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O95685

- PPR3D_HUMAN

UniProt

O95685 - PPR3D_HUMAN

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Protein

Protein phosphatase 1 regulatory subunit 3D

Gene

PPP1R3D

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. protein serine/threonine phosphatase activity Source: ProtInc

GO - Biological processi

  1. dephosphorylation Source: GOC
  2. glycogen metabolic process Source: UniProtKB-KW
  3. regulation of glycogen biosynthetic process Source: Ensembl
  4. regulation of glycogen catabolic process Source: Ensembl
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: Chromosome 20

Organism-specific databases

HGNCiHGNC:9294. PPP1R3D.

Subcellular locationi

GO - Cellular componenti

  1. glycogen granule Source: Ensembl
  2. intracellular membrane-bounded organelle Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33654.

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.
GenevestigatoriO95685.

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. 7 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_Glycogen_target-su_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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
Y18206 mRNA. Translation: CAA77081.1 .
AL109928 Genomic DNA. Translation: CAB92096.1 .
BC074860 mRNA. Translation: AAH74860.2 .
BC074861 mRNA. Translation: AAH74861.2 .
CCDSi CCDS13483.1.
RefSeqi NP_006233.1. NM_006242.3.
UniGenei Hs.42215.

3D structure databases

ProteinModelPortali O95685.
SMRi O95685. Positions 155-277.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111501. 7 interactions.
IntActi O95685. 4 interactions.
MINTi MINT-5003974.
STRINGi 9606.ENSP00000360035.

Protein family/group databases

CAZyi CBM21. Carbohydrate-Binding Module Family 21.

PTM databases

PhosphoSitei O95685.

Proteomic databases

MaxQBi O95685.
PaxDbi O95685.
PeptideAtlasi O95685.
PRIDEi O95685.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370996 ; ENSP00000360035 ; ENSG00000132825 .
GeneIDi 5509.
KEGGi hsa:5509.
UCSCi uc002ybb.3. human.

Organism-specific databases

CTDi 5509.
GeneCardsi GC20M058511.
HGNCi HGNC:9294. PPP1R3D.
HPAi HPA041146.
MIMi 603326. gene.
neXtProti NX_O95685.
PharmGKBi PA33654.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG288354.
GeneTreei ENSGT00530000062978.
HOGENOMi HOG000231580.
HOVERGENi HBG053658.
InParanoidi O95685.
KOi K07189.
OMAi QCLVPDF.
OrthoDBi EOG76HQ2B.
PhylomeDBi O95685.
TreeFami TF105537.

Miscellaneous databases

GenomeRNAii 5509.
NextBioi 21308.
PROi O95685.
SOURCEi Search...

Gene expression databases

Bgeei O95685.
CleanExi HS_PPP1R3D.
Genevestigatori O95685.

Family and domain databases

InterProi IPR005036. CBM_21.
IPR017434. Pase-1_Glycogen_target-su_met.
[Graphical view ]
Pfami PF03370. CBM_21. 1 hit.
[Graphical view ]
PIRSFi PIRSF038207. PP1_GT_animal. 1 hit.
PROSITEi PS51159. CBM21. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. 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.

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: October 29, 2014
This is version 105 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