Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Interferon regulatory factor 5 (IRF-5)

 IRF5_HUMAN              Reviewed;         498 AA.
Q13568; A4D1J8; A8DUA8; A8DUA9; E7EQ16; E7EW54; Q1A7B4; Q64GA9;
Q64GB1; Q64GB2; Q6RCM8; Q9BQF0;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
16-APR-2002, sequence version 2.
05-DEC-2018, entry version 166.
RecName: Full=Interferon regulatory factor 5;
Short=IRF-5;
Name=IRF5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND FUNCTION.
PubMed=11303025; DOI=10.1074/jbc.M101216200;
Barnes B.J., Moore P.A., Pitha P.M.;
"Virus-specific activation of a novel interferon regulatory factor,
IRF-5, results in the induction of distinct interferon alpha genes.";
J. Biol. Chem. 276:23382-23390(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND FUNCTION.
PubMed=15695821; DOI=10.1074/jbc.M412584200;
Schoenemeyer A., Barnes B.J., Mancl M.E., Latz E., Goutagny N.,
Pitha P.M., Fitzgerald K.A., Golenbock D.T.;
"The interferon regulatory factor, IRF5, is a central mediator of
toll-like receptor 7 signaling.";
J. Biol. Chem. 280:17005-17012(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 5), AND ALTERNATIVE
SPLICING.
PubMed=15805103; DOI=10.1074/jbc.M500543200;
Mancl M.E., Hu G., Sangster-Guity N., Olshalsky S.L., Hoops K.,
Fitzgerald-Bocarsly P., Pitha P.M., Pinder K., Barnes B.J.;
"Two discrete promoters regulate the alternatively spliced human
interferon regulatory factor-5 isoforms. Multiple isoforms with
distinct cell type-specific expression, localization, regulation, and
function.";
J. Biol. Chem. 280:21078-21090(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 6).
PubMed=16642019; DOI=10.1038/ng1782;
Graham R.R., Kozyrev S.V., Baechler E.C., Reddy M.V., Plenge R.M.,
Bauer J.W., Ortmann W.A., Koeuth T., Escribano M.F.,
Collaborative Groups T.A., Pons-Estel B., Petri M., Daly M.,
Gregersen P.K., Martin J., Altshuler D., Behrens T.W.,
Alarcon-Riquelme M.E.;
"A common haplotype of interferon regulatory factor 5 (IRF5) regulates
splicing and expression and is associated with increased risk of
systemic lupus erythematosus.";
Nat. Genet. 38:550-555(2006).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Grossman A., Mittrucker H.W., Lantonio L., Mak T.W.;
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
Nickerson D.A.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
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).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 130-253 (ISOFORMS 2 AND 3).
Kozyrev S.V., Lewen S., Linga-Reddy P.M.V., Alarcon-Riquelme M.E.;
"Structural indel variation in IRF5 is associated with a risk
haplotype and defines the precise IRF5 isoforms expressed in SLE.";
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[12]
SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
PubMed=12138184; DOI=10.1128/MCB.22.16.5721-5740.2002;
Barnes B.J., Kellum M.J., Field A.E., Pitha P.M.;
"Multiple regulatory domains of IRF-5 control activation, cellular
localization, and induction of chemokines that mediate recruitment of
T lymphocytes.";
Mol. Cell. Biol. 22:5721-5740(2002).
[13]
INVOLVEMENT IN SUSCEPTIBILITY TO SLEB10.
PubMed=15657875; DOI=10.1086/428480;
Sigurdsson S., Nordmark G., Goering H.H.H., Lindroos K., Wiman A.-C.,
Sturfelt G., Joensen A., Rantapaeae-Dahlqvist S., Moeller B., Kere J.,
Koskenmies S., Widen E., Eloranta M.-L., Julkunen H.,
Kristjansdottir H., Steinsson K., Alm G., Roennblom L.,
Syvaenen A.-C.;
"Polymorphisms in the tyrosine kinase 2 and interferon regulatory
factor 5 genes are associated with systemic lupus erythematosus.";
Am. J. Hum. Genet. 76:528-537(2005).
[14]
SUBCELLULAR LOCATION, AND NUCLEAR EXPORT SIGNAL.
PubMed=15556946; DOI=10.1074/jbc.M408452200;
Lin R., Yang L., Arguello M., Penafuerte C., Hiscott J.;
"A CRM1-dependent nuclear export pathway is involved in the regulation
of IRF-5 subcellular localization.";
J. Biol. Chem. 280:3088-3095(2005).
[15]
INVOLVEMENT IN SUSCEPTIBILITY TO RHEUMATOID ARTHRITIS.
PubMed=17599733; DOI=10.1002/art.22704;
Sigurdsson S., Padyukov L., Kurreeman F.A., Liljedahl U., Wiman A.C.,
Alfredsson L., Toes R., Ronnelid J., Klareskog L., Huizinga T.W.,
Alm G., Syvanen A.C., Ronnblom L.;
"Association of a haplotype in the promoter region of the interferon
regulatory factor 5 gene with rheumatoid arthritis.";
Arthritis Rheum. 56:2202-2210(2007).
[16]
INVOLVEMENT IN SUSCEPTIBILITY TO IBD14.
PubMed=17881657; DOI=10.1093/hmg/ddm259;
Dideberg V., Kristjansdottir G., Milani L., Libioulle C.,
Sigurdsson S., Louis E., Wiman A.-C., Vermeire S., Rutgeerts P.,
Belaiche J., Franchimont D., Van Gossum A., Bours V., Syvaenen A.-C.;
"An insertion-deletion polymorphism in the interferon regulatory
Factor 5 (IRF5) gene confers risk of inflammatory bowel diseases.";
Hum. Mol. Genet. 16:3008-3016(2007).
[17]
UBIQUITINATION AT LYS-411 AND LYS-412 BY TRAF6.
PubMed=18824541; DOI=10.1128/MCB.00662-08;
Balkhi M.Y., Fitzgerald K.A., Pitha P.M.;
"Functional regulation of MyD88-activated interferon regulatory factor
5 by K63-linked polyubiquitination.";
Mol. Cell. Biol. 28:7296-7308(2008).
[18]
PHOSPHORYLATION AT THR-10; SER-158; SER-293; SER-301; SER-435 AND
SER-446, AND SUBCELLULAR LOCATION.
PubMed=22412986; DOI=10.1371/journal.pone.0033098;
Chang Foreman H.C., Van Scoy S., Cheng T.F., Reich N.C.;
"Activation of interferon regulatory factor 5 by site specific
phosphorylation.";
PLoS ONE 7:E33098-E33098(2012).
[19]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 232-477 OF MUTANT ASP-440,
SUBUNIT, AND PHOSPHORYLATION AT SER-435; SER-437; SER-440 AND SER-446.
PubMed=18836453; DOI=10.1038/nsmb.1496;
Chen W., Lam S.S., Srinath H., Jiang Z., Correia J.J., Schiffer C.A.,
Fitzgerald K.A., Lin K., Royer W.E. Jr.;
"Insights into interferon regulatory factor activation from the
crystal structure of dimeric IRF5.";
Nat. Struct. Mol. Biol. 15:1213-1220(2008).
-!- FUNCTION: Transcription factor involved in the induction of
interferons IFNA and INFB and inflammatory cytokines upon virus
infection. Activated by TLR7 or TLR8 signaling.
{ECO:0000269|PubMed:11303025, ECO:0000269|PubMed:15695821}.
-!- SUBUNIT: Homodimer, when phosphorylated.
