[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). DOI=10.1126/science.2006423; PubMed=2006423 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1093/hmg/2.11.1895; PubMed=8281153 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1016/0378-1119(94)90823-0; PubMed=7907305 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1038/26254; PubMed=9751059 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1074/jbc.274.43.30353; PubMed=10521409 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1038/sj.onc.1202904; PubMed=10498867 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1074/jbc.275.6.4383; PubMed=10660609 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1074/jbc.M001358200; PubMed=10938077 [NCBI, ExPASy, EBI, Israel, Japan] 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]	ACETYLATION, AND INTERACTION WITH HDAC3. DOI=10.1126/science.1062374; PubMed=11533489 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[19]	INTERACTION WITH ETHE1. DOI=10.1016/S1535-6108(02)00152-6; PubMed=12398897 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[20]	ACETYLATION AT LYS-218; LYS-221 AND LYS-310. DOI=10.1093/emboj/cdf660; PubMed=12456660 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[21]	INTERACTION WITH CBP AND HDAC1, AND PHOSPHORYLATION. DOI=10.1016/S1097-2765(02)00477-X; PubMed=11931769 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[22]	INTERACTION WITH RPS6KA5, MUTAGENESIS OF SER-276, AND PHOSPHORYLATION AT SER-276. DOI=10.1093/emboj/cdg139; PubMed=12628924 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[23]	ACETYLATION AT LYS-122 AND LYS-123. DOI=10.1074/jbc.M209572200; PubMed=12419806 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[24]	INTERACTION WITH GSK3B. DOI=10.1074/jbc.M305676200; PubMed=12871932 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[25]	PHOSPHORYLATION AT THR-254, INTERACTION WITH PIN1 AND SOCS1, AND MUTAGENESIS OF THR-254. DOI=10.1016/S1097-2765(03)00490-8; PubMed=14690596 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[26]	INTERACTION WITH UNC5CL. DOI=10.1074/jbc.M310737200; PubMed=14769797 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[27]	PHOSPHORYLATION AT THR-435. DOI=10.1074/jbc.M402362200; PubMed=15073167 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[28]	UBIQUITINATION. DOI=10.1084/jem.20040196; PubMed=15226358 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[29]	INTERACTION WITH ING4. DOI=10.1038/nature02329; PubMed=15029197 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[30]	PHOSPHORYLATION AT THR-505. DOI=10.1038/sj.emboj.7600608; PubMed=15775976 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[31]	PHOSPHORYLATION AT SER-468. DOI=10.1096/fj.05-3736fje; PubMed=16046471 [NCBI, ExPASy, EBI, Israel, Japan] Schwabe R.F., Sakurai H.; "IKKbeta phosphorylates p65 at S468 in transactivaton domain 2."; FASEB J. 19:1758-1760(2005).
[32]	PHOSPHORYLATION AT SER-281. DOI=10.1074/jbc.M409344200; PubMed=15516339 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[33]	ACETYLATION AT LYS-310. DOI=10.1128/MCB.25.18.7966-7975.2005; PubMed=16135789 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[34]	INTERACTION WITH HRSV PROTEIN M2-1. DOI=10.1016/j.virol.2004.10.031; PubMed=15629770 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[35]	INTERACTION WITH MTDH. DOI=10.1158/0008-5472.CAN-05-3029; PubMed=16452207 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[36]	INTERACTION WITH USP48. DOI=10.1016/j.cellsig.2005.03.017; PubMed=16214042 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[37]	PHOSPHORYLATION AT SER-468. DOI=10.1074/jbc.M508045200; PubMed=16407239 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[38]	INTERACTION WITH CARM1. DOI=10.1210/me.2005-0365; PubMed=16497732 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[39]	IDENTIFICATION IN THE NF-KAPPA-B P65-P52 COMPLEX. DOI=10.1073/pnas.0511096103; PubMed=16477006 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[40]	FUNCTION, AND INTERACTION WITH RELA. DOI=10.1083/jcb.200611081; PubMed=17620405 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[41]	X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). DOI=10.1016/S0092-8674(00)81698-0; PubMed=9865693 [NCBI, ExPASy, EBI, Israel, Japan] Jacobs M.D., Harrison S.C.; "Structure of an IkappaBalpha/NF-kappaB complex."; Cell 95:749-758(1998).

