Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Interleukin enhancer-binding factor 2

Gene

Ilf2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity). Essential for the efficient reshuttling of ILF3 into the nucleus (By similarity).By similarity

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: MGI
  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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1915031. Ilf2.

Subcellular locationi

Nucleusnucleolus 1 Publication. Cytoplasm By similarity. Nucleus By similarity
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390Interleukin enhancer-binding factor 2PRO_0000126064Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei388 – 3881PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9CXY6.
PaxDbiQ9CXY6.
PRIDEiQ9CXY6.

PTM databases

PhosphoSiteiQ9CXY6.

Expressioni

Tissue specificityi

Expressed in brain, kidney and ovary; highly expressed in testis, particularly within pachytene cells.1 Publication

Developmental stagei

Expression in testis begins with developmental differentiation of pachytene spermatocytes.1 Publication

Gene expression databases

BgeeiQ9CXY6.
CleanExiMM_ILF2.
GenevestigatoriQ9CXY6.

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi212438. 4 interactions.
IntActiQ9CXY6. 4 interactions.
MINTiMINT-4125797.

Structurei

Secondary structure

1
390
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 363Combined sources
Helixi38 – 403Combined sources
Helixi51 – 6414Combined sources
Helixi68 – 9023Combined sources
Turni94 – 985Combined sources
Beta strandi99 – 1057Combined sources
Helixi106 – 1105Combined sources
Beta strandi119 – 12810Combined sources
Helixi132 – 14918Combined sources
Beta strandi151 – 1533Combined sources
Beta strandi156 – 1605Combined sources
Beta strandi163 – 1675Combined sources
Beta strandi172 – 1798Combined sources
Helixi181 – 1855Combined sources
Turni189 – 1913Combined sources
Helixi195 – 21420Combined sources
Helixi218 – 23316Combined sources
Helixi235 – 2373Combined sources
Helixi242 – 25413Combined sources
Beta strandi256 – 2605Combined sources
Helixi264 – 27613Combined sources
Turni277 – 2804Combined sources
Beta strandi292 – 2943Combined sources
Helixi298 – 3014Combined sources
Helixi304 – 32219Combined sources
Helixi326 – 3294Combined sources
Beta strandi332 – 3343Combined sources
Helixi337 – 3404Combined sources
Beta strandi344 – 3463Combined sources
Beta strandi349 – 3513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AT7X-ray1.90A29-390[»]
4AT8X-ray2.69A/C29-390[»]
4AT9X-ray2.80A29-390[»]
4ATBX-ray3.10A/C29-390[»]
ProteinModelPortaliQ9CXY6.
SMRiQ9CXY6. 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.
HOGENOMiHOG000067801.
HOVERGENiHBG052120.
InParanoidiQ9CXY6.
KOiK13089.
OMAiYEKPPER.
OrthoDBiEOG75XGM4.
PhylomeDBiQ9CXY6.
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.

Q9CXY6-1 [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:May 31, 2001 - v1
Checksum:i75BAD022DCD4EE01
GO

Sequence cautioni

The sequence BAC27594.1 differs from that shown.Intron retention.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF458249 Genomic DNA. Translation: AAL59388.1.
AK013858 mRNA. Translation: BAB29021.1.
AK031892 mRNA. Translation: BAC27594.1. Sequence problems.
AK078003 mRNA. Translation: BAC37097.1.
AK157129 mRNA. Translation: BAE33972.1.
BC004033 mRNA. Translation: AAH04033.1.
BC024718 mRNA. Translation: AAH24718.1.
CCDSiCCDS17530.1.
RefSeqiNP_080650.1. NM_026374.3.
UniGeneiMm.227258.

Genome annotation databases

EnsembliENSMUST00000001042; ENSMUSP00000001042; ENSMUSG00000001016.
GeneIDi67781.
KEGGimmu:67781.
UCSCiuc008qcj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF458249 Genomic DNA. Translation: AAL59388.1.
AK013858 mRNA. Translation: BAB29021.1.
AK031892 mRNA. Translation: BAC27594.1. Sequence problems.
AK078003 mRNA. Translation: BAC37097.1.
AK157129 mRNA. Translation: BAE33972.1.
BC004033 mRNA. Translation: AAH04033.1.
BC024718 mRNA. Translation: AAH24718.1.
CCDSiCCDS17530.1.
RefSeqiNP_080650.1. NM_026374.3.
UniGeneiMm.227258.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AT7X-ray1.90A29-390[»]
4AT8X-ray2.69A/C29-390[»]
4AT9X-ray2.80A29-390[»]
4ATBX-ray3.10A/C29-390[»]
ProteinModelPortaliQ9CXY6.
SMRiQ9CXY6. Positions 29-361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212438. 4 interactions.
IntActiQ9CXY6. 4 interactions.
MINTiMINT-4125797.

PTM databases

PhosphoSiteiQ9CXY6.

Proteomic databases

MaxQBiQ9CXY6.
PaxDbiQ9CXY6.
PRIDEiQ9CXY6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001042; ENSMUSP00000001042; ENSMUSG00000001016.
GeneIDi67781.
KEGGimmu:67781.
UCSCiuc008qcj.1. mouse.

Organism-specific databases

CTDi3608.
MGIiMGI:1915031. Ilf2.

Phylogenomic databases

eggNOGiNOG247512.
GeneTreeiENSGT00550000074528.
HOGENOMiHOG000067801.
HOVERGENiHBG052120.
InParanoidiQ9CXY6.
KOiK13089.
OMAiYEKPPER.
OrthoDBiEOG75XGM4.
PhylomeDBiQ9CXY6.
TreeFamiTF320194.

Miscellaneous databases

ChiTaRSiIlf2. mouse.
NextBioi325549.
PROiQ9CXY6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CXY6.
CleanExiMM_ILF2.
GenevestigatoriQ9CXY6.

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].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Head, Medulla oblongata and Spleen.
  3. "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].
    Strain: Czech II.
    Tissue: Mammary tumor.
  4. "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.
  5. "Ilf2 is regulated during meiosis and associated to transcriptionally active chromatin."
    Lopez-Fernandez L.A., Parraga M., del Mazo J.
    Mech. Dev. 111:153-157(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.

Entry informationi

Entry nameiILF2_MOUSE
AccessioniPrimary (citable) accession number: Q9CXY6
Secondary accession number(s): Q3U083
, Q5RKG0, Q8CCY9, Q99KS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 11, 2005
Last sequence update: May 31, 2001
Last modified: March 3, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.