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Q01201 (RELB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor RelB
Alternative name(s):
I-Rel
Gene names
Name:RELB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length579 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.5 Ref.6 Ref.7 Ref.12

Subunit structure

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 By similarity. Ref.5 Ref.7

Subcellular location

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Colocalizes with NEK6 in the centrosome. Ref.10

Induction

Up-regulated by mitogens and NUPR1. Ref.12

Domain

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

Post-translational modification

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

Sequence similarities

Contains 1 RHD (Rel-like) domain.

Caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityPolymorphism
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT-helper 1 cell differentiation

Inferred from electronic annotation. Source: Ensembl

antigen processing and presentation

Inferred from electronic annotation. Source: Ensembl

myeloid dendritic cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from electronic annotation. Source: Ensembl

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 14743216PubMed 15799966PubMed 17962807PubMed 21217772PubMed 21988832. Source: IntAct

sequence-specific DNA binding transcription factor activity

Traceable author statement PubMed 8188306. Source: ProtInc

transcription corepressor activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 579579Transcription factor RelB
PRO_0000205173

Regions

Domain125 – 440316RHD
Region40 – 6829Leucine-zipper
Motif433 – 4386Nuclear localization signal Potential

Amino acid modifications

Modified residue371Phosphoserine Ref.8 Ref.11
Modified residue5731Phosphoserine Ref.8 Ref.9

Natural variations

Natural variant3961T → M.
Corresponds to variant rs2230682 [ dbSNP | Ensembl ].
VAR_051782

Experimental info

Sequence conflict1391R → P in AAA36127. Ref.1
Sequence conflict4111R → A in AAA36127. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q01201 [UniParc].

Last modified April 4, 2006. Version 2.
Checksum: C2C61C2C8640513E

FASTA57962,134
        10         20         30         40         50         60 
MLRSGPASGP SVPTGRAMPS RRVARPPAAP ELGALGSPDL SSLSLAVSRS TDELEIIDEY 

        70         80         90        100        110        120 
IKENGFGLDG GQPGPGEGLP RLVSRGAASL STVTLGPVAP PATPPPWGCP LGRLVSPAPG 

       130        140        150        160        170        180 
PGPQPHLVIT EQPKQRGMRF RYECEGRSAG SILGESSTEA SKTLPAIELR DCGGLREVEV 

       190        200        210        220        230        240 
TACLVWKDWP HRVHPHSLVG KDCTDGICRV RLRPHVSPRH SFNNLGIQCV RKKEIEAAIE 

       250        260        270        280        290        300 
RKIQLGIDPY NAGSLKNHQE VDMNVVRICF QASYRDQQGQ MRRMDPVLSE PVYDKKSTNT 

       310        320        330        340        350        360 
SELRICRINK ESGPCTGGEE LYLLCDKVQK EDISVVFSRA SWEGRADFSQ ADVHRQIAIV 

       370        380        390        400        410        420 
FKTPPYEDLE IVEPVTVNVF LQRLTDGVCS EPLPFTYLPR DHDSYGVDKK RKRGMPDVLG 

       430        440        450        460        470        480 
ELNSSDPHGI ESKRRKKKPA ILDHFLPNHG SGPFLPPSAL LPDPDFFSGT VSLPGLEPPG 

       490        500        510        520        530        540 
GPDLLDDGFA YDPTAPTLFT MLDLLPPAPP HASAVVCSGG AGAVVGETPG PEPLTLDSYQ 

       550        560        570 
APGPGDGGTA SLVGSNMFPN HYREAAFGGG LLSPGPEAT 

« Hide

References

« Hide 'large scale' references
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M83221 mRNA. Translation: AAA36127.1.
AF043463 expand/collapse EMBL AC list , 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.
CCDSCCDS46110.1.
PIRA42617.
RefSeqNP_006500.2. NM_006509.3.
UniGeneHs.654402.

3D structure databases

ProteinModelPortalQ01201.
SMRQ01201. Positions 123-400.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111903. 45 interactions.
DIPDIP-27531N.
IntActQ01201. 33 interactions.
MINTMINT-1131428.
STRING9606.ENSP00000221452.

PTM databases

PhosphoSiteQ01201.

Polymorphism databases

DMDM92090634.

Proteomic databases

MaxQBQ01201.
PaxDbQ01201.
PRIDEQ01201.

Protocols and materials databases

DNASU5971.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221452; ENSP00000221452; ENSG00000104856.
ENST00000540120; ENSP00000445542; ENSG00000104856.
GeneID5971.
KEGGhsa:5971.
UCSCuc021uvp.1. human.

Organism-specific databases

CTD5971.
GeneCardsGC19P045504.
HGNCHGNC:9956. RELB.
HPACAB007753.
HPA040506.
MIM604758. gene.
neXtProtNX_Q01201.
PharmGKBPA34322.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG119056.
HOGENOMHOG000148598.
HOVERGENHBG017021.
InParanoidQ01201.
KOK09253.
OMADDGFAYD.
OrthoDBEOG7VHSWT.
PhylomeDBQ01201.
TreeFamTF325632.

Gene expression databases

ArrayExpressQ01201.
BgeeQ01201.
CleanExHS_RELB.
GenevestigatorQ01201.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]
PfamPF00554. RHD. 1 hit.
[Graphical view]
PRINTSPR00057. NFKBTNSCPFCT.
SMARTSM00429. IPT. 1 hit.
[Graphical view]
SUPFAMSSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRELB.
GenomeRNAi5971.
NextBio23245.
PROQ01201.
SOURCESearch...

Entry information

Entry nameRELB_HUMAN
AccessionPrimary (citable) accession number: Q01201
Secondary accession number(s): Q6GTX7, Q9UEI7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: April 4, 2006
Last modified: July 9, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM