Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q04206

- TF65_HUMAN

UniProt

Q04206 - TF65_HUMAN

Protein

Transcription factor p65

Gene

RELA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 177 (01 Oct 2014)
      Sequence version 2 (26 Apr 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. 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 DDX1.7 Publications

    GO - Molecular functioni

    1. activating transcription factor binding Source: BHF-UCL
    2. chromatin binding Source: UniProtKB
    3. DNA binding Source: UniProtKB
    4. identical protein binding Source: UniProtKB
    5. NF-kappaB binding Source: UniProtKB
    6. phosphate ion binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. protein kinase binding Source: UniProtKB
    9. protein N-terminus binding Source: UniProtKB
    10. repressing transcription factor binding Source: BHF-UCL
    11. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    12. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB
    13. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    14. RNA polymerase II distal enhancer sequence-specific DNA binding Source: NTNU_SB
    15. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: UniProtKB
    16. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    17. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    18. transcription factor binding Source: UniProtKB
    19. transcription regulatory region DNA binding Source: UniProtKB
    20. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. acetaldehyde metabolic process Source: Ensembl
    2. aging Source: Ensembl
    3. cellular defense response Source: UniProtKB
    4. cellular response to hydrogen peroxide Source: UniProtKB
    5. cellular response to interleukin-1 Source: UniProtKB
    6. cellular response to interleukin-6 Source: BHF-UCL
    7. cellular response to lipopolysaccharide Source: Ensembl
    8. cellular response to nicotine Source: BHF-UCL
    9. cellular response to peptide hormone stimulus Source: BHF-UCL
    10. cellular response to tumor necrosis factor Source: UniProtKB
    11. cytokine-mediated signaling pathway Source: UniProtKB
    12. defense response to virus Source: UniProtKB
    13. Fc-epsilon receptor signaling pathway Source: Reactome
    14. hair follicle development Source: Ensembl
    15. inflammatory response Source: UniProtKB
    16. innate immune response Source: Reactome
    17. liver development Source: Ensembl
    18. membrane protein intracellular domain proteolysis Source: Reactome
    19. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    20. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    21. negative regulation of apoptotic process Source: UniProtKB
    22. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
    23. negative regulation of insulin receptor signaling pathway Source: Ensembl
    24. negative regulation of protein catabolic process Source: Ensembl
    25. negative regulation of transcription, DNA-templated Source: UniProtKB
    26. negative regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
    27. neurotrophin TRK receptor signaling pathway Source: Reactome
    28. nucleotide-binding oligomerization domain containing 2 signaling pathway Source: MGI
    29. organ morphogenesis Source: Ensembl
    30. positive regulation of cell proliferation Source: UniProtKB
    31. positive regulation of chondrocyte differentiation Source: Ensembl
    32. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    33. positive regulation of interleukin-12 biosynthetic process Source: Ensembl
    34. positive regulation of miRNA metabolic process Source: BHF-UCL
    35. positive regulation of NF-kappaB transcription factor activity Source: MGI
    36. positive regulation of Schwann cell differentiation Source: Ensembl
    37. positive regulation of transcription, DNA-templated Source: UniProtKB
    38. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    39. positive regulation of type I interferon production Source: Reactome
    40. regulation of inflammatory response Source: UniProtKB
    41. response to amino acid Source: Ensembl
    42. response to cAMP Source: Ensembl
    43. response to cobalamin Source: Ensembl
    44. response to drug Source: Ensembl
    45. response to insulin Source: Ensembl
    46. response to interleukin-1 Source: BHF-UCL
    47. response to mechanical stimulus Source: Ensembl
    48. response to morphine Source: Ensembl
    49. response to muramyl dipeptide Source: Ensembl
    50. response to organic substance Source: UniProtKB
    51. response to progesterone Source: Ensembl
    52. response to UV-B Source: UniProtKB
    53. T cell receptor signaling pathway Source: Reactome
    54. toll-like receptor 10 signaling pathway Source: Reactome
    55. toll-like receptor 2 signaling pathway Source: Reactome
    56. toll-like receptor 3 signaling pathway Source: Reactome
    57. toll-like receptor 4 signaling pathway Source: Reactome
    58. toll-like receptor 5 signaling pathway Source: Reactome
    59. toll-like receptor 9 signaling pathway Source: Reactome
    60. toll-like receptor signaling pathway Source: Reactome
    61. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    62. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    63. transcription from RNA polymerase II promoter Source: GOC
    64. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
    65. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Host-virus interaction, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_12555. Downstream TCR signaling.
    REACT_13443. Regulated proteolysis of p75NTR.
    REACT_13696. NF-kB is activated and signals survival.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_23950. Interleukin-1 processing.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SABIO-RKQ04206.
    SignaLinkiQ04206.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:9955. RELA.

    Subcellular locationi

    Nucleus. Cytoplasm
    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 LPS stimulation.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. transcription factor complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving C11orf95 is found in more than two-thirds of supratentorial ependymomas. Translocation with C11orf95 produces a C11orf95-RELA fusion protein. C11orf95-RELA translocations are potent oncogenes that probably transform neural stem cells by driving an aberrant NF-kappa-B transcription program (PubMed:24553141).1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi254 – 2541T → A: Abolishes interaction with PIN1. 1 Publication
    Mutagenesisi276 – 2761S → C: Loss of phosphorylation. 1 Publication

    Organism-specific databases

    Orphaneti251636. Ependymoma.
    PharmGKBiPA296.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 551551Transcription factor p65PRO_0000205169Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Cross-linki37 – 37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)
    Modified residuei38 – 381Cysteine persulfide; alternateBy similarity
    Modified residuei38 – 381S-nitrosocysteine; alternateBy similarity
    Modified residuei122 – 1221N6-acetyllysine; by PCAF and EP300; alternate2 Publications
    Cross-linki122 – 122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate
    Modified residuei123 – 1231N6-acetyllysine; by PCAF and EP300; alternate2 Publications
    Cross-linki123 – 123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate
    Modified residuei218 – 2181N6-acetyllysine2 Publications
    Modified residuei221 – 2211N6-acetyllysine2 Publications
    Modified residuei254 – 2541Phosphothreonine2 Publications
    Modified residuei276 – 2761Phosphoserine; by RPS6KA4 and RPS6KA52 Publications
    Modified residuei281 – 2811Phosphoserine2 Publications
    Modified residuei310 – 3101N6-acetyllysine; alternate6 Publications
    Modified residuei310 – 3101N6-methyllysine; by SETD6; alternateBy similarity
    Modified residuei311 – 3111Phosphoserine; by PKC/PRKCZBy similarity
    Modified residuei435 – 4351Phosphothreonine2 Publications
    Modified residuei468 – 4681Phosphoserine; by IKKB and IKKE3 Publications
    Modified residuei505 – 5051Phosphothreonine; by CHEK12 Publications
    Modified residuei529 – 5291Phosphoserine; by CK22 Publications
    Modified residuei536 – 5361Phosphoserine; by IKKB2 Publications

    Post-translational modificationi

    Ubiquitinated, leading to its proteasomal degradation. Degradation is required for termination of NF-kappa-B response.1 Publication
    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 By similarity.By similarity
    Phosphorylation at Ser-311 disrupts the interaction with EHMT1 and promotes transcription factor activity By similarity. Phosphorylation on Ser-536 stimulates acetylation on Lys-310 and interaction with CBP; the phosphorylated and acetylated forms show enhanced transcriptional activity. Phosphorylation at Ser-276 by RPS6KA4 and RPS6KA5 promotes its transactivation and transcriptional activities.By similarity15 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 SIRT2.6 Publications
    S-nitrosylation of Cys-38 inactivates the enzyme activity.By similarity
    Sulfhydration at Cys-38 mediates the anti-apoptotic activity by promoting the interaction with RPS3 and activating the transcription factor activity.By similarity
    Sumoylation by PIAS3 negatively regulates DNA-bound activated NF-kappa-B.1 Publication

    Keywords - PTMi

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

    Proteomic databases

    MaxQBiQ04206.
    PaxDbiQ04206.
    PRIDEiQ04206.

    PTM databases

    PhosphoSiteiQ04206.

    Expressioni

    Gene expression databases

    ArrayExpressiQ04206.
    BgeeiQ04206.
    CleanExiHS_RELA.
    GenevestigatoriQ04206.

    Organism-specific databases

    HPAiCAB004264.
    CAB005030.

