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Protein

Nuclear inhibitor of protein phosphatase 1

Gene

Ppp1r8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Essential for cell proliferation and early embryonic development.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Protein phosphatase inhibitor, Repressor

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear inhibitor of protein phosphatase 1
Short name:
NIPP-1
Alternative name(s):
Protein phosphatase 1 regulatory inhibitor subunit 8
Gene namesi
Name:Ppp1r8
Synonyms:Nipp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2140494. Ppp1r8.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Disruption phenotypei

Mice display a retarded growth and embryonic lethality at E6.5, due to defects in proliferation rate.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000715061 – 351Nuclear inhibitor of protein phosphatase 1Add BLAST351

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei161PhosphothreonineBy similarity1
Modified residuei178PhosphoserineBy similarity1
Modified residuei199PhosphoserineBy similarity1
Modified residuei249PhosphoserineBy similarity1
Modified residuei264PhosphotyrosineBy similarity1

Post-translational modificationi

May be inactivated by phosphorylation on Ser-199 or Ser-204.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8R3G1.
MaxQBiQ8R3G1.
PaxDbiQ8R3G1.
PRIDEiQ8R3G1.

PTM databases

iPTMnetiQ8R3G1.
PhosphoSitePlusiQ8R3G1.

Expressioni

Gene expression databases

BgeeiENSMUSG00000028882.
ExpressionAtlasiQ8R3G1. baseline and differential.
GenevisibleiQ8R3G1. MM.

Interactioni

Subunit structurei

Interacts with phosphorylated CDC5L, SF3B1 and MELK. Part of the spliceosome. Interacts with PPP1CA, PPP1CB and PPP1CC (By similarity). Interacts with EED. Part of a complex consisting of PPP1R8, EED, HDAC2 and PP-1.By similarity2 Publications

Protein-protein interaction databases

IntActiQ8R3G1. 1 interactor.
MINTiMINT-4119004.
STRINGi10090.ENSMUSP00000030702.

Structurei

Secondary structure

1351
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 9Combined sources3
Beta strandi18 – 20Combined sources3
Beta strandi28 – 41Combined sources14
Beta strandi51 – 53Combined sources3
Turni55 – 57Combined sources3
Beta strandi58 – 60Combined sources3
Beta strandi65 – 67Combined sources3
Beta strandi71 – 80Combined sources10
Beta strandi83 – 86Combined sources4
Beta strandi94 – 98Combined sources5
Beta strandi103 – 105Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JPENMR-A1-132[»]
ProteinModelPortaliQ8R3G1.
SMRiQ8R3G1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8R3G1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini49 – 101FHAPROSITE-ProRule annotationAdd BLAST53

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 142Interaction with CDC5L, SF3B1 and MELKBy similarityAdd BLAST142
Regioni143 – 224Interaction with EEDBy similarityAdd BLAST82
Regioni191 – 200Involved in PP-1 inhibitionBy similarity10
Regioni200 – 203Involved in PP-1 bindingBy similarity4
Regioni310 – 329Interaction with EEDBy similarityAdd BLAST20
Regioni330 – 351RNA-bindingBy similarityAdd BLAST22
Regioni331 – 337Involved in PP-1 inhibitionBy similarity7

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi185 – 209Nuclear localization signal 1By similarityAdd BLAST25
Motifi210 – 240Nuclear localization signal 2By similarityAdd BLAST31

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 5Poly-Ala4
Compositional biasi331 – 334Poly-Lys4

Domaini

Has a basic N- and C-terminal and an acidic central domain.1 Publication
The FHA domain mediates interactions with threonine-phosphorylated MELK.1 Publication

Sequence similaritiesi

Contains 1 FHA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1880. Eukaryota.
ENOG410XTHZ. LUCA.
GeneTreeiENSGT00730000110659.
HOGENOMiHOG000231315.
HOVERGENiHBG053645.
InParanoidiQ8R3G1.
KOiK13216.
OMAiMNPTPNP.
OrthoDBiEOG091G0D26.
PhylomeDBiQ8R3G1.
TreeFamiTF105539.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R3G1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAVNSGSS LPLFDCPTWA GKPPPGLHLD VVKGDKLIEK LIIDEKKYYL
60 70 80 90 100
FGRNPDLCDF TIDHQSCSRV HAALVYHKHL KRVFLIDLNS THGTFLGHIR
110 120 130 140 150
LEPHKPQQIP IDSTVSFGAS TRAYTLREKP QTLPSAVKGD EKMGGEDDEL
160 170 180 190 200
KGLLGLPEEE TELDNLTEFN TAHNKRISTL TIEEGNLDIQ RPKRKRKNSR
210 220 230 240 250
VTFSEDDEII NPEDVDPSVG RFRNMVQTAV VPVKKKRMEG SGSLGLEESG
260 270 280 290 300
SRRMQNFAFS GGLYGGLPPT HSETGSQPHG IHGTALIGGL PMPYPNLAPD
310 320 330 340 350
VDLTPVVPSA VAINPTPNPA VYNPEAVNEP KKKKYAKEAW PGKKPTPSLL

I
Length:351
Mass (Da):38,528
Last modified:June 1, 2002 - v1
Checksum:iD3A3BC4B2DF467A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC025479 mRNA. Translation: AAH25479.1.
AK032022 mRNA. Translation: BAC27653.1.
CCDSiCCDS18736.1.
RefSeqiNP_001277654.1. NM_001290725.1.
NP_666266.1. NM_146154.3.
UniGeneiMm.105230.

Genome annotation databases

EnsembliENSMUST00000030702; ENSMUSP00000030702; ENSMUSG00000028882.
GeneIDi100336.
KEGGimmu:100336.
UCSCiuc008vbw.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC025479 mRNA. Translation: AAH25479.1.
AK032022 mRNA. Translation: BAC27653.1.
CCDSiCCDS18736.1.
RefSeqiNP_001277654.1. NM_001290725.1.
NP_666266.1. NM_146154.3.
UniGeneiMm.105230.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JPENMR-A1-132[»]
ProteinModelPortaliQ8R3G1.
SMRiQ8R3G1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R3G1. 1 interactor.
MINTiMINT-4119004.
STRINGi10090.ENSMUSP00000030702.

PTM databases

iPTMnetiQ8R3G1.
PhosphoSitePlusiQ8R3G1.

Proteomic databases

EPDiQ8R3G1.
MaxQBiQ8R3G1.
PaxDbiQ8R3G1.
PRIDEiQ8R3G1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030702; ENSMUSP00000030702; ENSMUSG00000028882.
GeneIDi100336.
KEGGimmu:100336.
UCSCiuc008vbw.3. mouse.

Organism-specific databases

CTDi5511.
MGIiMGI:2140494. Ppp1r8.

Phylogenomic databases

eggNOGiKOG1880. Eukaryota.
ENOG410XTHZ. LUCA.
GeneTreeiENSGT00730000110659.
HOGENOMiHOG000231315.
HOVERGENiHBG053645.
InParanoidiQ8R3G1.
KOiK13216.
OMAiMNPTPNP.
OrthoDBiEOG091G0D26.
PhylomeDBiQ8R3G1.
TreeFamiTF105539.

Miscellaneous databases

EvolutionaryTraceiQ8R3G1.
PROiQ8R3G1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028882.
ExpressionAtlasiQ8R3G1. baseline and differential.
GenevisibleiQ8R3G1. MM.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPP1R8_MOUSE
AccessioniPrimary (citable) accession number: Q8R3G1
Secondary accession number(s): Q8C087
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2002
Last modified: November 2, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.