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Transcription factor p65 (Nuclear factor NF-kappa-B p65 subunit) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3)

 TF65_HUMAN              Reviewed;         551 AA.
Q04206; Q6GTV1; Q6SLK1;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 2.
30-AUG-2017, entry version 210.
RecName: Full=Transcription factor p65;
AltName: Full=Nuclear factor NF-kappa-B p65 subunit;
AltName: Full=Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3;
Name=RELA; Synonyms=NFKB3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2006423; DOI=10.1126/science.2006423;
Ruben S.M., Dillon P.J., Schreck R., Henkel T., Chen C.-H., Maher M.,
Baeuerle P.A., Rosen C.A.;
"Isolation of a rel-related human cDNA that potentially encodes the
65-kD subunit of NF-kappa B.";
Science 251:1490-1493(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
PubMed=8281153; DOI=10.1093/hmg/2.11.1895;
Deloukas P., van Loon A.P.G.M.;
"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.";
Hum. Mol. Genet. 2:1895-1900(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Bone;
PubMed=7907305; DOI=10.1016/0378-1119(94)90823-0;
Lyle R., Valleley E.M., Sharpe P.T., Hewitt J.E.;
"An alternatively spliced transcript, p65 delta 2, of the gene
encoding the p65 subunit of the transcription factor NF-kappa B.";
Gene 138:265-266(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-551.
SeattleSNPs variation discovery resource;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 214-239 (ISOFORMS 1/2 AND 3), AND
ACTIVATION DOMAIN.
PubMed=1732726; DOI=10.1128/MCB.12.2.444;
Ruben S.M., Narayanan R., Klement J.F., Chen C.-H., Rosen C.A.;
"Functional characterization of the NF-kappa B p65 transcriptional
activator and an alternatively spliced derivative.";
Mol. Cell. Biol. 12:444-454(1992).
[7]
IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX, AND IDENTIFICATION
IN THE NF-KAPPA-B P65-C-REL COMPLEX.
PubMed=1740106;
Hansen S.K., Nerlov C., Zabel U., Verde P., Johnsen M., Baeuerle P.A.,
Blasi F.;
"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.";
EMBO J. 11:205-213(1992).
[8]
INTERACTION WITH NFKBIA.
PubMed=1493333; DOI=10.1091/mbc.3.12.1339;
Ganchi P.A., Sun S.C., Greene W.C., Ballard D.W.;
"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.";
Mol. Biol. Cell 3:1339-1352(1992).
[9]
IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX, AND IDENTIFICATION
IN THE NF-KAPPA-B P65-P52 COMPLEX.
PubMed=8152812;
Beg A.A., Baldwin A.S. Jr.;
"Activation of multiple NF-kappa B/Rel DNA-binding complexes by tumor
necrosis factor.";
Oncogene 9:1487-1492(1994).
[10]
IDENTIFICATION IN THE NF-KAPPA-B P65-P65 COMPLEX, AND IDENTIFICATION
IN THE NF-KAPPA-B P65-C-REL COMPLEX.
PubMed=9056676;
Aoudjit F., Brochu N., Belanger B., Stratowa C., Hiscott J.,
Audette M.;
"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.";
Cell Growth Differ. 8:335-342(1997).
[11]
INTERACTION WITH NFKBIE.
PubMed=9315679; DOI=10.1128/MCB.17.10.6184;
Li Z., Nabel G.J.;
"A new member of the IkappaB protein family, IkappaB epsilon, inhibits
RelA (p65)-mediated NF-kappaB transcription.";
Mol. Cell. Biol. 17:6184-6190(1997).
[12]
IDENTIFICATION IN A COMPLEX WITH CHUK; IKBKB; NFKBIA; IKBKAP AND
MAP3K14.
PubMed=9751059; DOI=10.1038/26254;
Cohen L., Henzel W.J., Baeuerle P.A.;
"IKAP is a scaffold protein of the IkappaB kinase complex.";
Nature 395:292-296(1998).
[13]
PHOSPHORYLATION AT SER-536.
PubMed=10521409; DOI=10.1074/jbc.274.43.30353;
Sakurai H., Chiba H., Miyoshi H., Sugita T., Toriumi W.;
"IkappaB kinases phosphorylate NF-kappaB p65 subunit on serine 536 in
the transactivation domain.";
J. Biol. Chem. 274:30353-30356(1999).
[14]
TISSUE SPECIFICITY, AND INTERACTION WITH TP53BP2.
PubMed=10498867; DOI=10.1038/sj.onc.1202904;
Yang J.-P., Hori M., Takahashi N., Kawabe T., Kato H., Okamoto T.;
"NF-kappaB subunit p65 binds to 53BP2 and inhibits cell death induced
by 53BP2.";
Oncogene 18:5177-5186(1999).
[15]
FUNCTION, AND IDENTIFICATION IN THE NF-KAPPA-B P65-P65 COMPLEX.
PubMed=10928981; DOI=10.1096/fj.14.11.1471;
Schulte R., Grassl G.A., Preger S., Fessele S., Jacobi C.A.,
Schaller M., Nelson P.J., Autenrieth I.B.;
"Yersinia enterocolitica invasin protein triggers IL-8 production in
epithelial cells via activation of Rel p65-p65 homodimers.";
FASEB J. 14:1471-1484(2000).
[16]
INTERACTION WITH AES AND TLE1.
PubMed=10660609; DOI=10.1074/jbc.275.6.4383;
Tetsuka T., Uranishi H., Imai H., Ono T., Sonta S., Takahashi N.,
Asamitsu K., Okamoto T.;
"Inhibition of nuclear factor-kappaB-mediated transcription by
association with the amino-terminal enhancer of split, a Groucho-
related protein lacking WD40 repeats.";
J. Biol. Chem. 275:4383-4390(2000).
[17]
PHOSPHORYLATION AT SER-529.
PubMed=10938077; DOI=10.1074/jbc.M001358200;
Wang D., Westerheide S.D., Hanson J.L., Baldwin A.S. Jr.;
"Tumor necrosis factor alpha-induced phosphorylation of RelA/p65 on
Ser529 is controlled by casein kinase II.";
J. Biol. Chem. 275:32592-32597(2000).
[18]
INTERACTION WITH MEN1.
PubMed=11526476; DOI=10.1038/sj.onc.1204529;
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.;
"The tumor suppressor protein menin interacts with NF-kappaB proteins
and inhibits NF-kappaB-mediated transactivation.";
Oncogene 20:4917-4925(2001).
[19]
ACETYLATION, AND INTERACTION WITH HDAC3.
PubMed=11533489; DOI=10.1126/science.1062374;
Chen L.F., Fischle W., Verdin E., Greene W.C.;
"Duration of nuclear NF-kappaB action regulated by reversible
acetylation.";
Science 293:1653-1657(2001).
[20]
INTERACTION WITH ETHE1.
PubMed=12398897; DOI=10.1016/S1535-6108(02)00152-6;
Higashitsuji H., Higashitsuji H., Nagao T., Nonoguchi K., Fujii S.,
Itoh K., Fujita J.;
"A novel protein overexpressed in hepatoma accelerates export of NF-
kappa B from the nucleus and inhibits p53-dependent apoptosis.";
Cancer Cell 2:335-346(2002).
[21]
ACETYLATION AT LYS-218; LYS-221 AND LYS-310.
PubMed=12456660; DOI=10.1093/emboj/cdf660;
Chen L.F., Mu Y., Greene W.C.;
"Acetylation of RelA at discrete sites regulates distinct nuclear
functions of NF-kappaB.";
EMBO J. 21:6539-6548(2002).
[22]
INTERACTION WITH CBP AND HDAC1, AND PHOSPHORYLATION.
PubMed=11931769; DOI=10.1016/S1097-2765(02)00477-X;
Zhong H., May M.J., Jimi E., Ghosh S.;
"The phosphorylation status of nuclear NF-kappa B determines its
association with CBP/p300 or HDAC-1.";
Mol. Cell 9:625-636(2002).
[23]
INTERACTION WITH RPS6KA5, MUTAGENESIS OF SER-276, AND PHOSPHORYLATION
AT SER-276.
PubMed=12628924; DOI=10.1093/emboj/cdg139;
Vermeulen L., De Wilde G., Van Damme P., Vanden Berghe W.,
Haegeman G.;
"Transcriptional activation of the NF-kappaB p65 subunit by
mitogen- and stress-activated protein kinase-1 (MSK1).";
EMBO J. 22:1313-1324(2003).
[24]
ACETYLATION AT LYS-122 AND LYS-123.
PubMed=12419806; DOI=10.1074/jbc.M209572200;
Kiernan R., Bres V., Ng R.W., Coudart M.-P., El Messaoudi S.,
Sardet C., Jin D.-Y., Emiliani S., Benkirane M.;
"Post-activation turn-off of NF-kappa B-dependent transcription is
regulated by acetylation of p65.";
J. Biol. Chem. 278:2758-2766(2003).
[25]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RNF25.
PubMed=12748188; DOI=10.1074/jbc.M211831200;
Asamitsu K., Tetsuka T., Kanazawa S., Okamoto T.;
"RING finger protein AO7 supports NF-kappaB-mediated transcription by
interacting with the transactivation domain of the p65 subunit.";
J. Biol. Chem. 278:26879-26887(2003).
[26]
INTERACTION WITH GSK3B.
PubMed=12871932; DOI=10.1074/jbc.M305676200;
Demarchi F., Bertoli C., Sandy P., Schneider C.;
"Glycogen synthase kinase-3 beta regulates NF-kappa B1/p105
stability.";
J. Biol. Chem. 278:39583-39590(2003).
[27]
PHOSPHORYLATION AT THR-254, INTERACTION WITH PIN1 AND SOCS1, AND
MUTAGENESIS OF THR-254.
PubMed=14690596; DOI=10.1016/S1097-2765(03)00490-8;
Ryo A., Suizu F., Yoshida Y., Perrem K., Liou Y.C., Wulf G.,
Rottapel R., Yamaoka S., Lu K.P.;
"Regulation of NF-kappaB signaling by Pin1-dependent prolyl
isomerization and ubiquitin-mediated proteolysis of p65/RelA.";
Mol. Cell 12:1413-1426(2003).
[28]
INTERACTION WITH UNC5CL.
PubMed=14769797; DOI=10.1074/jbc.M310737200;
Zhang J., Xu L.-G., Han K.-J., Shu H.-B.;
"Identification of a ZU5 and death domain-containing inhibitor of NF-
kappaB.";
J. Biol. Chem. 279:17819-17825(2004).
[29]
PHOSPHORYLATION AT THR-435.
PubMed=15073167; DOI=10.1074/jbc.M402362200;
Yeh P.Y., Yeh K.H., Chuang S.E., Song Y.C., Cheng A.L.;
"Suppression of MEK/ERK signaling pathway enhances cisplatin-induced
NF-kappaB activation by protein phosphatase 4-mediated NF-kappaB p65
Thr dephosphorylation.";
J. Biol. Chem. 279:26143-26148(2004).
[30]
UBIQUITINATION.
PubMed=15226358; DOI=10.1084/jem.20040196;
Saccani S., Marazzi I., Beg A.A., Natoli G.;
"Degradation of promoter-bound p65/RelA is essential for the prompt
termination of the nuclear factor kappaB response.";
J. Exp. Med. 200:107-113(2004).
[31]
INTERACTION WITH ARRB2.
PubMed=15125834; DOI=10.1016/S1097-2765(04)00216-3;
Gao H., Sun Y., Wu Y., Luan B., Wang Y., Qu B., Pei G.;
"Identification of beta-arrestin2 as a G protein-coupled receptor-
stimulated regulator of NF-kappaB pathways.";
Mol. Cell 14:303-317(2004).
[32]
INTERACTION WITH ING4.
PubMed=15029197; DOI=10.1038/nature02329;
Garkavtsev I., Kozin S.V., Chernova O., Xu L., Winkler F., Brown E.,
Barnett G.H., Jain R.K.;
"The candidate tumour suppressor protein ING4 regulates brain tumour
growth and angiogenesis.";
Nature 428:328-332(2004).
[33]
PHOSPHORYLATION AT THR-505.
PubMed=15775976; DOI=10.1038/sj.emboj.7600608;
Rocha S., Garrett M.D., Campbell K.J., Schumm K., Perkins N.D.;
"Regulation of NF-kappaB and p53 through activation of ATR and Chk1 by
the ARF tumour suppressor.";
EMBO J. 24:1157-1169(2005).
[34]
PHOSPHORYLATION AT SER-468.
PubMed=16046471; DOI=10.1096/fj.05-3736fje;
Schwabe R.F., Sakurai H.;
"IKKbeta phosphorylates p65 at S468 in transactivation domain 2.";
FASEB J. 19:1758-1760(2005).
[35]
PHOSPHORYLATION AT SER-281.
PubMed=15516339; DOI=10.1074/jbc.M409344200;
Anrather J., Racchumi G., Iadecola C.;
"cis-acting, element-specific transcriptional activity of
differentially phosphorylated nuclear factor-kappa B.";
J. Biol. Chem. 280:244-252(2005).
[36]
INTERACTION WITH COMMD1, AND SUBCELLULAR LOCATION.
PubMed=15799966; DOI=10.1074/jbc.M501928200;
Burstein E., Hoberg J.E., Wilkinson A.S., Rumble J.M., Csomos R.A.,
Komarck C.M., Maine G.N., Wilkinson J.C., Mayo M.W., Duckett C.S.;
"COMMD proteins, a novel family of structural and functional homologs
of MURR1.";
J. Biol. Chem. 280:22222-22232(2005).
[37]
ACETYLATION AT LYS-310.
PubMed=16135789; DOI=10.1128/MCB.25.18.7966-7975.2005;
Chen L.F., Williams S.A., Mu Y., Nakano H., Duerr J.M., Buckbinder L.,
Greene W.C.;
"NF-kappaB RelA phosphorylation regulates RelA acetylation.";
Mol. Cell. Biol. 25:7966-7975(2005).
[38]
FUNCTION, AND INTERACTION WITH FOXP3.
PubMed=15790681; DOI=10.1073/pnas.0501675102;
Bettelli E., Dastrange M., Oukka M.;
"Foxp3 interacts with nuclear factor of activated T cells and NF-kappa
B to repress cytokine gene expression and effector functions of T
helper cells.";
Proc. Natl. Acad. Sci. U.S.A. 102:5138-5143(2005).
[39]
INTERACTION WITH HRSV PROTEIN M2-1.
PubMed=15629770; DOI=10.1016/j.virol.2004.10.031;
Reimers K., Buchholz K., Werchau H.;
"Respiratory syncytial virus M2-1 protein induces the activation of
nuclear factor kappa B.";
Virology 331:260-268(2005).
[40]
INTERACTION WITH MTDH.
PubMed=16452207; DOI=10.1158/0008-5472.CAN-05-3029;
Emdad L., Sarkar D., Su Z.-Z., Randolph A., Boukerche H., Valerie K.,
Fisher P.B.;
"Activation of the nuclear factor kappaB pathway by astrocyte elevated
gene-1: implications for tumor progression and metastasis.";
Cancer Res. 66:1509-1516(2006).
[41]
INTERACTION WITH USP48.
PubMed=16214042; DOI=10.1016/j.cellsig.2005.03.017;
Tzimas C., Michailidou G., Arsenakis M., Kieff E., Mosialos G.,
Hatzivassiliou E.G.;
"Human ubiquitin specific protease 31 is a deubiquitinating enzyme
implicated in activation of nuclear factor-kappaB.";
Cell. Signal. 18:83-92(2006).
[42]
PHOSPHORYLATION AT SER-468.
PubMed=16407239; DOI=10.1074/jbc.M508045200;
Mattioli I., Geng H., Sebald A., Hodel M., Bucher C., Kracht M.,
Schmitz M.L.;
"Inducible phosphorylation of NF-kappa B p65 at serine 468 by T cell
costimulation is mediated by IKK epsilon.";
J. Biol. Chem. 281:6175-6183(2006).
[43]
INTERACTION WITH BRMS1, FUNCTION, AND ACETYLATION AT LYS-310.
PubMed=17000776; DOI=10.1128/MCB.00940-06;
Liu Y., Smith P.W., Jones D.R.;
"Breast cancer metastasis suppressor 1 functions as a corepressor by
enhancing histone deacetylase 1-mediated deacetylation of RelA/p65 and
promoting apoptosis.";
Mol. Cell. Biol. 26:8683-8696(2006).
[44]
INTERACTION WITH CARM1.
PubMed=16497732; DOI=10.1210/me.2005-0365;
Miao F., Li S., Chavez V., Lanting L., Natarajan R.;
"Coactivator-associated arginine methyltransferase-1 enhances nuclear
factor-kappaB-mediated gene transcription through methylation of
histone H3 at arginine 17.";
Mol. Endocrinol. 20:1562-1573(2006).
[45]
IDENTIFICATION IN THE NF-KAPPA-B P65-P52 COMPLEX.
PubMed=16477006; DOI=10.1073/pnas.0511096103;
Song Y.J., Jen K.Y., Soni V., Kieff E., Cahir-McFarland E.;
"IL-1 receptor-associated kinase 1 is critical for latent membrane
protein 1-induced p65/RelA serine 536 phosphorylation and NF-kappaB
activation.";
Proc. Natl. Acad. Sci. U.S.A. 103:2689-2694(2006).
[46]
INTERACTION WITH CDK5RAP3; HDAC1; HDAC2 AND HADC3, AND PHOSPHORYLATION
AT SER-536.
PubMed=17785205; DOI=10.1016/j.ccr.2007.07.002;
Wang J., An H., Mayo M.W., Baldwin A.S., Yarbrough W.G.;
"LZAP, a putative tumor suppressor, selectively inhibits NF-kappaB.";
Cancer Cell 12:239-251(2007).
[47]
DOMAIN.
PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P.,
Piskacek M.;
"Nine-amino-acid transactivation domain: establishment and prediction
utilities.";
Genomics 89:756-768(2007).
[48]
FUNCTION, AND INTERACTION WITH UXT.
