PPR3B_HUMAN
ID PPR3B_HUMAN Reviewed; 285 AA.
AC Q86XI6; B3KTV3; Q9H812;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 3B;
DE AltName: Full=Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 4;
DE Short=PP1 subunit R4;
DE AltName: Full=Protein phosphatase 1 subunit GL;
DE Short=PTG;
GN Name=PPP1R3B; Synonyms=PPP1R4;
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 [LARGE SCALE MRNA].
RC TISSUE=Liver, and Retinoblastoma;
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 [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 TISSUE SPECIFICITY.
RX PubMed=11872655; DOI=10.2337/diabetes.51.3.591;
RA Munro S., Cuthbertson D.J., Cunningham J., Sales M., Cohen P.T.W.;
RT "Human skeletal muscle expresses a glycogen-targeting subunit of PP1 that
RT is identical to the insulin-sensitive glycogen-targeting subunit G(L) of
RT liver.";
RL Diabetes 51:591-598(2002).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=17555403; DOI=10.1042/bj20061572;
RA Montori-Grau M., Guitart M., Lerin C., Andreu A.L., Newgard C.B.,
RA Garcia-Martinez C., Gomez-Foix A.M.;
RT "Expression and glycogenic effect of glycogen-targeting protein phosphatase
RT 1 regulatory subunit GL in cultured human muscle.";
RL Biochem. J. 405:107-113(2007).
RN [6]
RP IDENTIFICATION BY 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).
RN [7]
RP STRUCTURE BY NMR OF 105-253.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CBM21 domain from human protein phosphatase 1,
RT regulatory (inhibitor) subunit 3B.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: Acts as a glycogen-targeting subunit for phosphatase PP1.
CC Facilitates interaction of the PP1 with enzymes of the glycogen
CC metabolism and regulates its activity. Suppresses the rate at which PP1
CC dephosphorylates (inactivates) glycogen phosphorylase and enhances the
CC rate at which it activates glycogen synthase and therefore limits
CC glycogen breakdown. Its activity is inhibited by PYGL, resulting in
CC inhibition of the glycogen synthase and glycogen phosphorylase
CC phosphatase activities of PP1. Dramatically increases basal and
CC insulin-stimulated glycogen synthesis upon overexpression in
CC hepatocytes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with glycogen, PPP1CC catalytic subunit of PP1 and
CC PYGL. Associates with glycogen particles. Forms complexes with
CC debranching enzyme, glycogen phosphorylase, glycogen synthase and
CC phosphorylase kinase which is necessary for its regulation of PP1
CC activity (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q86XI6; P62136: PPP1CA; NbExp=4; IntAct=EBI-3918864, EBI-357253;
CC Q86XI6; P36873: PPP1CC; NbExp=3; IntAct=EBI-3918864, EBI-356283;
CC Q86XI6; P11216: PYGB; NbExp=3; IntAct=EBI-3918864, EBI-1047231;
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver and, at lower levels,
CC in skeletal muscle, including in vastus lateralis, gastrocnemius and
CC soleus (at protein level). Highest mRNA levels are observed in skeletal
CC muscle, and only moderate levels in liver and heart. Weak expression in
CC placenta and lung. {ECO:0000269|PubMed:11872655,
CC ECO:0000269|PubMed:17555403}.
CC -!- DOMAIN: The N-terminal region is required for binding to PP1, the
CC central region is required for binding to glycogen and the C-terminal
CC region is required for binding to PYGL. {ECO:0000250}.
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DR EMBL; AK024067; BAB14811.1; -; mRNA.
DR EMBL; AK096119; BAG53215.1; -; mRNA.
DR EMBL; CH471157; EAW65572.1; -; Genomic_DNA.
DR EMBL; BC043388; AAH43388.1; -; mRNA.
DR CCDS; CCDS5973.1; -.
DR RefSeq; NP_001188258.1; NM_001201329.1.
DR RefSeq; NP_078883.2; NM_024607.3.
DR RefSeq; XP_006716316.1; XM_006716253.3.
DR RefSeq; XP_016869324.1; XM_017013835.1.
DR PDB; 2EEF; NMR; -; A=105-253.
DR PDB; 5ZT0; X-ray; 3.32 A; G/H/I/J=31-105.
DR PDBsum; 2EEF; -.
DR PDBsum; 5ZT0; -.
DR AlphaFoldDB; Q86XI6; -.
DR BMRB; Q86XI6; -.
DR SMR; Q86XI6; -.
DR BioGRID; 122786; 18.
DR IntAct; Q86XI6; 10.
DR MINT; Q86XI6; -.
DR STRING; 9606.ENSP00000308318; -.
DR CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR iPTMnet; Q86XI6; -.
DR PhosphoSitePlus; Q86XI6; -.
DR BioMuta; PPP1R3B; -.
DR DMDM; 74727837; -.
DR EPD; Q86XI6; -.
DR MassIVE; Q86XI6; -.
DR MaxQB; Q86XI6; -.
DR PaxDb; Q86XI6; -.
DR PeptideAtlas; Q86XI6; -.
DR PRIDE; Q86XI6; -.
DR ProteomicsDB; 70281; -.
DR Antibodypedia; 22075; 136 antibodies from 21 providers.
DR DNASU; 79660; -.
DR Ensembl; ENST00000310455.4; ENSP00000308318.3; ENSG00000173281.5.
DR Ensembl; ENST00000519699.1; ENSP00000428642.1; ENSG00000173281.5.
DR Ensembl; ENST00000644687.1; ENSP00000493491.1; ENSG00000285343.2.
DR Ensembl; ENST00000645121.2; ENSP00000494659.1; ENSG00000285343.2.
DR GeneID; 79660; -.
DR KEGG; hsa:79660; -.
DR MANE-Select; ENST00000310455.4; ENSP00000308318.3; NM_024607.4; NP_078883.2.
DR UCSC; uc003wsn.5; human.
DR CTD; 79660; -.
DR DisGeNET; 79660; -.
DR GeneCards; PPP1R3B; -.
DR HGNC; HGNC:14942; PPP1R3B.
DR HPA; ENSG00000173281; Tissue enhanced (liver, skeletal muscle).
DR MIM; 610541; gene.
DR neXtProt; NX_Q86XI6; -.
DR OpenTargets; ENSG00000173281; -.
DR PharmGKB; PA33652; -.
DR VEuPathDB; HostDB:ENSG00000173281; -.
DR eggNOG; KOG3986; Eukaryota.
DR GeneTree; ENSGT00940000159475; -.
DR HOGENOM; CLU_040215_2_1_1; -.
DR InParanoid; Q86XI6; -.
DR OMA; GIAFDQF; -.
DR OrthoDB; 1232750at2759; -.
DR PhylomeDB; Q86XI6; -.
DR TreeFam; TF105537; -.
DR PathwayCommons; Q86XI6; -.
DR SignaLink; Q86XI6; -.
DR BioGRID-ORCS; 79660; 13 hits in 1079 CRISPR screens.
DR ChiTaRS; PPP1R3B; human.
DR EvolutionaryTrace; Q86XI6; -.
DR GenomeRNAi; 79660; -.
DR Pharos; Q86XI6; Tbio.
DR PRO; PR:Q86XI6; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q86XI6; protein.
DR Bgee; ENSG00000173281; Expressed in skeletal muscle tissue and 104 other tissues.
DR Genevisible; Q86XI6; 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:0050196; F:[phosphorylase] phosphatase activity; IEA:Ensembl.
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:0019888; F:protein phosphatase regulator activity; IEA:Ensembl.
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; IDA:MGI.
DR DisProt; DP03015; -.
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 InterPro; IPR030682; PP1_3B.
DR PANTHER; PTHR12307:SF13; PTHR12307:SF13; 1.
DR Pfam; PF03370; CBM_21; 1.
DR PIRSF; PIRSF500814; PP1_GL; 1.
DR PIRSF; PIRSF038207; PP1_GT_animal; 1.
DR PROSITE; PS51159; CBM21; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycogen metabolism; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..285
FT /note="Protein phosphatase 1 regulatory subunit 3B"
FT /id="PRO_0000324543"
FT DOMAIN 125..233
FT /note="CBM21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT MOTIF 62..65
FT /note="PP1-binding motif"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C767"
FT VARIANT 48
FT /note="G -> E (in dbSNP:rs3748140)"
FT /id="VAR_039814"
FT CONFLICT 149
FT /note="V -> A (in Ref. 1; BAB14811)"
FT /evidence="ECO:0000305"
FT TURN 66..70
FT /evidence="ECO:0007829|PDB:5ZT0"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5ZT0"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:2EEF"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:2EEF"
FT STRAND 131..141
FT /evidence="ECO:0007829|PDB:2EEF"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:2EEF"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2EEF"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:2EEF"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:2EEF"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2EEF"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:2EEF"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:2EEF"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:2EEF"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:2EEF"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:2EEF"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:2EEF"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:2EEF"
SQ SEQUENCE 285 AA; 32695 MW; 77178FE100947989 CRC64;
MMAVDIEYRY NCMAPSLRQE RFAFKISPKP SKPLRPCIQL SSKNEASGMV APAVQEKKVK
KRVSFADNQG LALTMVKVFS EFDDPLDMPF NITELLDNIV SLTTAESESF VLDFSQPSAD
YLDFRNRLQA DHVCLENCVL KDKAIAGTVK VQNLAFEKTV KIRMTFDTWK SYTDFPCQYV
KDTYAGSDRD TFSFDISLPE KIQSYERMEF AVYYECNGQT YWDSNRGKNY RIIRAELKST
QGMTKPHSGP DLGISFDQFG SPRCSYGLFP EWPSYLGYEK LGPYY
