TF65_HUMAN
ID TF65_HUMAN Reviewed; 551 AA.
AC Q04206; Q6GTV1; Q6SLK1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 249.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2006423; DOI=10.1126/science.2006423;
RA Ruben S.M., Dillon P.J., Schreck R., Henkel T., Chen C.-H., Maher M.,
RA Baeuerle P.A., Rosen C.A.;
RT "Isolation of a rel-related human cDNA that potentially encodes the 65-kD
RT subunit of NF-kappa B.";
RL Science 251:1490-1493(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Bone;
RX PubMed=7907305; DOI=10.1016/0378-1119(94)90823-0;
RA Lyle R., Valleley E.M., Sharpe P.T., Hewitt J.E.;
RT "An alternatively spliced transcript, p65 delta 2, of the gene encoding the
RT p65 subunit of the transcription factor NF-kappa B.";
RL Gene 138:265-266(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Colon;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-551.
RG SeattleSNPs variation discovery resource;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 214-239 (ISOFORMS 1/2 AND 3), AND REGION.
RX PubMed=1732726; DOI=10.1128/mcb.12.2.444-454.1992;
RA Ruben S.M., Narayanan R., Klement J.F., Chen C.-H., Rosen C.A.;
RT "Functional characterization of the NF-kappa B p65 transcriptional
RT activator and an alternatively spliced derivative.";
RL Mol. Cell. Biol. 12:444-454(1992).
RN [7]
RP IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX, AND IDENTIFICATION IN THE
RP NF-KAPPA-B P65-C-REL COMPLEX.
RX PubMed=1740106; DOI=10.1002/j.1460-2075.1992.tb05043.x;
RA Hansen S.K., Nerlov C., Zabel U., Verde P., Johnsen M., Baeuerle P.A.,
RA Blasi F.;
RT "A novel complex between the p65 subunit of NF-kappa B and c-Rel binds to a
RT DNA element involved in the phorbol ester induction of the human urokinase
RT gene.";
RL EMBO J. 11:205-213(1992).
RN [8]
RP INTERACTION WITH NFKBIA, AND SUBCELLULAR LOCATION.
RX PubMed=1493333; DOI=10.1091/mbc.3.12.1339;
RA Ganchi P.A., Sun S.C., Greene W.C., Ballard D.W.;
RT "I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B p65
RT and requires the transactivation domain to inhibit NF-kappa B p65 DNA
RT binding.";
RL Mol. Biol. Cell 3:1339-1352(1992).
RN [9]
RP IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX, AND IDENTIFICATION IN
RP THE NF-KAPPA-B P65-P52 COMPLEX.
RX PubMed=8152812;
RA Beg A.A., Baldwin A.S. Jr.;
RT "Activation of multiple NF-kappa B/Rel DNA-binding complexes by tumor
RT necrosis factor.";
RL Oncogene 9:1487-1492(1994).
RN [10]
RP IDENTIFICATION IN THE NF-KAPPA-B P65-P65 COMPLEX, AND IDENTIFICATION IN THE
RP NF-KAPPA-B P65-C-REL COMPLEX.
RX PubMed=9056676;
RA Aoudjit F., Brochu N., Belanger B., Stratowa C., Hiscott J., Audette M.;
RT "Regulation of intercellular adhesion molecule-1 gene by tumor necrosis
RT factor-alpha is mediated by the nuclear factor-kappaB heterodimers p65/p65
RT and p65/c-Rel in the absence of p50.";
RL Cell Growth Differ. 8:335-342(1997).
RN [11]
RP INTERACTION WITH NFKBIE.
RX PubMed=9315679; DOI=10.1128/mcb.17.10.6184;
RA Li Z., Nabel G.J.;
RT "A new member of the IkappaB protein family, IkappaB epsilon, inhibits RelA
RT (p65)-mediated NF-kappaB transcription.";
RL Mol. Cell. Biol. 17:6184-6190(1997).
RN [12]
RP IDENTIFICATION IN A COMPLEX WITH CHUK; IKBKB; NFKBIA; ELP1 AND MAP3K14.
RX PubMed=9751059; DOI=10.1038/26254;
RA Cohen L., Henzel W.J., Baeuerle P.A.;
RT "IKAP is a scaffold protein of the IkappaB kinase complex.";
RL Nature 395:292-296(1998).
RN [13]
RP PHOSPHORYLATION AT SER-536.
RX PubMed=10521409; DOI=10.1074/jbc.274.43.30353;
RA Sakurai H., Chiba H., Miyoshi H., Sugita T., Toriumi W.;
RT "IkappaB kinases phosphorylate NF-kappaB p65 subunit on serine 536 in the
RT transactivation domain.";
RL J. Biol. Chem. 274:30353-30356(1999).
RN [14]
RP TISSUE SPECIFICITY, AND INTERACTION WITH TP53BP2.
RX PubMed=10498867; DOI=10.1038/sj.onc.1202904;
RA Yang J.-P., Hori M., Takahashi N., Kawabe T., Kato H., Okamoto T.;
RT "NF-kappaB subunit p65 binds to 53BP2 and inhibits cell death induced by
RT 53BP2.";
RL Oncogene 18:5177-5186(1999).
RN [15]
RP FUNCTION, AND IDENTIFICATION IN THE NF-KAPPA-B P65-P65 COMPLEX.
RX PubMed=10928981; DOI=10.1096/fj.99-0847com;
RA Schulte R., Grassl G.A., Preger S., Fessele S., Jacobi C.A., Schaller M.,
RA Nelson P.J., Autenrieth I.B.;
RT "Yersinia enterocolitica invasin protein triggers IL-8 production in
RT epithelial cells via activation of Rel p65-p65 homodimers.";
RL FASEB J. 14:1471-1484(2000).
RN [16]
RP INTERACTION WITH TLE5 AND TLE1.
RX PubMed=10660609; DOI=10.1074/jbc.275.6.4383;
RA Tetsuka T., Uranishi H., Imai H., Ono T., Sonta S., Takahashi N.,
RA Asamitsu K., Okamoto T.;
RT "Inhibition of nuclear factor-kappaB-mediated transcription by association
RT with the amino-terminal enhancer of split, a Groucho-related protein
RT lacking WD40 repeats.";
RL J. Biol. Chem. 275:4383-4390(2000).
RN [17]
RP PHOSPHORYLATION AT SER-529.
RX PubMed=10938077; DOI=10.1074/jbc.m001358200;
RA Wang D., Westerheide S.D., Hanson J.L., Baldwin A.S. Jr.;
RT "Tumor necrosis factor alpha-induced phosphorylation of RelA/p65 on Ser529
RT is controlled by casein kinase II.";
RL J. Biol. Chem. 275:32592-32597(2000).
RN [18]
RP INTERACTION WITH MEN1.
RX PubMed=11526476; DOI=10.1038/sj.onc.1204529;
RA Heppner C., Bilimoria K.Y., Agarwal S.K., Kester M., Whitty L.J.,
RA Guru S.C., Chandrasekharappa S.C., Collins F.S., Spiegel A.M., Marx S.J.,
RA Burns A.L.;
RT "The tumor suppressor protein menin interacts with NF-kappaB proteins and
RT inhibits NF-kappaB-mediated transactivation.";
RL Oncogene 20:4917-4925(2001).
RN [19]
RP ACETYLATION, AND INTERACTION WITH HDAC3.
RX PubMed=11533489; DOI=10.1126/science.1062374;
RA Chen L.F., Fischle W., Verdin E., Greene W.C.;
RT "Duration of nuclear NF-kappaB action regulated by reversible
RT acetylation.";
RL Science 293:1653-1657(2001).
RN [20]
RP INTERACTION WITH ETHE1.
RX PubMed=12398897; DOI=10.1016/s1535-6108(02)00152-6;
RA Higashitsuji H., Higashitsuji H., Nagao T., Nonoguchi K., Fujii S.,
RA Itoh K., Fujita J.;
RT "A novel protein overexpressed in hepatoma accelerates export of NF-kappa B
RT from the nucleus and inhibits p53-dependent apoptosis.";
RL Cancer Cell 2:335-346(2002).
RN [21]
RP ACETYLATION AT LYS-218; LYS-221 AND LYS-310.
RX PubMed=12456660; DOI=10.1093/emboj/cdf660;
RA Chen L.F., Mu Y., Greene W.C.;
RT "Acetylation of RelA at discrete sites regulates distinct nuclear functions
RT of NF-kappaB.";
RL EMBO J. 21:6539-6548(2002).
RN [22]
RP INTERACTION WITH CBP AND HDAC1, AND PHOSPHORYLATION.
RX PubMed=11931769; DOI=10.1016/s1097-2765(02)00477-x;
RA Zhong H., May M.J., Jimi E., Ghosh S.;
RT "The phosphorylation status of nuclear NF-kappa B determines its
RT association with CBP/p300 or HDAC-1.";
RL Mol. Cell 9:625-636(2002).
RN [23]
RP INTERACTION WITH RPS6KA5, MUTAGENESIS OF SER-276, AND PHOSPHORYLATION AT
RP SER-276.
RX PubMed=12628924; DOI=10.1093/emboj/cdg139;
RA Vermeulen L., De Wilde G., Van Damme P., Vanden Berghe W., Haegeman G.;
RT "Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and
RT stress-activated protein kinase-1 (MSK1).";
RL EMBO J. 22:1313-1324(2003).
RN [24]
RP ACETYLATION AT LYS-122 AND LYS-123.
RX PubMed=12419806; DOI=10.1074/jbc.m209572200;
RA Kiernan R., Bres V., Ng R.W., Coudart M.-P., El Messaoudi S., Sardet C.,
RA Jin D.-Y., Emiliani S., Benkirane M.;
RT "Post-activation turn-off of NF-kappa B-dependent transcription is
RT regulated by acetylation of p65.";
RL J. Biol. Chem. 278:2758-2766(2003).
RN [25]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RNF25.
RX PubMed=12748188; DOI=10.1074/jbc.m211831200;
RA Asamitsu K., Tetsuka T., Kanazawa S., Okamoto T.;
RT "RING finger protein AO7 supports NF-kappaB-mediated transcription by
RT interacting with the transactivation domain of the p65 subunit.";
RL J. Biol. Chem. 278:26879-26887(2003).
RN [26]
RP INTERACTION WITH GSK3B.
RX PubMed=12871932; DOI=10.1074/jbc.m305676200;
RA Demarchi F., Bertoli C., Sandy P., Schneider C.;
RT "Glycogen synthase kinase-3 beta regulates NF-kappa B1/p105 stability.";
RL J. Biol. Chem. 278:39583-39590(2003).
RN [27]
RP PHOSPHORYLATION AT THR-254, INTERACTION WITH PIN1 AND SOCS1, AND
RP MUTAGENESIS OF THR-254.
RX PubMed=14690596; DOI=10.1016/s1097-2765(03)00490-8;
RA Ryo A., Suizu F., Yoshida Y., Perrem K., Liou Y.C., Wulf G., Rottapel R.,
RA Yamaoka S., Lu K.P.;
RT "Regulation of NF-kappaB signaling by Pin1-dependent prolyl isomerization
RT and ubiquitin-mediated proteolysis of p65/RelA.";
RL Mol. Cell 12:1413-1426(2003).
RN [28]
RP INTERACTION WITH DHX9.
RX PubMed=15355351; DOI=10.1111/j.1432-1033.2004.04314.x;
RA Tetsuka T., Uranishi H., Sanda T., Asamitsu K., Yang J.-P., Wong-Staal F.,
RA Okamoto T.;
RT "RNA helicase A interacts with nuclear factor kappaB p65 and functions as a
RT transcriptional coactivator.";
RL Eur. J. Biochem. 271:3741-3751(2004).
RN [29]
RP INTERACTION WITH UNC5CL.
RX PubMed=14769797; DOI=10.1074/jbc.m310737200;
RA Zhang J., Xu L.-G., Han K.-J., Shu H.-B.;
RT "Identification of a ZU5 and death domain-containing inhibitor of NF-
RT kappaB.";
RL J. Biol. Chem. 279:17819-17825(2004).
RN [30]
RP PHOSPHORYLATION AT THR-435.
RX PubMed=15073167; DOI=10.1074/jbc.m402362200;
RA Yeh P.Y., Yeh K.H., Chuang S.E., Song Y.C., Cheng A.L.;
RT "Suppression of MEK/ERK signaling pathway enhances cisplatin-induced NF-
RT kappaB activation by protein phosphatase 4-mediated NF-kappaB p65 Thr
RT dephosphorylation.";
RL J. Biol. Chem. 279:26143-26148(2004).
RN [31]
RP UBIQUITINATION.
RX PubMed=15226358; DOI=10.1084/jem.20040196;
RA Saccani S., Marazzi I., Beg A.A., Natoli G.;
RT "Degradation of promoter-bound p65/RelA is essential for the prompt
RT termination of the nuclear factor kappaB response.";
RL J. Exp. Med. 200:107-113(2004).
RN [32]
RP INTERACTION WITH ARRB2.
RX PubMed=15125834; DOI=10.1016/s1097-2765(04)00216-3;
RA Gao H., Sun Y., Wu Y., Luan B., Wang Y., Qu B., Pei G.;
RT "Identification of beta-arrestin2 as a G protein-coupled receptor-
RT stimulated regulator of NF-kappaB pathways.";
RL Mol. Cell 14:303-317(2004).
RN [33]
RP INTERACTION WITH ING4.
RX PubMed=15029197; DOI=10.1038/nature02329;
RA Garkavtsev I., Kozin S.V., Chernova O., Xu L., Winkler F., Brown E.,
RA Barnett G.H., Jain R.K.;
RT "The candidate tumour suppressor protein ING4 regulates brain tumour growth
RT and angiogenesis.";
RL Nature 428:328-332(2004).
RN [34]
RP PHOSPHORYLATION AT THR-505.
RX PubMed=15775976; DOI=10.1038/sj.emboj.7600608;
RA Rocha S., Garrett M.D., Campbell K.J., Schumm K., Perkins N.D.;
RT "Regulation of NF-kappaB and p53 through activation of ATR and Chk1 by the
RT ARF tumour suppressor.";
RL EMBO J. 24:1157-1169(2005).
RN [35]
RP PHOSPHORYLATION AT SER-468.
RX PubMed=16046471; DOI=10.1096/fj.05-3736fje;
RA Schwabe R.F., Sakurai H.;
RT "IKKbeta phosphorylates p65 at S468 in transactivation domain 2.";
RL FASEB J. 19:1758-1760(2005).
RN [36]
RP PHOSPHORYLATION AT SER-281.
RX PubMed=15516339; DOI=10.1074/jbc.m409344200;
RA Anrather J., Racchumi G., Iadecola C.;
RT "cis-acting, element-specific transcriptional activity of differentially
RT phosphorylated nuclear factor-kappa B.";
RL J. Biol. Chem. 280:244-252(2005).
RN [37]
RP INTERACTION WITH COMMD1, AND SUBCELLULAR LOCATION.
RX PubMed=15799966; DOI=10.1074/jbc.m501928200;
RA Burstein E., Hoberg J.E., Wilkinson A.S., Rumble J.M., Csomos R.A.,
RA Komarck C.M., Maine G.N., Wilkinson J.C., Mayo M.W., Duckett C.S.;
RT "COMMD proteins, a novel family of structural and functional homologs of
RT MURR1.";
RL J. Biol. Chem. 280:22222-22232(2005).
RN [38]
RP ACETYLATION AT LYS-310.
RX PubMed=16135789; DOI=10.1128/mcb.25.18.7966-7975.2005;
RA Chen L.F., Williams S.A., Mu Y., Nakano H., Duerr J.M., Buckbinder L.,
RA Greene W.C.;
RT "NF-kappaB RelA phosphorylation regulates RelA acetylation.";
RL Mol. Cell. Biol. 25:7966-7975(2005).
RN [39]
RP FUNCTION, AND INTERACTION WITH FOXP3.
RX PubMed=15790681; DOI=10.1073/pnas.0501675102;
RA Bettelli E., Dastrange M., Oukka M.;
RT "Foxp3 interacts with nuclear factor of activated T cells and NF-kappa B to
RT repress cytokine gene expression and effector functions of T helper
RT cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:5138-5143(2005).
RN [40]
RP INTERACTION WITH HRSV PROTEIN M2-1 (MICROBIAL INFECTION).
RX PubMed=15629770; DOI=10.1016/j.virol.2004.10.031;
RA Reimers K., Buchholz K., Werchau H.;
RT "Respiratory syncytial virus M2-1 protein induces the activation of nuclear
RT factor kappa B.";
RL Virology 331:260-268(2005).
RN [41]
RP INTERACTION WITH MTDH.
RX PubMed=16452207; DOI=10.1158/0008-5472.can-05-3029;
RA Emdad L., Sarkar D., Su Z.-Z., Randolph A., Boukerche H., Valerie K.,
RA Fisher P.B.;
RT "Activation of the nuclear factor kappaB pathway by astrocyte elevated
RT gene-1: implications for tumor progression and metastasis.";
RL Cancer Res. 66:1509-1516(2006).
RN [42]
RP INTERACTION WITH USP48.
RX PubMed=16214042; DOI=10.1016/j.cellsig.2005.03.017;
RA Tzimas C., Michailidou G., Arsenakis M., Kieff E., Mosialos G.,
RA Hatzivassiliou E.G.;
RT "Human ubiquitin specific protease 31 is a deubiquitinating enzyme
RT implicated in activation of nuclear factor-kappaB.";
RL Cell. Signal. 18:83-92(2006).
RN [43]
RP PHOSPHORYLATION AT SER-468.
RX PubMed=16407239; DOI=10.1074/jbc.m508045200;
RA Mattioli I., Geng H., Sebald A., Hodel M., Bucher C., Kracht M.,
RA Schmitz M.L.;
RT "Inducible phosphorylation of NF-kappa B p65 at serine 468 by T cell
RT costimulation is mediated by IKK epsilon.";
RL J. Biol. Chem. 281:6175-6183(2006).
RN [44]
RP INTERACTION WITH BRMS1, FUNCTION, AND ACETYLATION AT LYS-310.
RX PubMed=17000776; DOI=10.1128/mcb.00940-06;
RA Liu Y., Smith P.W., Jones D.R.;
RT "Breast cancer metastasis suppressor 1 functions as a corepressor by
RT enhancing histone deacetylase 1-mediated deacetylation of RelA/p65 and
RT promoting apoptosis.";
RL Mol. Cell. Biol. 26:8683-8696(2006).
RN [45]
RP INTERACTION WITH CARM1.
