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Q12906

- ILF3_HUMAN

UniProt

Q12906 - ILF3_HUMAN

Protein

Interleukin enhancer-binding factor 3

Gene

ILF3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 3 (12 Apr 2005)
      Previous versions | rss
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    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 regulate protein arginine N-methyltransferase 1 activity. May regulate transcription of the IL2 gene during T-cell activation. Can promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA. 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
    2. double-stranded RNA binding Source: UniProtKB
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. RNA binding Source: UniProtKB

    GO - Biological processi

    1. defense response to virus Source: UniProtKB-KW
    2. M phase Source: UniProtKB
    3. negative regulation of transcription, DNA-templated Source: UniProtKB
    4. negative regulation of translation Source: UniProtKB
    5. negative regulation of viral genome replication Source: UniProtKB
    6. positive regulation of transcription, DNA-templated Source: UniProtKB
    7. protein phosphorylation Source: UniProtKB
    8. transcription, DNA-templated Source: UniProtKB-KW

    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
    Alternative name(s):
    Double-stranded RNA-binding protein 76
    Short name:
    DRBP76
    M-phase phosphoprotein 4
    Short name:
    MPP4
    Nuclear factor associated with dsRNA
    Short name:
    NFAR
    Nuclear factor of activated T-cells 90 kDa
    Short name:
    NF-AT-90
    Translational control protein 80
    Short name:
    TCP80
    Gene namesi
    Name:ILF3
    Synonyms:DRBF, MPHOSPH4, NF90
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:6038. ILF3.

    Subcellular locationi

    Nucleusnucleolus. Cytoplasm. Nucleus
    Note: Localizes in the cytoplasm in response to viral dsRNA. The 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.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. membrane Source: UniProtKB
    3. mitochondrion Source: HPA
    4. nucleolus Source: HPA
    5. nucleus Source: UniProtKB
    6. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29853.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 894894Interleukin enhancer-binding factor 3PRO_0000126070Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei62 – 621Phosphoserine2 Publications
    Modified residuei100 – 1001N6-acetyllysine1 Publication
    Modified residuei188 – 1881Phosphothreonine; by PKR1 Publication
    Modified residuei190 – 1901Phosphoserine3 Publications
    Modified residuei315 – 3151Phosphothreonine; by PKR1 Publication
    Modified residuei382 – 3821Phosphoserine2 Publications
    Modified residuei384 – 3841Phosphoserine1 Publication
    Modified residuei460 – 4601N6-acetyllysine1 Publication
    Modified residuei476 – 4761Phosphoserine1 Publication
    Modified residuei482 – 4821Phosphoserine3 Publications
    Modified residuei592 – 5921Phosphothreonine5 Publications
    Modified residuei792 – 7921Phosphoserine3 Publications
    Modified residuei812 – 8121Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated at Thr-188 and Thr-315 by PKR in response to certain 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.7 Publications
    Methylated by protein arginine N-methyltransferase 1.
    Arg-609 is dimethylated, probably to asymmetric dimethylarginine.

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ12906.
    PaxDbiQ12906.
    PRIDEiQ12906.

    2D gel databases

    SWISS-2DPAGEQ12906.

    PTM databases

    PhosphoSiteiQ12906.

    Miscellaneous databases

    PMAP-CutDBQ12906.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ12906.
    BgeeiQ12906.
    GenevestigatoriQ12906.

    Organism-specific databases

    HPAiHPA001897.

    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. Forms a complex with ILF2, YLPM1, KHDRBS1, RBMX, NCOA5 and PPP1CA. Interacts with AGO1 and AGO2.11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRMT1Q998732EBI-78756,EBI-78738

    Protein-protein interaction databases

    BioGridi109822. 314 interactions.
    DIPiDIP-29853N.
    IntActiQ12906. 56 interactions.
    MINTiMINT-4999319.

    Structurei

    Secondary structure

    1
    894
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi528 – 5358
    Beta strandi541 – 5488
    Beta strandi554 – 5618
    Beta strandi564 – 5729
    Helixi573 – 58816

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L33NMR-A521-600[»]
    3P1XX-ray1.90A/B520-594[»]
    ProteinModelPortaliQ12906.
    SMRiQ12906. Positions 6-374, 399-594.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12906.

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni609 – 894286Interaction 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 – 7099Poly-Gly
    Compositional biasi794 – 7985Poly-Gly

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG307678.
    HOVERGENiHBG069915.
    InParanoidiQ12906.
    KOiK13090.
    OMAiPPKHAGK.
    OrthoDBiEOG72ZCDC.
    PhylomeDBiQ12906.
    TreeFamiTF320194.

    Family and domain databases

    Gene3Di3.30.160.20. 2 hits.
    InterProiIPR014720. dsRNA-bd_dom.
    IPR006561. DZF.
    [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.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q12906-1) [UniParc]FASTAAdd to Basket

    Also known as: NFAR-2, ILF3-E

    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

    MRPMRIFVND DRHVMAKHSS VYPTQEELEA VQNMVSHTER ALKAVSDWID    50
    EQEKGSSEQA ESDNMDVPPE DDSKEGAGEQ KTEHMTRTLR GVMRVGLVAK 100
    GLLLKGDLDL ELVLLCKEKP TTALLDKVAD NLAIQLAAVT EDKYEILQSV 150
    DDAAIVIKNT KEPPLSLTIH LTSPVVREEM EKVLAGETLS VNDPPDVLDR 200
    QKCLAALASL RHAKWFQARA NGLKSCVIVI RVLRDLCTRV PTWGPLRGWP 250
    LELLCEKSIG TANRPMGAGE ALRRVLECLA SGIVMPDGSG IYDPCEKEAT 300
    DAIGHLDRQQ REDITQSAQH ALRLAAFGQL HKVLGMDPLP SKMPKKPKNE 350
    NPVDYTVQIP PSTTYAITPM KRPMEEDGEE KSPSKKKKKI QKKEEKAEPP 400
    QAMNALMRLN QLKPGLQYKL VSQTGPVHAP IFTMSVEVDG NSFEASGPSK 450
    KTAKLHVAVK VLQDMGLPTG AEGRDSSKGE DSAEETEAKP AVVAPAPVVE 500
    AVSTPSAAFP SDATAEQGPI LTKHGKNPVM ELNEKRRGLK YELISETGGS 550
    HDKRFVMEVE VDGQKFQGAG SNKKVAKAYA ALAALEKLFP DTPLALDANK 600
    KKRAPVPVRG GPKFAAKPHN PGFGMGGPMH NEVPPPPNLR GRGRGGSIRG 650
    RGRGRGFGGA NHGGYMNAGA GYGSYGYGGN SATAGYSQFY SNGGHSGNAS 700
    GGGGGGGGGS SGYGSYYQGD NYNSPVPPKH AGKKQPHGGQ QKPSYGSGYQ 750
    SHQGQQQSYN QSPYSNYGPP QGKQKGYNHG QGSYSYSNSY NSPGGGGGSD 800
    YNYESKFNYS GSGGRSGGNS YGSGGASYNP GSHGGYGGGS GGGSSYQGKQ 850
    GGYSQSNYNS PGSGQNYSGP PSSYQSSQGG YGRNADHSMN YQYR 894
    Length:894
    Mass (Da):95,338
    Last modified:April 12, 2005 - v3
    Checksum:i20903ABD0331F370
    GO
    Isoform 2 (identifier: Q12906-2) [UniParc]FASTAAdd to Basket

    Also known as: NFAR-1, DRBP76

    The sequence of this isoform differs from the canonical sequence as follows:
         688-702: QFYSNGGHSGNASGG → DFFTDCYGYHDFGSS
         703-894: Missing.

    Show »
    Length:702
    Mass (Da):76,033
    Checksum:i3DDE63929988DED4
    GO
    Isoform 3 (identifier: Q12906-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         690-764: YSNGGHSGNA...QQQSYNQSPY → SRPPPPSRPR...LRVSGNSVCL
         765-894: Missing.

