PP1R8_HUMAN - dbPTM
PP1R8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PP1R8_HUMAN
UniProt AC Q12972
Protein Name Nuclear inhibitor of protein phosphatase 1
Gene Name PPP1R8
Organism Homo sapiens (Human).
Sequence Length 351
Subcellular Localization Nucleus. Nucleus speckle. Primarily, but not exclusively, nuclear.
Isoform Gamma: Cytoplasm. Found mainly in the cytoplasm.
Protein Description Inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. May also be involved in pre-mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.; Isoform Gamma is a site-specific single-strand endoribonuclease that cleaves single strand RNA 3' to purines and pyrimidines in A+U-rich regions. It generates 5'-phosphate termini at the site of cleavage. This isoform does not inhibit PP-1. May be implicated in mRNA splicing..
Protein Sequence MAAAANSGSSLPLFDCPTWAGKPPPGLHLDVVKGDKLIEKLIIDEKKYYLFGRNPDLCDFTIDHQSCSRVHAALVYHKHLKRVFLIDLNSTHGTFLGHIRLEPHKPQQIPIDSTVSFGASTRAYTLREKPQTLPSAVKGDEKMGGEDDELKGLLGLPEEETELDNLTEFNTAHNKRISTLTIEEGNLDIQRPKRKRKNSRVTFSEDDEIINPEDVDPSVGRFRNMVQTAVVPVKKKRVEGPGSLGLEESGSRRMQNFAFSGGLYGGLPPTHSEAGSQPHGIHGTALIGGLPMPYPNLAPDVDLTPVVPSAVNMNPAPNPAVYNPEAVNEPKKKKYAKEAWPGKKPTPSLLI
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
19 (in isoform 2)Phosphorylation-6.53-
19 (in isoform 3)Phosphorylation-6.53-
25 (in isoform 3)Phosphorylation-67.51-
36 (in isoform 2)Phosphorylation-61.09-
40AcetylationKGDKLIEKLIIDEKK
ECCHHHHHHHCCCCC		37.6826822725
40 (in isoform 3)Phosphorylation-37.68-
57 (in isoform 2)Phosphorylation-2.96-
62 (in isoform 2)Phosphorylation-4.49-
101 (in isoform 2)Phosphorylation-13.69-
107 (in isoform 2)Phosphorylation-59.65-
111 (in isoform 3)Phosphorylation-7.54-
120PhosphorylationSTVSFGASTRAYTLR
CEEECCCCCCEEECC		20.8527251275
121PhosphorylationTVSFGASTRAYTLRE
EEECCCCCCEEECCC		20.8427251275
122 (in isoform 2)Phosphorylation-24.09-
124PhosphorylationFGASTRAYTLREKPQ
CCCCCCEEECCCCCC		11.7421406692
125PhosphorylationGASTRAYTLREKPQT
CCCCCEEECCCCCCC		20.5324719451
132PhosphorylationTLREKPQTLPSAVKG
ECCCCCCCCCCCCCC		49.5221406692
135PhosphorylationEKPQTLPSAVKGDEK
CCCCCCCCCCCCCHH		49.1321406692
138SumoylationQTLPSAVKGDEKMGG
CCCCCCCCCCHHCCC		61.43-
151SumoylationGGEDDELKGLLGLPE
CCCCHHHHHHHCCCH		45.52-
161PhosphorylationLGLPEEETELDNLTE
HCCCHHHHHHHHHHC		45.169407077
175UbiquitinationEFNTAHNKRISTLTI
CHHHHCCCCCEEEEE		41.04-
178PhosphorylationTAHNKRISTLTIEEG
HHCCCCCEEEEEECC		22.7726055452
179PhosphorylationAHNKRISTLTIEEGN
HCCCCCEEEEEECCC		26.0830576142
181PhosphorylationNKRISTLTIEEGNLD
CCCCEEEEEECCCCC		26.8220068231
193 (in isoform 2)Phosphorylation-73.13-
193SumoylationNLDIQRPKRKRKNSR
CCCCCCCCCCCCCCC		73.13-
199PhosphorylationPKRKRKNSRVTFSED
CCCCCCCCCCCCCCC		31.0325159151
202PhosphorylationKRKNSRVTFSEDDEI
CCCCCCCCCCCCCCC		21.9729507054
204PhosphorylationKNSRVTFSEDDEIIN
CCCCCCCCCCCCCCC		30.6525159151
218PhosphorylationNPEDVDPSVGRFRNM
CHHHCCCCHHHHHHH		32.5127251275
225SulfoxidationSVGRFRNMVQTAVVP
CHHHHHHHEEEEEEE		1.7421406390
228PhosphorylationRFRNMVQTAVVPVKK
HHHHHEEEEEEEEEC		15.2620068231
234AcetylationQTAVVPVKKKRVEGP
EEEEEEEECCCCCCC		46.6525953088
236MethylationAVVPVKKKRVEGPGS
EEEEEECCCCCCCCC		56.83116252631
243PhosphorylationKRVEGPGSLGLEESG
CCCCCCCCCCCCCCC		23.5420068231
249PhosphorylationGSLGLEESGSRRMQN
CCCCCCCCCCHHCEE		32.4720068231
251PhosphorylationLGLEESGSRRMQNFA
CCCCCCCCHHCEEEE		26.4520068231
264PhosphorylationFAFSGGLYGGLPPTH
EEECCCCCCCCCCCC		16.6611104670
284O-linked_GlycosylationQPHGIHGTALIGGLP
CCCCCCCCEEECCCC		12.2528510447
335PhosphorylationNEPKKKKYAKEAWPG
CCCCHHHCCHHHCCC		31.6110827081
343AcetylationAKEAWPGKKPTPSLL
CHHHCCCCCCCCCCC		52.0425953088
346PhosphorylationAWPGKKPTPSLLI--
HCCCCCCCCCCCC--		34.1023312004
348PhosphorylationPGKKPTPSLLI----
CCCCCCCCCCC----		37.9828555341
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
161TPhosphorylationKinaseCK2-FAMILY-GPS
161TPhosphorylationKinaseCK2_GROUP-PhosphoELM
178SPhosphorylationKinasePKA-FAMILY-GPS
178SPhosphorylationKinasePKA_GROUP-PhosphoELM
199SPhosphorylationKinasePKA-FAMILY-GPS
199SPhosphorylationKinasePKA_GROUP-PhosphoELM
204SPhosphorylationKinaseCK2-FAMILY-GPS
204SPhosphorylationKinaseCK2_GROUP-PhosphoELM
264YPhosphorylationKinaseLYNP07948
Uniprot
335YPhosphorylationKinaseLYNP07948
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
199SPhosphorylation

11034904
204SPhosphorylation

11034904
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 PP1R8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EED_HUMANEEDphysical
12788942
HDAC2_HUMANHDAC2physical
12788942
DPYL1_HUMANCRMP1physical
16169070
SETB1_HUMANSETDB1physical
16169070
ERG28_HUMANC14orf1physical
16169070
RBM48_HUMANRBM48physical
16169070
GBP2_HUMANGBP2physical
16169070
STC2_HUMANSTC2physical
16169070
SF3B1_HUMANSF3B1physical
12105215
PP1G_HUMANPPP1CCphysical
11104670
EZH2_HUMANEZH2physical
17804093
EED_HUMANEEDphysical
17804093
PP1A_HUMANPPP1CAphysical
20671031
EZH2_HUMANEZH2physical
20671031
SUZ12_HUMANSUZ12physical
20671031
RBBP4_HUMANRBBP4physical
20671031
PP1A_HUMANPPP1CAphysical
20516061
PP1B_HUMANPPP1CBphysical
20516061
PP1G_HUMANPPP1CCphysical
20516061
A4_HUMANAPPphysical
21832049
CTBL1_HUMANCTNNBL1physical
22365833
PPIL1_HUMANPPIL1physical
22365833
PP1A_HUMANPPP1CAphysical
22365833
MEP50_HUMANWDR77physical
22365833
HMGA1_HUMANHMGA1physical
18850631
APBP2_HUMANAPPBP2physical
25416956
DDX1_HUMANDDX1physical
26344197
FA98B_HUMANFAM98Bphysical
26344197
PP1A_HUMANPPP1CAphysical
26344197
PP1G_HUMANPPP1CCphysical
26344197
SHC1_HUMANSHC1physical
26344197
GLYM_HUMANSHMT2physical
26344197
SPN1_HUMANSNUPNphysical
26344197
VPS4B_HUMANVPS4Bphysical
26344197
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 PP1R8_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The C-terminus of NIPP1 (nuclear inhibitor of protein phosphatase-1)contains a novel binding site for protein phosphatase-1 that iscontrolled by tyrosine phosphorylation and RNA binding.";
Beullens M., Vulsteke V., Van Eynde A., Jagiello I., Stalmans W.,Bollen M.;
Biochem. J. 352:651-658(2000).
Cited for: FUNCTION, MUTAGENESIS OF TYR-264; TYR-335; THR-346 AND SER-348, ANDPHOSPHORYLATION AT TYR-264 AND TYR-335.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory