TF65_MOUSE
ID TF65_MOUSE Reviewed; 549 AA.
AC Q04207; Q62025;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 228.
DE RecName: Full=Transcription factor p65;
DE AltName: Full=Nuclear factor NF-kappa-B p65 subunit;
DE AltName: Full=Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3;
GN Name=Rela; Synonyms=Nfkb3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P65).
RX PubMed=2001591; DOI=10.1016/0092-8674(91)90320-x;
RA Nolan G.P., Ghosh S., Liou H.C., Tempst P., Baltimore D.;
RT "DNA binding and I kappa B inhibition of the cloned p65 subunit of NF-kappa
RT B, a rel-related polypeptide.";
RL Cell 64:961-969(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P65).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
RC STRAIN=BALB/cJ;
RX PubMed=8918242; DOI=10.1016/0378-1119(96)00231-4;
RA Linker R.A., Baeuerle P.A., Kaltschmidt C.;
RT "Cloning of the murine relA (p65 NF-kappa B) gene and comparison to the
RT human gene reveals a distinct first intron.";
RL Gene 176:119-124(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 188-252, AND ALTERNATIVE SPLICING.
RC STRAIN=BALB/cJ;
RX PubMed=8281153; DOI=10.1093/hmg/2.11.1895;
RA Deloukas P., van Loon A.P.G.M.;
RT "Genomic organization of the gene encoding the p65 subunit of NF-kappa B:
RT multiple variants of the p65 protein may be generated by alternative
RT splicing.";
RL Hum. Mol. Genet. 2:1895-1900(1993).
RN [5]
RP INTERACTION WITH NFKBIB.
RX PubMed=8816457; DOI=10.1128/mcb.16.10.5444;
RA Suyang H., Phillips R.J., Douglas I., Ghosh S.;
RT "Role of unphosphorylated, newly synthesized IkappaB beta in persistent
RT activation of NF-kappaB.";
RL Mol. Cell. Biol. 16:5444-5449(1996).
RN [6]
RP INTERACTION WITH NFKBIA.
RX PubMed=9990853; DOI=10.1101/gad.13.3.284;
RA Spencer E., Jiang J., Chen Z.J.;
RT "Signal-induced ubiquitination of IkappaBalpha by the F-box protein
RT Slimb/beta-TrCP.";
RL Genes Dev. 13:284-294(1999).
RN [7]
RP INTERACTION WITH NFKBID.
RX PubMed=11931770; DOI=10.1016/s1097-2765(02)00469-0;
RA Fiorini E., Schmitz I., Marissen W.E., Osborn S.L., Touma M., Sasada T.,
RA Reche P.A., Tibaldi E.V., Hussey R.E., Kruisbeek A.M., Reinherz E.L.,
RA Clayton L.K.;
RT "Peptide-induced negative selection of thymocytes activates transcription
RT of an NF-kappa B inhibitor.";
RL Mol. Cell 9:637-648(2002).
RN [8]
RP PHOSPHORYLATION AT SER-311.
RX PubMed=12881425; DOI=10.1093/emboj/cdg370;
RA Duran A., Diaz-Meco M.T., Moscat J.;
RT "Essential role of RelA Ser311 phosphorylation by zetaPKC in NF-kappaB
RT transcriptional activation.";
RL EMBO J. 22:3910-3918(2003).
RN [9]
RP MUTAGENESIS OF SER-281.
RX PubMed=12874295; DOI=10.1074/jbc.m301521200;
RA Maier H.J., Marienfeld R., Wirth T., Baumann B.;
RT "Critical role of RelB serine 368 for dimerization and p100
RT stabilization.";
RL J. Biol. Chem. 278:39242-39250(2003).
RN [10]
RP IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX, AND IDENTIFICATION IN THE
RP NF-KAPPA-B P65-P65 COMPLEX.
RX PubMed=15051764; DOI=10.1084/jem.20031272;
RA Goriely S., Van Lint C., Dadkhah R., Libin M., De Wit D., Demonte D.,
RA Willems F., Goldman M.;
RT "A defect in nucleosome remodeling prevents IL-12(p35) gene transcription
RT in neonatal dendritic cells.";
RL J. Exp. Med. 199:1011-1016(2004).
RN [11]
RP INTERACTION WITH IRAK1BP1.
RX PubMed=15485901; DOI=10.1128/mcb.24.21.9317-9326.2004;
RA Kwon H.-J., Breese E.H., Vig-Varga E., Luo Y., Lee Y., Goebl M.G.,
RA Harrington M.A.;
RT "Tumor necrosis factor alpha induction of NF-kappaB requires the novel
RT coactivator SIMPL.";
RL Mol. Cell. Biol. 24:9317-9326(2004).
RN [12]
RP INTERACTION WITH CARM1.
RX PubMed=15616592; DOI=10.1038/sj.emboj.7600500;
RA Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C.,
RA Imhof R., Bedford M.T., Natoli G., Hottiger M.O.;
RT "Arginine methyltransferase CARM1 is a promoter-specific regulator of NF-
RT kappaB-dependent gene expression.";
RL EMBO J. 24:85-96(2005).
RN [13]
RP INTERACTION WITH NOTCH2.
RX PubMed=18710934; DOI=10.1128/mcb.00299-08;
RA Fukushima H., Nakao A., Okamoto F., Shin M., Kajiya H., Sakano S.,
RA Bigas A., Jimi E., Okabe K.;
RT "The association of Notch2 and NF-kappaB accelerates RANKL-induced
RT osteoclastogenesis.";
RL Mol. Cell. Biol. 28:6402-6412(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-176, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, METHYLATION AT LYS-310, PHOSPHORYLATION AT
RP SER-311, INTERACTION WITH EHMT1, AND MUTAGENESIS OF LYS-310.
RX PubMed=21131967; DOI=10.1038/ni.1968;
RA Levy D., Kuo A.J., Chang Y., Schaefer U., Kitson C., Cheung P., Espejo A.,
RA Zee B.M., Liu C.L., Tangsombatvisit S., Tennen R.I., Kuo A.Y., Tanjing S.,
RA Cheung R., Chua K.F., Utz P.J., Shi X., Prinjha R.K., Lee K., Garcia B.A.,
RA Bedford M.T., Tarakhovsky A., Cheng X., Gozani O.;
RT "Lysine methylation of the NF-kappaB subunit RelA by SETD6 couples activity
RT of the histone methyltransferase GLP at chromatin to tonic repression of
RT NF-kappaB signaling.";
RL Nat. Immunol. 12:29-36(2011).
RN [16]
RP FUNCTION, SULFHYDRATION AT CYS-38, S-NITROSYLATION AT CYS-38, AND
RP MUTAGENESIS OF CYS-38.
RX PubMed=22244329; DOI=10.1016/j.molcel.2011.10.021;
RA Sen N., Paul B.D., Gadalla M.M., Mustafa A.K., Sen T., Xu R., Kim S.,
RA Snyder S.H.;
RT "Hydrogen sulfide-linked sulfhydration of NF-kappaB mediates its
RT antiapoptotic actions.";
RL Mol. Cell 45:13-24(2012).
RN [17]
RP INTERACTION WITH PHF2.
RX PubMed=22921934; DOI=10.1016/j.molcel.2012.07.020;
RA Stender J.D., Pascual G., Liu W., Kaikkonen M.U., Do K., Spann N.J.,
RA Boutros M., Perrimon N., Rosenfeld M.G., Glass C.K.;
RT "Control of proinflammatory gene programs by regulated trimethylation and
RT demethylation of histone H4K20.";
RL Mol. Cell 48:28-38(2012).
RN [18]
RP INTERACTION WITH CLOCK.
RX PubMed=22895791; DOI=10.1073/pnas.1206274109;
RA Spengler M.L., Kuropatwinski K.K., Comas M., Gasparian A.V., Fedtsova N.,
RA Gleiberman A.S., Gitlin I.I., Artemicheva N.M., Deluca K.A., Gudkov A.V.,
RA Antoch M.P.;
RT "Core circadian protein CLOCK is a positive regulator of NF-kappaB-mediated
RT transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E2457-E2465(2012).
RN [19]
RP INTERACTION WITH TBX21.
RX PubMed=23616576; DOI=10.4049/jimmunol.1203403;
RA Jang E.J., Park H.R., Hong J.H., Hwang E.S.;
RT "Lysine 313 of T-box is crucial for modulation of protein stability, DNA
RT binding, and threonine phosphorylation of T-bet.";
RL J. Immunol. 190:5764-5770(2013).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-310, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [21]
RP INTERACTION WITH KAT2A.
RX PubMed=25024434; DOI=10.15252/embj.201487870;
RA Stilling R.M., Roenicke R., Benito E., Urbanke H., Capece V., Burkhardt S.,
RA Bahari-Javan S., Barth J., Sananbenesi F., Schuetz A.L., Dyczkowski J.,
RA Martinez-Hernandez A., Kerimoglu C., Dent S.Y., Bonn S., Reymann K.G.,
RA Fischer A.;
RT "K-Lysine acetyltransferase 2a regulates a hippocampal gene expression
RT network linked to memory formation.";
RL EMBO J. 33:1912-1927(2014).
RN [22]
RP DISRUPTION PHENOTYPE.
RX PubMed=28600438; DOI=10.1084/jem.20160724;
RA Badran Y.R., Dedeoglu F., Leyva Castillo J.M., Bainter W., Ohsumi T.K.,
RA Bousvaros A., Goldsmith J.D., Geha R.S., Chou J.;
RT "Human RELA haploinsufficiency results in autosomal-dominant chronic
RT mucocutaneous ulceration.";
RL J. Exp. Med. 214:1937-1947(2017).
RN [23]
RP INTERACTION WITH MKRN2, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=28378844; DOI=10.1038/srep46097;
RA Shin C., Ito Y., Ichikawa S., Tokunaga M., Sakata-Sogawa K., Tanaka T.;
RT "MKRN2 is a novel ubiquitin E3 ligase for the p65 subunit of NF-kappaB and
RT negatively regulates inflammatory responses.";
RL Sci. Rep. 7:46097-46097(2017).
