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Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (EC 3.1.3.16) (EC 3.1.3.53)

 PP1B_RAT                Reviewed;         327 AA.
P62142; P37140;
21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 132.
RecName: Full=Serine/threonine-protein phosphatase PP1-beta catalytic subunit;
Short=PP-1B;
EC=3.1.3.16;
EC=3.1.3.53;
Name=Ppp1cb;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2177460; DOI=10.1111/j.1349-7006.1990.tb02690.x;
Sasaki K., Shima H., Kitagawa Y., Irino S., Sugimura T., Nagao M.;
"Identification of members of the protein phosphatase 1 gene family in
the rat and enhanced expression of protein phosphatase 1 alpha gene in
rat hepatocellular carcinomas.";
Jpn. J. Cancer Res. 81:1272-1280(1990).
[2]
ERRATUM.
PubMed=1653777;
Sasaki K., Shima H., Kitagawa Y., Irino S., Sugimura T., Nagao M.;
Jpn. J. Cancer Res. 82:873-873(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=7751917;
da Cruz e Silva E.F., Fox C.A., Ouimet C.C., Gustafson E.,
Watson S.J., Greengard P.;
"Differential expression of protein phosphatase 1 isoforms in
mammalian brain.";
J. Neurosci. 15:3375-3389(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 26-35.
PubMed=7720853; DOI=10.1016/0014-5793(95)00197-H;
Moorhead G., MacKintosh C., Morrice N., Cohen P.;
"Purification of the hepatic glycogen-associated form of protein
phosphatase-1 by microcystin-Sepharose affinity chromatography.";
FEBS Lett. 362:101-105(1995).
-!- FUNCTION: Protein phosphatase that associates with over 200
regulatory proteins to form highly specific holoenzymes which
dephosphorylate hundreds of biological targets. Protein
phosphatase (PP1) is essential for cell division, it participates
in the regulation of glycogen metabolism, muscle contractility and
protein synthesis. Involved in regulation of ionic conductances
and long-term synaptic plasticity. Component of the PTW/PP1
phosphatase complex, which plays a role in the control of
chromatin structure and cell cycle progression during the
transition from mitosis into interphase. In balance with CSNK1D
and CSNK1E, determines the circadian period length, through the
regulation of the speed and rhythmicity of PER1 and PER2
phosphorylation. May dephosphorylate CSNK1D and CSNK1E (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- CATALYTIC ACTIVITY: [Myosin light-chain] phosphate + H(2)O =
[myosin light-chain] + phosphate.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 manganese ions per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by the toxins okadaic acid,
tautomycin and microcystin Leu-Arg. The phosphatase activity of
the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited
by Salubrinal, a drug that protects cells from endoplasmic
reticulum stress (By similarity). {ECO:0000250}.
-!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or
PPP1CC, which is folded into its native form by inhibitor 2 and
glycogen synthetase kinase 3, and then complexed to one or several
targeting or regulatory subunits. The targeting or regulatory
subunits determine the substrate specificity of PP1. PPP1R12A,
PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in
skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F
(in brain) mediate binding to glycogen. PPP1R15A and PPP1R15B
mediate binding to EIF2S1. Part of a complex containing PPP1R15B,
PP1 and NCK1/2. Interacts with PPP1R7 and PPP1R12C. Interacts with
PPP1R16B. Component of the PTW/PP1 phosphatase complex, composed
of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC.
Interacts with PPP1R8. Interacts with PPP1R12A and NUAK1; the
interaction is direct. Interacts with TRIM28; the interaction is
weak. Interacts with FOXP3. Interacts with RRP1B. Interacts with
SERPINE1 (By similarity). {ECO:0000250|UniProtKB:P62140,
ECO:0000250|UniProtKB:P62141}.
-!- INTERACTION:
O35867:Ppp1r9a; NbExp=2; IntAct=EBI-352326, EBI-7092421;
P09895:Rpl5; NbExp=2; IntAct=EBI-352326, EBI-916235;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62140}.
Nucleus {ECO:0000250|UniProtKB:P62140}. Nucleus, nucleoplasm
{ECO:0000250|UniProtKB:P62140}. Nucleus, nucleolus
{ECO:0000250|UniProtKB:P62140}. Note=Highly mobile in cells and
can be relocalized through interaction with targeting subunits. In
the presence of PPP1R8 relocalizes from the nucleus to nuclear
speckles. {ECO:0000250|UniProtKB:P62140}.