{ECO:0000269|PubMed:18836453}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-3931258, EBI-3931258;
Q92793:CREBBP; NbExp=3; IntAct=EBI-3931258, EBI-81215;
Q7Z434:MAVS; NbExp=2; IntAct=EBI-3931258, EBI-995373;
Q04206:RELA; NbExp=4; IntAct=EBI-3931258, EBI-73886;
O43765:SGTA; NbExp=3; IntAct=EBI-3931258, EBI-347996;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between
the nucleus and the cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q13568-1; Sequence=Displayed;
Name=2;
IsoId=Q13568-2; Sequence=VSP_041375;
Name=3;
IsoId=Q13568-3; Sequence=VSP_043924;
Name=4;
IsoId=Q13568-4; Sequence=VSP_043925;
Name=5;
IsoId=Q13568-5; Sequence=VSP_044822;
Name=6;
IsoId=Q13568-6; Sequence=VSP_053330, VSP_053331;
-!- PTM: Phosphorylation of serine and threonine residues in a C-
terminal autoinhibitory region, stimulates dimerization, transport
into the nucleus, assembly with the coactivator CBP/p300 and
initiation of transcription. {ECO:0000269|PubMed:18836453,
ECO:0000269|PubMed:22412986}.
-!- PTM: 'Lys-63'-linked polyubiquitination by TRAF6 is required for
activation. {ECO:0000269|PubMed:18824541}.
-!- DISEASE: Inflammatory bowel disease 14 (IBD14) [MIM:612245]: A
chronic, relapsing inflammation of the gastrointestinal tract with
a complex etiology. It is subdivided into Crohn disease and
ulcerative colitis phenotypes. Crohn disease may affect any part
of the gastrointestinal tract from the mouth to the anus, but most
frequently it involves the terminal ileum and colon. Bowel
inflammation is transmural and discontinuous; it may contain
granulomas or be associated with intestinal or perianal fistulas.
In contrast, in ulcerative colitis, the inflammation is continuous
and limited to rectal and colonic mucosal layers; fistulas and
granulomas are not observed. Both diseases include extraintestinal
inflammation of the skin, eyes, or joints.
{ECO:0000269|PubMed:17881657}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Systemic lupus erythematosus 10 (SLEB10) [MIM:612251]: A
chronic, relapsing, inflammatory, and often febrile multisystemic
disorder of connective tissue, characterized principally by
involvement of the skin, joints, kidneys and serosal membranes. It
is of unknown etiology, but is thought to represent a failure of
the regulatory mechanisms of the autoimmune system. The disease is
marked by a wide range of system dysfunctions, an elevated
erythrocyte sedimentation rate, and the formation of LE cells in
the blood or bone marrow. {ECO:0000269|PubMed:15657875}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Rheumatoid arthritis (RA) [MIM:180300]: An inflammatory
disease with autoimmune features and a complex genetic component.
It primarily affects the joints and is characterized by
inflammatory changes in the synovial membranes and articular
structures, widespread fibrinoid degeneration of the collagen
fibers in mesenchymal tissues, and by atrophy and rarefaction of
bony structures. {ECO:0000269|PubMed:17599733}. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE-
ProRule:PRU00840}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AY504947; AAR90326.1; -; mRNA.
EMBL; AY504946; AAR90325.1; -; mRNA.
EMBL; AY693665; AAU12877.1; -; mRNA.
EMBL; AY693666; AAU12878.1; -; mRNA.
EMBL; AY693668; AAU12880.1; -; mRNA.
EMBL; DQ277633; ABB88960.1; -; mRNA.
EMBL; DQ277634; ABB88961.1; -; mRNA.
EMBL; U51127; AAA96056.1; -; mRNA.
EMBL; EF064718; ABK41901.1; -; Genomic_DNA.
EMBL; AC025594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236950; EAL24107.1; -; Genomic_DNA.
EMBL; CH236950; EAL24108.1; -; Genomic_DNA.
EMBL; CH471070; EAW83703.1; -; Genomic_DNA.
EMBL; CH471070; EAW83705.1; -; Genomic_DNA.
EMBL; BC004201; AAH04201.1; -; mRNA.
EMBL; BC004139; AAH04139.1; -; mRNA.
EMBL; DQ995495; ABL96293.1; -; Genomic_DNA.
EMBL; DQ995496; ABL96294.1; -; Genomic_DNA.
CCDS; CCDS43645.1; -. [Q13568-2]
CCDS; CCDS56512.1; -. [Q13568-5]
CCDS; CCDS5808.1; -. [Q13568-1]
PIR; G02474; G02474.