RN [24]
RP FUNCTION, INTERACTION WITH ZBTB7A, DOMAIN, REGION, AND MUTAGENESIS OF
RP 361-ASP--SER-370.
RX PubMed=29813070; DOI=10.1371/journal.pbio.2004526;
RA Ramos Pittol J.M., Oruba A., Mittler G., Saccani S., van Essen D.;
RT "Zbtb7a is a transducer for the control of promoter accessibility by NF-
RT kappa B and multiple other transcription factors.";
RL PLoS Biol. 16:E2004526-E2004526(2018).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 19-291.
RX PubMed=9865694; DOI=10.1016/s0092-8674(00)81699-2;
RA Huxford T., Huang D.B., Malek S., Ghosh G.;
RT "The crystal structure of the IkappaBalpha/NF-kappaB complex reveals
RT mechanisms of NF-kappaB inactivation.";
RL Cell 95:759-770(1998).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 19-291.
RX PubMed=9437432; DOI=10.1038/nsb0198-67;
RA Chen Y.Q., Ghosh S., Ghosh G.;
RT "A novel DNA recognition mode by the NF-kappa B p65 homodimer.";
RL Nat. Struct. Biol. 5:67-73(1998).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=9450761; DOI=10.1038/34956;
RA Chen F.E., Huang D.B., Chen Y.Q., Ghosh G.;
RT "Crystal structure of p50/p65 heterodimer of transcription factor NF-kappaB
RT bound to DNA.";
RL Nature 391:410-413(1998).
CC -!- FUNCTION: NF-kappa-B is a pleiotropic transcription factor present in
CC almost all cell types and is the endpoint of a series of signal
CC transduction events that are initiated by a vast array of stimuli
CC related to many biological processes such as inflammation, immunity,
CC differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B
CC is a homo- or heterodimeric complex formed by the Rel-like domain-
CC containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and
CC NFKB2/p52. The heterodimeric RELA-NFKB1 complex appears to be most
CC abundant one. The dimers bind at kappa-B sites in the DNA of their
CC target genes and the individual dimers have distinct preferences for
CC different kappa-B sites that they can bind with distinguishable
CC affinity and specificity. Different dimer combinations act as
CC transcriptional activators or repressors, respectively. The NF-kappa-B
CC heterodimeric RELA-NFKB1 and RELA-REL complexes, for instance, function
CC as transcriptional activators. NF-kappa-B is controlled by various
CC mechanisms of post-translational modification and subcellular
CC compartmentalization as well as by interactions with other cofactors or
CC corepressors. NF-kappa-B complexes are held in the cytoplasm in an
CC inactive state complexed with members of the NF-kappa-B inhibitor (I-
CC kappa-B) family. In a conventional activation pathway, I-kappa-B is
CC phosphorylated by I-kappa-B kinases (IKKs) in response to different
CC activators, subsequently degraded thus liberating the active NF-kappa-B
CC complex which translocates to the nucleus. The inhibitory effect of I-
CC kappa-B on NF-kappa-B through retention in the cytoplasm is exerted
CC primarily through the interaction with RELA. RELA shows a weak DNA-
CC binding site which could contribute directly to DNA binding in the NF-
CC kappa-B complex. Beside its activity as a direct transcriptional
CC activator, it is also able to modulate promoters accessibility to
CC transcription factors and thereby indirectly regulate gene expression
CC (PubMed:29813070). Associates with chromatin at the NF-kappa-B promoter
CC region via association with DDX1. Essential for cytokine gene
CC expression in T-cells (By similarity). The NF-kappa-B homodimeric RELA-
CC RELA complex appears to be involved in invasin-mediated activation of
CC IL-8 expression (By similarity). {ECO:0000250|UniProtKB:Q04206,
CC ECO:0000269|PubMed:21131967, ECO:0000269|PubMed:22244329,
CC ECO:0000269|PubMed:29813070}.
CC -!- SUBUNIT: Component of the NF-kappa-B p65-p50 complex. Component of the
CC NF-kappa-B p65-c-Rel complex. Homodimer; component of the NF-kappa-B
CC p65-p65 complex. Component of the NF-kappa-B p65-p52 complex. May
CC interact with ETHE1. Binds TLE5 and TLE1. Interacts with TP53BP2. Binds
CC to and is phosphorylated by the activated form of either RPS6KA4 or
CC RPS6KA5. Interacts with ING4 and this interaction may be indirect.
CC Interacts with CARM1, USP48 and UNC5CL. Interacts with IRAK1BP1.
CC Interacts with NFKBIA. Interacts with GSK3B. Interacts with NFKBIB.
CC Interacts with NFKBIE. Interacts with NFKBIZ. Part of a 70-90 kDa
CC complex at least consisting of CHUK, IKBKB, NFKBIA, RELA, ELP1 and
CC MAP3K14. Interacts with HDAC3; HDAC3 mediates the deacetylation of
CC RELA. Interacts with HDAC1; the interaction requires non-phosphorylated
CC RELA. Interacts with CBP; the interaction requires phosphorylated RELA.