Comments

FUNCTION: NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed 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.
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 (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. Interacts with human respiratory syncytial virus (HRSV) protein M2-1.
INTERACTION:
Self; NbExp=3; IntAct=EBI-73886, EBI-73886;
Q9NY61:AATF; NbExp=2; IntAct=EBI-73886, EBI-372428;
P18847:ATF3; NbExp=1; IntAct=EBI-73886, EBI-712767;
Q96JB5:CDK5RAP3; NbExp=3; IntAct=EBI-73886, EBI-718818;
O15111:CHUK; NbExp=1; IntAct=EBI-73886, EBI-81249;
Q8N668:COMMD1; NbExp=2; IntAct=EBI-73886, EBI-1550112;
Q92793:CREBBP; NbExp=1; IntAct=EBI-73886, EBI-81215;
Q08211:DHX9; NbExp=3; IntAct=EBI-73886, EBI-352022;
Q13547:HDAC1; NbExp=2; IntAct=EBI-73886, EBI-301834;
Q86UE4:MTDH; NbExp=1; IntAct=EBI-73886, EBI-1046588;
P19838:NFKB1; NbExp=2; IntAct=EBI-73886, EBI-300010;
P25963:NFKBIA; NbExp=3; IntAct=EBI-73886, EBI-307386;
Q15653:NFKBIB; NbExp=3; IntAct=EBI-73886, EBI-352889;
Q14690:PDCD11; NbExp=1; IntAct=EBI-73886, EBI-300028;
Q04864:REL; NbExp=2; IntAct=EBI-73886, EBI-307352;
P23396:RPS3; NbExp=5; IntAct=EBI-73886, EBI-351193;
O75582:RPS6KA5; NbExp=1; IntAct=EBI-73886, EBI-73869;
Q8N6T7:SIRT6; NbExp=3; IntAct=EBI-73886, EBI-712415;
P21980:TGM2; NbExp=2; IntAct=EBI-73886, EBI-727668;
Q13625-2:TP53BP2; NbExp=5; IntAct=EBI-73886, EBI-287091;
Q9UBK9:UXT; NbExp=3; IntAct=EBI-73886, EBI-357355;
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B).

ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	p65
Isoform ID	Q04206-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	p65 delta 2
Isoform ID	Q04206-2
Features which should be applied to build the isoform sequence: VSP_005587, VSP_005588.

Name	3
Synonyms	p65 delta
Isoform ID	Q04206-3
Features which should be applied to build the isoform sequence: VSP_012031.

Name	4
Isoform ID	Q04206-4
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_031245.

PTM: Ubiquitinated, leading to its proteosomal degradation. Degradation is required for termination of NF-kappa-B response.
PTM: Phosphorylation on 'Ser-536' stimulates acetylation on 'Lys-310' and interaction with CBP; the phosphorylated and acetylated forms show enhanced transcriptional activity.
PTM: Reversibly acetylated; the acetylation seems to be mediated by CBP, the deacetylation by HDAC3. 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 can also lower DNA-binding and results in nuclear export.
SIMILARITY: Contains 1 RHD (Rel-like) domain.
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/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M62399; AAA36408.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z22948; CAA80524.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z22949; CAA80524.2; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z22953; CAA80524.2; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z22950; CAA80524.2; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z22951; CAA80524.2; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L19067; AAA20946.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC033522; AAH33522.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY455868; AAR13863.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00219084; -.
IPI00386448; -.
IPI00479470; -.
IPI00884950; -.

PIR

A40851; A40851.
I53719; I53719.
S51782; A42017.

RefSeq

NP_001138610.1; -.
NP_068810.3; -.

UniGene

Hs.502875

3D structure databases

PDB

1NFI; X-ray; 2.70 A; A/C=20-320.	[ExPASy / RCSB / EBI]
2O61; X-ray; 2.80 A; A=20-291.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

1NFI; -.
2O61; -.

DP00085; -.

Protein-protein interaction databases

DIP

DIP:170N; -.
DIP:24238N; -.

IntAct

Q04206; 126.

PTM databases

PhosphoSite

Q04206; -.

Enzyme and pathway databases

Pathway_Interaction_DB

angiopoietinreceptor_pathway; Angiopoietin receptor Tie2-mediated signaling.
nfkappabatypicalpathway; Atypical NF-kappaB pathway.
bcr_5pathway; BCR signaling pathway.
nfkappabcanonicalpathway; Canonical NF-kappaB pathway.
ceramidepathway; Ceramide signaling pathway.
fcer1pathway; Fc-epsilon receptor I signaling in mast cells.
hivnefpathway; HIV-1 Nef: Negative effector of Fas and TNF-alpha.
il1pathway; IL1-mediated signaling events.
il12_2pathway; IL12-mediated signaling events.
il2_pi3kpathway; IL2 signaling events mediated by PI3K.
il23pathway; IL23-mediated signaling events.
lysophospholipid_pathway; LPA receptor mediated events.
avb3_opn_pathway; Osteopontin-mediated events.
hdac_classi_pathway; Signaling events mediated by HDAC Class I.
tnfpathway; TNF receptor signaling pathway.

Reactome

REACT_11061; Signalling by NGF.
REACT_6900; Signaling in Immune system.

Organism-specific databases

GC11M065178; -.

HIX0009804; -.

HGNC:9955; RELA.

CAB004264; -.
CAB005030; -.

MIM

164014; gene. [NCBI / EBI]

PharmGKB

PA296; -.

Gene expression databases

Q04206; -.

Q04206; -.

HS_RELA; -.

ENSG00000173039; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005667;	Cellular component: transcription factor complex (inferred from direct assay from UniProtKB).
GO:0042802;	Molecular function: identical protein binding (inferred from direct assay from UniProtKB).
GO:0051059;	Molecular function: NF-kappaB binding (inferred from physical interaction from UniProtKB).
GO:0042301;	Molecular function: phosphate binding (inferred from direct assay from UniProtKB).
GO:0019901;	Molecular function: protein kinase binding (inferred from physical interaction from UniProtKB).
GO:0047485;	Molecular function: protein N-terminus binding (inferred from physical interaction from UniProtKB).
GO:0003705;	Molecular function: RNA polymerase II transcription factor activity, enhancer binding (inferred from direct assay from UniProtKB).
GO:0006916;	Biological process: anti-apoptosis (inferred from direct assay from UniProtKB).
GO:0006968;	Biological process: cellular defense response (non-traceable author statement from UniProtKB).
GO:0019221;	Biological process: cytokine-mediated signaling pathway (inferred from direct assay from UniProtKB).
GO:0051607;	Biological process: defense response to virus (non-traceable author statement from UniProtKB).
GO:0006954;	Biological process: inflammatory response (inferred from direct assay from UniProtKB).
GO:0043123;	Biological process: positive regulation of I-kappaB kinase/NF-kappaB cascade (inferred from expression pattern from UniProtKB).
GO:0051092;	Biological process: positive regulation of NF-kappaB transcription factor activity (inferred from direct assay from MGI).
GO:0010033;	Biological process: response to organic substance (inferred from direct assay from UniProtKB).
GO:0010224;	Biological process: response to UV-B (inferred from direct assay from UniProtKB).
GO:0006350;	Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013783; Ig-like_fold.
IPR002909; IPT_TIG_rcpt.
IPR000451; NF_Rel_dor.
IPR011539; RHD.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.10; Ig-like_fold; 1.
G3DSA:2.60.40.340; RHD; 1.

Pfam

PF00554; RHD; 1.
PF01833; TIG; 1.
Pfam graphical view of domain structure.

PRINTS

PR00057; NFKBTNSCPFCT.

SMART

SM00429; IPT; 1.
SMART graphical view of domain structure.

PROSITE

PS01204; REL_1; 1.
PS50254; REL_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

Q04206; -.

Genome annotation databases

Ensembl

ENSG00000173039; Homo sapiens. [Contig view]

GeneID

5970; -.

KEGG

hsa:5970; -.

NMPDR

fig|9606.3.peg.6043; -.

Phylogenomic databases

HOGENOM

Q04206; -.

HOVERGEN

Q04206; -.

Other

23241; -.

RELA; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Activator; Alternative splicing; Cytoplasm; DNA-binding; Host-virus interaction; Nucleus; Phosphoprotein; Transcription; Transcription regulation; Ubl conjugation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 551`	`551`	`Transcription factor p65.`	`PRO_0000205169`
`DOMAIN`	`19 306`	`288`	`RHD.`
`REGION`	`415 459`	`45`	`Activation domain.`
`MOTIF`	`301 304`	`4`	`Nuclear localization signal (Potential).`
`MOD_RES`	`122 122`		`N6-acetyllysine; by PCAF and EP300.`
`MOD_RES`	`123 123`		`N6-acetyllysine; by PCAF and EP300.`
`MOD_RES`	`254 254`		`Phosphothreonine.`
`MOD_RES`	`276 276`		`Phosphoserine; by RPS6KA4 and RPS6KA5.`
`MOD_RES`	`281 281`		`Phosphoserine (Probable).`
`MOD_RES`	`310 310`		`N6-acetyllysine.`
`MOD_RES`	`311 311`		`Phosphoserine; by PKC/PRKCZ (By similarity).`
`MOD_RES`	`435 435`		`Phosphothreonine.`
`MOD_RES`	`468 468`		`Phosphoserine; by IKKB and IKKE.`
`MOD_RES`	`505 505`		`Phosphothreonine; by CHK1.`
`MOD_RES`	`529 529`		`Phosphoserine; by CK2.`
`MOD_RES`	`536 536`		`Phosphoserine; by IKKB.`
`VAR_SEQ`	`13 25`		`Missing (in isoform 2).`	`VSP_005587`
`VAR_SEQ`	`143 145`		`Missing (in isoform 4).`	`VSP_031245`
`VAR_SEQ`	`222 231`		`Missing (in isoform 3).`	`VSP_012031`
`VAR_SEQ`	`506 506`		`Missing (in isoform 2).`	`VSP_005588`
`MUTAGEN`	`254 254`		`T->A: Abolishes interaction with PIN1.`
`MUTAGEN`	`276 276`		`S->C: Loss of phosphorylation.`
`CONFLICT`	`49 49`		`E -> R (in Ref. 2; CAA80524).`
`CONFLICT`	`180 180`		`S -> P (in Ref. 1; AAA36408).`
`CONFLICT`	`372 380`		`QISQASALA -> RSARPRLG (in Ref. 2; CAA80524).`
`STRAND`	`21 25`	`5`
`STRAND`	`30 32`	`3`
`STRAND`	`39 41`	`3`
`STRAND`	`53 55`	`3`
`STRAND`	`60 63`	`4`
`STRAND`	`68 80`	`13`
`STRAND`	`87 92`	`6`
`STRAND`	`97 104`	`8`
`STRAND`	`117 119`	`3`
`HELIX`	`126 129`	`4`
`TURN`	`130 137`	`8`
`STRAND`	`156 166`	`11`
`STRAND`	`168 173`	`6`
`STRAND`	`183 188`	`6`
`STRAND`	`196 200`	`5`
`STRAND`	`202 205`	`4`
`STRAND`	`211 217`	`7`
`STRAND`	`225 230`	`6`
`STRAND`	`233 238`	`6`
`HELIX`	`241 243`	`3`
`TURN`	`246 248`	`3`
`STRAND`	`249 253`	`5`
`STRAND`	`266 273`	`8`
`TURN`	`275 277`	`3`
`STRAND`	`284 289`	`6`
`HELIX`	`294 302`	`9`
`HELIX`	`306 312`	`7`

Sequence information

Length: 551 AA [This is the length of the unprocessed precursor]

Molecular weight: 60219 Da [This is the MW of the unprocessed precursor]

CRC64: 8147A6AF9F2445C6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDELFPLIFP AEPAQASGPY VEIIEQPKQR GMRFRYKCEG RSAGSIPGER STDTTKTHPT 

        70         80         90        100        110        120 
IKINGYTGPG TVRISLVTKD PPHRPHPHEL VGKDCRDGFY EAELCPDRCI HSFQNLGIQC 

       130        140        150        160        170        180 
VKKRDLEQAI SQRIQTNNNP FQVPIEEQRG DYDLNAVRLC FQVTVRDPSG RPLRLPPVLS 

       190        200        210        220        230        240 
HPIFDNRAPN TAELKICRVN RNSGSCLGGD EIFLLCDKVQ KEDIEVYFTG PGWEARGSFS 

       250        260        270        280        290        300 
QADVHRQVAI VFRTPPYADP SLQAPVRVSM QLRRPSDREL SEPMEFQYLP DTDDRHRIEE 

       310        320        330        340        350        360 
KRKRTYETFK SIMKKSPFSG PTDPRPPPRR IAVPSRSSAS VPKPAPQPYP FTSSLSTINY 

       370        380        390        400        410        420 
DEFPTMVFPS GQISQASALA PAPPQVLPQA PAPAPAPAMV SALAQAPAPV PVLAPGPPQA 

       430        440        450        460        470        480 
VAPPAPKPTQ AGEGTLSEAL LQLQFDDEDL GALLGNSTDP AVFTDLASVD NSEFQQLLNQ 

       490        500        510        520        530        540 
GIPVAPHTTE PMLMEYPEAI TRLVTGAQRP PDPAPAPLGA PGLPNGLLSG DEDFSSIADM 

       550 
DFSALLSQIS S

Q04206 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools