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Q04863

- RELB_MOUSE

UniProt

Q04863 - RELB_MOUSE

Protein

Transcription factor RelB

Gene

Relb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    4. 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

    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. cytosol Source: MGI
    2. microtubule organizing center Source: UniProtKB-SubCell
    3. nucleus Source: MGI

    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

    PRIDEiQ04863.

    PTM databases

    PhosphoSiteiQ04863.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiQ04863.
    BgeeiQ04863.
    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 – 973
    Beta strandi104 – 1096
    Beta strandi113 – 1164
    Helixi121 – 1233
    Beta strandi132 – 1343
    Beta strandi137 – 1393
    Beta strandi145 – 1495
    Beta strandi156 – 1605
    Beta strandi165 – 1684
    Beta strandi173 – 1786
    Beta strandi182 – 1843
    Beta strandi186 – 1905
    Turni192 – 1943
    Beta strandi197 – 1993
    Beta strandi204 – 2074
    Turni210 – 2123
    Helixi213 – 22210
    Beta strandi234 – 2363
    Beta strandi241 – 2455
    Beta strandi250 – 2523
    Beta strandi255 – 2573
    Beta strandi270 – 2745
    Helixi276 – 2783
    Beta strandi279 – 2813
    Beta strandi283 – 2875
    Beta strandi289 – 2924
    Beta strandi297 – 2993
    Beta strandi301 – 3044
    Helixi308 – 3103
    Beta strandi314 – 3174
    Beta strandi320 – 3234
    Helixi328 – 3303
    Turni333 – 3353
    Beta strandi336 – 3405
    Beta strandi353 – 3575
    Turni362 – 3643
    Beta strandi371 – 3755

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    InParanoidiQ8VE46.
    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

    MPSRRAARES APELGALGSS DLSSLSLTVS RTTDELEIID EYIKENGFGL    50
    DGTQLSEMPR LVPRGPASLS SVTLGPAAPP PPATPSWSCT LGRLVSPGPC 100
    PRPYLVITEQ PKQRGMRFRY ECEGRSAGSI LGESSTEASK TLPAIELRDC 150
    GGLREVEVTA CLVWKDWPHR VHPHSLVGKD CTDGVCRVRL RPHVSPRHSF 200
    NNLGIQCVRK KEIEAAIERK IQLGIDPYNA GSLKNHQEVD MNVVRICFQA 250
    SYRDQQGHLH RMDPILSEPV YDKKSTNTSE LRICRINKES GPCTGGEELY 300
    LLCDKVQKED ISVVFSTASW EGRADFSQAD VHRQIAIVFK TPPYEDLEIS 350
    EPVTVNVFLQ RLTDGVCSEP LPFTYLPRDH DSYGVDKKRK RGLPDVLGEL 400
    SSSDPHGIES KRRKKKPVFL DHFLPGHSSG LFLPPSALQP ADSDFFPASI 450
    SLPGLEPPGG PDLLDDGFAY DPSAPTLFTM LDLLPPAPPL ASAVVGSGGA 500
    GATVVESSGP EPLSLDSFAA PGPGDVGTAS LVGSNMFPNQ YREAAFGGGL 550
    LSPGPEAT 558
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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

    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 Q8VE46.
    KOi K09253.
    OMAi DDGFAYD.
    OrthoDBi EOG7VHSWT.
    TreeFami TF325632.

    Miscellaneous databases

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

    Gene expression databases

    ArrayExpressi Q04863.
    Bgeei Q04863.
    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

    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: October 1, 2014
    This is version 118 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