Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transcription factor RelB

Gene

Relb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 (By similarity). As a member of the NUPR1/RELB/IER3 survival pathway, may allow the development of pancreatic intraepithelial neoplasias. 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 (By similarity).By similarity2 Publications

GO - Molecular functioni

  • chromatin binding Source: GO_Central
  • core promoter binding Source: UniProtKB
  • DNA binding Source: MGI
  • DNA binding transcription factor activity Source: InterPro
  • identical protein binding Source: IntAct
  • protein kinase binding Source: MGI

GO - Biological processi

  • antigen processing and presentation Source: MGI
  • cellular response to osmotic stress Source: Ensembl
  • circadian regulation of gene expression Source: UniProtKB
  • I-kappaB kinase/NF-kappaB signaling Source: GO_Central
  • inflammatory response Source: GO_Central
  • innate immune response Source: GO_Central
  • lymphocyte differentiation Source: MGI
  • myeloid dendritic cell differentiation Source: MGI
  • negative regulation of interferon-beta production Source: MGI
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription by RNA polymerase II Source: GO_Central
  • NIK/NF-kappaB signaling Source: MGI
  • positive regulation of gene expression Source: MGI
  • response to cytokine Source: GO_Central
  • T-helper 1 cell differentiation Source: MGI
  • T-helper 1 type immune response Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionActivator, Repressor
Biological processBiological rhythms, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-MMU-5621575 CD209 (DC-SIGN) signaling
R-MMU-5676590 NIK-->noncanonical NF-kB signaling

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor RelB
Gene namesi
Name:Relb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:103289 Relb

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi368S → A or E: Strongly reduces transcriptional activity and interaction with NFKB1/p50 and NFKB2/p52. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002051741 – 558Transcription factor RelBAdd BLAST558

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei19PhosphoserineBy similarity1
Modified residuei84Phosphothreonine1 Publication1
Modified residuei552Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylation at 'Thr-103' and 'Ser-573' is followed by proteasomal degradation.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ04863
PaxDbiQ04863
PeptideAtlasiQ04863
PRIDEiQ04863

PTM databases

iPTMnetiQ04863
PhosphoSitePlusiQ04863

Expressioni

Tissue specificityi

Expressed in intestine, thymus and spleen. Undetectable in liver, bome marrow, kidney and testis.

Gene expression databases

BgeeiENSMUSG00000002983
ExpressionAtlasiQ04863 baseline and differential
GenevisibleiQ04863 MM

Interactioni

Subunit structurei

Component of the NF-kappa-B RelB-p50 complex. Component of the NF-kappa-B RelB-p52 complex (By similarity). Self-associates; the interaction seems to be transient and may prevent degradation allowing for heterodimer formation 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 similarity4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein kinase binding Source: MGI

Protein-protein interaction databases

BioGridi202854, 3 interactors
DIPiDIP-39585N
IntActiQ04863, 5 interactors
MINTiQ04863
STRINGi10090.ENSMUSP00000092355

Structurei

Secondary structure

1558
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi95 – 97Combined sources3
Beta strandi104 – 109Combined sources6
Beta strandi113 – 116Combined sources4
Helixi121 – 123Combined sources3
Beta strandi132 – 134Combined sources3
Beta strandi137 – 139Combined sources3
Beta strandi145 – 149Combined sources5
Beta strandi156 – 160Combined sources5
Beta strandi165 – 168Combined sources4
Beta strandi173 – 178Combined sources6
Beta strandi182 – 184Combined sources3
Beta strandi186 – 190Combined sources5
Turni192 – 194Combined sources3
Beta strandi197 – 199Combined sources3
Beta strandi204 – 207Combined sources4
Turni210 – 212Combined sources3
Helixi213 – 222Combined sources10
Beta strandi234 – 236Combined sources3
Beta strandi241 – 245Combined sources5
Beta strandi250 – 252Combined sources3
Beta strandi255 – 257Combined sources3
Beta strandi270 – 274Combined sources5
Helixi276 – 278Combined sources3
Beta strandi279 – 281Combined sources3
Beta strandi283 – 287Combined sources5
Beta strandi289 – 292Combined sources4
Beta strandi297 – 299Combined sources3
Beta strandi301 – 304Combined sources4
Helixi308 – 310Combined sources3
Beta strandi314 – 317Combined sources4
Beta strandi320 – 323Combined sources4
Helixi328 – 330Combined sources3
Turni333 – 335Combined sources3
Beta strandi336 – 340Combined sources5
Beta strandi353 – 357Combined sources5
Turni362 – 364Combined sources3
Beta strandi371 – 375Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZK9X-ray2.18A277-378[»]
1ZKAX-ray2.20A277-378[»]
2V2TX-ray3.05A91-378[»]
3DO7X-ray3.05A88-383[»]
3JSSX-ray2.60A278-378[»]
3JUZX-ray2.51A278-378[»]
3JV0X-ray2.65A278-378[»]
3JV4X-ray3.15A/C/E278-378[»]
3JV6X-ray2.78A/C/E278-378[»]
4JGMX-ray3.00A277-378[»]
4JHBX-ray2.44A277-378[»]
ProteinModelPortaliQ04863
SMRiQ04863
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04863

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini103 – 418RHDPROSITE-ProRule annotationAdd BLAST316

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 50Leucine-zipperAdd BLAST29

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi387 – 391Nuclear localization signalSequence analysis5
Motifi411 – 416Nuclear localization signalSequence analysis6

Domaini

Both N- and C-terminal domains are required for transcriptional activation.

Phylogenomic databases

eggNOGiENOG410IFBK Eukaryota
ENOG410ZMME LUCA
GeneTreeiENSGT00500000044765
HOGENOMiHOG000148598
HOVERGENiHBG017021
InParanoidiQ04863
KOiK09253
OMAiDFFSGTV
OrthoDBiEOG091G08JD
TreeFamiTF325632

Family and domain databases

CDDicd01177 IPT_NFkappaB, 1 hit
Gene3Di2.60.40.10, 1 hit
2.60.40.340, 1 hit
InterProiView protein in InterPro
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR002909 IPT_dom
IPR033926 IPT_NFkappaB
IPR000451 NFkB/Dor
IPR008967 p53-like_TF_DNA-bd
IPR030496 RelB
IPR032399 RelB_leu_zip
IPR032400 RelB_transact
IPR030492 RHD_CS
IPR032397 RHD_dimer
IPR011539 RHD_DNA_bind_dom
IPR037059 RHD_DNA_bind_dom_sf
PANTHERiPTHR24169 PTHR24169, 1 hit
PTHR24169:SF18 PTHR24169:SF18, 1 hit
PfamiView protein in Pfam
PF16180 RelB_leu_zip, 1 hit
PF16181 RelB_transactiv, 1 hit
PF16179 RHD_dimer, 1 hit
PF00554 RHD_DNA_bind, 1 hit
PRINTSiPR00057 NFKBTNSCPFCT
SMARTiView protein in SMART
SM00429 IPT, 1 hit
SUPFAMiSSF49417 SSF49417, 1 hit
SSF81296 SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS01204 REL_1, 1 hit
PS50254 REL_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q04863-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSRRAARES APELGALGSS DLSSLSLTVS RTTDELEIID EYIKENGFGL
60 70 80 90 100
DGTQLSEMPR LVPRGPASLS SVTLGPAAPP PPATPSWSCT LGRLVSPGPC
110 120 130 140 150
PRPYLVITEQ PKQRGMRFRY ECEGRSAGSI LGESSTEASK TLPAIELRDC
160 170 180 190 200
GGLREVEVTA CLVWKDWPHR VHPHSLVGKD CTDGVCRVRL RPHVSPRHSF
210 220 230 240 250
NNLGIQCVRK KEIEAAIERK IQLGIDPYNA GSLKNHQEVD MNVVRICFQA
260 270 280 290 300
SYRDQQGHLH RMDPILSEPV YDKKSTNTSE LRICRINKES GPCTGGEELY
310 320 330 340 350
LLCDKVQKED ISVVFSTASW EGRADFSQAD VHRQIAIVFK TPPYEDLEIS
360 370 380 390 400
EPVTVNVFLQ RLTDGVCSEP LPFTYLPRDH DSYGVDKKRK RGLPDVLGEL
410 420 430 440 450
SSSDPHGIES KRRKKKPVFL DHFLPGHSSG LFLPPSALQP ADSDFFPASI
460 470 480 490 500
SLPGLEPPGG PDLLDDGFAY DPSAPTLFTM LDLLPPAPPL ASAVVGSGGA
510 520 530 540 550
GATVVESSGP EPLSLDSFAA PGPGDVGTAS LVGSNMFPNQ YREAAFGGGL

LSPGPEAT
Length:558
Mass (Da):60,305
Last modified:July 27, 2011 - v2
Checksum:iAA49781A891ED7B8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti51D → V in AAA40041 (PubMed:1732739).Curated1
Sequence conflicti142L → Q in AAA40041 (PubMed:1732739).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83380 mRNA Translation: AAA40041.1
AK146932 mRNA Translation: BAE27543.1
BC019765 mRNA Translation: AAH19765.1
BC117793 mRNA Translation: AAI17794.1
S56076 mRNA Translation: AAB25493.2
S76754 Genomic DNA Translation: AAB33259.1
CCDSiCCDS39799.1
PIRiA42023
I58091
RefSeqiNP_001277386.1, NM_001290457.1
NP_033072.2, NM_009046.2
UniGeneiMm.1741

Genome annotation databases

EnsembliENSMUST00000094762; ENSMUSP00000092355; ENSMUSG00000002983
ENSMUST00000098754; ENSMUSP00000096350; ENSMUSG00000002983
GeneIDi19698
KEGGimmu:19698
UCSCiuc012fbg.1 mouse

Similar proteinsi

Entry informationi

Entry nameiRELB_MOUSE
AccessioniPrimary (citable) accession number: Q04863
Secondary accession number(s): Q8VE46
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 27, 2011
Last modified: April 25, 2018
This is version 151 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health