Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P62143 (PP1B_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

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 By similarity.

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. Ref.2

[Myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate. Ref.2

Cofactor

Binds 2 manganese ions per subunit By similarity.

Enzyme regulation

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

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, 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' and forms a complex at the p21 promoter site By similarity. Interacts with PPP1R12B. Ref.2 Ref.3

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.

Biophysicochemical properties

Kinetic parameters:

KM=5 µM for phosphorylase Ref.2

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 sequence or structural similarity. Source: UniProtKB

entrainment of circadian clock by photoperiod

Inferred from sequence or structural similarity. Source: UniProtKB

glycogen metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

protein dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of circadian rhythm

Inferred from sequence or structural similarity. 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 electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

myosin phosphatase activity

Inferred from direct assay Ref.2. Source: UniProtKB

myosin-light-chain-phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

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_0000058782

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

Sequences

Sequence LengthMass (Da)Tools
P62143 [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

[1]"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.
[2]"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.
[3]"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.

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61639 mRNA. Translation: CAA43820.1.
PIRS13829.
RefSeqNP_001095192.1. NM_001101722.1.
UniGeneOcu.3270.

3D structure databases

ProteinModelPortalP62143.
SMRP62143. Positions 1-308.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP62143.

Proteomic databases

PRIDEP62143.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009587.

Organism-specific databases

CTD100009587.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172697.
HOVERGENHBG000216.

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...

Entry information

Entry namePP1B_RABIT
AccessionPrimary (citable) accession number: P62143
Secondary accession number(s): P37140
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 88 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