dbPTM

YAP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	YAP1_MOUSE
UniProt AC	P46938
Protein Name	Transcriptional coactivator YAP1
Gene Name	Yap1
Organism	Mus musculus (Mouse).
Sequence Length	488
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. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Plays a key role in tissue tension and 3D tissue shape by regulating cortical actomyosin network formation. Acts via ARHGAP18, a Rho GTPase activating protein that suppresses F-actin polymerization. Plays a key role to control cell proliferation in response to cell contact. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. The presence of TEAD transcription factors are required for it to stimulate gene expression, cell growth, anchorage-independent growth, and epithelial mesenchymal transition (EMT) induction..
Protein Sequence	MEPAQQPPPQPAPQGPAPPSVSPAGTPAAPPAPPAGHQVVHVRGDSETDLEALFNAVMNPKTANVPQTVPMRLRKLPDSFFKPPEPKSHSRQASTDAGTAGALTPQHVRAHSSPASLQLGAVSPGTLTASGVVSGPAAAPAAQHLRQSSFEIPDDVPLPAGWEMAKTSSGQRYFLNHNDQTTTWQDPRKAMLSQLNVPAPASPAVPQTLMNSASGPLPDGWEQAMTQDGEVYYINHKNKTTSWLDPRLDPRFAMNQRITQSAPVKQPPPLAPQSPQGGVLGGGSSNQQQQIQLQQLQMEKERLRLKQQELFRQAIRNINPSTANAPKCQELALRSQLPTLEQDGGTPNAVSSPGMSQELRTMTTNSSDPFLNSGTYHSRDESTDSGLSMSSYSIPRTPDDFLNSVDEMDTGDTISQSTLPSQQSRFPDYLEALPGTNVDLGTLEGDAMNIEGEELMPSLQEALSSEILDVESVLAATKLDKESFLTWL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
20	Phosphorylation	PQGPAPPSVSPAGTP CCCCCCCCCCCCCCC	33.88	29233185
22	Phosphorylation	GPAPPSVSPAGTPAA CCCCCCCCCCCCCCC	17.23	26824392
26	Phosphorylation	PSVSPAGTPAAPPAP CCCCCCCCCCCCCCC	16.32	29233185
46	Phosphorylation	VVHVRGDSETDLEAL EEEECCCCHHHHHHH	45.26	24925903
48	Phosphorylation	HVRGDSETDLEALFN EECCCCHHHHHHHHH	50.24	24925903
68	Phosphorylation	KTANVPQTVPMRLRK CCCCCCCCCCCHHHC	22.10	27149854
79	Phosphorylation	RLRKLPDSFFKPPEP HHHCCCHHHCCCCCC	30.55	21376238
88	Phosphorylation	FKPPEPKSHSRQAST CCCCCCCCCCCCCCC	37.09	27087446
90	Phosphorylation	PPEPKSHSRQASTDA CCCCCCCCCCCCCCC	32.93	27087446
94	Phosphorylation	KSHSRQASTDAGTAG CCCCCCCCCCCCCCC	20.62	27087446
95	Phosphorylation	SHSRQASTDAGTAGA CCCCCCCCCCCCCCC	32.65	25521595
99	Phosphorylation	QASTDAGTAGALTPQ CCCCCCCCCCCCCHH	24.52	27087446
104	Phosphorylation	AGTAGALTPQHVRAH CCCCCCCCHHHHHCC	21.99	26824392
112	Phosphorylation	PQHVRAHSSPASLQL HHHHHCCCCCCEEEC	36.71	27087446
113	Phosphorylation	QHVRAHSSPASLQLG HHHHCCCCCCEEECC	18.02	27087446
116	Phosphorylation	RAHSSPASLQLGAVS HCCCCCCEEECCCCC	21.74	27087446
123	Phosphorylation	SLQLGAVSPGTLTAS EEECCCCCCCEEEEC	19.65	27087446
126	Phosphorylation	LGAVSPGTLTASGVV CCCCCCCEEEECCEE	25.07	27087446
128	Phosphorylation	AVSPGTLTASGVVSG CCCCCEEEECCEECC	20.72	25619855
130	Phosphorylation	SPGTLTASGVVSGPA CCCEEEECCEECCCC	27.21	25619855
134	Phosphorylation	LTASGVVSGPAAAPA EEECCEECCCCHHHH	36.33	25619855
148	Phosphorylation	AAQHLRQSSFEIPDD HHHHHHHHCCCCCCC	30.47	21082442
149	Phosphorylation	AQHLRQSSFEIPDDV HHHHHHHCCCCCCCC	20.68	25521595
202	Phosphorylation	LNVPAPASPAVPQTL CCCCCCCCCCCCHHH	16.60	22006019
259	Phosphorylation	FAMNQRITQSAPVKQ HHHCCCCCCCCCCCC	20.75	25619855
261	Phosphorylation	MNQRITQSAPVKQPP HCCCCCCCCCCCCCC	26.37	25619855
274	Phosphorylation	PPPLAPQSPQGGVLG CCCCCCCCCCCCCCC	20.38	27087446
284	Phosphorylation	GGVLGGGSSNQQQQI CCCCCCCCCHHHHHH	29.41	25619855
285	Phosphorylation	GVLGGGSSNQQQQIQ CCCCCCCCHHHHHHH	41.77	25619855
306	Ubiquitination	EKERLRLKQQELFRQ HHHHHHHHHHHHHHH	43.43	27667366
308	Ubiquitination	ERLRLKQQELFRQAI HHHHHHHHHHHHHHH	48.01	27667366
335	Phosphorylation	CQELALRSQLPTLEQ HHHHHHHHCCCCHHH	36.60	25619855
339	Phosphorylation	ALRSQLPTLEQDGGT HHHHCCCCHHHCCCC	52.07	25619855
340	Phosphorylation	LRSQLPTLEQDGGTP HHHCCCCHHHCCCCC	5.41	17525332
346	Phosphorylation	TLEQDGGTPNAVSSP CHHHCCCCCCCCCCC	20.92	25619855
351	Phosphorylation	GGTPNAVSSPGMSQE CCCCCCCCCCCCCHH	28.53	25619855
352	Phosphorylation	GTPNAVSSPGMSQEL CCCCCCCCCCCCHHH	20.90	27087446
356	Phosphorylation	AVSSPGMSQELRTMT CCCCCCCCHHHHHHC	26.81	25619855
361	Phosphorylation	GMSQELRTMTTNSSD CCCHHHHHHCCCCCC	31.34	23737553
363	Phosphorylation	SQELRTMTTNSSDPF CHHHHHHCCCCCCCC	23.39	23737553
364	Phosphorylation	QELRTMTTNSSDPFL HHHHHHCCCCCCCCC	23.45	23737553
366	Phosphorylation	LRTMTTNSSDPFLNS HHHHCCCCCCCCCCC	33.74	25521595
367	Phosphorylation	RTMTTNSSDPFLNSG HHHCCCCCCCCCCCC	51.91	25521595
373	Phosphorylation	SSDPFLNSGTYHSRD CCCCCCCCCCCCCCC	34.36	23984901
375	Phosphorylation	DPFLNSGTYHSRDES CCCCCCCCCCCCCCC	20.20	23984901
376	Phosphorylation	PFLNSGTYHSRDEST CCCCCCCCCCCCCCC	11.00	25777480
378	Phosphorylation	LNSGTYHSRDESTDS CCCCCCCCCCCCCCC	30.89	23984901
382	Phosphorylation	TYHSRDESTDSGLSM CCCCCCCCCCCCCCC	41.63	25521595
383	Phosphorylation	YHSRDESTDSGLSMS CCCCCCCCCCCCCCC	31.94	27742792
385	Phosphorylation	SRDESTDSGLSMSSY CCCCCCCCCCCCCCC	41.54	28507225
388	Phosphorylation	ESTDSGLSMSSYSIP CCCCCCCCCCCCCCC	21.83	27742792
390	Phosphorylation	TDSGLSMSSYSIPRT CCCCCCCCCCCCCCC	23.81	23984901
391	Phosphorylation	DSGLSMSSYSIPRTP CCCCCCCCCCCCCCH	17.79	23984901
392	Phosphorylation	SGLSMSSYSIPRTPD CCCCCCCCCCCCCHH	11.87	29472430
393	Phosphorylation	GLSMSSYSIPRTPDD CCCCCCCCCCCCHHH	28.23	23984901
397	Phosphorylation	SSYSIPRTPDDFLNS CCCCCCCCHHHHHHH	26.22	26370283
404	Phosphorylation	TPDDFLNSVDEMDTG CHHHHHHHCCCCCCC	32.85	25338131
410	Phosphorylation	NSVDEMDTGDTISQS HHCCCCCCCCCCCHH	35.33	25338131
429	Phosphorylation	QQSRFPDYLEALPGT CHHHCCHHHHHCCCC	13.48	-
481	Ubiquitination	LAATKLDKESFLTWL HHHHCCCHHHHHHCC	66.74	-

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
104	T	Phosphorylation	Kinase	MAPK9	Q9WTU6	Uniprot
104	T	Phosphorylation	Kinase	MAPK8	Q91Y86	Uniprot
112	S	Phosphorylation	Kinase	LATS1	O95835	PSP
112	S	Phosphorylation	Kinase	STK38	Q91VJ4	GPS
112	S	Phosphorylation	Kinase	STK38L	Q7TSE6	GPS
112	S	Phosphorylation	Kinase	LATS1	Q8BYR2	PSP
112	S	Phosphorylation	Kinase	LATS2	Q9NRM7	PSP
149	S	Phosphorylation	Kinase	LATS1	Q8BYR2	Uniprot
149	S	Phosphorylation	Kinase	LATS2	Q7TSJ6	Uniprot
352	S	Phosphorylation	Kinase	MAPK8	Q91Y86	Uniprot
352	S	Phosphorylation	Kinase	MAPK9	Q9WTU6	Uniprot
382	S	Phosphorylation	Kinase	LATS2	Q7TSJ6	Uniprot
382	S	Phosphorylation	Kinase	LATS2	Q9NRM7	PSP
382	S	Phosphorylation	Kinase	STK38L	Q7TSE6	GPS
382	S	Phosphorylation	Kinase	LATS1	Q8BYR2	Uniprot
382	S	Phosphorylation	Kinase	STK38	Q91VJ4	GPS
382	S	Phosphorylation	Kinase	LATS1	O95835	PSP
385	S	Phosphorylation	Kinase	CK1	-	Uniprot
388	S	Phosphorylation	Kinase	CK1	-	Uniprot
392	Y	Phosphorylation	Kinase	ABL1	P00520	Uniprot
397	T	Phosphorylation	Kinase	MAPK8	Q91Y86	Uniprot
397	T	Phosphorylation	Kinase	MAPK9	Q9WTU6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
104	T	Phosphorylation	-
Phosphorylated at Thr-104, Ser-123, Ser-352 and Thr-397 by MAPK8/JNK1 and MAPK9/JNK2, which is required for the regulation of apoptosis by YAP1 (By similarity).
123	S	Phosphorylation	-
Phosphorylated at Thr-104, Ser-123, Ser-352 and Thr-397 by MAPK8/JNK1 and MAPK9/JNK2, which is required for the regulation of apoptosis by YAP1 (By similarity).
352	S	Phosphorylation	-
Phosphorylated at Thr-104, Ser-123, Ser-352 and Thr-397 by MAPK8/JNK1 and MAPK9/JNK2, which is required for the regulation of apoptosis by YAP1 (By similarity).
382	S	Phosphorylation	-
Phosphorylation at Ser-385 and Ser-388 by CK1 is triggered by previous phosphorylation at Ser-382 by LATS proteins and leads to YAP1 ubiquitination by SCF(beta-TRCP) E3 ubiquitin ligase and subsequent degradation (By similarity).
382	S	ubiquitylation	-
Phosphorylation at Ser-385 and Ser-388 by CK1 is triggered by previous phosphorylation at Ser-382 by LATS proteins and leads to YAP1 ubiquitination by SCF(beta-TRCP) E3 ubiquitin ligase and subsequent degradation (By similarity).
385	S	Phosphorylation	-
Phosphorylation at Ser-385 and Ser-388 by CK1 is triggered by previous phosphorylation at Ser-382 by LATS proteins and leads to YAP1 ubiquitination by SCF(beta-TRCP) E3 ubiquitin ligase and subsequent degradation (By similarity).
385	S	ubiquitylation	-
Phosphorylation at Ser-385 and Ser-388 by CK1 is triggered by previous phosphorylation at Ser-382 by LATS proteins and leads to YAP1 ubiquitination by SCF(beta-TRCP) E3 ubiquitin ligase and subsequent degradation (By similarity).
388	S	Phosphorylation	-
Phosphorylation at Ser-385 and Ser-388 by CK1 is triggered by previous phosphorylation at Ser-382 by LATS proteins and leads to YAP1 ubiquitination by SCF(beta-TRCP) E3 ubiquitin ligase and subsequent degradation (By similarity).
388	S	ubiquitylation	-
Phosphorylation at Ser-385 and Ser-388 by CK1 is triggered by previous phosphorylation at Ser-382 by LATS proteins and leads to YAP1 ubiquitination by SCF(beta-TRCP) E3 ubiquitin ligase and subsequent degradation (By similarity).
397	T	Phosphorylation	-
Phosphorylated at Thr-104, Ser-123, Ser-352 and Thr-397 by MAPK8/JNK1 and MAPK9/JNK2, which is required for the regulation of apoptosis by YAP1 (By similarity).

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 YAP1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMAD2_MOUSE	Smad2	physical	21145499
MPP5_HUMAN	MPP5	physical	21145499
LIN7C_HUMAN	LIN7C	physical	21145499
INADL_HUMAN	INADL	physical	21145499
AMOT_HUMAN	AMOT	physical	21145499
LATS1_HUMAN	LATS1	physical	21145499
1433T_HUMAN	YWHAQ	physical	21145499
MPDZ_HUMAN	MPDZ	physical	21145499
MPP7_HUMAN	MPP7	physical	21145499
AMOL1_HUMAN	AMOTL1	physical	21145499
AMOL2_HUMAN	AMOTL2	physical	21145499
1433E_HUMAN	YWHAE	physical	21145499
1433B_HUMAN	YWHAB	physical	21145499
1433G_HUMAN	YWHAG	physical	21145499
1433Z_HUMAN	YWHAZ	physical	21145499
1433F_HUMAN	YWHAH	physical	21145499
WWTR1_MOUSE	Wwtr1	physical	16332960
MERL_HUMAN	NF2	physical	26496610
PP1A_HUMAN	PPP1CA	physical	26496610
TEAD1_HUMAN	TEAD1	physical	26496610
TEAD4_HUMAN	TEAD4	physical	26496610
TEAD3_HUMAN	TEAD3	physical	26496610
ASPP2_HUMAN	TP53BP2	physical	26496610
1433B_HUMAN	YWHAB	physical	26496610
1433G_HUMAN	YWHAG	physical	26496610
1433F_HUMAN	YWHAH	physical	26496610
1433Z_HUMAN	YWHAZ	physical	26496610
GEMI2_HUMAN	GEMIN2	physical	26496610
MPDZ_HUMAN	MPDZ	physical	26496610
INADL_HUMAN	INADL	physical	26496610
RASF8_HUMAN	RASSF8	physical	26496610
MECR_HUMAN	MECR	physical	26496610
AMOL2_HUMAN	AMOTL2	physical	26496610
LIN7C_HUMAN	LIN7C	physical	26496610
PARD3_HUMAN	PARD3	physical	26496610
MPP5_HUMAN	MPP5	physical	26496610
AMOL1_HUMAN	AMOTL1	physical	26496610

Drug and Disease Associations

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

Regulatory Network of YAP1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-356, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 AND SER-113, ANDMASS SPECTROMETRY.	17242355 [Abstract]

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