UniProt Accession

 PP1B_MOUSE; P62141; P37140; Q3TBE5; Q3TL90; Q542E7; Q8C285; Q9DBY2 

Genbank Protein ID

 M27073; AK004686; AK088893; AK089067; AK147112; AK160743; AK166168; AK166623; AK168141; AK169379; AK171283; BC046832 

Genbank Nucleotide ID

 AAA37527.1; BAB23473.1; BAC40636.1; BAC40733.1; BAE27684.1; BAE35984.1; BAE38608.1; BAE38902.1; BAE40108.1; BAE41126.1; BAE42366.1; AAH46832.1 

Protein Name

 Serine/threonine-protein phosphatase PP1-beta catalytic subunit 

Protein Synonyms/Alias

 PP-1B 

Gene Name

 Ppp1cb 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
25	VRGCRPGKIVQMTEA	acetylation	[1, 2]
25	VRGCRPGKIVQMTEA	ubiquitination	[3]
112	LLLAYKIKYPENFFL	acetylation	[1]
112	LLLAYKIKYPENFFL	ubiquitination	[3]
146	CKRRFNIKLWKTFTD	acetylation	[1]
146	CKRRFNIKLWKTFTD	ubiquitination	[3]
303	KPSEKKAKYQYGGLN	ubiquitination	[3]

Reference

 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 

Functional Description

 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). 

Sequence Annotation

 ACT_SITE 124 124 Proton donor (By similarity).
 METAL 63 63 Iron (By similarity).
 METAL 65 65 Iron (By similarity).
 METAL 91 91 Iron (By similarity).
 METAL 91 91 Manganese (By similarity).
 METAL 123 123 Manganese (By similarity).
 METAL 172 172 Manganese (By similarity).
 METAL 247 247 Manganese (By similarity).
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 316 316 Phosphothreonine.  

Keyword

 Acetylation; Carbohydrate metabolism; Cell cycle; Cell division; Complete proteome; Cytoplasm; Direct protein sequencing; Glycogen metabolism; Hydrolase; Iron; Manganese; Metal-binding; Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 327 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0042587; C:glycogen granule; IEA:Compara.
 GO:0070688; C:MLL5-L complex; IEA:Compara.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0000164; C:protein phosphatase type 1 complex; IEA:Compara.
 GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0017018; F:myosin phosphatase activity; ISS:UniProtKB.
 GO:0050115; F:myosin-light-chain-phosphatase activity; ISS:UniProtKB.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
 GO:0006470; P:protein dephosphorylation; IDA:MGI.
 GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
 GO:0005979; P:regulation of glycogen biosynthetic process; IEA:Compara.
 GO:0005981; P:regulation of glycogen catabolic process; IEA:Compara. 

Interpro

 IPR004843; Metallo_PEstase_dom.
 IPR006186; Ser/Thr-sp_prot-phosphatase. 

Pfam

 PF00149; Metallophos 

SMART

 SM00156; PP2Ac 

PROSITE

 PS00125; SER_THR_PHOSPHATASE 

PRINTS

 PR00114; STPHPHTASE.