CC Interacts (phosphorylated at 'Thr-254') with PIN1; the interaction
CC inhibits p65 binding to NFKBIA. Interacts with SOCS1. Interacts with
CC MTDH and PHF11. Interacts with NFKBID. Interacts with ARRB2. Interacts
CC with NFKBIA (when phosphorylated), the interaction is direct;
CC phosphorylated NFKBIA is associated with a SCF(BTRC)-like complex
CC lacking CUL1. Interacts with RNF25. Interacts (via C-terminus) with
CC DDX1 (By similarity). Interacts with UFL1 and COMMD1 (By similarity).
CC Interacts with BRMS1; this promotes deacetylation of 'Lys-310'.
CC Interacts (when acetylated at Lys-310) with BRD4; leading to activation
CC of the NF-kappa-B pathway (By similarity). Interacts with EHMT1 (via
CC ANK repeats). Interacts with NOTCH2. Directly interacts with MEN1; this
CC interaction represses NFKB-mediated transactivation (By similarity).
CC Interacts with AKIP1, which promotes the phosphorylation and nuclear
CC retention of RELA (By similarity). Interacts (via the RHD) with GFI1;
CC the interaction, after bacterial lipopolysaccharide (LPS) stimulation,
CC inhibits the transcriptional activity by interfering with the DNA-
CC binding activity to target gene promoter DNA. Interacts with MEFV (By
CC similarity). Interacts with CLOCK. Interacts with FOXP3 (By
CC similarity). Interacts (via N-terminus) with CPEN1; this interaction
CC induces proteolytic cleavage of p65/RELA subunit and inhibition of NF-
CC kappa-B transcriptional activity (By similarity). Interacts with
CC CDK5RAP3; stimulates the interaction of RELA with HDAC1, HDAC2 and
CC HDAC3 thereby inhibiting NF-kappa-B transcriptional activity (By
CC similarity). Interacts with DHX9; this interaction is direct and
CC activates NF-kappa-B-mediated transcription (By similarity). Interacts
CC with TBX21 (PubMed:23616576). Interacts with LRRC25 (By similarity).
CC Interacts with KAT2A (PubMed:25024434). Interacts (via transcriptional
CC activation domain 3) with ZBTB7A; involved in the control by RELA of
CC the accessibility of target gene promoters (PubMed:29813070). Directly
CC interacts with DDX3X; this interaction may trap RELA in the cytoplasm,
CC impairing nuclear relocalization upon TNF activating signals (By
CC similarity). Interacts with PHF2 (PubMed:22921934). Interacts with
CC MKRN2; the interaction leads to its polyubiquitination and proteasome-
CC dependent degradation (PubMed:28378844). {ECO:0000250|UniProtKB:Q04206,
CC ECO:0000269|PubMed:11931770, ECO:0000269|PubMed:15051764,
CC ECO:0000269|PubMed:15485901, ECO:0000269|PubMed:15616592,
CC ECO:0000269|PubMed:18710934, ECO:0000269|PubMed:21131967,
CC ECO:0000269|PubMed:22895791, ECO:0000269|PubMed:22921934,
CC ECO:0000269|PubMed:23616576, ECO:0000269|PubMed:25024434,
CC ECO:0000269|PubMed:28378844, ECO:0000269|PubMed:29813070,
CC ECO:0000269|PubMed:8816457, ECO:0000269|PubMed:9990853}.
CC -!- INTERACTION:
CC Q04207; P45481: Crebbp; NbExp=9; IntAct=EBI-644400, EBI-296306;
CC Q04207; Q02248: Ctnnb1; NbExp=5; IntAct=EBI-644400, EBI-397872;
CC Q04207; O09106: Hdac1; NbExp=2; IntAct=EBI-644400, EBI-301912;
CC Q04207; Q8VCD5: Med17; NbExp=4; IntAct=EBI-644400, EBI-5744951;
CC Q04207; P25799: Nfkb1; NbExp=6; IntAct=EBI-644400, EBI-643958;
CC Q04207; P25799-1: Nfkb1; NbExp=6; IntAct=EBI-644400, EBI-643974;
CC Q04207; PRO_0000030312 [P25799]: Nfkb1; NbExp=3; IntAct=EBI-644400, EBI-1209193;
CC Q04207; Q9WTK5: Nfkb2; NbExp=3; IntAct=EBI-644400, EBI-1209166;
CC Q04207; Q9Z1E3: Nfkbia; NbExp=9; IntAct=EBI-644400, EBI-644427;
CC Q04207; Q60778: Nfkbib; NbExp=12; IntAct=EBI-644400, EBI-644469;
CC Q04207; P29477: Nos2; NbExp=3; IntAct=EBI-644400, EBI-298897;
CC Q04207; Q62227: Nr0b2; NbExp=3; IntAct=EBI-644400, EBI-4310440;
CC Q04207; P12813: Nr4a1; NbExp=2; IntAct=EBI-644400, EBI-10896863;
CC Q04207; Q06219: Nr4a2; NbExp=2; IntAct=EBI-644400, EBI-2337255;
CC Q04207; Q04207: Rela; NbExp=2; IntAct=EBI-644400, EBI-644400;
CC Q04207; Q9H9B1: EHMT1; Xeno; NbExp=5; IntAct=EBI-644400, EBI-766087;
CC Q04207; Q8TBK2: SETD6; Xeno; NbExp=4; IntAct=EBI-644400, EBI-3863032;
CC Q04207; Q8WTS6: SETD7; Xeno; NbExp=2; IntAct=EBI-644400, EBI-1268586;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21131967,
CC ECO:0000269|PubMed:28378844}. Cytoplasm {ECO:0000269|PubMed:21131967}.
