UniProt Accession

 ILF2_HUMAN; Q12905; A6NDB0; B2R8G7; Q5SR10; Q5SR11; Q7L7R3; Q9BWD4; Q9P1N0 

Genbank Protein ID

 U10323; AY099265; AK313364; AL713889; AL713889; AL713889; AL592150; AL592150; AL713889; CH471121; BC000382; AF113702 

Genbank Nucleotide ID

 AAA20993.1; AAM45141.1; BAG36164.1; CAI13610.1; CAI13611.1; CAI13612.1; CAI13612.1; CAI18796.1; CAI18796.1; EAW53286.1; AAH00382.1; AAF29591.1 

Protein Name

 Interleukin enhancer-binding factor 2 

Protein Synonyms/Alias

 Nuclear factor of activated T-cells 45 kDa 

Gene Name

 ILF2 

Gene Synonyms/Alias

 NF45; PRO3063 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
45	EMAFPRVKPAPDETS	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8]
59	SFSEALLKRNQDLAP	acetylation	[8]
59	SFSEALLKRNQDLAP	ubiquitination	[2, 3, 5, 6, 7, 8, 9, 10]
110	RQVGSYKKGTMTTGH	ubiquitination	[3]
141	AVAALGNKVVESLRA	ubiquitination	[4, 6, 7, 11]
186	TVPPNLRKLDPELHL	ubiquitination	[2, 3, 6, 7]
196	PELHLDIKVLQSALA	ubiquitination	[2, 3, 7]
221	NASQSTVKVLIRLLK	ubiquitination	[2, 3, 4]
328	LSHGGFRKILGQEGD	ubiquitination	[2, 3, 4, 6, 7, 11]
356	VIVTPSEKAYEKPPE	ubiquitination	[2, 3]
360	PSEKAYEKPPEKKEG	ubiquitination	[3]
364	AYEKPPEKKEGEEEE	ubiquitination	[3]
365	YEKPPEKKEGEEEEE	ubiquitination	[3]

Reference

 [1] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [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] 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]
 [4] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [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] 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]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865] 

Functional Description

 Appears to function predominantly as a heterodimeric complex with ILF3. This complex may regulate transcription of the IL2 gene during T-cell activation. It can also promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA. Essential for the efficient reshuttling of ILF3 (isoform 1 and isoform 2) into the nucleus. 

Sequence Annotation

 DOMAIN 104 338 DZF.
 MOD_RES 388 388 Phosphothreonine.  

Keyword

 Activator; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 390 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0003677; F:DNA binding; IDA:UniProtKB.
 GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
 GO:0016740; F:transferase activity; IEA:InterPro.
 GO:0006955; P:immune response; IEA:InterPro.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IDA:UniProtKB. 

Interpro

 IPR006116; 2-5-oligoadenylate_synth_N.
 IPR006561; DZF. 

Pfam

 PF07528; DZF 

SMART

 SM00572; DZF 

PROSITE

  

PRINTS