RefSeq; NP_001092097.2; NM_001098627.3. [Q13568-1]
RefSeq; NP_001092099.1; NM_001098629.2. [Q13568-2]
RefSeq; NP_001092100.1; NM_001098630.2. [Q13568-1]
RefSeq; NP_001229381.1; NM_001242452.2. [Q13568-5]
RefSeq; NP_001334857.1; NM_001347928.1. [Q13568-2]
RefSeq; NP_116032.1; NM_032643.4. [Q13568-1]
RefSeq; XP_005250374.1; XM_005250317.3.
RefSeq; XP_006716037.1; XM_006715974.2. [Q13568-2]
RefSeq; XP_011514460.1; XM_011516158.2. [Q13568-2]
RefSeq; XP_011514461.1; XM_011516159.2. [Q13568-2]
RefSeq; XP_011514462.1; XM_011516160.1. [Q13568-2]
RefSeq; XP_011514463.1; XM_011516161.1.
RefSeq; XP_011514464.1; XM_011516162.1.
RefSeq; XP_011514465.1; XM_011516163.2.
RefSeq; XP_011514466.1; XM_011516164.1.
UniGene; Hs.521181; -.
PDB; 3DSH; X-ray; 2.00 A; A=232-477.
PDBsum; 3DSH; -.
ProteinModelPortal; Q13568; -.
SMR; Q13568; -.
BioGrid; 109871; 34.
DIP; DIP-46348N; -.
IntAct; Q13568; 13.
STRING; 9606.ENSP00000349770; -.
iPTMnet; Q13568; -.
PhosphoSitePlus; Q13568; -.
BioMuta; IRF5; -.
DMDM; 20178305; -.
MaxQB; Q13568; -.
PaxDb; Q13568; -.
PeptideAtlas; Q13568; -.
PRIDE; Q13568; -.
ProteomicsDB; 59569; -.
ProteomicsDB; 59570; -. [Q13568-2]
ProteomicsDB; 59571; -. [Q13568-3]
ProteomicsDB; 59572; -. [Q13568-4]
DNASU; 3663; -.
Ensembl; ENST00000249375; ENSP00000249375; ENSG00000128604. [Q13568-1]
Ensembl; ENST00000357234; ENSP00000349770; ENSG00000128604. [Q13568-2]
Ensembl; ENST00000402030; ENSP00000385352; ENSG00000128604. [Q13568-1]
Ensembl; ENST00000465603; ENSP00000418534; ENSG00000128604. [Q13568-6]
Ensembl; ENST00000473745; ENSP00000419149; ENSG00000128604. [Q13568-1]
Ensembl; ENST00000477535; ENSP00000419950; ENSG00000128604. [Q13568-5]
Ensembl; ENST00000489702; ENSP00000418037; ENSG00000128604. [Q13568-2]
Ensembl; ENST00000619830; ENSP00000483292; ENSG00000128604. [Q13568-6]
GeneID; 3663; -.
KEGG; hsa:3663; -.
UCSC; uc003vog.4; human. [Q13568-1]
CTD; 3663; -.
DisGeNET; 3663; -.
EuPathDB; HostDB:ENSG00000128604.18; -.
GeneCards; IRF5; -.
HGNC; HGNC:6120; IRF5.
HPA; HPA046700; -.
MalaCards; IRF5; -.
MIM; 180300; phenotype.
MIM; 607218; gene.
MIM; 612245; phenotype.
MIM; 612251; phenotype.
neXtProt; NX_Q13568; -.
OpenTargets; ENSG00000128604; -.
Orphanet; 220393; Diffuse cutaneous systemic sclerosis.
Orphanet; 220402; Limited cutaneous systemic sclerosis.
Orphanet; 206; NON RARE IN EUROPE: Crohn disease.
Orphanet; 536; NON RARE IN EUROPE: Systemic lupus erythematosus.
Orphanet; 771; NON RARE IN EUROPE: Ulcerative colitis.
Orphanet; 186; Primary biliary cholangitis.
PharmGKB; PA29919; -.
eggNOG; ENOG410IFCV; Eukaryota.
eggNOG; ENOG410XRXT; LUCA.
GeneTree; ENSGT00940000159926; -.
HOGENOM; HOG000037433; -.
HOVERGEN; HBG105715; -.
InParanoid; Q13568; -.
KO; K09446; -.
OMA; SHPNPIQ; -.
PhylomeDB; Q13568; -.
TreeFam; TF328512; -.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
SIGNOR; Q13568; -.
EvolutionaryTrace; Q13568; -.
GeneWiki; IRF5; -.
GenomeRNAi; 3663; -.
PRO; PR:Q13568; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000128604; Expressed in 168 organ(s), highest expression level in cortex of kidney.
CleanEx; HS_IRF5; -.
ExpressionAtlas; Q13568; baseline and differential.
Genevisible; Q13568; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IC:NTNU_SB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043565; F:sequence-specific DNA binding; IMP:NTNU_SB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IEA:InterPro.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:BHF-UCL.
GO; GO:0032727; P:positive regulation of interferon-alpha production; IC:BHF-UCL.
GO; GO:0032728; P:positive regulation of interferon-beta production; IC:BHF-UCL.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IC:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0032495; P:response to muramyl dipeptide; IDA:BHF-UCL.
GO; GO:0032494; P:response to peptidoglycan; IDA:BHF-UCL.
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; IPR029838; IRF5.
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.
PANTHER; PTHR11949:SF10; PTHR11949:SF10; 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;
3D-structure; Alternative splicing; Antiviral defense;
Complete proteome; Cytoplasm; DNA-binding; Immunity; Innate immunity;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
Systemic lupus erythematosus; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 498 Interferon regulatory factor 5.
/FTId=PRO_0000154558.
DNA_BIND 14 122 IRF tryptophan pentad repeat.
{ECO:0000255|PROSITE-ProRule:PRU00840}.
MOTIF 12 18 Nuclear localization signal.
{ECO:0000269|PubMed:12138184}.
MOTIF 150 160 Nuclear export signal.
COMPBIAS 142 149 Poly-Glu.
MOD_RES 10 10 Phosphothreonine.
{ECO:0000269|PubMed:22412986}.
MOD_RES 158 158 Phosphoserine; by TBK1.
{ECO:0000269|PubMed:22412986}.
MOD_RES 293 293 Phosphoserine; by TBK1.
{ECO:0000269|PubMed:22412986}.
MOD_RES 301 301 Phosphoserine.
{ECO:0000269|PubMed:22412986}.
MOD_RES 435 435 Phosphoserine.
{ECO:0000269|PubMed:18836453,
ECO:0000269|PubMed:22412986}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000269|PubMed:18836453}.
MOD_RES 440 440 Phosphoserine.
{ECO:0000269|PubMed:18836453}.
MOD_RES 446 446 Phosphoserine.
{ECO:0000269|PubMed:18836453,
ECO:0000269|PubMed:22412986}.
CROSSLNK 411 411 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:18824541}.
CROSSLNK 412 412 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:18824541}.
VAR_SEQ 120 147 VCSNGPAPTDSQPPEDYSFGAGEEEEEE -> TPSPLRITL
LVQERRRKKRKSCRGCCQA (in isoform 6).
{ECO:0000303|PubMed:16642019}.
/FTId=VSP_053330.
VAR_SEQ 148 498 Missing (in isoform 6).
{ECO:0000303|PubMed:16642019}.
/FTId=VSP_053331.
VAR_SEQ 160 160 T -> TDAVQSGPHMTPYSLLK (in isoform 2).
{ECO:0000303|PubMed:15805103,
ECO:0000303|Ref.11}.
/FTId=VSP_041375.
VAR_SEQ 161 247 EDVKWPPTLQPPTLRPPTLQPPTLQPPVVLGPPAPDPSPLA
PPPGNPAGFRELLSEVLEPGPLPASLPPAGEQLLPDLLISP
HMLPL -> V (in isoform 5).
{ECO:0000303|PubMed:15805103}.
/FTId=VSP_044822.
VAR_SEQ 161 175 EDVKWPPTLQPPTLR -> DAVQSGPHMTPYSLLKEDVKW
(in isoform 3). {ECO:0000303|Ref.11,
ECO:0000303|Ref.5}.
/FTId=VSP_043924.
