CPLM-000769

Genbank Nucleotide ID

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
47	KYPSLGQKPGGSDFL	ubiquitination	[1]
63	KRLQKGQKYFDSGDY	acetylation	[2]
63	KRLQKGQKYFDSGDY	ubiquitination	[1, 3]
74	SGDYNMAKAKMKNKQ	ubiquitination	[1, 4, 5]
76	DYNMAKAKMKNKQLP	ubiquitination	[1]
114	KSSLVTSKLAGGQVE	ubiquitination	[1]

[1] 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]
[2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[3] 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]
[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] 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]

Functional Description

Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-67 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase (By similarity). Also acts as a stimulator of insulin secretion by interacting with sulfonylurea receptor (ABCC8), thereby preventing sulfonylurea from binding to its receptor and reducing K(ATP) channel currents.

MOD_RES 2 2 N-acetylserine.
MOD_RES 2 2 Phosphoserine.
MOD_RES 67 67 Phosphoserine; by GWL (Probable).
MOD_RES 109 109 Phosphoserine; by PKA.

Acetylation; Alternative splicing; Cell cycle; Cell division; Complete proteome; Cytoplasm; Mitosis; Phosphoprotein; Protein phosphatase inhibitor; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0008200; F:ion channel inhibitor activity; TAS:ProtInc.
GO:0019212; F:phosphatase inhibitor activity; ISS:UniProtKB.
GO:0051721; F:protein phosphatase 2A binding; ISS:UniProtKB.
GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
GO:0008601; F:protein phosphatase type 2A regulator activity; ISS:UniProtKB.
GO:0005102; F:receptor binding; TAS:ProtInc.
GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
GO:0007067; P:mitosis; ISS:UniProtKB.
GO:0009749; P:response to glucose stimulus; IEA:Compara.
GO:0007584; P:response to nutrient; TAS:ProtInc.
GO:0006810; P:transport; TAS:ProtInc.

IPR006760; Endosulphine.

PF04667; Endosulfine