ETS1

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ETS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1GVJ, 2NNY, 2STT, 2STW, 3MFK, 3RI4, 3WTS, 3WTT, 3WTU, 3WTV, 3WTW, 3WTX, 3WTY, 3WTZ, 3WU0, 3WU1, 4L0Y, 4L0Z, 4L18, 4LG0
Identifiers
Aliases	ETS1, ETS-1, EWSR2, p54, c-ets-1, ETS proto-oncogene 1, transcription factor
External IDs	MGI: 95455 HomoloGene: 3837 GeneCards: ETS1
Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11q24.3 Start 128,458,761 bp[1] End 128,587,558 bp[1]
Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9 A4|9 17.97 cM Start 32,636,221 bp[2] End 32,757,820 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • DNA binding • sequence-specific DNA binding • transcription factor activity, sequence-specific DNA binding • transcription factor binding • protein binding • identical protein binding • transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding • RNA polymerase II core promoter proximal region sequence-specific DNA binding • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding • sequence-specific double-stranded DNA binding • RNA polymerase II transcription factor activity, sequence-specific DNA binding • histone acetyltransferase binding • transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding Cellular component • cytoplasm • transcription factor complex • nucleoplasm • cell nucleus Biological process • regulation of apoptotic process • pituitary gland development • response to estradiol • response to interleukin-1 • response to hypoxia • regulation of transcription, DNA-templated • positive regulation of erythrocyte differentiation • cell motility • estrous cycle • immune system process • regulation of transcription from RNA polymerase II promoter • response to antibiotic • female pregnancy • angiogenesis involved in wound healing • positive regulation of cell migration • response to mechanical stimulus • response to laminar fluid shear stress • negative regulation of cell cycle • regulation of angiogenesis • transcription from RNA polymerase II promoter • regulation of extracellular matrix disassembly • transcription, DNA-templated • positive regulation of endothelial cell migration • positive regulation of transcription, DNA-templated • PML body organization • response to wounding • immune response • positive regulation of cell proliferation • hypothalamus development • positive regulation of cellular component movement • negative regulation of inflammatory response • positive regulation of transcription from RNA polymerase II promoter • negative regulation of cell proliferation • cellular response to hydrogen peroxide • positive regulation of inflammatory response • pri-miRNA transcription from RNA polymerase II promoter • positive regulation of leukocyte adhesion to vascular endothelial cell • positive regulation of gene expression • positive regulation of blood vessel endothelial cell migration • positive regulation of angiogenesis • cell differentiation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	2113	23871
Ensembl	ENSG00000134954	ENSMUSG00000032035
UniProt	P14921	P27577
RefSeq (mRNA)	NM_001143820 NM_001162422 NM_005238 NM_001330451	NM_001038642 NM_011808
RefSeq (protein)	NP_001137292 NP_001155894 NP_001317380 NP_005229	NP_001033731 NP_035938
Location (UCSC)	Chr 11: 128.46 – 128.59 Mb	Chr 9: 32.64 – 32.76 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Protein C-ets-1 is a protein that in humans is encoded by the ETS1 gene.^[5] The protein encoded by this gene belongs to the ETS family of transcription factors.^[6]

Contents

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  1 Function
  


• 
  2 Knockout mice
  


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  3 Clinical significance
  


• 
  4 Interactions
  


• 
  5 Interaction with DNA repair promoters and proteins
  
  
  
  • 
    5.1 DNA repair promoters
    
  
  
  • 
    5.2 DNA repair protein interactions
    
  
  
  
  


• 
  6 References
  


• 
  7 Further reading
  


• 
  8 External links
  

Function

There are 28 ETS genes in humans and 27 in mice. They bind the DNA via their winged-helix-turn-helix DNA binding motif known as the Ets domain that specifically recognizes DNA sequences that contain a GGAA/T core element. However, Ets proteins differ significantly in their preference for the sequence flanking the GGAA/T core motif. For instance, the consensus sequence for Ets1 is PuCC/a-GGAA/T-GCPy. On the other hand, many natural Ets1-responsive GGAA/T elements differ from this consensus sequence. The later suggests that several other transcription factors may facilitate Ets1 binding to unfavorable DNA sequences. ChIP-Seq studies have shown that Ets1 can bind both AGGAAG and CGGAAG motifs.^[7]