CC Note=Nuclear, but also found in the cytoplasm in an inactive form
CC complexed to an inhibitor (I-kappa-B) (PubMed:21131967). Colocalized
CC with DDX1 in the nucleus upon TNF-alpha induction (By similarity).
CC Colocalizes with GFI1 in the nucleus after lipopolysaccharide (LPS)
CC stimulation. {ECO:0000250|UniProtKB:Q04206,
CC ECO:0000269|PubMed:21131967}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=p65;
CC IsoId=Q04207-1; Sequence=Displayed;
CC Name=p65 delta;
CC IsoId=Q04207-2; Sequence=VSP_005589;
CC -!- DOMAIN: The transcriptional activation domain 3/TA3 does not
CC participate in the direct transcriptional activity of RELA but is
CC involved in the control by RELA of the accessibility of target gene
CC promoters. Mediates interaction with ZBTB7A.
CC {ECO:0000269|PubMed:29813070}.
CC -!- DOMAIN: The transcriptional activation domain 1/TA1 and the
CC transcriptional activation domain 2/TA2 have direct transcriptional
CC activation properties (PubMed:29813070). The 9aaTAD motif found within
CC the transcriptional activation domain 2 is a conserved motif present in
CC a large number of transcription factors that is required for their
CC transcriptional transactivation activity (By similarity).
CC {ECO:0000250|UniProtKB:Q04206, ECO:0000269|PubMed:29813070}.
CC -!- PTM: Ubiquitinated by MKRN2, leading to its proteasomal degradation
CC (PubMed:28378844). Degradation is required for termination of NF-kappa-
CC B response (By similarity). {ECO:0000250|UniProtKB:Q04206,
CC ECO:0000269|PubMed:28378844}.
CC -!- PTM: Monomethylated at Lys-310 by SETD6. Monomethylation at Lys-310 is
CC recognized by the ANK repeats of EHMT1 and promotes the formation of
CC repressed chromatin at target genes, leading to down-regulation of NF-
CC kappa-B transcription factor activity. Phosphorylation at Ser-311
CC disrupts the interaction with EHMT1 without preventing monomethylation
CC at Lys-310 and relieves the repression of target genes.
CC {ECO:0000269|PubMed:12881425, ECO:0000269|PubMed:21131967}.
CC -!- PTM: Phosphorylation on Ser-534 stimulates acetylation on Lys-310 and
CC interaction with CBP; the phosphorylated and acetylated forms show
CC enhanced transcriptional activity (By similarity). Phosphorylation at
CC Ser-311 disrupts the interaction with EHMT1 and promotes transcription
CC factor activity. Phosphorylation at Ser-276 by RPS6KA4 and RPS6KA5
CC promotes its transactivation and transcriptional activities.
CC {ECO:0000250, ECO:0000269|PubMed:12881425,
CC ECO:0000269|PubMed:21131967}.
CC -!- PTM: Reversibly acetylated; the acetylation seems to be mediated by
CC CBP, the deacetylation by HDAC3 and SIRT2. Acetylation at Lys-122
CC enhances DNA binding and impairs association with NFKBIA. Acetylation
CC at Lys-310 is required for full transcriptional activity in the absence
CC of effects on DNA binding and NFKBIA association. Acetylation at Lys-
CC 310 promotes interaction with BRD4. Acetylation can also lower DNA-
CC binding and results in nuclear export. Interaction with BRMS1 promotes
CC deacetylation of Lys-310. Lys-310 is deacetylated by SIRT2 (By
CC similarity). {ECO:0000250}.
CC -!- PTM: S-nitrosylation of Cys-38 inactivates the enzyme activity.
CC {ECO:0000269|PubMed:22244329}.
CC -!- PTM: Sulfhydration at Cys-38 mediates the anti-apoptotic activity by
CC promoting the interaction with RPS3 and activating the transcription
CC factor activity.
CC -!- PTM: Sumoylation by PIAS3 negatively regulates DNA-bound activated NF-
CC kappa-B. {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved within a conserved N-terminus region
CC required for base-specific contact with DNA in a CPEN1-mediated manner,
CC and hence inhibits NF-kappa-B transcriptional activity.
