PPM1H_HUMAN - dbPTM
PPM1H_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPM1H_HUMAN
UniProt AC Q9ULR3
Protein Name Protein phosphatase 1H
Gene Name PPM1H
Organism Homo sapiens (Human).
Sequence Length 514
Subcellular Localization Nucleus . Cytoplasm .
Protein Description Dephosphorylates CDKN1B at 'Thr-187', thus removing a signal for proteasomal degradation..
Protein Sequence MLTRVKSAVANFMGGIMAGSSGSEHGGGSCGGSDLPLRFPYGRPEFLGLSQDEVECSADHIARPILILKETRRLPWATGYAEVINAGKSTHNEDQASCEVLTVKKKAGAVTSTPNRNSSKRRSSLPNGEGLQLKENSESEGVSCHYWSLFDGHAGSGAAVVASRLLQHHITEQLQDIVDILKNSAVLPPTCLGEEPENTPANSRTLTRAASLRGGVGAPGSPSTPPTRFFTEKKIPHECLVIGALESAFKEMDLQIERERSSYNISGGCTALIVICLLGKLYVANAGDSRAIIIRNGEIIPMSSEFTPETERQRLQYLAFMQPHLLGNEFTHLEFPRRVQRKELGKKMLYRDFNMTGWAYKTIEDEDLKFPLIYGEGKKARVMATIGVTRGLGDHDLKVHDSNIYIKPFLSSAPEVRIYDLSKYDHGSDDVLILATDGLWDVLSNEEVAEAITQFLPNCDPDDPHRYTLAAQDLVMRARGVLKDRGWRISNDRLGSGDDISVYVIPLIHGNKLS
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
7Phosphorylation-MLTRVKSAVANFMG
-CCHHHHHHHHHHHC
25.7228857561
95UbiquitinationKSTHNEDQASCEVLT
CCCCCCCCCCCEEEE
29.0624816145
104UbiquitinationSCEVLTVKKKAGAVT
CCEEEEEEECCCCCC
43.2329967540
111PhosphorylationKKKAGAVTSTPNRNS
EECCCCCCCCCCCCC
26.7528152594
112PhosphorylationKKAGAVTSTPNRNSS
ECCCCCCCCCCCCCC
34.9628102081
113PhosphorylationKAGAVTSTPNRNSSK
CCCCCCCCCCCCCCC
18.4123401153
118PhosphorylationTSTPNRNSSKRRSSL
CCCCCCCCCCCCCCC
33.7225159151
119PhosphorylationSTPNRNSSKRRSSLP
CCCCCCCCCCCCCCC
33.4625262027
123PhosphorylationRNSSKRRSSLPNGEG
CCCCCCCCCCCCCCC
40.0123401153
124PhosphorylationNSSKRRSSLPNGEGL
CCCCCCCCCCCCCCE
46.1429255136
199PhosphorylationLGEEPENTPANSRTL
CCCCCCCCCCCCHHH
23.3226074081
203PhosphorylationPENTPANSRTLTRAA
CCCCCCCCHHHHHHH
28.8426074081
205PhosphorylationNTPANSRTLTRAASL
CCCCCCHHHHHHHHH
32.1026074081
207PhosphorylationPANSRTLTRAASLRG
CCCCHHHHHHHHHCC
20.0426074081
211PhosphorylationRTLTRAASLRGGVGA
HHHHHHHHHCCCCCC
20.0223401153
213MethylationLTRAASLRGGVGAPG
HHHHHHHCCCCCCCC
37.0116186173
221PhosphorylationGGVGAPGSPSTPPTR
CCCCCCCCCCCCCCC
18.0223401153
223PhosphorylationVGAPGSPSTPPTRFF
CCCCCCCCCCCCCCC
56.0729255136
224PhosphorylationGAPGSPSTPPTRFFT
CCCCCCCCCCCCCCC
36.3529255136
227PhosphorylationGSPSTPPTRFFTEKK
CCCCCCCCCCCCCCC
41.1129255136
289PhosphorylationYVANAGDSRAIIIRN
HHCCCCCCCEEEEEC
23.77-
308UbiquitinationPMSSEFTPETERQRL
CCCCCCCCHHHHHHH
52.4024816145
342AcetylationFPRRVQRKELGKKML
CCHHHHHHHHHHHHH
39.9522361687
346UbiquitinationVQRKELGKKMLYRDF
HHHHHHHHHHHHHHH
47.8624816145
346AcetylationVQRKELGKKMLYRDF
HHHHHHHHHHHHHHH
47.8622361243
369UbiquitinationTIEDEDLKFPLIYGE
ECCCCCCCCCEEECC
58.2029967540
419PhosphorylationSAPEVRIYDLSKYDH
CCCEEEEEEHHHCCC
10.5618669648
422PhosphorylationEVRIYDLSKYDHGSD
EEEEEEHHHCCCCCC
26.6922586611
476SulfoxidationLAAQDLVMRARGVLK
HHHHHHHHHHHHHHH
3.4521406390
490PhosphorylationKDRGWRISNDRLGSG
HHCCEEECCCCCCCC
24.8924719451
496PhosphorylationISNDRLGSGDDISVY
ECCCCCCCCCCEEEE
43.5728348404

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPM1H_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 PPM1H_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BLM_HUMANBLMphysical
27880917
PPM1J_HUMANPPM1Jphysical
27880917
1433B_HUMANYWHABphysical
27880917
1433E_HUMANYWHAEphysical
27880917
1433G_HUMANYWHAGphysical
27880917
1433F_HUMANYWHAHphysical
27880917
1433T_HUMANYWHAQphysical
27880917
1433Z_HUMANYWHAZphysical
27880917
S12A4_HUMANSLC12A4physical
27880917
LCAP_HUMANLNPEPphysical
27880917
MPRI_HUMANIGF2Rphysical
27880917
STX16_HUMANSTX16physical
27880917
RHG01_HUMANARHGAP1physical
27880917
MIO_HUMANMIOSphysical
27880917
CBPD_HUMANCPDphysical
27880917
TPD52_HUMANTPD52physical
27880917
TPD54_HUMANTPD52L2physical
27880917
WDR11_HUMANWDR11physical
27880917
F91A1_HUMANFAM91A1physical
27880917
GOGA4_HUMANGOLGA4physical
27880917
VAMP2_HUMANVAMP2physical
27880917
S6A15_HUMANSLC6A15physical
27880917
LMAN1_HUMANLMAN1physical
27880917
VAMP3_HUMANVAMP3physical
27880917
TSC1_HUMANTSC1physical
27880917
TMF1_HUMANTMF1physical
27880917
SCAM1_HUMANSCAMP1physical
27880917
PGRC2_HUMANPGRMC2physical
27880917
ITB1_HUMANITGB1physical
27880917
KCTD3_HUMANKCTD3physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
LRFN1_HUMANLRFN1physical
27173435
CING_HUMANCGNphysical
27173435
DEN1A_HUMANDENND1Aphysical
27173435
SRGP2_HUMANSRGAP2physical
27173435
RTKN_HUMANRTKNphysical
27173435
MAST3_HUMANMAST3physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
LIMA1_HUMANLIMA1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
TESK2_HUMANTESK2physical
27173435
DCLK1_HUMANDCLK1physical
27173435
ZN638_HUMANZNF638physical
27173435
SIN1_HUMANMAPKAP1physical
27173435
HDAC4_HUMANHDAC4physical
27173435
NF1_HUMANNF1physical
27173435
SRS12_HUMANSRSF12physical
27173435
CBY1_HUMANCBY1physical
27173435
LPIN3_HUMANLPIN3physical
27173435
SYDE1_HUMANSYDE1physical
27173435
AGAP1_HUMANAGAP1physical
27173435
MPIP2_HUMANCDC25Bphysical
27173435
CDK16_HUMANCDK16physical
27173435
MPIP3_HUMANCDC25Cphysical
27173435
NADK_HUMANNADKphysical
27173435
GGYF2_HUMANGIGYF2physical
27173435
F110B_HUMANFAM110Bphysical
27173435
CAMP2_HUMANCAMSAP2physical
27173435
UBP21_HUMANUSP21physical
27173435
AN34A_HUMANANKRD34Aphysical
27173435
FA53C_HUMANFAM53Cphysical
27173435
M3K21_HUMANKIAA1804physical
27173435
TIAM1_HUMANTIAM1physical
27173435
NGAP_HUMANRASAL2physical
27173435
RGPS2_HUMANRALGPS2physical
27173435
PKHA7_HUMANPLEKHA7physical
27173435
F110A_HUMANFAM110Aphysical
27173435
KIF1C_HUMANKIF1Cphysical
27173435
NAV1_HUMANNAV1physical
27173435
TANC2_HUMANTANC2physical
27173435
MELK_HUMANMELKphysical
27173435
OSBL6_HUMANOSBPL6physical
27173435
STA13_HUMANSTARD13physical
27173435
RPTOR_HUMANRPTORphysical
27173435
DEP1B_HUMANDEPDC1Bphysical
27173435
HDAC7_HUMANHDAC7physical
27173435
LARP1_HUMANLARP1physical
27173435
TBC25_HUMANTBC1D25physical
27173435
PKHA5_HUMANPLEKHA5physical
27173435
INP5E_HUMANINPP5Ephysical
27173435

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 PPM1H_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-211, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-211; SER-221;THR-224; TYR-419 AND SER-422, AND MASS SPECTROMETRY.

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