RX PubMed=16497732; DOI=10.1210/me.2005-0365;
RA Miao F., Li S., Chavez V., Lanting L., Natarajan R.;
RT "Coactivator-associated arginine methyltransferase-1 enhances nuclear
RT factor-kappaB-mediated gene transcription through methylation of histone H3
RT at arginine 17.";
RL Mol. Endocrinol. 20:1562-1573(2006).
RN [46]
RP IDENTIFICATION IN THE NF-KAPPA-B P65-P52 COMPLEX.
RX PubMed=16477006; DOI=10.1073/pnas.0511096103;
RA Song Y.J., Jen K.Y., Soni V., Kieff E., Cahir-McFarland E.;
RT "IL-1 receptor-associated kinase 1 is critical for latent membrane protein
RT 1-induced p65/RelA serine 536 phosphorylation and NF-kappaB activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:2689-2694(2006).
RN [47]
RP INTERACTION WITH CDK5RAP3; HDAC1; HDAC2 AND HADC3, AND PHOSPHORYLATION AT
RP SER-536.
RX PubMed=17785205; DOI=10.1016/j.ccr.2007.07.002;
RA Wang J., An H., Mayo M.W., Baldwin A.S., Yarbrough W.G.;
RT "LZAP, a putative tumor suppressor, selectively inhibits NF-kappaB.";
RL Cancer Cell 12:239-251(2007).
RN [48]
RP DOMAIN.
RX PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
RA Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.;
RT "Nine-amino-acid transactivation domain: establishment and prediction
RT utilities.";
RL Genomics 89:756-768(2007).
RN [49]
RP FUNCTION, AND INTERACTION WITH UXT.
RX PubMed=17620405; DOI=10.1083/jcb.200611081;
RA Sun S., Tang Y., Lou X., Zhu L., Yang K., Zhang B., Shi H., Wang C.;
RT "UXT is a novel and essential cofactor in the NF-kappaB transcriptional
RT enhanceosome.";
RL J. Cell Biol. 178:231-244(2007).
RN [50]
RP INTERACTION WITH MEFV.
RX PubMed=18577712; DOI=10.1182/blood-2008-01-134932;
RA Chae J.J., Wood G., Richard K., Jaffe H., Colburn N.T., Masters S.L.,
RA Gumucio D.L., Shoham N.G., Kastner D.L.;
RT "The familial Mediterranean fever protein, pyrin, is cleaved by caspase-1
RT and activates NF-kappaB through its N-terminal fragment.";
RL Blood 112:1794-1803(2008).
RN [51]
RP INTERACTION WITH PHF11.
RX PubMed=18405956; DOI=10.1016/j.jaci.2008.02.028;
RA Clarke E., Rahman N., Page N., Rolph M.S., Stewart G.J., Jones G.J.;
RT "Functional characterization of the atopy-associated gene PHF11.";
RL J. Allergy Clin. Immunol. 121:1148-1154(2008).
RN [52]
RP INTERACTION WITH AKIP1.
RX PubMed=18178962; DOI=10.1074/jbc.m710285200;
RA Gao N., Asamitsu K., Hibi Y., Ueno T., Okamoto T.;
RT "AKIP1 enhances NF-kappaB-dependent gene expression by promoting the
RT nuclear retention and phosphorylation of p65.";
RL J. Biol. Chem. 283:7834-7843(2008).
RN [53]
RP INTERACTION WITH CPEN1, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=18212740; DOI=10.1038/sj.onc.1211030;
RA Ramsey C.S., Yeung F., Stoddard P.B., Li D., Creutz C.E., Mayo M.W.;
RT "Copine-I represses NF-kappaB transcription by endoproteolysis of p65.";
RL Oncogene 27:3516-3526(2008).
RN [54]
RP FUNCTION, INTERACTION WITH DDX1, AND SUBCELLULAR LOCATION.
RX PubMed=19058135; DOI=10.1002/jcb.22004;
RA Ishaq M., Ma L., Wu X., Mu Y., Pan J., Hu J., Hu T., Fu Q., Guo D.;
RT "The DEAD-box RNA helicase DDX1 interacts with RelA and enhances nuclear
RT factor kappaB-mediated transcription.";
RL J. Cell. Biochem. 106:296-305(2009).
RN [55]
RP FUNCTION, INTERACTION WITH BRD4, AND ACETYLATION AT LYS-310.
RX PubMed=19103749; DOI=10.1128/mcb.01365-08;
RA Huang B., Yang X.D., Zhou M.M., Ozato K., Chen L.F.;
RT "Brd4 coactivates transcriptional activation of NF-kappaB via specific
RT binding to acetylated RelA.";
RL Mol. Cell. Biol. 29:1375-1387(2009).
RN [56]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-310, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [57]
RP INTERACTION WITH UFL1.
RX PubMed=20164180; DOI=10.1074/jbc.m109.065920;
RA Kwon J., Cho H.J., Han S.H., No J.G., Kwon J.Y., Kim H.;
RT "A novel LZAP-binding protein, NLBP, inhibits cell invasion.";
RL J. Biol. Chem. 285:12232-12240(2010).
RN [58]
RP DEACETYLATION BY SIRT2.
RX PubMed=21081649; DOI=10.1242/jcs.073783;
RA Rothgiesser K.M., Erener S., Waibel S., Luscher B., Hottiger M.O.;
RT "SIRT2 regulates NF-kappaB dependent gene expression through deacetylation
RT of p65 Lys310.";
RL J. Cell Sci. 123:4251-4258(2010).
RN [59]
RP INTERACTION WITH GFI1, SUBCELLULAR LOCATION, INDUCTION, AND FUNCTION.
RX PubMed=20547752; DOI=10.1128/mcb.00087-10;
RA Sharif-Askari E., Vassen L., Kosan C., Khandanpour C., Gaudreau M.C.,
RA Heyd F., Okayama T., Jin J., Rojas M.E., Grimes H.L., Zeng H., Moroy T.;
RT "Zinc finger protein Gfi1 controls the endotoxin-mediated Toll-like
RT receptor inflammatory response by antagonizing NF-kappaB p65.";
RL Mol. Cell. Biol. 30:3929-3942(2010).
RN [60]
RP SUBCELLULAR LOCATION (MICROBIAL INFECTION).
RX PubMed=20855622; DOI=10.1073/pnas.1007765107;
RA Gouin E., Adib-Conquy M., Balestrino D., Nahori M.A., Villiers V.,
RA Colland F., Dramsi S., Dussurget O., Cossart P.;
RT "The Listeria monocytogenes InlC protein interferes with innate immune
RT responses by targeting the I{kappa}B kinase subunit IKK{alpha}.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:17333-17338(2010).
RN [61]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [62]
RP INTERACTION WITH HERPES VIRUS 8 PROTEIN LANA1 (MICROBIAL INFECTION).
RX PubMed=21697472; DOI=10.1128/jvi.00733-11;
RA Li X., Liang D., Lin X., Robertson E.S., Lan K.;
RT "Kaposi's sarcoma-associated herpesvirus-encoded latency-associated nuclear
RT antigen reduces interleukin-8 expression in endothelial cells and impairs
RT neutrophil chemotaxis by degrading nuclear p65.";
RL J. Virol. 85:8606-8615(2011).
RN [63]
RP INTERACTION WITH EHMT1, AND METHYLATION AT LYS-310.
RX PubMed=21515635; DOI=10.1093/nar/gkr256;
RA Chang Y., Levy D., Horton J.R., Peng J., Zhang X., Gozani O., Cheng X.;
RT "Structural basis of SETD6-mediated regulation of the NF-kB network via
RT methyl-lysine signaling.";
RL Nucleic Acids Res. 39:6380-6389(2011).
RN [64]
RP SUMOYLATION AT LYS-37; LYS-122 AND LYS-123 BY PIAS3.
RX PubMed=22649547; DOI=10.1371/journal.pone.0037636;
RA Liu Y., Bridges R., Wortham A., Kulesz-Martin M.;
RT "NF-kappaB repression by PIAS3 mediated RelA SUMOylation.";
RL PLoS ONE 7:E37636-E37636(2012).
RN [65]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [66]
RP CHROMOSOMAL TRANSLOCATION WITH ZFTA.
RX PubMed=24553141; DOI=10.1038/nature13109;
RA Parker M., Mohankumar K.M., Punchihewa C., Weinlich R., Dalton J.D., Li Y.,
RA Lee R., Tatevossian R.G., Phoenix T.N., Thiruvenkatam R., White E.,
RA Tang B., Orisme W., Gupta K., Rusch M., Chen X., Li Y., Nagahawhatte P.,
RA Hedlund E., Finkelstein D., Wu G., Shurtleff S., Easton J., Boggs K.,
RA Yergeau D., Vadodaria B., Mulder H.L., Becksfort J., Becksford J.,
RA Gupta P., Huether R., Ma J., Song G., Gajjar A., Merchant T., Boop F.,
RA Smith A.A., Ding L., Lu C., Ochoa K., Zhao D., Fulton R.S., Fulton L.L.,
RA Mardis E.R., Wilson R.K., Downing J.R., Green D.R., Zhang J., Ellison D.W.,
RA Gilbertson R.J.;
RT "C11orf95-RELA fusions drive oncogenic NF-kappaB signalling in
RT ependymoma.";
RL Nature 506:451-455(2014).
RN [67]
RP INTERACTION WITH MOLLUSCUM CONTAGIOSUM VIRUS PROTEIN MC132 (MICROBIAL
RP INFECTION).
RX PubMed=26041281; DOI=10.1128/jvi.00799-15;
RA Brady G., Haas D.A., Farrell P.J., Pichlmair A., Bowie A.G.;
RT "Poxvirus protein MC132 from molluscum contagiosum virus inhibits NF-B
RT activation by targeting p65 for degradation.";
RL J. Virol. 89:8406-8415(2015).
RN [68]
RP INTERACTION WITH DDX3X, AND SUBCELLULAR LOCATION.
RX PubMed=27736973; DOI=10.1371/journal.pone.0164471;
RA Xiang N., He M., Ishaq M., Gao Y., Song F., Guo L., Ma L., Sun G., Liu D.,
RA Guo D., Chen Y.;
RT "The DEAD-Box RNA Helicase DDX3 Interacts with NF-kappaB Subunit p65 and
RT Suppresses p65-Mediated Transcription.";
RL PLoS ONE 11:E0164471-E0164471(2016).
RN [69]
RP INVOLVEMENT IN CMCU.
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 [70]
RP INTERACTION WITH LRRC25.
RX PubMed=29044191; DOI=10.1038/s41598-017-12573-3;
RA Feng Y., Duan T., Du Y., Jin S., Wang M., Cui J., Wang R.F.;
RT "LRRC25 functions as an inhibitor of NF-kappaB signaling pathway by
RT promoting p65/RelA for autophagic degradation.";
RL Sci. Rep. 7:13448-13448(2017).
RN [71]
RP INTERACTION WITH ZBTB7A.
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 [72]
RP UBIQUITINATION.
RX PubMed=31432514; DOI=10.1002/1873-3468.13583;
RA Cao Y., Sun Y., Chang H., Sun X., Yang S.;
RT "The E3 ubiquitin ligase RNF182 inhibits TLR-triggered cytokine production
RT through promoting p65 ubiquitination and degradation.";
RL FEBS Lett. 593:3210-3219(2019).
RN [73]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL44 (MICROBIAL INFECTION).
RX PubMed=30867312; DOI=10.1128/jvi.00181-19;
RA Fu Y.Z., Su S., Zou H.M., Guo Y., Wang S.Y., Li S., Luo M.H., Wang Y.Y.;
RT "Human Cytomegalovirus DNA Polymerase Subunit UL44 Antagonizes Antiviral
RT Immune Responses by Suppressing IRF3- and NF-kappaB-Mediated
RT Transcription.";
RL J. Virol. 93:0-0(2019).
RN [74]
RP FUNCTION.
RX PubMed=33440148; DOI=10.1016/j.celrep.2020.108628;
RA Yin X., Riva L., Pu Y., Martin-Sancho L., Kanamune J., Yamamoto Y.,
RA Sakai K., Gotoh S., Miorin L., De Jesus P.D., Yang C.C., Herbert K.M.,
RA Yoh S., Hultquist J.F., Garcia-Sastre A., Chanda S.K.;
RT "MDA5 Governs the Innate Immune Response to SARS-CoV-2 in Lung Epithelial
RT Cells.";
RL Cell Rep. 34:108628-108628(2021).
RN [75]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=9865693; DOI=10.1016/s0092-8674(00)81698-0;
RA Jacobs M.D., Harrison S.C.;
RT "Structure of an IkappaBalpha/NF-kappaB complex.";
RL Cell 95:749-758(1998).
RN [76]
RP VARIANT 246-ARG--SER-549 DEL.
RX PubMed=29305315; DOI=10.1016/j.jaci.2017.11.036;
RA Comrie W.A., Faruqi A.J., Price S., Zhang Y., Rao V.K., Su H.C.,
RA Lenardo M.J.;
RT "RELA haploinsufficiency in CD4 lymphoproliferative disease with autoimmune
RT cytopenias.";
RL J. Allergy Clin. Immunol. 141:1507-1510(2018).
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 Associates with chromatin at the NF-kappa-B promoter region via
CC association with DDX1. Essential for cytokine gene expression in T-
CC cells (PubMed:15790681). The NF-kappa-B homodimeric RELA-RELA complex
CC appears to be involved in invasin-mediated activation of IL-8
CC expression. Key transcription factor regulating the IFN response during
CC SARS-CoV-2 infection (PubMed:33440148). {ECO:0000269|PubMed:10928981,
CC ECO:0000269|PubMed:12748188, ECO:0000269|PubMed:15790681,
CC ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:17620405,
CC ECO:0000269|PubMed:19058135, ECO:0000269|PubMed:19103749,
CC ECO:0000269|PubMed:20547752, ECO:0000269|PubMed:33440148}.
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 (By
CC similarity). Interacts with NFKBID (By similarity). Interacts with
CC NFKBIA (PubMed:1493333). Interacts with GSK3B. Interacts with NFKBIB
CC (By similarity). Interacts with NFKBIE. Interacts with NFKBIZ.
CC Interacts with EHMT1 (via ANK repeats) (PubMed:21515635). Part of a 70-
CC 90 kDa complex at least consisting of CHUK, IKBKB, NFKBIA, RELA, ELP1
CC and 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 UXT. Interacts with MTDH and PHF11. Interacts with ARRB2. Interacts
CC with NFKBIA (when phosphorylated), the interaction is direct;
CC phosphorylated NFKBIA is part of a SCF(BTRC)-like complex lacking CUL1.
CC Interacts with RNF25. Interacts (via C-terminus) with DDX1. Interacts
CC with UFL1 and COMMD1. Interacts with BRMS1; this promotes deacetylation
CC of 'Lys-310'. Interacts with NOTCH2 (By similarity). Directly interacts
CC with MEN1; this interaction represses NFKB-mediated transactivation.
CC Interacts with AKIP1, which promotes the phosphorylation and nuclear
CC retention of RELA. Interacts (via the RHD) with GFI1; the interaction,
CC after bacterial lipopolysaccharide (LPS) stimulation, inhibits the
CC transcriptional activity by interfering with the DNA-binding activity
CC to target gene promoter DNA. Interacts (when acetylated at Lys-310)
CC with BRD4; leading to activation of the NF-kappa-B pathway. Interacts
CC with MEFV. Interacts with CLOCK (By similarity). Interacts (via N-
CC terminus) with CPEN1; this interaction induces proteolytic cleavage of
CC p65/RELA subunit and inhibition of NF-kappa-B transcriptional activity
CC (PubMed:18212740). Interacts with FOXP3. Interacts with CDK5RAP3;
CC stimulates the interaction of RELA with HDAC1, HDAC2 and HDAC3 thereby
CC inhibiting NF-kappa-B transcriptional activity (PubMed:17785205).
CC Interacts with DHX9; this interaction is direct and activates NF-kappa-
CC B-mediated transcription (PubMed:15355351). Interacts with LRRC25
CC (PubMed:29044191). Interacts with TBX21 (By similarity). Interacts with
CC KAT2A (By similarity). Interacts with ZBTB7A; involved in the control
CC by RELA of the accessibility of target gene promoters
CC (PubMed:29813070). Directly interacts with DDX3X; this interaction may
CC trap RELA in the cytoplasm, impairing nuclear relocalization upon TNF
CC activating signals (PubMed:27736973). Interacts with PHF2 (By
CC similarity). Interacts with MKRN2; the interaction leads to its
CC polyubiquitination and proteasome-dependent degradation (By
CC similarity). {ECO:0000250|UniProtKB:Q04207, ECO:0000269|PubMed:1493333,
CC ECO:0000269|PubMed:15355351, ECO:0000269|PubMed:15790681,
CC ECO:0000269|PubMed:17785205, ECO:0000269|PubMed:18212740,
CC ECO:0000269|PubMed:21515635, ECO:0000269|PubMed:27736973,
CC ECO:0000269|PubMed:29044191, ECO:0000269|PubMed:29813070}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human respiratory
CC syncytial virus (HRSV) protein M2-1. {ECO:0000269|PubMed:15629770}.
CC -!- SUBUNIT: (Microbial infection) Interacts with molluscum contagiosum
CC virus MC132. {ECO:0000269|PubMed:26041281}.
CC -!- SUBUNIT: (Microbial infection) Interacts with herpes virus 8 virus
CC protein LANA1. {ECO:0000269|PubMed:21697472}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC protein UL44; this interaction prevents NF-kappa-B binding to its
CC promoters. {ECO:0000269|PubMed:30867312}.
CC -!- INTERACTION:
CC Q04206; Q9NY61: AATF; NbExp=3; IntAct=EBI-73886, EBI-372428;
CC Q04206; P18847-3: ATF3; NbExp=5; IntAct=EBI-73886, EBI-9844134;
CC Q04206; O60885: BRD4; NbExp=8; IntAct=EBI-73886, EBI-723869;
CC Q04206; P55212: CASP6; NbExp=3; IntAct=EBI-73886, EBI-718729;
CC Q04206; P06307: CCK; NbExp=3; IntAct=EBI-73886, EBI-6624398;
CC Q04206; Q96JB5: CDK5RAP3; NbExp=4; IntAct=EBI-73886, EBI-718818;
CC Q04206; P28329-3: CHAT; NbExp=3; IntAct=EBI-73886, EBI-25837549;
CC Q04206; O15111: CHUK; NbExp=2; IntAct=EBI-73886, EBI-81249;
CC Q04206; Q8N668: COMMD1; NbExp=7; IntAct=EBI-73886, EBI-1550112;
CC Q04206; Q92793: CREBBP; NbExp=6; IntAct=EBI-73886, EBI-81215;
CC Q04206; P52943: CRIP2; NbExp=2; IntAct=EBI-73886, EBI-947590;
CC Q04206; P35222: CTNNB1; NbExp=3; IntAct=EBI-73886, EBI-491549;
CC Q04206; Q9UER7: DAXX; NbExp=5; IntAct=EBI-73886, EBI-77321;
CC Q04206; Q08211: DHX9; NbExp=4; IntAct=EBI-73886, EBI-352022;
CC Q04206; Q9H9B1: EHMT1; NbExp=3; IntAct=EBI-73886, EBI-766087;
CC Q04206; P03372: ESR1; NbExp=9; IntAct=EBI-73886, EBI-78473;
CC Q04206; P22607: FGFR3; NbExp=3; IntAct=EBI-73886, EBI-348399;
CC Q04206; Q99684: GFI1; NbExp=2; IntAct=EBI-73886, EBI-949368;
CC Q04206; P06396: GSN; NbExp=3; IntAct=EBI-73886, EBI-351506;
CC Q04206; Q13547: HDAC1; NbExp=6; IntAct=EBI-73886, EBI-301834;
CC Q04206; P46695: IER3; NbExp=6; IntAct=EBI-73886, EBI-1748945;
CC Q04206; O14920: IKBKB; NbExp=2; IntAct=EBI-73886, EBI-81266;
CC Q04206; Q13568: IRF5; NbExp=4; IntAct=EBI-73886, EBI-3931258;
CC Q04206; Q9Y2K7: KDM2A; NbExp=2; IntAct=EBI-73886, EBI-765758;
CC Q04206; Q14145: KEAP1; NbExp=4; IntAct=EBI-73886, EBI-751001;
CC Q04206; Q99612: KLF6; NbExp=6; IntAct=EBI-73886, EBI-714994;
CC Q04206; P13473-2: LAMP2; NbExp=3; IntAct=EBI-73886, EBI-21591415;
CC Q04206; P25791: LMO2; NbExp=3; IntAct=EBI-73886, EBI-739696;
CC Q04206; Q9BQ69: MACROD1; NbExp=7; IntAct=EBI-73886, EBI-5324932;
CC Q04206; P53779: MAPK10; NbExp=2; IntAct=EBI-73886, EBI-713543;
CC Q04206; O00255-2: MEN1; NbExp=4; IntAct=EBI-73886, EBI-9869387;
CC Q04206; Q16236: NFE2L2; NbExp=5; IntAct=EBI-73886, EBI-2007911;
CC Q04206; P19838: NFKB1; NbExp=14; IntAct=EBI-73886, EBI-300010;
CC Q04206; PRO_0000030311 [P19838]: NFKB1; NbExp=7; IntAct=EBI-73886, EBI-697771;
CC Q04206; P25963: NFKBIA; NbExp=25; IntAct=EBI-73886, EBI-307386;
CC Q04206; Q15653: NFKBIB; NbExp=6; IntAct=EBI-73886, EBI-352889;
CC Q04206; P22736-1: NR4A1; NbExp=3; IntAct=EBI-73886, EBI-16085263;
CC Q04206; Q96L73: NSD1; NbExp=2; IntAct=EBI-73886, EBI-2862434;
CC Q04206; O15294: OGT; NbExp=2; IntAct=EBI-73886, EBI-539828;
CC Q04206; Q53EL6: PDCD4; NbExp=6; IntAct=EBI-73886, EBI-935824;
CC Q04206; Q8N2W9: PIAS4; NbExp=2; IntAct=EBI-73886, EBI-473160;
CC Q04206; P67775: PPP2CA; NbExp=6; IntAct=EBI-73886, EBI-712311;
CC Q04206; P30153: PPP2R1A; NbExp=2; IntAct=EBI-73886, EBI-302388;
CC Q04206; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-73886, EBI-5280197;
CC Q04206; P62826: RAN; NbExp=3; IntAct=EBI-73886, EBI-286642;
CC Q04206; Q04206: RELA; NbExp=3; IntAct=EBI-73886, EBI-73886;
CC Q04206; P23396: RPS3; NbExp=8; IntAct=EBI-73886, EBI-351193;
CC Q04206; Q8WTS6: SETD7; NbExp=12; IntAct=EBI-73886, EBI-1268586;
CC Q04206; Q96EB6: SIRT1; NbExp=5; IntAct=EBI-73886, EBI-1802965;
CC Q04206; Q8IXJ6: SIRT2; NbExp=2; IntAct=EBI-73886, EBI-477232;
CC Q04206; Q8N6T7: SIRT6; NbExp=4; IntAct=EBI-73886, EBI-712415;
CC Q04206; O95863: SNAI1; NbExp=5; IntAct=EBI-73886, EBI-1045459;
CC Q04206; O15524: SOCS1; NbExp=2; IntAct=EBI-73886, EBI-968198;
CC Q04206; P40763: STAT3; NbExp=4; IntAct=EBI-73886, EBI-518675;
CC Q04206; Q13148: TARDBP; NbExp=3; IntAct=EBI-73886, EBI-372899;
CC Q04206; P21980: TGM2; NbExp=3; IntAct=EBI-73886, EBI-727668;
CC Q04206; Q13625: TP53BP2; NbExp=4; IntAct=EBI-73886, EBI-77642;
CC Q04206; Q13625-2: TP53BP2; NbExp=6; IntAct=EBI-73886, EBI-287091;
CC Q04206; P0CG48: UBC; NbExp=6; IntAct=EBI-73886, EBI-3390054;
CC Q04206; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-73886, EBI-741480;
CC Q04206; Q9UBK9: UXT; NbExp=5; IntAct=EBI-73886, EBI-357355;
CC Q04206; Q9Y649; NbExp=3; IntAct=EBI-73886, EBI-25900580;
CC Q04206; Q9ESU6: Brd4; Xeno; NbExp=6; IntAct=EBI-73886, EBI-6260864;
CC Q04206; O41974: GAMMAHV.ORF73; Xeno; NbExp=3; IntAct=EBI-73886, EBI-6933128;
CC Q04206; Q8VIM5-1: Myocd; Xeno; NbExp=2; IntAct=EBI-73886, EBI-15626132;
CC Q04206; Q8X834: nleC; Xeno; NbExp=2; IntAct=EBI-73886, EBI-10039193;
CC Q04206; B3CRR2: OTT_0753; Xeno; NbExp=3; IntAct=EBI-73886, EBI-26357571;
CC Q04206; B3CTB0: OTT_1912; Xeno; NbExp=2; IntAct=EBI-73886, EBI-26357538;
CC Q04206; P0C774: P/V; Xeno; NbExp=3; IntAct=EBI-73886, EBI-3650423;
CC Q04206; P69976: sctL; Xeno; NbExp=2; IntAct=EBI-73886, EBI-2846298;
CC Q04206; P10226: UL42; Xeno; NbExp=6; IntAct=EBI-73886, EBI-1029310;
CC Q04206; P31491: yerA; Xeno; NbExp=2; IntAct=EBI-73886, EBI-2840013;
CC Q04206; A0A384KL23: YPO2940; Xeno; NbExp=2; IntAct=EBI-73886, EBI-20592225;
CC Q04206; A0A380PFV1: YPO3877; Xeno; NbExp=2; IntAct=EBI-73886, EBI-20592206;
CC Q04206-1; Q9NPC8: SIX2; NbExp=2; IntAct=EBI-10826776, EBI-12695166;
CC Q04206-1; Q8VIM5-1: Myocd; Xeno; NbExp=2; IntAct=EBI-10826776, EBI-15626132;
CC Q04206-2; P25963: NFKBIA; NbExp=2; IntAct=EBI-289947, EBI-307386;
CC Q04206-2; Q04864: REL; NbExp=2; IntAct=EBI-289947, EBI-307352;
CC Q04206-2; Q01201: RELB; NbExp=2; IntAct=EBI-289947, EBI-357837;
CC Q04206-3; P35637: FUS; NbExp=3; IntAct=EBI-10223388, EBI-400434;
CC Q04206-3; Q04864: REL; NbExp=3; IntAct=EBI-10223388, EBI-307352;
CC Q04206-3; P15884: TCF4; NbExp=3; IntAct=EBI-10223388, EBI-533224;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1493333,
CC ECO:0000269|PubMed:15799966, ECO:0000269|PubMed:19058135,
CC ECO:0000269|PubMed:20547752}. Cytoplasm {ECO:0000269|PubMed:1493333,
CC ECO:0000269|PubMed:19058135, ECO:0000269|PubMed:20547752,
CC ECO:0000269|PubMed:27736973}. Note=Nuclear, but also found in the
CC cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B)
CC (PubMed:1493333). Colocalized with DDX1 in the nucleus upon TNF-alpha
CC induction (PubMed:19058135). Colocalizes with GFI1 in the nucleus after
CC LPS stimulation (PubMed:20547752). Translocation to the nucleus is
CC impaired in L.monocytogenes infection (PubMed:20855622).
CC {ECO:0000269|PubMed:1493333, ECO:0000269|PubMed:19058135,
CC ECO:0000269|PubMed:20547752, ECO:0000269|PubMed:20855622}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=p65;
CC IsoId=Q04206-1; Sequence=Displayed;
CC Name=2; Synonyms=p65 delta 2;
CC IsoId=Q04206-2; Sequence=VSP_005587, VSP_005588;
CC Name=3; Synonyms=p65 delta;
CC IsoId=Q04206-3; Sequence=VSP_012031;
CC Name=4;
CC IsoId=Q04206-4; Sequence=VSP_031245;
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:0000250|UniProtKB:Q04207}.
CC -!- DOMAIN: The transcriptional activation domain 1/TA1 and the
CC transcriptional activation domain 2/TA2 have direct transcriptional
CC activation properties (By similarity). 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 (PubMed:17467953).
CC {ECO:0000250|UniProtKB:Q04207, ECO:0000269|PubMed:17467953}.
CC -!- PTM: Ubiquitinated by RNF182, leading to its proteasomal degradation.
CC Degradation is required for termination of NF-kappa-B response.
CC {ECO:0000269|PubMed:15226358, ECO:0000269|PubMed:31432514}.
CC -!- PTM: Monomethylated at Lys-310 by SETD6 (PubMed:21515635).
CC Monomethylation at Lys-310 is recognized by the ANK repeats of EHMT1
CC and promotes the formation of repressed chromatin at target genes,
CC leading to down-regulation of NF-kappa-B transcription factor activity.
CC Phosphorylation at Ser-311 disrupts the interaction with EHMT1 without
CC preventing monomethylation at Lys-310 and relieves the repression of
CC target genes (By similarity). {ECO:0000250|UniProtKB:Q04207,
CC ECO:0000269|PubMed:21515635}.
CC -!- PTM: Phosphorylation at Ser-311 disrupts the interaction with EHMT1 and
CC promotes transcription factor activity (By similarity). Phosphorylation
CC on Ser-536 stimulates acetylation on Lys-310 and interaction with CBP;
CC the phosphorylated and acetylated forms show enhanced transcriptional
CC activity. Phosphorylation at Ser-276 by RPS6KA4 and RPS6KA5 promotes
CC its transactivation and transcriptional activities. {ECO:0000250,
CC ECO:0000269|PubMed:10521409, ECO:0000269|PubMed:10938077,
CC ECO:0000269|PubMed:11931769, ECO:0000269|PubMed:12456660,
CC ECO:0000269|PubMed:12628924, ECO:0000269|PubMed:14690596,
CC ECO:0000269|PubMed:15073167, ECO:0000269|PubMed:15516339,
CC ECO:0000269|PubMed:15775976, ECO:0000269|PubMed:16046471,
CC ECO:0000269|PubMed:16135789, ECO:0000269|PubMed:16407239,
CC ECO:0000269|PubMed:17000776, ECO:0000269|PubMed:19103749}.
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.
CC {ECO:0000269|PubMed:12419806, ECO:0000269|PubMed:12456660,
CC ECO:0000269|PubMed:16135789, ECO:0000269|PubMed:17000776,
CC ECO:0000269|PubMed:19103749}.
CC -!- PTM: S-nitrosylation of Cys-38 inactivates the enzyme activity.
CC {ECO:0000250}.
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. {ECO:0000250}.
CC -!- PTM: Sumoylation by PIAS3 negatively regulates DNA-bound activated NF-
CC kappa-B. {ECO:0000269|PubMed:22649547}.
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 (PubMed:18212740). {ECO:0000269|PubMed:18212740}.
CC -!- DISEASE: Note=A chromosomal aberration involving ZFTA is found in more
CC than two-thirds of supratentorial ependymomas. Translocation with ZFTA
CC produces a ZFTA-RELA fusion protein. ZFTA-RELA translocations are
CC potent oncogenes that probably transform neural stem cells by driving
CC an aberrant NF-kappa-B transcription program (PubMed:24553141).
CC {ECO:0000269|PubMed:24553141}.
CC -!- DISEASE: Mucocutaneous ulceration, chronic (CMCU) [MIM:618287]: An
CC autosomal dominant, mucocutaneous disease characterized by chronic
CC mucosal lesions, in absence of recurrent infections.
CC {ECO:0000269|PubMed:28600438}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RELAID325.html";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/rela/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
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DR EMBL; M62399; AAA36408.1; -; mRNA.
DR EMBL; Z22948; CAA80524.2; -; Genomic_DNA.
DR EMBL; Z22949; CAA80524.2; JOINED; Genomic_DNA.
DR EMBL; Z22953; CAA80524.2; JOINED; Genomic_DNA.
DR EMBL; Z22950; CAA80524.2; JOINED; Genomic_DNA.
DR EMBL; Z22951; CAA80524.2; JOINED; Genomic_DNA.
DR EMBL; L19067; AAA20946.1; -; mRNA.
DR EMBL; BC033522; AAH33522.1; -; mRNA.
DR EMBL; AY455868; AAR13863.1; -; Genomic_DNA.
DR CCDS; CCDS31609.1; -. [Q04206-1]
DR CCDS; CCDS44651.1; -. [Q04206-4]
DR PIR; A40851; A40851.
DR PIR; I53719; I53719.
DR PIR; S51782; A42017.
DR RefSeq; NP_001138610.1; NM_001145138.1. [Q04206-4]
DR RefSeq; NP_001230913.1; NM_001243984.1.
DR RefSeq; NP_068810.3; NM_021975.3. [Q04206-1]
DR PDB; 1NFI; X-ray; 2.70 A; A/C=20-320.
DR PDB; 2LSP; NMR; -; A=304-316.
DR PDB; 2O61; X-ray; 2.80 A; A=20-291.
DR PDB; 3GUT; X-ray; 3.59 A; A/C/E/G=20-291.
DR PDB; 3QXY; X-ray; 2.09 A; P/Q=302-316.
DR PDB; 3RC0; X-ray; 2.19 A; P/Q=302-316.
DR PDB; 4KV1; X-ray; 1.50 A; C/D=308-314.
DR PDB; 4KV4; X-ray; 2.00 A; B=308-314.
DR PDB; 5U4K; NMR; -; B=521-551.
DR PDB; 5URN; NMR; -; B=521-551.
DR PDB; 6NV2; X-ray; 1.13 A; P=39-51.
DR PDB; 6QHL; X-ray; 1.20 A; P=38-51.
DR PDB; 6QHM; X-ray; 1.25 A; P=275-287.
DR PDB; 6YOW; X-ray; 1.23 A; P=39-51.
DR PDB; 6YOX; X-ray; 2.05 A; P=39-51.
DR PDB; 6YOY; X-ray; 1.80 A; P=39-51.
DR PDB; 6YP2; X-ray; 1.80 A; P=39-51.
DR PDB; 6YP3; X-ray; 1.80 A; P=39-51.
DR PDB; 6YP8; X-ray; 1.80 A; P=39-51.
DR PDB; 6YPL; X-ray; 1.80 A; P=39-51.
DR PDB; 6YPY; X-ray; 1.40 A; P=39-51.
DR PDB; 6YQ2; X-ray; 1.40 A; P=39-51.
DR PDB; 7BI3; X-ray; 1.20 A; P=39-51.
DR PDB; 7BIQ; X-ray; 1.20 A; P=39-51.
DR PDB; 7BIW; X-ray; 1.20 A; P=39-51.
DR PDB; 7BIY; X-ray; 1.80 A; P=39-51.
DR PDB; 7BJB; X-ray; 1.80 A; P=39-51.
DR PDB; 7BJF; X-ray; 1.40 A; P=39-51.
DR PDB; 7BJL; X-ray; 1.40 A; P=39-51.
DR PDB; 7BJW; X-ray; 1.40 A; P=39-51.
DR PDB; 7BKH; X-ray; 1.40 A; P=39-51.
DR PDB; 7LET; X-ray; 2.40 A; C=294-315.
DR PDB; 7LEU; X-ray; 2.82 A; B/C=294-315.
DR PDB; 7LF4; X-ray; 2.85 A; D/E=294-315.
DR PDB; 7NJ9; X-ray; 1.40 A; P=39-51.
DR PDB; 7NJB; X-ray; 1.40 A; P=39-51.
DR PDB; 7NK3; X-ray; 1.40 A; P=39-51.
DR PDB; 7NK5; X-ray; 1.40 A; P=39-51.
DR PDB; 7NLA; X-ray; 1.40 A; P=39-51.
DR PDB; 7NLE; X-ray; 1.40 A; P=39-51.
DR PDB; 7NM1; X-ray; 1.40 A; P=39-51.
DR PDB; 7NM3; X-ray; 1.40 A; P=39-51.
DR PDB; 7NM9; X-ray; 1.70 A; P=39-51.
DR PDB; 7NMH; X-ray; 1.40 A; P=39-51.
DR PDB; 7NQP; X-ray; 1.24 A; P=39-51.
DR PDB; 7NR7; X-ray; 1.40 A; P=39-51.
DR PDB; 7NSV; X-ray; 1.33 A; P=39-51.
DR PDB; 7NV4; X-ray; 1.20 A; P=39-51.
DR PDB; 7NVI; X-ray; 1.20 A; P=39-51.
DR PDB; 7NWS; X-ray; 1.20 A; P=39-51.
DR PDB; 7NXS; X-ray; 1.20 A; P=39-51.
DR PDB; 7NXT; X-ray; 1.20 A; P=39-51.
DR PDB; 7NXW; X-ray; 1.20 A; P=39-51.
