dbPTM

PPM1G_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PPM1G_HUMAN
UniProt AC	O15355
Protein Name	Protein phosphatase 1G
Gene Name	PPM1G
Organism	Homo sapiens (Human).
Sequence Length	546
Subcellular Localization	Cytoplasm . Membrane Lipid-anchor .
Protein Description
Protein Sequence	MGAYLSQPNTVKCSGDGVGAPRLPLPYGFSAMQGWRVSMEDAHNCIPELDSETAMFSVYDGHGGEEVALYCAKYLPDIIKDQKAYKEGKLQKALEDAFLAIDAKLTTEEVIKELAQIAGRPTEDEDEKEKVADEDDVDNEEAALLHEEATMTIEELLTRYGQNCHKGPPHSKSGGGTGEEPGSQGLNGEAGPEDSTRETPSQENGPTAKAYTGFSSNSERGTEAGQVGEPGIPTGEAGPSCSSASDKLPRVAKSKFFEDSEDESDEAEEEEEDSEECSEEEDGYSSEEAENEEDEDDTEEAEEDDEEEEEEMMVPGMEGKEEPGSDSGTTAVVALIRGKQLIVANAGDSRCVVSEAGKALDMSYDHKPEDEVELARIKNAGGKVTMDGRVNGGLNLSRAIGDHFYKRNKNLPPEEQMISALPDIKVLTLTDDHEFMVIACDGIWNVMSSQEVVDFIQSKISQRDENGELRLLSSIVEELLDQCLAPDTSGDGTGCDNMTCIIICFKPRNTAELQPESGKRKLEEVLSTEGAEENGNSDKKKKAKRD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Myristoylation	------MGAYLSQPN ------CCCCCCCCC	23.95	25807930
4	Phosphorylation	----MGAYLSQPNTV ----CCCCCCCCCCE	10.93	29759185
6	Phosphorylation	--MGAYLSQPNTVKC --CCCCCCCCCCEEC	30.80	-
10	Phosphorylation	AYLSQPNTVKCSGDG CCCCCCCCEECCCCC	28.20	-
13	S-nitrosocysteine	SQPNTVKCSGDGVGA CCCCCEECCCCCCCC	4.83	-
13	S-nitrosylation	SQPNTVKCSGDGVGA CCCCCEECCCCCCCC	4.83	22178444
22	Methylation	GDGVGAPRLPLPYGF CCCCCCCCCCCCCCC	48.69	24129315
53	O-linked_Glycosylation	IPELDSETAMFSVYD CCCCCCCEEEEEEEC	27.63	OGP
74	Phosphorylation	VALYCAKYLPDIIKD HHHHHHHHHHHHHHC	12.63	28152594
80	2-Hydroxyisobutyrylation	KYLPDIIKDQKAYKE HHHHHHHHCHHHHHC	55.21	-
80	Ubiquitination	KYLPDIIKDQKAYKE HHHHHHHHCHHHHHC	55.21	-
80	Sumoylation	KYLPDIIKDQKAYKE HHHHHHHHCHHHHHC	55.21	-
83	Acetylation	PDIIKDQKAYKEGKL HHHHHCHHHHHCCHH	64.91	25953088
86	Ubiquitination	IKDQKAYKEGKLQKA HHCHHHHHCCHHHHH	65.92	-
92	Ubiquitination	YKEGKLQKALEDAFL HHCCHHHHHHHHHHH	66.43	21890473
104	Ubiquitination	AFLAIDAKLTTEEVI HHHHHCCCCCHHHHH	42.49	-
112	Ubiquitination	LTTEEVIKELAQIAG CCHHHHHHHHHHHHC	52.42	-
122	Phosphorylation	AQIAGRPTEDEDEKE HHHHCCCCCCHHHHH	55.50	29255136
128	Acetylation	PTEDEDEKEKVADED CCCCHHHHHHCCCHH	75.14	23236377
128	Ubiquitination	PTEDEDEKEKVADED CCCCHHHHHHCCCHH	75.14	-
128	Sumoylation	PTEDEDEKEKVADED CCCCHHHHHHCCCHH	75.14	-
160	Phosphorylation	IEELLTRYGQNCHKG HHHHHHHHHCCCCCC	20.16	-
166	Acetylation	RYGQNCHKGPPHSKS HHHCCCCCCCCCCCC	75.27	25953088
166	Ubiquitination	RYGQNCHKGPPHSKS HHHCCCCCCCCCCCC	75.27	-
172	Acetylation	HKGPPHSKSGGGTGE CCCCCCCCCCCCCCC	50.51	26051181
172	Ubiquitination	HKGPPHSKSGGGTGE CCCCCCCCCCCCCCC	50.51	21906983
173	Phosphorylation	KGPPHSKSGGGTGEE CCCCCCCCCCCCCCC	45.76	28450419
177	Phosphorylation	HSKSGGGTGEEPGSQ CCCCCCCCCCCCCCC	44.70	21815630
183	Phosphorylation	GTGEEPGSQGLNGEA CCCCCCCCCCCCCCC	31.61	17525332
195	Phosphorylation	GEAGPEDSTRETPSQ CCCCCCCCCCCCCCC	27.92	25159151
196	Phosphorylation	EAGPEDSTRETPSQE CCCCCCCCCCCCCCC	44.86	28450419
199	Phosphorylation	PEDSTRETPSQENGP CCCCCCCCCCCCCCC	25.58	29255136
201	Phosphorylation	DSTRETPSQENGPTA CCCCCCCCCCCCCCC	58.51	29255136
207	Phosphorylation	PSQENGPTAKAYTGF CCCCCCCCCCCCCCC	42.03	28450419
209	Ubiquitination	QENGPTAKAYTGFSS CCCCCCCCCCCCCCC	44.39	21890473
209	Acetylation	QENGPTAKAYTGFSS CCCCCCCCCCCCCCC	44.39	23236377
211	Phosphorylation	NGPTAKAYTGFSSNS CCCCCCCCCCCCCCC	13.49	28152594
212	Phosphorylation	GPTAKAYTGFSSNSE CCCCCCCCCCCCCCC	36.29	23186163
215	Phosphorylation	AKAYTGFSSNSERGT CCCCCCCCCCCCCCC	29.92	20873877
216	Phosphorylation	KAYTGFSSNSERGTE CCCCCCCCCCCCCCC	41.96	20873877
218	Phosphorylation	YTGFSSNSERGTEAG CCCCCCCCCCCCCCC	30.53	20873877
234	Phosphorylation	VGEPGIPTGEAGPSC CCCCCCCCCCCCCCC	45.81	28348404
240	Phosphorylation	PTGEAGPSCSSASDK CCCCCCCCCCCCHHC	26.22	25159151
242	Phosphorylation	GEAGPSCSSASDKLP CCCCCCCCCCHHCCC	33.02	29978859
243	Phosphorylation	EAGPSCSSASDKLPR CCCCCCCCCHHCCCH	35.80	29978859
245	Phosphorylation	GPSCSSASDKLPRVA CCCCCCCHHCCCHHH	36.91	25159151
247	Ubiquitination	SCSSASDKLPRVAKS CCCCCHHCCCHHHHH	58.87	-
247	Acetylation	SCSSASDKLPRVAKS CCCCCHHCCCHHHHH	58.87	23954790
260	Phosphorylation	KSKFFEDSEDESDEA HHHHCCCCCCCCCHH	39.49	-
264	Phosphorylation	FEDSEDESDEAEEEE CCCCCCCCCHHHHHH	53.74	-
325	Phosphorylation	EGKEEPGSDSGTTAV CCCCCCCCCCCCHHH	39.04	28985074
327	Phosphorylation	KEEPGSDSGTTAVVA CCCCCCCCCCHHHEE	39.47	20068231
329	Phosphorylation	EPGSDSGTTAVVALI CCCCCCCCHHHEEEE	18.61	20873877
330	Phosphorylation	PGSDSGTTAVVALIR CCCCCCCHHHEEEEC	22.45	20068231
339	Ubiquitination	VVALIRGKQLIVANA HEEEECCCEEEEEEC	31.89	21890473
339	2-Hydroxyisobutyrylation	VVALIRGKQLIVANA HEEEECCCEEEEEEC	31.89	-
349	Phosphorylation	IVANAGDSRCVVSEA EEEECCCCCEEEECC	27.02	30387612
354	Phosphorylation	GDSRCVVSEAGKALD CCCCEEEECCCCCCC	11.00	30387612
358	Ubiquitination	CVVSEAGKALDMSYD EEEECCCCCCCCCCC	53.47	21890473
367	Ubiquitination	LDMSYDHKPEDEVEL CCCCCCCCCHHHEHH	47.40	-
367	Sumoylation	LDMSYDHKPEDEVEL CCCCCCCCCHHHEHH	47.40	-
367	Sumoylation	LDMSYDHKPEDEVEL CCCCCCCCCHHHEHH	47.40	-
378	Ubiquitination	EVELARIKNAGGKVT HEHHEEEECCCCEEE	34.88	-
383	Ubiquitination	RIKNAGGKVTMDGRV EEECCCCEEEECCEE	33.35	19608861
383	Acetylation	RIKNAGGKVTMDGRV EEECCCCEEEECCEE	33.35	19608861
397	Phosphorylation	VNGGLNLSRAIGDHF ECCCCCHHHHHHHHH	20.70	21406692
406	Ubiquitination	AIGDHFYKRNKNLPP HHHHHHHHHCCCCCH	48.85	-
406	Succinylation	AIGDHFYKRNKNLPP HHHHHHHHHCCCCCH	48.85	23954790
406	Methylation	AIGDHFYKRNKNLPP HHHHHHHHHCCCCCH	48.85	66713279
406	Acetylation	AIGDHFYKRNKNLPP HHHHHHHHHCCCCCH	48.85	27452117
406	2-Hydroxyisobutyrylation	AIGDHFYKRNKNLPP HHHHHHHHHCCCCCH	48.85	-
409	Ubiquitination	DHFYKRNKNLPPEEQ HHHHHHCCCCCHHHH	64.99	21906983
419	Phosphorylation	PPEEQMISALPDIKV CHHHHHHHHCCCCEE	20.57	21406692
