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O95685 (PPR3D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PPP1R3D
Synonyms:PPP1R6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.1 Ref.5 Ref.6

Tissue specificity

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

Domain

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

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 299299Protein phosphatase 1 regulatory subunit 3D
PRO_0000071503

Regions

Domain169 – 278110CBM21
Motif101 – 1044PP1-binding motif

Amino acid modifications

Modified residue231Phosphoserine Ref.4
Modified residue281Phosphoserine Ref.4
Modified residue741Phosphoserine Ref.4

Sequences

Sequence LengthMass (Da)Tools
O95685 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: DB848FB1CF55E49E

FASTA29932,559
        10         20         30         40         50         60 
MSRGPSSAVL PSALGSRKLG PRSLSCLSDL DGGVALEPRA CRPPGSPGRA PPPTPAPSGC 

        70         80         90        100        110        120 
DPRLRPIILR RARSLPSSPE RRQKAAGAPG AACRPGCSQK LRVRFADALG LELAQVKVFN 

       130        140        150        160        170        180 
AGDDPSVPLH VLSRLAINSD LCCSSQDLEF TLHCLVPDFP PPVEAADFGE RLQRQLVCLE 

       190        200        210        220        230        240 
RVTCSDLGIS GTVRVCNVAF EKQVAVRYTF SGWRSTHEAV ARWRGPAGPE GTEDVFTFGF 

       250        260        270        280        290 
PVPPFLLELG SRVHFAVRYQ VAGAEYWDNN DHRDYSLTCR NHALHMPRGE CEESWIHFI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-28 AND SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"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.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y18206 mRNA. Translation: CAA77081.1.
AL109928 Genomic DNA. Translation: CAB92096.1.
BC074860 mRNA. Translation: AAH74860.2.
BC074861 mRNA. Translation: AAH74861.2.
CCDSCCDS13483.1.
RefSeqNP_006233.1. NM_006242.3.
UniGeneHs.42215.

3D structure databases

ProteinModelPortalO95685.
SMRO95685. Positions 155-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111501. 5 interactions.
IntActO95685. 4 interactions.
MINTMINT-5003974.
STRING9606.ENSP00000360035.

Protein family/group databases

CAZyCBM21. Carbohydrate-Binding Module Family 21.

PTM databases

PhosphoSiteO95685.

Proteomic databases

MaxQBO95685.
PaxDbO95685.
PeptideAtlasO95685.
PRIDEO95685.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370996; ENSP00000360035; ENSG00000132825.
GeneID5509.
KEGGhsa:5509.
UCSCuc002ybb.3. human.

Organism-specific databases

CTD5509.
GeneCardsGC20M058511.
HGNCHGNC:9294. PPP1R3D.
HPAHPA041146.
MIM603326. gene.
neXtProtNX_O95685.
PharmGKBPA33654.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG288354.
HOGENOMHOG000231580.
HOVERGENHBG053658.
InParanoidO95685.
KOK07189.
OMAQCLVPDF.
OrthoDBEOG76HQ2B.
PhylomeDBO95685.
TreeFamTF105537.

Gene expression databases

BgeeO95685.
CleanExHS_PPP1R3D.
GenevestigatorO95685.

Family and domain databases

InterProIPR005036. CBM_21.
IPR017434. Pase-1_Glycogen_target-su_met.
[Graphical view]
PfamPF03370. CBM_21. 1 hit.
[Graphical view]
PIRSFPIRSF038207. PP1_GT_animal. 1 hit.
PROSITEPS51159. CBM21. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi5509.
NextBio21308.
PROO95685.
SOURCESearch...

Entry information

Entry namePPR3D_HUMAN
AccessionPrimary (citable) accession number: O95685
Secondary accession number(s): Q6DK02
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM