PPM1D_HUMAN - dbPTM
PPM1D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPM1D_HUMAN
UniProt AC O15297
Protein Name Protein phosphatase 1D
Gene Name PPM1D
Organism Homo sapiens (Human).
Sequence Length 605
Subcellular Localization Nucleus . Cytoplasm, cytosol .
Protein Description Involved in the negative regulation of p53 expression. [PubMed: 23242139 Required for the relief of p53-dependent checkpoint mediated cell cycle arrest. Binds to and dephosphorylates 'Ser-15' of TP53 and 'Ser-345' of CHEK1 which contributes to the functional inactivation of these proteins]
Protein Sequence MAGLYSLGVSVFSDQGGRKYMEDVTQIVVEPEPTAEEKPSPRRSLSQPLPPRPSPAALPGGEVSGKGPAVAAREARDPLPDAGASPAPSRCCRRRSSVAFFAVCDGHGGREAAQFAREHLWGFIKKQKGFTSSEPAKVCAAIRKGFLACHLAMWKKLAEWPKTMTGLPSTSGTTASVVIIRGMKMYVAHVGDSGVVLGIQDDPKDDFVRAVEVTQDHKPELPKERERIEGLGGSVMNKSGVNRVVWKRPRLTHNGPVRRSTVIDQIPFLAVARALGDLWSYDFFSGEFVVSPEPDTSVHTLDPQKHKYIILGSDGLWNMIPPQDAISMCQDQEEKKYLMGEHGQSCAKMLVNRALGRWRQRMLRADNTSAIVICISPEVDNQGNFTNEDELYLNLTDSPSYNSQETCVMTPSPCSTPPVKSLEEDPWPRVNSKDHIPALVRSNAFSENFLEVSAEIARENVQGVVIPSKDPEPLEENCAKALTLRIHDSLNNSLPIGLVPTNSTNTVMDQKNLKMSTPGQMKAQEIERTPPTNFKRTLEESNSGPLMKKHRRNGLSRSSGAQPASLPTTSQRKNSVKLTMRRRLRGQKKIGNPLLHQHRKTVCVC
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
10PhosphorylationGLYSLGVSVFSDQGG
CCEECEEEEECCCCC		18.69-
19UbiquitinationFSDQGGRKYMEDVTQ
ECCCCCCCCCEEEEE		52.8321890473
25PhosphorylationRKYMEDVTQIVVEPE
CCCCEEEEEEEECCC		25.5426074081
34PhosphorylationIVVEPEPTAEEKPSP
EEECCCCCCCCCCCC		45.0723663014
40PhosphorylationPTAEEKPSPRRSLSQ
CCCCCCCCCCCCCCC		41.9530266825
44PhosphorylationEKPSPRRSLSQPLPP
CCCCCCCCCCCCCCC		33.3830266825
46PhosphorylationPSPRRSLSQPLPPRP
CCCCCCCCCCCCCCC		30.8830266825
54PhosphorylationQPLPPRPSPAALPGG
CCCCCCCCCCCCCCC		28.5730266825
64PhosphorylationALPGGEVSGKGPAVA
CCCCCCCCCCCHHHH		30.4123312004
66AcetylationPGGEVSGKGPAVAAR
CCCCCCCCCHHHHCH		54.9726051181
85PhosphorylationPLPDAGASPAPSRCC
CCCCCCCCCCCHHHC		22.2223242139
89PhosphorylationAGASPAPSRCCRRRS
CCCCCCCHHHCCCCC		39.8030266825
96PhosphorylationSRCCRRRSSVAFFAV
HHHCCCCCCEEEEEE		27.6130266825
97PhosphorylationRCCRRRSSVAFFAVC
HHCCCCCCEEEEEEE		18.6930266825
162AcetylationKKLAEWPKTMTGLPS
HHHHHCCCHHCCCCC		52.597491787
184AcetylationVVIIRGMKMYVAHVG
EEEECCCEEEEEEEC		29.887491797
218UbiquitinationVEVTQDHKPELPKER
EEECCCCCCCCCHHH		48.77-
223UbiquitinationDHKPELPKERERIEG
CCCCCCCHHHHHHCC		80.28-
234PhosphorylationRIEGLGGSVMNKSGV
HHCCCCCCCCCCCCC		19.18-
238UbiquitinationLGGSVMNKSGVNRVV
CCCCCCCCCCCCCEE		30.4121890473
238UbiquitinationLGGSVMNKSGVNRVV
CCCCCCCCCCCCCEE		30.4121890473
238UbiquitinationLGGSVMNKSGVNRVV
CCCCCCCCCCCCCEE		30.4121890473
239PhosphorylationGGSVMNKSGVNRVVW
CCCCCCCCCCCCEEE		42.86-
260PhosphorylationHNGPVRRSTVIDQIP
CCCCCCCCHHHHHHH		19.2327050516
308PhosphorylationLDPQKHKYIILGSDG
CCCCCCEEEEECCCC		7.9122817900
432PhosphorylationDPWPRVNSKDHIPAL
CCCCCCCCCCCHHHH		36.2825849741
468PhosphorylationVQGVVIPSKDPEPLE
CCEEEECCCCCCCHH		38.2724719451
469UbiquitinationQGVVIPSKDPEPLEE
CEEEECCCCCCCHHH		72.45-
517PhosphorylationQKNLKMSTPGQMKAQ
CCCCCCCCCCCHHHH		28.13-
529PhosphorylationKAQEIERTPPTNFKR
HHHHHCCCCCCCHHH		22.3425849741
535MethylationRTPPTNFKRTLEESN
CCCCCCHHHHHHHCC		46.68115975533
537O-linked_GlycosylationPPTNFKRTLEESNSG
CCCCHHHHHHHCCCC		38.8330379171
537PhosphorylationPPTNFKRTLEESNSG
CCCCHHHHHHHCCCC		38.8325278378
541PhosphorylationFKRTLEESNSGPLMK
HHHHHHHCCCCCCCH		27.2421712546
543PhosphorylationRTLEESNSGPLMKKH
HHHHHCCCCCCCHHH		51.5825849741
547SulfoxidationESNSGPLMKKHRRNG
HCCCCCCCHHHHHCC		6.4721406390
558PhosphorylationRRNGLSRSSGAQPAS
HHCCCCCCCCCCCCC		29.7325849741
559PhosphorylationRNGLSRSSGAQPASL
HCCCCCCCCCCCCCC		36.7225849741
565PhosphorylationSSGAQPASLPTTSQR
CCCCCCCCCCCCCCC		41.38-
568PhosphorylationAQPASLPTTSQRKNS
CCCCCCCCCCCCCCH		44.3522210691
570PhosphorylationPASLPTTSQRKNSVK
CCCCCCCCCCCCHHH		30.39-
589UbiquitinationRRLRGQKKIGNPLLH
HHHCCCCCCCCCCCC		48.21-
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
54SPhosphorylationKinaseHIPK2Q9H2X6
PSP
85SPhosphorylationKinaseHIPK2Q9H2X6
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPM1D_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 PPM1D_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MDM2_HUMANMDM2physical
17936559
H2AX_HUMANH2AFXphysical
20101220
H2AX_HUMANH2AFXphysical
20460517
H2AX_HUMANH2AFXphysical
20118229
RAD21_HUMANRAD21physical
22145905
KDM1A_HUMANKDM1Aphysical
25999347
BEX2_HUMANBEX2physical
25640309
CASZ1_HUMANCASZ1physical
25640309
DIRA3_HUMANDIRAS3physical
25640309
DKK3_HUMANDKK3physical
25640309
ESIP1_HUMANEPSTI1physical
25640309
ERRFI_HUMANERRFI1physical
25640309
GLCE_HUMANGLCEphysical
25640309
ITIH5_HUMANITIH5physical
25640309
LYPD3_HUMANLYPD3physical
25640309
MRC2_HUMANMRC2physical
25640309
ARY2_HUMANNAT2physical
25640309
OSGI1_HUMANOSGIN1physical
25640309
RHBT2_HUMANRHOBTB2physical
25640309
NSD3_HUMANWHSC1L1physical
25640309
IMA1_HUMANKPNA2physical
27880917
IMA4_HUMANKPNA3physical
27880917
IMB1_HUMANKPNB1physical
27880917
NU153_HUMANNUP153physical
27880917
PSMD4_HUMANPSMD4physical
27880917
RBP2_HUMANRANBP2physical
27880917
JIP4_HUMANSPAG9physical
27880917
CHK2_HUMANCHEK2physical
16311512
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 PPM1D_HUMAN

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Related Literatures of Post-Translational Modification
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-40, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASSSPECTROMETRY.

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