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
Homo sapiens (Human)
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. 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).5 Publications

Caution

Was originally thought to inhibit the transcriptional activity of nuclear factor NF-kappa-B.1 Publication

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActivator, DNA-binding, Repressor
Biological processBiological rhythms, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5621575 CD209 (DC-SIGN) signaling
R-HSA-5676590 NIK-->noncanonical NF-kB signaling
SIGNORiQ01201

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor RelB
Alternative name(s):
I-Rel
Gene namesi
Name:RELB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000104856.13
HGNCiHGNC:9956 RELB
MIMi604758 gene
neXtProtiNX_Q01201

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

Involvement in diseasei

Immunodeficiency 53 (IMD53)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:617585
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_079201397 – 579Missing in IMD53. 1 PublicationAdd BLAST183

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi5971
MalaCardsiRELB
MIMi617585 phenotype
OpenTargetsiENSG00000104856
PharmGKBiPA34322

Polymorphism and mutation databases

BioMutaiRELB
DMDMi92090634

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002051731 – 579Transcription factor RelBAdd BLAST579

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei16Omega-N-methylarginineCombined sources1
Modified residuei37PhosphoserineCombined sources1
Modified residuei573PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation at 'Thr-103' and 'Ser-573' is followed by proteasomal degradation.By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiQ01201
MaxQBiQ01201
PaxDbiQ01201
PeptideAtlasiQ01201
PRIDEiQ01201

PTM databases

iPTMnetiQ01201
PhosphoSitePlusiQ01201

Expressioni

Inductioni

Up-regulated by mitogens and NUPR1.1 Publication

Gene expression databases

BgeeiENSG00000104856
CleanExiHS_RELB
ExpressionAtlasiQ01201 baseline and differential
GenevisibleiQ01201 HS

Organism-specific databases

HPAiCAB007753
HPA040506

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: Ensembl
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111903, 52 interactors
CORUMiQ01201
DIPiDIP-27531N
IntActiQ01201, 32 interactors
MINTiQ01201
STRINGi9606.ENSP00000221452

Structurei

3D structure databases

ProteinModelPortaliQ01201
SMRiQ01201
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini125 – 440RHDPROSITE-ProRule annotationAdd BLAST316

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni40 – 68Leucine-zipperAdd BLAST29

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi433 – 438Nuclear localization signalSequence analysis6

Domaini

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

Phylogenomic databases

eggNOGiENOG410IFBK Eukaryota
ENOG410ZMME LUCA
GeneTreeiENSGT00500000044765
HOGENOMiHOG000148598
HOVERGENiHBG017021
InParanoidiQ01201
KOiK09253
OMAiDFFSGTV
OrthoDBiEOG091G08JD
PhylomeDBiQ01201
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.

Q01201-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRSGPASGP SVPTGRAMPS RRVARPPAAP ELGALGSPDL SSLSLAVSRS
60 70 80 90 100
TDELEIIDEY IKENGFGLDG GQPGPGEGLP RLVSRGAASL STVTLGPVAP
110 120 130 140 150
PATPPPWGCP LGRLVSPAPG PGPQPHLVIT EQPKQRGMRF RYECEGRSAG
160 170 180 190 200
SILGESSTEA SKTLPAIELR DCGGLREVEV TACLVWKDWP HRVHPHSLVG
210 220 230 240 250
KDCTDGICRV RLRPHVSPRH SFNNLGIQCV RKKEIEAAIE RKIQLGIDPY
260 270 280 290 300
NAGSLKNHQE VDMNVVRICF QASYRDQQGQ MRRMDPVLSE PVYDKKSTNT
310 320 330 340 350
SELRICRINK ESGPCTGGEE LYLLCDKVQK EDISVVFSRA SWEGRADFSQ
360 370 380 390 400
ADVHRQIAIV FKTPPYEDLE IVEPVTVNVF LQRLTDGVCS EPLPFTYLPR
410 420 430 440 450
DHDSYGVDKK RKRGMPDVLG ELNSSDPHGI ESKRRKKKPA ILDHFLPNHG
460 470 480 490 500
SGPFLPPSAL LPDPDFFSGT VSLPGLEPPG GPDLLDDGFA YDPTAPTLFT
510 520 530 540 550
MLDLLPPAPP HASAVVCSGG AGAVVGETPG PEPLTLDSYQ APGPGDGGTA
560 570
SLVGSNMFPN HYREAAFGGG LLSPGPEAT
Length:579
Mass (Da):62,134
Last modified:April 4, 2006 - v2
Checksum:iC2C61C2C8640513E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti139R → P in AAA36127 (PubMed:1577270).Curated1
Sequence conflicti411R → A in AAA36127 (PubMed:1577270).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_051782396T → M. Corresponds to variant dbSNP:rs2230682Ensembl.1
Natural variantiVAR_079201397 – 579Missing in IMD53. 1 PublicationAdd BLAST183

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83221 mRNA Translation: AAA36127.1
AF043463
, AF043454, AF043455, AF043456, AF043457, AF043458, AF043459, AF043460, AF043461, AF043462 Genomic DNA Translation: AAC82346.1
DQ314887 Genomic DNA Translation: ABC40746.1
BC028013 mRNA Translation: AAH28013.1
CCDSiCCDS46110.1
PIRiA42617
RefSeqiNP_006500.2, NM_006509.3
UniGeneiHs.654402

Genome annotation databases

EnsembliENST00000221452; ENSP00000221452; ENSG00000104856
ENST00000625761; ENSP00000485826; ENSG00000104856
GeneIDi5971
KEGGihsa:5971
UCSCiuc060zvi.1 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiRELB_HUMAN
AccessioniPrimary (citable) accession number: Q01201
Secondary accession number(s): Q6GTX7, Q9UEI7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: April 4, 2006
Last modified: May 23, 2018
This is version 179 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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