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Q04207

- TF65_MOUSE

UniProt

Q04207 - TF65_MOUSE

Protein

Transcription factor p65

Gene

Rela

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes 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 and the heterodimeric p65-p50 complex appears to be most abundant one. 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 p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression By similarity. The inhibitory effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1.By similarity2 Publications

    GO - Molecular functioni

    1. ankyrin repeat binding Source: UniProtKB
    2. chromatin binding Source: UniProtKB
    3. DNA binding Source: MGI
    4. enzyme binding Source: UniProtKB
    5. phosphate ion binding Source: Ensembl
    6. protein binding Source: UniProtKB
    7. protein kinase binding Source: UniProtKB
    8. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: UniProtKB
    9. sequence-specific DNA binding Source: MGI
    10. sequence-specific DNA binding transcription factor activity Source: MGI
    11. transcription regulatory region DNA binding Source: Ensembl

    GO - Biological processi

    1. acetaldehyde metabolic process Source: Ensembl
    2. aging Source: Ensembl
    3. cellular response to hydrogen peroxide Source: UniProtKB
    4. cellular response to interleukin-1 Source: Ensembl
    5. cellular response to lipopolysaccharide Source: UniProtKB
    6. cellular response to tumor necrosis factor Source: UniProtKB
    7. cytokine-mediated signaling pathway Source: Ensembl
    8. defense response Source: MGI
    9. hair follicle development Source: MGI
    10. inflammatory response Source: Ensembl
    11. liver development Source: UniProtKB
    12. negative regulation of apoptotic process Source: UniProtKB
    13. negative regulation of extrinsic apoptotic signaling pathway Source: MGI
    14. negative regulation of insulin receptor signaling pathway Source: Ensembl
    15. negative regulation of protein catabolic process Source: MGI
    16. negative regulation of transcription, DNA-templated Source: Ensembl
    17. nucleotide-binding oligomerization domain containing 2 signaling pathway Source: Ensembl
    18. organ morphogenesis Source: MGI
    19. positive regulation of cell proliferation Source: UniProtKB
    20. positive regulation of chondrocyte differentiation Source: Ensembl
    21. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    22. positive regulation of interleukin-12 biosynthetic process Source: MGI
    23. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    24. positive regulation of Schwann cell differentiation Source: Ensembl
    25. positive regulation of transcription, DNA-templated Source: UniProtKB
    26. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    27. regulation of inflammatory response Source: UniProtKB
    28. response to amino acid Source: Ensembl
    29. response to bacterium Source: MGI
    30. response to cAMP Source: Ensembl
    31. response to cobalamin Source: Ensembl
    32. response to drug Source: Ensembl
    33. response to insulin Source: Ensembl
    34. response to mechanical stimulus Source: Ensembl
    35. response to morphine Source: Ensembl
    36. response to muramyl dipeptide Source: MGI
    37. response to progesterone Source: Ensembl
    38. response to UV-B Source: Ensembl
    39. transcription from RNA polymerase II promoter Source: GOC

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_198700. Interleukin-1 processing.
    REACT_199121. Activation of NF-kappaB in B cells.
    REACT_202898. TRAF6 mediated NF-kB activation.
    REACT_205561. FCERI mediated NF-kB activation.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_218614. Regulated proteolysis of p75NTR.
    REACT_218887. NF-kB is activated and signals survival.
    REACT_219800. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_222971. RIP-mediated NFkB activation via ZBP1.
    REACT_225145. Downstream TCR signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor p65
    Alternative name(s):
    Nuclear factor NF-kappa-B p65 subunit
    Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3
    Gene namesi
    Name:Rela
    Synonyms:Nfkb3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:103290. Rela.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Colocalized with DDX1 in the nucleus upon TNF-alpha induction By similarity. Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B). Colocalizes with GFI1 in the nucleus after lipopolysaccharide (LPS) stimulation.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: MGI
    3. NF-kappaB complex Source: UniProtKB
    4. nucleus Source: UniProtKB
    5. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi38 – 381C → S: Abolishes sulfhydration and impairs interaction with RPS3. 1 Publication
    Mutagenesisi281 – 2811S → A or E: Abolishes DNA-binding and transcriptional activity. 1 Publication
    Mutagenesisi310 – 3101K → R: Abolishes monomethylation by SETD6 and interaction with EHMT1. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 549549Transcription factor p65PRO_0000205170Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Cross-linki37 – 37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)By similarity
    Modified residuei38 – 381Cysteine persulfide; alternate1 Publication
    Modified residuei38 – 381S-nitrosocysteine; alternate1 Publication
    Modified residuei122 – 1221N6-acetyllysine; by PCAF and EP300; alternateBy similarity
    Cross-linki122 – 122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternateBy similarity
    Modified residuei123 – 1231N6-acetyllysine; by PCAF and EP300; alternateBy similarity
    Cross-linki123 – 123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternateBy similarity
    Modified residuei218 – 2181N6-acetyllysineBy similarity
    Modified residuei221 – 2211N6-acetyllysineBy similarity
    Modified residuei254 – 2541PhosphothreonineBy similarity
    Modified residuei276 – 2761Phosphoserine; by RPS6KA4 and RPS6KA5By similarity
    Modified residuei310 – 3101N6-acetyllysine; alternate1 Publication
    Modified residuei310 – 3101N6-methyllysine; by SETD6; alternate1 Publication
    Modified residuei311 – 3111Phosphoserine; by PKC/PRKCZ2 Publications
    Modified residuei433 – 4331PhosphothreonineBy similarity
    Modified residuei467 – 4671Phosphoserine; by IKKB and IKKEBy similarity
    Modified residuei504 – 5041Phosphothreonine; by CHEK1By similarity
    Modified residuei527 – 5271Phosphoserine; by CK2By similarity
    Modified residuei534 – 5341Phosphoserine; by IKKBBy similarity

    Post-translational modificationi

    Ubiquitinated, leading to its proteasomal degradation. Degradation is required for termination of NF-kappa-B response By similarity.By similarity
    Monomethylated at Lys-310 by SETD6. Monomethylation at Lys-310 is recognized by the ANK repeats of EHMT1 and promotes the formation of repressed chromatin at target genes, leading to down-regulation of NF-kappa-B transcription factor activity. Phosphorylation at Ser-311 disrupts the interaction with EHMT1 without preventing monomethylation at Lys-310 and relieves the repression of target genes.2 Publications
    Phosphorylation on Ser-534 stimulates acetylation on Lys-310 and interaction with CBP; the phosphorylated and acetylated forms show enhanced transcriptional activity By similarity. Phosphorylation at Ser-311 disrupts the interaction with EHMT1 and promotes transcription factor activity. Phosphorylation at Ser-276 by RPS6KA4 and RPS6KA5 promotes its transactivation and transcriptional activities.By similarity3 Publications
    Reversibly acetylated; the acetylation seems to be mediated by CBP, the deacetylation by HDAC3 and SIRT2. Acetylation at Lys-122 enhances DNA binding and impairs association with NFKBIA. Acetylation at Lys-310 is required for full transcriptional activity in the absence of effects on DNA binding and NFKBIA association. Acetylation at Lys-310 promotes interaction with BRD4. Acetylation can also lower DNA-binding and results in nuclear export. Interaction with BRMS1 promotes deacetylation of Lys-310. Lys-310 is deacetylated by SIRT2 By similarity.By similarity
    S-nitrosylation of Cys-38 inactivates the enzyme activity.1 Publication
    Sulfhydration at Cys-38 mediates the anti-apoptotic activity by promoting the interaction with RPS3 and activating the transcription factor activity.
    Sumoylation by PIAS3 negatively regulates DNA-bound activated NF-kappa-B.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

    Proteomic databases

    MaxQBiQ04207.
    PaxDbiQ04207.
    PRIDEiQ04207.

    PTM databases

    PhosphoSiteiQ04207.

    Expressioni

    Gene expression databases

    ArrayExpressiQ04207.
    BgeeiQ04207.
    GenevestigatoriQ04207.

    Interactioni

    Subunit structurei

    Component of the NF-kappa-B p65-p50 complex. Component of the NF-kappa-B p65-c-Rel complex. Homodimer; component of the NF-kappa-B p65-p65 complex. Component of the NF-kappa-B p65-p52 complex. May interact with ETHE1. Binds AES and TLE1. Interacts with TP53BP2. Binds to and is phosphorylated by the activated form of either RPS6KA4 or RPS6KA5. Interacts with ING4 and this interaction may be indirect. Interacts with CARM1, USP48 and UNC5CL. Interacts with IRAK1BP1. Interacts with NFKBIA. Interacts with GSK3B. Interacts with NFKBIB. Interacts with NFKBIE. Interacts with NFKBIZ. Part of a 70-90 kDa complex at least consisting of CHUK, IKBKB, NFKBIA, RELA, IKBKAP and MAP3K14. Interacts with HDAC3; HDAC3 mediates the deacetylation of RELA. Interacts with HDAC1; the interaction requires non-phosphorylated RELA. Interacts with CBP; the interaction requires phosphorylated RELA. Interacts (phosphorylated at 'Thr-254') with PIN1; the interaction inhibits p65 binding to NFKBIA. Interacts with SOCS1. Interacts with MTDH and PHF11. Interacts with NFKBID. Interacts with ARRB2. Interacts with NFKBIA (when phosphorylated), the interaction is direct; phosphorylated NFKBIA is associated with a SCF(BTRC)-like complex lacking CUL1. Interacts with RNF25. Interacts (via C-terminus) with DDX1 By similarity. Interacts with UFL1 and COMMD1 By similarity. Interacts with BRMS1; this promotes deacetylation of 'Lys-310'. Interacts (when acetylated at Lys-310) with BRD4; leading to activation of the NF-kappa-B pathway By similarity. Interacts with EHMT1 (via ANK repeats). Interacts with NOTCH2. Directly interacts with MEN1; this interaction represses NFKB-mediated transactivation By similarity. Interacts with AKIP1, which promotes the phosphorylation and nuclear retention of RELA By similarity. Interacts (via the RHD) with GFI1; the interaction, after bacterial lipopolysaccharide (LPS) stimulation, inhibits the transcriptional activity by interfering with the DNA-binding activity to target gene promoter DNA. Interacts with MEFV By similarity. Interacts with CLOCK.By similarity9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ctnnb1Q022485EBI-644400,EBI-397872
    EHMT1Q9H9B15EBI-644400,EBI-766087From a different organism.
    Hdac1O091062EBI-644400,EBI-301912
    Nfkb1P257995EBI-644400,EBI-643958
    NfkbiaQ9Z1E37EBI-644400,EBI-644427
    NfkbibQ607788EBI-644400,EBI-644469
    Nr0b2Q622273EBI-644400,EBI-4310440
    Nr4a2Q062192EBI-644400,EBI-2337255
    SETD6Q8TBK24EBI-644400,EBI-3863032From a different organism.
    SETD7Q8WTS62EBI-644400,EBI-1268586From a different organism.
    UbcP629912EBI-644400,EBI-413074

    Protein-protein interaction databases

    BioGridi202853. 31 interactions.
    DIPiDIP-6219N.
    IntActiQ04207. 23 interactions.
    MINTiMINT-236104.

    Structurei

    Secondary structure

    1
    549
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi20 – 256
    Beta strandi30 – 323
    Turni37 – 393
    Beta strandi48 – 503
    Beta strandi53 – 553
    Beta strandi60 – 656
    Beta strandi71 – 777
    Beta strandi79 – 824
    Beta strandi87 – 926
    Beta strandi99 – 1035
    Beta strandi109 – 1124
    Beta strandi117 – 1204
    Helixi123 – 1253
    Helixi126 – 13510
    Turni145 – 1484
    Beta strandi156 – 16611
    Beta strandi168 – 1747
    Beta strandi178 – 1847
    Beta strandi186 – 1883
    Turni189 – 1913
    Beta strandi196 – 2005
    Beta strandi202 – 2054
    Beta strandi211 – 2177
    Helixi221 – 2233
    Beta strandi225 – 2306
    Beta strandi233 – 2364
    Helixi241 – 2433
    Beta strandi248 – 2536
    Beta strandi266 – 2749
    Turni275 – 2784
    Beta strandi284 – 2896
    Helixi294 – 30411
    Helixi306 – 31510
    Helixi433 – 4397
    Beta strandi444 – 4474
    Turni450 – 4534
    Helixi459 – 4613
    Helixi465 – 4673
    Helixi471 – 4777
    Beta strandi480 – 4845

