PPR3D_HUMAN
ID PPR3D_HUMAN Reviewed; 299 AA.
AC O95685; Q6DK02;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 3D;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 6;
DE Short=PP1 subunit R6;
DE AltName: Full=Protein phosphatase 1-binding subunit R6;
GN Name=PPP1R3D; Synonyms=PPP1R6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ASSOCIATION WITH GLYCOGEN, AND INTERACTION WITH
RP PPP1CC.
RC TISSUE=Brain;
RX PubMed=9414128; DOI=10.1016/s0014-5793(97)01385-9;
RA Armstrong C.G., Browne G.J., Cohen P., Cohen P.T.W.;
RT "PPP1R6, a novel member of the family of glycogen-targeting subunits of
RT protein phosphatase 1.";
RL FEBS Lett. 418:210-214(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH EPM2A.
RX PubMed=16901901; DOI=10.1074/jbc.m606117200;
RA Worby C.A., Gentry M.S., Dixon J.E.;
RT "Laforin, a dual specificity phosphatase that dephosphorylates complex
RT carbohydrates.";
RL J. Biol. Chem. 281:30412-30418(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-28 AND SER-74, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP INTERACTION WITH EPM2A.
RX PubMed=23624058; DOI=10.1016/j.biocel.2013.04.019;
RA Rubio-Villena C., Garcia-Gimeno M.A., Sanz P.;
RT "Glycogenic activity of R6, a protein phosphatase 1 regulatory subunit, is
RT modulated by the laforin-malin complex.";
RL Int. J. Biochem. Cell Biol. 45:1479-1488(2013).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-133, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Seems to act as a glycogen-targeting subunit for PP1. PP1 is
CC essential for cell division, and participates in the regulation of
CC glycogen metabolism, muscle contractility and protein synthesis.
CC -!- SUBUNIT: Interacts with PPP1CC catalytic subunit of PP1, and associates
CC with glycogen. Interacts with EPM2A; in the presence of NHLC1/malin the
CC interaction leads to PPP1R3D ubiquitination and autophagic degradation.
CC {ECO:0000269|PubMed:16901901, ECO:0000269|PubMed:23624058,
CC ECO:0000269|PubMed:9414128}.
CC -!- INTERACTION:
CC O95685; P62136: PPP1CA; NbExp=3; IntAct=EBI-1045661, EBI-357253;
CC O95685; P63104: YWHAZ; NbExp=3; IntAct=EBI-1045661, EBI-347088;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested. High expression in
CC skeletal muscle and heart.
CC -!- DOMAIN: The CBM21 domain is known to be involved in the localization to
CC glycogen and is characteristic of some regulatory subunit of
CC phosphatase complexes.
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DR EMBL; Y18206; CAA77081.1; -; mRNA.
DR EMBL; AL109928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC074860; AAH74860.2; -; mRNA.
DR EMBL; BC074861; AAH74861.2; -; mRNA.
DR CCDS; CCDS13483.1; -.
DR RefSeq; NP_006233.1; NM_006242.3.
DR AlphaFoldDB; O95685; -.
DR SMR; O95685; -.
DR BioGRID; 111501; 18.
DR IntAct; O95685; 14.
DR MINT; O95685; -.
DR STRING; 9606.ENSP00000360035; -.
DR CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR iPTMnet; O95685; -.
DR PhosphoSitePlus; O95685; -.
DR BioMuta; PPP1R3D; -.
DR EPD; O95685; -.
DR jPOST; O95685; -.
DR MassIVE; O95685; -.
DR MaxQB; O95685; -.
DR PaxDb; O95685; -.
DR PeptideAtlas; O95685; -.
DR PRIDE; O95685; -.
DR ProteomicsDB; 50999; -.
DR Antibodypedia; 48192; 18 antibodies from 13 providers.
DR DNASU; 5509; -.
DR Ensembl; ENST00000370996.5; ENSP00000360035.3; ENSG00000132825.7.
DR GeneID; 5509; -.
DR KEGG; hsa:5509; -.
DR MANE-Select; ENST00000370996.5; ENSP00000360035.3; NM_006242.4; NP_006233.1.
DR UCSC; uc002ybb.4; human.
DR CTD; 5509; -.
DR GeneCards; PPP1R3D; -.
DR HGNC; HGNC:9294; PPP1R3D.
DR HPA; ENSG00000132825; Low tissue specificity.
DR MIM; 603326; gene.
DR neXtProt; NX_O95685; -.
DR OpenTargets; ENSG00000132825; -.
DR PharmGKB; PA33654; -.
DR VEuPathDB; HostDB:ENSG00000132825; -.
DR eggNOG; KOG3986; Eukaryota.
DR GeneTree; ENSGT00940000161921; -.
DR HOGENOM; CLU_040215_0_1_1; -.
DR InParanoid; O95685; -.
DR OMA; KNYSLTC; -.
DR OrthoDB; 1047478at2759; -.
DR PhylomeDB; O95685; -.
DR TreeFam; TF105537; -.
DR PathwayCommons; O95685; -.
DR SignaLink; O95685; -.
DR BioGRID-ORCS; 5509; 12 hits in 1087 CRISPR screens.
DR GenomeRNAi; 5509; -.
DR Pharos; O95685; Tdark.
DR PRO; PR:O95685; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O95685; protein.
DR Bgee; ENSG00000132825; Expressed in secondary oocyte and 182 other tissues.
DR Genevisible; O95685; HS.
DR GO; GO:0042587; C:glycogen granule; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IBA:GO_Central.
DR GO; GO:2001069; F:glycogen binding; IBA:GO_Central.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; TAS:ProtInc.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0005979; P:regulation of glycogen biosynthetic process; IBA:GO_Central.
DR GO; GO:0005981; P:regulation of glycogen catabolic process; IEA:Ensembl.
DR Gene3D; 2.60.40.2440; -; 1.
DR InterPro; IPR005036; CBM21_dom.
DR InterPro; IPR038175; CBM21_dom_sf.
DR InterPro; IPR017434; Pase-1_reg-su_3B/C/D_met.
DR Pfam; PF03370; CBM_21; 1.
DR PIRSF; PIRSF038207; PP1_GT_animal; 1.
DR PROSITE; PS51159; CBM21; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycogen metabolism; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..299
FT /note="Protein phosphatase 1 regulatory subunit 3D"
FT /id="PRO_0000071503"
FT DOMAIN 169..278
FT /note="CBM21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 101..104
FT /note="PP1-binding motif"
FT COMPBIAS 44..60
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
SQ SEQUENCE 299 AA; 32559 MW; DB848FB1CF55E49E CRC64;
MSRGPSSAVL PSALGSRKLG PRSLSCLSDL DGGVALEPRA CRPPGSPGRA PPPTPAPSGC
DPRLRPIILR RARSLPSSPE RRQKAAGAPG AACRPGCSQK LRVRFADALG LELAQVKVFN
AGDDPSVPLH VLSRLAINSD LCCSSQDLEF TLHCLVPDFP PPVEAADFGE RLQRQLVCLE
RVTCSDLGIS GTVRVCNVAF EKQVAVRYTF SGWRSTHEAV ARWRGPAGPE GTEDVFTFGF
PVPPFLLELG SRVHFAVRYQ VAGAEYWDNN DHRDYSLTCR NHALHMPRGE CEESWIHFI
