dbPTM

PPME1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PPME1_HUMAN
UniProt AC	Q9Y570
Protein Name	Protein phosphatase methylesterase 1
Gene Name	PPME1
Organism	Homo sapiens (Human).
Sequence Length	386
Subcellular Localization
Protein Description	Demethylates proteins that have been reversibly carboxymethylated. Demethylates PPP2CB (in vitro) and PPP2CA. Binding to PPP2CA displaces the manganese ion and inactivates the enzyme..
Protein Sequence	MSALEKSMHLGRLPSRPPLPGSGGSQSGAKMRMGPGRKRDFSPVPWSQYFESMEDVEVENETGKDTFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAIISRVQCRIVALDLRSHGETKVKNPEDLSAETMAKDVGNVVEAMYGDLPPPIMLIGHSMGGAIAVHTASSNLVPSLLGLCMIDVVEGTAMDALNSMQNFLRGRPKTFKSLENAIEWSVKSGQIRNLESARVSMVGQVKQCEGITSPEGSKSIVEGIIEEEEEDEEGSESISKRKKEDDMETKKDHPYTWRIELAKTEKYWDGWFRGLSNLFLSCPIPKLLLLAGVDRLDKDLTIGQMQGKFQMQVLPQCGHAVHEDAPDKVAEAVATFLIRHRFAEPIGGFQCVFPGC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSALEKSMH ------CCHHHHHHH	41.37	28857561
6	Acetylation	--MSALEKSMHLGRL --CCHHHHHHHHCCC	54.66	23749302
6	Ubiquitination	--MSALEKSMHLGRL --CCHHHHHHHHCCC	54.66	19608861
7	Phosphorylation	-MSALEKSMHLGRLP -CCHHHHHHHHCCCC	11.32	29496963
15	Phosphorylation	MHLGRLPSRPPLPGS HHHCCCCCCCCCCCC	63.11	25159151
16	Asymmetric dimethylarginine	HLGRLPSRPPLPGSG HHCCCCCCCCCCCCC	34.61	-
16	Methylation	HLGRLPSRPPLPGSG HHCCCCCCCCCCCCC	34.61	24129315
22	Phosphorylation	SRPPLPGSGGSQSGA CCCCCCCCCCCCCCC	37.73	25159151
25	Phosphorylation	PLPGSGGSQSGAKMR CCCCCCCCCCCCCCC	25.38	21712546
27	Phosphorylation	PGSGGSQSGAKMRMG CCCCCCCCCCCCCCC	42.27	25159151
30 (in isoform 2)	Ubiquitination	-	30.48	21906983
30	Acetylation	GGSQSGAKMRMGPGR CCCCCCCCCCCCCCC	30.48	25953088
42	Phosphorylation	PGRKRDFSPVPWSQY CCCCCCCCCCCHHHH	29.31	25159151
47	Phosphorylation	DFSPVPWSQYFESME CCCCCCHHHHCHHCC	14.66	23663014
49	Phosphorylation	SPVPWSQYFESMEDV CCCCHHHHCHHCCCE	12.09	27732954
52	Phosphorylation	PWSQYFESMEDVEVE CHHHHCHHCCCEEEE	19.99	28464451
62	Phosphorylation	DVEVENETGKDTFRV CEEEECCCCCCEEEE	62.20	23898821
121	Ubiquitination	SHGETKVKNPEDLSA HCCCCCCCCHHHCCH	69.23	-
131	Sulfoxidation	EDLSAETMAKDVGNV HHCCHHHHHHHHHHH	3.08	21406390
193	Phosphorylation	TAMDALNSMQNFLRG CHHHHHHHHHHHHCC	23.69	20068231
206	Ubiquitination	RGRPKTFKSLENAIE CCCCCHHHHHHHHHH	60.40	-
207	Phosphorylation	GRPKTFKSLENAIEW CCCCHHHHHHHHHHH	36.40	22210691
215	Phosphorylation	LENAIEWSVKSGQIR HHHHHHHHHHCCCCC	13.58	22210691
217 (in isoform 1)	Ubiquitination	-	43.27	21906983
217	Ubiquitination	NAIEWSVKSGQIRNL HHHHHHHHCCCCCCC	43.27	2190698
217	Ubiquitination	NAIEWSVKSGQIRNL HHHHHHHHCCCCCCC	43.27	21906983
217	Acetylation	NAIEWSVKSGQIRNL HHHHHHHHCCCCCCC	43.27	25953088
230	Phosphorylation	NLESARVSMVGQVKQ CCHHCEEEEEEEEEE	11.38	22210691
242	Phosphorylation	VKQCEGITSPEGSKS EEECCCCCCCCCCCH	49.43	29255136
243	Phosphorylation	KQCEGITSPEGSKSI EECCCCCCCCCCCHH	21.02	29255136
247	Phosphorylation	GITSPEGSKSIVEGI CCCCCCCCCHHHEEC	22.90	29255136
248	Ubiquitination	ITSPEGSKSIVEGII CCCCCCCCHHHEECC	55.87	-
249	Phosphorylation	TSPEGSKSIVEGIIE CCCCCCCHHHEECCC	33.30	29523821
265	Phosphorylation	EEEDEEGSESISKRK HHCCCCCCCCHHHHH	31.30	28857561
270	Ubiquitination	EGSESISKRKKEDDM CCCCCHHHHHCCCCC	67.57	-
277	Sulfoxidation	KRKKEDDMETKKDHP HHHCCCCCCCCCCCC	12.47	30846556
281	Ubiquitination	EDDMETKKDHPYTWR CCCCCCCCCCCCEEE	69.55	-
293	2-Hydroxyisobutyrylation	TWRIELAKTEKYWDG EEEEEEECCCCCCCC	70.60	-
294	Phosphorylation	WRIELAKTEKYWDGW EEEEEECCCCCCCCH	31.91	28857561
295	Ubiquitination	RIELAKTEKYWDGWF EEEEECCCCCCCCHH	43.36	-
296	Acetylation	IELAKTEKYWDGWFR EEEECCCCCCCCHHH	57.80	26051181
306	Phosphorylation	DGWFRGLSNLFLSCP CCHHHHHHHHHHHCC	34.02	28857561
312	S-nitrosocysteine	LSNLFLSCPIPKLLL HHHHHHHCCHHHHHH	3.73	-
312	S-nitrosylation	LSNLFLSCPIPKLLL HHHHHHHCCHHHHHH	3.73	19483679
328	2-Hydroxyisobutyrylation	AGVDRLDKDLTIGQM HCCCCCCCCCCHHHC	60.26	-
335	Sulfoxidation	KDLTIGQMQGKFQMQ CCCCHHHCCCEEEEE	4.84	21406390
338	Ubiquitination	TIGQMQGKFQMQVLP CHHHCCCEEEEEECC	18.61	-

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
15	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
15	S	Phosphorylation	Kinase	CAMK1A	Q14012	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PPME1_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 PPME1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
2AAA_HUMAN	PPP2R1A	physical	19156129
PP2AA_HUMAN	PPP2CA	physical	19156129
TDRD1_HUMAN	TDRD1	physical	19156129
PP4C_HUMAN	PPP4C	physical	19156129
PP2AB_HUMAN	PPP2CB	physical	19156129
NFKB1_HUMAN	NFKB1	physical	19156129
TJAP1_HUMAN	TJAP1	physical	22939629
RFA1_HUMAN	RPA1	physical	22939629
GUAA_HUMAN	GMPS	physical	22863883
GPN1_HUMAN	GPN1	physical	22863883
HNRPF_HUMAN	HNRNPF	physical	22863883
HPBP1_HUMAN	HSPBP1	physical	22863883
OGT1_HUMAN	OGT	physical	22863883
PNPH_HUMAN	PNP	physical	22863883
PSMD5_HUMAN	PSMD5	physical	22863883
RPR1B_HUMAN	RPRD1B	physical	22863883
TM1L1_HUMAN	TOM1L1	physical	22863883
FCL_HUMAN	TSTA3	physical	22863883
WDR4_HUMAN	WDR4	physical	22863883