473	Phosphorylation	NGELRLLSSIVEELL CCHHHHHHHHHHHHH	23.70	22817901
517	Phosphorylation	TAELQPESGKRKLEE CCCCCCCCHHHHHHH	57.19	25159151
519	Acetylation	ELQPESGKRKLEEVL CCCCCCHHHHHHHHH	56.49	23749302
519	Ubiquitination	ELQPESGKRKLEEVL CCCCCCHHHHHHHHH	56.49	21890473
519	2-Hydroxyisobutyrylation	ELQPESGKRKLEEVL CCCCCCHHHHHHHHH	56.49	-
519	Sumoylation	ELQPESGKRKLEEVL CCCCCCHHHHHHHHH	56.49	-
519	Sumoylation	ELQPESGKRKLEEVL CCCCCCHHHHHHHHH	56.49	-
527	Phosphorylation	RKLEEVLSTEGAEEN HHHHHHHCCCCHHHC	29.59	29255136
528	Phosphorylation	KLEEVLSTEGAEENG HHHHHHCCCCHHHCC	33.99	30266825
537	Phosphorylation	GAEENGNSDKKKKAK CHHHCCCCHHHHHHH	52.81	30266825
539	Acetylation	EENGNSDKKKKAKRD HHCCCCHHHHHHHCC	67.33	23954790

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
183	S	Phosphorylation	Kinase	ATM	Q13315	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PPM1G_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 PPM1G_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SNX12_HUMAN	SNX12	physical	22939629
SNX3_HUMAN	SNX3	physical	22939629
SPRE_HUMAN	SPR	physical	22939629
SRXN1_HUMAN	SRXN1	physical	22939629
STAT6_HUMAN	STAT6	physical	22939629
THOP1_HUMAN	THOP1	physical	22939629
TLE3_HUMAN	TLE3	physical	22939629
TTC9C_HUMAN	TTC9C	physical	22939629
UBE2C_HUMAN	UBE2C	physical	22939629
ST1A1_HUMAN	SULT1A1	physical	22939629
STMN2_HUMAN	STMN2	physical	22939629
S100P_HUMAN	S100P	physical	22939629
STAM1_HUMAN	STAM	physical	22939629
PSA1_HUMAN	PSMA1	physical	22939629
SAHH2_HUMAN	AHCYL1	physical	22939629
CAND1_HUMAN	CAND1	physical	22863883
SYCC_HUMAN	CARS	physical	22863883
GARS_HUMAN	GARS	physical	22863883
HIRP3_HUMAN	HIRIP3	physical	22863883
HS105_HUMAN	HSPH1	physical	22863883
PUF60_HUMAN	PUF60	physical	22863883
RO60_HUMAN	TROVE2	physical	22863883
TTC1_HUMAN	TTC1	physical	22863883
XPO7_HUMAN	XPO7	physical	22863883
SAHH2_HUMAN	AHCYL1	physical	26344197
MED4_HUMAN	MED4	physical	26344197
PAIP1_HUMAN	PAIP1	physical	26344197
SBK1_HUMAN	SBK1	physical	26344197
STMN1_HUMAN	STMN1	physical	26344197
COPA_HUMAN	COPA	physical	27880917
COPB2_HUMAN	COPB2	physical	27880917
COPE_HUMAN	COPE	physical	27880917
GUAA_HUMAN	GMPS	physical	27880917
H2B1B_HUMAN	HIST1H2BB	physical	27880917
H2B1D_HUMAN	HIST1H2BD	physical	27880917
H2B1C_HUMAN	HIST1H2BD	physical	27880917
PARP1_HUMAN	PARP1	physical	27880917
TRUA_HUMAN	PUS1	physical	27880917
RCC1_HUMAN	RCC1	physical	27880917
GLYM_HUMAN	SHMT2	physical	27880917
UBP7_HUMAN	USP7	physical	27880917

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 PPM1G_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-383, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-183, AND MASSSPECTROMETRY.	17525332 [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-527, AND MASSSPECTROMETRY.	17287340 [Abstract]