    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 By similarity. Interacts with NFKBID By similarity. Interacts with NFKBIA. Interacts with GSK3B. Interacts with NFKBIB By similarity. Interacts with NFKBIE. Interacts with NFKBIZ. Interacts with EHMT1 (via ANK repeats) By similarity. 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 UXT. Interacts with MTDH and PHF11. Interacts with ARRB2. Interacts with human respiratory syncytial virus (HRSV) protein M2-1. Interacts with NFKBIA (when phosphorylated), the interaction is direct; phosphorylated NFKBIA is part of a SCF(BTRC)-like complex lacking CUL1. Interacts with RNF25. Interacts (via C-terminus) with DDX1. Interacts with UFL1 and COMMD1. Interacts with BRMS1; this promotes deacetylation of 'Lys-310'. Interacts with NOTCH2 By similarity. Directly interacts with MEN1; this interaction represses NFKB-mediated transactivation. Interacts with AKIP1, which promotes the phosphorylation and nuclear retention of RELA. 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 (when acetylated at Lys-310) with BRD4; leading to activation of the NF-kappa-B pathway. Interacts with MEFV. Interacts with CLOCK By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-73886,EBI-73886
    AATFQ9NY613EBI-73886,EBI-372428
    ATF3P188474EBI-73886,EBI-712767
    CDK5RAP3Q96JB54EBI-73886,EBI-718818
    CHUKO151112EBI-73886,EBI-81249
    COMMD1Q8N6687EBI-73886,EBI-1550112
    CREBBPQ927933EBI-73886,EBI-81215
    CTNNB1P352222EBI-73886,EBI-491549
    DHX9Q082114EBI-73886,EBI-352022
    EHMT1Q9H9B13EBI-73886,EBI-766087
    ESR1P033727EBI-73886,EBI-78473
    GAMMAHV.ORF73O419743EBI-73886,EBI-6933128From a different organism.
    GFI1Q996842EBI-73886,EBI-949368
    HDAC1Q135475EBI-73886,EBI-301834
    KEAP1Q141454EBI-73886,EBI-751001
    LMO2P257913EBI-73886,EBI-739696
    MAPK10P537792EBI-73886,EBI-713543
    NFKB1P198389EBI-73886,EBI-300010
    NFKBIAP2596314EBI-73886,EBI-307386
    NFKBIBQ156536EBI-73886,EBI-352889
    OGTO152942EBI-73886,EBI-539828
    P/VP0C7743EBI-73886,EBI-3650423From a different organism.
    PPP2CAP677754EBI-73886,EBI-712311
    PPP2R1AP301532EBI-73886,EBI-302388
    RELBQ012012EBI-73886,EBI-357837
    RPS3P233967EBI-73886,EBI-351193
    RPS6KA5O755822EBI-73886,EBI-73869
    SETD7Q8WTS610EBI-73886,EBI-1268586
    SIRT1Q96EB64EBI-73886,EBI-1802965
    SIRT6Q8N6T74EBI-73886,EBI-712415
    SOCS1O155242EBI-73886,EBI-968198
    STAT3P407634EBI-73886,EBI-518675
    TGM2P219803EBI-73886,EBI-727668
    TP53BP2Q136254EBI-73886,EBI-77642
    TP53BP2Q13625-26EBI-73886,EBI-287091
    UBCP0CG486EBI-73886,EBI-3390054
    UL42P102266EBI-73886,EBI-1029310From a different organism.
    UXTQ9UBK95EBI-73886,EBI-357355

    Protein-protein interaction databases

    BioGridi111902. 222 interactions.
    DIPiDIP-24238N.
    IntActiQ04206. 107 interactions.
    MINTiMINT-106444.
    STRINGi9606.ENSP00000384273.

    Structurei

    Secondary structure

    1
    551
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi21 – 255
    Beta strandi30 – 323
    Beta strandi39 – 413
    Beta strandi53 – 553
    Beta strandi60 – 634
    Beta strandi68 – 8013
    Beta strandi87 – 926
    Beta strandi97 – 1048
    Beta strandi109 – 1124
    Beta strandi117 – 1193
    Helixi123 – 1253
    Helixi126 – 1294
    Turni130 – 1378
    Turni145 – 1484
    Beta strandi156 – 16611
    Beta strandi168 – 1736
    Beta strandi183 – 1886
    Beta strandi196 – 2005
    Beta strandi202 – 2054
    Beta strandi211 – 2177
    Beta strandi225 – 2306
    Beta strandi233 – 2386
    Helixi241 – 2433
    Turni246 – 2483
    Beta strandi249 – 2535
    Beta strandi258 – 2603
    Beta strandi266 – 2738
    Turni275 – 2773
    Beta strandi284 – 2896
    Helixi294 – 3029
    Helixi309 – 3113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NFIX-ray2.70A/C20-320[»]
    2LSPNMR-A304-316[»]
    2O61X-ray2.80A20-291[»]
    3GUTX-ray3.59A/C/E/G20-291[»]
    3QXYX-ray2.09P/Q302-316[»]
    3RC0X-ray2.19P/Q302-316[»]
    4KV1X-ray1.50C/D308-314[»]
    4KV4X-ray2.00B308-314[»]
    DisProtiDP00085.
    ProteinModelPortaliQ04206.
    SMRiQ04206. Positions 20-319, 427-491.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04206.

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni415 – 45945Activation domainAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi301 – 3044Nuclear localization signalSequence Analysis
    Motifi536 – 54499aaTAD

    Domaini

    the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.1 Publication

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG119056.
    HOGENOMiHOG000230474.
    HOVERGENiHBG017916.
    InParanoidiQ04206.
    KOiK04735.
    OMAiEFSPMVF.
    OrthoDBiEOG7VHSWT.
    PhylomeDBiQ04206.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q04206-1) [UniParc]FASTAAdd to Basket

    Also known as: p65

    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

    MDELFPLIFP AEPAQASGPY VEIIEQPKQR GMRFRYKCEG RSAGSIPGER    50
    STDTTKTHPT IKINGYTGPG TVRISLVTKD PPHRPHPHEL VGKDCRDGFY 100
    EAELCPDRCI HSFQNLGIQC VKKRDLEQAI SQRIQTNNNP FQVPIEEQRG 150
    DYDLNAVRLC FQVTVRDPSG RPLRLPPVLS HPIFDNRAPN TAELKICRVN 200
    RNSGSCLGGD EIFLLCDKVQ KEDIEVYFTG PGWEARGSFS QADVHRQVAI 250
    VFRTPPYADP SLQAPVRVSM QLRRPSDREL SEPMEFQYLP DTDDRHRIEE 300
    KRKRTYETFK SIMKKSPFSG PTDPRPPPRR IAVPSRSSAS VPKPAPQPYP 350
    FTSSLSTINY DEFPTMVFPS GQISQASALA PAPPQVLPQA PAPAPAPAMV 400
    SALAQAPAPV PVLAPGPPQA VAPPAPKPTQ AGEGTLSEAL LQLQFDDEDL 450
    GALLGNSTDP AVFTDLASVD NSEFQQLLNQ GIPVAPHTTE PMLMEYPEAI 500
    TRLVTGAQRP PDPAPAPLGA PGLPNGLLSG DEDFSSIADM DFSALLSQIS 550
    S 551
    Length:551
    Mass (Da):60,219
    Last modified:April 26, 2005 - v2
    Checksum:i8147A6AF9F2445C6
    GO
    Isoform 2 (identifier: Q04206-2) [UniParc]FASTAAdd to Basket

    Also known as: p65 delta 2

    The sequence of this isoform differs from the canonical sequence as follows:
         13-25: Missing.
         506-506: Missing.

    Show »
    Length:537
    Mass (Da):58,807
    Checksum:iA1F26DF2F53E662E
    GO
    Isoform 3 (identifier: Q04206-3) [UniParc]FASTAAdd to Basket

    Also known as: p65 delta

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

    Show »
    Length:541
    Mass (Da):59,068
    Checksum:i49F0493E19798AD1
    GO
    Isoform 4 (identifier: Q04206-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         143-145: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:548
    Mass (Da):59,910
    Checksum:iED40EF8B91F0A19A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti49 – 491E → R in CAA80524. (PubMed:8281153)Curated
    Sequence conflicti180 – 1801S → P in AAA36408. (PubMed:2006423)Curated
    Sequence conflicti372 – 3809QISQASALA → RSARPRLG in CAA80524. (PubMed:8281153)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei13 – 2513Missing in isoform 2. 1 PublicationVSP_005587Add
    BLAST
    Alternative sequencei143 – 1453Missing in isoform 4. 1 PublicationVSP_031245
    Alternative sequencei222 – 23110Missing in isoform 3. 1 PublicationVSP_012031
    Alternative sequencei506 – 5061Missing in isoform 2. 1 PublicationVSP_005588

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62399 mRNA. Translation: AAA36408.1.
    Z22948
    , Z22949, Z22953, Z22950, Z22951 Genomic DNA. Translation: CAA80524.2.
    L19067 mRNA. Translation: AAA20946.1.
    BC033522 mRNA. Translation: AAH33522.1.
    AY455868 Genomic DNA. Translation: AAR13863.1.
    CCDSiCCDS31609.1. [Q04206-1]
    CCDS44651.1. [Q04206-4]
    PIRiA40851.
    I53719.
    S51782. A42017.
    RefSeqiNP_001138610.1. NM_001145138.1. [Q04206-4]
    NP_001230913.1. NM_001243984.1.
    NP_068810.3. NM_021975.3. [Q04206-1]
    UniGeneiHs.502875.

