YAP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: YAP1_HUMAN
• UniProt AC: P46937
• Protein Name: Transcriptional coactivator YAP1
• Gene Name: YAP1
• Organism: Homo sapiens (Human).
• Sequence Length: 504
• Subcellular Localization: Cytoplasm . Nucleus . Both phosphorylation and cell density can regulate its subcellular localization. Phosphorylation sequesters it in the cytoplasm by inhibiting its translocation into the nucleus. At low density, predominantly nuclear and is trans
• Protein Description: Transcriptional regulator which can act both as a coactivator and a corepressor and is the critical downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. [PubMed: 17974916]
• Protein Sequence: MDPGQQPPPQPAPQGQGQPPSQPPQGQGPPSGPGQPAPAATQAAPQAPPAGHQIVHVRGDSETDLEALFNAVMNPKTANVPQTVPMRLRKLPDSFFKPPEPKSHSRQASTDAGTAGALTPQHVRAHSSPASLQLGAVSPGTLTPTGVVSGPAATPTAQHLRQSSFEIPDDVPLPAGWEMAKTSSGQRYFLNHIDQTTTWQDPRKAMLSQMNVTAPTSPPVQQNMMNSASGPLPDGWEQAMTQDGEIYYINHKNKTTSWLDPRLDPRFAMNQRISQSAPVKQPPPLAPQSPQGGVMGGSNSNQQQQMRLQQLQMEKERLRLKQQELLRQAMRNINPSTANSPKCQELALRSQLPTLEQDGGTQNPVSSPGMSQELRTMTTNSSDPFLNSGTYHSRDESTDSGLSMSSYSVPRTPDDFLNSVDEMDTGDTINQSTLPSQQNRFPDYLEAIPGTNVDLGTLEGDGMNIEGEELMPSLQEALSSDILNDMESVLAATKLDKESFLTWL

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5 (in isoform 4)	Phosphorylation	-	58.98	27135362
6 (in isoform 4)	Phosphorylation	-	59.38	27135362
41	Phosphorylation	GQPAPAATQAAPQAP CCCCCHHHHCCCCCC	22.35	-
61	Phosphorylation	IVHVRGDSETDLEAL EEEECCCCHHHHHHH	45.26	29255136
61 (in isoform 5)	Phosphorylation	-	45.26	24719451
63	Phosphorylation	HVRGDSETDLEALFN EECCCCHHHHHHHHH	50.24	29255136
77	Phosphorylation	NAVMNPKTANVPQTV HHHHCCCCCCCCCCC	25.40	-
83	Phosphorylation	KTANVPQTVPMRLRK CCCCCCCCCCCHHHC	22.10	23312004
83	O-linked_Glycosylation	KTANVPQTVPMRLRK CCCCCCCCCCCHHHC	22.10	30620550
90	Ubiquitination	TVPMRLRKLPDSFFK CCCCHHHCCCHHHCC	69.80	-
90	Acetylation	TVPMRLRKLPDSFFK CCCCHHHCCCHHHCC	69.80	-
90	Acetylation	TVPMRLRKLPDSFFK CCCCHHHCCCHHHCC	69.80	22424773
94	Phosphorylation	RLRKLPDSFFKPPEP HHHCCCHHHCCCCCC	30.55	19141641
97	Acetylation	KLPDSFFKPPEPKSH CCCHHHCCCCCCCCC	58.62	23954790
97	Sumoylation	KLPDSFFKPPEPKSH CCCHHHCCCCCCCCC	58.62	-
97	Sumoylation	KLPDSFFKPPEPKSH CCCHHHCCCCCCCCC	58.62	-
97	Ubiquitination	KLPDSFFKPPEPKSH CCCHHHCCCCCCCCC	58.62	-
97	Acetylation	KLPDSFFKPPEPKSH CCCHHHCCCCCCCCC	58.62	-
102	Ubiquitination	FFKPPEPKSHSRQAS HCCCCCCCCCCCCCC	60.17	-
103	Phosphorylation	FKPPEPKSHSRQAST CCCCCCCCCCCCCCC	37.09	27273156
105	Phosphorylation	PPEPKSHSRQASTDA CCCCCCCCCCCCCCC	32.93	26503892
109	Phosphorylation	KSHSRQASTDAGTAG CCCCCCCCCCCCCCC	20.62	29255136
109 (in isoform 5)	Phosphorylation	-	20.62	24719451
110	Phosphorylation	SHSRQASTDAGTAGA CCCCCCCCCCCCCCC	32.65	22167270
110 (in isoform 5)	Phosphorylation	-	32.65	24719451
114	Phosphorylation	QASTDAGTAGALTPQ CCCCCCCCCCCCCHH	24.52	29255136
119	Phosphorylation	AGTAGALTPQHVRAH CCCCCCCCHHHHHCC	21.99	29255136
119 (in isoform 5)	Phosphorylation	-	21.99	24719451
127	Phosphorylation	PQHVRAHSSPASLQL HHHHHCCCCCCEEEC	36.71	29255136
128	Phosphorylation	QHVRAHSSPASLQLG HHHHCCCCCCEEECC	18.02	29255136
128 (in isoform 5)	Phosphorylation	-	18.02	24719451
131	Phosphorylation	RAHSSPASLQLGAVS HCCCCCCEEECCCCC	21.74	29255136
131 (in isoform 5)	Phosphorylation	-	21.74	24719451
138	Phosphorylation	SLQLGAVSPGTLTPT EEECCCCCCCEECCC	19.65	29255136
138 (in isoform 5)	Phosphorylation	-	19.65	24719451
141	Phosphorylation	LGAVSPGTLTPTGVV CCCCCCCEECCCCCE	30.73	29255136
141 (in isoform 5)	Phosphorylation	-	30.73	24719451
143	Phosphorylation	AVSPGTLTPTGVVSG CCCCCEECCCCCEEC	20.74	29255136
143 (in isoform 5)	Phosphorylation	-	20.74	24719451
145	Phosphorylation	SPGTLTPTGVVSGPA CCCEECCCCCEECCC	37.06	29255136
149	Phosphorylation	LTPTGVVSGPAATPT ECCCCCEECCCCCCC	36.33	29255136
154	Phosphorylation	VVSGPAATPTAQHLR CEECCCCCCCHHHHH	24.23	30278072
156	Phosphorylation	SGPAATPTAQHLRQS ECCCCCCCHHHHHHH	34.30	23927012
163	Phosphorylation	TAQHLRQSSFEIPDD CHHHHHHHCCCCCCC	30.47	27273156
164	Phosphorylation	AQHLRQSSFEIPDDV HHHHHHHCCCCCCCC	20.68	22167270
181	Ubiquitination	PAGWEMAKTSSGQRY CCCCEEEECCCCCEE	47.86	-
182	Phosphorylation	AGWEMAKTSSGQRYF CCCEEEECCCCCEEE	20.70	25072903
183	Phosphorylation	GWEMAKTSSGQRYFL CCEEEECCCCCEEEE	31.59	25072903
184	Phosphorylation	WEMAKTSSGQRYFLN CEEEECCCCCEEEEE	44.15	25072903
188	Phosphorylation	KTSSGQRYFLNHIDQ ECCCCCEEEEECCCC	12.44	25072903
188 (in isoform 3)	Phosphorylation	-	12.44	22210691
188 (in isoform 5)	Phosphorylation	-	12.44	22210691
188 (in isoform 6)	Phosphorylation	-	12.44	22210691
188 (in isoform 7)	Phosphorylation	-	12.44	22210691
208 (in isoform 3)	Phosphorylation	-	17.82	23532336
208 (in isoform 5)	Phosphorylation	-	17.82	23532336
208 (in isoform 6)	Phosphorylation	-	17.82	23532336
208 (in isoform 7)	Phosphorylation	-	17.82	23532336
213	Phosphorylation	MLSQMNVTAPTSPPV HHHHCCCCCCCCCHH	23.16	22210691
213 (in isoform 3)	Phosphorylation	-	23.16	29514088
213 (in isoform 5)	Phosphorylation	-	23.16	29514088
213 (in isoform 6)	Phosphorylation	-	23.16	29514088
213 (in isoform 7)	Phosphorylation	-	23.16	29514088
216 (in isoform 5)	Phosphorylation	-	51.94	22199227
216	Phosphorylation	QMNVTAPTSPPVQQN HCCCCCCCCCHHHHH	51.94	22210691
216 (in isoform 3)	Phosphorylation	-	51.94	22199227
216 (in isoform 6)	Phosphorylation	-	51.94	22199227
216 (in isoform 7)	Phosphorylation	-	51.94	22199227
217	Phosphorylation	MNVTAPTSPPVQQNM CCCCCCCCCHHHHHH	26.58	20068231
217 (in isoform 5)	Phosphorylation	-	26.58	29116813
217 (in isoform 3)	Phosphorylation	-	26.58	22199227
217 (in isoform 6)	Phosphorylation	-	26.58	22199227
217 (in isoform 7)	Phosphorylation	-	26.58	22199227
227	Phosphorylation	VQQNMMNSASGPLPD HHHHHHHCCCCCCCC	13.10	22210691
227 (in isoform 3)	Phosphorylation	-	13.10	20068231
227 (in isoform 5)	Phosphorylation	-	13.10	20068231
227 (in isoform 6)	Phosphorylation	-	13.10	20068231
227 (in isoform 7)	Phosphorylation	-	13.10	20068231
229	Phosphorylation	QNMMNSASGPLPDGW HHHHHCCCCCCCCCH	40.54	22210691
229 (in isoform 3)	Phosphorylation	-	40.54	23532336
229 (in isoform 5)	Phosphorylation	-	40.54	23532336
229 (in isoform 6)	Phosphorylation	-	40.54	23532336
229 (in isoform 7)	Phosphorylation	-	40.54	23532336
236 (in isoform 3)	Phosphorylation	-	11.25	20068231
236 (in isoform 5)	Phosphorylation	-	11.25	20068231
236 (in isoform 6)	Phosphorylation	-	11.25	20068231
236 (in isoform 7)	Phosphorylation	-	11.25	20068231
236	Phosphorylation	SGPLPDGWEQAMTQD CCCCCCCHHHHCCCC	11.25	18669648
238 (in isoform 3)	Phosphorylation	-	29.89	29743597
238 (in isoform 5)	Phosphorylation	-	29.89	29743597
238 (in isoform 6)	Phosphorylation	-	29.89	29743597
238 (in isoform 7)	Phosphorylation	-	29.89	29743597
238	Phosphorylation	PLPDGWEQAMTQDGE CCCCCHHHHCCCCCE	29.89	16964243
241	O-linked_Glycosylation	DGWEQAMTQDGEIYY CCHHHHCCCCCEEEE	26.90	31373491
251 (in isoform 5)	Phosphorylation	-	26.05	24719451
251	Phosphorylation	GEIYYINHKNKTTSW CEEEEEECCCCCCCC	26.05	18669648
254	Ubiquitination	YYINHKNKTTSWLDP EEEECCCCCCCCCCC	58.96	-
257	Phosphorylation	NHKNKTTSWLDPRLD ECCCCCCCCCCCCCC	30.76	28857561
260	Phosphorylation	NKTTSWLDPRLDPRF CCCCCCCCCCCCHHH	21.73	18669648
274	Phosphorylation	FAMNQRISQSAPVKQ HHHCCCCCCCCCCCC	21.92	30266825
276	Phosphorylation	MNQRISQSAPVKQPP HCCCCCCCCCCCCCC	27.96	30266825
277	Acetylation	NQRISQSAPVKQPPP CCCCCCCCCCCCCCC	12.79	-
280	Sumoylation	ISQSAPVKQPPPLAP CCCCCCCCCCCCCCC	56.90	-
280	Sumoylation	ISQSAPVKQPPPLAP CCCCCCCCCCCCCCC	56.90	-
280	Ubiquitination	ISQSAPVKQPPPLAP CCCCCCCCCCCCCCC	56.90	-
280	Acetylation	ISQSAPVKQPPPLAP CCCCCCCCCCCCCCC	56.90	26051181
289	Phosphorylation	PPPLAPQSPQGGVMG CCCCCCCCCCCCCCC	20.38	29255136
298	Phosphorylation	QGGVMGGSNSNQQQQ CCCCCCCCCHHHHHH	31.21	29255136
300	Phosphorylation	GVMGGSNSNQQQQMR CCCCCCCHHHHHHHH	37.40	30243723
307 (in isoform 5)	Phosphorylation	-	25.63	24719451
313 (in isoform 5)	Phosphorylation	-	12.35	24719451
315	Ubiquitination	LQQLQMEKERLRLKQ HHHHHHHHHHHHHHH	42.67	-
315	Acetylation	LQQLQMEKERLRLKQ HHHHHHHHHHHHHHH	42.67	26051181
315	Malonylation	LQQLQMEKERLRLKQ HHHHHHHHHHHHHHH	42.67	26320211
317 (in isoform 5)	Phosphorylation	-	35.85	24719451
317	Phosphorylation	QLQMEKERLRLKQQE HHHHHHHHHHHHHHH	35.85	18669648
321	Ubiquitination	EKERLRLKQQELLRQ HHHHHHHHHHHHHHH	43.43	-
321	Phosphorylation	EKERLRLKQQELLRQ HHHHHHHHHHHHHHH	43.43	17525332
331	Phosphorylation	ELLRQAMRNINPSTA HHHHHHHHCCCHHHC	43.84	18669648
336	Phosphorylation	AMRNINPSTANSPKC HHHCCCHHHCCCHHH	35.35	27461979
336	O-linked_Glycosylation	AMRNINPSTANSPKC HHHCCCHHHCCCHHH	35.35	30620550
337	Phosphorylation	MRNINPSTANSPKCQ HHCCCHHHCCCHHHH	30.99	29255136
340	Phosphorylation	INPSTANSPKCQELA CCHHHCCCHHHHHHH	24.23	29255136
342	Ubiquitination	PSTANSPKCQELALR HHHCCCHHHHHHHHH	48.66	-
343 (in isoform 5)	Phosphorylation	-	4.28	24719451
346 (in isoform 5)	Phosphorylation	-	1.93	24719451
347	Phosphorylation	SPKCQELALRSQLPT CHHHHHHHHHHCCCC	10.52	18669648
348	Phosphorylation	PKCQELALRSQLPTL HHHHHHHHHHCCCCE	9.40	15302935
350	Phosphorylation	CQELALRSQLPTLEQ HHHHHHHHCCCCEEC	36.60	23403867
353	Phosphorylation	LALRSQLPTLEQDGG HHHHHCCCCEECCCC	27.57	18669648
354	Phosphorylation	ALRSQLPTLEQDGGT HHHHCCCCEECCCCC	52.07	29255136
361	Phosphorylation	TLEQDGGTQNPVSSP CEECCCCCCCCCCCC	30.60	23403867
365 (in isoform 5)	Phosphorylation	-	13.35	24719451
366	Phosphorylation	GGTQNPVSSPGMSQE CCCCCCCCCCCCCHH	31.88	30266825
366	O-linked_Glycosylation	GGTQNPVSSPGMSQE CCCCCCCCCCCCCHH	31.88	30620550
367	Phosphorylation	GTQNPVSSPGMSQEL CCCCCCCCCCCCHHH	26.21	29255136
370	Sulfoxidation	NPVSSPGMSQELRTM CCCCCCCCCHHHHHH	4.19	30846556
371	Phosphorylation	PVSSPGMSQELRTMT CCCCCCCCHHHHHHC	26.81	17525332
376	O-linked_Glycosylation	GMSQELRTMTTNSSD CCCHHHHHHCCCCCC	31.34	30620550
376	Phosphorylation	GMSQELRTMTTNSSD CCCHHHHHHCCCCCC	31.34	28857561
378	Phosphorylation	SQELRTMTTNSSDPF CHHHHHHCCCCCCCC	23.39	29496963
379	Phosphorylation	QELRTMTTNSSDPFL HHHHHHCCCCCCCCC	23.45	29496963
381	Phosphorylation	LRTMTTNSSDPFLNS HHHHCCCCCCCCCCC	33.74	23911959
382	Phosphorylation	RTMTTNSSDPFLNSG HHHCCCCCCCCCCCC	51.91	22617229
388	Phosphorylation	SSDPFLNSGTYHSRD CCCCCCCCCCCCCCC	34.36	24702127
390	Phosphorylation	DPFLNSGTYHSRDES CCCCCCCCCCCCCCC	20.20	24043423
391	Phosphorylation	PFLNSGTYHSRDEST CCCCCCCCCCCCCCC	11.00	23312004
393	Phosphorylation	LNSGTYHSRDESTDS CCCCCCCCCCCCCCC	30.89	24043423
397	Phosphorylation	TYHSRDESTDSGLSM CCCCCCCCCCCCCCC	41.63	21945579
398	Phosphorylation	YHSRDESTDSGLSMS CCCCCCCCCCCCCCC	31.94	21945579
400	Phosphorylation	SRDESTDSGLSMSSY CCCCCCCCCCCCCCC	41.54	21945579
403	Phosphorylation	ESTDSGLSMSSYSVP CCCCCCCCCCCCCCC	21.83	21945579
404	Sulfoxidation	STDSGLSMSSYSVPR CCCCCCCCCCCCCCC	3.57	30846556
405	Phosphorylation	TDSGLSMSSYSVPRT CCCCCCCCCCCCCCC	23.81	21945579
406	Phosphorylation	DSGLSMSSYSVPRTP CCCCCCCCCCCCCCH	16.88	21945579
407	Phosphorylation	SGLSMSSYSVPRTPD CCCCCCCCCCCCCHH	13.33	21945579
408	Phosphorylation	GLSMSSYSVPRTPDD CCCCCCCCCCCCHHH	27.82	21945579
412	Phosphorylation	SSYSVPRTPDDFLNS CCCCCCCCHHHHHHC	25.62	30266825
419	Phosphorylation	TPDDFLNSVDEMDTG CHHHHHHCCCCCCCC	32.85	25159151
423	Sulfoxidation	FLNSVDEMDTGDTIN HHHCCCCCCCCCCCC	4.90	30846556
425	Phosphorylation	NSVDEMDTGDTINQS HCCCCCCCCCCCCHH	35.33	25841592
428	Phosphorylation	DEMDTGDTINQSTLP CCCCCCCCCCHHCCC	24.15	27251275
432	Phosphorylation	TGDTINQSTLPSQQN CCCCCCHHCCCCCCC	27.68	19141641
433	Phosphorylation	GDTINQSTLPSQQNR CCCCCHHCCCCCCCC	32.69	27251275
443	Ubiquitination	SQQNRFPDYLEAIPG CCCCCCCHHHHHCCC	58.92	-
444	Phosphorylation	QQNRFPDYLEAIPGT CCCCCCHHHHHCCCC	13.48	-
447	Ubiquitination	RFPDYLEAIPGTNVD CCCHHHHHCCCCCCC	15.64	21906983
485	Ubiquitination	LSSDILNDMESVLAA HCCCHHHHHHHHHHH	38.49	21906983
494	Methylation	ESVLAATKLDKESFL HHHHHHHCCCHHHHH	50.38	-
497	Methylation	LAATKLDKESFLTWL HHHHCCCHHHHHHCC	66.74	-
497	Ubiquitination	LAATKLDKESFLTWL HHHHCCCHHHHHHCC	66.74	2190698
499	Phosphorylation	ATKLDKESFLTWL-- HHCCCHHHHHHCC--	31.15	22199227

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
41	T	Phosphorylation	Kinase	MST4	Q9P289	PSP
61	S	Phosphorylation	Kinase	LATS2	Q9NRM7	Uniprot
61	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
61	S	Phosphorylation	Kinase	LATS1	O95835	Uniprot
61	S	Phosphorylation	Kinase	STK38	Q15208	GPS
77	T	Phosphorylation	Kinase	PLK1	P53350	PSP
77	T	Phosphorylation	Kinase	MST4	Q9P289	PSP
83	T	Phosphorylation	Kinase	MST4	Q9P289	PSP
94	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
94	S	Phosphorylation	Kinase	MST4	Q9P289	PSP
109	S	Phosphorylation	Kinase	PRKCZ	Q05513	GPS
109	S	Phosphorylation	Kinase	STK38	Q15208	GPS
109	S	Phosphorylation	Kinase	LATS1	O95835	Uniprot
109	S	Phosphorylation	Kinase	LATS2	Q9NRM7	Uniprot
110	T	Phosphorylation	Kinase	MST4	Q9P289	PSP
110	T	Phosphorylation	Kinase	PRKCZ	Q05513	GPS
119	T	Phosphorylation	Kinase	CDK1	P06493	PSP
119	T	Phosphorylation	Kinase	JNK2	P45984	PSP
119	T	Phosphorylation	Kinase	MAPK9	P45984	Uniprot
119	T	Phosphorylation	Kinase	MAPK8	P45983	Uniprot
127	S	Phosphorylation	Kinase	STK3	Q13188	GPS
127	S	Phosphorylation	Kinase	STK38	Q15208	GPS
127	S	Phosphorylation	Kinase	STK38L	Q9Y2H1	GPS
127	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
127	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
127	S	Phosphorylation	Kinase	LATS1	O95835	Uniprot
127	S	Phosphorylation	Kinase	AKT1	P31749	PSP
127	S	Phosphorylation	Kinase	LATS2	Q9NRM7	Uniprot
128	S	Phosphorylation	Kinase	NLK	Q9UBE8	PSP
128	S	Phosphorylation	Kinase	CDK1	P06493	PSP
138	S	Phosphorylation	Kinase	MAPK8	P45983	Uniprot
138	S	Phosphorylation	Kinase	CDK1	P06493	PSP
138	S	Phosphorylation	Kinase	JNK2	P45984	PSP
138	S	Phosphorylation	Kinase	MAPK9	P45984	Uniprot
143	T	Phosphorylation	Kinase	CDK1	P06493	PSP
154	T	Phosphorylation	Kinase	MAPK9	P45984	Uniprot
154	T	Phosphorylation	Kinase	JNK2	P45984	PSP
154	T	Phosphorylation	Kinase	JNK1	P45983	PSP
154	T	Phosphorylation	Kinase	MAPK8	P45983	Uniprot
164	S	Phosphorylation	Kinase	LATS2	Q9NRM7	Uniprot
164	S	Phosphorylation	Kinase	STK38	Q15208	GPS
164	S	Phosphorylation	Kinase	LATS1	O95835	Uniprot
217	S	Phosphorylation	Kinase	CDK1	P06493	PSP
289	S	Phosphorylation	Kinase	CDK1	P06493	PSP
317	S	Phosphorylation	Kinase	JNK1	P45983	PSP
317	S	Phosphorylation	Kinase	JNK2	P45984	PSP
341	Y	Phosphorylation	Kinase	SRC	P12931	PSP
357	Y	Phosphorylation	Kinase	SRC	P12931	PSP
362	T	Phosphorylation	Kinase	JNK1	P45983	PSP
362	T	Phosphorylation	Kinase	JNK2	P45984	PSP
367	S	Phosphorylation	Kinase	MAPK8	P45983	Uniprot
367	S	Phosphorylation	Kinase	CDK1	P06493	PSP
367	S	Phosphorylation	Kinase	MAPK9	P45984	Uniprot
394	Y	Phosphorylation	Kinase	SRC	P12931	PSP
397	S	Phosphorylation	Kinase	LATS1	O95835	Uniprot
397	S	Phosphorylation	Kinase	AURKA	O14965	GPS
397	S	Phosphorylation	Kinase	LATS2	Q9NRM7	Uniprot
400	S	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
400	S	Phosphorylation	Kinase	CK1	-	Uniprot
403	S	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
403	S	Phosphorylation	Kinase	CK1	-	Uniprot
407	Y	Phosphorylation	Kinase	ABL	P00519	PSP
412	T	Phosphorylation	Kinase	MAPK9	P45984	Uniprot
412	T	Phosphorylation	Kinase	MAPK8	P45983	Uniprot
419	S	Phosphorylation	Kinase	IKBKE	Q14164	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW11	Q9UKB1	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	CNOT4	O95628	PMID:22707721
-	K	Ubiquitination	E3 ubiquitin ligase	SKP2	Q13309	PMID:29891922
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:23564455

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
119	T	Phosphorylation	Phosphorylated at Thr-119, Ser-138, Thr-154, Ser-367 and Thr-412 by MAPK8/JNK1 and MAPK9/JNK2, which is required for the regulation of apoptosis by YAP1.	21364637
138	S	Phosphorylation	Phosphorylated at Thr-119, Ser-138, Thr-154, Ser-367 and Thr-412 by MAPK8/JNK1 and MAPK9/JNK2, which is required for the regulation of apoptosis by YAP1.	21364637
154	T	Phosphorylation	Phosphorylated at Thr-119, Ser-138, Thr-154, Ser-367 and Thr-412 by MAPK8/JNK1 and MAPK9/JNK2, which is required for the regulation of apoptosis by YAP1.	21364637
367	S	Phosphorylation	Phosphorylated at Thr-119, Ser-138, Thr-154, Ser-367 and Thr-412 by MAPK8/JNK1 and MAPK9/JNK2, which is required for the regulation of apoptosis by YAP1.	21364637
397	S	Phosphorylation	Phosphorylation at Ser-400 and Ser-403 by CK1 is triggered by previous phosphorylation at Ser-397 by LATS proteins and leads to YAP1 ubiquitination by SCF(beta-TRCP) E3 ubiquitin ligase and subsequent degradation.	20048001
397	S	ubiquitylation	Phosphorylation at Ser-400 and Ser-403 by CK1 is triggered by previous phosphorylation at Ser-397 by LATS proteins and leads to YAP1 ubiquitination by SCF(beta-TRCP) E3 ubiquitin ligase and subsequent degradation.	20048001
400	S	Phosphorylation	Phosphorylation at Ser-400 and Ser-403 by CK1 is triggered by previous phosphorylation at Ser-397 by LATS proteins and leads to YAP1 ubiquitination by SCF(beta-TRCP) E3 ubiquitin ligase and subsequent degradation.	20048001
400	S	ubiquitylation	Phosphorylation at Ser-400 and Ser-403 by CK1 is triggered by previous phosphorylation at Ser-397 by LATS proteins and leads to YAP1 ubiquitination by SCF(beta-TRCP) E3 ubiquitin ligase and subsequent degradation.	20048001
403	S	Phosphorylation	Phosphorylation at Ser-400 and Ser-403 by CK1 is triggered by previous phosphorylation at Ser-397 by LATS proteins and leads to YAP1 ubiquitination by SCF(beta-TRCP) E3 ubiquitin ligase and subsequent degradation.	20048001
403	S	ubiquitylation	Phosphorylation at Ser-400 and Ser-403 by CK1 is triggered by previous phosphorylation at Ser-397 by LATS proteins and leads to YAP1 ubiquitination by SCF(beta-TRCP) E3 ubiquitin ligase and subsequent degradation.	20048001
412	T	Phosphorylation	Phosphorylated at Thr-119, Ser-138, Thr-154, Ser-367 and Thr-412 by MAPK8/JNK1 and MAPK9/JNK2, which is required for the regulation of apoptosis by YAP1.	21364637

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of YAP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ASPP2_HUMAN	TP53BP2	physical	11278422
KIF5A_HUMAN	KIF5A	physical	11278422
RUNX3_HUMAN	RUNX3	physical	10228168
RUNX2_HUMAN	RUNX2	physical	10228168
RUNX1_HUMAN	RUNX1	physical	10228168
WBP1_HUMAN	WBP1	physical	11604498
WBP1_MOUSE	Wbp1	physical	7644498
WBP2_MOUSE	Wbp2	physical	7644498
SMAD7_HUMAN	SMAD7	genetic	12118366
SMAD7_HUMAN	SMAD7	physical	12118366
SMAD6_HUMAN	SMAD6	physical	12118366
ITCH_HUMAN	ITCH	physical	17110958
P73_HUMAN	TP73	physical	17110958
P73_HUMAN	TP73	physical	15893728
EP300_HUMAN	EP300	physical	15893728
FBW1A_HUMAN	BTRC	physical	20048001
SMAD1_HUMAN	SMAD1	physical	19914168
SMAD5_HUMAN	SMAD5	physical	19914168
EGFR_HUMAN	EGFR	physical	12807903
LATS1_HUMAN	LATS1	physical	18413746
LATS2_HUMAN	LATS2	physical	18413746
LATS1_HUMAN	LATS1	physical	21041411
LATS2_HUMAN	LATS2	physical	21041411
SMAD1_HUMAN	SMAD1	physical	21685363
RUNX1_HUMAN	RUNX1	physical	18701449
PML_HUMAN	PML	physical	19111660
P73_HUMAN	TP73	physical	19111660
SUMO1_HUMAN	SUMO1	physical	19111660
PTN14_HUMAN	PTPN14	physical	22948661
ERBB4_HUMAN	ERBB4	physical	19047365
LATS2_HUMAN	LATS2	physical	18565851
LATS1_HUMAN	LATS1	physical	18158288
LATS1_HUMAN	LATS1	physical	17889669
LATS1_HUMAN	LATS1	physical	18640976
P73_HUMAN	TP73	physical	18640976
ANCHR_HUMAN	ZFYVE19	physical	22939629
ZPR1_HUMAN	ZPR1	physical	22939629
TEAD1_HUMAN	TEAD1	physical	22863277
1433T_HUMAN	YWHAQ	physical	22863277
CREB1_HUMAN	CREB1	physical	23532963
AMOT_HUMAN	AMOT	physical	23564455
AMOT_HUMAN	AMOT	physical	24255178
AMOL1_HUMAN	AMOTL1	physical	24255178
AMOL2_HUMAN	AMOTL2	physical	24255178
ARI1A_HUMAN	ARID1A	physical	24255178
ARI1B_HUMAN	ARID1B	physical	24255178
ATIF1_HUMAN	ATPIF1	physical	24255178
BCL9L_HUMAN	BCL9L	physical	24255178
CC85C_HUMAN	CCDC85C	physical	24255178
REQU_HUMAN	DPF2	physical	24255178
INADL_HUMAN	INADL	physical	24255178
LATS1_HUMAN	LATS1	physical	24255178
LIN7C_HUMAN	LIN7C	physical	24255178
MPDZ_HUMAN	MPDZ	physical	24255178
MPP5_HUMAN	MPP5	physical	24255178
MERL_HUMAN	NF2	physical	24255178
PARD3_HUMAN	PARD3	physical	24255178
PDLI7_HUMAN	PDLIM7	physical	24255178
PP1A_HUMAN	PPP1CA	physical	24255178
PTN14_HUMAN	PTPN14	physical	24255178
RAE1L_HUMAN	RAE1	physical	24255178
RPGF2_HUMAN	RAPGEF2	physical	24255178
RASF8_HUMAN	RASSF8	physical	24255178
NHRF2_HUMAN	SLC9A3R2	physical	24255178
SMRD1_HUMAN	SMARCD1	physical	24255178
TEAD1_HUMAN	TEAD1	physical	24255178
TEAD3_HUMAN	TEAD3	physical	24255178
ZO2_HUMAN	TJP2	physical	24255178
ASPP2_HUMAN	TP53BP2	physical	24255178
WBP2_HUMAN	WBP2	physical	24255178
1433B_HUMAN	YWHAB	physical	24255178
1433E_HUMAN	YWHAE	physical	24255178
1433G_HUMAN	YWHAG	physical	24255178
1433F_HUMAN	YWHAH	physical	24255178
1433T_HUMAN	YWHAQ	physical	24255178
1433Z_HUMAN	YWHAZ	physical	24255178
AMOT_HUMAN	AMOT	physical	24101513
MP2K1_HUMAN	MAP2K1	physical	24211253
ARFP1_HUMAN	ARFIP1	physical	22863883
PAPOA_HUMAN	PAPOLA	physical	22863883
ANM3_HUMAN	PRMT3	physical	22863883
RTF1_HUMAN	RTF1	physical	22863883
STAT1_HUMAN	STAT1	physical	22863883
TSNAX_HUMAN	TSNAX	physical	22863883
FBXW7_HUMAN	FBXW7	physical	24884509
ABL1_HUMAN	ABL1	physical	18280240
P73_HUMAN	TP73	physical	18280240
1433B_HUMAN	YWHAB	physical	24366813
1433E_HUMAN	YWHAE	physical	24366813
1433F_HUMAN	YWHAH	physical	24366813
1433G_HUMAN	YWHAG	physical	24366813
1433T_HUMAN	YWHAQ	physical	24366813
AMOL1_HUMAN	AMOTL1	physical	24366813
AMOL2_HUMAN	AMOTL2	physical	24366813
AMOT_HUMAN	AMOT	physical	24366813
ASPP2_HUMAN	TP53BP2	physical	24366813
CHIP_HUMAN	STUB1	physical	24366813
CPVL_HUMAN	CPVL	physical	24366813
ERP44_HUMAN	ERP44	physical	24366813
FAS_HUMAN	FASN	physical	24366813
HS105_HUMAN	HSPH1	physical	24366813
HS74L_HUMAN	HSPA4L	physical	24366813
HSP74_HUMAN	HSPA4	physical	24366813
HYOU1_HUMAN	HYOU1	physical	24366813
INADL_HUMAN	INADL	physical	24366813
LATS1_HUMAN	LATS1	physical	24366813
LIN7C_HUMAN	LIN7C	physical	24366813
MCMBP_HUMAN	MCMBP	physical	24366813
MERL_HUMAN	NF2	physical	24366813
MPDZ_HUMAN	MPDZ	physical	24366813
MPP5_HUMAN	MPP5	physical	24366813
PP1A_HUMAN	PPP1CA	physical	24366813
PTN14_HUMAN	PTPN14	physical	24366813
RPGF2_HUMAN	RAPGEF2	physical	24366813
RPGF6_HUMAN	RAPGEF6	physical	24366813
TEAD3_HUMAN	TEAD3	physical	24366813
WBP2_HUMAN	WBP2	physical	24366813
WBP1_HUMAN	WBP1	physical	25283809
SMAD7_HUMAN	SMAD7	physical	25283809
LATS1_HUMAN	LATS1	physical	25283809
RUNX1_HUMAN	RUNX1	physical	25283809
PTN14_HUMAN	PTPN14	physical	25283809
ERBB4_HUMAN	ERBB4	physical	25283809
P73_HUMAN	TP73	physical	25283809
PTC1_HUMAN	PTCH1	physical	25283809
TMG2_HUMAN	PRRG2	physical	25283809
WBP2_HUMAN	WBP2	physical	25283809
NEDD8_HUMAN	NEDD8	physical	26344197
USP9X_HUMAN	USP9X	physical	26598551
SMAD2_HUMAN	SMAD2	physical	27292796
P73_HUMAN	TP73	physical	27292796
ASPP2_HUMAN	TP53BP2	physical	10358088
ENAH_HUMAN	ENAH	physical	10358088
PTN14_HUMAN	PTPN14	physical	27432908
PTN21_HUMAN	PTPN21	physical	27432908
CTNB1_HUMAN	CTNNB1	physical	27173435
TEAD1_HUMAN	TEAD1	physical	25796446
AMOL2_HUMAN	AMOTL2	physical	25796446
PTN14_HUMAN	PTPN14	physical	25796446
AMOL1_HUMAN	AMOTL1	physical	25796446
XRCC5_HUMAN	XRCC5	physical	25796446
XRCC6_HUMAN	XRCC6	physical	25796446
MPDZ_HUMAN	MPDZ	physical	25796446
INADL_HUMAN	INADL	physical	25796446
AHNK_HUMAN	AHNAK	physical	25796446
TEAD3_HUMAN	TEAD3	physical	25796446
1433E_HUMAN	YWHAE	physical	25796446
SYEP_HUMAN	EPRS	physical	25796446
1433G_HUMAN	YWHAG	physical	25796446
TSP1_HUMAN	THBS1	physical	25796446
EF1A1_HUMAN	EEF1A1	physical	25796446
WWC3_HUMAN	WWC3	physical	25796446
TBB5_HUMAN	TUBB	physical	25796446
HORN_HUMAN	HRNR	physical	25796446
LATS1_HUMAN	LATS1	physical	25796446
ASPP2_HUMAN	TP53BP2	physical	25796446
PFKAP_HUMAN	PFKP	physical	25796446
MPP5_HUMAN	MPP5	physical	25796446
1433T_HUMAN	YWHAQ	physical	25796446
MERL_HUMAN	NF2	physical	25796446
RL6_HUMAN	RPL6	physical	25796446
COPA_HUMAN	COPA	physical	25796446
TERA_HUMAN	VCP	physical	25796446
EIF3B_HUMAN	EIF3B	physical	25796446
PYR1_HUMAN	CAD	physical	25796446
RBM10_HUMAN	RBM10	physical	25796446
HS105_HUMAN	HSPH1	physical	25796446
1433F_HUMAN	YWHAH	physical	25796446
SUN2_HUMAN	SUN2	physical	25796446
ADT2_HUMAN	SLC25A5	physical	25796446
PSMD2_HUMAN	PSMD2	physical	25796446
ACTN1_HUMAN	ACTN1	physical	25796446
RRBP1_HUMAN	RRBP1	physical	25796446
DDX3X_HUMAN	DDX3X	physical	25796446
RS4X_HUMAN	RPS4X	physical	25796446
F120A_HUMAN	FAM120A	physical	25796446
1433B_HUMAN	YWHAB	physical	25796446
NUCL_HUMAN	NCL	physical	25796446
CSTF1_HUMAN	CSTF1	physical	25796446
LAP2A_HUMAN	TMPO	physical	25796446
LAP2B_HUMAN	TMPO	physical	25796446
MAP4_HUMAN	MAP4	physical	25796446
UBP15_HUMAN	USP15	physical	25796446
RL7A_HUMAN	RPL7A	physical	25796446
RSMB_HUMAN	SNRPB	physical	25796446
RL18_HUMAN	RPL18	physical	25796446
SF3B3_HUMAN	SF3B3	physical	25796446
FILA2_HUMAN	FLG2	physical	25796446
HSPB1_HUMAN	HSPB1	physical	25796446
TCPB_HUMAN	CCT2	physical	25796446
SND1_HUMAN	SND1	physical	25796446
PRP8_HUMAN	PRPF8	physical	25796446
IF4B_HUMAN	EIF4B	physical	25796446
ENPL_HUMAN	HSP90B1	physical	25796446
NPM_HUMAN	NPM1	physical	25796446
2AAA_HUMAN	PPP2R1A	physical	25796446
CYFP1_HUMAN	CYFIP1	physical	25796446
MATR3_HUMAN	MATR3	physical	25796446
TBB6_HUMAN	TUBB6	physical	25796446
ROA2_HUMAN	HNRNPA2B1	physical	25796446
HSP74_HUMAN	HSPA4	physical	25796446
RS6_HUMAN	RPS6	physical	25796446
PRS7_HUMAN	PSMC2	physical	25796446
EIF3L_HUMAN	EIF3L	physical	25796446
HNRPR_HUMAN	HNRNPR	physical	25796446
MIC60_HUMAN	IMMT	physical	25796446
PHB2_HUMAN	PHB2	physical	25796446
RS8_HUMAN	RPS8	physical	25796446
CAVN1_HUMAN	PTRF	physical	25796446
RL10A_HUMAN	RPL10A	physical	25796446
PARP1_HUMAN	PARP1	physical	25796446
H14_HUMAN	HIST1H1E	physical	25796446
LMNB1_HUMAN	LMNB1	physical	25796446
CC85C_HUMAN	CCDC85C	physical	25796446
PA2G4_HUMAN	PA2G4	physical	25796446
HNRPF_HUMAN	HNRNPF	physical	25796446
ITB1_HUMAN	ITGB1	physical	25796446
NUMA1_HUMAN	NUMA1	physical	25796446
TEAD4_HUMAN	TEAD4	physical	25796446
SRSF6_HUMAN	SRSF6	physical	25796446
TGM2_HUMAN	TGM2	physical	25796446
ODO1_HUMAN	OGDH	physical	25796446
PDIA3_HUMAN	PDIA3	physical	25796446
RL24_HUMAN	RPL24	physical	25796446
SERA_HUMAN	PHGDH	physical	25796446
HS74L_HUMAN	HSPA4L	physical	25796446
IPO5_HUMAN	IPO5	physical	25796446
TSR1_HUMAN	TSR1	physical	25796446
TRIP6_HUMAN	TRIP6	physical	25796446
PP1A_HUMAN	PPP1CA	physical	25796446
YBOX1_HUMAN	YBX1	physical	25796446
SMCA4_HUMAN	SMARCA4	physical	25796446
ATD3A_HUMAN	ATAD3A	physical	25796446
RL19_HUMAN	RPL19	physical	25796446
TCPE_HUMAN	CCT5	physical	25796446
PGAM5_HUMAN	PGAM5	physical	25796446
SC16A_HUMAN	SEC16A	physical	25796446
LATS2_HUMAN	LATS2	physical	25796446
AJUBA_HUMAN	AJUBA	physical	25796446
PRS8_HUMAN	PSMC5	physical	25796446
RENT1_HUMAN	UPF1	physical	25796446
RL15_HUMAN	RPL15	physical	25796446
XRN2_HUMAN	XRN2	physical	25796446
ARI1A_HUMAN	ARID1A	physical	25796446
RL13A_HUMAN	RPL13A	physical	25796446
PRS10_HUMAN	PSMC6	physical	25796446
CNN2_HUMAN	CNN2	physical	25796446
HDAC1_HUMAN	HDAC1	physical	25796446
HDAC2_HUMAN	HDAC2	physical	25796446
1433S_HUMAN	SFN	physical	25796446
SP16H_HUMAN	SUPT16H	physical	25796446
RBBP7_HUMAN	RBBP7	physical	25796446
PRDX6_HUMAN	PRDX6	physical	25796446
SEPT2_HUMAN	SEPT2	physical	25796446
PDLI7_HUMAN	PDLIM7	physical	25796446
LIN7C_HUMAN	LIN7C	physical	25796446
QCR2_HUMAN	UQCRC2	physical	25796446
MVD1_HUMAN	MVD	physical	25796446
MYH10_HUMAN	MYH10	physical	25796446
PLOD2_HUMAN	PLOD2	physical	25796446
PSMD6_HUMAN	PSMD6	physical	25796446
PURA2_HUMAN	ADSS	physical	25796446
PUR6_HUMAN	PAICS	physical	25796446
FUBP1_HUMAN	FUBP1	physical	25796446
CPIN1_HUMAN	CIAPIN1	physical	25796446
SFXN1_HUMAN	SFXN1	physical	25796446
PSA5_HUMAN	PSMA5	physical	25796446
RL9_HUMAN	RPL9	physical	25796446
DJC10_HUMAN	DNAJC10	physical	25796446
PTBP1_HUMAN	PTBP1	physical	25796446
ANXA5_HUMAN	ANXA5	physical	25796446
IMA1_HUMAN	KPNA2	physical	25796446
WDR1_HUMAN	WDR1	physical	25796446
CK084_HUMAN	C11orf84	physical	25796446
H2AY_HUMAN	H2AFY	physical	25796446
JUN_HUMAN	JUN	physical	25796446
NHRF2_HUMAN	SLC9A3R2	physical	25796446
RTN4_HUMAN	RTN4	physical	25796446
RL14_HUMAN	RPL14	physical	25796446
H1X_HUMAN	H1FX	physical	25796446
REQU_HUMAN	DPF2	physical	25796446
IBP7_HUMAN	IGFBP7	physical	25796446
ACL6A_HUMAN	ACTL6A	physical	25796446
RL17_HUMAN	RPL17	physical	25796446
ZYX_HUMAN	ZYX	physical	25796446
PSB4_HUMAN	PSMB4	physical	25796446
TWF1_HUMAN	TWF1	physical	25796446
H15_HUMAN	HIST1H1B	physical	25796446
KITH_HUMAN	TK1	physical	25796446
CDC20_HUMAN	CDC20	physical	25796446
RAN_HUMAN	RAN	physical	25796446
RL21_HUMAN	RPL21	physical	25796446
SV2B_HUMAN	SV2B	physical	25796446
JUPI2_HUMAN	HN1L	physical	25796446
TAZ_HUMAN	TAZ	physical	28346439
TBK1_HUMAN	TBK1	physical	28346439

