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P15307

- REL_MOUSE

UniProt

P15307 - REL_MOUSE

Protein

Proto-oncogene c-Rel

Gene

Rel

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (01 Oct 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 By similarity.By similarity

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: MGI
    3. sequence-specific DNA binding transcription factor activity Source: MGI

    GO - Biological processi

    1. cytokine production Source: MGI
    2. positive regulation of interleukin-12 biosynthetic process Source: MGI
    3. positive regulation of transcription, DNA-templated Source: MGI
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proto-oncogene c-Rel
    Gene namesi
    Name:Rel
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:97897. Rel.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 587586Proto-oncogene c-RelPRO_0000205166Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei267 – 2671Phosphoserine; by PKASequence Analysis

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP15307.
    PRIDEiP15307.

    PTM databases

    PhosphoSiteiP15307.

    Expressioni

    Gene expression databases

    CleanExiMM_REL.
    GenevestigatoriP15307.

    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. Interacts with NKIRAS1. Interacts with NFKBIB. Interacts with NFKBIE By similarity.By similarity

    Protein-protein interaction databases

    DIPiDIP-59241N.
    IntActiP15307. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP15307.
    SMRiP15307. Positions 8-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni403 – 46866Transriptional transactivatorAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi291 – 2966Nuclear localization signalSequence Analysis

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG119056.
    HOVERGENiHBG017916.
    InParanoidiP15307.

    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.

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

    P15307-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASSGYNPYV EIIEQPRQRG MRFRYKCEGR SAGSIPGERS TDNNRTYPSV    50
    QIMNYYGKGK IRITLVTKND PYKPHPHDLV GKDCRDGYYE AEFGPERRPL 100
    FFQNLGIRCV KKKEVKGAII LRISAGINPF NVGEQQLLDI EDCDLNVVRC 150
    VFMFFLPDED GNFTTALPPI VSNPIYDNRA PNTAELRICR VNKNCGSVRG 200
    GDEIFLLCDK VQKDDIEVRF VLNDWEARGV FSQADVHRQV AIVFKTPPYC 250
    KAILEPVTVK MQLRRPSDQE VSESMDFRYL PDEKDAYGNK SKKQKTTLIF 300
    QKLLQDCGHF TEKPRTAPLG STGEGRFIKK ESNLFSHGTV LPEMPRSSGV 350
    PGQAEPYYSS CGSISSGLPH HPPAIPSVAH QPTSWPPVTH PTSHPVSTNT 400
    LSTFSAGTLS SNSQGILPFL EGPGVSDLSA SNSCLYNPDD LARMETPSMS 450
    PTDLYSISDV NMLSTRPLSV MAPSTDGMGD TDNPRLVSIN LENPSCNARL 500
    GPRDLRQLHQ MSPASLSAGT SSSSVFVSQS DAFDRSNFSC VDNGLMNEPG 550
    LSDDANNPTF VQSSHYSVNT LQSEQLSDPF TYGFFKI 587
    Length:587
    Mass (Da):64,960
    Last modified:October 1, 1994 - v2
    Checksum:i98FC237B6D140416
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti117 – 1171G → E(PubMed:2204816)Curated
    Sequence conflicti133 – 1331G → P(PubMed:2204816)Curated
    Sequence conflicti150 – 1545CVFMF → LCFQV(PubMed:2204816)Curated
    Sequence conflicti160 – 1601D → H(PubMed:2204816)Curated
    Sequence conflicti567 – 5671S → SS(PubMed:2204816)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15842 mRNA. Translation: CAA33843.1. Sequence problems.
    X60271 mRNA. Translation: CAA42817.1.
    PIRiA60367.
    UniGeneiMm.4869.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15842 mRNA. Translation: CAA33843.1 . Sequence problems.
    X60271 mRNA. Translation: CAA42817.1 .
    PIRi A60367.
    UniGenei Mm.4869.

    3D structure databases

    ProteinModelPortali P15307.
    SMRi P15307. Positions 8-282.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59241N.
    IntActi P15307. 2 interactions.

    PTM databases

    PhosphoSitei P15307.

    Proteomic databases

    PaxDbi P15307.
    PRIDEi P15307.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:97897. Rel.

    Phylogenomic databases

    eggNOGi NOG119056.
    HOVERGENi HBG017916.
    InParanoidi P15307.

    Miscellaneous databases

    PROi P15307.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_REL.
    Genevestigatori P15307.

    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. "Structure of a mammalian c-rel protein deduced from the nucleotide sequence of murine cDNA clones."
      Grumont R.J., Gerondakis S.
      Oncogene Res. 4:1-8(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Spleen.
    2. "The murine c-rel proto-oncogene encodes two mRNAs the expression of which is modulated by lymphoid stimuli."
      Grumont R.J., Gerondakis S.
      Oncogene Res. 5:245-254(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    3. "The mouse c-rel protein has an N-terminal regulatory domain and a C-terminal transcriptional transactivation domain."
      Bull P., Morley K.L., Hoekstra M.F., Hunter T., Verma I.M.
      Mol. Cell. Biol. 10:5473-5485(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Role of unphosphorylated, newly synthesized IkappaB beta in persistent activation of NF-kappaB."
      Suyang H., Phillips R.J., Douglas I., Ghosh S.
      Mol. Cell. Biol. 16:5444-5449(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFKBIB.

    Entry informationi

    Entry nameiREL_MOUSE
    AccessioniPrimary (citable) accession number: P15307
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 113 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

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3