Generic transcription pathway (Homo sapiens)

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3, 4, 7, 8, 10...2, 16, 28, 30, 32...2, 7, 9, 13, 16...2, 16, 28, 30, 326, 12, 14, 22, 252, 4, 10, 16, 28...nucleoplasmZFP90 MED7 ZNF320 MED23 NR4A1 ZNF268 ZNF662 ZNF205 NR1H4-2 ZKSCAN5 MED10 RORA ZNF625 ZNF550 ZNF570 ZNF726 NRBP1 RARG ZNF382 ZNF699 ZNF700 ZNF696 ZNF417 ZNF383 ZNF761 RORB NR2C2AP NR1H4-1 ZNF343 ZNF200 MED6NRBF2-1 ZNF212 ZNF324 ZNF710 ZNF175 ZNF41 ZNF510 ZNF273 ZNF660 THRB ZNF34 ZNF776 MED23 ZNF624 NR1H3-1 ZNF454 ZNF767 NR1I2-1 ZNF606 NR2F6 PRDM7 ZNF416 ZNF547 ZNF658 MED4 NR3C1-7 ZNF43 ZNF565 PRDM7 ZNF248 NR1I2-6 ZNF839 ZNF679 ZNF615 KAT2A MED4 ZNF716 ZNF37A ZNF215 ZNF705G ZNF233 MED26ZNF33A ZNF354A KRBA1 ZNF350 ZNF599 ZNF599 ZNF420 MED4 CREBBP ZNF354C ZNF382 PPARD ZNF735 ZNF331 NR0B1-1 ZNF804B ZNF726P1 ZNF417 ZNF224 ESRRG ZNF135 ZNF549 ZNF641 NR3C1-4 ZNF234 NR3C1-2 ZNF791 ZNF425 KRBOX4 ZKSCAN7 ZNF559 ZNF556 ZNF792 ZNF669 NR3C1-3 NR1I2-5 ZNF544 ZNF75D ZNF770 ZNF333 ZNF75A ZNF587 ZNF548 ZNF697 ZNF205 MAMLD1 ZNF736 ESR2 MED12 NR3C2-1 RXRA ZNF696 ZFP69B MED4ZNF300 ZNF585A MED31ZNF445 CCNC TRIM28 NR5A1 ZNF160 CSL NICD coactivatorcomplexNR3C1-6 ZNF286A NR3C1-2 NR1H3-1 ZNF570 ZNF26 NR1H4-1 ZNF250 ZNF440 NR-MED1 CoactivatorComplexZNF782 RXRG ZNF737 ZNF563 ZKSCAN7 ZNF17 ZNF350 ZNF253 NR3C1-1 NR5A2-1 ZNF761 ZNF101 ZNF254 NR1D2 ZIM2 MAML3 ZNF506 ZNF225 ZNF621 NR3C1-4 ZNF586 ZNF708 ZNF20 ZNF571 ZNF420 NR0B1-1 ZNF266 ZNF565 ZNF736 KRAB-ZNF / KAPComplexZNF429 NR0B1-2 NRBP1 NICD1 ZNF600 ZNF114 ZNF133 ZNF563 YAP1- and WWTR1(TAZ)-stimulatedgene expressionZNF442 RORC ZNF253 ZNF496 NR3C2-3 ZKSCAN5 ZNF226 CCNCZNF737 ZNF343 ZNF92 MED17 ZNF443 ZNF589 ZNF285 ZNF17 ZNF124 ZSCAN32 ZNF257(1-535) ZNF732 ZNF544 ZNF724P ZNF559 ZNF490 ZNF750 ZNF790 NR6A1-3 ZNF324B PPARA ZNF595 ZNF664 PCAFZNF671 ZNF184 MED23 ZNF704 ZNF613 ZNF658B ZNF772 MED7 ZNF839 ZNF679 ZNF202 ZNF705E HNF4A ZNF735 ZNF43 NR6A1-1 ZNF138 ZNF485 ZIM2 ZNF14 ZNF33A TRIM28 ZNF431 ZNF611 ZNF506 NR3C2-2 ZNF793 ZNF665 ZNF568 ZNF75D MED1MED26 NR3C1-8 ZNF621 ZNF441 ZNF767 ZNF33B ZNF557 NR3C1-5 ZNF804B ZNF461 NR1I2-5 PPARG MED16 ZNF169 MED20ZNF747 ZNF615 ZNF799 ZNF112 ZNF550 ZNF613 ZNF133 RARA MED27ZNF446 ZNF468 NR3C2-4 ZNF729 ZNF720 ZNF480 ZNF230 ZNF430 ZNF585A ZNF558 MED30NR1I3-2 ZKSCAN8 ZNF717 ZNF649 ZNF302 RBPJZNF560 ZNF470 ZNF699 ZNF577 ZNF786 CDK8 ZNF221 ZNF620 ZNF184 NR1H3-2 ZNF75CP ZNF551 ZNF45 MED30 MAML3 NR5A2-2 ZNF611 ZNF446 MED20 PPARA ZNF773 ZNF79 ZNF705D ZNF26 ZNF14 RORA NR0B1-2 NR4A3-1 ZNF92 ZIM3 ZNF41 ZNF675 MED12CCNC ZNF709 ZNF529 ZSCAN25 ZNF684 ZNF441 ZNF567 ZNF169 ZNF665 ZNF473 ZNF749 ZNF543 NR2C1 NR6A1-4 ZNF433 CBPZNF587 NR6A1-3 ZNF678 ZNF514 ZNF684 NR4A3-2 ZNF74 ZNF471 MED24 ZNF383 ZNF331 ZNF627 NR1I2-4 ZNF709 ZNF337 ZNF689 NR2E1 ZNF619 ZNF711 ZNF721 ZNF136 Transcriptionalactivity ofSMAD2/SMAD3:SMAD4heterotrimerZNF222 ZNF557 NR2E3-2 NR3C1-7 ZNF540 ZNF589 ZNF484 ZNF302 NR1H4-2 NR0B2 NR1I3-1 ZNF394 ZNF616 MAMLD1 MED1 ZNF610 ZNF337 KAT2B ZNF774 ZNF519 ZNF114 ZNF140 ZNF692 ZNF211 ZFP28 NR5A2-3 NICD2 RXRB ZNF429 PGR-2 ZNF354B RARB ZNF793 ZNF10 ZNF223 ZNF45 NR1H4-3 ZNF655 ZNF860 MED13 ZNF702P MED1 ZNF418 ZNF300 NR1I2-2 NR1H4-3 ZNF263 NR1D1 ZFP37 RARA ZNF221 ZNF547 ZFP30 ZNF746 ESRRA ZNF248 ZNF626 ZNF77 ZNF141 ZNF770 NR6A1-1 ZNF415 ZNF583 ZNF486 NRBF2-2 NR6A1-2 ZNF347 ZNF528 ZNF573 ZNF222 ZNF583 ARC coactivatorcomplexZNF749 ZNF681 NR6A1-5 ZNF528 PGR ZNF705F ZNF678 ZNF778 ZNF577 ZNF180 ZNF705E ZNF562 ZNF697 NR1I2-2 ZNF702P ZNF19 ZNF680 ZNF230 ZNF658B ZFP69 ZNF30 ZNF79 NR2F6 MAML2 ZNF485 ZNF212 NRBF2-1 ZNF195 ZNF2 ZNF724P ZNF267 ZNF304 MED15 ZIM3 ESRRB ZNF710 ZNF225 ZNF354A NR5A2-1 ZNF747 NR5A2-2 ZNF540 ZNF746 RORC ZNF548 ZNF569 NR1I2-3 ZNF840 ZNF676 MED27 ZNF70 NR2C2AP NICD4 NR4A2 ZNF517 ZNF74 NICD2 ZNF514 ZNF460 ZNF704 ZNF213 NR3C2-2 ZNF667 ZNF549 ZNF311 THRB NR4A2 ZNF490 ZNF718 ZNF250 ZNF726P1 ZNF223 ZNF492 CDK8 ZNF398 ZNF442 ZNF688 ZNF30 ZNF214 ZNF267 ZNF430 ZNF597 ZNF792 ZNF555 ZNF200 ZNF616 ZNF764 MED13ZNF776 KRAB-ZNFZNF713 ZNF154 ZNF774 ZNF655 ZNF614 ZNF493 ZNF738 ZNF707 ZNF607 ZNF484 ZNF791 ZNF691 ZNF235 ZNF394 ZNF175 ZNF546 RARG ZNF500 NR4A3-2 ZNF101 ZNF470 MED31 ZNF471 ZNF596 ZNF496 ZNF264 ZNF483 ZNF676 ZNF529 MED8 ZNF432 ZNF37A ZNF479 ZNF740 ZNF691 ESR1 PPARD ZNF517 ZNF680 ZNF333 ZNF567 SNWMED14 ZNF227 MED15ZNF714 ZNF155 ZNF257(1-535) ZNF483 NR1H4-4 ZNF439 RARB ZNF707 ZNF71 ZNF682 ZFP1 ZNF624 ZNF778 ZNF286A ZNF180 NR1H2 ZNF705D HNF4G DRIP coactivatorcomplexZNF614 ZNF775 MED25 ZNF772 ZNF573 ZNF415 ZNF585B SNW1 NR1H3-2 ZNF727 MED24 SNW1 ZNF141 ZKSCAN4 ZNF433 ZNF692 ZFP30 ZNF493 MED8ZNF610 NICD4 ZNF782 ZNF571 ZNF140 ZNF582 ZNF566 ZNF717 ZNF479 ZNF436 ZNF189 NR4A3-1 ZNF99 ZKSCAN8 ZNF439 ZNF18 NRCREBBP ZNF256 ZNF700 ZFP2 ZNF677 NR4A1 ZNF416 RXRB ZNF595 ZNF675 ZNF519 ZNF510 NR5A2-3 ZNF274 ZKSCAN1 AR ZNF197 ZNF334 ZNF492 ZNF226 ZNF208 ZNF670 ZNF254 NR2C2 ZNF398 ZNF461 ZFP90 ZNF436 ZNF840 ZNF100 ZNF671 RXRA ZNF668 ZNF20 ZNF263 ZNF268 ZNF285 MED14 ZNF860 ZNF664 ZNF649 ZNF124 ZNF235 PGR-2 NR1I2-6 ZNF716 ZNF112 NR2C1 NICD3 ZSCAN25 MED16 MED24ZNF764 ZNF432 ZNF468 ZNF626 MED10 ZNF597 ZNF600 ZNF34 ZNF19 ZNF564 ZNF100 ZNF682 NR1H2 ZNF274 MED16MED13 ZNF551 ZNF786 VDR ZNF3 NR6A1-5 ZNF71 ZNF480 ZNF454 ZNF500 ZNF619 ZNF605 NRBF2-2 RORB VDR ZNF701 ZKSCAN3 KRBOX4 ZNF569 THRA ZNF426 ESRRA ZNF705A ZNF705G ZNF750 NR6A1-2 MED6 NICD1 ZNF554 ZNF324B ZNF28 ZNF668 ZNF224 MED16 CDK8 ZNF605 ZNF689 ZNF620 ZNF726 ZNF287 NR1H4-4 ZNF627 ZNF460 ZNF197 ZNF304 ZNF688 KAT2A ZNF562 NR1I2-3 ZNF543 ZNF701 ESR1 ZNF99 NR2E3-1 ZSCAN32 ZNF215 ZNF530 ZNF155 ZNF12(1-501) ZNF561 ZNF28 ZKSCAN1 PPARG ZNF625 ZNF713 MAMLNR1I2-1 ZNF703 ZNF740 MED10 MED12 MED6 ZNF25 ZNF790 ZNF606 NR2C2 NR2F1 ZNF711 ZNF681 ZNF552 NR1D2 MAML2 ZNF443 ZIK1 MED17ZNF568 ZNF662 MED14ZFP69B ZNF266 ZNF195 ZNF287 RXRG ZNF324 NR5A1 ZNF555 ZNF317 ZNF708 ZKSCAN4 ZNF558 MED13 CCNC ZNF554 KAP (KRAB-DomainAssociated Protein)ZNF227 ZNF154 ZNF658 NICDMED6 ZNF730 ZNF23 CDK8NR3C1-8 ZFP14 ZNF282 NICD3 ZNF785 HKR1 HKR1 ZKSCAN3 ZNF552 AR ZNF566 ZNF596 MED25ZNF320 ZNF785 ZNF732 ZNF334 ZNF418 ZNF431 RBPJ ZNF311 ZFP14 ZNF419 NR3C1-1 ZNF473 MED10ZFP2 ZNF660 ZNF706 ZFP69 TranscriptionalRegulation by TP53ZNF561 NR3C1-9 ZNF721 ZNF138 ZNF669 NR3C1-5 ZNF135 ZNF18 NR2F1 ZNF670 ZNF799 ESRRG MED1 ZNF157 MED12 ZNF440 ZNF23 MED17 ZNF560 ZNF718 MAML1 ZNF234 ZNF584 ZNF720 ZNF530 ZFP37 KAT2B ZNF256 ZNF282 MED24 ZNF777 ZNF425 ZNF486 HNF4A ZNF546 ZNF354B NR2E1 NR3C2-3 ZNF641 ZNF25 ZNF771 MAML1 ZNF556 ZNF705A ZNF584 ZNF3 ZNF77 ZFP1 ZNF233 ZNF2 ZNF273 ZNF738 NR1I2-4 NR2E3-2 ZNF213 ZNF10 THRA ZNF75A MED14 NR0B2 NR1I2-7 ZNF730 ZNF157 ZNF208 NR3C2-4 MED17 ZNF677 ZNF214 ZNF607 MED23ZNF773 ZNF586 ZNF777 ZNF160 ESR2 NR1I2-7 NR1D1 ZNF211 ZNF419 ZNF317 ZFP28 KRBA1 ZNF706 NR3C2-1 ZNF70 NR6A1-4 ZNF12(1-501) ZNF33B ZNF264 NR1I3-2 ZNF445 NR2E3-1 NR3C1-9 PGR ZNF705F MED7 ZNF426 NR1I3-1 ZNF582 ZNF667 MED7ZNF714 ZNF136 TRAP coactivatorcomplexZNF202 ZNF564 NR3C1-6 ZNF189 ZNF75CP ZNF775 NR3C1-3 MED1 ZNF354C ZIK1 HNF4G ZNF347 ZNF585B ZNF771 ZNF727 ESRRB ZNF729 ZNF703 19, 21, 24, 26, 27, 345, 291


Description

OVERVIEW OF TRANSCRIPTION REGULATION:

Detailed studies of gene transcription regulation in a wide variety of eukaryotic systems has revealed the general principles and mechanisms by which cell- or tissue-specific regulation of differential gene transcription is mediated (reviewed in Naar, 2001. Kadonaga, 2004, Maston, 2006, Barolo, 2002; Roeder, 2005, Rosenfeld, 2006). Of the three major classes of DNA polymerase involved in eukaryotic gene transcription, Polymerase II generally regulates protein-encoding genes. Figure 1 shows a diagram of the various components involved in cell-specific regulation of Pol-II gene transcription.

Core Promoter: Pol II-regulated genes typically have a Core Promoter where Pol II and a variety of general factors bind to specific DNA motifs:
i: the TATA box (TATA DNA sequence), which is bound by the "TATA-binding protein" (TBP).
ii: the Initiator motif (INR), where Pol II and certain other core factors bind, is present in many Pol II-regulated genes.
iii: the Downstream Promoter Element (DPE), which is present in a subset of Pol II genes, and where additional core factors bind.
The core promoter binding factors are generally ubiquitously expressed, although there are exceptions to this.

Proximal Promoter: immediately upstream (5') of the core promoter, Pol II target genes often have a Proximal Promoter region that spans up to 500 base pairs (b.p.), or even to 1000 b.p.. This region contains a number of functional DNA binding sites for a specific set of transcription activator (TA) and transcription repressor (TR) proteins. These TA and TR factors are generally cell- or tissue-specific in expression, rather than ubiquitous, so that the presence of their cognate binding sites in the proximal promoter region programs cell- or tissue-specific expression of the target gene, perhaps in conjunction with TA and TR complexes bound in distal enhancer regions.

Distal Enhancer(s): many or most Pol II regulated genes in higher eukaryotes have one or more distal Enhancer regions which are essential for proper regulation of the gene, often in a cell or tissue-specific pattern. Like the proximal promoter region, each of the distal enhancer regions typically contain a cluster of binding sites for specific TA and/or TR DNA-binding factors, rather than just a single site.

Enhancers generally have three defining characteristics:
i: They can be located very long distances from the promoter of the target gene they regulate, sometimes as far as 100 Kb, or more.
ii: They can be either upstream (5') or downstream (3') of the target gene, including within introns of that gene.
iii: They can function in either orientation in the DNA.

Combinatorial mechanisms of transcription regulation: The specific combination of TA and TR binding sites within the proximal promoter and/or distal enhancer(s) provides a "combinatorial transcription code" that mediates cell- or tissue-specific expression of the associated target gene. Each promoter or enhancer region mediates expression in a specific subset of the overall expression pattern. In at least some cases, each enhancer region functions completely independently of the others, so that the overall expression pattern is a linear combination of the expression patterns of each of the enhancer modules.

Co-Activator and Co-Repressor Complexes: DNA-bound TA and TR proteins typically recruit the assembly of specific Co-Activator (Co-A) and Co-Repressor (Co-R) Complexes, respectively, which are essential for regulating target gene transcription. Both Co-A's and Co-R's are multi-protein complexes that contain several specific protein components.

Co-Activator complexes generally contain at lease one component protein that has Histone Acetyl Transferase (HAT) enzymatic activity. This functions to acetylate Histones and/or other chromatin-associated factors, which typically increases that transcription activation of the target gene. By contrast, Co-Repressor complexes generally contain at lease one component protein that has Histone De-Acetylase (HDAC) enzymatic activity. This functions to de-acetylate Histones and/or other chromatin-associated factors. This typically increases the transcription repression of the target gene.

Adaptor (Mediator) complexes: In addition to the co-activator complexes that assemble on particular cell-specific TA factors, - there are at least two additional transcriptional co-activator complexes common to most cells. One of these is the Mediator complex, which functions as an "adaptor" complex that bridges between the tissue-specific co-activator complexes assembled in the proximal promoter (or distal enhancers). The human Mediator complex has been shown to contain at least 19 protein distinct components. Different combinations of these co-activator proteins are also found to be components of specific transcription Co-Activator complexes, such as the DRIP, TRAP and ARC complexes described below.

TBP/TAF complex: Another large Co-A complex is the "TBP-associated factors" (TAFs) that assemble on TBP (TATA-Binding Protein), which is bound to the TATA box present in many promoters. There are at least 23 human TAF proteins that have been identified. Many of these are ubiquitously expressed, but TAFs can also be expressed in a cell or tissue-specific pattern.


Specific Coactivator Complexes for DNA-binding Transcription Factors.

A number of specific co-activator complexes for DNA-binding transcription factors have been identified, including DRIP, TRAP, and ARC (reviewed in Bourbon, 2004, Blazek, 2005, Conaway, 2005, and Malik, 2005). The DRIP co-activator complex was originally identified and named as a specific complex associated with the Vitamin D Receptor member of the nuclear receptor family of transcription factors (Rachez, 1998). Similarly, the TRAP co-activator complex was originally identified as a complex that associates with the thyroid receptor (Yuan, 1998). It was later determined that all of the components of the DRIP complex are also present in the TRAP complex, and the ARC complex (discussed further below). For example, the DRIP205 and TRAP220 proteins were show to be identical, as were specific pairs of the other components of these complexes (Rachez, 1999).

In addition, these various transcription co-activator proteins identified in mammalian cells were found to be the orthologues or homologues of the Mediator ("adaptor") complex proteins (reviewed in Bourbon, 2004). The Mediator proteins were originally identified in yeast by Kornberg and colleagues, as complexes associated with DNA polymerase (Kelleher, 1990). In higher organisms, Adapter complexes bridge between the basal transcription factors (including Pol II) and tissue-specific transcription factors (TFs) bound to sites within upstream Proximal Promoter regions or distal Enhancer regions (Figure 1). However, many of the Mediator homologues can also be found in complexes associated with specific transcription factors in higher organisms. A unified nomenclature system for these adapter / co-activator proteins now labels them Mediator 1 through Mediator 31 (Bourbon, 2004). For example, the DRIP205 / TRAP220 proteins are now identified as Mediator 1 (Rachez, 1999), based on homology with yeast Mediator 1.


Example Pathway: Specific Regulation of Target Genes During Notch Signaling:

One well-studied example of cell-specific regulation of gene transcription is selective regulation of target genes during Notch signaling. Notch signaling was first identified in Drosophila, where it has been studied in detail at the genetic, molecular, biochemical and cellular levels (reviewed in Justice, 2002; Bray, 2006; Schweisguth, 2004; Louvri, 2006). In Drosophila, Notch signaling to the nucleus is thought always to be mediated by one specific DNA binding transcription factor, Suppressor of Hairless. In mammals, the homologous genes are called CBF1 (or RBPJkappa), while in worms they are called Lag-1, so that the acronym "CSL" has been given to this conserved transcription factor family. There are at least two human CSL homologues, which are now named RBPJ and RBPJL.

In Drosophila, Su(H) is known to be bifunctional, in that it represses target gene transcription in the absence of Notch signaling, but activates target genes during Notch signaling. At least some of the mammalian CSL homologues are believed also to be bifunctional, and to mediate target gene repression in the absence of Notch signaling, and activation in the presence of Notch signaling.

