Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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P62143 (PP1B_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

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

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity.
Catalytic activity	A phosphoprotein + H₂O = a protein + phosphate. Ref.2 [Myosin light-chain] phosphate + H₂O = [myosin light-chain] + phosphate. Ref.2
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion 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 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. 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.
Sequence similarities	Belongs to the PPP phosphatase family. PP-1 subfamily.
Biophysicochemical properties	Kinetic parameters: K_M=5 µM for phosphorylase Ref.2

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell cycle Cell division Glycogen metabolism
Cellular component	Cytoplasm Nucleus
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW glycogen metabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein dephosphorylation Inferred from electronic annotation. Source: Compara regulation of cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	MLL5-L complex Inferred from electronic annotation. Source: Compara 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_function	metal 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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 327

326

Serine/threonine-protein phosphatase PP1-beta catalytic subunit

PRO_0000058782

Sites

Active site

124

Proton donor By similarity

Metal binding

Iron By similarity

Metal binding

Iron By similarity

Metal binding

Iron By similarity

Metal binding

Manganese By similarity

Metal binding

123

Manganese By similarity

Metal binding

172

Manganese By similarity

Metal binding

247

Manganese By similarity

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

316

Phosphothreonine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P62143 [UniParc].

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

327

37,187

        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

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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.
PIR	S13829.
RefSeq	NP_001095192.1. NM_001101722.1.
UniGene	Ocu.3270.
3D structure databases
ProteinModelPortal	P62143.
ModBase	Search...
Proteomic databases
PRIDE	P62143.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100009587.
Organism-specific databases
CTD	100009587.
Phylogenomic databases
eggNOG	COG0639.
HOGENOM	HOG000172697.
HOVERGEN	HBG000216.
OrthoDB	EOG4MKNGK.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P62143.
ChEMBL	CHEMBL5590.

Entry information

Entry name

PP1B_RABIT

Accession

Primary (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:	May 1, 2013
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents