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Q9CXY6

- ILF2_MOUSE

UniProt

Q9CXY6 - ILF2_MOUSE

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Protein
Interleukin enhancer-binding factor 2
Gene
Ilf2, Nf45
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.1 Publication

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. DNA binding Source: UniProtKB
  3. double-stranded RNA binding Source: UniProtKB
  4. transferase activity Source: InterPro
Complete GO annotation...

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: Chromosome 3

Organism-specific databases

MGIiMGI:1915031. Ilf2.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleolus Source: UniProtKB
  3. nucleus Source: UniProtKB
  4. 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 2
PRO_0000126064Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei388 – 3881Phosphothreonine By 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.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 371348DZF
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 DZF domain.

Phylogenomic databases

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

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9CXY6-1 [UniParc]FASTAAdd to Basket

« Hide

MRGDRGRGRG GRFGSRGGPG GGFRPFVPHI PFDFYLCEMA FPRVKPAPDE    50
TSFSEALLKR NQDLAPNSAE QASILSLVTK INNVIDNLIV APGTFEVQIE 100
EVRQVGSYKK GTMTTGHNVA DLVVILKILP TLEAVAALGN KVVESLRAQD 150
PSEVLTMLTN ETGFEISSSD ATVKILITTV PPNLRKLDPE LHLDIKVLQS 200
ALAAIRHARW FEENASQSTV KVLIRLLKDL RIRFPGFEPL TPWILDLLGH 250
YAVMNNPTRQ PLALNVAYRR CLQILAAGLF LPGSVGITDP CESGNFRVHT 300
VMTLEQQDMV CYTAQTLVRI LSHGGFRKIL GQEGDASYLA SEISTWDGVI 350
VTPSEKAYEK PPEKKEGEEE EENTEEPPQG EEEESMETQE 390
Length:390
Mass (Da):43,062
Last modified:June 1, 2001 - v1
Checksum:i75BAD022DCD4EE01
GO

Sequence cautioni

The sequence BAC27594.1 differs from that shown. Reason: Intron retention.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS17530.1.
RefSeqi NP_080650.1. NM_026374.3.
UniGenei Mm.227258.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4AT7 X-ray 1.90 A 29-390 [» ]
4AT8 X-ray 2.69 A/C 29-390 [» ]
4AT9 X-ray 2.80 A 29-390 [» ]
4ATB X-ray 3.10 A/C 29-390 [» ]
ProteinModelPortali Q9CXY6.
SMRi Q9CXY6. Positions 29-361.
ModBasei Search...

Protein-protein interaction databases

BioGridi 212438. 4 interactions.
IntActi Q9CXY6. 4 interactions.
MINTi MINT-4125797.

PTM databases

PhosphoSitei Q9CXY6.

Proteomic databases

MaxQBi Q9CXY6.
PaxDbi Q9CXY6.
PRIDEi Q9CXY6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000001042 ; ENSMUSP00000001042 ; ENSMUSG00000001016 .
GeneIDi 67781.
KEGGi mmu:67781.
UCSCi uc008qcj.1. mouse.

Organism-specific databases

CTDi 3608.
MGIi MGI:1915031. Ilf2.

Phylogenomic databases

eggNOGi NOG247512.
GeneTreei ENSGT00550000074528.
HOGENOMi HOG000067801.
HOVERGENi HBG052120.
InParanoidi Q9CXY6.
KOi K13089.
OMAi FEENAHH.
OrthoDBi EOG75XGM4.
PhylomeDBi Q9CXY6.
TreeFami TF320194.

Miscellaneous databases

ChiTaRSi ILF2. mouse.
NextBioi 325549.
PROi Q9CXY6.
SOURCEi Search...

Gene expression databases

Bgeei Q9CXY6.
CleanExi MM_ILF2.
Genevestigatori Q9CXY6.

Family and domain databases

InterProi IPR006116. 2-5-oligoadenylate_synth_N.
IPR006561. DZF.
[Graphical view ]
Pfami PF07528. DZF. 1 hit.
[Graphical view ]
SMARTi SM00572. DZF. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1994) [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(2005) [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(2004) [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(1999) [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(2002) [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 12, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 98 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

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