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Q01201

- RELB_HUMAN

UniProt

Q01201 - RELB_HUMAN

Protein

Transcription factor RelB

Gene

RELB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (04 Apr 2006)
      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. 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. 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/p52.4 Publications

    GO - Molecular functioni

    1. core promoter binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. sequence-specific DNA binding transcription factor activity Source: ProtInc
    4. transcription corepressor activity Source: ProtInc

    GO - Biological processi

    1. antigen processing and presentation Source: Ensembl
    2. circadian regulation of gene expression Source: UniProtKB
    3. myeloid dendritic cell differentiation Source: Ensembl
    4. positive regulation of gene expression Source: Ensembl
    5. T-helper 1 cell differentiation Source: Ensembl
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Biological rhythms, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor RelB
    Alternative name(s):
    I-Rel
    Gene namesi
    Name:RELB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9956. RELB.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
    Note: Colocalizes with NEK6 in the centrosome.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Ensembl
    3. microtubule organizing center Source: UniProtKB-SubCell
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34322.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 579579Transcription factor RelBPRO_0000205173Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei37 – 371Phosphoserine2 Publications
    Modified residuei573 – 5731Phosphoserine2 Publications

    Post-translational modificationi

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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ01201.
    PaxDbiQ01201.
    PRIDEiQ01201.

    PTM databases

    PhosphoSiteiQ01201.

    Expressioni

    Inductioni

    Up-regulated by mitogens and NUPR1.1 Publication

    Gene expression databases

    ArrayExpressiQ01201.
    BgeeiQ01201.
    CleanExiHS_RELB.
    GenevestigatoriQ01201.

    Organism-specific databases

    HPAiCAB007753.
    HPA040506.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    COMMD1Q8N6682EBI-357837,EBI-1550112
    GSK3BP498414EBI-357837,EBI-373586
    NFKB1P198384EBI-357837,EBI-300010
    NFKB2Q006533EBI-357837,EBI-307326
    RELAQ042062EBI-357837,EBI-73886

    Protein-protein interaction databases

    BioGridi111903. 45 interactions.
    DIPiDIP-27531N.
    IntActiQ01201. 33 interactions.
    MINTiMINT-1131428.
    STRINGi9606.ENSP00000221452.

    Structurei

    3D structure databases

    ProteinModelPortaliQ01201.
    SMRiQ01201. Positions 123-400.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini125 – 440316RHDPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni40 – 6829Leucine-zipperAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi433 – 4386Nuclear 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.
    HOGENOMiHOG000148598.
    HOVERGENiHBG017021.
    InParanoidiQ01201.
    KOiK09253.
    OMAiDDGFAYD.
    OrthoDBiEOG7VHSWT.
    PhylomeDBiQ01201.
    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.

    Q01201-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRSGPASGP SVPTGRAMPS RRVARPPAAP ELGALGSPDL SSLSLAVSRS    50
    TDELEIIDEY IKENGFGLDG GQPGPGEGLP RLVSRGAASL STVTLGPVAP 100
    PATPPPWGCP LGRLVSPAPG PGPQPHLVIT EQPKQRGMRF RYECEGRSAG 150
    SILGESSTEA SKTLPAIELR DCGGLREVEV TACLVWKDWP HRVHPHSLVG 200
    KDCTDGICRV RLRPHVSPRH SFNNLGIQCV RKKEIEAAIE RKIQLGIDPY 250
    NAGSLKNHQE VDMNVVRICF QASYRDQQGQ MRRMDPVLSE PVYDKKSTNT 300
    SELRICRINK ESGPCTGGEE LYLLCDKVQK EDISVVFSRA SWEGRADFSQ 350
    ADVHRQIAIV FKTPPYEDLE IVEPVTVNVF LQRLTDGVCS EPLPFTYLPR 400
    DHDSYGVDKK RKRGMPDVLG ELNSSDPHGI ESKRRKKKPA ILDHFLPNHG 450
    SGPFLPPSAL LPDPDFFSGT VSLPGLEPPG GPDLLDDGFA YDPTAPTLFT 500
    MLDLLPPAPP HASAVVCSGG AGAVVGETPG PEPLTLDSYQ APGPGDGGTA 550
    SLVGSNMFPN HYREAAFGGG LLSPGPEAT 579
    Length:579
    Mass (Da):62,134
    Last modified:April 4, 2006 - v2
    Checksum:iC2C61C2C8640513E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti139 – 1391R → P in AAA36127. (PubMed:1577270)Curated
    Sequence conflicti411 – 4111R → A in AAA36127. (PubMed:1577270)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti396 – 3961T → M.
    Corresponds to variant rs2230682 [ dbSNP | Ensembl ].
    VAR_051782

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83221 mRNA. Translation: AAA36127.1.
    AF043463
    , 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.
    CCDSiCCDS46110.1.
    PIRiA42617.
    RefSeqiNP_006500.2. NM_006509.3.
    UniGeneiHs.654402.

    Genome annotation databases

    EnsembliENST00000221452; ENSP00000221452; ENSG00000104856.
    GeneIDi5971.
    KEGGihsa:5971.
    UCSCiuc021uvp.1. human.

    Polymorphism databases

    DMDMi92090634.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83221 mRNA. Translation: AAA36127.1 .
    AF043463
    , 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 .
    CCDSi CCDS46110.1.
    PIRi A42617.
    RefSeqi NP_006500.2. NM_006509.3.
    UniGenei Hs.654402.

    3D structure databases

    ProteinModelPortali Q01201.
    SMRi Q01201. Positions 123-400.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111903. 45 interactions.
    DIPi DIP-27531N.
    IntActi Q01201. 33 interactions.
    MINTi MINT-1131428.
    STRINGi 9606.ENSP00000221452.

    PTM databases

    PhosphoSitei Q01201.

    Polymorphism databases

    DMDMi 92090634.

    Proteomic databases

    MaxQBi Q01201.
    PaxDbi Q01201.
    PRIDEi Q01201.

    Protocols and materials databases

    DNASUi 5971.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000221452 ; ENSP00000221452 ; ENSG00000104856 .
    GeneIDi 5971.
    KEGGi hsa:5971.
    UCSCi uc021uvp.1. human.

    Organism-specific databases

    CTDi 5971.
    GeneCardsi GC19P045504.
    HGNCi HGNC:9956. RELB.
    HPAi CAB007753.
    HPA040506.
    MIMi 604758. gene.
    neXtProti NX_Q01201.
    PharmGKBi PA34322.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG119056.
    HOGENOMi HOG000148598.
    HOVERGENi HBG017021.
    InParanoidi Q01201.
    KOi K09253.
    OMAi DDGFAYD.
    OrthoDBi EOG7VHSWT.
    PhylomeDBi Q01201.
    TreeFami TF325632.

    Miscellaneous databases

    GeneWikii RELB.
    GenomeRNAii 5971.
    NextBioi 23245.
    PROi Q01201.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01201.
    Bgeei Q01201.
    CleanExi HS_RELB.
    Genevestigatori Q01201.

    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. "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. 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.

    Entry informationi

    Entry nameiRELB_HUMAN
    AccessioniPrimary (citable) accession number: Q01201
    Secondary accession number(s): Q6GTX7, Q9UEI7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: April 4, 2006
    Last modified: October 1, 2014
    This is version 145 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Caution

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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3