CPLM-012542

Genbank Nucleotide ID

Poly(rC)-binding protein 2

Protein Synonyms/Alias

Alpha-CP2; Heterogeneous nuclear ribonucleoprotein E2; hnRNP E2

Homo sapiens (Human)

Position	Peptide	Type	References
23	IRLLMHGKEVGSIIG	ubiquitination	[1, 2, 3, 4]
31	EVGSIIGKKGESVKK	ubiquitination	[1, 2, 3]
115	QCGSLIGKGGCKIKE	ubiquitination	[1, 2, 3, 4, 5, 6]
185	VTIPYRPKPSSSPVI	ubiquitination	[1, 4, 6]
309	IIGRQGAKINEIRQM	ubiquitination	[6]
322	QMSGAQIKIANPVEG	ubiquitination	[1, 2, 3, 4, 5, 6]

[1] 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]
[2] 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]
[3] 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]
[4] 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]
[5] 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]
[6] 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]

Functional Description

Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. Major cellular poly(rC)-binding protein. Binds also poly(rU). Negatively regulates cellular antiviral responses mediated by MAVS signaling. It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitinationa and degradation.

DOMAIN 13 75 KH 1.
DOMAIN 97 162 KH 2.
DOMAIN 287 351 KH 3.
MOD_RES 173 173 Phosphoserine.
MOD_RES 189 189 Phosphoserine.
MOD_RES 272 272 Phosphoserine.
MOD_RES 364 364 Phosphoserine.
MOD_RES 365 365 Phosphoserine.

3D-structure; Alternative splicing; Antiviral defense; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Immunity; Innate immunity; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO:0003723; F:RNA binding; IDA:UniProtKB.
GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO:0045087; P:innate immune response; TAS:Reactome.
GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO:0050687; P:negative regulation of defense response to virus; IMP:UniProtKB.
GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.

IPR004087; KH_dom.
IPR004088; KH_dom_type_1.