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Protein

Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Gene

Ppp1cb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.
[Myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Enzyme regulationi

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).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi63Manganese 1By similarity1
Metal bindingi65Manganese 1By similarity1
Metal bindingi91Manganese 1By similarity1
Metal bindingi91Manganese 2By similarity1
Metal bindingi123Manganese 2By similarity1
Active sitei124Proton donorBy similarity1
Metal bindingi172Manganese 2By similarity1
Metal bindingi247Manganese 2By similarity1

GO - Molecular functioni

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • circadian regulation of gene expression Source: UniProtKB
  • entrainment of circadian clock by photoperiod Source: UniProtKB
  • glycogen metabolic process Source: UniProtKB-KW
  • protein dephosphorylation Source: UniProtKB
  • regulation of cell adhesion Source: UniProtKB
  • regulation of circadian rhythm Source: UniProtKB
  • regulation of glycogen biosynthetic process Source: Ensembl
  • regulation of glycogen catabolic process Source: Ensembl

Keywordsi

Molecular functionHydrolase, Protein phosphatase
Biological processBiological rhythms, Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism
LigandManganese, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-2565942 Regulation of PLK1 Activity at G2/M Transition
R-MMU-5625740 RHO GTPases activate PKNs
R-MMU-5627123 RHO GTPases activate PAKs

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP1-beta catalytic subunit (EC:3.1.3.16, EC:3.1.3.53)
Short name:
PP-1B
Gene namesi
Name:Ppp1cb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:104871 Ppp1cb

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000587802 – 327Serine/threonine-protein phosphatase PP1-beta catalytic subunitAdd BLAST326

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei316PhosphothreonineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP62141
MaxQBiP62141
PaxDbiP62141
PeptideAtlasiP62141
PRIDEiP62141

PTM databases

iPTMnetiP62141
PhosphoSitePlusiP62141
SwissPalmiP62141

Expressioni

Gene expression databases

BgeeiENSMUSG00000014956
ExpressionAtlasiP62141 baseline and differential
GenevisibleiP62141 MM

Interactioni

Subunit structurei

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. Interacts with PPP1R7 and PPP1R12C. Interacts with PPP1R12A and NUAK1; the interaction is direct. Interacts with TRIM28; the interaction is weak (By similarity). Interacts with PPP1R15A; the interaction mediates binding to EIF2S1. 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 TRIM28; the interaction is weak (By similarity). Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with PPP1R15B; the interaction mediates binding to EIF2S1. Interacts with FOXP3 (By similarity). Interacts with RRP1B (By similarity). Interacts with SERPINE1 (By similarity).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202336, 82 interactors
IntActiP62141, 81 interactors
MINTiP62141
STRINGi10090.ENSMUSP00000015100

Structurei

3D structure databases

ProteinModelPortaliP62141
SMRiP62141
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

Phylogenomic databases

eggNOGiENOG410IN85 Eukaryota
ENOG410XPVF LUCA
GeneTreeiENSGT00530000062911
HOVERGENiHBG000216
InParanoidiP62141
KOiK06269
OMAiDHQEADI
OrthoDBiEOG091G0EKF
PhylomeDBiP62141
TreeFamiTF354243

Family and domain databases

Gene3Di3.60.21.10, 1 hit
InterProiView protein in InterPro
IPR004843 Calcineurin-like_PHP_ApaH
IPR029052 Metallo-depent_PP-like
IPR037979 PPP1CA/PPP1CB
IPR006186 Ser/Thr-sp_prot-phosphatase
IPR031675 STPPase_N
PANTHERiPTHR11668:SF377 PTHR11668:SF377, 1 hit
PfamiView protein in Pfam
PF00149 Metallophos, 1 hit
PF16891 STPPase_N, 1 hit
PRINTSiPR00114 STPHPHTASE
SMARTiView protein in SMART
SM00156 PP2Ac, 1 hit
PROSITEiView protein in PROSITE
PS00125 SER_THR_PHOSPHATASE, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62141-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI
60 70 80 90 100
LLELEAPLKI CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL
110 120 130 140 150
ETICLLLAYK IKYPENFFLL RGNHECASIN RIYGFYDECK RRFNIKLWKT
160 170 180 190 200
FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ SMEQIRRIMR PTDVPDTGLL
210 220 230 240 250
CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL DLICRAHQVV
260 270 280 290 300
EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK
310 320
KAKYQYGGLN SGRPVTPPRT ANPPKKR
Length:327
Mass (Da):37,187
Last modified:January 23, 2007 - v3
Checksum:iE8356022E9B94ECD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti64I → N in BAC40733 (PubMed:16141072).Curated1
Sequence conflicti148W → R in BAE42366 (PubMed:16141072).Curated1
Sequence conflicti223S → F in BAE38902 (PubMed:16141072).Curated1
Sequence conflicti250V → E in BAB23473 (PubMed:16141072).Curated1
Sequence conflicti269P → S in BAE42366 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27073 mRNA Translation: AAA37527.1
AK004686 mRNA Translation: BAB23473.1
AK088893 mRNA Translation: BAC40636.1
AK089067 mRNA Translation: BAC40733.1
AK147112 mRNA Translation: BAE27684.1
AK160743 mRNA Translation: BAE35984.1
AK166168 mRNA Translation: BAE38608.1
AK166623 mRNA Translation: BAE38902.1
AK168141 mRNA Translation: BAE40108.1
AK169379 mRNA Translation: BAE41126.1
AK171283 mRNA Translation: BAE42366.1
BC046832 mRNA Translation: AAH46832.1
CCDSiCCDS19193.1
PIRiD32550
RefSeqiNP_766295.2, NM_172707.3
UniGeneiMm.241931
Mm.456635

Genome annotation databases

EnsembliENSMUST00000015100; ENSMUSP00000015100; ENSMUSG00000014956
ENSMUST00000201360; ENSMUSP00000144047; ENSMUSG00000014956
GeneIDi19046
KEGGimmu:19046
UCSCiuc008wzq.2 mouse

Similar proteinsi

Entry informationi

Entry nameiPP1B_MOUSE
AccessioniPrimary (citable) accession number: P62141
Secondary accession number(s): P37140
, Q3TBE5, Q3TL90, Q542E7, Q8C285, Q9DBY2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 153 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

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