Ets1 binds to DNA as a monomer. Phosphorylation of serine residues of the C-terminal domain (in the nucleotide sequence they belong to exon VII) known as autoinhibition makes Ets1 inactive. There are several ways to activate Ets1. First, Ets1 can be dephosphorylated. Second, two Ets1 can be activated If two Ets molecules homodimerize. The homodimerization occurs if DNA binding sites are present in the correct orientation and spacing. Thus, the exact layout of binding sites within an enhancer or promoter segment to either relieve or allow autoinhibition of Ets1 to occur may strongly influence whether or not Ets1 actually binds to particular site. Third, Ets1 can be activated by Erk2 and Ras at Thr38. The truncated isoform cannot be phosphorylated by the Erk2. It is localized in the cytoplasm and acts as a dominant negative isoform. Contrary, another isoform that misses exon VII is constitutively active. Many Ras responsive genes harbor combinatorial Ets/AP1 recognition motifs through which Ets1 and AP1 synergistically activate transcription when stimulated by Ras.^[8]

In adult humans, Ets1 is expressed at high levels mainly in immune tissues such as thymus, spleen, and lymph node (B cells, T cells, NK cells, and NK T cells and non-lymphoid immune cells).
An enforced expression of Ets1 blocks differentiation of B- and T-cells. Contrary, knocking Ets1 down is causing multiple defects in the immune system.

Knockout mice

Ets1 knockout mice have aberrant thymic differentiation, reduced peripheral T cell numbers, reduced IL-2 production, a skewing towards a memory/effector phenotype and impairments in the production of Th1 and Th2 cytokines. Although Ets1 knockout mice have an impaired development of Th1, Th2, and Treg cells, they have higher numbers of Th17 cells. In CD4/CD8 double positive thymocytes from Ets knockout mice, both the suppression of gene expression programs corresponding to alternative lineages and upregulation of T-cell specific genes are impaired.^[7] There are also partial defects in bone marrow B cell development with reduced cellularity and inefficient transition from pro-B to pre-B cell stages.

Clinical significance

Meta-analyses of multiple genome-wide association studies has suggested an association of SNPs in the ETS1 locus with psoriasis in European populations. This is not surprising because Ets1 is a negative regulator of Th17 cells.

Ets1 overexpression in stratified squamous epithelial cells causes pro-oncogenic changes, such as suspension of terminal differentiation, high secretion of matrix metalloproteases (Mmps), epidermal growth factor ligands, and inflammatory mediators.

Interactions

Ets1 directly interacts with various transcription factors. Their interaction results in formation of multiprotein complexes. When Ets1 interacts with other transcription factors (Runx1, Pax5, TFE3, and USF1) its final effect on transcription depends on whether C-terminal domain is phosphorylated. Acetyltransferases CBP and p300 bind to the transactivation domain. AP1, STAT5 and VDR bind to C-terminal domain.

Also, ETS1 has been shown to interact with TTRAP,^[9]UBE2I^[10] and Death associated protein 6.^[11]

Importantly, ETS1 was shown to be able to bind both nucleosome-bound and -depleted DNA, with its suppression leading to increases in nucleosomal occupancy at sites normally bound by ETS1. ^[7]

Interaction with DNA repair promoters and proteins

DNA repair promoters

The messenger RNA and protein levels of DNA repair protein PARP1 are controlled, in part, by the expression level of the ETS1 transcription factor which interacts with multiple ETS1 binding sites in the promoter region of PARP1.^[12] The degree to which the ETS1 transcription factor can bind to its binding sites on the PARP1 promoter depends on the methylation status of the CpG islands in the ETS1 binding sites in the PARP1 promoter.^[13] If these CpG islands in ETS1 binding sites of the PARP1 promoter are epigenetically hypomethylated, PARP1 is expressed at an elevated level.^[13][14] The high constitutive levels of PARP1 in centenarians, providing more effective DNA repair, is thought to contribute to their unusual longevity. These levels of PARP1 expression are considered to be due to altered epigenetic control of transactivation of PARP1 expression.^[15]

As shown by Wilson et al.,^[16] increased ETS1 expression causes about 50 target genes to increase expression, including DNA repair genes MUTYH, BARD1, ERCC1 and XPA. Increased ETS1 expression causes resistance to cell killing by cisplatin, the resistance thought to be partly due to increased expression of DNA repair genes.

DNA repair protein interactions

ETS1 functions are regulated by protein – protein interactions.^[17][18] In particular, ETS1 protein interacts with several DNA repair proteins. ETS1 binds with DNA-dependent protein kinase (DNA-PK) [where the DNA-PK complex is made up of DNA-PKcs and DNA repair Ku (protein), and where Ku itself is a heterodimer of two polypeptides, Ku70 (XRCC6) and Ku80 (XRCC5)].^[18] ETS1 interaction with DNA-PK phosphorylates ETS1.^[18] Such phosphorylation of ETS1 alters its target gene repertoire.^[19] The Ku80 portion of DNA-PK, acting alone, interacts with ETS1 to down-regulate at least one of its transcriptional activities.^[18]

As shown by Legrand et al.,^[20] ETS1 protein interacts with PARP1 protein. ETS1 activates PARP1, causing poly ADP-ribosylation of PARP1 itself and of other proteins, even in the absence of nicked DNA. PARP1 (without self- poly ADP-ribosylation), in turn, is needed for activation of the transactivating activity of ETS1 on a tested promoter. Active PARP1 subsequently causes poly ADP-ribosylation of ETS1, and this appears to promote ETS1 ubiquitination and proteasomal degradation, preventing excessive activity of ETS1.

References

1. 
   ^ ^abc GRCh38: Ensembl release 89: ENSG00000134954 - Ensembl, May 2017
   


2. 
   ^ ^abc GRCm38: Ensembl release 89: ENSMUSG00000032035 - Ensembl, May 2017
   


3. 
   ^ "Human PubMed Reference:"..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output .citation q{quotes:"""""""'""'"}.mw-parser-output .citation .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-limited a,.mw-parser-output .citation .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Wikisource-logo.svg/12px-Wikisource-logo.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-maint{display:none;color:#33aa33;margin-left:0.3em}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
   


4. 
   ^ "Mouse PubMed Reference:".
   


5. 
   ^ Delattre O, Zucman J, Plougastel B, Desmaze C, Melot T, Peter M, Kovar H, Joubert I, de Jong P, Rouleau G (Sep 1992). "Gene fusion with an ETS DNA-binding domain caused by chromosome translocation in human tumours". Nature. 359 (6391): 162–5. doi:10.1038/359162a0. PMID 1522903.
   


6. 
   ^ Dwyer J, Li H, Xu D, Liu JP (Oct 2007). "Transcriptional regulation of telomerase activity: roles of the Ets transcription factor family". Annals of the New York Academy of Sciences. 1114 (1): 36–47. doi:10.1196/annals.1396.022. PMID 17986575.
   


7. 
   ^ ^abc Cauchy P, MA, Zacarias-Cabeza J, Vanhille L (2016-05-05). "Dynamic recruitment of Ets1 to both nucleosome-occupied and -depleted enhancer regions mediates a transcriptional program switch during early T-cell differentiation". Nucleic Acids Research. 44 (8): 3567–85. doi:10.1093/nar/gkv1475. ISSN 0305-1048. PMID 26673693.
   


8. 
   ^ Wasylyk B, Hagman J, Gutierrez-Hartmann A (1998). "Ets transcription factors: nuclear effectors of the Ras-MAP-kinase signaling pathway". Trends Biochem. Sci. 23 (6): 213–6. doi:10.1016/S0968-0004(98)01211-0. PMID 9644975.
   


9. 
   ^ Pei H, Yordy JS, Leng Q, Zhao Q, Watson DK, Li R (May 2003). "EAPII interacts with ETS1 and modulates its transcriptional function". Oncogene. 22 (18): 2699–709. doi:10.1038/sj.onc.1206374. PMID 12743594.
   


10. 
    ^ Hahn SL, Wasylyk B, Criqui-Filipe P, Criqui P (Sep 1997). "Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-conjugating enzyme". Oncogene. 15 (12): 1489–95. doi:10.1038/sj.onc.1201301. PMID 9333025.
    


11. 
    ^ Li R, Pei H, Watson DK, Papas TS (Feb 2000). "EAP1/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes". Oncogene. 19 (6): 745–53. doi:10.1038/sj.onc.1203385. PMID 10698492.
    


12. 
    ^ Soldatenkov VA, Albor A, Patel BK, Dreszer R, Dritschilo A, Notario V (1999). "Regulation of the human poly(ADP-ribose) polymerase promoter by the ETS transcription factor". Oncogene. 18 (27): 3954–62. doi:10.1038/sj.onc.1202778. PMID 10435618.
    


13. 
    ^ ^ab Bi FF, Li D, Yang Q (2013). "Hypomethylation of ETS transcription factor binding sites and upregulation of PARP1 expression in endometrial cancer". Biomed Res Int. 2013: 946268. doi:10.1155/2013/946268. PMC 3666359. PMID 23762867.
    


14. 
    ^ Li D, Bi FF, Cao JM, Cao C, Li CY, Liu B, Yang Q (2014). "Poly (ADP-ribose) polymerase 1 transcriptional regulation: a novel crosstalk between histone modification H3K9ac and ETS1 motif hypomethylation in BRCA1-mutated ovarian cancer". Oncotarget. 5 (1): 291–7. doi:10.18632/oncotarget.1549. PMC 3960209. PMID 24448423.
    


15. 
    ^ Chevanne M, Calia C, Zampieri M, Cecchinelli B, Caldini R, Monti D, Bucci L, Franceschi C, Caiafa P (2007). "Oxidative DNA damage repair and parp 1 and parp 2 expression in Epstein-Barr virus-immortalized B lymphocyte cells from young subjects, old subjects, and centenarians" (PDF). Rejuvenation Res. 10 (2): 191–204. doi:10.1089/rej.2006.0514. PMID 17518695.
    


16. 
    ^ Wilson LA, Yamamoto H, Singh G (2004). "Role of the transcription factor Ets-1 in cisplatin resistance". Mol. Cancer Ther. 3 (7): 823–32. PMID 15252143.
    


17. 
    ^ Li R, Pei H, Watson DK (2000). "Regulation of Ets function by protein - protein interactions". Oncogene. 19 (55): 6514–23. doi:10.1038/sj.onc.1204035. PMID 11175367.
    


18. 
    ^ ^abcd Choul-li S, Drobecq H, Aumercier M (2009). "DNA-dependent protein kinase is a novel interaction partner for Ets-1 isoforms". Biochem. Biophys. Res. Commun. 390 (3): 839–44. doi:10.1016/j.bbrc.2009.10.059. PMID 19836356.
    


19. 
    ^ Shiina M, Hamada K, Inoue-Bungo T, Shimamura M, Uchiyama A, Baba S, Sato K, Yamamoto M, Ogata K (2015). "A novel allosteric mechanism on protein-DNA interactions underlying the phosphorylation-dependent regulation of Ets1 target gene expressions". J. Mol. Biol. 427 (8): 1655–69. doi:10.1016/j.jmb.2014.07.020. PMID 25083921.
    


20. 
    ^ Legrand AJ, Choul-Li S, Spriet C, Idziorek T, Vicogne D, Drobecq H, Dantzer F, Villeret V, Aumercier M (2013). "The level of Ets-1 protein is regulated by poly(ADP-ribose) polymerase-1 (PARP-1) in cancer cells to prevent DNA damage". PLoS ONE. 8 (2): e55883. doi:10.1371/journal.pone.0055883. PMC 3566071. PMID 23405229.
    

Further reading

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• 
  Reddy ES, Rao VN (1988). "Structure, expression and alternative splicing of the human c-ets-1 proto-oncogene". Oncogene Research. 3 (3): 239–46. PMID 3060801.
  


• 
  Lincoln DW, Bove K (Jan 2005). "The transcription factor Ets-1 in breast cancer". Frontiers in Bioscience. 10 (1–3): 506–11. doi:10.2741/1546. PMID 15574387.
  

