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P62141

- PP1B_MOUSE

UniProt

P62141 - PP1B_MOUSE

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Protein

Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Gene
Ppp1cb
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - 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

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631Manganese 1 By similarity
Metal bindingi65 – 651Manganese 1 By similarity
Metal bindingi91 – 911Manganese 1 By similarity
Metal bindingi91 – 911Manganese 2 By similarity
Metal bindingi123 – 1231Manganese 2 By similarity
Active sitei124 – 1241Proton donor By similarity
Metal bindingi172 – 1721Manganese 2 By similarity
Metal bindingi247 – 2471Manganese 2 By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. myosin-light-chain-phosphatase activity Source: UniProtKB
  3. myosin phosphatase activity Source: UniProtKB
  4. phosphatase activity Source: UniProtKB
  5. protein binding Source: MGI
  6. protein serine/threonine phosphatase activity Source: MGI

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. circadian regulation of gene expression Source: UniProtKB
  4. entrainment of circadian clock by photoperiod Source: UniProtKB
  5. glycogen metabolic process Source: UniProtKB-KW
  6. protein dephosphorylation Source: UniProtKB
  7. regulation of cell adhesion Source: UniProtKB
  8. regulation of circadian rhythm Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Biological rhythms, Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_215733. Downregulation of TGF-beta receptor signaling.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:104871. Ppp1cb.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. MLL5-L complex Source: Ensembl
  3. nucleolus Source: UniProtKB-SubCell
  4. PTW/PP1 phosphatase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 327326Serine/threonine-protein phosphatase PP1-beta catalytic subunitPRO_0000058780Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei316 – 3161Phosphothreonine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP62141.
PaxDbiP62141.
PRIDEiP62141.

PTM databases

PhosphoSiteiP62141.

Expressioni

Gene expression databases

BgeeiP62141.
GenevestigatoriP62141.

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. 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 EIF2S1.2 Publications

Protein-protein interaction databases

BioGridi202336. 8 interactions.
IntActiP62141. 9 interactions.
MINTiMINT-4428444.
STRINGi10090.ENSMUSP00000015100.

Structurei

3D structure databases

ProteinModelPortaliP62141.
SMRiP62141. Positions 1-308.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000062911.
HOVERGENiHBG000216.
InParanoidiQ542E7.
KOiK06269.
OMAiPDLQGME.
OrthoDBiEOG7TJ3K3.
PhylomeDBiP62141.
TreeFamiTF354243.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62141-1 [UniParc]FASTAAdd to Basket

« Hide

MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI    50
LLELEAPLKI CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL 100
ETICLLLAYK IKYPENFFLL RGNHECASIN RIYGFYDECK RRFNIKLWKT 150
FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ SMEQIRRIMR PTDVPDTGLL 200
CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL DLICRAHQVV 250
EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK 300
KAKYQYGGLN SGRPVTPPRT ANPPKKR 327
Length:327
Mass (Da):37,187
Last modified:January 23, 2007 - v3
Checksum:iE8356022E9B94ECD
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641I → N in BAC40733. 1 Publication
Sequence conflicti148 – 1481W → R in BAE42366. 1 Publication
Sequence conflicti223 – 2231S → F in BAE38902. 1 Publication
Sequence conflicti250 – 2501V → E in BAB23473. 1 Publication
Sequence conflicti269 – 2691P → S in BAE42366. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENSMUST00000131300; ENSMUSP00000121550; ENSMUSG00000014956.
GeneIDi19046.
KEGGimmu:19046.
UCSCiuc008wzq.2. mouse.

Cross-referencesi

Web resourcesi

Protein Spotlight

The things we forget - Issue 32 of March 2003

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS19193.1.
PIRi D32550.
RefSeqi NP_766295.2. NM_172707.3.
UniGenei Mm.241931.
Mm.456635.

3D structure databases

ProteinModelPortali P62141.
SMRi P62141. Positions 1-308.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202336. 8 interactions.
IntActi P62141. 9 interactions.
MINTi MINT-4428444.
STRINGi 10090.ENSMUSP00000015100.

Chemistry

BindingDBi P62141.

PTM databases

PhosphoSitei P62141.

Proteomic databases

MaxQBi P62141.
PaxDbi P62141.
PRIDEi P62141.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000015100 ; ENSMUSP00000015100 ; ENSMUSG00000014956 .
ENSMUST00000131300 ; ENSMUSP00000121550 ; ENSMUSG00000014956 .
GeneIDi 19046.
KEGGi mmu:19046.
UCSCi uc008wzq.2. mouse.

Organism-specific databases

CTDi 5500.
MGIi MGI:104871. Ppp1cb.

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00530000062911.
HOVERGENi HBG000216.
InParanoidi Q542E7.
KOi K06269.
OMAi PDLQGME.
OrthoDBi EOG7TJ3K3.
PhylomeDBi P62141.
TreeFami TF354243.

Enzyme and pathway databases

Reactomei REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_215733. Downregulation of TGF-beta receptor signaling.

Miscellaneous databases

ChiTaRSi PPP1CB. mouse.
NextBioi 295509.
PROi P62141.
SOURCEi Search...

Gene expression databases

Bgeei P62141.
Genevestigatori P62141.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPP1B_MOUSE
AccessioniPrimary (citable) accession number: P62141
Secondary accession number(s): P37140
, Q3TBE5, Q3TL90, Q542E7, Q8C285, Q9DBY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 116 of the entry and version 3 of the sequence. [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

External Data

Dasty 3

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