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Q04864

- REL_HUMAN

UniProt

Q04864 - REL_HUMAN

Protein

Proto-oncogene c-Rel

Gene

REL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Proto-oncogene that may play a role in differentiation and lymphopoiesis. 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. The NF-kappa-B heterodimer RELA/p65-c-Rel is a transcriptional activator.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. RNA polymerase II distal enhancer sequence-specific DNA binding Source: NTNU_SB
    3. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    4. sequence-specific DNA binding transcription factor activity Source: ProtInc

    GO - Biological processi

    1. cytokine production Source: Ensembl
    2. I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    3. negative regulation of neuron death Source: Ensembl
    4. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    5. positive regulation of interleukin-12 biosynthetic process Source: Ensembl
    6. positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_118656. Activation of NF-kappaB in B cells.
    SignaLinkiQ04864.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proto-oncogene c-Rel
    Gene namesi
    Name:REL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:9954. REL.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB-KW
    4. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA34321.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 619618Proto-oncogene c-RelPRO_0000205165Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei267 – 2671Phosphoserine; by PKASequence Analysis
    Modified residuei503 – 5031Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ04864.
    PaxDbiQ04864.
    PRIDEiQ04864.

    PTM databases

    PhosphoSiteiQ04864.

    Expressioni

    Gene expression databases

    ArrayExpressiQ04864.
    BgeeiQ04864.
    CleanExiHS_REL.
    GenevestigatoriQ04864.

    Organism-specific databases

    HPAiCAB004404.

    Interactioni

    Subunit structurei

    Component of the NF-kappa-B p65-c-Rel complex. Component of the NF-kappa-B p50-c-Rel complex. Component of the NF-kappa-B p52-c-Rel complex. Homodimer; component of the NF-kappa-B c-Rel-c-Rel complex By similarity. Interacts with NKIRAS1. Interacts with NFKBIB By similarity. Interacts with NFKBIE.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    COMMD1Q8N6683EBI-307352,EBI-1550112
    NFKB2Q006533EBI-307352,EBI-307326

    Protein-protein interaction databases

    BioGridi111898. 36 interactions.
    DIPiDIP-301N.
    IntActiQ04864. 19 interactions.
    MINTiMINT-1137552.
    STRINGi9606.ENSP00000295025.

    Structurei

    3D structure databases

    ProteinModelPortaliQ04864.
    SMRiQ04864. Positions 8-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 297290RHDPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi290 – 2956Nuclear localization signalSequence Analysis

    Sequence similaritiesi

    Contains 1 RHD (Rel-like) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG119056.
    HOGENOMiHOG000264257.
    HOVERGENiHBG017916.
    InParanoidiQ04864.
    KOiK09254.
    OMAiWEAKGIF.
    OrthoDBiEOG7VHSWT.
    PhylomeDBiQ04864.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q04864-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASGAYNPYI EIIEQPRQRG MRFRYKCEGR SAGSIPGEHS TDNNRTYPSI    50
    QIMNYYGKGK VRITLVTKND PYKPHPHDLV GKDCRDGYYE AEFGQERRPL 100
    FFQNLGIRCV KKKEVKEAII TRIKAGINPF NVPEKQLNDI EDCDLNVVRL 150
    CFQVFLPDEH GNLTTALPPV VSNPIYDNRA PNTAELRICR VNKNCGSVRG 200
    GDEIFLLCDK VQKDDIEVRF VLNDWEAKGI FSQADVHRQV AIVFKTPPYC 250
    KAITEPVTVK MQLRRPSDQE VSESMDFRYL PDEKDTYGNK AKKQKTTLLF 300
    QKLCQDHVET GFRHVDQDGL ELLTSGDPPT LASQSAGITV NFPERPRPGL 350
    LGSIGEGRYF KKEPNLFSHD AVVREMPTGV SSQAESYYPS PGPISSGLSH 400
    HASMAPLPSS SWSSVAHPTP RSGNTNPLSS FSTRTLPSNS QGIPPFLRIP 450
    VGNDLNASNA CIYNNADDIV GMEASSMPSA DLYGISDPNM LSNCSVNMMT 500
    TSSDSMGETD NPRLLSMNLE NPSCNSVLDP RDLRQLHQMS SSSMSAGANS 550
    NTTVFVSQSD AFEGSDFSCA DNSMINESGP SNSTNPNSHG FVQDSQYSGI 600
    GSMQNEQLSD SFPYEFFQV 619
    Length:619
    Mass (Da):68,520
    Last modified:June 1, 1994 - v1
    Checksum:i03E1033BDF7B1B30
    GO
    Isoform 2 (identifier: Q04864-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         308-339: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:587
    Mass (Da):65,225
    Checksum:iE312A59CF1D306A2
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei308 – 33932Missing in isoform 2. 1 PublicationVSP_055857Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75042 mRNA. Translation: CAA52954.1.
    DQ314888 Genomic DNA. Translation: ABC40747.1.
    AC010733 Genomic DNA. No translation available.
    BC117191 mRNA. Translation: AAI17192.1.
    BC143885 mRNA. Translation: AAI43886.1.
    M11595 Genomic DNA. Translation: AAA52073.1.
    CCDSiCCDS1864.1.
    PIRiA60646.
    RefSeqiNP_002899.1. NM_002908.3.
    UniGeneiHs.631886.
    Hs.633256.

    Genome annotation databases

    EnsembliENST00000295025; ENSP00000295025; ENSG00000162924. [Q04864-1]
    ENST00000394479; ENSP00000377989; ENSG00000162924. [Q04864-2]
    GeneIDi5966.
    KEGGihsa:5966.
    UCSCiuc002sam.1. human.

    Polymorphism databases

    DMDMi548720.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75042 mRNA. Translation: CAA52954.1 .
    DQ314888 Genomic DNA. Translation: ABC40747.1 .
    AC010733 Genomic DNA. No translation available.
    BC117191 mRNA. Translation: AAI17192.1 .
    BC143885 mRNA. Translation: AAI43886.1 .
    M11595 Genomic DNA. Translation: AAA52073.1 .
    CCDSi CCDS1864.1.
    PIRi A60646.
    RefSeqi NP_002899.1. NM_002908.3.
    UniGenei Hs.631886.
    Hs.633256.

    3D structure databases

    ProteinModelPortali Q04864.
    SMRi Q04864. Positions 8-282.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111898. 36 interactions.
    DIPi DIP-301N.
    IntActi Q04864. 19 interactions.
    MINTi MINT-1137552.
    STRINGi 9606.ENSP00000295025.

    PTM databases

    PhosphoSitei Q04864.

    Polymorphism databases

    DMDMi 548720.

    Proteomic databases

    MaxQBi Q04864.
    PaxDbi Q04864.
    PRIDEi Q04864.

    Protocols and materials databases

    DNASUi 5966.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295025 ; ENSP00000295025 ; ENSG00000162924 . [Q04864-1 ]
    ENST00000394479 ; ENSP00000377989 ; ENSG00000162924 . [Q04864-2 ]
    GeneIDi 5966.
    KEGGi hsa:5966.
    UCSCi uc002sam.1. human.

    Organism-specific databases

    CTDi 5966.
    GeneCardsi GC02P061108.
    HGNCi HGNC:9954. REL.
    HPAi CAB004404.
    MIMi 164910. gene.
    neXtProti NX_Q04864.
    PharmGKBi PA34321.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG119056.
    HOGENOMi HOG000264257.
    HOVERGENi HBG017916.
    InParanoidi Q04864.
    KOi K09254.
    OMAi WEAKGIF.
    OrthoDBi EOG7VHSWT.
    PhylomeDBi Q04864.
    TreeFami TF325632.

    Enzyme and pathway databases

    Reactomei REACT_118656. Activation of NF-kappaB in B cells.
    SignaLinki Q04864.

    Miscellaneous databases

    GeneWikii REL.
    GenomeRNAii 5966.
    NextBioi 23226.
    PROi Q04864.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q04864.
    Bgeei Q04864.
    CleanExi HS_REL.
    Genevestigatori Q04864.

    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. "A human rel proto-oncogene cDNA containing an Alu fragment as a potential coding exon."
      Brownell E., Mittereder N., Rice N.R.
      Oncogene 4:935-942(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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] (ISOFORM 2).
      Tissue: Colon.
    5. "Genetic characterization of human c-rel sequences."
      Brownell E., O'Brien S.J., Nash W.G., Rice N.R.
      Mol. Cell. Biol. 5:2826-2831(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-284.
    6. "A novel complex between the p65 subunit of NF-kappa B and c-Rel binds to a DNA element involved in the phorbol ester induction of the human urokinase gene."
      Hansen S.K., Nerlov C., Zabel U., Verde P., Johnsen M., Baeuerle P.A., Blasi F.
      EMBO J. 11:205-213(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX.
    7. "Activation of multiple NF-kappa B/Rel DNA-binding complexes by tumor necrosis factor."
      Beg A.A., Baldwin A.S. Jr.
      Oncogene 9:1487-1492(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NF-KAPPA-B P50-C-REL COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P52-C-REL COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX.
    8. "Regulation of intercellular adhesion molecule-1 gene by tumor necrosis factor-alpha is mediated by the nuclear factor-kappaB heterodimers p65/p65 and p65/c-Rel in the absence of p50."
      Aoudjit F., Brochu N., Belanger B., Stratowa C., Hiscott J., Audette M.
      Cell Growth Differ. 8:335-342(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX.
    9. "A new member of the IkappaB protein family, IkappaB epsilon, inhibits RelA (p65)-mediated NF-kappaB transcription."
      Li Z., Nabel G.J.
      Mol. Cell. Biol. 17:6184-6190(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFKBIE.
    10. "Tumor necrosis factor-alpha activation of NF-kappa B requires the phosphorylation of Ser-471 in the transactivation domain of c-Rel."
      Martin A.G., Fresno M.
      J. Biol. Chem. 275:24383-24391(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-503.
    11. "Leishmania major amastigotes induce p50/c-Rel NF-kappa B transcription factor in human macrophages: involvement in cytokine synthesis."
      Guizani-Tabbane L., Ben-Aissa K., Belghith M., Sassi A., Dellagi K.
      Infect. Immun. 72:2582-2589(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NF-KAPPA-B P50-C-REL COMPLEX.
    12. "Inhibition of NF-kappaB activity by IkappaBbeta in association with kappaB-Ras."
      Chen Y., Vallee S., Wu J., Vu D., Sondek J., Ghosh G.
      Mol. Cell. Biol. 24:3048-3056(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NKIRAS1.
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiREL_HUMAN
    AccessioniPrimary (citable) accession number: Q04864
    Secondary accession number(s): Q17RU2, Q2PNZ7, Q6LDY0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 136 of the entry and version 1 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3