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Protein

Serine/threonine-protein phosphatase 1 regulatory subunit 10

Gene

Ppp1r10

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA, single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri838 – 86629C3H1-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • protein phosphatase 1 binding Source: RGD
  • protein phosphatase inhibitor activity Source: RGD
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

  • negative regulation of catalytic activity Source: GOC
  • transcription, DNA-templated Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Protein phosphatase inhibitor

Keywords - Ligandi

DNA-binding, Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 1 regulatory subunit 10
Alternative name(s):
MHC class I region proline-rich protein CAT53
Phosphatase 1 nuclear targeting subunit
Short name:
Protein PNUTS
Gene namesi
Name:Ppp1r10
Synonyms:Cat53, Pnuts
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620079. Ppp1r10.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

  • Note: Found in discrete nucleoplasmic bodies and within nucleoli. Associates with chromatin during interphase, excluded from condensed chromosomes during early mitosis and is reloaded onto chromosomes at the late telophase (By similarity).By similarity

GO - Cellular componenti

  • nuclear chromatin Source: RGD
  • PTW/PP1 phosphatase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi396 – 3961R → A: Does not abolish interaction with PPP1CA and does not reduce PPP1CA inhibition. 1 Publication
Mutagenesisi397 – 3971K → A: Does not abolish interaction with PPP1CA and reduces a little PPP1CA inhibition. 1 Publication
Mutagenesisi399 – 3991V → A: Reduces interaction with PPP1CA and reduces strongly PPP1CA inhibition. 1 Publication
Mutagenesisi401 – 4011W → A: Abolishes interaction with PPP1CA and PPP1CA inhibition. 1 Publication
Mutagenesisi445 – 4506Missing : Abolishes PPP1CA inhibition. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 872872Serine/threonine-protein phosphatase 1 regulatory subunit 10PRO_0000071515Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei313 – 3131PhosphoserineCombined sources
Modified residuei382 – 3821PhosphoserineCombined sources
Modified residuei398 – 3981Phosphothreonine; by PKA1 Publication
Modified residuei545 – 5451PhosphoserineBy similarity
Modified residuei591 – 5911PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on Thr-398 by PKA within the region necessary for interaction with PPP1CA.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiO55000.

PTM databases

iPTMnetiO55000.
PhosphoSiteiO55000.

Expressioni

Tissue specificityi

Expressed in testis, brain and intestine (at protein level). Highly expressed in testis.2 Publications

Interactioni

Subunit structurei

Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1CC. Interacts with PPP1CA, WDR82 and TOX4 (By similarity).By similarity

GO - Molecular functioni

  • protein phosphatase 1 binding Source: RGD

Structurei

Secondary structure

1
872
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi404 – 4063Combined sources
Beta strandi407 – 4137Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MOYX-ray2.20B393-433[»]
4MP0X-ray2.10B/D394-433[»]
ProteinModelPortaliO55000.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini73 – 14775TFIIS N-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 348348Interaction with TOX4By similarityAdd
BLAST
Regioni357 – 43377Necessary for interaction with PPP1CAAdd
BLAST
Regioni382 – 45069Essential for PPP1CA inhibitionAdd
BLAST
Regioni393 – 40816Necessary for interaction with PPP1CCBy similarityAdd
BLAST
Regioni418 – 619202Interaction with WDR82By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi420 – 4234PP1-binding motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi304 – 3107Poly-Lys
Compositional biasi540 – 836297Gly-richAdd
BLAST

Sequence similaritiesi

Contains 1 C3H1-type zinc finger.PROSITE-ProRule annotation
Contains 1 TFIIS N-terminal domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri838 – 86629C3H1-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOGENOMiHOG000049285.
HOVERGENiHBG053646.
InParanoidiO55000.
KOiK17552.
PhylomeDBiO55000.

Family and domain databases

Gene3Di1.20.930.10. 1 hit.
InterProiIPR003617. TFIIS/CRSP70_N_sub.
IPR017923. TFIIS_N.
IPR000571. Znf_CCCH.
[Graphical view]
PfamiPF08711. Med26. 1 hit.
PF00642. zf-CCCH. 1 hit.
[Graphical view]
SMARTiSM00509. TFS2N. 1 hit.
SM00356. ZnF_C3H1. 1 hit.
[Graphical view]
SUPFAMiSSF47676. SSF47676. 1 hit.
SSF90229. SSF90229. 1 hit.
PROSITEiPS51319. TFIIS_N. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O55000-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSGPIDPKE LLKGLDSFLT RDGEVKSVDG IAKIFSLMKE ARKMVSRCTY
60 70 80 90 100
LNIILQTRAP EVLVKFIDVG GYKLLNSWLT YSKTTNNIPL LQQILLTLQH
110 120 130 140 150
LPLTVDHLKQ NNTAKLVKQL SKSSEDEELR KLASVLVSDW MAVIRSQSST
160 170 180 190 200
QPAEKDKKKR KEEGKSRTTL PERPLTEVKA ETRAEEAPEK KKEKPKSLRT
210 220 230 240 250
TAPSHAKFRS TGLELDTPSL VPVKKNSSTV VVSDKYNLKP IPLKRQSATA
260 270 280 290 300
APGDAAPPAE KKYKPLNTTP NTTKEIKVKI IPPQPMEGLG FLDALNSAPV
310 320 330 340 350
PGIKIKKKKK VLSPTAAKPS PFEGKTSTEP STAKPSSPEP AAPAEPMDTD
360 370 380 390 400
RPGTPVPAVE VPELMDAASS EPGALDAKPV ESPGDPNQLT RKGRKRKTVT
410 420 430 440 450
WPEEGKLREY FYFELDETER VNVNKIKDFG EAAKREILSD RHAFETARRL
460 470 480 490 500
SHDNMEEKVP WVCPRPLVLP SPLVIPGSNS QERYIQAERE KGILQELFLN
510 520 530 540 550
KESPHEPDPE PYEPIPPKLI PLDEECAMDE TPYVETLEPG GSGGSPDGAG
560 570 580 590 600
GSKLPPVLAN LMGSMGAGKS PQGPGGGGIN VQEILTSIMG SPNNHPSEEL
610 620 630 640 650
LKQPDYSDKL KQMLVPHGLL GPGPVANGFP PGGPGGPKGM QHFPPGPGGP
660 670 680 690 700
MPGPHGGPGG PVGPRLLGPP PPSRGGDPFW DGPGDPMRGG PMRGGPGPGP
710 720 730 740 750
GPYHRGRGGR GGNEPPPPPP FRGARGGRSG GGPPNGRGGP GGGGMVGGGG
760 770 780 790 800
HRPHEGPGGS MGSGHRSHEG PGGSMGSGHR SHEGPGHGGP HGHRPHDVPS
810 820 830 840 850
HRGHDHRGPP PHEHRGHDGH GGGGHRGHDG GHSHGGDMSN RPVCRHFMMK
860 870
GNCRYENNCA FYHPGVNGPP LP
Length:872
Mass (Da):92,828
Last modified:June 1, 1998 - v1
Checksum:i23CC61B4B296E948
GO

Sequence cautioni

The sequence CAE84038.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF040954 mRNA. Translation: AAB96775.1.
BX883048 Genomic DNA. Translation: CAE84038.1. Sequence problems.
RefSeqiNP_075240.1. NM_022951.2.
UniGeneiRn.37758.

Genome annotation databases

GeneIDi65045.
KEGGirno:65045.
UCSCiRGD:620079. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF040954 mRNA. Translation: AAB96775.1.
BX883048 Genomic DNA. Translation: CAE84038.1. Sequence problems.
RefSeqiNP_075240.1. NM_022951.2.
UniGeneiRn.37758.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MOYX-ray2.20B393-433[»]
4MP0X-ray2.10B/D394-433[»]
ProteinModelPortaliO55000.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiO55000.
PhosphoSiteiO55000.

Proteomic databases

PRIDEiO55000.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi65045.
KEGGirno:65045.
UCSCiRGD:620079. rat.

Organism-specific databases

CTDi5514.
RGDi620079. Ppp1r10.

Phylogenomic databases

HOGENOMiHOG000049285.
HOVERGENiHBG053646.
InParanoidiO55000.
KOiK17552.
PhylomeDBiO55000.

Miscellaneous databases

NextBioi613876.
PROiO55000.

Family and domain databases

Gene3Di1.20.930.10. 1 hit.
InterProiIPR003617. TFIIS/CRSP70_N_sub.
IPR017923. TFIIS_N.
IPR000571. Znf_CCCH.
[Graphical view]
PfamiPF08711. Med26. 1 hit.
PF00642. zf-CCCH. 1 hit.
[Graphical view]
SMARTiSM00509. TFS2N. 1 hit.
SM00356. ZnF_C3H1. 1 hit.
[Graphical view]
SUPFAMiSSF47676. SSF47676. 1 hit.
SSF90229. SSF90229. 1 hit.
PROSITEiPS51319. TFIIS_N. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of PNUTS, a putative protein phosphatase 1 nuclear targeting subunit."
    Allen P.B., Kwon Y.G., Nairn A.C., Greengard P.
    J. Biol. Chem. 273:4089-4095(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN PPP1CA INHIBITION, INTERACTION WITH PPP1CA, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  2. "The genomic sequence and comparative analysis of the rat major histocompatibility complex."
    Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H., Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.
    Genome Res. 14:631-639(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "PNUTS, a protein phosphatase 1 (PP1) nuclear targeting subunit. Characterization of its PP1- and RNA-binding domains and regulation by phosphorylation."
    Kim Y.M., Watanabe T., Allen P.B., Kim Y.M., Lee S.J., Greengard P., Nairn A.C., Kwon Y.G.
    J. Biol. Chem. 278:13819-13828(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PPP1CA INHIBITION, IDENTIFICATION IN A COMPLEX WITH PPP1CA AND RNA HOMOPOLYMERS, PHOSPHORYLATION AT THR-398, MUTAGENESIS OF ARG-396; LYS-397; VAL-399; TRP-401 AND 445-GLU--LEU-450, DNA-BINDING, RNA-BINDING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313; SER-382 AND SER-591, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPP1RA_RAT
AccessioniPrimary (citable) accession number: O55000
Secondary accession number(s): Q6MG09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: June 1, 1998
Last modified: February 17, 2016
This is version 118 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.