PubMed=17620405; DOI=10.1083/jcb.200611081;
Sun S., Tang Y., Lou X., Zhu L., Yang K., Zhang B., Shi H., Wang C.;
"UXT is a novel and essential cofactor in the NF-kappaB
transcriptional enhanceosome.";
J. Cell Biol. 178:231-244(2007).
[49]
INTERACTION WITH MEFV.
PubMed=18577712; DOI=10.1182/blood-2008-01-134932;
Chae J.J., Wood G., Richard K., Jaffe H., Colburn N.T., Masters S.L.,
Gumucio D.L., Shoham N.G., Kastner D.L.;
"The familial Mediterranean fever protein, pyrin, is cleaved by
caspase-1 and activates NF-kappaB through its N-terminal fragment.";
Blood 112:1794-1803(2008).
[50]
INTERACTION WITH PHF11.
PubMed=18405956; DOI=10.1016/j.jaci.2008.02.028;
Clarke E., Rahman N., Page N., Rolph M.S., Stewart G.J., Jones G.J.;
"Functional characterization of the atopy-associated gene PHF11.";
J. Allergy Clin. Immunol. 121:1148-1154(2008).
[51]
INTERACTION WITH AKIP1.
PubMed=18178962; DOI=10.1074/jbc.M710285200;
Gao N., Asamitsu K., Hibi Y., Ueno T., Okamoto T.;
"AKIP1 enhances NF-kappaB-dependent gene expression by promoting the
nuclear retention and phosphorylation of p65.";
J. Biol. Chem. 283:7834-7843(2008).
[52]
INTERACTION WITH CPEN1, AND PROTEOLYTIC CLEAVAGE.
PubMed=18212740; DOI=10.1038/sj.onc.1211030;
Ramsey C.S., Yeung F., Stoddard P.B., Li D., Creutz C.E., Mayo M.W.;
"Copine-I represses NF-kappaB transcription by endoproteolysis of
p65.";
Oncogene 27:3516-3526(2008).
[53]
FUNCTION, INTERACTION WITH DDX1, AND SUBCELLULAR LOCATION.
PubMed=19058135; DOI=10.1002/jcb.22004;
Ishaq M., Ma L., Wu X., Mu Y., Pan J., Hu J., Hu T., Fu Q., Guo D.;
"The DEAD-box RNA helicase DDX1 interacts with RelA and enhances
nuclear factor kappaB-mediated transcription.";
J. Cell. Biochem. 106:296-305(2009).
[54]
FUNCTION, INTERACTION WITH BRD4, AND ACETYLATION AT LYS-310.
PubMed=19103749; DOI=10.1128/MCB.01365-08;
Huang B., Yang X.D., Zhou M.M., Ozato K., Chen L.F.;
"Brd4 coactivates transcriptional activation of NF-kappaB via specific
binding to acetylated RelA.";
Mol. Cell. Biol. 29:1375-1387(2009).
[55]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-310, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[56]
INTERACTION WITH UFL1.
PubMed=20164180; DOI=10.1074/jbc.M109.065920;
Kwon J., Cho H.J., Han S.H., No J.G., Kwon J.Y., Kim H.;
"A novel LZAP-binding protein, NLBP, inhibits cell invasion.";
J. Biol. Chem. 285:12232-12240(2010).
[57]
DEACETYLATION BY SIRT2.
PubMed=21081649; DOI=10.1242/jcs.073783;
Rothgiesser K.M., Erener S., Waibel S., Luscher B., Hottiger M.O.;
"SIRT2 regulates NF-kappaB dependent gene expression through
deacetylation of p65 Lys310.";
J. Cell Sci. 123:4251-4258(2010).
[58]
INTERACTION WITH GFI1, SUBCELLULAR LOCATION, INDUCTION, AND FUNCTION.
PubMed=20547752; DOI=10.1128/MCB.00087-10;
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.;
"Zinc finger protein Gfi1 controls the endotoxin-mediated Toll-like
receptor inflammatory response by antagonizing NF-kappaB p65.";
Mol. Cell. Biol. 30:3929-3942(2010).
[59]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[60]
SUMOYLATION AT LYS-37; LYS-122 AND LYS-123 BY PIAS3.
PubMed=22649547; DOI=10.1371/journal.pone.0037636;
Liu Y., Bridges R., Wortham A., Kulesz-Martin M.;
"NF-kappaB repression by PIAS3 mediated RelA SUMOylation.";
PLoS ONE 7:E37636-E37636(2012).
[61]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[62]
CHROMOSOMAL TRANSLOCATION WITH C11ORF95.
PubMed=24553141; DOI=10.1038/nature13109;
Parker M., Mohankumar K.M., Punchihewa C., Weinlich R., Dalton J.D.,
Li Y., Lee R., Tatevossian R.G., Phoenix T.N., Thiruvenkatam R.,
White E., Tang B., Orisme W., Gupta K., Rusch M., Chen X., Li Y.,
Nagahawhatte P., Hedlund E., Finkelstein D., Wu G., Shurtleff S.,
Easton J., Boggs K., Yergeau D., Vadodaria B., Mulder H.L.,
Becksfort J., Becksford J., Gupta P., Huether R., Ma J., Song G.,
Gajjar A., Merchant T., Boop F., Smith A.A., Ding L., Lu C., Ochoa K.,
Zhao D., Fulton R.S., Fulton L.L., Mardis E.R., Wilson R.K.,
Downing J.R., Green D.R., Zhang J., Ellison D.W., Gilbertson R.J.;
"C11orf95-RELA fusions drive oncogenic NF-kappaB signalling in
ependymoma.";
Nature 506:451-455(2014).
[63]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
PubMed=9865693; DOI=10.1016/S0092-8674(00)81698-0;
Jacobs M.D., Harrison S.C.;
"Structure of an IkappaBalpha/NF-kappaB complex.";
Cell 95:749-758(1998).
-!- FUNCTION: 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. Essential for cytokine gene
expression in T-cells (PubMed:15790681).
{ECO:0000269|PubMed:10928981, ECO:0000269|PubMed:12748188,
ECO:0000269|PubMed:15790681, ECO:0000269|PubMed:17000776,
ECO:0000269|PubMed:17620405, ECO:0000269|PubMed:19058135,
ECO:0000269|PubMed:19103749, ECO:0000269|PubMed:20547752}.
-!- SUBUNIT: 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). Interacts (via N-
terminus) with CPEN1; this interaction induces proteolytic
cleavage of p65/RELA subunit and inhibition of NF-kappa-B
transcriptional activity (PubMed:18212740). Interacts with FOXP3.
Interacts with CDK5RAP3; stimulates the interaction of RELA with
HDAC1, HDAC2 and HDAC3 thereby inhibiting NF-kappa-B
transcriptional activity (PubMed:17785205).
{ECO:0000250|UniProtKB:Q04206, ECO:0000269|PubMed:15790681,
ECO:0000269|PubMed:17785205, ECO:0000269|PubMed:18212740}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-73886, EBI-73886;
Q9NY61:AATF; NbExp=3; IntAct=EBI-73886, EBI-372428;
P18847-3:ATF3; NbExp=5; IntAct=EBI-73886, EBI-9844134;
O60885:BRD4; NbExp=8; IntAct=EBI-73886, EBI-723869;
Q9ESU6:Brd4 (xeno); NbExp=6; IntAct=EBI-73886, EBI-6260864;
Q96JB5:CDK5RAP3; NbExp=4; IntAct=EBI-73886, EBI-718818;
O15111:CHUK; NbExp=2; IntAct=EBI-73886, EBI-81249;
Q8N668:COMMD1; NbExp=7; IntAct=EBI-73886, EBI-1550112;
Q92793:CREBBP; NbExp=5; IntAct=EBI-73886, EBI-81215;
P35222:CTNNB1; NbExp=2; IntAct=EBI-73886, EBI-491549;
Q9UER7:DAXX; NbExp=5; IntAct=EBI-73886, EBI-77321;
Q08211:DHX9; NbExp=4; IntAct=EBI-73886, EBI-352022;
Q9H9B1:EHMT1; NbExp=3; IntAct=EBI-73886, EBI-766087;
P03372:ESR1; NbExp=7; IntAct=EBI-73886, EBI-78473;
O41974:GAMMAHV.ORF73 (xeno); NbExp=3; IntAct=EBI-73886, EBI-6933128;
Q99684:GFI1; NbExp=2; IntAct=EBI-73886, EBI-949368;
Q13547:HDAC1; NbExp=6; IntAct=EBI-73886, EBI-301834;
P46695:IER3; NbExp=6; IntAct=EBI-73886, EBI-1748945;
O14920:IKBKB; NbExp=2; IntAct=EBI-73886, EBI-81266;
Q13568:IRF5; NbExp=4; IntAct=EBI-73886, EBI-3931258;
Q14145:KEAP1; NbExp=4; IntAct=EBI-73886, EBI-751001;
Q99612:KLF6; NbExp=6; IntAct=EBI-73886, EBI-714994;
P25791:LMO2; NbExp=3; IntAct=EBI-73886, EBI-739696;
P53779:MAPK10; NbExp=2; IntAct=EBI-73886, EBI-713543;
O00255-2:MEN1; NbExp=4; IntAct=EBI-73886, EBI-9869387;
P19838:NFKB1; NbExp=13; IntAct=EBI-73886, EBI-300010;
P25963:NFKBIA; NbExp=21; IntAct=EBI-73886, EBI-307386;
Q15653:NFKBIB; NbExp=6; IntAct=EBI-73886, EBI-352889;
O15294:OGT; NbExp=2; IntAct=EBI-73886, EBI-539828;
P0C774:P/V (xeno); NbExp=3; IntAct=EBI-73886, EBI-3650423;
Q53EL6:PDCD4; NbExp=6; IntAct=EBI-73886, EBI-935824;
P67775:PPP2CA; NbExp=6; IntAct=EBI-73886, EBI-712311;
P30153:PPP2R1A; NbExp=2; IntAct=EBI-73886, EBI-302388;
Q04864:REL; NbExp=3; IntAct=EBI-10223388, EBI-307352;
Q01201:RELB; NbExp=2; IntAct=EBI-73886, EBI-357837;
P23396:RPS3; NbExp=8; IntAct=EBI-73886, EBI-351193;
O75582:RPS6KA5; NbExp=2; IntAct=EBI-73886, EBI-73869;
Q8WTS6:SETD7; NbExp=10; IntAct=EBI-73886, EBI-1268586;
Q96EB6:SIRT1; NbExp=5; IntAct=EBI-73886, EBI-1802965;
Q8IXJ6:SIRT2; NbExp=2; IntAct=EBI-73886, EBI-477232;
Q8N6T7:SIRT6; NbExp=4; IntAct=EBI-73886, EBI-712415;
O95863:SNAI1; NbExp=5; IntAct=EBI-73886, EBI-1045459;
O15524:SOCS1; NbExp=2; IntAct=EBI-73886, EBI-968198;
P40763:STAT3; NbExp=4; IntAct=EBI-73886, EBI-518675;
P15884:TCF4; NbExp=3; IntAct=EBI-10223388, EBI-533224;
P21980:TGM2; NbExp=3; IntAct=EBI-73886, EBI-727668;
Q13625:TP53BP2; NbExp=4; IntAct=EBI-73886, EBI-77642;
Q13625-2:TP53BP2; NbExp=6; IntAct=EBI-73886, EBI-287091;
P0CG48:UBC; NbExp=6; IntAct=EBI-73886, EBI-3390054;
P10226:UL42 (xeno); NbExp=6; IntAct=EBI-73886, EBI-1029310;
Q9UBK9:UXT; NbExp=5; IntAct=EBI-73886, EBI-357355;
-!- SUBCELLULAR LOCATION: 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. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=p65;
IsoId=Q04206-1; Sequence=Displayed;
Name=2; Synonyms=p65 delta 2;
IsoId=Q04206-2; Sequence=VSP_005587, VSP_005588;
Name=3; Synonyms=p65 delta;
IsoId=Q04206-3; Sequence=VSP_012031;
Name=4;
IsoId=Q04206-4; Sequence=VSP_031245;
Note=No experimental confirmation available.;
-!- DOMAIN: the 9aaTAD motif is a transactivation domain present in a
large number of yeast and animal transcription factors.
{ECO:0000269|PubMed:17467953}.
-!- PTM: Ubiquitinated, leading to its proteasomal degradation.
Degradation is required for termination of NF-kappa-B response.
{ECO:0000269|PubMed:15226358}.
-!- PTM: 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). {ECO:0000250}.
-!- PTM: 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. {ECO:0000250,
ECO:0000269|PubMed:10521409, ECO:0000269|PubMed:10938077,
ECO:0000269|PubMed:11931769, ECO:0000269|PubMed:12456660,
ECO:0000269|PubMed:12628924, ECO:0000269|PubMed:14690596,
ECO:0000269|PubMed:15073167, ECO:0000269|PubMed:15516339,
ECO:0000269|PubMed:15775976, ECO:0000269|PubMed:16046471,
ECO:0000269|PubMed:16135789, ECO:0000269|PubMed:16407239,
ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:19103749}.
-!- PTM: 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.
{ECO:0000269|PubMed:12419806, ECO:0000269|PubMed:12456660,
ECO:0000269|PubMed:16135789, ECO:0000269|PubMed:17000776,
ECO:0000269|PubMed:19103749}.
-!- PTM: S-nitrosylation of Cys-38 inactivates the enzyme activity.
{ECO:0000250}.
-!- PTM: Sulfhydration at Cys-38 mediates the anti-apoptotic activity
by promoting the interaction with RPS3 and activating the
transcription factor activity. {ECO:0000250}.
-!- PTM: Sumoylation by PIAS3 negatively regulates DNA-bound activated
NF-kappa-B. {ECO:0000269|PubMed:22649547}.
-!- PTM: Proteolytically cleaved within a conserved N-terminus region
required for base-specific contact with DNA in a CPEN1-mediated
manner, and hence inhibits NF-kappa-B transcriptional activity
(PubMed:18212740). {ECO:0000269|PubMed:18212740}.
-!- DISEASE: Note=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).
{ECO:0000269|PubMed:24553141}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RELAID325.html";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/rela/";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M62399; AAA36408.1; -; mRNA.
EMBL; Z22948; CAA80524.2; -; Genomic_DNA.
EMBL; Z22949; CAA80524.2; JOINED; Genomic_DNA.
EMBL; Z22953; CAA80524.2; JOINED; Genomic_DNA.
EMBL; Z22950; CAA80524.2; JOINED; Genomic_DNA.
EMBL; Z22951; CAA80524.2; JOINED; Genomic_DNA.
EMBL; L19067; AAA20946.1; -; mRNA.
EMBL; BC033522; AAH33522.1; -; mRNA.
EMBL; AY455868; AAR13863.1; -; Genomic_DNA.
CCDS; CCDS31609.1; -. [Q04206-1]
CCDS; CCDS44651.1; -. [Q04206-4]
PIR; A40851; A40851.
PIR; I53719; I53719.
PIR; S51782; A42017.
RefSeq; NP_001138610.1; NM_001145138.1. [Q04206-4]
RefSeq; NP_001230913.1; NM_001243984.1.
RefSeq; NP_068810.3; NM_021975.3. [Q04206-1]
UniGene; Hs.502875; -.
PDB; 1NFI; X-ray; 2.70 A; A/C=20-320.
PDB; 2LSP; NMR; -; A=304-316.
PDB; 2O61; X-ray; 2.80 A; A=20-291.
PDB; 3GUT; X-ray; 3.59 A; A/C/E/G=20-291.
PDB; 3QXY; X-ray; 2.09 A; P/Q=302-316.
PDB; 3RC0; X-ray; 2.19 A; P/Q=302-316.
PDB; 4KV1; X-ray; 1.50 A; C/D=308-314.
PDB; 4KV4; X-ray; 2.00 A; B=308-314.
PDB; 5U4K; NMR; -; B=521-551.
PDB; 5URN; NMR; -; B=521-551.
PDBsum; 1NFI; -.
PDBsum; 2LSP; -.
PDBsum; 2O61; -.
PDBsum; 3GUT; -.
PDBsum; 3QXY; -.
PDBsum; 3RC0; -.
PDBsum; 4KV1; -.
PDBsum; 4KV4; -.
PDBsum; 5U4K; -.
PDBsum; 5URN; -.
DisProt; DP00085; -.
ProteinModelPortal; Q04206; -.
SMR; Q04206; -.
BioGrid; 111902; 277.
DIP; DIP-24238N; -.
ELM; Q04206; -.
IntAct; Q04206; 135.
MINT; MINT-106444; -.
STRING; 9606.ENSP00000384273; -.
BindingDB; Q04206; -.
ChEMBL; CHEMBL5533; -.
iPTMnet; Q04206; -.
PhosphoSitePlus; Q04206; -.
SwissPalm; Q04206; -.
BioMuta; RELA; -.
DMDM; 62906901; -.
EPD; Q04206; -.
MaxQB; Q04206; -.
PaxDb; Q04206; -.
PeptideAtlas; Q04206; -.
PRIDE; Q04206; -.
DNASU; 5970; -.
Ensembl; ENST00000308639; ENSP00000311508; ENSG00000173039. [Q04206-4]
Ensembl; ENST00000406246; ENSP00000384273; ENSG00000173039. [Q04206-1]
GeneID; 5970; -.
KEGG; hsa:5970; -.
UCSC; uc001ofg.4; human. [Q04206-1]
CTD; 5970; -.
DisGeNET; 5970; -.
GeneCards; RELA; -.
HGNC; HGNC:9955; RELA.
HPA; CAB004264; -.
HPA; CAB005030; -.
HPA; HPA063461; -.
MalaCards; RELA; -.
MIM; 164014; gene.
neXtProt; NX_Q04206; -.
OpenTargets; ENSG00000173039; -.
Orphanet; 251636; Ependymoma.
PharmGKB; PA296; -.
eggNOG; ENOG410IG8F; Eukaryota.
eggNOG; ENOG410XT64; LUCA.
GeneTree; ENSGT00500000044765; -.
HOGENOM; HOG000230474; -.
HOVERGEN; HBG017916; -.
InParanoid; Q04206; -.
KO; K04735; -.
OMA; EFSPMVF; -.
OrthoDB; EOG091G08JD; -.
PhylomeDB; Q04206; -.
TreeFam; TF325632; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-HSA-193692; Regulated proteolysis of p75NTR.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-209560; NF-kB is activated and signals survival.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-446652; Interleukin-1 signaling.
Reactome; R-HSA-448706; Interleukin-1 processing.
Reactome; R-HSA-5603027; IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR).
Reactome; R-HSA-5603029; IkBA variant leads to EDA-ID.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-HSA-5660668; CLEC7A/inflammasome pathway.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
SABIO-RK; Q04206; -.
SignaLink; Q04206; -.
SIGNOR; Q04206; -.
ChiTaRS; RELA; human.
EvolutionaryTrace; Q04206; -.
GeneWiki; RELA; -.
GenomeRNAi; 5970; -.
PRO; PR:Q04206; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000173039; -.
CleanEx; HS_RELA; -.
ExpressionAtlas; Q04206; baseline and differential.
Genevisible; Q04206; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0033256; C:I-kappaB/NF-kappaB complex; IBA:GO_Central.
GO; GO:0035525; C:NF-kappaB p50/p65 complex; IDA:CAFA.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IDA:UniProtKB.
GO; GO:0042805; F:actinin binding; IPI:UniProtKB.
GO; GO:0033613; F:activating transcription factor binding; IPI:BHF-UCL.
GO; GO:0071532; F:ankyrin repeat binding; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
GO; GO:0042301; F:phosphate ion binding; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0070491; F:repressing transcription factor binding; IPI:BHF-UCL.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0000983; F:transcription factor activity, RNA polymerase II core promoter sequence-specific; IMP:BHF-UCL.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:NTNU_SB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0006117; P:acetaldehyde metabolic process; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
GO; GO:0006968; P:cellular defense response; NAS:UniProtKB.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; IDA:UniProtKB.
GO; GO:0071354; P:cellular response to interleukin-6; IMP:BHF-UCL.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071223; P:cellular response to lipoteichoic acid; IMP:UniProtKB.
GO; GO:0071316; P:cellular response to nicotine; IMP:BHF-UCL.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IMP:BHF-UCL.
GO; GO:0071224; P:cellular response to peptidoglycan; IMP:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; NAS:UniProtKB.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0031293; P:membrane protein intracellular domain proteolysis; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:BHF-UCL.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; IDA:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
GO; GO:0045084; P:positive regulation of interleukin-12 biosynthetic process; IEA:Ensembl.
GO; GO:2000630; P:positive regulation of miRNA metabolic process; IMP:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:MGI.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:CAFA.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0014040; P:positive regulation of Schwann cell differentiation; IEA:Ensembl.
GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IMP:CAFA.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
GO; GO:0043620; P:regulation of DNA-templated transcription in response to stress; IMP:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IGI:CAFA.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:CAFA.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0033590; P:response to cobalamin; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0070555; P:response to interleukin-1; IGI:BHF-UCL.
GO; GO:0043278; P:response to morphine; IEA:Ensembl.
GO; GO:0032495; P:response to muramyl dipeptide; IEA:Ensembl.
GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
GO; GO:0010033; P:response to organic substance; IDA:UniProtKB.
GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
GO; GO:0010224; P:response to UV-B; IDA:UniProtKB.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IDA:CAFA.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd01177; IPT_NFkappaB; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 2.60.40.340; -; 1.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002909; IPT.
InterPro; IPR033926; IPT_NFkappaB.
InterPro; IPR000451; NFkB/Dor.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR030495; RelA.
InterPro; IPR030492; RHD_CS.
InterPro; IPR032397; RHD_dimer.
InterPro; IPR011539; RHD_DNA_bind_dom.
PANTHER; PTHR24169; PTHR24169; 1.
PANTHER; PTHR24169:SF23; PTHR24169:SF23; 1.
Pfam; PF16179; RHD_dimer; 1.
Pfam; PF00554; RHD_DNA_bind; 1.
PRINTS; PR00057; NFKBTNSCPFCT.
SMART; SM00429; IPT; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS01204; REL_1; 1.
PROSITE; PS50254; REL_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Chromosomal rearrangement; Complete proteome; Cytoplasm; DNA-binding;
Host-virus interaction; Isopeptide bond; Methylation; Nucleus;
Phosphoprotein; Reference proteome; S-nitrosylation; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 551 Transcription factor p65.
/FTId=PRO_0000205169.
DOMAIN 19 306 RHD. {ECO:0000255|PROSITE-
ProRule:PRU00265}.
REGION 415 459 Activation domain.
MOTIF 301 304 Nuclear localization signal.
{ECO:0000255}.
MOTIF 536 544 9aaTAD.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 38 38 Cysteine persulfide; alternate.
{ECO:0000250}.
MOD_RES 38 38 S-nitrosocysteine; alternate.
{ECO:0000250|UniProtKB:Q04207}.
MOD_RES 122 122 N6-acetyllysine; by PCAF and EP300;
alternate. {ECO:0000269|PubMed:12419806}.
MOD_RES 123 123 N6-acetyllysine; by PCAF and EP300;
alternate. {ECO:0000269|PubMed:12419806}.
MOD_RES 218 218 N6-acetyllysine.
{ECO:0000269|PubMed:12456660}.
MOD_RES 221 221 N6-acetyllysine.
{ECO:0000269|PubMed:12456660}.
MOD_RES 254 254 Phosphothreonine.
{ECO:0000269|PubMed:14690596}.
MOD_RES 276 276 Phosphoserine; by RPS6KA4 and RPS6KA5.
{ECO:0000269|PubMed:12628924}.
MOD_RES 281 281 Phosphoserine.
{ECO:0000305|PubMed:15516339}.
MOD_RES 310 310 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:12456660,
ECO:0000269|PubMed:16135789,
ECO:0000269|PubMed:17000776,
ECO:0000269|PubMed:19103749}.
MOD_RES 310 310 N6-methyllysine; by SETD6; alternate.
{ECO:0000250|UniProtKB:Q04207}.
MOD_RES 311 311 Phosphoserine; by PKC/PRKCZ.
{ECO:0000250|UniProtKB:Q04207}.
MOD_RES 435 435 Phosphothreonine.
{ECO:0000269|PubMed:15073167}.
MOD_RES 468 468 Phosphoserine; by IKKB and IKKE.
{ECO:0000269|PubMed:16046471,
ECO:0000269|PubMed:16407239}.
MOD_RES 505 505 Phosphothreonine; by CHEK1.
{ECO:0000269|PubMed:15775976}.
MOD_RES 529 529 Phosphoserine; by CK2.
{ECO:0000269|PubMed:10938077}.
MOD_RES 536 536 Phosphoserine; by IKKB.
{ECO:0000269|PubMed:10521409,
ECO:0000269|PubMed:17785205}.
CROSSLNK 37 37 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO3).
{ECO:0000269|PubMed:22649547}.
CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO3);
alternate.
CROSSLNK 123 123 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO3);
alternate.
VAR_SEQ 13 25 Missing (in isoform 2).
{ECO:0000303|PubMed:7907305}.
/FTId=VSP_005587.
VAR_SEQ 143 145 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_031245.
VAR_SEQ 222 231 Missing (in isoform 3).
{ECO:0000303|PubMed:1732726}.
/FTId=VSP_012031.
VAR_SEQ 506 506 Missing (in isoform 2).
{ECO:0000303|PubMed:7907305}.
/FTId=VSP_005588.
MUTAGEN 254 254 T->A: Abolishes interaction with PIN1.
{ECO:0000269|PubMed:14690596}.
MUTAGEN 276 276 S->C: Loss of phosphorylation.
{ECO:0000269|PubMed:12628924}.
CONFLICT 49 49 E -> R (in Ref. 2; CAA80524).
{ECO:0000305}.
CONFLICT 180 180 S -> P (in Ref. 1; AAA36408).
{ECO:0000305}.
CONFLICT 372 380 QISQASALA -> RSARPRLG (in Ref. 2;
CAA80524). {ECO:0000305}.
STRAND 21 25 {ECO:0000244|PDB:1NFI}.
STRAND 30 32 {ECO:0000244|PDB:1NFI}.
STRAND 39 41 {ECO:0000244|PDB:1NFI}.
STRAND 53 55 {ECO:0000244|PDB:1NFI}.
STRAND 60 63 {ECO:0000244|PDB:1NFI}.
STRAND 68 80 {ECO:0000244|PDB:1NFI}.
STRAND 87 92 {ECO:0000244|PDB:1NFI}.
STRAND 97 104 {ECO:0000244|PDB:1NFI}.
STRAND 109 112 {ECO:0000244|PDB:2O61}.
STRAND 117 119 {ECO:0000244|PDB:1NFI}.
HELIX 123 125 {ECO:0000244|PDB:2O61}.
HELIX 126 129 {ECO:0000244|PDB:1NFI}.
TURN 130 137 {ECO:0000244|PDB:1NFI}.
TURN 145 148 {ECO:0000244|PDB:2O61}.
STRAND 156 166 {ECO:0000244|PDB:1NFI}.
STRAND 168 173 {ECO:0000244|PDB:1NFI}.
STRAND 183 188 {ECO:0000244|PDB:1NFI}.
STRAND 196 200 {ECO:0000244|PDB:1NFI}.
STRAND 202 205 {ECO:0000244|PDB:1NFI}.
STRAND 211 217 {ECO:0000244|PDB:1NFI}.
STRAND 225 230 {ECO:0000244|PDB:1NFI}.
STRAND 233 238 {ECO:0000244|PDB:1NFI}.
HELIX 241 243 {ECO:0000244|PDB:1NFI}.
TURN 246 248 {ECO:0000244|PDB:1NFI}.
STRAND 249 253 {ECO:0000244|PDB:1NFI}.
STRAND 258 260 {ECO:0000244|PDB:2O61}.
STRAND 266 273 {ECO:0000244|PDB:1NFI}.
TURN 275 277 {ECO:0000244|PDB:1NFI}.
STRAND 284 289 {ECO:0000244|PDB:1NFI}.
HELIX 294 302 {ECO:0000244|PDB:1NFI}.
HELIX 309 311 {ECO:0000244|PDB:4KV1}.
HELIX 313 323 {ECO:0000244|PDB:2O61}.
STRAND 330 335 {ECO:0000244|PDB:2O61}.
STRAND 338 342 {ECO:0000244|PDB:2O61}.
HELIX 358 360 {ECO:0000244|PDB:2O61}.
HELIX 361 369 {ECO:0000244|PDB:2O61}.
HELIX 388 406 {ECO:0000244|PDB:2O61}.
STRAND 528 530 {ECO:0000244|PDB:5URN}.
HELIX 532 536 {ECO:0000244|PDB:5URN}.
HELIX 537 546 {ECO:0000244|PDB:5URN}.
SEQUENCE 551 AA; 60219 MW; 8147A6AF9F2445C6 CRC64;
MDELFPLIFP AEPAQASGPY VEIIEQPKQR GMRFRYKCEG RSAGSIPGER STDTTKTHPT
IKINGYTGPG TVRISLVTKD PPHRPHPHEL VGKDCRDGFY EAELCPDRCI HSFQNLGIQC
VKKRDLEQAI SQRIQTNNNP FQVPIEEQRG DYDLNAVRLC FQVTVRDPSG RPLRLPPVLS
HPIFDNRAPN TAELKICRVN RNSGSCLGGD EIFLLCDKVQ KEDIEVYFTG PGWEARGSFS
QADVHRQVAI VFRTPPYADP SLQAPVRVSM QLRRPSDREL SEPMEFQYLP DTDDRHRIEE
KRKRTYETFK SIMKKSPFSG PTDPRPPPRR IAVPSRSSAS VPKPAPQPYP FTSSLSTINY
DEFPTMVFPS GQISQASALA PAPPQVLPQA PAPAPAPAMV SALAQAPAPV PVLAPGPPQA
VAPPAPKPTQ AGEGTLSEAL LQLQFDDEDL GALLGNSTDP AVFTDLASVD NSEFQQLLNQ
GIPVAPHTTE PMLMEYPEAI TRLVTGAQRP PDPAPAPLGA PGLPNGLLSG DEDFSSIADM
DFSALLSQIS S


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