DR PDB; 7NXY; X-ray; 1.20 A; P=39-51.
DR PDB; 7NY4; X-ray; 1.40 A; P=39-51.
DR PDB; 7NYE; X-ray; 1.40 A; P=39-51.
DR PDB; 7NYF; X-ray; 1.40 A; P=39-51.
DR PDB; 7NYG; X-ray; 1.40 A; P=39-51.
DR PDB; 7NZ6; X-ray; 1.40 A; P=39-51.
DR PDB; 7NZG; X-ray; 1.40 A; P=39-51.
DR PDB; 7NZK; X-ray; 1.40 A; P=39-51.
DR PDB; 7NZV; X-ray; 1.40 A; P=39-51.
DR PDB; 7O34; X-ray; 1.20 A; P=39-51.
DR PDB; 7O3A; X-ray; 1.20 A; P=39-51.
DR PDB; 7O3F; X-ray; 1.40 A; P=39-51.
DR PDB; 7O3P; X-ray; 1.40 A; P=39-51.
DR PDB; 7O3Q; X-ray; 1.80 A; P=39-51.
DR PDB; 7O3R; X-ray; 1.80 A; P=39-51.
DR PDB; 7O3S; X-ray; 2.00 A; P=39-51.
DR PDB; 7O57; X-ray; 1.40 A; P=39-51.
DR PDB; 7O59; X-ray; 1.20 A; P=39-51.
DR PDB; 7O5A; X-ray; 1.80 A; P=39-51.
DR PDB; 7O5C; X-ray; 1.80 A; P=39-51.
DR PDB; 7O5D; X-ray; 1.80 A; P=39-51.
DR PDB; 7O5F; X-ray; 1.80 A; P=39-51.
DR PDB; 7O5G; X-ray; 1.80 A; P=39-51.
DR PDB; 7O5O; X-ray; 1.80 A; P=39-51.
DR PDB; 7O5P; X-ray; 1.80 A; P=39-51.
DR PDB; 7O5S; X-ray; 1.80 A; P=39-51.
DR PDB; 7O5U; X-ray; 1.80 A; P=39-51.
DR PDB; 7O5X; X-ray; 1.80 A; P=39-51.
DR PDB; 7O6F; X-ray; 2.00 A; P=39-51.
DR PDB; 7O6G; X-ray; 1.80 A; P=39-51.
DR PDB; 7O6I; X-ray; 1.80 A; P=39-51.
DR PDB; 7O6J; X-ray; 1.40 A; P=39-51.
DR PDB; 7O6K; X-ray; 1.40 A; P=39-51.
DR PDB; 7O6M; X-ray; 1.40 A; P=39-51.
DR PDB; 7O6O; X-ray; 1.40 A; P=39-51.
DR PDBsum; 1NFI; -.
DR PDBsum; 2LSP; -.
DR PDBsum; 2O61; -.
DR PDBsum; 3GUT; -.
DR PDBsum; 3QXY; -.
DR PDBsum; 3RC0; -.
DR PDBsum; 4KV1; -.
DR PDBsum; 4KV4; -.
DR PDBsum; 5U4K; -.
DR PDBsum; 5URN; -.
DR PDBsum; 6NV2; -.
DR PDBsum; 6QHL; -.
DR PDBsum; 6QHM; -.
DR PDBsum; 6YOW; -.
DR PDBsum; 6YOX; -.
DR PDBsum; 6YOY; -.
DR PDBsum; 6YP2; -.
DR PDBsum; 6YP3; -.
DR PDBsum; 6YP8; -.
DR PDBsum; 6YPL; -.
DR PDBsum; 6YPY; -.
DR PDBsum; 6YQ2; -.
DR PDBsum; 7BI3; -.
DR PDBsum; 7BIQ; -.
DR PDBsum; 7BIW; -.
DR PDBsum; 7BIY; -.
DR PDBsum; 7BJB; -.
DR PDBsum; 7BJF; -.
DR PDBsum; 7BJL; -.
DR PDBsum; 7BJW; -.
DR PDBsum; 7BKH; -.
DR PDBsum; 7LET; -.
DR PDBsum; 7LEU; -.
DR PDBsum; 7LF4; -.
DR PDBsum; 7NJ9; -.
DR PDBsum; 7NJB; -.
DR PDBsum; 7NK3; -.
DR PDBsum; 7NK5; -.
DR PDBsum; 7NLA; -.
DR PDBsum; 7NLE; -.
DR PDBsum; 7NM1; -.
DR PDBsum; 7NM3; -.
DR PDBsum; 7NM9; -.
DR PDBsum; 7NMH; -.
DR PDBsum; 7NQP; -.
DR PDBsum; 7NR7; -.
DR PDBsum; 7NSV; -.
DR PDBsum; 7NV4; -.
DR PDBsum; 7NVI; -.
DR PDBsum; 7NWS; -.
DR PDBsum; 7NXS; -.
DR PDBsum; 7NXT; -.
DR PDBsum; 7NXW; -.
DR PDBsum; 7NXY; -.
DR PDBsum; 7NY4; -.
DR PDBsum; 7NYE; -.
DR PDBsum; 7NYF; -.
DR PDBsum; 7NYG; -.
DR PDBsum; 7NZ6; -.
DR PDBsum; 7NZG; -.
DR PDBsum; 7NZK; -.
DR PDBsum; 7NZV; -.
DR PDBsum; 7O34; -.
DR PDBsum; 7O3A; -.
DR PDBsum; 7O3F; -.
DR PDBsum; 7O3P; -.
DR PDBsum; 7O3Q; -.
DR PDBsum; 7O3R; -.
DR PDBsum; 7O3S; -.
DR PDBsum; 7O57; -.
DR PDBsum; 7O59; -.
DR PDBsum; 7O5A; -.
DR PDBsum; 7O5C; -.
DR PDBsum; 7O5D; -.
DR PDBsum; 7O5F; -.
DR PDBsum; 7O5G; -.
DR PDBsum; 7O5O; -.
DR PDBsum; 7O5P; -.
DR PDBsum; 7O5S; -.
DR PDBsum; 7O5U; -.
DR PDBsum; 7O5X; -.
DR PDBsum; 7O6F; -.
DR PDBsum; 7O6G; -.
DR PDBsum; 7O6I; -.
DR PDBsum; 7O6J; -.
DR PDBsum; 7O6K; -.
DR PDBsum; 7O6M; -.
DR PDBsum; 7O6O; -.
DR AlphaFoldDB; Q04206; -.
DR SMR; Q04206; -.
DR BioGRID; 111902; 387.
DR ComplexPortal; CPX-5828; NF-kappaB DNA-binding transcription factor complex, p50/p65.
DR ComplexPortal; CPX-5829; NF-kappaB DNA-binding transcription factor complex, p52/p65.
DR ComplexPortal; CPX-5834; NF-kappaB DNA-binding transcription factor complex, p65/c-Rel.
DR ComplexPortal; CPX-5835; NF-kappaB DNA-binding transcription factor complex, p65/p65.
DR CORUM; Q04206; -.
DR DIP; DIP-24238N; -.
DR ELM; Q04206; -.
DR IntAct; Q04206; 182.
DR MINT; Q04206; -.
DR STRING; 9606.ENSP00000384273; -.
DR BindingDB; Q04206; -.
DR ChEMBL; CHEMBL5533; -.
DR DrugBank; DB08908; Dimethyl fumarate.
DR DrugBank; DB01296; Glucosamine.
DR DrugBank; DB14059; SC-236.
DR DrugCentral; Q04206; -.
DR GlyGen; Q04206; 7 sites, 2 O-linked glycans (7 sites).
DR iPTMnet; Q04206; -.
DR MetOSite; Q04206; -.
DR PhosphoSitePlus; Q04206; -.
DR SwissPalm; Q04206; -.
DR BioMuta; RELA; -.
DR DMDM; 62906901; -.
DR EPD; Q04206; -.
DR jPOST; Q04206; -.
DR MassIVE; Q04206; -.
DR MaxQB; Q04206; -.
DR PaxDb; Q04206; -.
DR PeptideAtlas; Q04206; -.
DR PRIDE; Q04206; -.
DR ProteomicsDB; 58236; -. [Q04206-1]
DR ProteomicsDB; 58237; -. [Q04206-2]
DR ProteomicsDB; 58238; -. [Q04206-3]
DR ProteomicsDB; 58239; -. [Q04206-4]
DR Antibodypedia; 3557; 3912 antibodies from 51 providers.
DR DNASU; 5970; -.
DR Ensembl; ENST00000308639.13; ENSP00000311508.9; ENSG00000173039.20. [Q04206-4]
DR Ensembl; ENST00000406246.8; ENSP00000384273.3; ENSG00000173039.20. [Q04206-1]
DR GeneID; 5970; -.
DR KEGG; hsa:5970; -.
DR MANE-Select; ENST00000406246.8; ENSP00000384273.3; NM_021975.4; NP_068810.3.
DR UCSC; uc001ofg.4; human. [Q04206-1]
DR CTD; 5970; -.
DR DisGeNET; 5970; -.
DR GeneCards; RELA; -.
DR HGNC; HGNC:9955; RELA.
DR HPA; ENSG00000173039; Low tissue specificity.
DR MalaCards; RELA; -.
DR MIM; 164014; gene.
DR MIM; 618287; phenotype.
DR neXtProt; NX_Q04206; -.