ZPR1_HUMAN	ZPR1	physical	22863883
2ABD_HUMAN	PPP2R2D	physical	26186194
ACY1_HUMAN	ACY1	physical	26186194
PP2AA_HUMAN	PPP2CA	physical	26186194
PP4R2_HUMAN	PPP4R2	physical	26186194
2A5D_HUMAN	PPP2R5D	physical	26186194
HXK2_HUMAN	HK2	physical	26344197
PP2AA_HUMAN	PPP2CA	physical	26499835
2AAA_HUMAN	PPP2R1A	physical	26499835
CMYA5_HUMAN	CMYA5	physical	26499835
CAD23_HUMAN	CDH23	physical	26499835
SYNE1_HUMAN	SYNE1	physical	26499835
PP2AB_HUMAN	PPP2CB	physical	26499835
CAR14_HUMAN	CARD14	physical	26499835
PPME1_HUMAN	PPME1	physical	26499835
LRC8E_HUMAN	LRRC8E	physical	26499835
HORN_HUMAN	HRNR	physical	26499835
DHRS2_HUMAN	DHRS2	physical	26499835
GSTO1_HUMAN	GSTO1	physical	26499835
RAN_HUMAN	RAN	physical	26499835
MYH1_HUMAN	MYH1	physical	26499835
CATD_HUMAN	CTSD	physical	26499835
PCNA_HUMAN	PCNA	physical	26499835
LDHA_HUMAN	LDHA	physical	26499835
LDHB_HUMAN	LDHB	physical	26499835
MDHM_HUMAN	MDH2	physical	26499835
EF1D_HUMAN	EEF1D	physical	26499835
FPPS_HUMAN	FDPS	physical	26499835
G3P_HUMAN	GAPDH	physical	26499835
NUDC_HUMAN	NUDC	physical	26499835
CALR_HUMAN	CALR	physical	26499835
G6PI_HUMAN	GPI	physical	26499835
PDIA3_HUMAN	PDIA3	physical	26499835
PDIA1_HUMAN	P4HB	physical	26499835
KPYM_HUMAN	PKM	physical	26499835
WDR1_HUMAN	WDR1	physical	26499835
LG3BP_HUMAN	LGALS3BP	physical	26499835
HSP7C_HUMAN	HSPA8	physical	26499835
LMNA_HUMAN	LMNA	physical	26499835
SYK_HUMAN	KARS	physical	26499835
PLSL_HUMAN	LCP1	physical	26499835
TKT_HUMAN	TKT	physical	26499835
ANXA6_HUMAN	ANXA6	physical	26499835
EZRI_HUMAN	EZR	physical	26499835
PDIA4_HUMAN	PDIA4	physical	26499835
MCM3_HUMAN	MCM3	physical	26499835
EF2_HUMAN	EEF2	physical	26499835
ENPL_HUMAN	HSP90B1	physical	26499835
XPO2_HUMAN	CSE1L	physical	26499835
TIF1B_HUMAN	TRIM28	physical	26499835
CLH1_HUMAN	CLTC	physical	26499835
FLNA_HUMAN	FLNA	physical	26499835
IQGA1_HUMAN	IQGAP1	physical	26499835
RUVB1_HUMAN	RUVBL1	physical	26499835
2ABA_HUMAN	PPP2R2A	physical	26499835
2ABD_HUMAN	PPP2R2D	physical	28514442
PP2AA_HUMAN	PPP2CA	physical	28514442
PP4R2_HUMAN	PPP4R2	physical	28514442
ACY1_HUMAN	ACY1	physical	28514442
2A5D_HUMAN	PPP2R5D	physical	28514442

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 PPME1_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-6, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-42, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND MASSSPECTROMETRY.	19413330 [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-15, AND MASSSPECTROMETRY.	17287340 [Abstract]