PPM1A_HUMAN - dbPTM
PPM1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPM1A_HUMAN
UniProt AC P35813
Protein Name Protein phosphatase 1A
Gene Name PPM1A
Organism Homo sapiens (Human).
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. 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 MGAFLDKPKMEKHNAQGQGNGLRYGLSSMQGWRVEMEDAHTAVIGLPSGLESWSFFAVYDGHAGSQVAKYCCEHLLDHITNNQDFKGSAGAPSVENVKNGIRTGFLEIDEHMRVMSEKKHGADRSGSTAVGVLISPQHTYFINCGDSRGLLCRNRKVHFFTQDHKPSNPLEKERIQNAGGSVMIQRVNGSLAVSRALGDFDYKCVHGKGPTEQLVSPEPEVHDIERSEEDDQFIILACDGIWDVMGNEELCDFVRSRLEVTDDLEKVCNEVVDTCLYKGSRDNMSVILICFPNAPKVSPEAVKKEAELDKYLECRVEEIIKKQGEGVPDLVHVMRTLASENIPSLPPGGELASKRNVIEAVYNRLNPYKNDDTDSTSTDDMW
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		25.6520213681
2N-myristoyl glycine------MGAFLDKPK
------CCCCCCCHH		25.65-
86UbiquitinationITNNQDFKGSAGAPS
HHCCCCCCCCCCCCC		61.31-
98UbiquitinationAPSVENVKNGIRTGF
CCCHHHHHCCCCCCC		62.12-
112SulfoxidationFLEIDEHMRVMSEKK
CEEHHHHHHHHHHHC		3.0421406390
116PhosphorylationDEHMRVMSEKKHGAD
HHHHHHHHHHCCCCC		43.3324719451
165UbiquitinationHFFTQDHKPSNPLEK
EEECCCCCCCCHHHH		59.43-
181PhosphorylationRIQNAGGSVMIQRVN
HHHHCCCCEEEEEEC		13.9528857561
189PhosphorylationVMIQRVNGSLAVSRA
EEEEEECCCHHHHHH		22.6024719451
190PhosphorylationMIQRVNGSLAVSRAL
EEEEECCCHHHHHHH		14.1426699800
194PhosphorylationVNGSLAVSRALGDFD
ECCCHHHHHHHCCCC		13.2621406692
203UbiquitinationALGDFDYKCVHGKGP
HHCCCCEEECCCCCC		31.46-
261O-linked_GlycosylationVRSRLEVTDDLEKVC
HHHHCCCCHHHHHHH		17.8923301498
263PhosphorylationSRLEVTDDLEKVCNE
HHCCCCHHHHHHHHH		47.5724719451
278UbiquitinationVVDTCLYKGSRDNMS
HHHHHHHCCCCCCEE		37.14-
285PhosphorylationKGSRDNMSVILICFP
CCCCCCEEEEEEECC		16.56-
298PhosphorylationFPNAPKVSPEAVKKE
CCCCCCCCHHHHHHH		24.1326437602
310UbiquitinationKKEAELDKYLECRVE
HHHHHHHHHHHHHHH		65.44-
311PhosphorylationKEAELDKYLECRVEE
HHHHHHHHHHHHHHH		13.85-
362PhosphorylationRNVIEAVYNRLNPYK
HHHHHHHHHHHCCCC		11.1226074081
368PhosphorylationVYNRLNPYKNDDTDS
HHHHHCCCCCCCCCC		22.7326074081
373PhosphorylationNPYKNDDTDSTSTDD
CCCCCCCCCCCCCCC		34.4128450419
375PhosphorylationYKNDDTDSTSTDDMW
CCCCCCCCCCCCCCC		26.7522617229
376PhosphorylationKNDDTDSTSTDDMW-
CCCCCCCCCCCCCC-		38.1630576142
377PhosphorylationNDDTDSTSTDDMW--
CCCCCCCCCCCCC--		33.5222115753
378PhosphorylationDDTDSTSTDDMW---
CCCCCCCCCCCC---		35.7928450419
435Phosphorylation------------------------------------------------------------
------------------------------------------------------------		27642862
441Phosphorylation------------------------------------------------------------------
------------------------------------------------------------------		27642862
448Phosphorylation-------------------------------------------------------------------------
-------------------------------------------------------------------------		24719451
451Phosphorylation----------------------------------------------------------------------------
----------------------------------------------------------------------------		27251275
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 PPM1A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPM1A_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 PPM1A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RLA0_HUMANRPLP0physical
21988832
AAPK1_HUMANPRKAA1physical
20801214
INT14_HUMANVWA9physical
26186194
SHIP2_HUMANINPPL1physical
26186194
PPM1B_HUMANPPM1Bphysical
26186194
RTEL1_HUMANRTEL1physical
26186194
CHK1_HUMANCHEK1physical
26344197
M4K5_HUMANMAP4K5physical
26344197
NAA10_HUMANNAA10physical
26344197
BCKD_HUMANBCKDKphysical
27880917
FANCI_HUMANFANCIphysical
27880917
GCN1_HUMANGCN1L1physical
27880917
DHB4_HUMANHSD17B4physical
27880917
HSDL2_HUMANHSDL2physical
27880917
IWS1_HUMANIWS1physical
27880917
LETM1_HUMANLETM1physical
27880917
PAK4_HUMANPAK4physical
27880917
ADT2_HUMANSLC25A5physical
27880917
SLN11_HUMANSLFN11physical
27880917
UGGG1_HUMANUGGT1physical
27880917
PPM1B_HUMANPPM1Bphysical
28514442
SHIP2_HUMANINPPL1physical
28514442
SYQ_HUMANQARSphysical
28514442
RTEL1_HUMANRTEL1physical
28514442
PAK1_HUMANPAK1physical
18586681
PAK2_HUMANPAK2physical
18586681
MRCKA_HUMANCDC42BPAphysical
18586681
MRCKB_HUMANCDC42BPBphysical
18586681
KPCA_HUMANPRKCAphysical
18586681
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 PPM1A_HUMAN

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"Strategy for comprehensive identification of human N-myristoylatedproteins using an insect cell-free protein synthesis system.";
Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,Tsunasawa S., Utsumi T.;
Proteomics 10:1780-1793(2010).
Cited for: MYRISTOYLATION AT GLY-2.
Phosphorylation
ReferencePubMed
"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-375, AND MASSSPECTROMETRY.

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