CPLM-022362

Genbank Nucleotide ID

Serine/threonine-protein phosphatase 4 regulatory subunit 2

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
11	ERLQEALKDFEKRGK	ubiquitination	[1]
15	EALKDFEKRGKKEVC	ubiquitination	[1]
52	FKGYFIFKLEKVMDD	ubiquitination	[1]
55	YFIFKLEKVMDDFRT	ubiquitination	[1, 2, 3]
84	YIPFDEMKERILKIV	ubiquitination	[1]
120	RNYTGTDKFLRGVEK	ubiquitination	[1]
127	KFLRGVEKNVMVVSC	ubiquitination	[1]
141	CVYPSSEKNNSNSLN	ubiquitination	[1, 4, 5]
252	VKRLRFDKEGEVRET	acetylation	[6]

[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] 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]
[3] 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]
[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] 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]
[6] 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]

Functional Description

Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers. Its interaction with the SMN complex leads to enhance the temporal localization of snRNPs, suggesting a role of PPP4C in maturation of spliceosomal snRNPs. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on 'Ser-140' (gamma-H2AFX) generated during DNA replication and required for DNA double strand break repair. Mediates RPA2 dephosphorylation by recruiting PPP4C to RPA2 in a DNA damage-dependent manner. RPA2 dephosphorylation is required for the efficient RPA2-mediated recruitment of RAD51 to chromatin following double strand breaks, an essential step for DNA repair.

MOD_RES 159 159 Phosphoserine.
MOD_RES 226 226 Phosphoserine.
MOD_RES 352 352 Phosphoserine (By similarity).

Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005813; C:centrosome; TAS:ProtInc.
GO:0005737; C:cytoplasm; IDA:HPA.
GO:0005634; C:nucleus; IDA:UniProtKB.
GO:0030289; C:protein phosphatase 4 complex; IDA:UniProtKB.
GO:0030674; F:protein binding, bridging; IMP:UniProtKB.
GO:0030362; F:protein phosphatase type 4 regulator activity; IMP:UniProtKB.
GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:UniProtKB.
GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.