    Genome annotation databases

    EnsembliENST00000308639; ENSP00000311508; ENSG00000173039. [Q04206-4]
    ENST00000406246; ENSP00000384273; ENSG00000173039. [Q04206-1]
    GeneIDi5970.
    KEGGihsa:5970.
    UCSCiuc001off.3. human. [Q04206-1]
    uc001ofh.3. human. [Q04206-4]

    Polymorphism databases

    DMDMi62906901.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62399 mRNA. Translation: AAA36408.1 .
    Z22948
    , Z22949 , Z22953 , Z22950 , Z22951 Genomic DNA. Translation: CAA80524.2 .
    L19067 mRNA. Translation: AAA20946.1 .
    BC033522 mRNA. Translation: AAH33522.1 .
    AY455868 Genomic DNA. Translation: AAR13863.1 .
    CCDSi CCDS31609.1. [Q04206-1 ]
    CCDS44651.1. [Q04206-4 ]
    PIRi A40851.
    I53719.
    S51782. A42017.
    RefSeqi NP_001138610.1. NM_001145138.1. [Q04206-4 ]
    NP_001230913.1. NM_001243984.1.
    NP_068810.3. NM_021975.3. [Q04206-1 ]
    UniGenei Hs.502875.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NFI X-ray 2.70 A/C 20-320 [» ]
    2LSP NMR - A 304-316 [» ]
    2O61 X-ray 2.80 A 20-291 [» ]
    3GUT X-ray 3.59 A/C/E/G 20-291 [» ]
    3QXY X-ray 2.09 P/Q 302-316 [» ]
    3RC0 X-ray 2.19 P/Q 302-316 [» ]
    4KV1 X-ray 1.50 C/D 308-314 [» ]
    4KV4 X-ray 2.00 B 308-314 [» ]
    DisProti DP00085.
    ProteinModelPortali Q04206.
    SMRi Q04206. Positions 20-319, 427-491.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111902. 222 interactions.
    DIPi DIP-24238N.
    IntActi Q04206. 107 interactions.
    MINTi MINT-106444.
    STRINGi 9606.ENSP00000384273.

    Chemistry

    BindingDBi Q04206.
    ChEMBLi CHEMBL5533.

    PTM databases

    PhosphoSitei Q04206.

    Polymorphism databases

    DMDMi 62906901.

    Proteomic databases

    MaxQBi Q04206.
    PaxDbi Q04206.
    PRIDEi Q04206.

    Protocols and materials databases

    DNASUi 5970.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000308639 ; ENSP00000311508 ; ENSG00000173039 . [Q04206-4 ]
    ENST00000406246 ; ENSP00000384273 ; ENSG00000173039 . [Q04206-1 ]
    GeneIDi 5970.
    KEGGi hsa:5970.
    UCSCi uc001off.3. human. [Q04206-1 ]
    uc001ofh.3. human. [Q04206-4 ]

    Organism-specific databases

    CTDi 5970.
    GeneCardsi GC11M065421.
    HGNCi HGNC:9955. RELA.
    HPAi CAB004264.
    CAB005030.
    MIMi 164014. gene.
    neXtProti NX_Q04206.
    Orphaneti 251636. Ependymoma.
    PharmGKBi PA296.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG119056.
    HOGENOMi HOG000230474.
    HOVERGENi HBG017916.
    InParanoidi Q04206.
    KOi K04735.
    OMAi EFSPMVF.
    OrthoDBi EOG7VHSWT.
    PhylomeDBi Q04206.
    TreeFami TF325632.

    Enzyme and pathway databases

    Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_12555. Downstream TCR signaling.
    REACT_13443. Regulated proteolysis of p75NTR.
    REACT_13696. NF-kB is activated and signals survival.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_23950. Interleukin-1 processing.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SABIO-RK Q04206.
    SignaLinki Q04206.

    Miscellaneous databases

    ChiTaRSi RELA. human.
    EvolutionaryTracei Q04206.
    GeneWikii RELA.
    GenomeRNAii 5970.
    NextBioi 23241.
    PROi Q04206.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q04206.
    Bgeei Q04206.
    CleanExi HS_RELA.
    Genevestigatori Q04206.

    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. "Isolation of a rel-related human cDNA that potentially encodes the 65-kD subunit of NF-kappa B."
      Ruben S.M., Dillon P.J., Schreck R., Henkel T., Chen C.-H., Maher M., Baeuerle P.A., Rosen C.A.
      Science 251:1490-1493(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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], ALTERNATIVE SPLICING.
    3. "An alternatively spliced transcript, p65 delta 2, of the gene encoding the p65 subunit of the transcription factor NF-kappa B."
      Lyle R., Valleley E.M., Sharpe P.T., Hewitt J.E.
      Gene 138:265-266(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Bone.
    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 4).
      Tissue: Colon.
    5. SeattleSNPs variation discovery resource
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-551.
    6. "Functional characterization of the NF-kappa B p65 transcriptional activator and an alternatively spliced derivative."
      Ruben S.M., Narayanan R., Klement J.F., Chen C.-H., Rosen C.A.
      Mol. Cell. Biol. 12:444-454(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 214-239 (ISOFORMS 1/2 AND 3), ACTIVATION DOMAIN.
    7. "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-P50 COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX.
    8. "I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B p65 and requires the transactivation domain to inhibit NF-kappa B p65 DNA binding."
      Ganchi P.A., Sun S.C., Greene W.C., Ballard D.W.
      Mol. Biol. Cell 3:1339-1352(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFKBIA.
    9. "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 P65-C-REL COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P65-P52 COMPLEX.
    10. "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-P65 COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX.
    11. "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.
    12. "IKAP is a scaffold protein of the IkappaB kinase complex."
      Cohen L., Henzel W.J., Baeuerle P.A.
      Nature 395:292-296(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH CHUK; IKBKB; NFKBIA; IKBKAP AND MAP3K14.
    13. "IkappaB kinases phosphorylate NF-kappaB p65 subunit on serine 536 in the transactivation domain."
      Sakurai H., Chiba H., Miyoshi H., Sugita T., Toriumi W.
      J. Biol. Chem. 274:30353-30356(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-536.
    14. "NF-kappaB subunit p65 binds to 53BP2 and inhibits cell death induced by 53BP2."
      Yang J.-P., Hori M., Takahashi N., Kawabe T., Kato H., Okamoto T.
      Oncogene 18:5177-5186(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INTERACTION WITH TP53BP2.
    15. "Yersinia enterocolitica invasin protein triggers IL-8 production in epithelial cells via activation of Rel p65-p65 homodimers."
      Schulte R., Grassl G.A., Preger S., Fessele S., Jacobi C.A., Schaller M., Nelson P.J., Autenrieth I.B.
      FASEB J. 14:1471-1484(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE NF-KAPPA-B P65-P65 COMPLEX.
    16. "Inhibition of nuclear factor-kappaB-mediated transcription by association with the amino-terminal enhancer of split, a Groucho-related protein lacking WD40 repeats."
      Tetsuka T., Uranishi H., Imai H., Ono T., Sonta S., Takahashi N., Asamitsu K., Okamoto T.
      J. Biol. Chem. 275:4383-4390(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AES AND TLE1.
    17. "Tumor necrosis factor alpha-induced phosphorylation of RelA/p65 on Ser529 is controlled by casein kinase II."
      Wang D., Westerheide S.D., Hanson J.L., Baldwin A.S. Jr.
      J. Biol. Chem. 275:32592-32597(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-529.
    18. "The tumor suppressor protein menin interacts with NF-kappaB proteins and inhibits NF-kappaB-mediated transactivation."
      Heppner C., Bilimoria K.Y., Agarwal S.K., Kester M., Whitty L.J., Guru S.C., Chandrasekharappa S.C., Collins F.S., Spiegel A.M., Marx S.J., Burns A.L.
      Oncogene 20:4917-4925(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MEN1.
    19. "Duration of nuclear NF-kappaB action regulated by reversible acetylation."
      Chen L.F., Fischle W., Verdin E., Greene W.C.
      Science 293:1653-1657(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION, INTERACTION WITH HDAC3.
    20. "A novel protein overexpressed in hepatoma accelerates export of NF-kappa B from the nucleus and inhibits p53-dependent apoptosis."
      Higashitsuji H., Higashitsuji H., Nagao T., Nonoguchi K., Fujii S., Itoh K., Fujita J.
      Cancer Cell 2:335-346(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ETHE1.
    21. "Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB."
      Chen L.F., Mu Y., Greene W.C.
      EMBO J. 21:6539-6548(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-218; LYS-221 AND LYS-310.
    22. "The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1."
      Zhong H., May M.J., Jimi E., Ghosh S.
      Mol. Cell 9:625-636(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBP AND HDAC1, PHOSPHORYLATION.
    23. "Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1)."
      Vermeulen L., De Wilde G., Van Damme P., Vanden Berghe W., Haegeman G.
      EMBO J. 22:1313-1324(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RPS6KA5, MUTAGENESIS OF SER-276, PHOSPHORYLATION AT SER-276.
    24. "Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65."
      Kiernan R., Bres V., Ng R.W., Coudart M.-P., El Messaoudi S., Sardet C., Jin D.-Y., Emiliani S., Benkirane M.
      J. Biol. Chem. 278:2758-2766(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-122 AND LYS-123.
    25. "RING finger protein AO7 supports NF-kappaB-mediated transcription by interacting with the transactivation domain of the p65 subunit."
      Asamitsu K., Tetsuka T., Kanazawa S., Okamoto T.
      J. Biol. Chem. 278:26879-26887(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RNF25.
    26. "Glycogen synthase kinase-3 beta regulates NF-kappa B1/p105 stability."
      Demarchi F., Bertoli C., Sandy P., Schneider C.
      J. Biol. Chem. 278:39583-39590(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GSK3B.
    27. "Regulation of NF-kappaB signaling by Pin1-dependent prolyl isomerization and ubiquitin-mediated proteolysis of p65/RelA."
      Ryo A., Suizu F., Yoshida Y., Perrem K., Liou Y.C., Wulf G., Rottapel R., Yamaoka S., Lu K.P.
      Mol. Cell 12:1413-1426(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-254, INTERACTION WITH PIN1 AND SOCS1, MUTAGENESIS OF THR-254.
    28. "Identification of a ZU5 and death domain-containing inhibitor of NF-kappaB."
      Zhang J., Xu L.-G., Han K.-J., Shu H.-B.
      J. Biol. Chem. 279:17819-17825(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UNC5CL.
    29. "Suppression of MEK/ERK signaling pathway enhances cisplatin-induced NF-kappaB activation by protein phosphatase 4-mediated NF-kappaB p65 Thr dephosphorylation."
      Yeh P.Y., Yeh K.H., Chuang S.E., Song Y.C., Cheng A.L.
      J. Biol. Chem. 279:26143-26148(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-435.
    30. "Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor kappaB response."
      Saccani S., Marazzi I., Beg A.A., Natoli G.
      J. Exp. Med. 200:107-113(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    31. "Identification of beta-arrestin2 as a G protein-coupled receptor-stimulated regulator of NF-kappaB pathways."
      Gao H., Sun Y., Wu Y., Luan B., Wang Y., Qu B., Pei G.
      Mol. Cell 14:303-317(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARRB2.
    32. "The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis."
      Garkavtsev I., Kozin S.V., Chernova O., Xu L., Winkler F., Brown E., Barnett G.H., Jain R.K.
      Nature 428:328-332(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ING4.
    33. "Regulation of NF-kappaB and p53 through activation of ATR and Chk1 by the ARF tumour suppressor."
      Rocha S., Garrett M.D., Campbell K.J., Schumm K., Perkins N.D.
      EMBO J. 24:1157-1169(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-505.
    34. "IKKbeta phosphorylates p65 at S468 in transactivation domain 2."
      Schwabe R.F., Sakurai H.
      FASEB J. 19:1758-1760(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-468.
    35. "cis-acting, element-specific transcriptional activity of differentially phosphorylated nuclear factor-kappa B."
      Anrather J., Racchumi G., Iadecola C.
      J. Biol. Chem. 280:244-252(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-281.
    36. Cited for: INTERACTION WITH COMMD1, SUBCELLULAR LOCATION.
    37. Cited for: ACETYLATION AT LYS-310.
    38. "Respiratory syncytial virus M2-1 protein induces the activation of nuclear factor kappa B."
      Reimers K., Buchholz K., Werchau H.
      Virology 331:260-268(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HRSV PROTEIN M2-1.
    39. "Activation of the nuclear factor kappaB pathway by astrocyte elevated gene-1: implications for tumor progression and metastasis."
      Emdad L., Sarkar D., Su Z.-Z., Randolph A., Boukerche H., Valerie K., Fisher P.B.
      Cancer Res. 66:1509-1516(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MTDH.
    40. "Human ubiquitin specific protease 31 is a deubiquitinating enzyme implicated in activation of nuclear factor-kappaB."
      Tzimas C., Michailidou G., Arsenakis M., Kieff E., Mosialos G., Hatzivassiliou E.G.
      Cell. Signal. 18:83-92(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH USP48.
    41. "Inducible phosphorylation of NF-kappa B p65 at serine 468 by T cell costimulation is mediated by IKK epsilon."
      Mattioli I., Geng H., Sebald A., Hodel M., Bucher C., Kracht M., Schmitz M.L.