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 120433: Coloboma, ocular, with or without hearing impairment, cleft lip/palate, and/or mental retardation (COB1)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"A coordinated phosphorylation by Lats and CK1 regulates YAP stabilitythrough SCF(beta-TRCP).";
Zhao B., Li L., Tumaneng K., Wang C.-Y., Guan K.-L.;
Genes Dev. 24:72-85(2010).
Cited for: PHOSPHORYLATION AT SER-400 AND SER-403 BY CSNK1D/CK1, PHOSPHORYLATIONAT SER-127 AND SER-397 BY LATS PROTEINS, UBIQUITINATION BYSCF(BETA-TRCP), AND SUBCELLULAR LOCATION.
PubMed: 20048001

"JNK phosphorylates Yes-associated protein (YAP) to regulateapoptosis.";
Tomlinson V., Gudmundsdottir K., Luong P., Leung K.Y., Knebel A.,Basu S.;
Cell Death Dis. 1:E29-E29(2010).
Cited for: PHOSPHORYLATION AT THR-119; SER-138; THR-154; SER-367 AND THR-412 BYMAPK8/JNK1 AND MAPK9/JNK2, AND FUNCTION.
PubMed: 21364637

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371, AND MASSSPECTROMETRY.
PubMed: 19413330

"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 SER-61; SER-127; SER-128;SER-131; SER-138; THR-143; SER-149; THR-154; SER-274; SER-289 ANDSER-367, AND MASS SPECTROMETRY.
PubMed: 18669648

"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASSSPECTROMETRY.
PubMed: 18220336

"Tumor suppressor LATS1 is a negative regulator of oncogene YAP.";
Hao Y., Chun A., Cheung K., Rashidi B., Yang X.;
J. Biol. Chem. 283:5496-5509(2008).
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LATS1 AND LATS2,PHOSPHORYLATION AT SER-61; SER-109; SER-127; SER-164 AND SER-397, ANDMUTAGENESIS OF HIS-122; ARG-124; SER-127 AND SER-397.
PubMed: 18158288

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371, AND MASSSPECTROMETRY.
PubMed: 17525332

"Inactivation of YAP oncoprotein by the Hippo pathway is involved incell contact inhibition and tissue growth control.";
Zhao B., Wei X., Li W., Udan R.S., Yang Q., Kim J., Xie J.,Ikenoue T., Yu J., Li L., Zheng P., Ye K., Chinnaiyan A., Halder G.,Lai Z.C., Guan K.L.;
Genes Dev. 21:2747-2761(2007).
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH YWHAB,PHOSPHORYLATION AT SER-61; SER-109; SER-127; SER-164 AND SER-397,MUTAGENESIS OF HIS-122; SER-127 AND PRO-129, AND TISSUE SPECIFICITY.
PubMed: 17974916

"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND MASSSPECTROMETRY.
PubMed: 16964243

"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND THR-110, ANDMASS SPECTROMETRY.
PubMed: 15302935

"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 THR-110; THR-143 ANDTHR-154, AND MASS SPECTROMETRY.
PubMed: 17081983

"Yap1 phosphorylation by c-Abl is a critical step in selectiveactivation of proapoptotic genes in response to DNA damage.";
Levy D., Adamovich Y., Reuven N., Shaul Y.;
Mol. Cell 29:350-361(2008).
Cited for: FUNCTION, PHOSPHORYLATION AT TYR-407 BY ABL1, MUTAGENESIS OF TYR-407,SUBCELLULAR LOCATION, AND INTERACTION WITH RUNX1 AND TP73.
PubMed: 18280240