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Q9JIL3

- ILF3_RAT

UniProt

Q9JIL3 - ILF3_RAT

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Protein

Interleukin enhancer-binding factor 3

Gene

Ilf3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

May facilitate double-stranded RNA-regulated gene expression at the level of post-transcription. Can act as a translation inhibitory protein which binds to coding sequences of acid beta-glucosidase (GCase) and other mRNAs and functions at the initiation phase of GCase mRNA translation, probably by inhibiting its binding to polysomes. Can promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA (By similarity). Can regulate protein arginine N-methyltransferase 1 activity. The phosphorylated form at Thr-188 and Thr-315, in concert with EIF2AK2/PKR can inhibit vesicular stomatitis virus (VSV) replication (By similarity).By similarity

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. enzyme binding Source: RGD
  3. RNA binding Source: UniProtKB-KW
  4. sequence-specific DNA binding transcription factor activity Source: RGD

GO - Biological processi

  1. defense response to virus Source: UniProtKB-KW
  2. negative regulation of translation Source: UniProtKB
  3. negative regulation of viral genome replication Source: UniProtKB
  4. protein methylation Source: MGI
  5. protein phosphorylation Source: UniProtKB
  6. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin enhancer-binding factor 3
Gene namesi
Name:Ilf3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi619734. Ilf3.

Subcellular locationi

Nucleusnucleolus By similarity. Cytoplasm By similarity. Nucleus By similarity
Note: TThe unphosphorylated form is retained in the nucleus by ILF2. Phosphorylation at Thr-188 and Thr-315 causes the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3. Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 897897Interleukin enhancer-binding factor 3PRO_0000126072Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei100 – 1001N6-acetyllysineBy similarity
Modified residuei188 – 1881Phosphothreonine; by PKRBy similarity
Modified residuei190 – 1901PhosphoserineBy similarity
Modified residuei315 – 3151Phosphothreonine; by PKRBy similarity
Modified residuei382 – 3821PhosphoserineBy similarity
Modified residuei384 – 3841PhosphoserineBy similarity
Modified residuei460 – 4601N6-acetyllysineBy similarity
Modified residuei476 – 4761PhosphoserineBy similarity
Modified residuei482 – 4821PhosphoserineBy similarity
Modified residuei609 – 6091Omega-N-methylated arginineBy similarity
Modified residuei794 – 7941PhosphoserineBy similarity
Modified residuei814 – 8141PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated at Thr-188 and Thr-315 by PKR in response to RNA viruses. This phosphorylation results in the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3 where it can bind to viral RNAs and impede viral replication (By similarity).By similarity
Methylated by protein arginine N-methyltransferase 1.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ9JIL3.
PRIDEiQ9JIL3.

PTM databases

PhosphoSiteiQ9JIL3.

Expressioni

Gene expression databases

GenevestigatoriQ9JIL3.

Interactioni

Subunit structurei

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with FUS and SMN proteins and with PRMT1. Forms a complex with ILF2. Can also bind to PRKDC/XRCC7: this may stabilize the interaction of PRKDC/XRCC7 and the heterodimeric complex of XRCC6/KU70 and XRCC5/KU80. Forms a heteromeric complex with ZNF346 and ILF3. Found in a nuclear export complex with XPO5, ILF3, Ran and double-stranded RNA or double-stranded minihelix VA1 RNA. Found in a nuclear export complex with XPO5, RAN, ILF3, ZNF346 and double-stranded RNA. Interacts with XPO5 and ZNF346 (By similarity). Forms a complex with ILF2, YLPM1, KHDRBS1, RBMX, NCOA5 and PPP1CA. Interacts with AGO1 and AGO2 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Prmt1Q630092EBI-78714,EBI-78708

Protein-protein interaction databases

BioGridi249972. 1 interaction.
IntActiQ9JIL3. 1 interaction.
STRINGi10116.ENSRNOP00000062871.

Structurei

3D structure databases

ProteinModelPortaliQ9JIL3.
SMRiQ9JIL3. Positions 403-470, 525-589.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 378374DZFPROSITE-ProRule annotationAdd
BLAST
Domaini398 – 46770DRBM 1PROSITE-ProRule annotationAdd
BLAST
Domaini524 – 59067DRBM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni609 – 897289Interaction with PRMT1Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi371 – 38919Bipartite nuclear localization signalSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi385 – 3895Poly-Lys
Compositional biasi634 – 6374Poly-Pro
Compositional biasi640 – 65920Arg/Gly-richAdd
BLAST
Compositional biasi701 – 71010Poly-Gly
Compositional biasi796 – 8005Poly-Gly

Sequence similaritiesi

Contains 2 DRBM (double-stranded RNA-binding) domains.PROSITE-ProRule annotation
Contains 1 DZF domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG307678.
HOGENOMiHOG000232164.
HOVERGENiHBG069915.
InParanoidiQ9JIL3.
KOiK13090.
PhylomeDBiQ9JIL3.

Family and domain databases

Gene3Di3.30.160.20. 2 hits.
InterProiIPR014720. dsRNA-bd_dom.
IPR006561. DZF_dom.
[Graphical view]
PfamiPF00035. dsrm. 2 hits.
PF07528. DZF. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 2 hits.
SM00572. DZF. 1 hit.
[Graphical view]
PROSITEiPS50137. DS_RBD. 2 hits.
PS51703. DZF. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9JIL3-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRPMRIFVND DRHVMAKHSS VYPTQEELEA VQNMVSHTER ALKAVSDWID
60 70 80 90 100
EQEKGNSELS EAENMDTPPD DESKEGAGEQ KAEHMTRTLR GVMRVGLVAK
110 120 130 140 150
GLLLKGDLDL ELVLLCKEKP TTALLDKVAD NLAIQLTTVT EDKYEILQSV
160 170 180 190 200
DDAAIVIKNT KEPPLSLTIH LTSPVVREEM EKVLAGETLS VNDPPDVLDR
210 220 230 240 250
QKCLAALASL RHAKWFQARA NGLKSCVIVI RVLRDLCTRV PTWGPLRGWP
260 270 280 290 300
LELLCEKSIG TANRPMGAGE ALRRVLECLA SGIVMPDGSG IYDPCEKEAT
310 320 330 340 350
DAIGHLDRQQ REDITQSAQH ALRLAAFGQL HKVLGMDPLP SKMPKKPKNE
360 370 380 390 400
NPVDYTVQIP PSTTYAITPM KRPMEEDGEE KSPSKKKKKI QKKEEKAEPP
410 420 430 440 450
QAMNALMRLN QLKPGLQYKL ISQTGPVHAP IFTMSVEVDG STFEASGPSK
460 470 480 490 500
KTAKLHVAVK VLQDMGLPTG AEGRDSSKGE DSAEESDGKP AVVAPPPVVE
510 520 530 540 550
AVSNPSSVFP SDATTEQGPI LTKHGKNPVM ELNEKRRGLK YELISETGGS
560 570 580 590 600
HDKRFVMEVE VDGQKFQGAG SNKKVAKAYA ALAALEKLFP DAPLALEANK
610 620 630 640 650
KKRAPVPVRG GPKFAAKPHN PGFGMGGPMH NEAPPPPNIR GRGRGGNIRG
660 670 680 690 700
RGRGRGFGGT NHGGGYMNAG AGYGSYGYSS NSATAGYSQF YSNGGHYGNA
710 720 730 740 750
GGGGSGGGGG SSSYSSYYQG DSYNSPVPPK HAGKKPLHGG QQKPSYSSGY
760 770 780 790 800
QSHQGQQQPY NQSQYSSYGT PQGKQKGYGH GQGSYSSYSN SYNSPGGGGG
810 820 830 840 850
SDYSYDSKFN YSGSGGRSGG NSYGSSGSSY NTGSHGGYGA GSGGSSSYQG
860 870 880 890
KQGGYSSQSN YSSPGSSQSY SGPASSYQSS QGGYSRNTEH SMNYQYR
Length:897
Mass (Da):95,935
Last modified:April 12, 2005 - v2
Checksum:iACD800D1858539BB
GO
Isoform 2 (identifier: Q9JIL3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MALYHHHFITRRRR

Show »
Length:910
Mass (Da):97,680
Checksum:iD6AB97A4B52E442A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MALYHHHFITRRRR in isoform 2. 1 PublicationVSP_013409

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF220102 mRNA. Translation: AAF31446.1.
AABR03063190 Genomic DNA. No translation available.
AABR03065470 Genomic DNA. No translation available.
RefSeqiNP_445864.1. NM_053412.1. [Q9JIL3-2]
UniGeneiRn.203881.

Genome annotation databases

GeneIDi84472.
KEGGirno:84472.
UCSCiRGD:619734. rat. [Q9JIL3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF220102 mRNA. Translation: AAF31446.1 .
AABR03063190 Genomic DNA. No translation available.
AABR03065470 Genomic DNA. No translation available.
RefSeqi NP_445864.1. NM_053412.1. [Q9JIL3-2 ]
UniGenei Rn.203881.

3D structure databases

ProteinModelPortali Q9JIL3.
SMRi Q9JIL3. Positions 403-470, 525-589.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 249972. 1 interaction.
IntActi Q9JIL3. 1 interaction.
STRINGi 10116.ENSRNOP00000062871.

PTM databases

PhosphoSitei Q9JIL3.

Proteomic databases

PaxDbi Q9JIL3.
PRIDEi Q9JIL3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 84472.
KEGGi rno:84472.
UCSCi RGD:619734. rat. [Q9JIL3-1 ]

Organism-specific databases

CTDi 3609.
RGDi 619734. Ilf3.

Phylogenomic databases

eggNOGi NOG307678.
HOGENOMi HOG000232164.
HOVERGENi HBG069915.
InParanoidi Q9JIL3.
KOi K13090.
PhylomeDBi Q9JIL3.

Miscellaneous databases

NextBioi 616960.
PROi Q9JIL3.

Gene expression databases

Genevestigatori Q9JIL3.

Family and domain databases

Gene3Di 3.30.160.20. 2 hits.
InterProi IPR014720. dsRNA-bd_dom.
IPR006561. DZF_dom.
[Graphical view ]
Pfami PF00035. dsrm. 2 hits.
PF07528. DZF. 1 hit.
[Graphical view ]
SMARTi SM00358. DSRM. 2 hits.
SM00572. DZF. 1 hit.
[Graphical view ]
PROSITEi PS50137. DS_RBD. 2 hits.
PS51703. DZF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3."
    Tang J., Kao P.N., Herschman H.R.
    J. Biol. Chem. 275:19866-19876(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
    Strain: Brown Norway.

Entry informationi

Entry nameiILF3_RAT
AccessioniPrimary (citable) accession number: Q9JIL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: April 12, 2005
Last modified: October 29, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3