PPM1A_MOUSE - dbPTM
PPM1A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPM1A_MOUSE
UniProt AC P49443
Protein Name Protein phosphatase 1A
Gene Name Ppm1a
Organism Mus musculus (Mouse).
Sequence Length 382
Subcellular Localization Nucleus . Cytoplasm, cytosol . Membrane
Lipid-anchor . Weakly associates at the membrane and N-myristoylation mediates the membrane localization.
Protein Description Enzyme with a broad specificity. Negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling (By similarity). Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB..
Protein Sequence MGAFLDKPKMEKHNAQGQGNGLRYGLSSMQGWRVEMEDAHTAVIGLPSGLETWSFFAVYDGHAGSQVAKYCCEHLLDHITNNQDFRGSAGAPSVENVKNGIRTGFLEIDEHMRVMSEKKHGADRSGSTAVGVLISPQHTYFINCGDSRGLLCRNRKVHFFTQDHKPSNPLEKERIQNAGGSVMIQRVNGSLAVSRALGDFDYKCVHGKGPTEQLVSPEPEVHDIERSEEDDQFIILACDGIWDVMGNEELCDFVRSRLEVTDDLEKVCNEVVDTCLYKGSRDNMSVILICFPSAPKVSAEAVKKEAELDKYLESRVEEIIKKQVEGVPDLVHVMRTLASENIPSLPPGGELASKRNVIEAVYNRLNPYKNDDTDSASTDDMW
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Myristoylation------MGAFLDKPK
------CCCCCCCHH
25.6523088624
88PhosphorylationNNQDFRGSAGAPSVE
CCCCCCCCCCCCCHH
21.1928059163
93PhosphorylationRGSAGAPSVENVKNG
CCCCCCCCHHHHHCC
41.3428059163
98UbiquitinationAPSVENVKNGIRTGF
CCCHHHHHCCCCCCC
62.1222790023
135PhosphorylationTAVGVLISPQHTYFI
CEEEEEECCCCEEEE
17.85-
181PhosphorylationRIQNAGGSVMIQRVN
HHHHCCCCEEEEEEC
13.9529514104
190PhosphorylationMIQRVNGSLAVSRAL
EEEEECCCHHHHHHH
14.1422324799
194PhosphorylationVNGSLAVSRALGDFD
ECCCHHHHHHHCCCC
13.2622324799
216PhosphorylationGPTEQLVSPEPEVHD
CCHHHCCCCCCCCCC
31.9420415495
277PhosphorylationEVVDTCLYKGSRDNM
HHHHHHHHCCCCCCE
18.5621454597
280PhosphorylationDTCLYKGSRDNMSVI
HHHHHCCCCCCEEEE
32.1021454597
310AcetylationKKEAELDKYLESRVE
HHHHHHHHHHHHHHH
65.4423954790
322UbiquitinationRVEEIIKKQVEGVPD
HHHHHHHHHHCCCCH
49.5222790023
368PhosphorylationVYNRLNPYKNDDTDS
HHHHHCCCCCCCCCC
22.7329899451
373PhosphorylationNPYKNDDTDSASTDD
CCCCCCCCCCCCCCC
34.4223737553
375PhosphorylationYKNDDTDSASTDDMW
CCCCCCCCCCCCCCC
26.6423684622
377PhosphorylationNDDTDSASTDDMW--
CCCCCCCCCCCCC--
36.0023088624
378PhosphorylationDDTDSASTDDMW---
CCCCCCCCCCCC---
35.4223737553
381OxidationDSASTDDMW------
CCCCCCCCC------
5.2117242355

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
375SPhosphorylationKinaseCSNK2A1Q60737
GPS
377SPhosphorylationKinaseCSNK2A1Q60737
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPM1A_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 PPM1A_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PPM1A_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND MASSSPECTROMETRY.

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