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P62141 (PP1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Short name=PP-1B
EC=3.1.3.16
EC=3.1.3.53
Gene names
Name:Ppp1cb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.7 Ref.8

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

[Myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate.

Cofactor

Binds 2 manganese ions per subunit By similarity.

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.

Subunit structure

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. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. 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. Ref.5 Ref.6

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Nucleusnucleoplasm By similarity. Nucleusnucleolus By similarity. 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 By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processBiological rhythms
Carbohydrate metabolism
Cell cycle
Cell division
Glycogen metabolism
   Cellular componentCytoplasm
Nucleus
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

circadian regulation of gene expression

Inferred from direct assay Ref.8. Source: UniProtKB

entrainment of circadian clock by photoperiod

Inferred from mutant phenotype Ref.7. Source: UniProtKB

glycogen metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

protein dephosphorylation

Inferred from direct assay Ref.8. Source: UniProtKB

regulation of cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of circadian rhythm

Inferred from direct assay Ref.8. Source: UniProtKB

   Cellular_componentMLL5-L complex

Inferred from electronic annotation. Source: Ensembl

PTW/PP1 phosphatase complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 21471512. Source: MGI

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

myosin phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

myosin-light-chain-phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatase activity

Inferred from direct assay Ref.8. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 21471512. Source: MGI

protein serine/threonine phosphatase activity

Inferred from direct assay PubMed 14640981. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 327326Serine/threonine-protein phosphatase PP1-beta catalytic subunit
PRO_0000058780

Sites

Active site1241Proton donor By similarity
Metal binding631Manganese 1 By similarity
Metal binding651Manganese 1 By similarity
Metal binding911Manganese 1 By similarity
Metal binding911Manganese 2 By similarity
Metal binding1231Manganese 2 By similarity
Metal binding1721Manganese 2 By similarity
Metal binding2471Manganese 2 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue3161Phosphothreonine By similarity

Experimental info

Sequence conflict641I → N in BAC40733. Ref.2
Sequence conflict1481W → R in BAE42366. Ref.2
Sequence conflict2231S → F in BAE38902. Ref.2
Sequence conflict2501V → E in BAB23473. Ref.2
Sequence conflict2691P → S in BAE42366. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P62141 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E8356022E9B94ECD

FASTA32737,187
        10         20         30         40         50         60 
MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI LLELEAPLKI 

        70         80         90        100        110        120 
CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL 

       130        140        150        160        170        180 
RGNHECASIN RIYGFYDECK RRFNIKLWKT FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ 

       190        200        210        220        230        240 
SMEQIRRIMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL 

       250        260        270        280        290        300 
DLICRAHQVV EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK 

       310        320 
KAKYQYGGLN SGRPVTPPRT ANPPKKR 

« Hide

References

« Hide 'large scale' references
[1]"The fission yeast dis2+ gene required for chromosome disjoining encodes one of two putative type 1 protein phosphatases."
Ohkura H., Kinoshita N., Miyatani S., Toda T., Yanagida M.
Cell 57:997-1007(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Dendritic cell, Embryonic head, Embryonic heart, Embryonic kidney, Lung, Mammary gland, Morula and Thymus.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[4]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 26-35; 60-73 AND 150-167, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[5]"Inhibition of a constitutive translation initiation factor 2alpha phosphatase, CReP, promotes survival of stressed cells."
Jousse C., Oyadomari S., Novoa I., Lu P., Zhang Y., Harding H.P., Ron D.
J. Cell Biol. 163:767-775(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP1R15B.
[6]"Nck in a complex containing the catalytic subunit of protein phosphatase 1 regulates eukaryotic initiation factor 2alpha signaling and cell survival to endoplasmic reticulum stress."
Latreille M., Larose L.
J. Biol. Chem. 281:26633-26644(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN COMPLEX WITH PPP1R15B AND NCK1.
[7]"Protein phosphatase 1 (PP1) is a post-translational regulator of the mammalian circadian clock."
Schmutz I., Wendt S., Schnell A., Kramer A., Mansuy I.M., Albrecht U.
PLoS ONE 6:E21325-E21325(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CIRCADIAN CLOCK.
[8]"The period of the circadian oscillator is primarily determined by the balance between casein kinase 1 and protein phosphatase 1."
Lee H.M., Chen R., Kim H., Etchegaray J.P., Weaver D.R., Lee C.
Proc. Natl. Acad. Sci. U.S.A. 108:16451-16456(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CIRCADIAN CLOCK.
+Additional computationally mapped references.

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS19193.1.
PIRD32550.
RefSeqNP_766295.2. NM_172707.3.
UniGeneMm.241931.
Mm.456635.

3D structure databases

ProteinModelPortalP62141.
SMRP62141. Positions 1-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202336. 8 interactions.
IntActP62141. 9 interactions.
MINTMINT-4428444.
STRING10090.ENSMUSP00000015100.

Chemistry

BindingDBP62141.

PTM databases

PhosphoSiteP62141.

Proteomic databases

MaxQBP62141.
PaxDbP62141.
PRIDEP62141.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000015100; ENSMUSP00000015100; ENSMUSG00000014956.
ENSMUST00000131300; ENSMUSP00000121550; ENSMUSG00000014956.
GeneID19046.
KEGGmmu:19046.
UCSCuc008wzq.2. mouse.

Organism-specific databases

CTD5500.
MGIMGI:104871. Ppp1cb.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00530000062911.
HOVERGENHBG000216.
InParanoidQ542E7.
KOK06269.
OMAPDLQGME.
OrthoDBEOG7TJ3K3.
PhylomeDBP62141.
TreeFamTF354243.

Gene expression databases

BgeeP62141.
GenevestigatorP62141.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPP1CB. mouse.
NextBio295509.
PROP62141.
SOURCESearch...

Entry information

Entry namePP1B_MOUSE
AccessionPrimary (citable) accession number: P62141
Secondary accession number(s): P37140 expand/collapse secondary AC list , Q3TBE5, Q3TL90, Q542E7, Q8C285, Q9DBY2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot