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Protein

Protein phosphatase 1 regulatory subunit 3D

Gene

PPP1R3D

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Seems to act as a glycogen-targeting subunit for PP1. PP1 is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis.

GO - Molecular functioni

  • protein serine/threonine phosphatase activity Source: ProtInc

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 3D
Alternative name(s):
Protein phosphatase 1 regulatory subunit 6
Short name:
PP1 subunit R6
Protein phosphatase 1-binding subunit R6
Gene namesi
Name:PPP1R3D
Synonyms:PPP1R6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:9294. PPP1R3D.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33654.

Polymorphism and mutation databases

BioMutaiPPP1R3D.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299Protein phosphatase 1 regulatory subunit 3DPRO_0000071503Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Phosphoserine1 Publication
Modified residuei28 – 281Phosphoserine1 Publication
Modified residuei74 – 741Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO95685.
PaxDbiO95685.
PeptideAtlasiO95685.
PRIDEiO95685.

PTM databases

PhosphoSiteiO95685.

Expressioni

Tissue specificityi

Expressed in all tissues tested. High expression in skeletal muscle and heart.

Gene expression databases

BgeeiO95685.
CleanExiHS_PPP1R3D.
GenevisibleiO95685. HS.

Organism-specific databases

HPAiHPA041146.

Interactioni

Subunit structurei

Interacts with PPP1CC catalytic subunit of PP1, and associates with glycogen. Interacts with EPM2A; in the presence of NHLC1/malin the interaction leads to PPP1R3D ubiquitination and autophagic degradation.3 Publications

Protein-protein interaction databases

BioGridi111501. 6 interactions.
IntActiO95685. 4 interactions.
MINTiMINT-5003974.
STRINGi9606.ENSP00000360035.

Structurei

3D structure databases

ProteinModelPortaliO95685.
SMRiO95685. Positions 155-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini169 – 278110CBM21PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi101 – 1044PP1-binding motif

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

eggNOGiNOG288354.
GeneTreeiENSGT00530000062978.
HOGENOMiHOG000231580.
HOVERGENiHBG053658.
InParanoidiO95685.
KOiK07189.
OMAiQCLVPDF.
OrthoDBiEOG76HQ2B.
PhylomeDBiO95685.
TreeFamiTF105537.

Family and domain databases

InterProiIPR005036. CBM_21.
IPR017434. Pase-1_reg-su_3B/C/D_met.
[Graphical view]
PfamiPF03370. CBM_21. 1 hit.
[Graphical view]
PIRSFiPIRSF038207. PP1_GT_animal. 1 hit.
PROSITEiPS51159. CBM21. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O95685-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRGPSSAVL PSALGSRKLG PRSLSCLSDL DGGVALEPRA CRPPGSPGRA
60 70 80 90 100
PPPTPAPSGC DPRLRPIILR RARSLPSSPE RRQKAAGAPG AACRPGCSQK
110 120 130 140 150
LRVRFADALG LELAQVKVFN AGDDPSVPLH VLSRLAINSD LCCSSQDLEF
160 170 180 190 200
TLHCLVPDFP PPVEAADFGE RLQRQLVCLE RVTCSDLGIS GTVRVCNVAF
210 220 230 240 250
EKQVAVRYTF SGWRSTHEAV ARWRGPAGPE GTEDVFTFGF PVPPFLLELG
260 270 280 290
SRVHFAVRYQ VAGAEYWDNN DHRDYSLTCR NHALHMPRGE CEESWIHFI
Length:299
Mass (Da):32,559
Last modified:May 1, 1999 - v1
Checksum:iDB848FB1CF55E49E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18206 mRNA. Translation: CAA77081.1.
AL109928 Genomic DNA. Translation: CAB92096.1.
BC074860 mRNA. Translation: AAH74860.2.
BC074861 mRNA. Translation: AAH74861.2.
CCDSiCCDS13483.1.
RefSeqiNP_006233.1. NM_006242.3.
UniGeneiHs.42215.

Genome annotation databases

EnsembliENST00000370996; ENSP00000360035; ENSG00000132825.
GeneIDi5509.
KEGGihsa:5509.
UCSCiuc002ybb.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18206 mRNA. Translation: CAA77081.1.
AL109928 Genomic DNA. Translation: CAB92096.1.
BC074860 mRNA. Translation: AAH74860.2.
BC074861 mRNA. Translation: AAH74861.2.
CCDSiCCDS13483.1.
RefSeqiNP_006233.1. NM_006242.3.
UniGeneiHs.42215.

3D structure databases

ProteinModelPortaliO95685.
SMRiO95685. Positions 155-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111501. 6 interactions.
IntActiO95685. 4 interactions.
MINTiMINT-5003974.
STRINGi9606.ENSP00000360035.

Protein family/group databases

CAZyiCBM21. Carbohydrate-Binding Module Family 21.

PTM databases

PhosphoSiteiO95685.

Polymorphism and mutation databases

BioMutaiPPP1R3D.

Proteomic databases

MaxQBiO95685.
PaxDbiO95685.
PeptideAtlasiO95685.
PRIDEiO95685.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370996; ENSP00000360035; ENSG00000132825.
GeneIDi5509.
KEGGihsa:5509.
UCSCiuc002ybb.3. human.

Organism-specific databases

CTDi5509.
GeneCardsiGC20M058511.
HGNCiHGNC:9294. PPP1R3D.
HPAiHPA041146.
MIMi603326. gene.
neXtProtiNX_O95685.
PharmGKBiPA33654.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG288354.
GeneTreeiENSGT00530000062978.
HOGENOMiHOG000231580.
HOVERGENiHBG053658.
InParanoidiO95685.
KOiK07189.
OMAiQCLVPDF.
OrthoDBiEOG76HQ2B.
PhylomeDBiO95685.
TreeFamiTF105537.

Miscellaneous databases

GenomeRNAii5509.
NextBioi21308.
PROiO95685.
SOURCEiSearch...

Gene expression databases

BgeeiO95685.
CleanExiHS_PPP1R3D.
GenevisibleiO95685. HS.

Family and domain databases

InterProiIPR005036. CBM_21.
IPR017434. Pase-1_reg-su_3B/C/D_met.
[Graphical view]
PfamiPF03370. CBM_21. 1 hit.
[Graphical view]
PIRSFiPIRSF038207. PP1_GT_animal. 1 hit.
PROSITEiPS51159. CBM21. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PPP1R6, a novel member of the family of glycogen-targeting subunits of protein phosphatase 1."
    Armstrong C.G., Browne G.J., Cohen P., Cohen P.T.W.
    FEBS Lett. 418:210-214(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ASSOCIATION WITH GLYCOGEN, INTERACTION WITH PPP1CC.
    Tissue: Brain.
  2. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Lung.
  4. "Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates."
    Worby C.A., Gentry M.S., Dixon J.E.
    J. Biol. Chem. 281:30412-30418(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPM2A.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-28 AND SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Glycogenic activity of R6, a protein phosphatase 1 regulatory subunit, is modulated by the laforin-malin complex."
    Rubio-Villena C., Garcia-Gimeno M.A., Sanz P.
    Int. J. Biochem. Cell Biol. 45:1479-1488(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPM2A.

Entry informationi

Entry nameiPPR3D_HUMAN
AccessioniPrimary (citable) accession number: O95685
Secondary accession number(s): Q6DK02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 1999
Last modified: July 22, 2015
This is version 111 of the entry and version 1 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 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.