VAR_SEQ 166 175 Missing (in isoform 4).
{ECO:0000303|PubMed:11303025,
ECO:0000303|PubMed:15695821,
ECO:0000303|PubMed:16642019}.
/FTId=VSP_043925.
CONFLICT 253 253 K -> KK (in Ref. 3; AAU12880).
{ECO:0000305}.
HELIX 235 239 {ECO:0000244|PDB:3DSH}.
TURN 242 244 {ECO:0000244|PDB:3DSH}.
STRAND 250 256 {ECO:0000244|PDB:3DSH}.
STRAND 262 266 {ECO:0000244|PDB:3DSH}.
STRAND 272 275 {ECO:0000244|PDB:3DSH}.
HELIX 283 285 {ECO:0000244|PDB:3DSH}.
HELIX 286 289 {ECO:0000244|PDB:3DSH}.
STRAND 294 298 {ECO:0000244|PDB:3DSH}.
HELIX 308 318 {ECO:0000244|PDB:3DSH}.
STRAND 325 330 {ECO:0000244|PDB:3DSH}.
STRAND 333 338 {ECO:0000244|PDB:3DSH}.
STRAND 340 342 {ECO:0000244|PDB:3DSH}.
STRAND 344 348 {ECO:0000244|PDB:3DSH}.
STRAND 367 371 {ECO:0000244|PDB:3DSH}.
HELIX 372 383 {ECO:0000244|PDB:3DSH}.
STRAND 395 401 {ECO:0000244|PDB:3DSH}.
HELIX 409 411 {ECO:0000244|PDB:3DSH}.
STRAND 413 420 {ECO:0000244|PDB:3DSH}.
HELIX 421 431 {ECO:0000244|PDB:3DSH}.
HELIX 450 465 {ECO:0000244|PDB:3DSH}.
SEQUENCE 498 AA; 56044 MW; 01B2ED95C28384E8 CRC64;
MNQSIPVAPT PPRRVRLKPW LVAQVNSCQY PGLQWVNGEK KLFCIPWRHA TRHGPSQDGD
NTIFKAWAKE TGKYTEGVDE ADPAKWKANL RCALNKSRDF RLIYDGPRDM PPQPYKIYEV
CSNGPAPTDS QPPEDYSFGA GEEEEEEEEL QRMLPSLSLT EDVKWPPTLQ PPTLRPPTLQ
PPTLQPPVVL GPPAPDPSPL APPPGNPAGF RELLSEVLEP GPLPASLPPA GEQLLPDLLI
SPHMLPLTDL EIKFQYRGRP PRALTISNPH GCRLFYSQLE ATQEQVELFG PISLEQVRFP
SPEDIPSDKQ RFYTNQLLDV LDRGLILQLQ GQDLYAIRLC QCKVFWSGPC ASAHDSCPNP
IQREVKTKLF SLEHFLNELI LFQKGQTNTP PPFEIFFCFG EEWPDRKPRE KKLITVQVVP
VAARLLLEMF SGELSWSADS IRLQISNPDL KDRMVEQFKE LHHIWQSQQR LQPVAQAPPG
AGLGVGQGPW PMHPAGMQ


Related products :

Catalog number Product name Quantity
31-202 Interferon regulatory factor 8 (IRF8, interferon consensus sequence-binding protein, Ion ChannelSBP) is a transcription factor of the interferon (IFN) regulatory factor (IRF) family. Proteins of this 0.05 mg
18-003-42263 Interferon regulatory factor 4 - IRF-4; Lymphocyte-specific interferon regulatory factor; LSIRF; NF-EM5; Multiple myeloma oncogene 1 Polyclonal 0.1 mg Protein A
orb80393 Human Interferon Regulatory Factor-1 protein Interferon Regulatory Factor-1 Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (1-114) wit 5
orb80394 Human Interferon Regulatory Factor-2 protein Interferon Regulatory Factor-2 Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 133 amino acids (1-113) wit 10
31-154 IRF2 encodes interferon regulatory factor 2, a member of the interferon regulatory transcription factor (IRF) family. IRF2 competitively inhibits the IRF1-mediated transcriptional activation of interf 0.05 mg
27-469 IRF3 is interferon regulatory factor 3, a member of the interferon regulatory transcription factor (IRF) family. IRF3 is found in an inactive cytoplasmic form that upon serine_threonine phosphorylatio 0.05 mg
28-780 IRF3 is interferon regulatory factor 3, a member of the interferon regulatory transcription factor (IRF) family. IRF3 is found in an inactive cytoplasmic form that upon serine_threonine phosphorylatio 0.1 mg
LF-PA41488 anti-Interferon Regulatory Factor 4, Rabbit polyclonal to Interferon Regulatory Factor 4, Isotype IgG, Host Rabbit 50 ug
LF-PA41805 anti-Interferon Regulatory Factor 3, Rabbit polyclonal to Interferon Regulatory Factor 3, Isotype IgG, Host Rabbit 50 ul
28-794 IRF1 is interferon regulatory factor 1, a member of the interferon regulatory transcription factor (IRF) family. IRF1 serves as an activator of interferons alpha and beta transcription, and in mouse i 0.05 mg
31-203 Interferon consensus sequence-binding protein (Ion ChannelSBP) is a transcription factor of the interferon (IFN) regulatory factor (IRF) family. Proteins of this family are composed of a conserved DNA 0.1 mg
18-003-43029 Interferon regulatory factor 8 - IRF-8; Interferon consensus sequence-binding protein; ICSBP Polyclonal 0.05 mg Aff Pur
18-661-15212 Interferon regulatory factor 8 - IRF-8; Interferon consensus sequence-binding protein; ICSBP Polyclonal 0.1 mg
18-003-43028 Interferon regulatory factor 8 - IRF-8; Interferon consensus sequence-binding protein; ICSBP Polyclonal 0.05 mg Aff Pur
18-003-43029 Interferon regulatory factor 8 - IRF-8; Interferon consensus sequence-binding protein; ICSBP Polyclonal 0.1 mg Protein A
18-003-43028 Interferon regulatory factor 8 - IRF-8; Interferon consensus sequence-binding protein; ICSBP Polyclonal 0.1 mg Protein A
28-795 IRF5 is a member of the interferon regulatory factor (IRF) family, a group of transcription factors with diverse roles, including virus-mediated activation of interferon, and modulation of cell growth 0.1 mg
18-003-42030 Transcriptional regulator ISGF3 subunit gamma - Interferon regulatory factor 9; IRF-9; IFN-alpha-responsive transcription factor subunit; Interferon-stimulated gene factor 3 gamma; ISGF3 p48 subunit; 0.05 mg Aff Pur
U1776m CLIA ICSBP,Icsbp,Icsbp1,Interferon consensus sequence-binding protein,Interferon regulatory factor 8,Irf8,IRF-8,Mouse,Mus musculus 96T
E1776m ELISA ICSBP,Icsbp,Icsbp1,Interferon consensus sequence-binding protein,Interferon regulatory factor 8,Irf8,IRF-8,Mouse,Mus musculus 96T
E1776m ELISA kit ICSBP,Icsbp,Icsbp1,Interferon consensus sequence-binding protein,Interferon regulatory factor 8,Irf8,IRF-8,Mouse,Mus musculus 96T
E1776h ELISA kit H-ICSBP,Homo sapiens,Human,ICSBP,ICSBP1,Interferon consensus sequence-binding protein,Interferon regulatory factor 8,IRF8,IRF-8 96T
U1776h CLIA H-ICSBP,Homo sapiens,Human,ICSBP,ICSBP1,Interferon consensus sequence-binding protein,Interferon regulatory factor 8,IRF8,IRF-8 96T
E1776h ELISA H-ICSBP,Homo sapiens,Human,ICSBP,ICSBP1,Interferon consensus sequence-binding protein,Interferon regulatory factor 8,IRF8,IRF-8 96T
EIAAB32304 Beta-interferon gene positive regulatory domain I-binding factor,BLIMP1,BLIMP-1,Homo sapiens,Human,Positive regulatory domain I-binding factor 1,PR domain zinc finger protein 1,PR domain-containing pr


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur