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Protein

Transcription factor RelB

Gene

Relb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.By similarity2 Publications

GO - Molecular functioni

  • chromatin binding Source: GO_Central
  • core promoter binding Source: UniProtKB
  • DNA binding Source: MGI
  • transcription factor activity, sequence-specific DNA binding Source: InterPro

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
  • 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 from RNA polymerase II promoter 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
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Biological 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:103289. Relb.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • I-kappaB/NF-kappaB complex Source: GO_Central
  • microtubule organizing center Source: UniProtKB-SubCell
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

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

WithEntry#Exp.IntActNotes
Nfkb1P257992EBI-1209145,EBI-1209141
Nfkb2Q9WTK52EBI-1209145,EBI-1209166
NfkbiaQ9Z1E34EBI-1209145,EBI-644427
NfkbieO549102EBI-1209145,EBI-6688774

Protein-protein interaction databases

BioGridi202854. 3 interactors.
DIPiDIP-39585N.
IntActiQ04863. 4 interactors.
MINTiMINT-225343.
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.

Sequence similaritiesi

Contains 1 RHD (Rel-like) domain.PROSITE-ProRule annotation

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.
InterProiIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
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.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 1 hit.
PTHR24169:SF18. PTHR24169:SF18. 1 hit.
PfamiPF16180. RelB_leu_zip. 1 hit.
PF16181. RelB_transactiv. 1 hit.
PF16179. RHD_dimer. 1 hit.
PF00554. RHD_DNA_bind. 1 hit.
[Graphical view]
PRINTSiPR00057. NFKBTNSCPFCT.
SMARTiSM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi202854. 3 interactors.
DIPiDIP-39585N.
IntActiQ04863. 4 interactors.
MINTiMINT-225343.
STRINGi10090.ENSMUSP00000092355.

PTM databases

iPTMnetiQ04863.
PhosphoSitePlusiQ04863.

Proteomic databases

MaxQBiQ04863.
PaxDbiQ04863.
PeptideAtlasiQ04863.
PRIDEiQ04863.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5971.
MGIiMGI:103289. Relb.

Phylogenomic databases

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

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.

Miscellaneous databases

EvolutionaryTraceiQ04863.
PROiQ04863.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000002983.
ExpressionAtlasiQ04863. baseline and differential.
GenevisibleiQ04863. MM.

Family and domain databases

CDDicd01177. IPT_NFkappaB. 1 hit.
Gene3Di2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
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.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 1 hit.
PTHR24169:SF18. PTHR24169:SF18. 1 hit.
PfamiPF16180. RelB_leu_zip. 1 hit.
PF16181. RelB_transactiv. 1 hit.
PF16179. RHD_dimer. 1 hit.
PF00554. RHD_DNA_bind. 1 hit.
[Graphical view]
PRINTSiPR00057. NFKBTNSCPFCT.
SMARTiSM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRELB_MOUSE
AccessioniPrimary (citable) accession number: Q04863
Secondary accession number(s): Q8VE46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.