UniProt Accession

 PP1A_MOUSE; P62137; P08129; P20653; P22802; Q3U7G7; Q9Z1G2 

Genbank Protein ID

 U25809; AK007932; AK028392; AK090070; AK151582; AK152667; AK153517; AK159575; AK167244; AK167538; AK167880; AK167981; BC014828 

Genbank Nucleotide ID

 AAC99814.1; BAB25358.1; BAC25928.1; BAC41078.1; BAE30522.1; BAE31402.1; BAE32060.1; BAE35196.1; BAE39365.1; BAE39605.1; BAE39893.1; BAE39973.1; AAH14828.1 

Protein Name

 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit 

Protein Synonyms/Alias

 PP-1A 

Gene Name

 Ppp1ca 

Gene Synonyms/Alias

 Ppp1a 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
26	VQGSRPGKNVQLTEN	ubiquitination	[1]
141	YGFYDECKRRYNIKL	acetylation	[2]
141	YGFYDECKRRYNIKL	ubiquitination	[1]
147	CKRRYNIKLWKTFTD	acetylation	[3]
147	CKRRYNIKLWKTFTD	ubiquitination	[1]
238	VVAKFLHKHDLDLIC	acetylation	[3]
260	DGYEFFAKRQLVTLF	acetylation	[3, 4]
260	DGYEFFAKRQLVTLF	ubiquitination	[1]
305	PADKNKGKYGQFSGL	acetylation	[2, 3]

Reference

 [1] 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]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] 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]
 [4] 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] 

Functional Description

 Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. 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. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. 

Sequence Annotation

 ACT_SITE 125 125 Proton donor (By similarity).
 METAL 64 64 Iron (By similarity).
 METAL 66 66 Iron (By similarity).
 METAL 92 92 Iron (By similarity).
 METAL 92 92 Manganese (By similarity).
 METAL 124 124 Manganese (By similarity).
 METAL 173 173 Manganese (By similarity).
 METAL 248 248 Manganese (By similarity).
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 306 306 Phosphotyrosine.
 MOD_RES 320 320 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

 330 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0043197; C:dendritic spine; IEA:Compara.
 GO:0042587; C:glycogen granule; IEA:Compara.
 GO:0070688; C:MLL5-L complex; IEA:Compara.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; IDA:MGI.
 GO:0043204; C:perikaryon; IEA:Compara.
 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:0004722; F:protein serine/threonine phosphatase activity; IDA:MGI.
 GO:0043021; F:ribonucleoprotein complex binding; IEA:Compara.
 GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007143; P:female meiosis; TAS:MGI.
 GO:0005977; P:glycogen metabolic process; TAS:MGI.
 GO:0030324; P:lung development; IMP:MGI.
 GO:0006470; P:protein dephosphorylation; IDA:MGI.
 GO:0005979; P:regulation of glycogen biosynthetic process; IEA:Compara.
 GO:0005981; P:regulation of glycogen catabolic process; IEA:Compara.
 GO:0006417; P:regulation of translation; TAS:MGI. 

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.