dbPTM

PYGO2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PYGO2_HUMAN
UniProt AC	Q9BRQ0
Protein Name	Pygopus homolog 2
Gene Name	PYGO2
Organism	Homo sapiens (Human).
Sequence Length	406
Subcellular Localization	Nucleus .
Protein Description	Involved in signal transduction through the Wnt pathway..
Protein Sequence	MAASAPPPPDKLEGGGGPAPPPAPPSTGRKQGKAGLQMKSPEKKRRKSNTQGPAYSHLTEFAPPPTPMVDHLVASNPFEDDFGAPKVGVAAPPFLGSPVPFGGFRVQGGMAGQVPPGYSTGGGGGPQPLRRQPPPFPPNPMGPAFNMPPQGPGYPPPGNMNFPSQPFNQPLGQNFSPPSGQMMPGPVGGFGPMISPTMGQPPRAELGPPSLSQRFAQPGAPFGPSPLQRPGQGLPSLPPNTSPFPGPDPGFPGPGGEDGGKPLNPPASTAFPQEPHSGSPAAAVNGNQPSFPPNSSGRGGGTPDANSLAPPGKAGGGSGPQPPPGLVYPCGACRSEVNDDQDAILCEASCQKWFHRECTGMTESAYGLLTTEASAVWACDLCLKTKEIQSVYIREGMGQLVAANDG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAASAPPPP ------CCCCCCCCC	15.32	19413330
4	Phosphorylation	----MAASAPPPPDK ----CCCCCCCCCCC	31.60	22210691
11	Acetylation	SAPPPPDKLEGGGGP CCCCCCCCCCCCCCC	54.96	23236377
26	Phosphorylation	APPPAPPSTGRKQGK CCCCCCCCCCCCCCC	42.29	25159151
27	Phosphorylation	PPPAPPSTGRKQGKA CCCCCCCCCCCCCCC	46.94	25159151
40	Phosphorylation	KAGLQMKSPEKKRRK CCCCCCCCHHHHHCC	32.71	23927012
48	Phosphorylation	PEKKRRKSNTQGPAY HHHHHCCCCCCCCCH	43.21	29496963
50	Phosphorylation	KKRRKSNTQGPAYSH HHHCCCCCCCCCHHH	41.83	29496963
55	Phosphorylation	SNTQGPAYSHLTEFA CCCCCCCHHHHHHCC	10.35	22210691
56	Phosphorylation	NTQGPAYSHLTEFAP CCCCCCHHHHHHCCC	17.71	26657352
59	Phosphorylation	GPAYSHLTEFAPPPT CCCHHHHHHCCCCCC	24.51	20068231
66	Phosphorylation	TEFAPPPTPMVDHLV HHCCCCCCCCCCEEC	29.77	20068231
75	Phosphorylation	MVDHLVASNPFEDDF CCCEECCCCCCCCCC	37.24	20068231
97	Phosphorylation	AAPPFLGSPVPFGGF CCCCCCCCCCCCCCE	25.52	29255136
105	Methylation	PVPFGGFRVQGGMAG CCCCCCEEECCCCCC	24.11	54558417
120	Phosphorylation	QVPPGYSTGGGGGPQ CCCCCCCCCCCCCCC	31.21	-
130	Dimethylation	GGGPQPLRRQPPPFP CCCCCCCCCCCCCCC	41.70	-
130	Methylation	GGGPQPLRRQPPPFP CCCCCCCCCCCCCCC	41.70	30760767
131	Methylation	GGPQPLRRQPPPFPP CCCCCCCCCCCCCCC	62.13	30762985
131	Dimethylation	GGPQPLRRQPPPFPP CCCCCCCCCCCCCCC	62.13	-
210	Phosphorylation	RAELGPPSLSQRFAQ CHHHCCCCHHHHHCC	43.73	24732914
212	Phosphorylation	ELGPPSLSQRFAQPG HHCCCCHHHHHCCCC	24.52	24732914
277	Phosphorylation	AFPQEPHSGSPAAAV CCCCCCCCCCCCCCC	52.24	25627689
279	Phosphorylation	PQEPHSGSPAAAVNG CCCCCCCCCCCCCCC	17.87	25627689
302	Phosphorylation	SSGRGGGTPDANSLA CCCCCCCCCCHHHCC	22.67	19664994
307	Phosphorylation	GGTPDANSLAPPGKA CCCCCHHHCCCCCCC	27.85	30266825
313	Acetylation	NSLAPPGKAGGGSGP HHCCCCCCCCCCCCC	50.02	26051181
318	Phosphorylation	PGKAGGGSGPQPPPG CCCCCCCCCCCCCCC	51.04	28985074
386	Ubiquitination	CDLCLKTKEIQSVYI CHHHHCCCCCEEEEE	51.76	-

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
48	S	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PYGO2_HUMAN !!

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 PYGO2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ASH2L_HUMAN	ASH2L	physical	20937768
WDR5_HUMAN	WDR5	physical	20937768
RBBP5_HUMAN	RBBP5	physical	20937768
KMT2D_HUMAN	KMT2D	physical	20937768
MERL_HUMAN	NF2	physical	20937768
PYGO2_HUMAN	PYGO2	physical	20937768
KAT2A_HUMAN	KAT2A	physical	20937768
TRRAP_HUMAN	TRRAP	physical	20937768
SUPT3_HUMAN	SUPT3H	physical	20937768
CBP_HUMAN	CREBBP	physical	19555349
BCL9_HUMAN	BCL9	physical	17113272
CTNB1_HUMAN	CTNNB1	physical	24360964
DDB1_HUMAN	DDB1	physical	26170450
DCAF1_HUMAN	VPRBP	physical	26170450
CUL4A_HUMAN	CUL4A	physical	26170450
AKT1_HUMAN	AKT1	physical	26170450

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 PYGO2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-302, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"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-97 AND THR-302, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-302, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-302, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-302, AND MASSSPECTROMETRY.	18187866 [Abstract]
"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 THR-302, AND MASSSPECTROMETRY.	16964243 [Abstract]