      J. Biol. Chem. 281:6175-6183(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-468.
    42. "Breast cancer metastasis suppressor 1 functions as a corepressor by enhancing histone deacetylase 1-mediated deacetylation of RelA/p65 and promoting apoptosis."
      Liu Y., Smith P.W., Jones D.R.
      Mol. Cell. Biol. 26:8683-8696(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BRMS1, FUNCTION, ACETYLATION AT LYS-310.
    43. "Coactivator-associated arginine methyltransferase-1 enhances nuclear factor-kappaB-mediated gene transcription through methylation of histone H3 at arginine 17."
      Miao F., Li S., Chavez V., Lanting L., Natarajan R.
      Mol. Endocrinol. 20:1562-1573(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CARM1.
    44. "IL-1 receptor-associated kinase 1 is critical for latent membrane protein 1-induced p65/RelA serine 536 phosphorylation and NF-kappaB activation."
      Song Y.J., Jen K.Y., Soni V., Kieff E., Cahir-McFarland E.
      Proc. Natl. Acad. Sci. U.S.A. 103:2689-2694(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-P52 COMPLEX.
    45. "Nine-amino-acid transactivation domain: establishment and prediction utilities."
      Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.
      Genomics 89:756-768(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    46. "UXT is a novel and essential cofactor in the NF-kappaB transcriptional enhanceosome."
      Sun S., Tang Y., Lou X., Zhu L., Yang K., Zhang B., Shi H., Wang C.
      J. Cell Biol. 178:231-244(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH UXT.
    47. "The familial Mediterranean fever protein, pyrin, is cleaved by caspase-1 and activates NF-kappaB through its N-terminal fragment."
      Chae J.J., Wood G., Richard K., Jaffe H., Colburn N.T., Masters S.L., Gumucio D.L., Shoham N.G., Kastner D.L.
      Blood 112:1794-1803(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MEFV.
    48. "Functional characterization of the atopy-associated gene PHF11."
      Clarke E., Rahman N., Page N., Rolph M.S., Stewart G.J., Jones G.J.
      J. Allergy Clin. Immunol. 121:1148-1154(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHF11.
    49. "AKIP1 enhances NF-kappaB-dependent gene expression by promoting the nuclear retention and phosphorylation of p65."
      Gao N., Asamitsu K., Hibi Y., Ueno T., Okamoto T.
      J. Biol. Chem. 283:7834-7843(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AKIP1.
    50. "The DEAD-box RNA helicase DDX1 interacts with RelA and enhances nuclear factor kappaB-mediated transcription."
      Ishaq M., Ma L., Wu X., Mu Y., Pan J., Hu J., Hu T., Fu Q., Guo D.
      J. Cell. Biochem. 106:296-305(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DDX1, SUBCELLULAR LOCATION.
    51. "Brd4 coactivates transcriptional activation of NF-kappaB via specific binding to acetylated RelA."
      Huang B., Yang X.D., Zhou M.M., Ozato K., Chen L.F.
      Mol. Cell. Biol. 29:1375-1387(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BRD4, ACETYLATION AT LYS-310.
    52. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    53. "A novel LZAP-binding protein, NLBP, inhibits cell invasion."
      Kwon J., Cho H.J., Han S.H., No J.G., Kwon J.Y., Kim H.
      J. Biol. Chem. 285:12232-12240(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UFL1.
    54. "SIRT2 regulates NF-kappaB dependent gene expression through deacetylation of p65 Lys310."
      Rothgiesser K.M., Erener S., Waibel S., Luscher B., Hottiger M.O.
      J. Cell Sci. 123:4251-4258(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEACETYLATION BY SIRT2.
    55. "Zinc finger protein Gfi1 controls the endotoxin-mediated Toll-like receptor inflammatory response by antagonizing NF-kappaB p65."
      Sharif-Askari E., Vassen L., Kosan C., Khandanpour C., Gaudreau M.C., Heyd F., Okayama T., Jin J., Rojas M.E., Grimes H.L., Zeng H., Moroy T.
      Mol. Cell. Biol. 30:3929-3942(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GFI1, SUBCELLULAR LOCATION, INDUCTION, FUNCTION.
    56. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    57. "NF-kappaB repression by PIAS3 mediated RelA SUMOylation."
      Liu Y., Bridges R., Wortham A., Kulesz-Martin M.
      PLoS ONE 7:E37636-E37636(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-37; LYS-122 AND LYS-123 BY PIAS3.
    58. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    59. Cited for: CHROMOSOMAL TRANSLOCATION WITH C11ORF95.
    60. "Structure of an IkappaBalpha/NF-kappaB complex."
      Jacobs M.D., Harrison S.C.
      Cell 95:749-758(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).

    Entry informationi

    Entry nameiTF65_HUMAN
    AccessioniPrimary (citable) accession number: Q04206
    Secondary accession number(s): Q6GTV1, Q6SLK1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 177 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3