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The things we forget
- Issue 32 of March 2003;
URL="https://web.expasy.org/spotlight/back_issues/032";
-----------------------------------------------------------------------
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EMBL; D90164; BAA14195.1; -; mRNA.
EMBL; BC062033; AAH62033.1; -; mRNA.
PIR; I76571; I76571.
RefSeq; NP_037197.1; NM_013065.2.
RefSeq; XP_008762727.1; XM_008764505.2.
UniGene; Rn.128769; -.
UniGene; Rn.39034; -.
ProteinModelPortal; P62142; -.
SMR; P62142; -.
BioGrid; 247624; 2.
IntAct; P62142; 7.
MINT; P62142; -.
STRING; 10116.ENSRNOP00000006190; -.
iPTMnet; P62142; -.
PhosphoSitePlus; P62142; -.
PaxDb; P62142; -.
PRIDE; P62142; -.
Ensembl; ENSRNOT00000006190; ENSRNOP00000006190; ENSRNOG00000004612.
GeneID; 25594; -.
KEGG; rno:25594; -.
UCSC; RGD:3376; rat.
CTD; 5500; -.
RGD; 3376; Ppp1cb.
eggNOG; ENOG410IN85; Eukaryota.
eggNOG; ENOG410XPVF; LUCA.
GeneTree; ENSGT00530000062911; -.
HOGENOM; HOG000172697; -.
HOVERGEN; HBG000216; -.
InParanoid; P62142; -.
KO; K06269; -.
OMA; DHQEADI; -.
OrthoDB; EOG091G0EKF; -.
PhylomeDB; P62142; -.
TreeFam; TF354243; -.
Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-RNO-5625740; RHO GTPases activate PKNs.
Reactome; R-RNO-5627123; RHO GTPases activate PAKs.
PRO; PR:P62142; -.
Proteomes; UP000002494; Chromosome 6.
Bgee; ENSRNOG00000004612; -.
Genevisible; P62142; RN.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0042587; C:glycogen granule; IDA:RGD.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000164; C:protein phosphatase type 1 complex; IDA:RGD.
GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0017018; F:myosin phosphatase activity; ISS:UniProtKB.
GO; GO:0050115; F:myosin-light-chain-phosphatase activity; ISS:UniProtKB.
GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:RGD.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; TAS:Reactome.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
GO; GO:0006470; P:protein dephosphorylation; IDA:RGD.
GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0005979; P:regulation of glycogen biosynthetic process; IDA:RGD.
GO; GO:0005981; P:regulation of glycogen catabolic process; IDA:RGD.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR037979; PPP1CA/PPP1CB.
InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
InterPro; IPR031675; STPPase_N.
PANTHER; PTHR11668:SF377; PTHR11668:SF377; 1.
Pfam; PF00149; Metallophos; 1.
Pfam; PF16891; STPPase_N; 1.
PRINTS; PR00114; STPHPHTASE.
SMART; SM00156; PP2Ac; 1.
PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
1: Evidence at protein level;
Acetylation; Biological rhythms; Carbohydrate metabolism; Cell cycle;
Cell division; Complete proteome; Cytoplasm;
Direct protein sequencing; Glycogen metabolism; Hydrolase; Manganese;
Metal-binding; Nucleus; Phosphoprotein; Protein phosphatase;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P62140}.
CHAIN 2 327 Serine/threonine-protein phosphatase PP1-
beta catalytic subunit.
/FTId=PRO_0000058783.
ACT_SITE 124 124 Proton donor. {ECO:0000250}.
METAL 63 63 Manganese 1. {ECO:0000250}.
METAL 65 65 Manganese 1. {ECO:0000250}.
METAL 91 91 Manganese 1. {ECO:0000250}.
METAL 91 91 Manganese 2. {ECO:0000250}.
METAL 123 123 Manganese 2. {ECO:0000250}.
METAL 172 172 Manganese 2. {ECO:0000250}.
METAL 247 247 Manganese 2. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P62140}.
MOD_RES 316 316 Phosphothreonine.
{ECO:0000250|UniProtKB:P62140}.
SEQUENCE 327 AA; 37187 MW; E8356022E9B94ECD CRC64;
MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI LLELEAPLKI
CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL
RGNHECASIN RIYGFYDECK RRFNIKLWKT FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ
SMEQIRRIMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL
DLICRAHQVV EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK
KAKYQYGGLN SGRPVTPPRT ANPPKKR


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