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Protein

Transcription factor RelB

Gene

RELB

Organism
Homo sapiens (Human)
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. 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/p52.4 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_188330. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_355503. CD209 (DC-SIGN) signaling.

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
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:9956. RELB.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34322.

Polymorphism and mutation databases

BioMutaiRELB.
DMDMi92090634.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 579579Transcription factor RelBPRO_0000205173Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371Phosphoserine2 Publications
Modified residuei573 – 5731Phosphoserine2 Publications

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ01201.
PaxDbiQ01201.
PRIDEiQ01201.

PTM databases

PhosphoSiteiQ01201.

Expressioni

Inductioni

Up-regulated by mitogens and NUPR1.1 Publication

Gene expression databases

BgeeiQ01201.
CleanExiHS_RELB.
ExpressionAtlasiQ01201. baseline and differential.
GenevestigatoriQ01201.

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

WithEntry#Exp.IntActNotes
COMMD1Q8N6682EBI-357837,EBI-1550112
GSK3BP498414EBI-357837,EBI-373586
NFKB1P198384EBI-357837,EBI-300010
NFKB2Q006533EBI-357837,EBI-307326
RELAQ042062EBI-357837,EBI-73886

Protein-protein interaction databases

BioGridi111903. 55 interactions.
DIPiDIP-27531N.
IntActiQ01201. 33 interactions.
MINTiMINT-1131428.
STRINGi9606.ENSP00000221452.

Structurei

3D structure databases

ProteinModelPortaliQ01201.
SMRiQ01201. Positions 123-400.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini125 – 440316RHDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 6829Leucine-zipperAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi433 – 4386Nuclear localization signalSequence Analysis

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

eggNOGiNOG119056.
GeneTreeiENSGT00500000044765.
HOGENOMiHOG000148598.
HOVERGENiHBG017021.
InParanoidiQ01201.
KOiK09253.
OMAiDDGFAYD.
OrthoDBiEOG7VHSWT.
PhylomeDBiQ01201.
TreeFamiTF325632.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NFkB/Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR030496. RelB.
IPR011539. RHD.
IPR030492. RHD_CS.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 1 hit.
PTHR24169:SF18. PTHR24169:SF18. 1 hit.
PfamiPF00554. RHD. 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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391R → P in AAA36127 (PubMed:1577270).Curated
Sequence conflicti411 – 4111R → A in AAA36127 (PubMed:1577270).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti396 – 3961T → M.
Corresponds to variant rs2230682 [ dbSNP | Ensembl ].
VAR_051782

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.
UCSCiuc021uvp.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

3D structure databases

ProteinModelPortaliQ01201.
SMRiQ01201. Positions 123-400.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111903. 55 interactions.
DIPiDIP-27531N.
IntActiQ01201. 33 interactions.
MINTiMINT-1131428.
STRINGi9606.ENSP00000221452.

PTM databases

PhosphoSiteiQ01201.

Polymorphism and mutation databases

BioMutaiRELB.
DMDMi92090634.

Proteomic databases

MaxQBiQ01201.
PaxDbiQ01201.
PRIDEiQ01201.

Protocols and materials databases

DNASUi5971.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221452; ENSP00000221452; ENSG00000104856.
ENST00000625761; ENSP00000485826; ENSG00000104856.
GeneIDi5971.
KEGGihsa:5971.
UCSCiuc021uvp.1. human.

Organism-specific databases

CTDi5971.
GeneCardsiGC19P045504.
HGNCiHGNC:9956. RELB.
HPAiCAB007753.
HPA040506.
MIMi604758. gene.
neXtProtiNX_Q01201.
PharmGKBiPA34322.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG119056.
GeneTreeiENSGT00500000044765.
HOGENOMiHOG000148598.
HOVERGENiHBG017021.
InParanoidiQ01201.
KOiK09253.
OMAiDDGFAYD.
OrthoDBiEOG7VHSWT.
PhylomeDBiQ01201.
TreeFamiTF325632.

Enzyme and pathway databases

ReactomeiREACT_188330. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_355503. CD209 (DC-SIGN) signaling.

Miscellaneous databases

GeneWikiiRELB.
GenomeRNAii5971.
NextBioi23245.
PROiQ01201.
SOURCEiSearch...

Gene expression databases

BgeeiQ01201.
CleanExiHS_RELB.
ExpressionAtlasiQ01201. baseline and differential.
GenevestigatoriQ01201.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NFkB/Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR030496. RelB.
IPR011539. RHD.
IPR030492. RHD_CS.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 1 hit.
PTHR24169:SF18. PTHR24169:SF18. 1 hit.
PfamiPF00554. RHD. 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...

Publicationsi

« Hide 'large scale' publications
  1. "I-Rel: a novel rel-related protein that inhibits NF-kappa B transcriptional activity."
    Ruben S.M., Klement J.F., Maher M., Coleman T.A., Chen C.H., Rosen C.A.
    Genes Dev. 6:745-760(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: T-cell.
  2. "A transcriptional map in the region of 19q13 derived using direct sequencing and exon trapping."
    Yoshiura K., Murray J.C.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Blood.
  5. "RelB, a new Rel family transcription activator that can interact with p50-NF-kappa B."
    Ryseck R.P., Bull P., Takamiya M., Bours V., Siebenlist U., Dobrzanski P., Bravo R.
    Mol. Cell. Biol. 12:674-684(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE NF-KAPPA-B RELB-P50 COMPLEX.
  6. "Both N- and C-terminal domains of RelB are required for full transactivation: role of the N-terminal leucine zipper-like motif."
    Dobrzanski P., Ryseck R.P., Bravo R.
    Mol. Cell. Biol. 13:1572-1582(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Differential interactions of Rel-NF-kappa B complexes with I kappa B alpha determine pools of constitutive and inducible NF-kappa B activity."
    Dobrzanski P., Ryseck R.P., Bravo R.
    EMBO J. 13:4608-4616(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE NF-KAPPA-B RELB-P50 COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B RELB-P52 COMPLEX.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-573, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome."
    Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J.
    J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Nuclear protein 1 promotes pancreatic cancer development and protects cells from stress by inhibiting apoptosis."
    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.
    J. Clin. Invest. 122:2092-2103(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY NUPR1.

Entry informationi

Entry nameiRELB_HUMAN
AccessioniPrimary (citable) accession number: Q01201
Secondary accession number(s): Q6GTX7, Q9UEI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: April 4, 2006
Last modified: May 27, 2015
This is version 152 of the entry and version 2 of the sequence. [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

Caution

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.