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Transcription factor RelB (I-Rel)

 RELB_HUMAN              Reviewed;         579 AA.
Q01201; Q6GTX7; Q9UEI7;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
04-APR-2006, sequence version 2.
23-MAY-2018, entry version 179.
RecName: Full=Transcription factor RelB;
AltName: Full=I-Rel;
Name=RELB;
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=T-cell;
PubMed=1577270; DOI=10.1101/gad.6.5.745;
Ruben S.M., Klement J.F., Maher M., Coleman T.A., Chen C.H.,
Rosen C.A.;
"I-Rel: a novel rel-related protein that inhibits NF-kappa B
transcriptional activity.";
Genes Dev. 6:745-760(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Yoshiura K., Murray J.C.;
"A transcriptional map in the region of 19q13 derived using direct
sequencing and exon trapping.";
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Blood;
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).
[5]
FUNCTION, AND IDENTIFICATION IN THE NF-KAPPA-B RELB-P50 COMPLEX.
PubMed=1732739; DOI=10.1128/MCB.12.2.674;
Ryseck R.P., Bull P., Takamiya M., Bours V., Siebenlist U.,
Dobrzanski P., Bravo R.;
"RelB, a new Rel family transcription activator that can interact with
p50-NF-kappa B.";
Mol. Cell. Biol. 12:674-684(1992).
[6]
FUNCTION.
PubMed=8441398; DOI=10.1128/MCB.13.3.1572;
Dobrzanski P., Ryseck R.P., Bravo R.;
"Both N- and C-terminal domains of RelB are required for full
transactivation: role of the N-terminal leucine zipper-like motif.";
Mol. Cell. Biol. 13:1572-1582(1993).
[7]
FUNCTION, IDENTIFICATION IN THE NF-KAPPA-B RELB-P50 COMPLEX, AND
IDENTIFICATION IN THE NF-KAPPA-B RELB-P52 COMPLEX.
PubMed=7925301;
Dobrzanski P., Ryseck R.P., Bravo R.;
"Differential interactions of Rel-NF-kappa B complexes with I kappa B
alpha determine pools of constitutive and inducible NF-kappa B
activity.";
EMBO J. 13:4608-4616(1994).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-573, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[10]
SUBCELLULAR LOCATION.
PubMed=20873783; DOI=10.1021/pr100562w;
Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C.,
Santana Bernachi J., Paes Leme A.F., Kobarg J.;
"Characterization of hNek6 interactome reveals an important role for
its short N-terminal domain and colocalization with proteins at the
centrosome.";
J. Proteome Res. 9:6298-6316(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
FUNCTION, AND INDUCTION BY NUPR1.
PubMed=22565310; DOI=10.1172/JCI60144;
Hamidi T., Algul H., Cano C.E., Sandi M.J., Molejon M.I., Riemann M.,
Calvo E.L., Lomberk G., Dagorn J.C., Weih F., Urrutia R., Schmid R.M.,
Iovanna J.L.;
"Nuclear protein 1 promotes pancreatic cancer development and protects
cells from stress by inhibiting apoptosis.";
J. Clin. Invest. 122:2092-2103(2012).
[13]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-16, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[14]
FUNCTION, INVOLVEMENT IN IMD53, AND VARIANT IMD53 397-TYR--THR-579
DEL.
PubMed=26385063; DOI=10.1016/j.jaut.2015.09.001;
Sharfe N., Merico D., Karanxha A., Macdonald C., Dadi H., Ngan B.,
Herbrick J.A., Roifman C.M.;
"The effects of RelB deficiency on lymphocyte development and
function.";
J. Autoimmun. 65:90-100(2015).
-!- FUNCTION: NF-kappa-B is a pleiotropic transcription factor which
is present in almost all cell types and is involved in many
biological processed such as inflammation, immunity,
differentiation, cell growth, tumorigenesis and apoptosis. NF-
kappa-B is a homo- or heterodimeric complex formed by the Rel-like
domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50,
REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of
their target genes and the individual dimers have distinct
preferences for different kappa-B sites that they can bind with
distinguishable affinity and specificity. Different dimer
combinations act as transcriptional activators or repressors,
respectively. NF-kappa-B is controlled by various mechanisms of
post-translational modification and subcellular
compartmentalization as well as by interactions with other
cofactors or corepressors. NF-kappa-B complexes are held in the
cytoplasm in an inactive state complexed with members of the NF-
kappa-B inhibitor (I-kappa-B) family. In a conventional activation
pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs)
in response to different activators, subsequently degraded thus
liberating the active NF-kappa-B complex which translocates to the
nucleus. NF-kappa-B heterodimeric RelB-p50 and RelB-p52 complexes
are transcriptional activators. RELB neither associates with DNA
nor with RELA/p65 or REL. Stimulates promoter activity in the
presence of NFKB2/p49. As a member of the NUPR1/RELB/IER3 survival
pathway, may provide pancreatic ductal adenocarcinoma with
remarkable resistance to cell stress, such as starvation or
gemcitabine treatment. Regulates the circadian clock by repressing
the transcriptional activator activity of the CLOCK-ARNTL/BMAL1
heterodimer in a CRY1/CRY2 independent manner. Increased
repression of the heterodimer is seen in the presence of
NFKB2/p52. Is required for both T and B lymphocyte maturation and
function (PubMed:26385063). {ECO:0000269|PubMed:1732739,
ECO:0000269|PubMed:22565310, ECO:0000269|PubMed:26385063,
ECO:0000269|PubMed:7925301, ECO:0000269|PubMed:8441398}.
-!- SUBUNIT: Component of the NF-kappa-B RelB-p50 complex. Component
of the NF-kappa-B RelB-p52 complex. Self-associates; the
interaction seems to be transient and may prevent degradation
allowing for heterodimer formation with p50 or p52. Interacts with
NFKB1/p50, NFKB2/p52 and NFKB2/p100. Interacts with NFKBID.
Interacts with ARNTL/BMAL1 and the interaction is enhanced in the
presence of CLOCK (By similarity). {ECO:0000250}.
-!- INTERACTION:
Q8N668:COMMD1; NbExp=2; IntAct=EBI-357837, EBI-1550112;
P49841:GSK3B; NbExp=4; IntAct=EBI-357837, EBI-373586;
P19838:NFKB1; NbExp=3; IntAct=EBI-357837, EBI-300010;
Q04206:RELA; NbExp=2; IntAct=EBI-357837, EBI-73886;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20873783}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:20873783}. Note=Colocalizes with NEK6 in the
centrosome.
-!- INDUCTION: Up-regulated by mitogens and NUPR1.
{ECO:0000269|PubMed:22565310}.
-!- DOMAIN: Both N- and C-terminal domains are required for
transcriptional activation.
-!- PTM: Phosphorylation at 'Thr-103' and 'Ser-573' is followed by
proteasomal degradation. {ECO:0000250}.
-!- DISEASE: Immunodeficiency 53 (IMD53) [MIM:617585]: An autosomal
recessive primary immunodeficiency apparent from early infancy and
resulting in recurrent infections, severe autoimmune skin disease
rheumatoid arthritis, and failure to thrive. Immunologic workup
shows increased CD4+/CD8+ ratio, impaired T-cell proliferative
response to multiple antigen, T-cell developmental and functional
defects, and impaired ability to produce specific immunoglobulins.
{ECO:0000269|PubMed:26385063}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- CAUTION: Was originally thought to inhibit the transcriptional
activity of nuclear factor NF-kappa-B.
{ECO:0000305|PubMed:1577270}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RELBID324.html";
-----------------------------------------------------------------------
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EMBL; M83221; AAA36127.1; -; mRNA.
EMBL; AF043463; AAC82346.1; -; Genomic_DNA.
EMBL; AF043454; AAC82346.1; JOINED; Genomic_DNA.
EMBL; AF043455; AAC82346.1; JOINED; Genomic_DNA.
EMBL; AF043456; AAC82346.1; JOINED; Genomic_DNA.
EMBL; AF043457; AAC82346.1; JOINED; Genomic_DNA.
EMBL; AF043458; AAC82346.1; JOINED; Genomic_DNA.
EMBL; AF043459; AAC82346.1; JOINED; Genomic_DNA.
EMBL; AF043460; AAC82346.1; JOINED; Genomic_DNA.
EMBL; AF043461; AAC82346.1; JOINED; Genomic_DNA.
EMBL; AF043462; AAC82346.1; JOINED; Genomic_DNA.
EMBL; DQ314887; ABC40746.1; -; Genomic_DNA.
EMBL; BC028013; AAH28013.1; -; mRNA.
CCDS; CCDS46110.1; -.
PIR; A42617; A42617.
RefSeq; NP_006500.2; NM_006509.3.
UniGene; Hs.654402; -.
ProteinModelPortal; Q01201; -.
SMR; Q01201; -.
BioGrid; 111903; 52.
CORUM; Q01201; -.
DIP; DIP-27531N; -.
IntAct; Q01201; 32.
MINT; Q01201; -.
STRING; 9606.ENSP00000221452; -.
iPTMnet; Q01201; -.
PhosphoSitePlus; Q01201; -.
BioMuta; RELB; -.
DMDM; 92090634; -.
EPD; Q01201; -.
MaxQB; Q01201; -.
PaxDb; Q01201; -.
PeptideAtlas; Q01201; -.
PRIDE; Q01201; -.
DNASU; 5971; -.
Ensembl; ENST00000221452; ENSP00000221452; ENSG00000104856.
Ensembl; ENST00000625761; ENSP00000485826; ENSG00000104856.
GeneID; 5971; -.
KEGG; hsa:5971; -.
UCSC; uc060zvi.1; human.
CTD; 5971; -.
DisGeNET; 5971; -.
EuPathDB; HostDB:ENSG00000104856.13; -.
GeneCards; RELB; -.
HGNC; HGNC:9956; RELB.
HPA; CAB007753; -.
HPA; HPA040506; -.
MalaCards; RELB; -.
MIM; 604758; gene.
MIM; 617585; phenotype.
neXtProt; NX_Q01201; -.
OpenTargets; ENSG00000104856; -.
PharmGKB; PA34322; -.
eggNOG; ENOG410IFBK; Eukaryota.
eggNOG; ENOG410ZMME; LUCA.
GeneTree; ENSGT00500000044765; -.
HOGENOM; HOG000148598; -.
HOVERGEN; HBG017021; -.
InParanoid; Q01201; -.
KO; K09253; -.
OMA; DFFSGTV; -.
OrthoDB; EOG091G08JD; -.
PhylomeDB; Q01201; -.
TreeFam; TF325632; -.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
SIGNOR; Q01201; -.
ChiTaRS; RELB; human.
GeneWiki; RELB; -.
GenomeRNAi; 5971; -.
PRO; PR:Q01201; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000104856; -.
CleanEx; HS_RELB; -.
ExpressionAtlas; Q01201; baseline and differential.
Genevisible; Q01201; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0033256; C:I-kappaB/NF-kappaB complex; IBA:GO_Central.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:CACAO.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
GO; GO:0001047; F:core promoter binding; ISS:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0019882; P:antigen processing and presentation; IEA:Ensembl.
GO; GO:0071470; P:cellular response to osmotic stress; IEA:Ensembl.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0030098; P:lymphocyte differentiation; IMP:UniProtKB.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IEA:Ensembl.
GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:CACAO.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0038061; P:NIK/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0045063; P:T-helper 1 cell differentiation; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd01177; IPT_NFkappaB; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 2.60.40.340; -; 1.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002909; IPT_dom.
InterPro; IPR033926; IPT_NFkappaB.
InterPro; IPR000451; NFkB/Dor.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR030496; RelB.
InterPro; IPR032399; RelB_leu_zip.
InterPro; IPR032400; RelB_transact.
InterPro; IPR030492; RHD_CS.
InterPro; IPR032397; RHD_dimer.
InterPro; IPR011539; RHD_DNA_bind_dom.
InterPro; IPR037059; RHD_DNA_bind_dom_sf.
PANTHER; PTHR24169; PTHR24169; 1.
PANTHER; PTHR24169:SF18; PTHR24169:SF18; 1.
Pfam; PF16180; RelB_leu_zip; 1.
Pfam; PF16181; RelB_transactiv; 1.
Pfam; PF16179; RHD_dimer; 1.
Pfam; PF00554; RHD_DNA_bind; 1.
PRINTS; PR00057; NFKBTNSCPFCT.
SMART; SM00429; IPT; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS01204; REL_1; 1.
PROSITE; PS50254; REL_2; 1.
1: Evidence at protein level;
Activator; Biological rhythms; Complete proteome; Cytoplasm;
Cytoskeleton; Disease mutation; DNA-binding; Methylation; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repressor;
Transcription; Transcription regulation.
CHAIN 1 579 Transcription factor RelB.
/FTId=PRO_0000205173.
DOMAIN 125 440 RHD. {ECO:0000255|PROSITE-
ProRule:PRU00265}.
REGION 40 68 Leucine-zipper.
MOTIF 433 438 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 16 16 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 573 573 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
VARIANT 396 396 T -> M (in dbSNP:rs2230682).
/FTId=VAR_051782.
VARIANT 397 579 Missing (in IMD53).
{ECO:0000269|PubMed:26385063}.
/FTId=VAR_079201.
CONFLICT 139 139 R -> P (in Ref. 1; AAA36127).
{ECO:0000305}.
CONFLICT 411 411 R -> A (in Ref. 1; AAA36127).
{ECO:0000305}.
SEQUENCE 579 AA; 62134 MW; C2C61C2C8640513E CRC64;
MLRSGPASGP SVPTGRAMPS RRVARPPAAP ELGALGSPDL SSLSLAVSRS TDELEIIDEY
IKENGFGLDG GQPGPGEGLP RLVSRGAASL STVTLGPVAP PATPPPWGCP LGRLVSPAPG
PGPQPHLVIT EQPKQRGMRF RYECEGRSAG SILGESSTEA SKTLPAIELR DCGGLREVEV
TACLVWKDWP HRVHPHSLVG KDCTDGICRV RLRPHVSPRH SFNNLGIQCV RKKEIEAAIE
RKIQLGIDPY NAGSLKNHQE VDMNVVRICF QASYRDQQGQ MRRMDPVLSE PVYDKKSTNT
SELRICRINK ESGPCTGGEE LYLLCDKVQK EDISVVFSRA SWEGRADFSQ ADVHRQIAIV
FKTPPYEDLE IVEPVTVNVF LQRLTDGVCS EPLPFTYLPR DHDSYGVDKK RKRGMPDVLG
ELNSSDPHGI ESKRRKKKPA ILDHFLPNHG SGPFLPPSAL LPDPDFFSGT VSLPGLEPPG
GPDLLDDGFA YDPTAPTLFT MLDLLPPAPP HASAVVCSGG AGAVVGETPG PEPLTLDSYQ
APGPGDGGTA SLVGSNMFPN HYREAAFGGG LLSPGPEAT


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