dbPTM

PPM1H_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PPM1H_MOUSE
UniProt AC	Q3UYC0
Protein Name	Protein phosphatase 1H
Gene Name	Ppm1h
Organism	Mus musculus (Mouse).
Sequence Length	513
Subcellular Localization	Nucleus . Cytoplasm .
Protein Description	Dephosphorylates CDKN1B at 'Thr-187', thus removing a signal for proteasomal degradation..
Protein Sequence	MLTRVKSAVANFMGGIMAGSSGSEHGGSGCGGSDLPLRFPYGRPEFLGLSQDEVECSADHIARPILILKETRRLPWATGYAEVINAGKSTHNEDQASCEVLTVKKKAGTITSTPNRNSKRRSSLPNGEGLQLKENSESEGISCHYWSLFDGHAGSGAAVVASRLLQHHITQQLQDIVEILKNSAILPPTCLGEEPESTPAHGRTLTRAASLRGGVGAPGSPSTPPTRFFTEKKIPHECLVIGALESAFKEMDLQIERERSAYNISGGCTALIVVCLLGKLYVANAGDSRAIIIRNGEIIPMSSEFTPETERQRLQYLAFMQPHLLGNEFTHLEFPRRVQRKELGKKMLYRDFNMTGWAYKTIEDDDLKFPLIYGEGKKARVMATIGVTRGLGDHDLKVHDSNIYIKPFLSSAPEVRVYDLSRYEHGADDVLILATDGLWDVLSNEEVAEAITQFLPNCDPDDPHRYTLAAQDLVMRARGVLKDRGWRISNDRLGSGDDISVYVIPLIHGNKLS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MLTRVKSAVANFMG -CCHHHHHHHHHHHC	25.72	22817900
109	Phosphorylation	TVKKKAGTITSTPNR EEEECCCCEECCCCC	26.41	29899451
111	Phosphorylation	KKKAGTITSTPNRNS EECCCCEECCCCCCC	26.79	22324799
112	Phosphorylation	KKAGTITSTPNRNSK ECCCCEECCCCCCCC	37.71	22324799
113	Phosphorylation	KAGTITSTPNRNSKR CCCCEECCCCCCCCC	18.88	25521595
118	Phosphorylation	TSTPNRNSKRRSSLP ECCCCCCCCCCCCCC	25.05	23375375
122	Phosphorylation	NRNSKRRSSLPNGEG CCCCCCCCCCCCCCC	40.01	23527152
123	Phosphorylation	RNSKRRSSLPNGEGL CCCCCCCCCCCCCCC	46.14	25521595
197	Phosphorylation	CLGEEPESTPAHGRT CCCCCCCCCCCCCCH	50.86	29899451
198	Phosphorylation	LGEEPESTPAHGRTL CCCCCCCCCCCCCHH	23.88	-
210	Phosphorylation	RTLTRAASLRGGVGA CHHHHHHHCCCCCCC	20.02	24925903
212	Methylation	LTRAASLRGGVGAPG HHHHHHCCCCCCCCC	37.01	24129315
220	Phosphorylation	GGVGAPGSPSTPPTR CCCCCCCCCCCCCCC	18.02	25521595
222	Phosphorylation	VGAPGSPSTPPTRFF CCCCCCCCCCCCCCC	56.07	22324799
223	Phosphorylation	GAPGSPSTPPTRFFT CCCCCCCCCCCCCCC	36.35	25521595
226	Phosphorylation	GSPSTPPTRFFTEKK CCCCCCCCCCCCCCC	41.11	22324799
262	Nitration	IERERSAYNISGGCT HHHHHHHHCCCCHHH	17.80	-
388	Phosphorylation	VMATIGVTRGLGDHD EEEEEECCCCCCCCC	17.51	28059163
421	Phosphorylation	EVRVYDLSRYEHGAD EEEEEEHHHCCCCCC	29.89	-
489	Phosphorylation	KDRGWRISNDRLGSG HHCCEEECCCCCCCC	24.89	29899451
495	Phosphorylation	ISNDRLGSGDDISVY ECCCCCCCCCCEEEE	43.57	29899451
513	Phosphorylation	LIHGNKLS------- EECCCCCC-------	39.52	29899451

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
Oops, there are no upstream regulatory protein records of PPM1H_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PPM1H_MOUSE !!

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 PPM1H_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PPM1H_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of PPM1H_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND MASSSPECTROMETRY.	17114649 [Abstract]