P62143 (PP1B_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified May 1, 2013. Version 78. History...
Names and origin
|Protein names||Recommended name:|
Serine/threonine-protein phosphatase PP1-beta catalytic subunit
|Organism||Oryctolagus cuniculus (Rabbit) [Reference proteome]|
|Taxonomic identifier||9986 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus|
|Sequence length||327 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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 By similarity.
A phosphoprotein + H2O = a protein + phosphate. Ref.2
[Myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate. Ref.2
Binds 1 iron ion per subunit By similarity.
Binds 1 manganese ion per subunit By similarity.
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. Inhibited by the toxins okadaic acid, tautomycin and microcystin Leu-Arg. Ref.2
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, 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 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' and forms a complex at the p21 promoter site By similarity. Interacts with PPP1R12B. Ref.2 Ref.3
Cytoplasm By similarity. Nucleus By similarity. Nucleus › nucleoplasm By similarity. Nucleus › nucleolus 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.
KM=5 µM for phosphorylase Ref.2
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Initiator methionine||1||1||Removed By similarity|
|Chain||2 – 327||326||Serine/threonine-protein phosphatase PP1-beta catalytic subunit||PRO_0000058782|
|Active site||124||1||Proton donor By similarity|
|Metal binding||63||1||Iron By similarity|
|Metal binding||65||1||Iron By similarity|
|Metal binding||91||1||Iron By similarity|
|Metal binding||91||1||Manganese By similarity|
|Metal binding||123||1||Manganese By similarity|
|Metal binding||172||1||Manganese By similarity|
|Metal binding||247||1||Manganese By similarity|
Amino acid modifications
|Modified residue||2||1||N-acetylalanine By similarity|
|Modified residue||316||1||Phosphothreonine By similarity|
|||"Drosophila contains three genes that encode distinct isoforms of protein phosphatase 1."|
Dombradi V., Axton J.M., Brewis N.D., da Cruz e Silva E.F., Alphey L., Cohen P.T.W.
Eur. J. Biochem. 194:739-745(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: New Zealand white.
|||"A myofibrillar protein phosphatase from rabbit skeletal muscle contains the beta isoform of protein phosphatase-1 complexed to a regulatory subunit which greatly enhances the dephosphorylation of myosin."|
Dent P., MacDougall L.K., MacKintosh C., Campbell D.G., Cohen P.
Eur. J. Biochem. 210:1037-1044(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-35; 60-73; 147-149; 168-186; 222-232; 246-259 AND 304-319, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Strain: New Zealand white.
Tissue: Skeletal muscle.
|||"The major myosin phosphatase in skeletal muscle is a complex between the beta-isoform of protein phosphatase 1 and the MYPT2 gene product."|
Moorhead G., Johnson D., Morrice N., Cohen P.
FEBS Lett. 438:141-144(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 43-48; 113-121; 132-140; 150-165; 168-186; 188-204; 246-255 AND 267-286, INTERACTION WITH PPP1R12B.
Tissue: Skeletal muscle.
|Protein Spotlight |
The things we forget - Issue 32 of March 2003
|X61639 mRNA. Translation: CAA43820.1.|
|RefSeq||NP_001095192.1. NM_001101722.1. |
3D structure databases
Protocols and materials databases
Genome annotation databases
Family and domain databases
|InterPro||IPR004843. Metallo_PEstase_dom. |
|Pfam||PF00149. Metallophos. 1 hit. |
|PRINTS||PR00114. STPHPHTASE. |
|SMART||SM00156. PP2Ac. 1 hit. |
|PROSITE||PS00125. SER_THR_PHOSPHATASE. 1 hit. |
|Accession||Primary (citable) accession number: P62143|
Secondary accession number(s): P37140
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|