PPM1B_HUMAN - dbPTM
PPM1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPM1B_HUMAN
UniProt AC O75688
Protein Name Protein phosphatase 1B
Gene Name PPM1B
Organism Homo sapiens (Human).
Sequence Length 479
Subcellular Localization Cytoplasm, cytosol . Membrane
Lipid-anchor . Weakly associates at the membrane and N-myristoylation mediates the membrane localization.
Protein Description Enzyme with a broad specificity. Dephosphorylates CDK2 and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB..
Protein Sequence MGAFLDKPKTEKHNAHGAGNGLRYGLSSMQGWRVEMEDAHTAVVGIPHGLEDWSFFAVYDGHAGSRVANYCSTHLLEHITTNEDFRAAGKSGSALELSVENVKNGIRTGFLKIDEYMRNFSDLRNGMDRSGSTAVGVMISPKHIYFINCGDSRAVLYRNGQVCFSTQDHKPCNPREKERIQNAGGSVMIQRVNGSLAVSRALGDYDYKCVDGKGPTEQLVSPEPEVYEILRAEEDEFIILACDGIWDVMSNEELCEYVKSRLEVSDDLENVCNWVVDTCLHKGSRDNMSIVLVCFSNAPKVSDEAVKKDSELDKHLESRVEEIMEKSGEEGMPDLAHVMRILSAENIPNLPPGGGLAGKRNVIEAVYSRLNPHRESDGASDEAEESGSQGKLVEALRQMRINHRGNYRQLLEEMLTSYRLAKVEGEESPAEPAATATSSNSDAGNPVTMQESHTESESGLAELDSSNEDAGTKMSGEKI
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
------CCCCCCCCC		25.6525255805
12UbiquitinationLDKPKTEKHNAHGAG
CCCCCCCCCCCCCCC		47.60-
27UbiquitinationNGLRYGLSSMQGWRV
CCHHHCHHHCCCEEE		21.2833845483
39UbiquitinationWRVEMEDAHTAVVGI
EEEEECCCCEEEECC		6.6632015554
89PhosphorylationNEDFRAAGKSGSALE
CHHHHHCCCCCCCEE		24.5532645325
90UbiquitinationEDFRAAGKSGSALEL
HHHHHCCCCCCCEEE		47.0933845483
91PhosphorylationDFRAAGKSGSALELS
HHHHCCCCCCCEEEE		36.7427251275
93PhosphorylationRAAGKSGSALELSVE
HHCCCCCCCEEEEHH		36.4527251275
103UbiquitinationELSVENVKNGIRTGF
EEEHHHHHCCCCCCC		62.1229967540
104UbiquitinationLSVENVKNGIRTGFL
EEHHHHHCCCCCCCC		47.0123000965
112UbiquitinationGIRTGFLKIDEYMRN
CCCCCCCHHHHHHHC		45.9423000965
116PhosphorylationGFLKIDEYMRNFSDL
CCCHHHHHHHCHHHH		9.5330576142
121PhosphorylationDEYMRNFSDLRNGMD
HHHHHCHHHHHCCCC		39.0130576142
135UbiquitinationDRSGSTAVGVMISPK
CCCCCCEEEEEECCC		6.3423503661
140PhosphorylationTAVGVMISPKHIYFI
CEEEEEECCCEEEEE		15.1424719451
163S-nitrosylationLYRNGQVCFSTQDHK
EEECCEEEEECCCCC		1.3922178444
172S-nitrosylationSTQDHKPCNPREKER
ECCCCCCCCHHHHHH		15.1522178444
186PhosphorylationRIQNAGGSVMIQRVN
HHHHCCCCEEEEEEC		13.9528857561
188SulfoxidationQNAGGSVMIQRVNGS
HHCCCCEEEEEECCC		2.0121406390
195PhosphorylationMIQRVNGSLAVSRAL
EEEEECCCCHHHHHH		14.1426699800
199PhosphorylationVNGSLAVSRALGDYD
ECCCCHHHHHHCCCC		13.2621406692
208UbiquitinationALGDYDYKCVDGKGP
HHCCCCCEECCCCCC		25.5333845483
265PhosphorylationVKSRLEVSDDLENVC
HHHHHCCCHHHHHHH		18.94-
289PhosphorylationKGSRDNMSIVLVCFS
CCCCCCEEEEEEEEC		18.7930243723
296PhosphorylationSIVLVCFSNAPKVSD
EEEEEEECCCCCCCH		27.2730243723
302PhosphorylationFSNAPKVSDEAVKKD
ECCCCCCCHHHHHHH		35.5430243723
3082-HydroxyisobutyrylationVSDEAVKKDSELDKH
CCHHHHHHHHHHHHH		60.94-
314UbiquitinationKKDSELDKHLESRVE
HHHHHHHHHHHHHHH		63.8133845483
326 (in isoform 1)Ubiquitination-46.5122053931
326 (in isoform 2)Ubiquitination-46.5121906983
326UbiquitinationRVEEIMEKSGEEGMP
HHHHHHHHHCCCCCC		46.5121906983
343PhosphorylationAHVMRILSAENIPNL
HHHHHHHCCCCCCCC		31.0327251275
367PhosphorylationRNVIEAVYSRLNPHR
HHHHHHHHHHHCCCC		8.6329978859
368PhosphorylationNVIEAVYSRLNPHRE
HHHHHHHHHHCCCCC		24.5629978859
376PhosphorylationRLNPHRESDGASDEA
HHCCCCCCCCCCHHH		41.1029255136
376 (in isoform 2)Phosphorylation-41.1028450419
380PhosphorylationHRESDGASDEAEESG
CCCCCCCCHHHHHHC		41.3229255136
386PhosphorylationASDEAEESGSQGKLV
CCHHHHHHCCHHHHH		34.9410934208
388PhosphorylationDEAEESGSQGKLVEA
HHHHHHCCHHHHHHH		45.0727542207
391UbiquitinationEESGSQGKLVEALRQ
HHHCCHHHHHHHHHH		41.5423000965
391 (in isoform 1)Ubiquitination-41.5422053931
399UbiquitinationLVEALRQMRINHRGN
HHHHHHHHCCCCCCC		3.6223000965
418PhosphorylationLEEMLTSYRLAKVEG
HHHHHHHHHHHHCCC		12.38-
422UbiquitinationLTSYRLAKVEGEESP
HHHHHHHHCCCCCCC		45.4723503661
430UbiquitinationVEGEESPAEPAATAT
CCCCCCCCCCCCCCC		44.6923503661
465PhosphorylationSGLAELDSSNEDAGT
CCCEECCCCCCCCCC		47.9222468782
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
195SPhosphorylationKinasePRKACAP17612
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPM1B_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 PPM1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRP1_HUMANRASGRP1physical
17353931
K1C18_HUMANKRT18physical
17353931
VILI_HUMANVIL1physical
17353931
S10A8_HUMANS100A8physical
17353931
GELS_HUMANGSNphysical
17353931
TERA_HUMANVCPphysical
17353931
PABP4_HUMANPABPC4physical
17353931
ANXA1_HUMANANXA1physical
17353931
ANXA2_HUMANANXA2physical
17353931
NEMO_HUMANIKBKGphysical
14585847
IKKB_HUMANIKBKBphysical
14585847
IKKA_HUMANCHUKphysical
14585847
CDK2_HUMANCDK2physical
10934208
CDK6_HUMANCDK6physical
10934208
M3K7_HUMANMAP3K7physical
11104763
UBL7_HUMANUBL7physical
22939629
PPARG_HUMANPPARGphysical
23320500
CSKP_HUMANCASKphysical
26344197
CDK1_HUMANCDK1physical
26344197
LRRK1_HUMANLRRK1physical
26344197
M4K5_HUMANMAP4K5physical
26344197
NAA10_HUMANNAA10physical
26344197
STK40_HUMANSTK40physical
26344197
IKKA_HUMANCHUKphysical
25241761
ACTS_HUMANACTA1physical
27880917
H2A1B_HUMANHIST1H2AEphysical
27880917
HSP72_HUMANHSPA2physical
27880917
SPTN1_HUMANSPTAN1physical
27880917
SPTB2_HUMANSPTBN1physical
27880917
VIME_HUMANVIMphysical
27880917
KIF15_HUMANKIF15physical
27880917
SYK_HUMANKARSphysical
27880917
HTR5A_HUMANHEATR5Aphysical
28514442
FEZ2_HUMANFEZ2physical
28514442
PMGE_HUMANBPGMphysical
28514442
THUM3_HUMANTHUMPD3physical
28514442
PAXX_HUMANC9orf142physical
28514442
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 PPM1B_HUMAN

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Related Literatures of Post-Translational Modification

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