DR OpenTargets; ENSG00000173039; -.
DR Orphanet; 251636; Ependymoma.
DR Orphanet; 476102; Hereditary pediatric Behcet-like disease.
DR Orphanet; 530792; RELA fusion-positive ependymoma.
DR PharmGKB; PA296; -.
DR VEuPathDB; HostDB:ENSG00000173039; -.
DR eggNOG; ENOG502QT4Z; Eukaryota.
DR GeneTree; ENSGT00940000159867; -.
DR InParanoid; Q04206; -.
DR OMA; PVRVHMQ; -.
DR OrthoDB; 916931at2759; -.
DR PhylomeDB; Q04206; -.
DR TreeFam; TF325632; -.
DR PathwayCommons; Q04206; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1.
DR Reactome; R-HSA-193692; Regulated proteolysis of p75NTR.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-209560; NF-kB is activated and signals survival.
DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-HSA-448706; Interleukin-1 processing.
DR Reactome; R-HSA-4755510; SUMOylation of immune response proteins.
DR Reactome; R-HSA-5603029; IkBA variant leads to EDA-ID.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-HSA-5660668; CLEC7A/inflammasome pathway.
DR Reactome; R-HSA-844456; The NLRP3 inflammasome.
DR Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
DR Reactome; R-HSA-9660826; Purinergic signaling in leishmaniasis infection.
DR SABIO-RK; Q04206; -.
DR SignaLink; Q04206; -.
DR SIGNOR; Q04206; -.
DR BioGRID-ORCS; 5970; 130 hits in 1106 CRISPR screens.
DR ChiTaRS; RELA; human.
DR EvolutionaryTrace; Q04206; -.
DR GeneWiki; RELA; -.
DR GenomeRNAi; 5970; -.
DR Pharos; Q04206; Tchem.
DR PRO; PR:Q04206; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q04206; protein.
DR Bgee; ENSG00000173039; Expressed in mucosa of stomach and 201 other tissues.
DR ExpressionAtlas; Q04206; baseline and differential.
DR Genevisible; Q04206; HS.
DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0071159; C:NF-kappaB complex; IPI:ComplexPortal.
DR GO; GO:0035525; C:NF-kappaB p50/p65 complex; IDA:CAFA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:UniProtKB.
DR GO; GO:0042805; F:actinin binding; IPI:UniProtKB.
DR GO; GO:0071532; F:ankyrin repeat binding; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
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; IPI:BHF-UCL.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0019899; F:enzyme binding; IPI:ARUK-UCL.
DR GO; GO:0140296; F:general transcription initiation factor binding; IPI:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
DR GO; GO:0042277; F:peptide binding; IPI:CAFA.
DR GO; GO:0042301; F:phosphate ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:ARUK-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
DR GO; GO:0006968; P:cellular defense response; NAS:UniProtKB.
DR GO; GO:1904385; P:cellular response to angiotensin; IMP:BHF-UCL.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; IDA:UniProtKB.
DR GO; GO:0071354; P:cellular response to interleukin-6; IMP:BHF-UCL.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:ARUK-UCL.
DR GO; GO:0071223; P:cellular response to lipoteichoic acid; IMP:UniProtKB.
DR GO; GO:0071316; P:cellular response to nicotine; IMP:BHF-UCL.
DR GO; GO:0071224; P:cellular response to peptidoglycan; IMP:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IMP:BHF-UCL.
DR GO; GO:0006325; P:chromatin organization; IEA:Ensembl.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0002357; P:defense response to tumor cell; IDA:ARUK-UCL.
DR GO; GO:0051607; P:defense response to virus; NAS:UniProtKB.
DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IGI:BHF-UCL.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:BHF-UCL.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; IMP:BHF-UCL.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0033234; P:negative regulation of protein sumoylation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IGI:ARUK-UCL.
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; IDA:MGI.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISS:ARUK-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IEA:Ensembl.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IGI:ARUK-UCL.
DR GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; IMP:ARUK-UCL.
DR GO; GO:2000630; P:positive regulation of miRNA metabolic process; IMP:BHF-UCL.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IMP:BHF-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:MGI.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:CAFA.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IMP:CAFA.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; IEA:Ensembl.
DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR GO; GO:0043620; P:regulation of DNA-templated transcription in response to stress; IMP:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IGI:CAFA.
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; IMP:CAFA.
DR GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
DR GO; GO:0070555; P:response to interleukin-1; IGI:BHF-UCL.
DR GO; GO:0032495; P:response to muramyl dipeptide; IEA:Ensembl.
DR GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
DR GO; GO:0010033; P:response to organic substance; IDA:UniProtKB.
DR GO; GO:0010224; P:response to UV-B; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IDA:UniProtKB.
DR CDD; cd01177; IPT_NFkappaB; 1.
DR DisProt; DP00085; -.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.340; -; 1.
DR IDEAL; IID00207; -.
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;
KW Chromosomal rearrangement; Cytoplasm; Disease variant; DNA-binding;
KW Host-virus interaction; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; S-nitrosylation; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..551
FT /note="Transcription factor p65"
FT /id="PRO_0000205169"
FT DOMAIN 19..306
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT REGION 309..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..389
FT /note="Transcriptional activation domain 3"
FT /evidence="ECO:0000250|UniProtKB:Q04207"
FT REGION 415..476
FT /note="Transcriptional activation domain 1"
FT /evidence="ECO:0000269|PubMed:1732726"
FT REGION 506..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..551
FT /note="Transcriptional activation domain 2"
FT /evidence="ECO:0000250|UniProtKB:Q04207"
FT MOTIF 301..304
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 536..544
FT /note="9aaTAD"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 38
FT /note="Cysteine persulfide; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 38
FT /note="S-nitrosocysteine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04207"
FT MOD_RES 122
FT /note="N6-acetyllysine; by PCAF and EP300; alternate"
FT /evidence="ECO:0000269|PubMed:12419806"
FT MOD_RES 123
FT /note="N6-acetyllysine; by PCAF and EP300; alternate"
FT /evidence="ECO:0000269|PubMed:12419806"
FT MOD_RES 218
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:12456660"
FT MOD_RES 221
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:12456660"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14690596"
FT MOD_RES 276
FT /note="Phosphoserine; by RPS6KA4 and RPS6KA5"
FT /evidence="ECO:0000269|PubMed:12628924"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:15516339"
FT MOD_RES 310
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:12456660,
FT ECO:0000269|PubMed:16135789, ECO:0000269|PubMed:17000776,
FT ECO:0000269|PubMed:19103749, ECO:0007744|PubMed:19608861"
FT MOD_RES 310
FT /note="N6-methyllysine; by SETD6; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q04207"
FT MOD_RES 311
FT /note="Phosphoserine; by PKC/PRKCZ"
FT /evidence="ECO:0000250|UniProtKB:Q04207"
FT MOD_RES 435
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15073167"
FT MOD_RES 468
FT /note="Phosphoserine; by IKKB and IKKE"
FT /evidence="ECO:0000269|PubMed:16046471,
FT ECO:0000269|PubMed:16407239"
FT MOD_RES 505
FT /note="Phosphothreonine; by CHEK1"
FT /evidence="ECO:0000269|PubMed:15775976"
FT MOD_RES 529
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:10938077"
FT MOD_RES 536
FT /note="Phosphoserine; by IKKB"
FT /evidence="ECO:0000269|PubMed:10521409,
FT ECO:0000269|PubMed:17785205"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO3)"
FT /evidence="ECO:0000269|PubMed:22649547"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO3); alternate"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO3); alternate"
FT VAR_SEQ 13..25
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7907305"
FT /id="VSP_005587"
FT VAR_SEQ 143..145
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031245"
FT VAR_SEQ 222..231
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1732726"
FT /id="VSP_012031"
FT VAR_SEQ 506
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7907305"
FT /id="VSP_005588"
FT VARIANT 246..549
FT /note="Missing (found in a patient diagnosed with
FT autoimmune lymphoproliferative syndrome; unknown
FT pathological significance)"
FT /evidence="ECO:0000269|PubMed:29305315"
FT /id="VAR_081858"
FT MUTAGEN 254
FT /note="T->A: Abolishes interaction with PIN1."
FT /evidence="ECO:0000269|PubMed:14690596"
FT MUTAGEN 276
FT /note="S->C: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:12628924"
FT CONFLICT 49
FT /note="E -> R (in Ref. 2; CAA80524)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="S -> P (in Ref. 1; AAA36408)"
FT /evidence="ECO:0000305"
FT CONFLICT 372..380
FT /note="QISQASALA -> RSARPRLG (in Ref. 2; CAA80524)"
FT /evidence="ECO:0000305"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 68..80
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:2O61"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1NFI"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2O61"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:1NFI"
FT TURN 130..137
FT /evidence="ECO:0007829|PDB:1NFI"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:2O61"
FT STRAND 156..166
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:1NFI"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:1NFI"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:2O61"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:1NFI"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:1NFI"
FT HELIX 294..302
FT /evidence="ECO:0007829|PDB:1NFI"
FT HELIX 306..312
FT /evidence="ECO:0007829|PDB:1NFI"
FT STRAND 527..534
FT /evidence="ECO:0007829|PDB:5U4K"
FT TURN 535..540
FT /evidence="ECO:0007829|PDB:5U4K"
FT HELIX 542..550
FT /evidence="ECO:0007829|PDB:5U4K"
SQ 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
