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Protein

Protein phosphatase 1 regulatory subunit 3E

Gene

PPP1R3E

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a glycogen-targeting subunit for PP1. PP1 is involved in glycogen metabolism and contributes to the activation of glycogen synthase leading to an increase in glycogen synthesis.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism

Protein family/group databases

CAZyiCBM21. Carbohydrate-Binding Module Family 21.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase 1 regulatory subunit 3E
Gene namesi
Name:PPP1R3E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:14943. PPP1R3E.

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000235194.

Polymorphism and mutation databases

DMDMi190359980.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003386381 – 279Protein phosphatase 1 regulatory subunit 3EAdd BLAST279

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei16PhosphoserineCombined sources1
Modified residuei33PhosphoserineCombined sources1
Modified residuei66PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H7J1.
PaxDbiQ9H7J1.
PeptideAtlasiQ9H7J1.
PRIDEiQ9H7J1.
TopDownProteomicsiQ9H7J1.

PTM databases

iPTMnetiQ9H7J1.
PhosphoSitePlusiQ9H7J1.

Expressioni

Tissue specificityi

Expressed in skeletal muscle and heart with barely detectable levels in liver.1 Publication

Gene expression databases

BgeeiENSG00000235194.
CleanExiHS_PPP1R3E.
ExpressionAtlasiQ9H7J1. baseline and differential.
GenevisibleiQ9H7J1. HS.

Organism-specific databases

HPAiHPA061600.

Interactioni

Protein-protein interaction databases

BioGridi124753. 1 interactor.
IntActiQ9H7J1. 2 interactors.
STRINGi9606.ENSP00000408288.

Structurei

3D structure databases

ProteinModelPortaliQ9H7J1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini154 – 259CBM21PROSITE-ProRule annotationAdd BLAST106

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni176 – 198Glycogen-binding motifAdd BLAST23
Regioni248 – 256Substrate-binding motif9

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi87 – 90PP1-binding motif4

Domaini

The CBM21 domain is known to be involved in the localization to glycogen and is characteristic of some regulatory subunit of phosphatase complexes.

Sequence similaritiesi

Contains 1 CBM21 (carbohydrate binding type-21) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3986. Eukaryota.
ENOG4111FT1. LUCA.
GeneTreeiENSGT00530000062978.
HOGENOMiHOG000231580.
HOVERGENiHBG108282.
InParanoidiQ9H7J1.
KOiK07189.
OMAiTGREFWD.
OrthoDBiEOG091G0PR9.
PhylomeDBiQ9H7J1.
TreeFamiTF105537.

Family and domain databases

InterProiIPR005036. CBM21_dom.
[Graphical view]
PfamiPF03370. CBM_21. 1 hit.
[Graphical view]
PROSITEiPS51159. CBM21. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H7J1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRERPPGTD IPRNLSFIAA LTERAYYRSQ RPSLEEEPEE EPGEGGTRFG
60 70 80 90 100
ARSRAHAPSR GRRARSAPAG GGGARAPRSR SPDTRKRVRF ADALGLELAV
110 120 130 140 150
VRRFRPGELP RVPRHVQIQL QRDALRHFAP CQPRARGLQE ARAALEPASE
160 170 180 190 200
PGFAARLLTQ RICLERAEAG PLGVAGSARV VDLAYEKRVS VRWSADGWRS
210 220 230 240 250
QREAPAAYAG PAPPPPRADR FAFRLPAPPI GGALLFALRY RVTGHEFWDN
260 270
NGGRDYALRG PEHPGSGGAP EPQGWIHFI
Length:279
Mass (Da):30,644
Last modified:June 10, 2008 - v2
Checksum:iE1FC0BEE683C97DC
GO

Sequence cautioni

The sequence BAB15779 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK024489 mRNA. Translation: BAB15779.1. Different initiation.
CH471078 Genomic DNA. Translation: EAW66170.1.
CH471078 Genomic DNA. Translation: EAW66172.1.
CH471078 Genomic DNA. Translation: EAW66173.1.
CCDSiCCDS61403.1.
RefSeqiNP_001263247.1. NM_001276318.1.
UniGeneiHs.601513.

Genome annotation databases

EnsembliENST00000452015; ENSP00000408288; ENSG00000235194.
GeneIDi90673.
KEGGihsa:90673.
UCSCiuc031qns.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK024489 mRNA. Translation: BAB15779.1. Different initiation.
CH471078 Genomic DNA. Translation: EAW66170.1.
CH471078 Genomic DNA. Translation: EAW66172.1.
CH471078 Genomic DNA. Translation: EAW66173.1.
CCDSiCCDS61403.1.
RefSeqiNP_001263247.1. NM_001276318.1.
UniGeneiHs.601513.

3D structure databases

ProteinModelPortaliQ9H7J1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124753. 1 interactor.
IntActiQ9H7J1. 2 interactors.
STRINGi9606.ENSP00000408288.

Protein family/group databases

CAZyiCBM21. Carbohydrate-Binding Module Family 21.

PTM databases

iPTMnetiQ9H7J1.
PhosphoSitePlusiQ9H7J1.

Polymorphism and mutation databases

DMDMi190359980.

Proteomic databases

MaxQBiQ9H7J1.
PaxDbiQ9H7J1.
PeptideAtlasiQ9H7J1.
PRIDEiQ9H7J1.
TopDownProteomicsiQ9H7J1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000452015; ENSP00000408288; ENSG00000235194.
GeneIDi90673.
KEGGihsa:90673.
UCSCiuc031qns.2. human.

Organism-specific databases

CTDi90673.
GeneCardsiPPP1R3E.
HGNCiHGNC:14943. PPP1R3E.
HPAiHPA061600.
neXtProtiNX_Q9H7J1.
OpenTargetsiENSG00000235194.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3986. Eukaryota.
ENOG4111FT1. LUCA.
GeneTreeiENSGT00530000062978.
HOGENOMiHOG000231580.
HOVERGENiHBG108282.
InParanoidiQ9H7J1.
KOiK07189.
OMAiTGREFWD.
OrthoDBiEOG091G0PR9.
PhylomeDBiQ9H7J1.
TreeFamiTF105537.

Miscellaneous databases

GenomeRNAii90673.
PROiQ9H7J1.

Gene expression databases

BgeeiENSG00000235194.
CleanExiHS_PPP1R3E.
ExpressionAtlasiQ9H7J1. baseline and differential.
GenevisibleiQ9H7J1. HS.

Family and domain databases

InterProiIPR005036. CBM21_dom.
[Graphical view]
PfamiPF03370. CBM_21. 1 hit.
[Graphical view]
PROSITEiPS51159. CBM21. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPPR3E_HUMAN
AccessioniPrimary (citable) accession number: Q9H7J1
Secondary accession number(s): D3DS47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: November 2, 2016
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  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.