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BFTX-ray2.00A/B191-291[»]
    1IKNX-ray2.30A19-304[»]
    1K3ZX-ray2.50A/B191-326[»]
    1LE5X-ray2.75A/E20-291[»]
    1LE9X-ray3.00A/E20-291[»]
    1LEIX-ray2.70A20-291[»]
    1MY5X-ray1.80A/B191-304[»]
    1MY7X-ray1.49A/B191-304[»]
    1OY3X-ray2.05B/C191-326[»]
    1RAMX-ray2.70A/B19-291[»]
    1VKXX-ray2.90A20-291[»]
    2I9TX-ray2.80A19-291[»]
    2LWWNMR-B425-490[»]
    2RAMX-ray2.40A/B19-291[»]
    DisProtiDP00129.
    ProteinModelPortaliQ04207.
    SMRiQ04207. Positions 20-325, 425-490.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04207.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 306288RHDPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi301 – 3044Nuclear localization signalSequence Analysis

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG119056.
    HOGENOMiHOG000230474.
    HOVERGENiHBG017916.
    InParanoidiQ04207.
    KOiK04735.
    OMAiEFSPMVF.
    OrthoDBiEOG7VHSWT.
    PhylomeDBiQ04207.
    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.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform p65 (identifier: Q04207-1) [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

    MDDLFPLIFP SEPAQASGPY VEIIEQPKQR GMRFRYKCEG RSAGSIPGER    50
    STDTTKTHPT IKINGYTGPG TVRISLVTKD PPHRPHPHEL VGKDCRDGYY 100
    EADLCPDRSI HSFQNLGIQC VKKRDLEQAI SQRIQTNNNP FHVPIEEQRG 150
    DYDLNAVRLC FQVTVRDPAG RPLLLTPVLS HPIFDNRAPN TAELKICRVN 200
    RNSGSCLGGD EIFLLCDKVQ KEDIEVYFTG PGWEARGSFS QADVHRQVAI 250
    VFRTPPYADP SLQAPVRVSM QLRRPSDREL SEPMEFQYLP DTDDRHRIEE 300
    KRKRTYETFK SIMKKSPFNG PTEPRPPTRR IAVPTRNSTS VPKPAPQPYT 350
    FPASLSTINF DEFSPMLLPS GQISNQALAL APSSAPVLAQ TMVPSSAMVP 400
    LAQPPAPAPV LTPGPPQSLS APVPKSTQAG EGTLSEALLH LQFDADEDLG 450
    ALLGNSTDPG VFTDLASVDN SEFQQLLNQG VSMSHSTAEP MLMEYPEAIT 500
    RLVTGSQRPP DPAPTPLGTS GLPNGLSGDE DFSSIADMDF SALLSQISS 549
    Length:549
    Mass (Da):60,212
    Last modified:October 1, 1993 - v1
    Checksum:iBDF1673D2FE398B9
    GO
    Isoform p65 delta (identifier: Q04207-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         222-231: Missing.

    Show »
    Length:539
    Mass (Da):59,061
    Checksum:iF834FD0302D351BD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281K → N in AAB00795. (PubMed:8918242)Curated
    Sequence conflicti61 – 611I → IQKD in AAB00795. (PubMed:8918242)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei222 – 23110Missing in isoform p65 delta. CuratedVSP_005589

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M61909 mRNA. Translation: AAA39811.1.
    BC003818 mRNA. Translation: AAH03818.1.
    L77155 Genomic DNA. Translation: AAB00795.1.
    Z22952 Genomic DNA. Translation: CAA80528.1.
    CCDSiCCDS29473.1. [Q04207-1]
    PIRiA37932.
    PC4233.
    S48113.
    RefSeqiNP_033071.1. NM_009045.4. [Q04207-1]
    UniGeneiMm.249966.

