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Q04863

- RELB_MOUSE

UniProt

Q04863 - RELB_MOUSE

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Protein

Transcription factor RelB

Gene

Relb

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 (By similarity). As a member of the NUPR1/RELB/IER3 survival pathway, may allow the development of pancreatic intraepithelial neoplasias. 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.By similarity2 Publications

GO - Molecular functioni

  1. core promoter binding Source: UniProtKB
  2. DNA binding Source: MGI
  3. sequence-specific DNA binding transcription factor activity Source: InterPro

GO - Biological processi

  1. antigen processing and presentation Source: MGI
  2. circadian regulation of gene expression Source: UniProtKB
  3. myeloid dendritic cell differentiation Source: MGI
  4. negative regulation of transcription, DNA-templated Source: UniProtKB
  5. NIK/NF-kappaB signaling Source: MGI
  6. positive regulation of gene expression Source: MGI
  7. T-helper 1 cell differentiation Source: MGI
  8. T-helper 1 type immune response Source: MGI
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor RelB
Gene namesi
Name:Relb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:103289. Relb.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoskeleton Source: UniProtKB-KW
  2. cytosol Source: MGI
  3. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi368 – 3681S → A or E: Strongly reduces transcriptional activity and interaction with NFKB1/p50 and NFKB2/p52. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 558558Transcription factor RelBPRO_0000205174Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191PhosphoserineBy similarity
Modified residuei84 – 841Phosphothreonine1 Publication
Modified residuei552 – 5521Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation at 'Thr-103' and 'Ser-573' is followed by proteasomal degradation.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ04863.
PRIDEiQ04863.

PTM databases

PhosphoSiteiQ04863.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ04863.
ExpressionAtlasiQ04863. baseline and differential.
GenevestigatoriQ04863.

Interactioni

Subunit structurei

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. Interacts with ARNTL/BMAL1 and the interaction is enhanced in the presence of CLOCK.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Nfkb1P257992EBI-1209145,EBI-1209141
Nfkb2Q9WTK52EBI-1209145,EBI-1209166
NfkbiaQ9Z1E34EBI-1209145,EBI-644427
NfkbieO549102EBI-1209145,EBI-6688774

Protein-protein interaction databases

BioGridi202854. 3 interactions.
DIPiDIP-39585N.
IntActiQ04863. 4 interactions.
MINTiMINT-225343.

Structurei

Secondary structure

1
558
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi95 – 973Combined sources
Beta strandi104 – 1096Combined sources
Beta strandi113 – 1164Combined sources
Helixi121 – 1233Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi137 – 1393Combined sources
Beta strandi145 – 1495Combined sources
Beta strandi156 – 1605Combined sources
Beta strandi165 – 1684Combined sources
Beta strandi173 – 1786Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi186 – 1905Combined sources
Turni192 – 1943Combined sources
Beta strandi197 – 1993Combined sources
Beta strandi204 – 2074Combined sources
Turni210 – 2123Combined sources
Helixi213 – 22210Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi241 – 2455Combined sources
Beta strandi250 – 2523Combined sources
Beta strandi255 – 2573Combined sources
Beta strandi270 – 2745Combined sources
Helixi276 – 2783Combined sources
Beta strandi279 – 2813Combined sources
Beta strandi283 – 2875Combined sources
Beta strandi289 – 2924Combined sources
Beta strandi297 – 2993Combined sources
Beta strandi301 – 3044Combined sources
Helixi308 – 3103Combined sources
Beta strandi314 – 3174Combined sources
Beta strandi320 – 3234Combined sources
Helixi328 – 3303Combined sources
Turni333 – 3353Combined sources
Beta strandi336 – 3405Combined sources
Beta strandi353 – 3575Combined sources
Turni362 – 3643Combined sources
Beta strandi371 – 3755Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ04863.
SMRiQ04863. Positions 88-383.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04863.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini103 – 418316RHDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 5029Leucine-zipperAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi387 – 3915Nuclear localization signalSequence Analysis
Motifi411 – 4166Nuclear 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.
InParanoidiQ04863.
KOiK09253.
OMAiDDGFAYD.
OrthoDBiEOG7VHSWT.
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. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]
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.

Q04863-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPSRRAARES APELGALGSS DLSSLSLTVS RTTDELEIID EYIKENGFGL
60 70 80 90 100
DGTQLSEMPR LVPRGPASLS SVTLGPAAPP PPATPSWSCT LGRLVSPGPC
110 120 130 140 150
PRPYLVITEQ PKQRGMRFRY ECEGRSAGSI LGESSTEASK TLPAIELRDC
160 170 180 190 200
GGLREVEVTA CLVWKDWPHR VHPHSLVGKD CTDGVCRVRL RPHVSPRHSF
210 220 230 240 250
NNLGIQCVRK KEIEAAIERK IQLGIDPYNA GSLKNHQEVD MNVVRICFQA
260 270 280 290 300
SYRDQQGHLH RMDPILSEPV YDKKSTNTSE LRICRINKES GPCTGGEELY
310 320 330 340 350
LLCDKVQKED ISVVFSTASW EGRADFSQAD VHRQIAIVFK TPPYEDLEIS
360 370 380 390 400
EPVTVNVFLQ RLTDGVCSEP LPFTYLPRDH DSYGVDKKRK RGLPDVLGEL
410 420 430 440 450
SSSDPHGIES KRRKKKPVFL DHFLPGHSSG LFLPPSALQP ADSDFFPASI
460 470 480 490 500
SLPGLEPPGG PDLLDDGFAY DPSAPTLFTM LDLLPPAPPL ASAVVGSGGA
510 520 530 540 550
GATVVESSGP EPLSLDSFAA PGPGDVGTAS LVGSNMFPNQ YREAAFGGGL

LSPGPEAT
Length:558
Mass (Da):60,305
Last modified:July 27, 2011 - v2
Checksum:iAA49781A891ED7B8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511D → V in AAA40041. (PubMed:1732739)Curated
Sequence conflicti142 – 1421L → Q in AAA40041. (PubMed:1732739)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS39799.1.
PIRiA42023.
I58091.
RefSeqiNP_001277386.1. NM_001290457.1.
NP_033072.2. NM_009046.2.
UniGeneiMm.1741.

Genome annotation databases

EnsembliENSMUST00000094762; ENSMUSP00000092355; ENSMUSG00000002983.
ENSMUST00000098754; ENSMUSP00000096350; ENSMUSG00000002983.
GeneIDi19698.
KEGGimmu:19698.
UCSCiuc009fmo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS39799.1.
PIRi A42023.
I58091.
RefSeqi NP_001277386.1. NM_001290457.1.
NP_033072.2. NM_009046.2.
UniGenei Mm.1741.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZK9 X-ray 2.18 A 277-378 [» ]
1ZKA X-ray 2.20 A 277-378 [» ]
2V2T X-ray 3.05 A 91-378 [» ]
3DO7 X-ray 3.05 A 88-383 [» ]
3JSS X-ray 2.60 A 278-378 [» ]
3JUZ X-ray 2.51 A 278-378 [» ]
3JV0 X-ray 2.65 A 278-378 [» ]
3JV4 X-ray 3.15 A/C/E 278-378 [» ]
3JV6 X-ray 2.78 A/C/E 278-378 [» ]
4JGM X-ray 3.00 A 277-378 [» ]
4JHB X-ray 2.44 A 277-378 [» ]
ProteinModelPortali Q04863.
SMRi Q04863. Positions 88-383.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202854. 3 interactions.
DIPi DIP-39585N.
IntActi Q04863. 4 interactions.
MINTi MINT-225343.

PTM databases

PhosphoSitei Q04863.

Proteomic databases

MaxQBi Q04863.
PRIDEi Q04863.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000094762 ; ENSMUSP00000092355 ; ENSMUSG00000002983 .
ENSMUST00000098754 ; ENSMUSP00000096350 ; ENSMUSG00000002983 .
GeneIDi 19698.
KEGGi mmu:19698.
UCSCi uc009fmo.1. mouse.

Organism-specific databases

CTDi 5971.
MGIi MGI:103289. Relb.

Phylogenomic databases

eggNOGi NOG119056.
GeneTreei ENSGT00500000044765.
HOGENOMi HOG000148598.
HOVERGENi HBG017021.
InParanoidi Q04863.
KOi K09253.
OMAi DDGFAYD.
OrthoDBi EOG7VHSWT.
TreeFami TF325632.

Miscellaneous databases

EvolutionaryTracei Q04863.
NextBioi 297052.
PROi Q04863.
SOURCEi Search...

Gene expression databases

Bgeei Q04863.
ExpressionAtlasi Q04863. baseline and differential.
Genevestigatori Q04863.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProi IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view ]
Pfami PF00554. RHD. 1 hit.
[Graphical view ]
PRINTSi PR00057. NFKBTNSCPFCT.
SMARTi SM00429. IPT. 1 hit.
[Graphical view ]
SUPFAMi SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. "The RelB subunit of NFkappaB acts as a negative regulator of circadian gene expression."
    Bellet M.M., Zocchi L., Sassone-Corsi P.
    Cell Cycle 11:3304-3311(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ARNTL.
  10. "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.
  11. "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.
  12. "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.

Entry informationi

Entry nameiRELB_MOUSE
AccessioniPrimary (citable) accession number: Q04863
Secondary accession number(s): Q8VE46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3