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Protein

Interleukin enhancer-binding factor 2

Gene

ILF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. DNA binding Source: UniProtKB
  3. double-stranded RNA binding Source: UniProtKB
  4. poly(A) RNA binding Source: UniProtKB
  5. transferase activity Source: InterPro

GO - Biological processi

  1. immune response Source: InterPro
  2. positive regulation of transcription, DNA-templated Source: UniProtKB
  3. transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin enhancer-binding factor 2
Alternative name(s):
Nuclear factor of activated T-cells 45 kDa
Gene namesi
Name:ILF2
Synonyms:NF45
ORF Names:PRO3063
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6037. ILF2.

Subcellular locationi

Nucleusnucleolus. Cytoplasm. Nucleus
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. membrane Source: UniProtKB
  3. nucleolus Source: UniProtKB
  4. nucleoplasm Source: HPA
  5. nucleus Source: UniProtKB
  6. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29852.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390Interleukin enhancer-binding factor 2PRO_0000126063Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei388 – 3881Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12905.
PaxDbiQ12905.
PRIDEiQ12905.

2D gel databases

SWISS-2DPAGEQ12905.

PTM databases

PhosphoSiteiQ12905.

Expressioni

Gene expression databases

BgeeiQ12905.
CleanExiHS_ILF2.
ExpressionAtlasiQ12905. baseline and differential.
GenevestigatoriQ12905.

Organism-specific databases

HPAiHPA007484.

Interactioni

Subunit structurei

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 IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with IGF2BP1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PPIDQ087524EBI-357925,EBI-716596

Protein-protein interaction databases

BioGridi109821. 250 interactions.
IntActiQ12905. 62 interactions.
MINTiMINT-4999942.
STRINGi9606.ENSP00000355011.

Structurei

3D structure databases

ProteinModelPortaliQ12905.
SMRiQ12905. Positions 29-361.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 371348DZFPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi366 – 3727Poly-Glu
Compositional biasi381 – 3844Poly-Glu

Sequence similaritiesi

Contains 1 DZF domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG247512.
GeneTreeiENSGT00550000074528.
HOVERGENiHBG052120.
InParanoidiQ12905.
KOiK13089.
OMAiYEKPPER.
OrthoDBiEOG75XGM4.
PhylomeDBiQ12905.
TreeFamiTF320194.

Family and domain databases

InterProiIPR006116. 2-5-oligoadenylate_synth_N.
IPR006561. DZF_dom.
[Graphical view]
PfamiPF07528. DZF. 1 hit.
[Graphical view]
SMARTiSM00572. DZF. 1 hit.
[Graphical view]
PROSITEiPS51703. DZF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12905-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGDRGRGRG GRFGSRGGPG GGFRPFVPHI PFDFYLCEMA FPRVKPAPDE
60 70 80 90 100
TSFSEALLKR NQDLAPNSAE QASILSLVTK INNVIDNLIV APGTFEVQIE
110 120 130 140 150
EVRQVGSYKK GTMTTGHNVA DLVVILKILP TLEAVAALGN KVVESLRAQD
160 170 180 190 200
PSEVLTMLTN ETGFEISSSD ATVKILITTV PPNLRKLDPE LHLDIKVLQS
210 220 230 240 250
ALAAIRHARW FEENASQSTV KVLIRLLKDL RIRFPGFEPL TPWILDLLGH
260 270 280 290 300
YAVMNNPTRQ PLALNVAYRR CLQILAAGLF LPGSVGITDP CESGNFRVHT
310 320 330 340 350
VMTLEQQDMV CYTAQTLVRI LSHGGFRKIL GQEGDASYLA SEISTWDGVI
360 370 380 390
VTPSEKAYEK PPEKKEGEEE EENTEEPPQG EEEESMETQE
Length:390
Mass (Da):43,062
Last modified:April 12, 2005 - v2
Checksum:i75BAD022DCD4EE01
GO

Sequence cautioni

The sequence AAA20993.1 differs from that shown. Reason: Frameshift at position 376. Curated
The sequence AAF29591.1 differs from that shown.Chimeric cDNA.Curated
The sequence CAI13611.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1050.1.
PIRiA54857.
RefSeqiNP_001254738.1. NM_001267809.1.
NP_004506.2. NM_004515.3.
UniGeneiHs.75117.

Genome annotation databases

EnsembliENST00000361891; ENSP00000355011; ENSG00000143621.
GeneIDi3608.
KEGGihsa:3608.
UCSCiuc001fcr.4. human.

Polymorphism databases

DMDMi62510764.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1050.1.
PIRiA54857.
RefSeqiNP_001254738.1. NM_001267809.1.
NP_004506.2. NM_004515.3.
UniGeneiHs.75117.

3D structure databases

ProteinModelPortaliQ12905.
SMRiQ12905. Positions 29-361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109821. 250 interactions.
IntActiQ12905. 62 interactions.
MINTiMINT-4999942.
STRINGi9606.ENSP00000355011.

PTM databases

PhosphoSiteiQ12905.

Polymorphism databases

DMDMi62510764.

2D gel databases

SWISS-2DPAGEQ12905.

Proteomic databases

MaxQBiQ12905.
PaxDbiQ12905.
PRIDEiQ12905.

Protocols and materials databases

DNASUi3608.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361891; ENSP00000355011; ENSG00000143621.
GeneIDi3608.
KEGGihsa:3608.
UCSCiuc001fcr.4. human.

Organism-specific databases

CTDi3608.
GeneCardsiGC01M153634.
HGNCiHGNC:6037. ILF2.
HPAiHPA007484.
MIMi603181. gene.
neXtProtiNX_Q12905.
PharmGKBiPA29852.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG247512.
GeneTreeiENSGT00550000074528.
HOVERGENiHBG052120.
InParanoidiQ12905.
KOiK13089.
OMAiYEKPPER.
OrthoDBiEOG75XGM4.
PhylomeDBiQ12905.
TreeFamiTF320194.

Miscellaneous databases

ChiTaRSiILF2. human.
GeneWikiiILF2.
GenomeRNAii3608.
NextBioi14105.
PROiQ12905.
SOURCEiSearch...

Gene expression databases

BgeeiQ12905.
CleanExiHS_ILF2.
ExpressionAtlasiQ12905. baseline and differential.
GenevestigatoriQ12905.

Family and domain databases

InterProiIPR006116. 2-5-oligoadenylate_synth_N.
IPR006561. DZF_dom.
[Graphical view]
PfamiPF07528. DZF. 1 hit.
[Graphical view]
SMARTiSM00572. DZF. 1 hit.
[Graphical view]
PROSITEiPS51703. DZF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1993) [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(2003) [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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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(2003) [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 (NOV-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(1997) [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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ILF3.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    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(2001) [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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH ILF3; YLPM1; KHDRBS1; RBMX; NCOA5 AND PPP1CA.
  13. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  15. "Phosphorylation of the NFAR proteins by the dsRNA-dependent protein kinase PKR constitutes a novel mechanism of translational regulation and cellular defense."
    Harashima A., Guettouche T., Barber G.N.
    Genes Dev. 24:2640-2653(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiILF2_HUMAN
AccessioniPrimary (citable) accession number: Q12905
Secondary accession number(s): A6NDB0
, B2R8G7, Q5SR10, Q5SR11, Q7L7R3, Q9BWD4, Q9P1N0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: April 12, 2005
Last modified: March 4, 2015
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.