CC {ECO:0000250|UniProtKB:Q04206}.
CC -!- DISRUPTION PHENOTYPE: RELA haploinsufficient mice show cutaneous
CC ulceration, epidermal skin loss and a predominance of neutrophils and
CC macrophages in the dermis and hypodermis in response to TNF treatment.
CC {ECO:0000269|PubMed:28600438}.
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DR EMBL; M61909; AAA39811.1; -; mRNA.
DR EMBL; BC003818; AAH03818.1; -; mRNA.
DR EMBL; L77155; AAB00795.1; -; Genomic_DNA.
DR EMBL; Z22952; CAA80528.1; -; Genomic_DNA.
DR CCDS; CCDS29473.1; -. [Q04207-1]
DR PIR; A37932; A37932.
DR PIR; PC4233; PC4233.
DR PIR; S48113; S48113.
DR RefSeq; NP_033071.1; NM_009045.4. [Q04207-1]
DR PDB; 1BFT; X-ray; 2.00 A; A/B=191-291.
DR PDB; 1IKN; X-ray; 2.30 A; A=19-304.
DR PDB; 1K3Z; X-ray; 2.50 A; A/B=191-326.
DR PDB; 1LE5; X-ray; 2.75 A; A/E=20-291.
DR PDB; 1LE9; X-ray; 3.00 A; A/E=20-291.
DR PDB; 1LEI; X-ray; 2.70 A; A=20-291.
DR PDB; 1MY5; X-ray; 1.80 A; A/B=191-304.
DR PDB; 1MY7; X-ray; 1.49 A; A/B=191-304.
DR PDB; 1OY3; X-ray; 2.05 A; B/C=191-326.
DR PDB; 1RAM; X-ray; 2.70 A; A/B=19-291.
DR PDB; 1VKX; X-ray; 2.90 A; A=20-291.
DR PDB; 2I9T; X-ray; 2.80 A; A=19-291.
DR PDB; 2LWW; NMR; -; B=425-490.
DR PDB; 2RAM; X-ray; 2.40 A; A/B=19-291.
DR PDB; 5U01; X-ray; 2.50 A; A/B/C/D=19-291.
DR PDB; 6GGR; X-ray; 2.10 A; A=20-188.
DR PDBsum; 1BFT; -.
DR PDBsum; 1IKN; -.
DR PDBsum; 1K3Z; -.
DR PDBsum; 1LE5; -.
DR PDBsum; 1LE9; -.
DR PDBsum; 1LEI; -.
DR PDBsum; 1MY5; -.
DR PDBsum; 1MY7; -.
DR PDBsum; 1OY3; -.
DR PDBsum; 1RAM; -.
DR PDBsum; 1VKX; -.
DR PDBsum; 2I9T; -.
DR PDBsum; 2LWW; -.
DR PDBsum; 2RAM; -.
DR PDBsum; 5U01; -.
DR PDBsum; 6GGR; -.
DR AlphaFoldDB; Q04207; -.
DR BMRB; Q04207; -.
DR SMR; Q04207; -.
DR BioGRID; 202853; 38.
DR CORUM; Q04207; -.
DR DIP; DIP-6219N; -.
DR IntAct; Q04207; 36.
DR MINT; Q04207; -.
DR STRING; 10090.ENSMUSP00000025867; -.
DR BindingDB; Q04207; -.
DR ChEMBL; CHEMBL5902; -.
DR iPTMnet; Q04207; -.
DR PhosphoSitePlus; Q04207; -.
DR EPD; Q04207; -.
DR MaxQB; Q04207; -.
DR PaxDb; Q04207; -.
DR PeptideAtlas; Q04207; -.
DR PRIDE; Q04207; -.
DR ProteomicsDB; 258860; -. [Q04207-1]
DR ProteomicsDB; 258861; -. [Q04207-2]
DR ABCD; Q04207; 3 sequenced antibodies.
DR Antibodypedia; 3557; 3912 antibodies from 51 providers.
DR DNASU; 19697; -.
DR Ensembl; ENSMUST00000025867; ENSMUSP00000025867; ENSMUSG00000024927. [Q04207-1]
DR GeneID; 19697; -.
DR KEGG; mmu:19697; -.
DR UCSC; uc008gee.1; mouse. [Q04207-1]
DR CTD; 5970; -.
DR MGI; MGI:103290; Rela.
DR VEuPathDB; HostDB:ENSMUSG00000024927; -.
DR eggNOG; ENOG502QT4Z; Eukaryota.
DR GeneTree; ENSGT00940000159867; -.
DR HOGENOM; CLU_004343_5_1_1; -.
DR InParanoid; Q04207; -.
DR OMA; PVRVHMQ; -.
DR OrthoDB; 916931at2759; -.
DR PhylomeDB; Q04207; -.
DR TreeFam; TF325632; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1810476; RIP-mediated NFkB activation via ZBP1.
DR Reactome; R-MMU-193692; Regulated proteolysis of p75NTR.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-209560; NF-kB is activated and signals survival.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR Reactome; R-MMU-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-MMU-448706; Interleukin-1 processing.
DR Reactome; R-MMU-4755510; SUMOylation of immune response proteins.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-933542; TRAF6 mediated NF-kB activation.
DR BioGRID-ORCS; 19697; 14 hits in 81 CRISPR screens.
DR ChiTaRS; Rela; mouse.
DR EvolutionaryTrace; Q04207; -.
DR PRO; PR:Q04207; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q04207; protein.
DR Bgee; ENSMUSG00000024927; Expressed in thoracic mammary gland and 288 other tissues.
DR ExpressionAtlas; Q04207; baseline and differential.
DR Genevisible; Q04207; MM.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0071159; C:NF-kappaB complex; ISO:MGI.
DR GO; GO:0035525; C:NF-kappaB p50/p65 complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0042805; F:actinin binding; IPI:UniProtKB.
DR GO; GO:0071532; F:ankyrin repeat binding; IPI:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0140296; F:general transcription initiation factor binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051059; F:NF-kappaB binding; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0042301; F:phosphate ion binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:1904385; P:cellular response to angiotensin; ISO:MGI.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IDA:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISO:MGI.
DR GO; GO:0071354; P:cellular response to interleukin-6; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB.
DR GO; GO:0071223; P:cellular response to lipoteichoic acid; ISO:MGI.
DR GO; GO:0071316; P:cellular response to nicotine; ISO:MGI.
DR GO; GO:0071224; P:cellular response to peptidoglycan; ISO:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IMP:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:0006952; P:defense response; IMP:MGI.
DR GO; GO:0002357; P:defense response to tumor cell; ISO:MGI.
DR GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISO:MGI.
DR GO; GO:0001889; P:liver development; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:MGI.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; ISO:MGI.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:MGI.
DR GO; GO:0033234; P:negative regulation of protein sumoylation; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISO:MGI.
DR GO; GO:0038061; P:NIK/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; ISO:MGI.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; IDA:ARUK-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:MGI.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; ISO:MGI.
DR GO; GO:2000630; P:positive regulation of miRNA metabolic process; ISO:MGI.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0014040; P:positive regulation of Schwann cell differentiation; ISO:MGI.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; IDA:SynGO.
DR GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR GO; GO:0043620; P:regulation of DNA-templated transcription in response to stress; ISO:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; IDA:UniProtKB.
DR GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IDA:MGI.
DR GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
DR GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
DR GO; GO:0032495; P:response to muramyl dipeptide; IDA:MGI.
DR GO; GO:0035994; P:response to muscle stretch; IDA:MGI.
DR GO; GO:0010033; P:response to organic substance; ISO:MGI.
DR GO; GO:0010224; P:response to UV-B; ISO:MGI.
DR GO; GO:0006351; P:transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR CDD; cd01177; IPT_NFkappaB; 1.
DR DisProt; DP00129; -.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.340; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR033926; IPT_NFkappaB.
DR InterPro; IPR000451; NFkB/Dor.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR030495; RelA.
DR InterPro; IPR030492; RHD_CS.
DR InterPro; IPR032397; RHD_dimer.
DR InterPro; IPR011539; RHD_DNA_bind_dom.
DR InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR PANTHER; PTHR24169; PTHR24169; 1.
DR PANTHER; PTHR24169:SF1; PTHR24169:SF1; 1.
DR Pfam; PF16179; RHD_dimer; 1.
DR Pfam; PF00554; RHD_DNA_bind; 1.
DR PRINTS; PR00057; NFKBTNSCPFCT.
DR SMART; SM00429; IPT; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS01204; REL_1; 1.
DR PROSITE; PS50254; REL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; Cytoplasm;
KW DNA-binding; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; S-nitrosylation; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..549
FT /note="Transcription factor p65"
FT /id="PRO_0000205170"
FT DOMAIN 19..306
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT REGION 41..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..390
FT /note="Transcriptional activation domain 3"
FT /evidence="ECO:0000269|PubMed:29813070"
FT REGION 407..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..475
FT /note="Transcriptional activation domain 1"
FT /evidence="ECO:0000269|PubMed:29813070"
FT REGION 504..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..549
FT /note="Transcriptional activation domain 2"
FT /evidence="ECO:0000269|PubMed:29813070"
FT MOTIF 301..304
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 534..542
FT /note="9aaTAD"
FT /evidence="ECO:0000255"
FT COMPBIAS 332..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q04206"
FT MOD_RES 38
FT /note="Cysteine persulfide; alternate"
FT /evidence="ECO:0000269|PubMed:22244329"
FT MOD_RES 38
FT /note="S-nitrosocysteine; alternate"
FT /evidence="ECO:0000269|PubMed:22244329"
FT MOD_RES 122
FT /note="N6-acetyllysine; by PCAF and EP300; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04206"
FT MOD_RES 123
FT /note="N6-acetyllysine; by PCAF and EP300; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04206"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 218
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q04206"
FT MOD_RES 221
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q04206"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04206"
FT MOD_RES 276
FT /note="Phosphoserine; by RPS6KA4 and RPS6KA5"
FT /evidence="ECO:0000250|UniProtKB:Q04206"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04206"
FT MOD_RES 310
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 310
FT /note="N6-methyllysine; by SETD6; alternate"
FT /evidence="ECO:0000269|PubMed:21131967"
FT MOD_RES 311
FT /note="Phosphoserine; by PKC/PRKCZ"
FT /evidence="ECO:0000269|PubMed:12881425,
FT ECO:0000269|PubMed:21131967"
FT MOD_RES 433
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04206"
FT MOD_RES 467
FT /note="Phosphoserine; by IKKB and IKKE"
FT /evidence="ECO:0000250|UniProtKB:Q04206"
FT MOD_RES 504
FT /note="Phosphothreonine; by CHEK1"
FT /evidence="ECO:0000250|UniProtKB:Q04206"
FT MOD_RES 527
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q04206"
FT MOD_RES 534
FT /note="Phosphoserine; by IKKB"
FT /evidence="ECO:0000250|UniProtKB:Q04206"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO3)"
FT /evidence="ECO:0000250"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO3); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO3); alternate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 222..231
FT /note="Missing (in isoform p65 delta)"
FT /evidence="ECO:0000305"
FT /id="VSP_005589"
FT MUTAGEN 38
FT /note="C->S: Abolishes sulfhydration and impairs
FT interaction with RPS3."
FT /evidence="ECO:0000269|PubMed:22244329"
FT MUTAGEN 281
FT /note="S->A,E: Abolishes DNA-binding and transcriptional
FT activity."
FT /evidence="ECO:0000269|PubMed:12874295"
FT MUTAGEN 310
FT /note="K->R: Abolishes monomethylation by SETD6 and
FT interaction with EHMT1."
FT /evidence="ECO:0000269|PubMed:21131967"
FT MUTAGEN 361..370
FT /note="DEFSPMLLPS->AAAAAAAAAA: Loss of interaction with
FT ZBTB7A."
FT /evidence="ECO:0000269|PubMed:29813070"
FT CONFLICT 28
FT /note="K -> N (in Ref. 3; AAB00795)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="I -> IQKD (in Ref. 3; AAB00795)"
FT /evidence="ECO:0000305"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:6GGR"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:6GGR"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:6GGR"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:5U01"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2RAM"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:6GGR"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:6GGR"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:6GGR"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:6GGR"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:6GGR"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:6GGR"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6GGR"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:6GGR"
FT HELIX 126..135
FT /evidence="ECO:0007829|PDB:6GGR"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:6GGR"
FT STRAND 156..166
FT /evidence="ECO:0007829|PDB:6GGR"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:5U01"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:6GGR"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:6GGR"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1VKX"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:2RAM"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:1MY7"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1MY7"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:1MY7"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:1BFT"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:1MY7"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:1MY7"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:1MY7"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:1MY7"
FT STRAND 266..274
FT /evidence="ECO:0007829|PDB:1MY7"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:1MY7"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:1MY7"
FT HELIX 294..304
FT /evidence="ECO:0007829|PDB:1OY3"
FT HELIX 306..315
FT /evidence="ECO:0007829|PDB:1OY3"
FT HELIX 433..439
FT /evidence="ECO:0007829|PDB:2LWW"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:2LWW"
FT TURN 450..453
FT /evidence="ECO:0007829|PDB:2LWW"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:2LWW"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:2LWW"
FT HELIX 471..477
FT /evidence="ECO:0007829|PDB:2LWW"
FT STRAND 480..484
FT /evidence="ECO:0007829|PDB:2LWW"
SQ SEQUENCE 549 AA; 60212 MW; BDF1673D2FE398B9 CRC64;
MDDLFPLIFP SEPAQASGPY VEIIEQPKQR GMRFRYKCEG RSAGSIPGER STDTTKTHPT
IKINGYTGPG TVRISLVTKD PPHRPHPHEL VGKDCRDGYY EADLCPDRSI HSFQNLGIQC
VKKRDLEQAI SQRIQTNNNP FHVPIEEQRG DYDLNAVRLC FQVTVRDPAG RPLLLTPVLS
HPIFDNRAPN TAELKICRVN RNSGSCLGGD EIFLLCDKVQ KEDIEVYFTG PGWEARGSFS
QADVHRQVAI VFRTPPYADP SLQAPVRVSM QLRRPSDREL SEPMEFQYLP DTDDRHRIEE
KRKRTYETFK SIMKKSPFNG PTEPRPPTRR IAVPTRNSTS VPKPAPQPYT FPASLSTINF
DEFSPMLLPS GQISNQALAL APSSAPVLAQ TMVPSSAMVP LAQPPAPAPV LTPGPPQSLS
APVPKSTQAG EGTLSEALLH LQFDADEDLG ALLGNSTDPG VFTDLASVDN SEFQQLLNQG
VSMSHSTAEP MLMEYPEAIT RLVTGSQRPP DPAPTPLGTS GLPNGLSGDE DFSSIADMDF
SALLSQISS
