CPLM-011943

Genbank Nucleotide ID

Interleukin enhancer-binding factor 3

Protein Synonyms/Alias

Double-stranded RNA-binding protein 76; DRBP76; M-phase phosphoprotein 4; MPP4; Nuclear factor associated with dsRNA; NFAR; Nuclear factor of activated T-cells 90 kDa; NF-AT-90; Translational control protein 80; TCP80

DRBF; MPHOSPH4; NF90

Homo sapiens (Human)

Position	Peptide	Type	References
17	DDRHVMAKHSSVYPT	ubiquitination	[1]
81	KEGAGEQKTEHMTRT	acetylation	[2]
100	MRVGLVAKGLLLKGD	acetylation	[2]
100	MRVGLVAKGLLLKGD	ubiquitination	[1, 3, 4, 5, 6]
119	LVLLCKEKPTTALLD	ubiquitination	[5]
202	PDVLDRQKCLAALAS	ubiquitination	[1, 4, 5]
214	LASLRHAKWFQARAN	acetylation	[2]
257	PLELLCEKSIGTANR	ubiquitination	[1, 4, 5]
297	GIYDPCEKEATDAIG	ubiquitination	[5, 7]
332	AAFGQLHKVLGMDPL	ubiquitination	[1, 5, 7]
342	GMDPLPSKMPKKPKN	ubiquitination	[1, 5, 7, 8]
413	LMRLNQLKPGLQYKL	acetylation	[7]
413	LMRLNQLKPGLQYKL	ubiquitination	[1, 4, 5]
460	AKLHVAVKVLQDMGL	acetylation	[2, 7, 9]
540	NEKRRGLKYELISET	ubiquitination	[1]
577	GSNKKVAKAYAALAA	ubiquitination	[1]
600	PLALDANKKKRAPVP	acetylation	[10]
613	VPVRGGPKFAAKPHN	methylation	[11]

[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] 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] 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]
[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] 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]
[6] 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]
[7] 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]
[8] 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]
[9] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
[10] 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]
[11] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837]

Functional Description

May facilitate double-stranded RNA-regulated gene expression at the level of post-transcription. Can act as a translation inhibitory protein which binds to coding sequences of acid beta-glucosidase (GCase) and other mRNAs and functions at the initiation phase of GCase mRNA translation, probably by inhibiting its binding to polysomes. Can regulate protein arginine N- methyltransferase 1 activity. May regulate transcription of the IL2 gene during T-cell activation. Can promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA. The phosphorylated form at Thr-188 and Thr-315, in concert with EIF2AK2/PKR can inhibit vesicular stomatitis virus (VSV) replication (By similarity).

DOMAIN 94 342 DZF.
DOMAIN 398 467 DRBM 1.
DOMAIN 524 590 DRBM 2.
REGION 609 894 Interaction with PRMT1.
MOTIF 371 389 Bipartite nuclear localization signal
MOD_RES 62 62 Phosphoserine.
MOD_RES 100 100 N6-acetyllysine.
MOD_RES 188 188 Phosphothreonine; by PKR.
MOD_RES 190 190 Phosphoserine.
MOD_RES 315 315 Phosphothreonine; by PKR.
MOD_RES 382 382 Phosphoserine.
MOD_RES 384 384 Phosphoserine.
MOD_RES 460 460 N6-acetyllysine.
MOD_RES 476 476 Phosphoserine.
MOD_RES 482 482 Phosphoserine.
MOD_RES 592 592 Phosphothreonine.
MOD_RES 792 792 Phosphoserine.
MOD_RES 812 812 Phosphoserine.

3D-structure; Acetylation; Alternative splicing; Antiviral defense; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Methylation; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding; Transcription; Transcription regulation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005739; C:mitochondrion; IDA:HPA.
GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO:0005634; C:nucleus; IDA:UniProtKB.
GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
GO:0003677; F:DNA binding; IDA:UniProtKB.
GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO:0000279; P:M phase; NAS:UniProtKB.
GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
GO:0045071; P:negative regulation of viral genome replication; ISS:UniProtKB.
GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

IPR001159; Ds-RNA-bd.
IPR014720; dsRNA-bd-like_dom.
IPR006561; DZF.

PF00035; dsrm
PF07528; DZF

SM00358; DSRM
SM00572; DZF