    Note: Dubious isoform produced through aberrant splice sites.

    Show »
    Length:764
    Mass (Da):82,802
    Checksum:i3C7C7565F5980B1E
    GO
    Isoform 4 (identifier: Q12906-4) [UniParc]FASTAAdd to Basket

    Also known as: DRBP76 Alpha, ILF3-A

    The sequence of this isoform differs from the canonical sequence as follows:
         516-516: E → ENVKQ
         688-694: QFYSNGG → KCAFLSV
         695-894: Missing.

    Note: Contains a phosphoserine at position 482.

    Show »
    Length:698
    Mass (Da):75,508
    Checksum:iF4ECBD8A7C428905
    GO
    Isoform 5 (identifier: Q12906-5) [UniParc]FASTAAdd to Basket

    Also known as: DRBP76 Delta, Gamma, ILF3-C

    The sequence of this isoform differs from the canonical sequence as follows:
         687-690: SQFY → TGFV
         691-894: Missing.

    Show »
    Length:690
    Mass (Da):74,607
    Checksum:i8DEC4DC15E80A8C5
    GO
    Isoform 6 (identifier: Q12906-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         516-516: E → ENVKQ
         688-702: QFYSNGGHSGNASGG → DFFTDCYGYHDFGSS
         703-894: Missing.

    Note: Contains a phosphoserine at position 482.

    Show »
    Length:706
    Mass (Da):76,502
    Checksum:iBC0B5D61BC51129C
    GO
    Isoform 7 (identifier: Q12906-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         516-516: E → ENVKQ

    Note: Gene prediction based on EST data. Contains a phosphoserine at position 482.

    Show »
    Length:898
    Mass (Da):95,808
    Checksum:i83A1755F05408949
    GO

    Sequence cautioni

    The sequence AAA20994.1 differs from that shown. Reason: Sequencing errors.
    The sequence AAH48314.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti101 – 1011G → C in AAD51098. (PubMed:11438536)Curated
    Sequence conflicti101 – 1011G → C in AAD51099. (PubMed:11438536)Curated
    Sequence conflicti101 – 1011G → C in AAK07424. (PubMed:11161820)Curated
    Sequence conflicti101 – 1011G → C in AAK07425. (PubMed:11161820)Curated
    Sequence conflicti260 – 2601G → V in AAD33966. (PubMed:10400669)Curated
    Sequence conflicti260 – 2601G → V in CAA66918. (PubMed:8885239)Curated
    Sequence conflicti647 – 6471S → T in AAD33966. (PubMed:10400669)Curated
    Sequence conflicti647 – 6471S → T in AAK07424. (PubMed:11161820)Curated
    Sequence conflicti647 – 6471S → T in AAK07425. (PubMed:11161820)Curated
    Sequence conflicti688 – 6892QF → N in AAF82687. 1 PublicationCurated
    Sequence conflicti763 – 7631P → L in CAC01407. (PubMed:11167023)Curated
    Sequence conflicti797 – 7971G → R in CAC01124. (PubMed:11167023)Curated
    Sequence conflicti797 – 7971G → R in AAK07425. (PubMed:11161820)Curated
    Sequence conflicti799 – 7991S → SGS in AAF82685. 1 PublicationCurated
    Sequence conflicti813 – 8131G → E in AAK07425. (PubMed:11161820)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti50 – 501D → H.1 Publication
    Corresponds to variant rs1064493 [ dbSNP | Ensembl ].
    VAR_022159
    Natural varianti501 – 5011A → S.
    Corresponds to variant rs34520379 [ dbSNP | Ensembl ].
    VAR_048906

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei516 – 5161E → ENVKQ in isoform 4, isoform 6 and isoform 7. 3 PublicationsVSP_003883
    Alternative sequencei687 – 6904SQFY → TGFV in isoform 5. 1 PublicationVSP_003886
    Alternative sequencei688 – 70215QFYSN…NASGG → DFFTDCYGYHDFGSS in isoform 2 and isoform 6. 7 PublicationsVSP_003888Add
    BLAST
    Alternative sequencei688 – 6947QFYSNGG → KCAFLSV in isoform 4. 1 PublicationVSP_003884
    Alternative sequencei690 – 76475YSNGG…NQSPY → SRPPPPSRPRCCVVRCSGSP CGPSCDPYLAVFGTPCLQWF VSCHYNFVWVEFLSFCSSVS LCLFTLRVSGNSVCL in isoform 3. 2 PublicationsVSP_003890Add
    BLAST
    Alternative sequencei691 – 894204Missing in isoform 5. 1 PublicationVSP_003887Add
    BLAST
    Alternative sequencei695 – 894200Missing in isoform 4. 1 PublicationVSP_003885Add
    BLAST
    Alternative sequencei703 – 894192Missing in isoform 2 and isoform 6. 7 PublicationsVSP_003889Add
    BLAST
    Alternative sequencei765 – 894130Missing in isoform 3. 2 PublicationsVSP_003891Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10324 mRNA. Translation: AAA20994.1. Sequence problems.
    AF147209 mRNA. Translation: AAD33966.1.
    AF141870 mRNA. Translation: AAD37575.1.
    AJ271741 Genomic DNA. Translation: CAC01121.1.
    AJ271741 Genomic DNA. Translation: CAC01122.1.
    AJ271741 Genomic DNA. Translation: CAC01123.1.
    AJ271741 Genomic DNA. Translation: CAC01124.1.
    AJ271744 mRNA. Translation: CAC01404.1.
    AJ271745 mRNA. Translation: CAC01405.1.
    AJ271746 mRNA. Translation: CAC01406.1.
    AJ271747 mRNA. Translation: CAC01407.1.
    AF167569 mRNA. Translation: AAD51098.1.
    AF167570 mRNA. Translation: AAD51099.1.
    AF320244
    , AF320228, AF320229, AF320230, AF320231, AF320232, AF320233, AF320234, AF320235, AF320236, AF320237, AF320238, AF320239, AF320240, AF320241, AF320242, AF320243 Genomic DNA. Translation: AAK07424.1.
    AF320247
    , AF320228, AF320229, AF320230, AF320231, AF320232, AF320233, AF320234, AF320235, AF320236, AF320237, AF320238, AF320239, AF320240, AF320241, AF320242, AF320243, AF320245, AF320246 Genomic DNA. Translation: AAK07425.1.
    AK291617 mRNA. Translation: BAF84306.1.
    AC011475 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84132.1.
    BC048314 mRNA. Translation: AAH48314.1. Sequence problems.
    BC064836 mRNA. Translation: AAH64836.1.
    X98264 mRNA. Translation: CAA66917.1.
    X98265 mRNA. Translation: CAA66918.1.
    AF202445 Genomic DNA. Translation: AAF82685.1.
    AF202445 Genomic DNA. Translation: AAF82686.1.
    AF202445 Genomic DNA. Translation: AAF82687.1.
    AF007140 mRNA. Translation: AAC19152.1.
    CCDSiCCDS12246.1. [Q12906-1]
    CCDS12247.1. [Q12906-2]
    CCDS45965.1. [Q12906-7]
    CCDS45966.1. [Q12906-5]
    CCDS45967.1. [Q12906-6]
    PIRiB54857.
    RefSeqiNP_001131145.1. NM_001137673.1. [Q12906-6]
    NP_004507.2. NM_004516.3. [Q12906-2]
    NP_036350.2. NM_012218.3. [Q12906-1]
    NP_060090.2. NM_017620.2. [Q12906-7]
    NP_703194.1. NM_153464.2. [Q12906-5]
    UniGeneiHs.465885.

