CPLM-009421

Genbank Nucleotide ID

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
6	**MSDSEKLNLDSII	ubiquitination	[1, 2, 3]
26	VQGSRPGKNVQLTEN	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
41	EIRGLCLKSREIFLS	ubiquitination	[3]
98	GDYVDRGKQSLETIC	ubiquitination	[3, 5, 7]
113	LLLAYKIKYPENFFL	ubiquitination	[2, 3, 5, 7]
141	YGFYDECKRRYNIKL	ubiquitination	[2, 3, 5]
147	CKRRYNIKLWKTFTD	ubiquitination	[2, 3, 4, 5, 6]
150	RYNIKLWKTFTDCFN	ubiquitination	[3]
238	VVAKFLHKHDLDLIC	ubiquitination	[2, 3, 7]
260	DGYEFFAKRQLVTLF	ubiquitination	[2, 3, 5, 6, 7]
305	PADKNKGKYGQFSGL	acetylation	[8, 9]
305	PADKNKGKYGQFSGL	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 9]

[1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[8] 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]
[9] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]

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.

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.
METAL 124 124 Manganese.
METAL 173 173 Manganese.
METAL 248 248 Manganese.
MOD_RES 2 2 N-acetylserine.
MOD_RES 306 306 Phosphotyrosine (By similarity).
MOD_RES 320 320 Phosphothreonine.

3D-structure; Acetylation; Alternative splicing; 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.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0043197; C:dendritic spine; IEA:Compara.
GO:0042587; C:glycogen granule; IEA:Compara.
GO:0070688; C:MLL5-L complex; IDA:UniProtKB.
GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO:0043204; C:perikaryon; IEA:Compara.
GO:0000164; C:protein phosphatase type 1 complex; IEA:Compara.
GO:0072357; C:PTW/PP1 phosphatase complex; IDA:UniProtKB.
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO:0004722; F:protein serine/threonine phosphatase activity; TAS:ProtInc.
GO:0043021; F:ribonucleoprotein complex binding; IEA:Compara.
GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Compara.
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:0030324; P:lung development; IEA:Compara.
GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
GO:0005979; P:regulation of glycogen biosynthetic process; IEA:Compara.
GO:0005981; P:regulation of glycogen catabolic process; IEA:Compara.
GO:0044281; P:small molecule metabolic process; TAS:Reactome.
GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO:0019433; P:triglyceride catabolic process; TAS:Reactome.

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

PF00149; Metallophos

PS00125; SER_THR_PHOSPHATASE

PR00114; STPHPHTASE.