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Q12906

- ILF3_HUMAN

UniProt

Q12906 - ILF3_HUMAN

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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

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. RNA binding Source: UniProtKB

GO - Biological processi

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

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

BgeeiQ12906.
ExpressionAtlasiQ12906. baseline and differential.
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. 316 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 – 5358Combined sources
Beta strandi541 – 5488Combined sources
Beta strandi554 – 5618Combined sources
Beta strandi564 – 5729Combined sources
Helixi573 – 58816Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 – 378374DZFPROSITE-ProRule annotationAdd
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.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG307678.
GeneTreeiENSGT00550000074528.
HOVERGENiHBG069915.
InParanoidiQ12906.
KOiK13090.
OMAiPPKHAGK.
OrthoDBiEOG72ZCDC.
PhylomeDBiQ12906.
TreeFamiTF320194.

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 (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

        10         20         30         40         50
MRPMRIFVND DRHVMAKHSS VYPTQEELEA VQNMVSHTER ALKAVSDWID
60 70 80 90 100
EQEKGSSEQA ESDNMDVPPE DDSKEGAGEQ KTEHMTRTLR GVMRVGLVAK
110 120 130 140 150
GLLLKGDLDL ELVLLCKEKP TTALLDKVAD NLAIQLAAVT 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 VSQTGPVHAP IFTMSVEVDG NSFEASGPSK
460 470 480 490 500
KTAKLHVAVK VLQDMGLPTG AEGRDSSKGE DSAEETEAKP AVVAPAPVVE
510 520 530 540 550
AVSTPSAAFP SDATAEQGPI LTKHGKNPVM ELNEKRRGLK YELISETGGS
560 570 580 590 600
HDKRFVMEVE VDGQKFQGAG SNKKVAKAYA ALAALEKLFP DTPLALDANK
610 620 630 640 650
KKRAPVPVRG GPKFAAKPHN PGFGMGGPMH NEVPPPPNLR GRGRGGSIRG
660 670 680 690 700
RGRGRGFGGA NHGGYMNAGA GYGSYGYGGN SATAGYSQFY SNGGHSGNAS
710 720 730 740 750
GGGGGGGGGS SGYGSYYQGD NYNSPVPPKH AGKKQPHGGQ QKPSYGSGYQ
760 770 780 790 800
SHQGQQQSYN QSPYSNYGPP QGKQKGYNHG QGSYSYSNSY NSPGGGGGSD
810 820 830 840 850
YNYESKFNYS GSGGRSGGNS YGSGGASYNP GSHGGYGGGS GGGSSYQGKQ
860 870 880 890
GGYSQSNYNS PGSGQNYSGP PSSYQSSQGG YGRNADHSMN YQYR
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.Curated
The sequence AAH48314.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 316 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.
GeneTreei ENSGT00550000074528.
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

Bgeei Q12906.
ExpressionAtlasi Q12906. baseline and differential.
Genevestigatori Q12906.

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. "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: November 26, 2014
This is version 164 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