ID   PPR3E_HUMAN             Reviewed;         279 AA.
AC   Q9H7J1; D3DS47;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 3E;
GN   Name=PPP1R3E;
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], MOTIF, REGIONS, FUNCTION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15752363; DOI=10.1111/j.1742-4658.2005.04585.x;
RA   Munro S., Ceulemans H., Bollen M., Diplexcito J., Cohen P.T.W.;
RT   "A novel glycogen-targeting subunit of protein phosphatase 1 that is
RT   regulated by insulin and shows differential tissue distribution in humans
RT   and rodents.";
RL   FEBS J. 272:1478-1489(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-33, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Acts as a glycogen-targeting subunit for PP1. PP1 is involved
CC       in glycogen metabolism and contributes to the activation of glycogen
CC       synthase leading to an increase in glycogen synthesis.
CC       {ECO:0000269|PubMed:15752363}.
CC   -!- TISSUE SPECIFICITY: Expressed in skeletal muscle and heart with barely
CC       detectable levels in liver. {ECO:0000269|PubMed:15752363}.
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.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15779.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK024489; BAB15779.1; ALT_INIT; mRNA.
DR   EMBL; CH471078; EAW66170.1; -; Genomic_DNA.
DR   EMBL; CH471078; EAW66172.1; -; Genomic_DNA.
DR   EMBL; CH471078; EAW66173.1; -; Genomic_DNA.
DR   CCDS; CCDS61403.1; -.
DR   RefSeq; NP_001263247.1; NM_001276318.1.
DR   AlphaFoldDB; Q9H7J1; -.
DR   SMR; Q9H7J1; -.
DR   BioGRID; 124753; 3.
DR   IntAct; Q9H7J1; 2.
DR   MINT; Q9H7J1; -.
DR   STRING; 9606.ENSP00000408288; -.
DR   CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR   iPTMnet; Q9H7J1; -.
DR   PhosphoSitePlus; Q9H7J1; -.
DR   BioMuta; PPP1R3E; -.
DR   DMDM; 190359980; -.
DR   jPOST; Q9H7J1; -.
DR   MassIVE; Q9H7J1; -.
DR   MaxQB; Q9H7J1; -.
DR   PaxDb; Q9H7J1; -.
DR   PeptideAtlas; Q9H7J1; -.
DR   PRIDE; Q9H7J1; -.
DR   ProteomicsDB; 81126; -.
DR   TopDownProteomics; Q9H7J1; -.
DR   Antibodypedia; 71726; 8 antibodies from 6 providers.
DR   DNASU; 90673; -.
DR   Ensembl; ENST00000452015.9; ENSP00000408288.3; ENSG00000235194.9.
DR   GeneID; 90673; -.
DR   KEGG; hsa:90673; -.
DR   MANE-Select; ENST00000452015.9; ENSP00000408288.3; NM_001276318.2; NP_001263247.1.
DR   UCSC; uc031qns.2; human.
DR   CTD; 90673; -.
DR   GeneCards; PPP1R3E; -.
DR   HGNC; HGNC:14943; PPP1R3E.
DR   HPA; ENSG00000235194; Tissue enhanced (retina).
DR   MIM; 619540; gene.
DR   neXtProt; NX_Q9H7J1; -.
DR   OpenTargets; ENSG00000235194; -.
DR   VEuPathDB; HostDB:ENSG00000235194; -.
DR   eggNOG; KOG3986; Eukaryota.
DR   GeneTree; ENSGT00940000161906; -.
DR   HOGENOM; CLU_040215_0_0_1; -.
DR   InParanoid; Q9H7J1; -.
DR   OMA; ERAYYRT; -.
DR   OrthoDB; 1232750at2759; -.
DR   PhylomeDB; Q9H7J1; -.
DR   TreeFam; TF105537; -.
DR   PathwayCommons; Q9H7J1; -.
DR   SignaLink; Q9H7J1; -.
DR   BioGRID-ORCS; 90673; 11 hits in 1023 CRISPR screens.
DR   ChiTaRS; PPP1R3E; human.
DR   GenomeRNAi; 90673; -.
DR   Pharos; Q9H7J1; Tdark.
DR   PRO; PR:Q9H7J1; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q9H7J1; protein.
DR   Bgee; ENSG00000235194; Expressed in right hemisphere of cerebellum and 170 other tissues.
DR   ExpressionAtlas; Q9H7J1; baseline and differential.
DR   Genevisible; Q9H7J1; HS.
DR   GO; GO:0042587; C:glycogen granule; ISS:UniProtKB.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; IBA:GO_Central.
DR   GO; GO:0050196; F:[phosphorylase] phosphatase activity; ISS:UniProtKB.
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:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0005979; P:regulation of glycogen biosynthetic process; IBA:GO_Central.
DR   Gene3D; 2.60.40.2440; -; 1.
DR   InterPro; IPR005036; CBM21_dom.
DR   InterPro; IPR038175; CBM21_dom_sf.
DR   Pfam; PF03370; CBM_21; 1.
DR   PROSITE; PS51159; CBM21; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycogen metabolism; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..279
FT                   /note="Protein phosphatase 1 regulatory subunit 3E"
FT                   /id="PRO_0000338638"
FT   DOMAIN          154..259
FT                   /note="CBM21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT   REGION          28..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..198
FT                   /note="Glycogen-binding motif"
FT   REGION          248..256
FT                   /note="Substrate-binding motif"
FT   MOTIF           87..90
FT                   /note="PP1-binding motif"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
SQ   SEQUENCE   279 AA;  30644 MW;  E1FC0BEE683C97DC CRC64;
     MSRERPPGTD IPRNLSFIAA LTERAYYRSQ RPSLEEEPEE EPGEGGTRFG ARSRAHAPSR
     GRRARSAPAG GGGARAPRSR SPDTRKRVRF ADALGLELAV VRRFRPGELP RVPRHVQIQL
     QRDALRHFAP CQPRARGLQE ARAALEPASE PGFAARLLTQ RICLERAEAG PLGVAGSARV
     VDLAYEKRVS VRWSADGWRS QREAPAAYAG PAPPPPRADR FAFRLPAPPI GGALLFALRY
     RVTGHEFWDN NGGRDYALRG PEHPGSGGAP EPQGWIHFI