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Q04863 (RELB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor RelB
Gene names
Name:Relb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length558 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 By similarity. As a member of the NUPR1/RELB/IER3 survival pathway, may allow the development of pancreatic intraepithelial neoplasias. Ref.9

Subunit structure

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. Ref.7 Ref.8

Subcellular location

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Note: Colocalizes with NEK6 in the centrosome By similarity.

Tissue specificity

Expressed in intestine, thymus and spleen. Undetectable in liver, bome marrow, kidney and testis.

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.

Sequence similarities

Contains 1 RHD (Rel-like) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 558558Transcription factor RelB
PRO_0000205174

Regions

Domain103 – 418316RHD
Region22 – 5029Leucine-zipper
Motif387 – 3915Nuclear localization signal Potential
Motif411 – 4166Nuclear localization signal Potential

Amino acid modifications

Modified residue191Phosphoserine By similarity
Modified residue841Phosphothreonine Ref.6
Modified residue5521Phosphoserine Ref.6

Experimental info

Mutagenesis3681S → A or E: Strongly reduces transcriptional activity and interaction with NFKB1/p50 and NFKB2/p52. Ref.8
Sequence conflict511D → V in AAA40041. Ref.1
Sequence conflict1421L → Q in AAA40041. Ref.1

Secondary structure

........................................................................ 558
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q04863 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: AA49781A891ED7B8

FASTA55860,305
        10         20         30         40         50         60 
MPSRRAARES APELGALGSS DLSSLSLTVS RTTDELEIID EYIKENGFGL DGTQLSEMPR 

        70         80         90        100        110        120 
LVPRGPASLS SVTLGPAAPP PPATPSWSCT LGRLVSPGPC PRPYLVITEQ PKQRGMRFRY 

       130        140        150        160        170        180 
ECEGRSAGSI LGESSTEASK TLPAIELRDC GGLREVEVTA CLVWKDWPHR VHPHSLVGKD 

       190        200        210        220        230        240 
CTDGVCRVRL RPHVSPRHSF NNLGIQCVRK KEIEAAIERK IQLGIDPYNA GSLKNHQEVD 

       250        260        270        280        290        300 
MNVVRICFQA SYRDQQGHLH RMDPILSEPV YDKKSTNTSE LRICRINKES GPCTGGEELY 

       310        320        330        340        350        360 
LLCDKVQKED ISVVFSTASW EGRADFSQAD VHRQIAIVFK TPPYEDLEIS EPVTVNVFLQ 

       370        380        390        400        410        420 
RLTDGVCSEP LPFTYLPRDH DSYGVDKKRK RGLPDVLGEL SSSDPHGIES KRRKKKPVFL 

       430        440        450        460        470        480 
DHFLPGHSSG LFLPPSALQP ADSDFFPASI SLPGLEPPGG PDLLDDGFAY DPSAPTLFTM 

       490        500        510        520        530        540 
LDLLPPAPPL ASAVVGSGGA GATVVESSGP EPLSLDSFAA PGPGDVGTAS LVGSNMFPNQ 

       550 
YREAAFGGGL LSPGPEAT 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[3]"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].
Strain: FVB/N.
Tissue: Mammary tumor.
[4]"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: NUCLEOTIDE SEQUENCE [MRNA] OF 1-116.
[5]"Expression of relB is required for the development of thymic medulla and dendritic cells."
Burkly L., Hession C., Ogata L., Reilly C., Marconi L.A., Olson D., Tizard R., Cate R., Lo D.
Nature 373:531-536(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 309-429.
Strain: C57BL/6.
Tissue: Liver.
[6]"Signal-specific and phosphorylation-dependent RelB degradation: a potential mechanism of NF-kappaB control."
Marienfeld R., Berberich-Siebelt F., Berberich I., Denk A., Serfling E., Neumann M.
Oncogene 20:8142-8147(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-84 AND SER-552.
[7]"Peptide-induced negative selection of thymocytes activates transcription of an NF-kappa B inhibitor."
Fiorini E., Schmitz I., Marissen W.E., Osborn S.L., Touma M., Sasada T., Reche P.A., Tibaldi E.V., Hussey R.E., Kruisbeek A.M., Reinherz E.L., Clayton L.K.
Mol. Cell 9:637-648(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NFKBID.
[8]"Critical role of RelB serine 368 for dimerization and p100 stabilization."
Maier H.J., Marienfeld R., Wirth T., Baumann B.
J. Biol. Chem. 278:39242-39250(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SELF-ASSOCIATION, INTERACTION WITH NFKB1 AND NFKB2, MUTAGENESIS OF SER-368.
[9]"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.
[10]"NF-kappaB RelB forms an intertwined homodimer."
Huang D.B., Vu D., Ghosh G.
Structure 13:1365-1373(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 277-378.
[11]"X-ray structure of a NF-kappaB p50/RelB/DNA complex reveals assembly of multiple dimers on tandem kappaB sites."
Moorthy A.K., Huang D.B., Wang V.Y., Vu D., Ghosh G.
J. Mol. Biol. 373:723-734(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 91-378 IN COMPLEX WITH NFKB1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS39799.1.
PIRA42023.
I58091.
RefSeqNP_001277386.1. NM_001290457.1.
NP_033072.2. NM_009046.2.
UniGeneMm.1741.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ04863.
SMRQ04863. Positions 88-383.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202854. 3 interactions.
DIPDIP-39585N.
IntActQ04863. 4 interactions.
MINTMINT-225343.

PTM databases

PhosphoSiteQ04863.

Proteomic databases

PRIDEQ04863.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000094762; ENSMUSP00000092355; ENSMUSG00000002983.
ENSMUST00000098754; ENSMUSP00000096350; ENSMUSG00000002983.
GeneID19698.
KEGGmmu:19698.
UCSCuc009fmo.1. mouse.

Organism-specific databases

CTD5971.
MGIMGI:103289. Relb.

Phylogenomic databases

eggNOGNOG119056.
GeneTreeENSGT00500000044765.
HOGENOMHOG000148598.
HOVERGENHBG017021.
InParanoidQ8VE46.
KOK09253.
OMADDGFAYD.
OrthoDBEOG7VHSWT.
TreeFamTF325632.

Gene expression databases

ArrayExpressQ04863.
BgeeQ04863.
GenevestigatorQ04863.

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

EvolutionaryTraceQ04863.
NextBio297052.
PROQ04863.
SOURCESearch...

Entry information

Entry nameRELB_MOUSE
AccessionPrimary (citable) accession number: Q04863
Secondary accession number(s): Q8VE46
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot