Transcription Factor

Accessions: T138173_1.02 (CISBP 1.02), TF65_HUMAN (HOCOMOCO 10), Q04206 (JASPAR 2024)
Names: RELA, T138173_1.02;, Nuclear factor NF-kappa-B p65 subunit, Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3, TF65_HUMAN, Transcription factor p65
Organisms: Homo sapiens
Libraries: CISBP 1.02 1, HOCOMOCO 10 2, JASPAR 2024 3
1 Weirauch MT, Yang A, Albu M, Cote AG, Montenegro-Montero A, Drewe P, Najafabadi HS, Lambert SA, Mann I, Cook K, Zheng H, Goity A, van Bakel H, Lozano JC, Galli M, Lewsey MG, Huang E, Mukherjee T, Chen X, Reece-Hoyes JS, Govindarajan S, Shaulsky G, et al. Determination and inference of eukaryotic transcription factor sequence specificity. Cell. 2014 Sep 11;158(6):1431-43. doi: 10.1016/j.cell.2014.08.009. [Pubmed]
2 Kulakovskiy IV, Vorontsov IE, Yevshin IS, Soboleva AV, Kasianov AS, Ashoor H, Ba-Alawi W, Bajic VB, Medvedeva YA, Kolpakov FA, Makeev VJ. HOCOMOCO: expansion and enhancement of the collection of transcription factor binding sites models. Nucleic Acids Res : (2016). [Pubmed]
3 Rauluseviciute I, Riudavets-Puig R, Blanc-Mathieu R, Castro-Mondragon JA, Ferenc K, Kumar V, Lemma RB, Lucas J, Cheneby J, Baranasic D, Khan A, Fornes O, Gundersen S, Johansen M, Hovig E, Lenhard B, Sandelin A, Wasserman WW, Parcy F, Mathelier A. JASPAR 2024: 20th anniversary of the open-access database of transcription factor binding profiles. Nucleic Acids Res : (2023). [Pubmed]
Uniprot: Q04206
Notes: experiment type:ChIP-seq, family:Rel
Length: 551
Pfam Domains: 21-186 Rel homology domain (RHD)
Sequence:
(in bold interface residues)
1 MDELFPLIFPAEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPT 60
61 IKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGFYEAELCPDRCIHSFQNLGIQC 120
121 VKKRDLEQAISQRIQTNNNPFQVPIEEQRGDYDLNAVRLCFQVTVRDPSGRPLRLPPVLS 180
181 HPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFS 240
241 QADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEE 300
301 KRKRTYETFKSIMKKSPFSGPTDPRPPPRRIAVPSRSSASVPKPAPQPYPFTSSLSTINY 360
361 DEFPTMVFPSGQISQASALAPAPPQVLPQAPAPAPAPAMVSALAQAPAPVPVLAPGPPQA 420
421 VAPPAPKPTQAGEGTLSEALLQLQFDDEDLGALLGNSTDPAVFTDLASVDNSEFQQLLNQ 480
481 GIPVAPHTTEPMLMEYPEAITRLVTGAQRPPDPAPAPLGAPGLPNGLLSGDEDFSSIADM 540
541 DFSALLSQISS
Interface Residues: 33, 35, 36, 38, 39, 41, 42, 43, 135, 187, 189, 218, 246, 404, 405, 450, 487
3D-footprint Homologues: 2o61_A, 1imh_C, 2ram_A, 1a3q_A, 1nfk_A, 7cli_B, 1a66_A, 1gji_A, 2bgw_A
Binding Motifs: M4444_1.02 rGGGrmTTTCCmrr
TF65_HUMAN.H10MO.A|M01566 GGGrmTTyCCm
MA0107.1 gGGraTTTCC
Binding Sites: MA0107.1.1
MA0107.1.10
MA0107.1.11
MA0107.1.12
MA0107.1.13
MA0107.1.14
MA0107.1.15
MA0107.1.16
MA0107.1.17
MA0107.1.18
MA0107.1.2
MA0107.1.3
MA0107.1.4
MA0107.1.5
MA0107.1.6
MA0107.1.7
MA0107.1.8
MA0107.1.9
Publications: Kunsch C., Ruben S. M., Rosen C. A. Selection of optimal kappaB/Rel DNA-binding motifs: interaction of both subunits of NF-kappaB with DNA is required for transcriptional activation. Mol. Cell. Biol. 12:4412-4421 (1992). [Pubmed]
Related annotations: PaperBLAST

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