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Interferon regulatory factor 8 (IRF-8) (Interferon consensus sequence-binding protein) (H-ICSBP) (ICSBP)

 IRF8_HUMAN              Reviewed;         426 AA.
Q02556; A0AV82;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
15-JUL-1999, sequence version 2.
23-MAY-2018, entry version 164.
RecName: Full=Interferon regulatory factor 8;
Short=IRF-8;
AltName: Full=Interferon consensus sequence-binding protein;
Short=H-ICSBP;
Short=ICSBP;
Name=IRF8; Synonyms=ICSBP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY IFNG.
TISSUE=Lung, and Monocyte;
PubMed=1460054;
Weisz A., Marx P., Sharf R., Appella E., Driggers P.H., Ozato K.,
Levi B.-Z.;
"Human interferon consensus sequence binding protein is a negative
regulator of enhancer elements common to interferon-inducible genes.";
J. Biol. Chem. 267:25589-25596(1992).
[2]
SEQUENCE REVISION.
Schmidt M.;
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH COPS2.
PubMed=10991940; DOI=10.1074/jbc.M004900200;
Cohen H., Azriel A., Cohen T., Meraro D., Hashmueli S.,
Bech-Otschir D., Kraft R., Dubiel W., Levi B.Z.;
"Interaction between interferon consensus sequence-binding protein and
COP9/signalosome subunit CSN2 (Trip15). A possible link between
interferon regulatory factor signaling and the COP9/signalosome.";
J. Biol. Chem. 275:39081-39089(2000).
[5]
INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=23166356; DOI=10.1084/jem.20121387;
Basso K., Schneider C., Shen Q., Holmes A.B., Setty M., Leslie C.,
Dalla-Favera R.;
"BCL6 positively regulates AID and germinal center gene expression via
repression of miR-155.";
J. Exp. Med. 209:2455-2465(2012).
[6]
VARIANTS [LARGE SCALE ANALYSIS] LYS-81 AND THR-197.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[7]
VARIANT IMD32A ALA-80, VARIANT IMD32B GLU-108, CHARACTERIZATION OF
VARIANT IMD32A ALA-80, CHARACTERIZATION OF VARIANT IMD32B GLU-108,
INVOLVEMENT IN IMD32A, AND INVOLVEMENT IN IMD32B.
PubMed=21524210; DOI=10.1056/NEJMoa1100066;
Hambleton S., Salem S., Bustamante J., Bigley V., Boisson-Dupuis S.,
Azevedo J., Fortin A., Haniffa M., Ceron-Gutierrez L., Bacon C.M.,
Menon G., Trouillet C., McDonald D., Carey P., Ginhoux F., Alsina L.,
Zumwalt T.J., Kong X.F., Kumararatne D., Butler K., Hubeau M.,
Feinberg J., Al-Muhsen S., Cant A., Abel L., Chaussabel D.,
Doffinger R., Talesnik E., Grumach A., Duarte A., Abarca K.,
Moraes-Vasconcelos D., Burk D., Berghuis A., Geissmann F., Collin M.,
Casanova J.L., Gros P.;
"IRF8 mutations and human dendritic-cell immunodeficiency.";
N. Engl. J. Med. 365:127-138(2011).
[8]
CHARACTERIZATION OF VARIANT IMD32B GLU-108, FUNCTION, SUBCELLULAR
LOCATION, UBIQUITINATION, DESUMOYLATION, AND MUTAGENESIS OF LYS-108.
PubMed=25122610; DOI=10.1182/blood-2014-04-570879;
Salem S., Langlais D., Lefebvre F., Bourque G., Bigley V., Haniffa M.,
Casanova J.L., Burk D., Berghuis A., Butler K.M., Leahy T.R.,
Hambleton S., Gros P.;
"Functional characterization of the human dendritic cell
immunodeficiency associated with the IRF8(K108E) mutation.";
Blood 124:1894-1904(2014).
-!- FUNCTION: Plays a role as a transcriptional activator or repressor
(PubMed:25122610). Specifically binds to the upstream regulatory
region of type I IFN and IFN-inducible MHC class I genes (the
interferon consensus sequence (ICS)). Plays a negative regulatory
role in cells of the immune system. Involved in CD8(+) dendritic
cell differentiation by forming a complex with the BATF-JUNB
heterodimer in immune cells, leading to recognition of AICE
sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory
element, followed by cooperative binding of BATF and IRF8 and
activation of genes (By similarity).
{ECO:0000250|UniProtKB:P23611, ECO:0000269|PubMed:25122610}.
-!- SUBUNIT: Interacts (via C-terminus) with TRIM21 (via C-terminus).
Interacts with the BATF-JUNB heterodimer. Interacts with BATF (via
bZIP domain); the interaction is direct (By similarity). Interacts
with COPS2. {ECO:0000250, ECO:0000269|PubMed:10991940}.
-!- INTERACTION:
O14896:IRF6; NbExp=3; IntAct=EBI-2866563, EBI-6115643;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23166356,
ECO:0000269|PubMed:25122610}. Cytoplasm
{ECO:0000269|PubMed:25122610}. Note=In resting macrophages,
localizes in the cytoplasm. Translocated in the nucleus upon IFN-
gamma induction. {ECO:0000269|PubMed:25122610}.
-!- TISSUE SPECIFICITY: Predominantly expressed in lymphoid tissues.
{ECO:0000269|PubMed:1460054, ECO:0000269|PubMed:23166356}.
-!- INDUCTION: By IFNG/IFN-gamma. Negatively regulated by microRNA-155
(miR155). {ECO:0000269|PubMed:1460054,
ECO:0000269|PubMed:23166356}.
-!- PTM: Ubiquitinated (PubMed:25122610). Ubiquitination by TRIM21 in
macrophages, a process that is strongly increased upon interferon
gamma stimulation, leds to the enhanced transcriptional activity
of target cytokine genes (By similarity). Ubiquitination leads to
its degradation by the proteasome (PubMed:25122610). {ECO:0000250,
ECO:0000269|PubMed:25122610}.
-!- PTM: Sumoylated with SUMO3. Desumoylated by SENP1.
{ECO:0000269|PubMed:25122610}.
-!- DISEASE: Immunodeficiency 32A (IMD32A) [MIM:614893]: An
immunologic disorder characterized by abnormal peripheral blood
myeloid phenotype with a marked loss of CD11C-positive/CD1C
dendritic cells, resulting in selective susceptibility to
mycobacterial infections. {ECO:0000269|PubMed:21524210}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Immunodeficiency 32B (IMD32B) [MIM:614894]: A life-
threatening pediatric disease characterized by monocyte and
dendritic cell deficiency, myeloproliferation, and susceptibility
to severe opportunistic infections, including disseminated BCG
infection and oral candidiasis. {ECO:0000269|PubMed:21524210,
ECO:0000269|PubMed:25122610}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
ProRule:PRU00840}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M91196; AAB63813.1; -; mRNA.
EMBL; BC126247; AAI26248.1; -; mRNA.
CCDS; CCDS10956.1; -.
PIR; A45064; A45064.
RefSeq; NP_002154.1; NM_002163.2.
UniGene; Hs.137427; -.
ProteinModelPortal; Q02556; -.
SMR; Q02556; -.
BioGrid; 109621; 23.
IntAct; Q02556; 10.
STRING; 9606.ENSP00000268638; -.
iPTMnet; Q02556; -.
PhosphoSitePlus; Q02556; -.
BioMuta; IRF8; -.
DMDM; 6016308; -.
MaxQB; Q02556; -.
PaxDb; Q02556; -.
PeptideAtlas; Q02556; -.
PRIDE; Q02556; -.
Ensembl; ENST00000268638; ENSP00000268638; ENSG00000140968.
GeneID; 3394; -.
KEGG; hsa:3394; -.
UCSC; uc002fjh.4; human.
CTD; 3394; -.
DisGeNET; 3394; -.
EuPathDB; HostDB:ENSG00000140968.10; -.
GeneCards; IRF8; -.
HGNC; HGNC:5358; IRF8.
HPA; CAB013480; -.
HPA; HPA002267; -.
HPA; HPA002531; -.
MalaCards; IRF8; -.
MIM; 601565; gene.
MIM; 614893; phenotype.
MIM; 614894; phenotype.
neXtProt; NX_Q02556; -.
OpenTargets; ENSG00000140968; -.
Orphanet; 319600; Mendelian susceptibility to mycobacterial diseases due to partial IRF8 deficiency.
PharmGKB; PA29606; -.
eggNOG; ENOG410IED8; Eukaryota.
eggNOG; ENOG410XNYR; LUCA.
GeneTree; ENSGT00760000119093; -.
HOGENOM; HOG000010107; -.
HOVERGEN; HBG003072; -.
InParanoid; Q02556; -.
KO; K10155; -.
OMA; CPEGCRL; -.
OrthoDB; EOG091G067P; -.
PhylomeDB; Q02556; -.
TreeFam; TF328512; -.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
SignaLink; Q02556; -.
SIGNOR; Q02556; -.
ChiTaRS; IRF8; human.
GeneWiki; IRF8; -.
GenomeRNAi; 3394; -.
PRO; PR:Q02556; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000140968; -.
CleanEx; HS_IRF8; -.
ExpressionAtlas; Q02556; baseline and differential.
Genevisible; Q02556; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; TAS:ProtInc.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0030099; P:myeloid cell differentiation; IEA:Ensembl.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0006909; P:phagocytosis; IEA:Ensembl.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
CDD; cd00103; IRF; 1.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 2.60.200.10; -; 1.
InterPro; IPR019817; Interferon_reg_fac_CS.
InterPro; IPR001346; Interferon_reg_fact_DNA-bd_dom.
InterPro; IPR019471; Interferon_reg_factor-3.
InterPro; IPR017855; SMAD-like_dom_sf.
InterPro; IPR008984; SMAD_FHA_dom_sf.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR11949; PTHR11949; 1.
Pfam; PF00605; IRF; 1.
Pfam; PF10401; IRF-3; 1.
PRINTS; PR00267; INTFRNREGFCT.
SMART; SM00348; IRF; 1.
SMART; SM01243; IRF-3; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF49879; SSF49879; 1.
PROSITE; PS00601; IRF_1; 1.
PROSITE; PS51507; IRF_2; 1.
1: Evidence at protein level;
Activator; Complete proteome; Cytoplasm; Disease mutation;
DNA-binding; Nucleus; Polymorphism; Reference proteome; Repressor;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 426 Interferon regulatory factor 8.
/FTId=PRO_0000154564.
DNA_BIND 7 114 IRF tryptophan pentad repeat.
{ECO:0000255|PROSITE-ProRule:PRU00840}.
VARIANT 80 80 T -> A (in IMD32A; impairs
transcriptional activity by disrupting
the interaction between IRF8 and DNA;
dbSNP:rs397514711).
{ECO:0000269|PubMed:21524210}.
/FTId=VAR_070084.
VARIANT 81 81 R -> K (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036490.
VARIANT 108 108 K -> E (in IMD32B; in resting
macrophages, no effect on cytoplasmic
subcellular localization; loss of nuclear
subcellular localization upon IFN-gamma
induction; decreased protein abundance;
increased proteasome-dependent
degradation; increased ubiquitination and
sumoylation; loss of transcriptional
repressor activity; loss of IRF1-
dependent transcriptional repressor
activity; loss of IRF1-dependent
transcriptional activator activity;
impairs transcriptional activity by
disrupting the interaction between IRF8
and DNA; dbSNP:rs397514710).
{ECO:0000269|PubMed:21524210,
ECO:0000269|PubMed:25122610}.
/FTId=VAR_070085.
VARIANT 197 197 A -> T (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036491.
MUTAGEN 108 108 K->H: In resting macrophages, no effect
on cytoplasmic subcellular localization.
Decreased nuclear subcellular
localization upon IFN-gamma induction.
Partial loss of IRF1-dependent
transcriptional activator activity.
{ECO:0000269|PubMed:25122610}.
MUTAGEN 108 108 K->Q: In resting macrophages, no effect
on cytoplasmic subcellular localization.
Loss of nuclear subcellular localization
upon IFN-gamma induction. Loss of IRF1-
dependent transcriptional activator
activity. {ECO:0000269|PubMed:25122610}.
MUTAGEN 108 108 K->R: In resting macrophages, no effect
on cytoplasmic subcellular localization.
No effect on nuclear subcellular
localization upon IFN-gamma induction. No
effect on transcriptional activator
activity. No effect on IRF1-dependent
transcriptional activator activity.
{ECO:0000269|PubMed:25122610}.
SEQUENCE 426 AA; 48356 MW; 1535D1B7C83E0355 CRC64;
MCDRNGGRRL RQWLIEQIDS SMYPGLIWEN EEKSMFRIPW KHAGKQDYNQ EVDASIFKAW
AVFKGKFKEG DKAEPATWKT RLRCALNKSP DFEEVTDRSQ LDISEPYKVY RIVPEEEQKC
KLGVATAGCV NEVTEMECGR SEIDELIKEP SVDDYMGMIK RSPSPPEACR SQLLPDWWAQ
QPSTGVPLVT GYTTYDAHHS AFSQMVISFY YGGKLVGQAT TTCPEGCRLS LSQPGLPGTK
LYGPEGLELV RFPPADAIPS ERQRQVTRKL FGHLERGVLL HSSRQGVFVK RLCQGRVFCS
GNAVVCKGRP NKLERDEVVQ VFDTSQFFRE LQQFYNSQGR LPDGRVVLCF GEEFPDMAPL
RSKLILVQIE QLYVRQLAEE AGKSCGAGSV MQAPEEPPPD QVFRMFPDIC ASHQRSFFRE
NQQITV


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