXR2_HUMAN	FXR2	physical	25416956
SSBP3_HUMAN	SSBP3	physical	25416956
THAP1_HUMAN	THAP1	physical	25416956
NIF3L_HUMAN	NIF3L1	physical	25416956
CA094_HUMAN	C1orf94	physical	25416956
FUND1_HUMAN	FUNDC1	physical	25416956
ZBT8A_HUMAN	ZBTB8A	physical	25416956
BECN1_HUMAN	BECN1	physical	25814554
OLIG1_HUMAN	OLIG1	physical	25814554
FGFR1_HUMAN	FGFR1	physical	16631103
SRC8_HUMAN	CTTN	physical	16631103
FGR_HUMAN	FGR	physical	28514442
CC186_HUMAN	CCDC186	physical	28514442
PAI2_HUMAN	SERPINB2	physical	28514442
CDC37_HUMAN	CDC37	physical	28514442
AIP_HUMAN	AIP	physical	28514442

Drug and Disease Associations

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

Regulatory Network of YES_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; TYR-194; TYR-222;TYR-336; TYR-345; TYR-426; TYR-446 AND TYR-537, AND MASS SPECTROMETRY.	19369195 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21; SER-40; TYR-194 ANDTYR-426, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-40; SER-111;SER-195; TYR-426 AND TYR-537, AND MASS SPECTROMETRY.	18691976 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-222; TYR-223; TYR-426AND TYR-446, AND MASS SPECTROMETRY.	19534553 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-426, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-426, AND MASSSPECTROMETRY.	17192257 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-32; TYR-222; TYR-223;TYR-426; TYR-446 AND TYR-537, AND MASS SPECTROMETRY.	18083107 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-426, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-426, AND MASSSPECTROMETRY.	16094384 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-537, AND MASSSPECTROMETRY.	15592455 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-426, AND MASSSPECTROMETRY.	15951569 [Abstract]

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