CPLM-009424

Genbank Nucleotide ID

Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
25	VRGCRPGKIVQMTEA	ubiquitination	[1, 2, 3]
59	LELEAPLKICGDIHG	ubiquitination	[4]
97	GDYVDRGKQSLETIC	ubiquitination	[4]
112	LLLAYKIKYPENFFL	ubiquitination	[5]
140	YGFYDECKRRFNIKL	ubiquitination	[4, 5]
146	CKRRFNIKLWKTFTD	ubiquitination	[1, 2, 3, 5, 6]
149	RFNIKLWKTFTDCFN	ubiquitination	[3]
210	LLWSDPDKDVQGWGE	ubiquitination	[7]
233	FGADVVSKFLNRHDL	ubiquitination	[1, 4, 7]
259	DGYEFFAKRQLVTLF	ubiquitination	[4, 5]
303	KPSEKKAKYQYGGLN	acetylation	[8]
303	KPSEKKAKYQYGGLN	ubiquitination	[1, 3, 5, 6, 7, 9]

[1] 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]
[2] 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]
[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] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[5] 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]
[6] 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]
[7] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[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 (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.

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.
MOD_RES 316 316 Phosphothreonine.

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.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0042587; C:glycogen granule; IEA:Compara.
GO:0070688; C:MLL5-L complex; IDA:UniProtKB.
GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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:0017018; F:myosin phosphatase activity; ISS:UniProtKB.
GO:0050115; F:myosin-light-chain-phosphatase activity; IDA:UniProtKB.
GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO:0006470; P:protein dephosphorylation; IEA:Compara.
GO:0030155; P:regulation of cell adhesion; IDA:UniProtKB.
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.