External links

• 
  ETS1+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)


• 
  Drosophila pointed - The Interactive Fly


• 
  FactorBook ETS1
  

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

v t e PDB gallery

1bqv: 1gvj: ETS-1 DNA BINDING AND AUTOINHIBITORY DOMAINS 1k78: Pax5(1-149)+Ets-1(331-440)+DNA 1k79: Ets-1(331-440)+GGAA duplex 1k7a: Ets-1(331-440)+GGAG duplex 1md0: CRYSTAL STRUCTURE OF AN INHIBITED FRAGMENT OF Ets-1 1mdm: INHIBITED FRAGMENT OF ETS-1 AND PAIRED DOMAIN OF PAX5 BOUND TO DNA 1r36: NMR-based structure of autoinhibited murine Ets-1 deltaN301 2stt: SOLUTION NMR STRUCTURE OF THE HUMAN ETS1/DNA COMPLEX, 25 STRUCTURES 2stw: SOLUTION NMR STRUCTURE OF THE HUMAN ETS1/DNA COMPLEX, RESTRAINED REGULARIZED MEAN STRUCTURE

v t e Transcription factors and intracellular receptors
(1) Basic domains (1.1) Basic leucine zipper (bZIP) Activating transcription factor AATF 1 2 3 4 5 6 7 AP-1 c-Fos FOSB FOSL1 FOSL2 JDP2 c-Jun JUNB JunD BACH 1 2 BATF BLZF1 C/EBP α β γ δ ε ζ CREB 1 3 L1 CREM DBP DDIT3 GABPA GCN4 HLF MAF B F G K NFE 2 L1 L2 L3 NFIL3 NRL NRF 1 2 3 XBP1 (1.2) Basic helix-loop-helix (bHLH) ATOH1 AhR AHRR ARNT ASCL1 BHLH 2 3 9 ARNTL ARNTL ARNTL2 CLOCK EPAS1 FIGLA HAND 1 2 HES 5 6 HEY 1 2 L HES1 HIF 1A 3A ID 1 2 3 4 LYL1 MESP2 MXD4 MYCL1 MYCN Myogenic regulatory factors MyoD Myogenin MYF5 MYF6 Neurogenins 1 2 3 NeuroD 1 2 NPAS 1 2 3 OLIG 1 2 Pho4 Scleraxis SIM 1 2 TAL 1 2 Twist USF1 (1.3) bHLH-ZIP AP-4 MAX MXD1 MXD3 MITF MNT MLX MLXIPL MXI1 Myc SREBP 1 2 (1.4) NF-1 NFI A B C X SMAD R-SMAD 1 2 3 5 9 I-SMAD 6 7 4) (1.5) RF-X RFX 1 2 3 4 5 6 ANK (1.6) Basic helix-span-helix (bHSH) AP-2 α β γ δ ε
(2) Zinc finger DNA-binding domains (2.1) Nuclear receptor (Cys4) .mw-parser-output .nobold{font-weight:normal} subfamily 1 Thyroid hormone α β CAR FXR LXR α β PPAR α β/δ γ PXR RAR α β γ ROR α β γ Rev-ErbA α β VDR subfamily 2 COUP-TF (I II Ear-2 HNF4 α γ PNR RXR α β γ Testicular receptor 2 4 TLX subfamily 3 Steroid hormone Androgen Estrogen α β Glucocorticoid Mineralocorticoid Progesterone Estrogen related α β γ subfamily 4 NUR NGFIB NOR1 NURR1 subfamily 5 LRH-1 SF1 subfamily 6 GCNF subfamily 0 DAX1 SHP (2.2) Other Cys4 GATA 1 2 3 4 5 6 MTA 1 2 3 TRPS1 (2.3) Cys2His2 General transcription factors TFIIA TFIIB TFIID TFIIE 1 2 TFIIF 1 2 TFIIH 1 2 4 2I 3A 3C1 3C2 ATBF1 BCL 6 11A 11B CTCF E4F1 EGR 1 2 3 4 ERV3 GFI1 GLI-Krüppel family 1 2 3 REST S1 S2 YY1 HIC 1 2 HIVEP 1 2 3 IKZF 1 2 3 ILF 2 3 KLF 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 17 MTF1 MYT1 OSR1 PRDM9 SALL 1 2 3 4 SP 1 2 4 7 8 TSHZ3 WT1 Zbtb7 7A 7B ZBTB 11 16 17 20 32 33 40 zinc finger 3 7 9 10 19 22 24 33B 34 35 41 43 44 51 74 143 146 148 165 202 217 219 238 239 259 267 268 281 295 300 318 330 346 350 365 366 384 423 451 452 471 593 638 644 649 655 (2.4) Cys6 HIVEP1 (2.5) Alternating composition AIRE DIDO1 GRLF1 ING 1 2 4 JARID 1A 1B 1C 1D 2 JMJD1B (2.6) WRKY WRKY
(3) Helix-turn-helix domains (3.1) Homeodomain ARX CDX 1 2 CRX CUTL1 DBX 1 2 DLX 1 2 3 4 5 6 EMX 1 2 EN 1 2 FHL 1 2 3 HESX1 HHEX HLX Homeobox A1 A2 A3 A4 A5 A7 A9 A10 A11 A13 B1 B2 B3 B4 B5 B6 B7 B8 B9 B13 C4 C5 C6 C8 C9 C10 C11 C12 C13 D1 D3 D4 D8 D9 D10 D11 D12 D13 HOPX IRX 1 2 3 4 5 6 MKX LMX 1A 1B MEIS 1 2 MEOX2 MNX1 MSX 1 2 NANOG NKX 2-1 2-2 2-3 2-5 3-1 3-2 6-1 6-2 NOBOX PBX 1 2 3 PHF 1 3 6 8 10 16 17 20 21A PHOX 2A 2B PITX 1 2 3 POU domain PIT-1 BRN-3: A B C Octamer transcription factor: 1 2 3/4 6 7 11 OTX 1 2 PDX1 SATB2 SHOX2 SIX 1 2 3 4 5 VAX1 ZEB 1 2 (3.2) Paired box PAX 1 2 3 4 5 6 7 8 9 PRRX 1 2 RAX (3.3) Fork head / winged helix E2F 1 2 3 4 5 FOX proteins A1 A2 A3 C1 C2 D3 D4 E1 E3 F1 G1 H1 I1 J1 J2 K1 K2 L2 M1 N1 N3 O1 O3 O4 P1 P2 P3 P4 (3.4) Heat shock factors HSF 1 2 4 (3.5) Tryptophan clusters ELF 2 4 5 EGF ELK 1 3 4 ERF ETS 1 2 ERG SPIB ETV 1 4 5 6 FLI1 Interferon regulatory factors 1 2 3 4 5 6 7 8 MYB MYBL2 (3.6) TEA domain transcriptional enhancer factor 1 2 3 4
(4) β-Scaffold factors with minor groove contacts (4.1) Rel homology region NF-κB NFKB1 NFKB2 REL RELA RELB NFAT C1 C2 C3 C4 5 (4.2) STAT STAT 1 2 3 4 5 6 (4.3) p53 p53 TBX 1 2 3 5 19 21 22 TBR1 TBR2 TFT MYRF TP63 (4.4) MADS box Mef2 A B C D SRF (4.6) TATA-binding proteins TBP TBPL1 (4.7) High-mobility group BBX HMGB 1 2 3 4 HMGN 1 2 3 4 HNF 1A 1B LEF1 SOX 1 2 3 4 5 6 8 9 10 11 12 13 14 15 18 21 SRY SSRP1 TCF 3 4 TOX 1 2 3 4 (4.9) Grainyhead TFCP2 (4.10) Cold-shock domain CSDA YBX1 (4.11) Runt CBF CBFA2T2 CBFA2T3 RUNX1 RUNX2 RUNX3 RUNX1T1
(0) Other transcription factors (0.2) HMGI(Y) HMGA 1 2 HBP1 (0.3) Pocket domain Rb RBL1 RBL2 (0.5) AP-2/EREBP-related factors Apetala 2 EREBP B3 (0.6) Miscellaneous ARID 1A 1B 2 3A 3B 4A CAP IFI 16 35 MLL 2 3 T1 MNDA NFY A B C Rho/Sigma
see also transcription factor/coregulator deficiencies

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