    Genome annotation databases

    EnsembliENST00000250241; ENSP00000250241; ENSG00000129351. [Q12906-5]
    ENST00000407004; ENSP00000384660; ENSG00000129351. [Q12906-6]
    ENST00000449870; ENSP00000404121; ENSG00000129351. [Q12906-7]
    ENST00000588657; ENSP00000468181; ENSG00000129351. [Q12906-7]
    ENST00000589998; ENSP00000465219; ENSG00000129351. [Q12906-2]
    ENST00000590261; ENSP00000468156; ENSG00000129351. [Q12906-1]
    ENST00000592763; ENSP00000465515; ENSG00000129351. [Q12906-4]
    GeneIDi3609.
    KEGGihsa:3609.
    UCSCiuc002mpk.2. human. [Q12906-5]
    uc002mpl.2. human. [Q12906-2]
    uc002mpm.2. human. [Q12906-6]
    uc002mpn.3. human. [Q12906-1]
    uc002mpo.3. human.
    uc002mpp.3. human. [Q12906-4]

    Polymorphism databases

    DMDMi62512150.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10324 mRNA. Translation: AAA20994.1 . Sequence problems.
    AF147209 mRNA. Translation: AAD33966.1 .
    AF141870 mRNA. Translation: AAD37575.1 .
    AJ271741 Genomic DNA. Translation: CAC01121.1 .
    AJ271741 Genomic DNA. Translation: CAC01122.1 .
    AJ271741 Genomic DNA. Translation: CAC01123.1 .
    AJ271741 Genomic DNA. Translation: CAC01124.1 .
    AJ271744 mRNA. Translation: CAC01404.1 .
    AJ271745 mRNA. Translation: CAC01405.1 .
    AJ271746 mRNA. Translation: CAC01406.1 .
    AJ271747 mRNA. Translation: CAC01407.1 .
    AF167569 mRNA. Translation: AAD51098.1 .
    AF167570 mRNA. Translation: AAD51099.1 .
    AF320244
    , AF320228 , AF320229 , AF320230 , AF320231 , AF320232 , AF320233 , AF320234 , AF320235 , AF320236 , AF320237 , AF320238 , AF320239 , AF320240 , AF320241 , AF320242 , AF320243 Genomic DNA. Translation: AAK07424.1 .
    AF320247
    , AF320228 , AF320229 , AF320230 , AF320231 , AF320232 , AF320233 , AF320234 , AF320235 , AF320236 , AF320237 , AF320238 , AF320239 , AF320240 , AF320241 , AF320242 , AF320243 , AF320245 , AF320246 Genomic DNA. Translation: AAK07425.1 .
    AK291617 mRNA. Translation: BAF84306.1 .
    AC011475 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84132.1 .
    BC048314 mRNA. Translation: AAH48314.1 . Sequence problems.
    BC064836 mRNA. Translation: AAH64836.1 .
    X98264 mRNA. Translation: CAA66917.1 .
    X98265 mRNA. Translation: CAA66918.1 .
    AF202445 Genomic DNA. Translation: AAF82685.1 .
    AF202445 Genomic DNA. Translation: AAF82686.1 .
    AF202445 Genomic DNA. Translation: AAF82687.1 .
    AF007140 mRNA. Translation: AAC19152.1 .
    CCDSi CCDS12246.1. [Q12906-1 ]
    CCDS12247.1. [Q12906-2 ]
    CCDS45965.1. [Q12906-7 ]
    CCDS45966.1. [Q12906-5 ]
    CCDS45967.1. [Q12906-6 ]
    PIRi B54857.
    RefSeqi NP_001131145.1. NM_001137673.1. [Q12906-6 ]
    NP_004507.2. NM_004516.3. [Q12906-2 ]
    NP_036350.2. NM_012218.3. [Q12906-1 ]
    NP_060090.2. NM_017620.2. [Q12906-7 ]
    NP_703194.1. NM_153464.2. [Q12906-5 ]
    UniGenei Hs.465885.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L33 NMR - A 521-600 [» ]
    3P1X X-ray 1.90 A/B 520-594 [» ]
    ProteinModelPortali Q12906.
    SMRi Q12906. Positions 6-374, 399-594.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109822. 314 interactions.
    DIPi DIP-29853N.
    IntActi Q12906. 56 interactions.
    MINTi MINT-4999319.

    PTM databases

    PhosphoSitei Q12906.

    Polymorphism databases

    DMDMi 62512150.

    2D gel databases

    SWISS-2DPAGE Q12906.

    Proteomic databases

    MaxQBi Q12906.
    PaxDbi Q12906.
    PRIDEi Q12906.

    Protocols and materials databases

    DNASUi 3609.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000250241 ; ENSP00000250241 ; ENSG00000129351 . [Q12906-5 ]
    ENST00000407004 ; ENSP00000384660 ; ENSG00000129351 . [Q12906-6 ]
    ENST00000449870 ; ENSP00000404121 ; ENSG00000129351 . [Q12906-7 ]
    ENST00000588657 ; ENSP00000468181 ; ENSG00000129351 . [Q12906-7 ]
    ENST00000589998 ; ENSP00000465219 ; ENSG00000129351 . [Q12906-2 ]
    ENST00000590261 ; ENSP00000468156 ; ENSG00000129351 . [Q12906-1 ]
    ENST00000592763 ; ENSP00000465515 ; ENSG00000129351 . [Q12906-4 ]
    GeneIDi 3609.
    KEGGi hsa:3609.
    UCSCi uc002mpk.2. human. [Q12906-5 ]
    uc002mpl.2. human. [Q12906-2 ]
    uc002mpm.2. human. [Q12906-6 ]
    uc002mpn.3. human. [Q12906-1 ]
    uc002mpo.3. human.
    uc002mpp.3. human. [Q12906-4 ]

    Organism-specific databases

    CTDi 3609.
    GeneCardsi GC19P010764.
    H-InvDB HIX0014753.
    HGNCi HGNC:6038. ILF3.
    HPAi HPA001897.
    MIMi 603182. gene.
    neXtProti NX_Q12906.
    PharmGKBi PA29853.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG307678.
    HOVERGENi HBG069915.
    InParanoidi Q12906.
    KOi K13090.
    OMAi PPKHAGK.
    OrthoDBi EOG72ZCDC.
    PhylomeDBi Q12906.
    TreeFami TF320194.

    Miscellaneous databases

    ChiTaRSi ILF3. human.
    EvolutionaryTracei Q12906.
    GeneWikii ILF3.
    GenomeRNAii 3609.
    NextBioi 14109.
    PMAP-CutDB Q12906.
    PROi Q12906.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12906.
    Bgeei Q12906.
    Genevestigatori Q12906.

