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P61292

- PP1B_PIG

UniProt

P61292 - PP1B_PIG

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Protein
Serine/threonine-protein phosphatase PP1-beta catalytic subunit
Gene
PPP1CB
Organism
Sus scrofa (Pig)
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 By similarity.

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 phosphatase activity Source: UniProtKB
  3. myosin-light-chain-phosphatase activity Source: UniProtKB
  4. phosphatase activity Source: UniProtKB
Complete GO annotation...

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

BRENDAi3.1.3.16. 6170.

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

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. PTW/PP1 phosphatase complex Source: UniProtKB
  2. cytoplasm Source: UniProtKB-SubCell
  3. nucleolus Source: UniProtKB-SubCell
  4. nucleoplasm Source: UniProtKB-SubCell
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 subunit
PRO_0000058781Add
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

PaxDbiP61292.
PRIDEiP61292.

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. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2. 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 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 dephosphorylates TRIM28 on 'Ser-824' By similarity. Interacts with asfivirus DP71L protein.1 Publication

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000009104.

Structurei

3D structure databases

ProteinModelPortaliP61292.
SMRiP61292. Positions 1-308.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
KOiK06269.

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.

P61292-1 [UniParc]FASTAAdd to Basket

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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 databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ396471 mRNA. Translation: ABD65256.1.
AB016735 mRNA. Translation: BAA32238.1.
RefSeqiNP_999349.1. NM_214184.2.
UniGeneiSsc.79343.

Genome annotation databases

GeneIDi397378.
KEGGissc:397378.

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
DQ396471 mRNA. Translation: ABD65256.1 .
AB016735 mRNA. Translation: BAA32238.1 .
RefSeqi NP_999349.1. NM_214184.2.
UniGenei Ssc.79343.

3D structure databases

ProteinModelPortali P61292.
SMRi P61292. Positions 1-308.
ModBasei Search...

Protein-protein interaction databases

STRINGi 9823.ENSSSCP00000009104.

Chemistry

BindingDBi P61292.

Proteomic databases

PaxDbi P61292.
PRIDEi P61292.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 397378.
KEGGi ssc:397378.

Organism-specific databases

CTDi 5500.

Phylogenomic databases

eggNOGi COG0639.
HOGENOMi HOG000172697.
HOVERGENi HBG000216.
KOi K06269.

Enzyme and pathway databases

BRENDAi 3.1.3.16. 6170.

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

  1. "Identification of a differentially expressed gene PPP1CB between porcine Longissimus dorsi of Meishan and Large WhitexMeishan hybrids."
    Huang T., Xiong Y.Z., Lei M.G., Xu D.Q., Deng C.Y.
    Acta Biochim. Biophys. Sin. 38:450-456(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Eto M., Yazawa M., Chung H., Brautigan D.L.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The MyD116 African swine fever virus homologue interacts with the catalytic subunit of protein phosphatase 1 and activates its phosphatase activity."
    Rivera J., Abrams C., Hernaez B., Alcazar A., Escribano J.M., Dixon L., Alonso C.
    J. Virol. 81:2923-2929(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ASFIVIRUS DP71L.

Entry informationi

Entry nameiPP1B_PIG
AccessioniPrimary (citable) accession number: P61292
Secondary accession number(s): Q20BD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 92 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, Reference proteome

Documents

  1. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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