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Reviewed, UniProtKB/Swiss-Prot Q01201 (RELB_HUMAN)

Last modified November 25, 2008. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length579 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Subcellular location

Nucleus.

Induction

By mitogens.

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 componentNucleus
   Molecular functionActivator
   PTMPhosphoprotein

Gene Ontology (GO)

   Biological processregulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: InterPro

   Cellular componentnucleus

Inferred from electronic annotation. Source: InterPro

   Molecular functiontranscription corepressor activity Ref.1

Traceable author statement. Source: ProtInc

transcription factor activity

Traceable author statement. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

COMMD1Q8N6681EBI-357837,EBI-1550112

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 579579Transcription factor RelB
PRO_0000205173

Regions

Domain40 – 6829Leucine-zipper
Domain125 – 440316RHD
Motif433 – 4386Nuclear localization signal Potential

Amino acid modifications

Modified residue371Phosphoserine
Modified residue1031Phosphothreonine By similarity
Modified residue5731Phosphoserine

Experimental info

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

Sequences

Sequence LengthMass (Da)Tools
Q01201-1 [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: 1577270] [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: 15489334] [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: 1732739] [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: 8441398] [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: 7925301] [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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-573, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
PIRA42617.
RefSeqNP_006500.2.
UniGeneHs.654402

3D structure databases

HSSPHSSP built from PDB template 1MY7 based on UniProtKB Q04207.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:27531N.
IntActQ01201.

PTM databases

PhosphoSiteQ01201.

Genome annotation databases

EnsemblENSG00000104856. Homo sapiens. [Contig view]
GeneID5971.
KEGGhsa:5971.

Organism-specific databases

H-InvDBHIX0015220.
HGNCHGNC:9956. RELB.
HPACAB007753.
MIM604758. gene.
PharmGKBPA34322.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMQ01201.
HOVERGENQ01201.

Gene expression databases

ArrayExpressQ01201.
CleanExHS_RELB.
GermOnlineENSG00000104856. Homo sapiens.

Family and domain databases

InterProIPR013783. Ig-like_fold.
IPR002909. IPT_TIG_rcpt.
IPR000451. NF_Rel_dor.
IPR011539. RHD.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 1 hit.
G3DSA:2.60.40.340. RHD. 1 hit.
PfamPF00554. RHD. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
PRINTSPR00057. NFKBTNSCPFCT.
SMARTSM00429. IPT. 1 hit.
[Graphical view]
PROSITEPS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio23245.
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: November 25, 2008
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 19

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents