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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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351Nuclear inhibitor of protein phosphatase 1PRO_0000071506Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei161 – 1611PhosphothreonineBy similarity
Modified residuei178 – 1781PhosphoserineBy similarity
Modified residuei199 – 1991PhosphoserineBy similarity
Modified residuei249 – 2491PhosphoserineBy similarity
Modified residuei264 – 2641PhosphotyrosineBy similarity

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.
PhosphoSiteiQ8R3G1.

Expressioni

Gene expression databases

BgeeiQ8R3G1.
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 interaction.
MINTiMINT-4119004.
STRINGi10090.ENSMUSP00000030702.

Structurei

Secondary structure

1
351
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93Combined sources
Beta strandi18 – 203Combined sources
Beta strandi28 – 4114Combined sources
Beta strandi51 – 533Combined sources
Turni55 – 573Combined sources
Beta strandi58 – 603Combined sources
Beta strandi65 – 673Combined sources
Beta strandi71 – 8010Combined sources
Beta strandi83 – 864Combined sources
Beta strandi94 – 985Combined sources
Beta strandi103 – 1053Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JPENMR-A1-132[»]
ProteinModelPortaliQ8R3G1.
SMRiQ8R3G1. Positions 1-132, 158-212.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8R3G1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 10153FHAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 142142Interaction with CDC5L, SF3B1 and MELKBy similarityAdd
BLAST
Regioni143 – 22482Interaction with EEDBy similarityAdd
BLAST
Regioni191 – 20010Involved in PP-1 inhibitionBy similarity
Regioni200 – 2034Involved in PP-1 bindingBy similarity
Regioni310 – 32920Interaction with EEDBy similarityAdd
BLAST
Regioni330 – 35122RNA-bindingBy similarityAdd
BLAST
Regioni331 – 3377Involved in PP-1 inhibitionBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi185 – 20925Nuclear localization signal 1By similarityAdd
BLAST
Motifi210 – 24031Nuclear localization signal 2By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 54Poly-Ala
Compositional biasi331 – 3344Poly-Lys

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.
OrthoDBiEOG7PS1FR.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
2JPENMR-A1-132[»]
ProteinModelPortaliQ8R3G1.
SMRiQ8R3G1. Positions 1-132, 158-212.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ8R3G1.
PhosphoSiteiQ8R3G1.

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.
OrthoDBiEOG7PS1FR.
PhylomeDBiQ8R3G1.
TreeFamiTF105539.

Miscellaneous databases

EvolutionaryTraceiQ8R3G1.
PROiQ8R3G1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R3G1.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-351.
    Strain: C57BL/6J.
    Tissue: Medulla oblongata.
  3. "The protein phosphatase-1 (PP1) regulator, nuclear inhibitor of PP1 (NIPP1), interacts with the polycomb group protein, embryonic ectoderm development (EED), and functions as a transcriptional repressor."
    Jin Q., van Eynde A., Beullens M., Roy N., Thiel G., Stalmans W., Bollen M.
    J. Biol. Chem. 278:30677-30685(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EED, IDENTIFICATION IN A COMPLEX WITH EED; HDAC2 AND PP1.
  4. "Interactor-mediated nuclear translocation and retention of protein phosphatase-1."
    Lesage B., Beullens M., Nuytten M., Van Eynde A., Keppens S., Himpens B., Bollen M.
    J. Biol. Chem. 279:55978-55984(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "The nuclear scaffold protein NIPP1 is essential for early embryonic development and cell proliferation."
    Van Eynde A., Nuytten M., Dewerchin M., Schoonjans L., Keppens S., Beullens M., Moons L., Carmeliet P., Stalmans W., Bollen M.
    Mol. Cell. Biol. 24:5863-5874(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.
  7. Cited for: STRUCTURE BY NMR OF 1-132, DOMAIN FHA, INTERACTION WITH MELK.

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: July 6, 2016
This is version 113 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.