    Genome annotation databases

    EnsembliENSMUST00000025867; ENSMUSP00000025867; ENSMUSG00000024927. [Q04207-1]
    GeneIDi19697.
    KEGGimmu:19697.
    UCSCiuc008gee.1. mouse. [Q04207-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M61909 mRNA. Translation: AAA39811.1 .
    BC003818 mRNA. Translation: AAH03818.1 .
    L77155 Genomic DNA. Translation: AAB00795.1 .
    Z22952 Genomic DNA. Translation: CAA80528.1 .
    CCDSi CCDS29473.1. [Q04207-1 ]
    PIRi A37932.
    PC4233.
    S48113.
    RefSeqi NP_033071.1. NM_009045.4. [Q04207-1 ]
    UniGenei Mm.249966.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BFT X-ray 2.00 A/B 191-291 [» ]
    1IKN X-ray 2.30 A 19-304 [» ]
    1K3Z X-ray 2.50 A/B 191-326 [» ]
    1LE5 X-ray 2.75 A/E 20-291 [» ]
    1LE9 X-ray 3.00 A/E 20-291 [» ]
    1LEI X-ray 2.70 A 20-291 [» ]
    1MY5 X-ray 1.80 A/B 191-304 [» ]
    1MY7 X-ray 1.49 A/B 191-304 [» ]
    1OY3 X-ray 2.05 B/C 191-326 [» ]
    1RAM X-ray 2.70 A/B 19-291 [» ]
    1VKX X-ray 2.90 A 20-291 [» ]
    2I9T X-ray 2.80 A 19-291 [» ]
    2LWW NMR - B 425-490 [» ]
    2RAM X-ray 2.40 A/B 19-291 [» ]
    DisProti DP00129.
    ProteinModelPortali Q04207.
    SMRi Q04207. Positions 20-325, 425-490.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202853. 31 interactions.
    DIPi DIP-6219N.
    IntActi Q04207. 23 interactions.
    MINTi MINT-236104.

    Chemistry

    ChEMBLi CHEMBL5902.

    PTM databases

    PhosphoSitei Q04207.

    Proteomic databases

    MaxQBi Q04207.
    PaxDbi Q04207.
    PRIDEi Q04207.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025867 ; ENSMUSP00000025867 ; ENSMUSG00000024927 . [Q04207-1 ]
    GeneIDi 19697.
    KEGGi mmu:19697.
    UCSCi uc008gee.1. mouse. [Q04207-1 ]

    Organism-specific databases

    CTDi 5970.
    MGIi MGI:103290. Rela.

    Phylogenomic databases

    eggNOGi NOG119056.
    HOGENOMi HOG000230474.
    HOVERGENi HBG017916.
    InParanoidi Q04207.
    KOi K04735.
    OMAi EFSPMVF.
    OrthoDBi EOG7VHSWT.
    PhylomeDBi Q04207.
    TreeFami TF325632.

    Enzyme and pathway databases

    Reactomei REACT_198700. Interleukin-1 processing.
    REACT_199121. Activation of NF-kappaB in B cells.
    REACT_202898. TRAF6 mediated NF-kB activation.
    REACT_205561. FCERI mediated NF-kB activation.
    REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
    REACT_218614. Regulated proteolysis of p75NTR.
    REACT_218887. NF-kB is activated and signals survival.
    REACT_219800. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_222971. RIP-mediated NFkB activation via ZBP1.
    REACT_225145. Downstream TCR signaling.

    Miscellaneous databases

    ChiTaRSi RELA. mouse.
    EvolutionaryTracei Q04207.
    NextBioi 297048.
    PROi Q04207.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q04207.
    Bgeei Q04207.
    Genevestigatori Q04207.

    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. "DNA binding and I kappa B inhibition of the cloned p65 subunit of NF-kappa B, a rel-related polypeptide."
      Nolan G.P., Ghosh S., Liou H.C., Tempst P., Baltimore D.
      Cell 64:961-969(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P65).
    2. "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 P65).
      Strain: C57BL/6J.
      Tissue: Mammary gland.
    3. "Cloning of the murine relA (p65 NF-kappa B) gene and comparison to the human gene reveals a distinct first intron."
      Linker R.A., Baeuerle P.A., Kaltschmidt C.
      Gene 176:119-124(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
      Strain: BALB/c.
    4. "Genomic organization of the gene encoding the p65 subunit of NF-kappa B: multiple variants of the p65 protein may be generated by alternative splicing."
      Deloukas P., van Loon A.P.G.M.
      Hum. Mol. Genet. 2:1895-1900(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 188-252, ALTERNATIVE SPLICING.
      Strain: BALB/c.
    5. "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.
    6. "Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP."
      Spencer E., Jiang J., Chen Z.J.
      Genes Dev. 13:284-294(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFKBIA.
    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. "Essential role of RelA Ser311 phosphorylation by zetaPKC in NF-kappaB transcriptional activation."
      Duran A., Diaz-Meco M.T., Moscat J.
      EMBO J. 22:3910-3918(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-311.
    9. "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: MUTAGENESIS OF SER-281.
    10. "A defect in nucleosome remodeling prevents IL-12(p35) gene transcription in neonatal dendritic cells."
      Goriely S., Van Lint C., Dadkhah R., Libin M., De Wit D., Demonte D., Willems F., Goldman M.
      J. Exp. Med. 199:1011-1016(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P65-P65 COMPLEX.
    11. "Tumor necrosis factor alpha induction of NF-kappaB requires the novel coactivator SIMPL."
      Kwon H.-J., Breese E.H., Vig-Varga E., Luo Y., Lee Y., Goebl M.G., Harrington M.A.
      Mol. Cell. Biol. 24:9317-9326(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IRAK1BP1.
    12. "Arginine methyltransferase CARM1 is a promoter-specific regulator of NF-kappaB-dependent gene expression."
      Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C., Imhof R., Bedford M.T., Natoli G., Hottiger M.O.
      EMBO J. 24:85-96(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CARM1.
    13. "The association of Notch2 and NF-kappaB accelerates RANKL-induced osteoclastogenesis."
      Fukushima H., Nakao A., Okamoto F., Shin M., Kajiya H., Sakano S., Bigas A., Jimi E., Okabe K.
      Mol. Cell. Biol. 28:6402-6412(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NOTCH2.
    14. "Lysine methylation of the NF-kappaB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-kappaB signaling."
      Levy D., Kuo A.J., Chang Y., Schaefer U., Kitson C., Cheung P., Espejo A., Zee B.M., Liu C.L., Tangsombatvisit S., Tennen R.I., Kuo A.Y., Tanjing S., Cheung R., Chua K.F., Utz P.J., Shi X., Prinjha R.K.
      , Lee K., Garcia B.A., Bedford M.T., Tarakhovsky A., Cheng X., Gozani O.
      Nat. Immunol. 12:29-36(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, METHYLATION AT LYS-310, PHOSPHORYLATION AT SER-311, INTERACTION WITH EHMT1, MUTAGENESIS OF LYS-310.
    15. "Hydrogen sulfide-linked sulfhydration of NF-kappaB mediates its antiapoptotic actions."
      Sen N., Paul B.D., Gadalla M.M., Mustafa A.K., Sen T., Xu R., Kim S., Snyder S.H.
      Mol. Cell 45:13-24(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SULFHYDRATION AT CYS-38, S-NITROSYLATION AT CYS-38, MUTAGENESIS OF CYS-38.
    16. Cited for: INTERACTION WITH CLOCK.
    17. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    18. "The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation."
      Huxford T., Huang D.B., Malek S., Ghosh G.
      Cell 95:759-770(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 19-291.
    19. "A novel DNA recognition mode by the NF-kappa B p65 homodimer."
      Chen Y.Q., Ghosh S., Ghosh G.
      Nat. Struct. Biol. 5:67-73(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 19-291.
    20. "Crystal structure of p50/p65 heterodimer of transcription factor NF-kappaB bound to DNA."
      Chen F.E., Huang D.B., Chen Y.Q., Ghosh G.
      Nature 391:410-413(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).

    Entry informationi

    Entry nameiTF65_MOUSE
    AccessioniPrimary (citable) accession number: Q04207
    Secondary accession number(s): Q62025
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 162 of the entry and version 1 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