dbPTM

IPP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IPP2_HUMAN
UniProt AC	P41236
Protein Name	Protein phosphatase inhibitor 2
Gene Name	PPP1R2
Organism	Homo sapiens (Human).
Sequence Length	205
Subcellular Localization
Protein Description	Inhibitor of protein-phosphatase 1..
Protein Sequence	MAASTASHRPIKGILKNKTSTTSSMVASAEQPRGNVDEELSKKSQKWDEMNILATYHPADKDYGLMKIDEPSTPYHSMMGDDEDACSDTEATEAMAPDILARKLAAAEGLEPKYRIQEQESSGEEDSDLSPEEREKKRQFEMKRKLHYNEGLNIKLARQLISKDLHDDDEDEEMLETADGESMNTEESNQGSTPSDQQQNKLRSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAASTASHR ------CCCCCCCCC	15.32	-
4	Phosphorylation	----MAASTASHRPI ----CCCCCCCCCCC	18.24	20068231
5	Phosphorylation	---MAASTASHRPIK ---CCCCCCCCCCCC	27.70	20068231
7	Phosphorylation	-MAASTASHRPIKGI -CCCCCCCCCCCCHH	21.81	20068231
19	O-linked_Glycosylation	KGILKNKTSTTSSMV CHHHCCCCCCCHHHC	40.47	31373491
19	Phosphorylation	KGILKNKTSTTSSMV CHHHCCCCCCCHHHC	40.47	30266825
20	Phosphorylation	GILKNKTSTTSSMVA HHHCCCCCCCHHHCC	31.15	23401153
21	Phosphorylation	ILKNKTSTTSSMVAS HHCCCCCCCHHHCCC	35.61	30266825
22	O-linked_Glycosylation	LKNKTSTTSSMVASA HCCCCCCCHHHCCCC	20.69	31373491
22	Phosphorylation	LKNKTSTTSSMVASA HCCCCCCCHHHCCCC	20.69	23401153
23	O-linked_Glycosylation	KNKTSTTSSMVASAE CCCCCCCHHHCCCCC	19.27	31373491
23	Phosphorylation	KNKTSTTSSMVASAE CCCCCCCHHHCCCCC	19.27	23401153
24	Phosphorylation	NKTSTTSSMVASAEQ CCCCCCHHHCCCCCC	18.38	23401153
25	Sulfoxidation	KTSTTSSMVASAEQP CCCCCHHHCCCCCCC	2.67	21406390
28	Phosphorylation	TTSSMVASAEQPRGN CCHHHCCCCCCCCCC	22.41	20068231
33	Methylation	VASAEQPRGNVDEEL CCCCCCCCCCCCHHH	49.35	115488493
44	Phosphorylation	DEELSKKSQKWDEMN CHHHHHHHHCHHHHH	40.50	22817900
55	Phosphorylation	DEMNILATYHPADKD HHHHHHEEECCCCCC	20.93	28796482
56	Phosphorylation	EMNILATYHPADKDY HHHHHEEECCCCCCC	10.53	28796482
63	Phosphorylation	YHPADKDYGLMKIDE ECCCCCCCCCEECCC	20.21	28796482
67	Phosphorylation	DKDYGLMKIDEPSTP CCCCCCEECCCCCCC	52.64	32142685
72	Phosphorylation	LMKIDEPSTPYHSMM CEECCCCCCCCHHCC	39.71	23401153
73	Phosphorylation	MKIDEPSTPYHSMMG EECCCCCCCCHHCCC	38.28	9405437
75	Phosphorylation	IDEPSTPYHSMMGDD CCCCCCCCHHCCCCC	13.45	23927012
77	Phosphorylation	EPSTPYHSMMGDDED CCCCCCHHCCCCCCC	12.48	30278072
83	Ubiquitination	HSMMGDDEDACSDTE HHCCCCCCCCCCCHH	52.85	24816145
87	Phosphorylation	GDDEDACSDTEATEA CCCCCCCCCHHHHHH	49.65	23927012
89	Phosphorylation	DEDACSDTEATEAMA CCCCCCCHHHHHHHC	15.95	23927012
92	Phosphorylation	ACSDTEATEAMAPDI CCCCHHHHHHHCHHH	20.32	30266825
93	Ubiquitination	CSDTEATEAMAPDIL CCCHHHHHHHCHHHH	43.42	29967540
95	Phosphorylation	DTEATEAMAPDILAR CHHHHHHHCHHHHHH	4.53	32142685
96	Phosphorylation	TEATEAMAPDILARK HHHHHHHCHHHHHHH	12.98	32142685
101	Phosphorylation	AMAPDILARKLAAAE HHCHHHHHHHHHHHC	13.59	32142685
102	Phosphorylation	MAPDILARKLAAAEG HCHHHHHHHHHHHCC	30.95	32142685
103	Ubiquitination	APDILARKLAAAEGL CHHHHHHHHHHHCCC	36.55	24816145
107	Phosphorylation	LARKLAAAEGLEPKY HHHHHHHHCCCCCCC	13.04	32142685
113	Acetylation	AAEGLEPKYRIQEQE HHCCCCCCCCCCCCC	37.47	23236377
113	Ubiquitination	AAEGLEPKYRIQEQE HHCCCCCCCCCCCCC	37.47	29967540
114	Phosphorylation	AEGLEPKYRIQEQES HCCCCCCCCCCCCCC	24.54	26503892
119	Ubiquitination	PKYRIQEQESSGEED CCCCCCCCCCCCCCC	39.22	29967540
121	Phosphorylation	YRIQEQESSGEEDSD CCCCCCCCCCCCCCC	43.25	29255136
122	Phosphorylation	RIQEQESSGEEDSDL CCCCCCCCCCCCCCC	49.85	29255136
125	Ubiquitination	EQESSGEEDSDLSPE CCCCCCCCCCCCCHH	67.36	29967540
127	Phosphorylation	ESSGEEDSDLSPEER CCCCCCCCCCCHHHH	43.67	22167270
129	Ubiquitination	SGEEDSDLSPEEREK CCCCCCCCCHHHHHH	12.16	23000965
130	Phosphorylation	GEEDSDLSPEEREKK CCCCCCCCHHHHHHH	34.94	23927012
135	Ubiquitination	DLSPEEREKKRQFEM CCCHHHHHHHHHHHH	67.23	23000965
145	Ubiquitination	RQFEMKRKLHYNEGL HHHHHHHHHHCCCCC	33.81	29967540
148	Phosphorylation	EMKRKLHYNEGLNIK HHHHHHHCCCCCHHH	25.91	25159151
155	Acetylation	YNEGLNIKLARQLIS CCCCCHHHHHHHHHH	34.71	25953088
155	Ubiquitination	YNEGLNIKLARQLIS CCCCCHHHHHHHHHH	34.71	23000965
156	Ubiquitination	NEGLNIKLARQLISK CCCCHHHHHHHHHHC	4.15	23000965
162	Phosphorylation	KLARQLISKDLHDDD HHHHHHHHCCCCCCC	28.80	24719451
163	Acetylation	LARQLISKDLHDDDE HHHHHHHCCCCCCCC	58.26	26051181
177	Phosphorylation	EDEEMLETADGESMN CCHHHHHHCCCCCCC	26.53	23186163
182	Phosphorylation	LETADGESMNTEESN HHHCCCCCCCHHHCC	23.90	23186163
185	Phosphorylation	ADGESMNTEESNQGS CCCCCCCHHHCCCCC	32.27	30576142
188	Phosphorylation	ESMNTEESNQGSTPS CCCCHHHCCCCCCCH	28.37	30576142
192	Phosphorylation	TEESNQGSTPSDQQQ HHHCCCCCCCHHHHH	27.64	30576142
193	Phosphorylation	EESNQGSTPSDQQQN HHCCCCCCCHHHHHH	33.37	18669648
195	Phosphorylation	SNQGSTPSDQQQNKL CCCCCCCHHHHHHHH	48.41	22468782
204	Phosphorylation	QQQNKLRSS------ HHHHHHHCC------	51.33	22468782
205	Phosphorylation	QQNKLRSS------- HHHHHHCC-------	37.49	22468782

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
44	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
72	S	Phosphorylation	Kinase	MARK3	P27448	PSP
73	T	Phosphorylation	Kinase	CDK5	Q00535	PSP
73	T	Phosphorylation	Kinase	GSK3	-	Uniprot
73	T	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
73	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
73	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
87	S	Phosphorylation	Kinase	CDK14	O94921	PSP
87	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
87	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
87	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
121	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
121	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
121	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
122	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
122	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
122	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
44	S	Phosphorylation	23506001
Phosphorylation on Ser-44 by ATM activates PP1 by dissociating the PP1-PPP1R2 complex.
73	T	Phosphorylation	23506001
Phosphorylation on Thr-73 by GSK3 activates PP1 by dissociating the PP1-PPP1R2 complex (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 IPP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NEB2_HUMAN	PPP1R9B	physical	12270929
PP12_YEAST	GLC7	physical	12270929
LMTK2_HUMAN	LMTK2	physical	12393858
NEK2_MOUSE	Nek2	physical	12221103
NEK2_HUMAN	NEK2	physical	12221103
SLD5_HUMAN	GINS4	physical	22863883
ISOC1_HUMAN	ISOC1	physical	22863883
ZN622_HUMAN	ZNF622	physical	22863883
PP1RB_HUMAN	PPP1R11	physical	26344197
ST1C3_HUMAN	SULT1C3	physical	26344197

Drug and Disease Associations

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

Regulatory Network of IPP2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-87, AND MASSSPECTROMETRY.	19690332 [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 SER-87 AND THR-89, AND MASSSPECTROMETRY.	18669648 [Abstract]
"A novel ATM-dependent pathway regulates protein phosphatase 1 inresponse to DNA damage."; Tang X., Hui Z.G., Cui X.L., Garg R., Kastan M.B., Xu B.; Mol. Cell. Biol. 28:2559-2566(2008). Cited for: PHOSPHORYLATION AT SER-44, AND SUBUNIT.	18250156 [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 SER-121 AND SER-122, ANDMASS SPECTROMETRY.	18088087 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-121 AND SER-122,AND MASS SPECTROMETRY.	17287340 [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 SER-121 AND SER-122, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"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-122, AND MASSSPECTROMETRY.	15302935 [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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-89, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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 THR-92, AND MASSSPECTROMETRY.	18220336 [Abstract]

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