Q12905 (ILF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Interleukin enhancer-binding factor 2

Alternative name(s):
Nuclear factor of activated T-cells 45 kDa

Gene names

Name:	ILF2
Synonyms:	NF45
ORF Names:	PRO3063

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7 Ref.8 Ref.11
Subunit structure	Forms heterodimers with ILF3. ILF2-ILF3 heterodimers may also bind to PRKDC/XRCC7: this may stabilize the interaction of PRKDC/XRCC7 and the heterodimeric complex of G22P1/KU70 and XRCC5/KU80. Forms a complex with ILF3, YLPM1, KHDRBS1, RBMX, NCOA5 and PPP1CA. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with IGF2BP1. Ref.7 Ref.8 Ref.11 Ref.12 Ref.13
Subcellular location	Nucleus › nucleolus. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.1 Ref.9 Ref.10 Ref.13
Sequence similarities	Contains 1 DZF domain.
Sequence caution	The sequence AAA20993.1 differs from that shown. Reason: Frameshift at position 376. The sequence AAF29591.1 differs from that shown. Reason: Chimeric cDNA. The sequence CAI13611.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	immune response Inferred from electronic annotation. Source: InterPro positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.11. Source: UniProtKB transcription, DNA-dependent Inferred from direct assay Ref.11. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay Ref.9. Source: UniProtKB ribonucleoprotein complex Inferred from direct assay Ref.13. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro DNA binding Inferred from direct assay Ref.8Ref.1. Source: UniProtKB double-stranded RNA binding Inferred from direct assay Ref.8. Source: UniProtKB transferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PPID	Q08752	4	EBI-357925,EBI-716596

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 390	390	Interleukin enhancer-binding factor 2		PRO_0000126063
Regions
	Domain	104 – 338	235	DZF
	Compositional bias	366 – 372	7	Poly-Glu
	Compositional bias	381 – 384	4	Poly-Glu
Amino acid modifications
	Modified residue	388	1	Phosphothreonine Ref.14

Sequences

	Sequence		Length	Mass (Da)
	Q12905 [UniParc]. Last modified April 12, 2005. Version 2. Checksum: 75BAD022DCD4EE01	FASTA	390	43,062
	10 20 30 40 50 60 MRGDRGRGRG GRFGSRGGPG GGFRPFVPHI PFDFYLCEMA FPRVKPAPDE TSFSEALLKR 70 80 90 100 110 120 NQDLAPNSAE QASILSLVTK INNVIDNLIV APGTFEVQIE EVRQVGSYKK GTMTTGHNVA 130 140 150 160 170 180 DLVVILKILP TLEAVAALGN KVVESLRAQD PSEVLTMLTN ETGFEISSSD ATVKILITTV 190 200 210 220 230 240 PPNLRKLDPE LHLDIKVLQS ALAAIRHARW FEENASQSTV KVLIRLLKDL RIRFPGFEPL 250 260 270 280 290 300 TPWILDLLGH YAVMNNPTRQ PLALNVAYRR CLQILAAGLF LPGSVGITDP CESGNFRVHT 310 320 330 340 350 360 VMTLEQQDMV CYTAQTLVRI LSHGGFRKIL GQEGDASYLA SEISTWDGVI VTPSEKAYEK 370 380 390 PPEKKEGEEE EENTEEPPQG EEEESMETQE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of cyclosporin A- and FK506-sensitive nuclear factor of activated T-cells: NF45 and NF90." Kao P.N., Chen L., Brock G., Ng J., Kenny J., Smith A.J., Corthesy B. J. Biol. Chem. 269:20691-20699(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 62-75; 82-102 AND 330-343, SUBCELLULAR LOCATION.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thymus.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[6]	"Functional prediction of the coding sequences of 32 new genes deduced by analysis of cDNA clones from human fetal liver." Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., Zhou W., Bi J., Zhang Y., Liu M., He F. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-390. Tissue: Fetal liver.
[7]	"DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45." Ting N.S.Y., Kao P.N., Chan D.W., Lintott L.G., Lees-Miller S.P. J. Biol. Chem. 273:2136-2145(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH G22P1; PRKDC AND XRCC5.
[8]	"Autoantibodies define a family of proteins with conserved double-stranded RNA-binding domains as well as DNA binding activity." Satoh M., Shaheen V.M., Kao P.N., Okano T., Shaw M., Yoshida H., Richards H.B., Reeves W.H. J. Biol. Chem. 274:34598-34604(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ILF3.
[9]	"Directed proteomic analysis of the human nucleolus." Andersen J.S., Lyon C.E., Fox A.H., Leung A.K.L., Lam Y.W., Steen H., Mann M., Lamond A.I. Curr. Biol. 12:1-11(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[10]	"Functional proteomic analysis of human nucleolus." Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J. Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"The RNA binding protein nuclear factor 90 functions as both a positive and negative regulator of gene expression in mammalian cells." Reichman T.W., Muniz L.C., Mathews M.B. Mol. Cell. Biol. 22:343-356(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ILF3.
[12]	"The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G." Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N., Glover M., Lamond A.I., Moorhead G.B.G. Biochim. Biophys. Acta 1774:1339-1350(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH ILF3; YLPM1; KHDRBS1; RBMX; NCOA5 AND PPP1CA.
[13]	"Molecular composition of IMP1 ribonucleoprotein granules." Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C. Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION.
[14]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-388, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U10323 mRNA. Translation: AAA20993.1. Frameshift. AY099265 Genomic DNA. Translation: AAM45141.1. AK313364 mRNA. Translation: BAG36164.1. AL713889 Genomic DNA. Translation: CAI13610.1. AL713889 Genomic DNA. Translation: CAI13611.1. Sequence problems. AL713889, AL592150 Genomic DNA. Translation: CAI13612.1. AL592150, AL713889 Genomic DNA. Translation: CAI18796.1. CH471121 Genomic DNA. Translation: EAW53286.1. BC000382 mRNA. Translation: AAH00382.1. AF113702 mRNA. Translation: AAF29591.1. Sequence problems.
IPI	IPI00005198.
PIR	A54857.
RefSeq	NP_001254738.1. NM_001267809.1. NP_004506.2. NM_004515.3.
UniGene	Hs.75117.
3D structure databases
ProteinModelPortal	Q12905.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q12905. 25 interactions.
MINT	MINT-4999942.
STRING	9606.ENSP00000355011.
PTM databases
PhosphoSite	Q12905.
Polymorphism databases
DMDM	62510764.
2D gel databases
SWISS-2DPAGE	Q12905.
Proteomic databases
PaxDb	Q12905.
PRIDE	Q12905.
Protocols and materials databases
DNASU	3608.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000361891; ENSP00000355011; ENSG00000143621. ENST00000368681; ENSP00000357670; ENSG00000143621. ENST00000368684; ENSP00000357673; ENSG00000143621.
GeneID	3608.
KEGG	hsa:3608.
UCSC	uc001fcr.3. human.
Organism-specific databases
CTD	3608.
GeneCards	GC01M153634.
HGNC	HGNC:6037. ILF2.
HPA	HPA007484.
MIM	603181. gene.
neXtProt	NX_Q12905.
PharmGKB	PA29852.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG247512.
HOVERGEN	HBG052120.
InParanoid	Q12905.
KO	K13089.
OMA	FEENAHH.
OrthoDB	EOG4HHP2Q.
Gene expression databases
ArrayExpress	Q12905.
Bgee	Q12905.
CleanEx	HS_ILF2.
Genevestigator	Q12905.
GermOnline	ENSG00000143621. Homo sapiens.
Family and domain databases
InterPro	IPR006116. 2-5-oligoadenylate_synth_N. IPR006561. DZF. [Graphical view]
Pfam	PF07528. DZF. 1 hit. [Graphical view]
SMART	SM00572. DZF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ILF2. human.
GenomeRNAi	3608.
NextBio	14105.
SOURCE	Search...

Entry information

Entry name

ILF2_HUMAN

Accession

Primary (citable) accession number: Q12905
Secondary accession number(s): A6NDB0 , B2R8G7, Q5SR10, Q5SR11, Q7L7R3, Q9BWD4, Q9P1N0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	April 12, 2005
Last modified:	May 1, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.