    Family and domain databases

    Gene3Di 3.30.160.20. 2 hits.
    InterProi IPR014720. dsRNA-bd_dom.
    IPR006561. DZF.
    [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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-41; 491-510 AND 555-565, FUNCTION.
      Tissue: T-cell lymphoma.
    2. "DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR."
      Patel R.C., Vestal D.J., Xu Z., Bandyopadhyay S., Guo W., Erme S.M., Williams B.R., Sen G.C.
      J. Biol. Chem. 274:20432-20437(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF N-TERMINUS.
      Tissue: Cervix carcinoma.
    3. "Molecular cloning and characterization of a translational inhibitory protein that binds to coding sequences of human acid beta-glucosidase and other mRNAs."
      Xu Y.-H., Grabowski G.A.
      Mol. Genet. Metab. 68:441-454(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), CHARACTERIZATION.
      Tissue: Liver.
    4. "Alternative splicing in the human interleukin enhancer binding factor 3 (ILF3) gene."
      Duchange N., Pidoux J., Camus E., Sauvaget D.
      Gene 261:345-353(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 4 AND 5), ALTERNATIVE SPLICING.
      Tissue: Melanoma.
    5. "Characterization of two evolutionarily conserved, alternatively spliced nuclear phosphoproteins, NFAR-1 and -2, that function in mRNA processing and interact with the double-stranded RNA-dependent protein kinase, PKR."
      Saunders L.R., Perkins D.J., Balachandran S., Michaels R., Ford R., Mayeda A., Barber G.N.
      J. Biol. Chem. 276:32300-32312(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), CHARACTERIZATION.
    6. "The 90- and 110-kDa human NFAR proteins are translated from two differentially spliced mRNAs encoded on chromosome 19p13."
      Saunders L.R., Jurecic V., Barber G.N.
      Genomics 71:256-259(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), VARIANT HIS-50.
      Tissue: T-cell.
    7. "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] (ISOFORM 6).
      Tissue: Placenta.
    8. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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] (ISOFORM 6).
      Tissue: Duodenum and Uterus.
    11. "Identification of novel M phase phosphoproteins by expression cloning."
      Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L., Westendorf J.M.
      Mol. Biol. Cell 7:1455-1469(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-611.
      Tissue: Blood and Cervix.
    12. "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: PROTEIN SEQUENCE OF 1-10, FUNCTION, INTERACTION WITH XRCC6; PRKDC AND XRCC5.
    13. "Structure and functional characterization of hDRBF gene."
      MacArdle J., Cantarella G.M., Veyrune J.-L., Krasnoselskaya I., Kumar A.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 188-894 (ISOFORMS 1; 2 AND 3).
    14. Yu W., Sarginson J., Gibbs R.A.
      Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 587-894 (ISOFORM 1).
      Tissue: Brain.
    15. "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: INTERACTION WITH ILF2.
    16. "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: INTERACTION WITH PRMT1.
    17. "Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins."
      Brownawell A.M., Macara I.G.
      J. Cell Biol. 156:53-64(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND DOUBLE-STRANDED RNA, INTERACTION WITH XPO5.
    18. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "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: INTERACTION WITH ILF2.
    20. "Minihelix-containing RNAs mediate exportin-5-dependent nuclear export of the double-stranded RNA-binding protein ILF3."
      Gwizdek C., Ossareh-Nazari B., Brownawell A.M., Evers S., Macara I.G., Dargemont C.
      J. Biol. Chem. 279:884-891(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN AND VA1 RNA.
    21. "Nucleocytoplasmic shuttling of JAZ, a new cargo protein for exportin-5."
      Chen T., Brownawell A.M., Macara I.G.
      Mol. Cell. Biol. 24:6608-6619(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH XPO5; RAN; ZNF346 AND DOUBLE-STRANDED RNA, INTERACTION WITH XPO5 AND ZNF346.
    22. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 AND THR-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "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 ILF2; YLPM1; KHDRBS1; RBMX; NCOA5 AND PPP1CA.
    25. "Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
      Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
      EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AGO1 AND AGO2.
    26. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    27. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-792 AND SER-812, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 (ISOFORMS 4; 6 AND 7), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
      Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
      RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A MRNP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    30. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-592 AND SER-792, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 (ISOFORMS 4; 6 AND 7), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    31. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-100 AND LYS-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "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(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-188 AND THR-315.
    33. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-190; SER-382; SER-384; SER-482; THR-592 AND SER-812, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    34. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    35. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-190; SER-382; SER-476; SER-482; THR-592; SER-792 AND SER-812, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. "Crystal structure of DRBM 2 domain of interleukin enhancer-binding factor 3 from Homo sapiens, Northeast structural genomics consortium target HR4527E."
      Northeast structural genomics consortium (NESG)
      Submitted (DEC-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 520-594.
    37. "Northeast structural genomics consortium target HR4527E."
      Northeast structural genomics consortium (NESG)
      Submitted (SEP-2010) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 521-600.

    Entry informationi

    Entry nameiILF3_HUMAN
    AccessioniPrimary (citable) accession number: Q12906
    Secondary accession number(s): A8K6F2
    , G5E9M5, O43409, Q6P1X1, Q86XY7, Q99544, Q99545, Q9BZH4, Q9BZH5, Q9NQ95, Q9NQ96, Q9NQ97, Q9NQ98, Q9NQ99, Q9NQA0, Q9NQA1, Q9NQA2, Q9NRN2, Q9NRN3, Q9NRN4, Q9UMZ9, Q9UN00, Q9UN84, Q9UNA2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: April 12, 2005
    Last modified: October 1, 2014
    This is version 162 of the entry and version 3 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3