Notch Co-Activator and Co-Repressor complexes: This repression is mediated by at least one specific co-repressor complexes (Co-R) bound to CSL in the absence of Notch signaling. In Drosophila, this co-repressor complex consists of at least three distinct co-repressor proteins: Hairless, Groucho, and dCtBP (Drosophila C-terminal Binding Protein). Hairless has been show to bind directly to Su(H), and Groucho and dCtBP have been shown to bind directly to Hairless (Barolo, 2002). All three of the co-repressor proteins have been shown to be necessary for proper gene regulation during Notch signaling in vivo (Nagel, 2005).

In mammals, the same general pathway and mechanisms are observed, where CSL proteins are bifunctional DNA binding transcription factors (TFs), that bind to Co-Repressor complexes to mediate repression in the absence of Notch signaling, and bind to Co-Activator complexes to mediate activation in the presence of Notch signaling. However, in mammals, there may be multiple co-repressor complexes, rather than the single Hairless co-repressor complex that has been observed in Drosophila.

During Notch signaling in all systems, the Notch transmembrane receptor is cleaved and the Notch intracellular domain (NICD) translocates to the nucleus, where it there functions as a specific transcription co-activator for CSL proteins. In the nucleus, NICD replaces the Co-R complex bound to CSL, thus resulting in de-repression of Notch target genes in the nucleus (Figure 2). Once bound to CSL, NICD and CSL proteins recruit an additional co-activator protein, Mastermind, to form a CSL-NICD-Mam ternary co-activator (Co-A) complex. This Co-R complex was initially thought to be sufficient to mediate activation of at least some Notch target genes. However, there now is evidence that still other co-activators and additional DNA-binding transcription factors are required in at least some contexts (reviewed in Barolo, 2002).

Thus, CSL is a good example of a bifunctional DNA-binding transcription factor that mediates repression of specific targets genes in one context, but activation of the same targets in another context. This bifunctionality is mediated by the association of specific Co-Repressor complexes vs. specific Co-Activator complexes in different contexts, namely in the absence or presence of Notch signaling.

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Bibliography

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  1. Franklin TB, Russig H, Weiss IC, Gräff J, Linder N, Michalon A, Vizi S, Mansuy IM.; ''Epigenetic transmission of the impact of early stress across generations.''; PubMed Europe PMC Scholia
  2. KhorshidAhmad T, Acosta C, Cortes C, Lakowski TM, Gangadaran S, Namaka M.; ''Transcriptional Regulation of Brain-Derived Neurotrophic Factor (BDNF) by Methyl CpG Binding Protein 2 (MeCP2): a Novel Mechanism for Re-Myelination and/or Myelin Repair Involved in the Treatment of Multiple Sclerosis (MS).''; PubMed Europe PMC Scholia
  3. Williamson SL, Ellaway CJ, Peters GB, Pelka GJ, Tam PP, Christodoulou J.; ''Deletion of protein tyrosine phosphatase, non-receptor type 4 (PTPN4) in twins with a Rett syndrome-like phenotype.''; PubMed Europe PMC Scholia
  4. Rachez C, Lemon BD, Suldan Z, Bromleigh V, Gamble M, Näär AM, Erdjument-Bromage H, Tempst P, Freedman LP.; ''Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex.''; PubMed Europe PMC Scholia
  5. Ito Y, Bae SC, Chuang LS.; ''The RUNX family: developmental regulators in cancer.''; PubMed Europe PMC Scholia
  6. Impens F, Radoshevich L, Cossart P, Ribet D.; ''Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.''; PubMed Europe PMC Scholia
  7. Underwood KF, D'Souza DR, Mochin-Peters M, Pierce AD, Kommineni S, Choe M, Bennett J, Gnatt A, Habtemariam B, MacKerell AD, Passaniti A.; ''Regulation of RUNX2 transcription factor-DNA interactions and cell proliferation by vitamin D3 (cholecalciferol) prohormone activity.''; PubMed Europe PMC Scholia
  8. Chimge NO, Frenkel B.; ''The RUNX family in breast cancer: relationships with estrogen signaling.''; PubMed Europe PMC Scholia
  9. McGill BE, Bundle SF, Yaylaoglu MB, Carson JP, Thaller C, Zoghbi HY.; ''Enhanced anxiety and stress-induced corticosterone release are associated with increased Crh expression in a mouse model of Rett syndrome.''; PubMed Europe PMC Scholia
  10. Gao H, Le Y, Wu X, Silberstein LE, Giese RW, Zhu Z.; ''VentX, a novel lymphoid-enhancing factor/T-cell factor-associated transcription repressor, is a putative tumor suppressor.''; PubMed Europe PMC Scholia
  11. Otto F, Kanegane H, Mundlos S.; ''Mutations in the RUNX2 gene in patients with cleidocranial dysplasia.''; PubMed Europe PMC Scholia
  12. Roeder RG.; ''Transcriptional regulation and the role of diverse coactivators in animal cells.''; PubMed Europe PMC Scholia
  13. Samaco RC, Mandel-Brehm C, McGraw CM, Shaw CA, McGill BE, Zoghbi HY.; ''Crh and Oprm1 mediate anxiety-related behavior and social approach in a mouse model of MECP2 duplication syndrome.''; PubMed Europe PMC Scholia
  14. Tao J, Hu K, Chang Q, Wu H, Sherman NE, Martinowich K, Klose RJ, Schanen C, Jaenisch R, Wang W, Sun YE.; ''Phosphorylation of MeCP2 at Serine 80 regulates its chromatin association and neurological function.''; PubMed Europe PMC Scholia
  15. Ducy P, Zhang R, Geoffroy V, Ridall AL, Karsenty G.; ''Osf2/Cbfa1: a transcriptional activator of osteoblast differentiation.''; PubMed Europe PMC Scholia
  16. Bourbon HM, Aguilera A, Ansari AZ, Asturias FJ, Berk AJ, Bjorklund S, Blackwell TK, Borggrefe T, Carey M, Carlson M, Conaway JW, Conaway RC, Emmons SW, Fondell JD, Freedman LP, Fukasawa T, Gustafsson CM, Han M, He X, Herman PK, Hinnebusch AG, Holmberg S, Holstege FC, Jaehning JA, Kim YJ, Kuras L, Leutz A, Lis JT, Meisterernest M, Naar AM, Nasmyth K, Parvin JD, Ptashne M, Reinberg D, Ronne H, Sadowski I, Sakurai H, Sipiczki M, Sternberg PW, Stillman DJ, Strich R, Struhl K, Svejstrup JQ, Tuck S, Winston F, Roeder RG, Kornberg RD.; ''A unified nomenclature for protein subunits of mediator complexes linking transcriptional regulators to RNA polymerase II.''; PubMed Europe PMC Scholia
  17. Onichtchouk D, Gawantka V, Dosch R, Delius H, Hirschfeld K, Blumenstock C, Niehrs C.; ''The Xvent-2 homeobox gene is part of the BMP-4 signalling pathway controlling [correction of controling] dorsoventral patterning of Xenopus mesoderm.''; PubMed Europe PMC Scholia
  18. Kammerer M, Gutzwiller S, Stauffer D, Delhon I, Seltenmeyer Y, Fournier B.; ''Estrogen Receptor α (ERα) and Estrogen Related Receptor α (ERRα) are both transcriptional regulators of the Runx2-I isoform.''; PubMed Europe PMC Scholia
  19. Ding X, Luo C, Zhou J, Zhong Y, Hu X, Zhou F, Ren K, Gan L, He A, Zhu J, Gao X, Zhang J.; ''The interaction of KCTD1 with transcription factor AP-2alpha inhibits its transactivation.''; PubMed Europe PMC Scholia
  20. Hwang CK, Kim CS, Kim DK, Law PY, Wei LN, Loh HH.; ''Up-regulation of the mu-opioid receptor gene is mediated through chromatin remodeling and transcriptional factors in differentiated neuronal cells.''; PubMed Europe PMC Scholia
  21. Trimarchi JM, Fairchild B, Verona R, Moberg K, Andon N, Lees JA.; ''E2F-6, a member of the E2F family that can behave as a transcriptional repressor.''; PubMed Europe PMC Scholia
  22. Hu K, Nan X, Bird A, Wang W.; ''Testing for association between MeCP2 and the brahma-associated SWI/SNF chromatin-remodeling complex.''; PubMed Europe PMC Scholia
  23. Ogawa H, Ishiguro K, Gaubatz S, Livingston DM, Nakatani Y.; ''A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells.''; PubMed Europe PMC Scholia
  24. Nishina S, Shiraha H, Nakanishi Y, Tanaka S, Matsubara M, Takaoka N, Uemura M, Horiguchi S, Kataoka J, Iwamuro M, Yagi T, Yamamoto K.; ''Restored expression of the tumor suppressor gene RUNX3 reduces cancer stem cells in hepatocellular carcinoma by suppressing Jagged1-Notch signaling.''; PubMed Europe PMC Scholia
  25. Lam K, Zhang DE.; ''RUNX1 and RUNX1-ETO: roles in hematopoiesis and leukemogenesis.''; PubMed Europe PMC Scholia
  26. Lau QC, Raja E, Salto-Tellez M, Liu Q, Ito K, Inoue M, Putti TC, Loh M, Ko TK, Huang C, Bhalla KN, Zhu T, Ito Y, Sukumar S.; ''RUNX3 is frequently inactivated by dual mechanisms of protein mislocalization and promoter hypermethylation in breast cancer.''; PubMed Europe PMC Scholia
  27. Bogachek MV, Chen Y, Kulak MV, Woodfield GW, Cyr AR, Park JM, Spanheimer PM, Li Y, Li T, Weigel RJ.; ''Sumoylation pathway is required to maintain the basal breast cancer subtype.''; PubMed Europe PMC Scholia
  28. Ogihara Y, Masuda T, Ozaki S, Yoshikawa M, Shiga T.; ''Runx3-regulated expression of two Ntrk3 transcript variants in dorsal root ganglion neurons.''; PubMed Europe PMC Scholia
  29. Zhao X, Chen A, Yan X, Zhang Y, He F, Hayashi Y, Dong Y, Rao Y, Li B, Conway RM, Maiques-Diaz A, Elf SE, Huang N, Zuber J, Xiao Z, Tse W, Tenen DG, Wang Q, Chen W, Mulloy JC, Nimer SD, Huang G.; ''Downregulation of RUNX1/CBFβ by MLL fusion proteins enhances hematopoietic stem cell self-renewal.''; PubMed Europe PMC Scholia
  30. Robledo RF, Rajan L, Li X, Lufkin T.; ''The Dlx5 and Dlx6 homeobox genes are essential for craniofacial, axial, and appendicular skeletal development.''; PubMed Europe PMC Scholia
  31. Zhong YF, Holland PW.; ''The dynamics of vertebrate homeobox gene evolution: gain and loss of genes in mouse and human lineages.''; PubMed Europe PMC Scholia
  32. Weisenberger DJ, Siegmund KD, Campan M, Young J, Long TI, Faasse MA, Kang GH, Widschwendter M, Weener D, Buchanan D, Koh H, Simms L, Barker M, Leggett B, Levine J, Kim M, French AJ, Thibodeau SN, Jass J, Haile R, Laird PW.; ''CpG island methylator phenotype underlies sporadic microsatellite instability and is tightly associated with BRAF mutation in colorectal cancer.''; PubMed Europe PMC Scholia
  33. Oberley MJ, Inman DR, Farnham PJ.; ''E2F6 negatively regulates BRCA1 in human cancer cells without methylation of histone H3 on lysine 9.''; PubMed Europe PMC Scholia
  34. Fryer CJ, White JB, Jones KA.; ''Mastermind recruits CycC:CDK8 to phosphorylate the Notch ICD and coordinate activation with turnover.''; PubMed Europe PMC Scholia
  35. Rachez C, Suldan Z, Ward J, Chang CP, Burakov D, Erdjument-Bromage H, Tempst P, Freedman LP.; ''A novel protein complex that interacts with the vitamin D3 receptor in a ligand-dependent manner and enhances VDR transactivation in a cell-free system.''; PubMed Europe PMC Scholia
  36. Maston GA, Evans SK, Green MR.; ''Transcriptional regulatory elements in the human genome.''; PubMed Europe PMC Scholia
  37. Chi XZ, Yang JO, Lee KY, Ito K, Sakakura C, Li QL, Kim HR, Cha EJ, Lee YH, Kaneda A, Ushijima T, Kim WJ, Ito Y, Bae SC.; ''RUNX3 suppresses gastric epithelial cell growth by inducing p21(WAF1/Cip1) expression in cooperation with transforming growth factor {beta}-activated SMAD.''; PubMed Europe PMC Scholia
  38. Livide G, Patriarchi T, Amenduni M, Amabile S, Yasui D, Calcagno E, Lo Rizzo C, De Falco G, Ulivieri C, Ariani F, Mari F, Mencarelli MA, Hell JW, Renieri A, Meloni I.; ''GluD1 is a common altered player in neuronal differentiation from both MECP2-mutated and CDKL5-mutated iPS cells.''; PubMed Europe PMC Scholia
  39. Accili D, Arden KC.; ''FoxOs at the crossroads of cellular metabolism, differentiation, and transformation.''; PubMed Europe PMC Scholia
  40. Durand S, Patrizi A, Quast KB, Hachigian L, Pavlyuk R, Saxena A, Carninci P, Hensch TK, Fagiolini M.; ''NMDA receptor regulation prevents regression of visual cortical function in the absence of Mecp2.''; PubMed Europe PMC Scholia
  41. Yoon HG, Chan DW, Reynolds AB, Qin J, Wong J.; ''N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso.''; PubMed Europe PMC Scholia
  42. Kuo YH, Zaidi SK, Gornostaeva S, Komori T, Stein GS, Castilla LH.; ''Runx2 induces acute myeloid leukemia in cooperation with Cbfbeta-SMMHC in mice.''; PubMed Europe PMC Scholia
  43. Wang X, Blagden C, Fan J, Nowak SJ, Taniuchi I, Littman DR, Burden SJ.; ''Runx1 prevents wasting, myofibrillar disorganization, and autophagy of skeletal muscle.''; PubMed Europe PMC Scholia
  44. Yasui DH, Gonzales ML, Aflatooni JO, Crary FK, Hu DJ, Gavino BJ, Golub MS, Vincent JB, Carolyn Schanen N, Olson CO, Rastegar M, Lasalle JM.; ''Mice with an isoform-ablating Mecp2 exon 1 mutation recapitulate the neurologic deficits of Rett syndrome.''; PubMed Europe PMC Scholia
  45. Pierce AD, Anglin IE, Vitolo MI, Mochin MT, Underwood KF, Goldblum SE, Kommineni S, Passaniti A.; ''Glucose-activated RUNX2 phosphorylation promotes endothelial cell proliferation and an angiogenic phenotype.''; PubMed Europe PMC Scholia
  46. Tsujimura K, Irie K, Nakashima H, Egashira Y, Fukao Y, Fujiwara M, Itoh M, Uesaka M, Imamura T, Nakahata Y, Yamashita Y, Abe T, Takamori S, Nakashima K.; ''miR-199a Links MeCP2 with mTOR Signaling and Its Dysregulation Leads to Rett Syndrome Phenotypes.''; PubMed Europe PMC Scholia
  47. Shigesada K, van de Sluis B, Liu PP.; ''Mechanism of leukemogenesis by the inv(16) chimeric gene CBFB/PEBP2B-MHY11.''; PubMed Europe PMC Scholia
  48. Imai Y, Gates MA, Melby AE, Kimelman D, Schier AF, Talbot WS.; ''The homeobox genes vox and vent are redundant repressors of dorsal fates in zebrafish.''; PubMed Europe PMC Scholia
  49. Berlato C, Chan KV, Price AM, Canosa M, Scibetta AG, Hurst HC.; ''Alternative TFAP2A isoforms have distinct activities in breast cancer.''; PubMed Europe PMC Scholia
  50. Kovall RA.; ''Structures of CSL, Notch and Mastermind proteins: piecing together an active transcription complex.''; PubMed Europe PMC Scholia
  51. Kimura H, Shiota K.; ''Methyl-CpG-binding protein, MeCP2, is a target molecule for maintenance DNA methyltransferase, Dnmt1.''; PubMed Europe PMC Scholia
  52. Chen Y, Shin BC, Thamotharan S, Devaskar SU.; ''Creb1-Mecp2-(m)CpG complex transactivates postnatal murine neuronal glucose transporter isoform 3 expression.''; PubMed Europe PMC Scholia
  53. Kanno T, Kanno Y, Chen LF, Ogawa E, Kim WY, Ito Y.; ''Intrinsic transcriptional activation-inhibition domains of the polyomavirus enhancer binding protein 2/core binding factor alpha subunit revealed in the presence of the beta subunit.''; PubMed Europe PMC Scholia
  54. Scerbo P, Marchal L, Kodjabachian L.; ''Lineage commitment of embryonic cells involves MEK1-dependent clearance of pluripotency regulator Ventx2.''; PubMed Europe PMC Scholia
  55. Gao J, Chen Y, Wu KC, Liu J, Zhao YQ, Pan YL, Du R, Zheng GR, Xiong YM, Xu HL, Fan DM.; ''RUNX3 directly interacts with intracellular domain of Notch1 and suppresses Notch signaling in hepatocellular carcinoma cells.''; PubMed Europe PMC Scholia
  56. Eijkelenboom A, Burgering BM.; ''FOXOs: signalling integrators for homeostasis maintenance.''; PubMed Europe PMC Scholia
  57. Kundu M, Javed A, Jeon JP, Horner A, Shum L, Eckhaus M, Muenke M, Lian JB, Yang Y, Nuckolls GH, Stein GS, Liu PP.; ''Cbfbeta interacts with Runx2 and has a critical role in bone development.''; PubMed Europe PMC Scholia
  58. Wang D, Shin TH, Kudlow JE.; ''Transcription factor AP-2 controls transcription of the human transforming growth factor-alpha gene.''; PubMed Europe PMC Scholia
  59. Plummer JT, Evgrafov OV, Bergman MY, Friez M, Haiman CA, Levitt P, Aldinger KA.; ''Transcriptional regulation of the MET receptor tyrosine kinase gene by MeCP2 and sex-specific expression in autism and Rett syndrome.''; PubMed Europe PMC Scholia
  60. Van Esch H, Bauters M, Ignatius J, Jansen M, Raynaud M, Hollanders K, Lugtenberg D, Bienvenu T, Jensen LR, Gecz J, Moraine C, Marynen P, Fryns JP, Froyen G.; ''Duplication of the MECP2 region is a frequent cause of severe mental retardation and progressive neurological symptoms in males.''; PubMed Europe PMC Scholia
  61. Bertoli C, Klier S, McGowan C, Wittenberg C, de Bruin RA.; ''Chk1 inhibits E2F6 repressor function in response to replication stress to maintain cell-cycle transcription.''; PubMed Europe PMC Scholia
  62. Zhou G, Zheng Q, Engin F, Munivez E, Chen Y, Sebald E, Krakow D, Lee B.; ''Dominance of SOX9 function over RUNX2 during skeletogenesis.''; PubMed Europe PMC Scholia
  63. Harikrishnan KN, Chow MZ, Baker EK, Pal S, Bassal S, Brasacchio D, Wang L, Craig JM, Jones PL, Sif S, El-Osta A.; ''Brahma links the SWI/SNF chromatin-remodeling complex with MeCP2-dependent transcriptional silencing.''; PubMed Europe PMC Scholia
  64. Blazek E, Mittler G, Meisterernst M.; ''The mediator of RNA polymerase II.''; PubMed Europe PMC Scholia
  65. Melnikova VO, Dobroff AS, Zigler M, Villares GJ, Braeuer RR, Wang H, Huang L, Bar-Eli M.; ''CREB inhibits AP-2alpha expression to regulate the malignant phenotype of melanoma.''; PubMed Europe PMC Scholia
  66. Whittle MC, Izeradjene K, Rani PG, Feng L, Carlson MA, DelGiorno KE, Wood LD, Goggins M, Hruban RH, Chang AE, Calses P, Thorsen SM, Hingorani SR.; ''RUNX3 Controls a Metastatic Switch in Pancreatic Ductal Adenocarcinoma.''; PubMed Europe PMC Scholia
  67. Zhang YY, Li X, Qian SW, Guo L, Huang HY, He Q, Liu Y, Ma CG, Tang QQ.; ''Down-regulation of type I Runx2 mediated by dexamethasone is required for 3T3-L1 adipogenesis.''; PubMed Europe PMC Scholia
  68. McPherson LA, Weigel RJ.; ''AP2alpha and AP2gamma: a comparison of binding site specificity and trans-activation of the estrogen receptor promoter and single site promoter constructs.''; PubMed Europe PMC Scholia
  69. Fainaru O, Woolf E, Lotem J, Yarmus M, Brenner O, Goldenberg D, Negreanu V, Bernstein Y, Levanon D, Jung S, Groner Y.; ''Runx3 regulates mouse TGF-beta-mediated dendritic cell function and its absence results in airway inflammation.''; PubMed Europe PMC Scholia
  70. Huang B, Qu Z, Ong CW, Tsang YH, Xiao G, Shapiro D, Salto-Tellez M, Ito K, Ito Y, Chen LF.; ''RUNX3 acts as a tumor suppressor in breast cancer by targeting estrogen receptor α.''; PubMed Europe PMC Scholia
  71. Jepsen K, Rosenfeld MG.; ''Biological roles and mechanistic actions of co-repressor complexes.''; PubMed Europe PMC Scholia
  72. Zarelli VE, Dawid IB.; ''Inhibition of neural crest formation by Kctd15 involves regulation of transcription factor AP-2.''; PubMed Europe PMC Scholia
  73. Wu X, Gao H, Bleday R, Zhu Z.; ''Homeobox transcription factor VentX regulates differentiation and maturation of human dendritic cells.''; PubMed Europe PMC Scholia
  74. Van Esch H.; ''MECP2 Duplication Syndrome.''; PubMed Europe PMC Scholia
  75. Vousden KH, Prives C.; ''Blinded by the Light: The Growing Complexity of p53.''; PubMed Europe PMC Scholia
  76. Yuan CX, Ito M, Fondell JD, Fu ZY, Roeder RG.; ''The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion.''; PubMed Europe PMC Scholia
  77. Storre J, Elsässer HP, Fuchs M, Ullmann D, Livingston DM, Gaubatz S.; ''Homeotic transformations of the axial skeleton that accompany a targeted deletion of E2f6.''; PubMed Europe PMC Scholia
  78. LiCalsi C, Christophe S, Steger DJ, Buescher M, Fischer W, Mellon PL.; ''AP-2 family members regulate basal and cAMP-induced expression of human chorionic gonadotropin.''; PubMed Europe PMC Scholia
  79. Lin X, Duan X, Liang YY, Su Y, Wrighton KH, Long J, Hu M, Davis CM, Wang J, Brunicardi FC, Shi Y, Chen YG, Meng A, Feng XH.; ''PPM1A functions as a Smad phosphatase to terminate TGFbeta signaling.''; PubMed Europe PMC Scholia
  80. Joss-Moore LA, Wang Y, Ogata EM, Sainz AJ, Yu X, Callaway CW, McKnight RA, Albertine KH, Lane RH.; ''IUGR differentially alters MeCP2 expression and H3K9Me3 of the PPARγ gene in male and female rat lungs during alveolarization.''; PubMed Europe PMC Scholia
  81. Dragich JM, Kim YH, Arnold AP, Schanen NC.; ''Differential distribution of the MeCP2 splice variants in the postnatal mouse brain.''; PubMed Europe PMC Scholia
  82. Maezawa I, Jin LW.; ''Rett syndrome microglia damage dendrites and synapses by the elevated release of glutamate.''; PubMed Europe PMC Scholia
  83. Puig-Kröger A, Aguilera-Montilla N, Martínez-Nuñez R, Domínguez-Soto A, Sánchez-Cabo F, Martín-Gayo E, Zaballos A, Toribio ML, Groner Y, Ito Y, Dopazo A, Corcuera MT, Alonso Martín MJ, Vega MA, Corbí AL.; ''The novel RUNX3/p33 isoform is induced upon monocyte-derived dendritic cell maturation and downregulates IL-8 expression.''; PubMed Europe PMC Scholia
  84. Bray SJ.; ''Notch signalling: a simple pathway becomes complex.''; PubMed Europe PMC Scholia
  85. Cheng TL, Wang Z, Liao Q, Zhu Y, Zhou WH, Xu W, Qiu Z.; ''MeCP2 suppresses nuclear microRNA processing and dendritic growth by regulating the DGCR8/Drosha complex.''; PubMed Europe PMC Scholia
  86. Umair Z, Kumar S, Kim DH, Rafiq K, Kumar V, Kim S, Park JB, Lee JY, Lee U, Kim J.; ''Ventx1.1 as a Direct Repressor of Early Neural Gene zic3 in Xenopus laevis.''; PubMed Europe PMC Scholia
  87. Long F.; ''Building strong bones: molecular regulation of the osteoblast lineage.''; PubMed Europe PMC Scholia
  88. Le Marer N.; ''GALECTIN-3 expression in differentiating human myeloid cells.''; PubMed Europe PMC Scholia
  89. Tropea D, Giacometti E, Wilson NR, Beard C, McCurry C, Fu DD, Flannery R, Jaenisch R, Sur M.; ''Partial reversal of Rett Syndrome-like symptoms in MeCP2 mutant mice.''; PubMed Europe PMC Scholia
  90. Sztainberg Y, Chen HM, Swann JW, Hao S, Tang B, Wu Z, Tang J, Wan YW, Liu Z, Rigo F, Zoghbi HY.; ''Reversal of phenotypes in MECP2 duplication mice using genetic rescue or antisense oligonucleotides.''; PubMed Europe PMC Scholia
  91. Scibetta AG, Wong PP, Chan KV, Canosa M, Hurst HC.; ''Dual association by TFAP2A during activation of the p21cip/CDKN1A promoter.''; PubMed Europe PMC Scholia
  92. Davidson AJ, Zon LI.; ''Turning mesoderm into blood: the formation of hematopoietic stem cells during embryogenesis.''; PubMed Europe PMC Scholia
  93. Mann J, Chu DC, Maxwell A, Oakley F, Zhu NL, Tsukamoto H, Mann DA.; ''MeCP2 controls an epigenetic pathway that promotes myofibroblast transdifferentiation and fibrosis.''; PubMed Europe PMC Scholia
  94. Wu X, Gao H, Ke W, Hager M, Xiao S, Freeman MR, Zhu Z.; ''VentX trans-activates p53 and p16ink4a to regulate cellular senescence.''; PubMed Europe PMC Scholia
  95. He LJ, Liu N, Cheng TL, Chen XJ, Li YD, Shu YS, Qiu ZL, Zhang XH.; ''Conditional deletion of Mecp2 in parvalbumin-expressing GABAergic cells results in the absence of critical period plasticity.''; PubMed Europe PMC Scholia
  96. Ebert DH, Gabel HW, Robinson ND, Kastan NR, Hu LS, Cohen S, Navarro AJ, Lyst MJ, Ekiert R, Bird AP, Greenberg ME.; ''Activity-dependent phosphorylation of MeCP2 threonine 308 regulates interaction with NCoR.''; PubMed Europe PMC Scholia
  97. Ebihara T, Ebihara T, Song C, Ryu SH, Plougastel-Douglas B, Yang L, Levanon D, Groner Y, Bern MD, Stappenbeck TS, Colonna M, Egawa T, Yokoyama WM.; ''Runx3 specifies lineage commitment of innate lymphoid cells.''; PubMed Europe PMC Scholia
  98. Orlic-Milacic M, Kaufman L, Mikhailov A, Cheung AY, Mahmood H, Ellis J, Gianakopoulos PJ, Minassian BA, Vincent JB.; ''Over-expression of either MECP2_e1 or MECP2_e2 in neuronally differentiated cells results in different patterns of gene expression.''; PubMed Europe PMC Scholia
  99. Li Y, Wang H, Muffat J, Cheng AW, Orlando DA, Lovén J, Kwok SM, Feldman DA, Bateup HS, Gao Q, Hockemeyer D, Mitalipova M, Lewis CA, Vander Heiden MG, Sur M, Young RA, Jaenisch R.; ''Global transcriptional and translational repression in human-embryonic-stem-cell-derived Rett syndrome neurons.''; PubMed Europe PMC Scholia
  100. Qiao Y, Lin SJ, Chen Y, Voon DC, Zhu F, Chuang LS, Wang T, Tan P, Lee SC, Yeoh KG, Sudol M, Ito Y.; ''RUNX3 is a novel negative regulator of oncogenic TEAD-YAP complex in gastric cancer.''; PubMed Europe PMC Scholia
  101. Li QL, Ito K, Sakakura C, Fukamachi H, Inoue Ki, Chi XZ, Lee KY, Nomura S, Lee CW, Han SB, Kim HM, Kim WJ, Yamamoto H, Yamashita N, Yano T, Ikeda T, Itohara S, Inazawa J, Abe T, Hagiwara A, Yamagishi H, Ooe A, Kaneda A, Sugimura T, Ushijima T, Bae SC, Ito Y.; ''Causal relationship between the loss of RUNX3 expression and gastric cancer.''; PubMed Europe PMC Scholia
  102. Jaruga A, Hordyjewska E, Kandzierski G, Tylzanowski P.; ''Cleidocranial dysplasia and RUNX2-clinical phenotype-genotype correlation.''; PubMed Europe PMC Scholia
  103. Cyr AR, Kulak MV, Park JM, Bogachek MV, Spanheimer PM, Woodfield GW, White-Baer LS, O'Malley YQ, Sugg SL, Olivier AK, Zhang W, Domann FE, Weigel RJ.; ''TFAP2C governs the luminal epithelial phenotype in mammary development and carcinogenesis.''; PubMed Europe PMC Scholia
  104. Domínguez-Soto A, Relloso M, Vega MA, Corbí AL, Puig-Kröger A.; ''RUNX3 regulates the activity of the CD11a and CD49d integrin gene promoters.''; PubMed Europe PMC Scholia
  105. Zhou S, Fujimuro M, Hsieh JJ, Chen L, Miyamoto A, Weinmaster G, Hayward SD.; ''SKIP, a CBF1-associated protein, interacts with the ankyrin repeat domain of NotchIC To facilitate NotchIC function.''; PubMed Europe PMC Scholia
  106. Reis BS, Rogoz A, Costa-Pinto FA, Taniuchi I, Mucida D.; ''Mutual expression of the transcription factors Runx3 and ThPOK regulates intestinal CD4⁺ T cell immunity.''; PubMed Europe PMC Scholia
  107. Wilson JJ, Kovall RA.; ''Crystal structure of the CSL-Notch-Mastermind ternary complex bound to DNA.''; PubMed Europe PMC Scholia
  108. Inoue K, Ozaki S, Shiga T, Ito K, Masuda T, Okado N, Iseda T, Kawaguchi S, Ogawa M, Bae SC, Yamashita N, Itohara S, Kudo N, Ito Y.; ''Runx3 controls the axonal projection of proprioceptive dorsal root ganglion neurons.''; PubMed Europe PMC Scholia
  109. Wotton D, Lo RS, Lee S, Massagué J.; ''A Smad transcriptional corepressor.''; PubMed Europe PMC Scholia
  110. Li W, Calfa G, Larimore J, Pozzo-Miller L.; ''Activity-dependent BDNF release and TRPC signaling is impaired in hippocampal neurons of Mecp2 mutant mice.''; PubMed Europe PMC Scholia
  111. Friedman JR, Fredericks WJ, Jensen DE, Speicher DW, Huang XP, Neilson EG, Rauscher FJ.; ''KAP-1, a novel corepressor for the highly conserved KRAB repression domain.''; PubMed Europe PMC Scholia
  112. Yoshida CA, Furuichi T, Fujita T, Fukuyama R, Kanatani N, Kobayashi S, Satake M, Takada K, Komori T.; ''Core-binding factor beta interacts with Runx2 and is required for skeletal development.''; PubMed Europe PMC Scholia
  113. Feldman D, Banerjee A, Sur M.; ''Developmental Dynamics of Rett Syndrome.''; PubMed Europe PMC Scholia
  114. Schulmann K, Sterian A, Berki A, Yin J, Sato F, Xu Y, Olaru A, Wang S, Mori Y, Deacu E, Hamilton J, Kan T, Krasna MJ, Beer DG, Pepe MS, Abraham JM, Feng Z, Schmiegel W, Greenwald BD, Meltzer SJ.; ''Inactivation of p16, RUNX3, and HPP1 occurs early in Barrett's-associated neoplastic progression and predicts progression risk.''; PubMed Europe PMC Scholia
  115. Lengner CJ, Hassan MQ, Serra RW, Lepper C, van Wijnen AJ, Stein JL, Lian JB, Stein GS.; ''Nkx3.2-mediated repression of Runx2 promotes chondrogenic differentiation.''; PubMed Europe PMC Scholia
  116. Williams T, Tjian R.; ''Characterization of a dimerization motif in AP-2 and its function in heterologous DNA-binding proteins.''; PubMed Europe PMC Scholia
  117. Urdinguio RG, Lopez-Serra L, Lopez-Nieva P, Alaminos M, Diaz-Uriarte R, Fernandez AF, Esteller M.; ''Mecp2-null mice provide new neuronal targets for Rett syndrome.''; PubMed Europe PMC Scholia
  118. Eckert D, Buhl S, Weber S, Jäger R, Schorle H.; ''The AP-2 family of transcription factors.''; PubMed Europe PMC Scholia
  119. Bertoli C, Herlihy AE, Pennycook BR, Kriston-Vizi J, de Bruin RAM.; ''Sustained E2F-Dependent Transcription Is a Key Mechanism to Prevent Replication-Stress-Induced DNA Damage.''; PubMed Europe PMC Scholia
  120. Olson CO, Zachariah RM, Ezeonwuka CD, Liyanage VR, Rastegar M.; ''Brain region-specific expression of MeCP2 isoforms correlates with DNA methylation within Mecp2 regulatory elements.''; PubMed Europe PMC Scholia
  121. Cai X, Gao L, Teng L, Ge J, Oo ZM, Kumar AR, Gilliland DG, Mason PJ, Tan K, Speck NA.; ''Runx1 Deficiency Decreases Ribosome Biogenesis and Confers Stress Resistance to Hematopoietic Stem and Progenitor Cells.''; PubMed Europe PMC Scholia
  122. Williams T, Tjian R.; ''Analysis of the DNA-binding and activation properties of the human transcription factor AP-2.''; PubMed Europe PMC Scholia
  123. Oh H, Irvine KD.; ''Yorkie: the final destination of Hippo signaling.''; PubMed Europe PMC Scholia
  124. Krishnan N, Krishnan K, Connors CR, Choy MS, Page R, Peti W, Van Aelst L, Shea SD, Tonks NK.; ''PTP1B inhibition suggests a therapeutic strategy for Rett syndrome.''; PubMed Europe PMC Scholia
  125. Yang DC, Yang MH, Tsai CC, Huang TF, Chen YH, Hung SC.; ''Hypoxia inhibits osteogenesis in human mesenchymal stem cells through direct regulation of RUNX2 by TWIST.''; PubMed Europe PMC Scholia
  126. Mortus JR, Zhang Y, Hughes DP.; ''Developmental pathways hijacked by osteosarcoma.''; PubMed Europe PMC Scholia
  127. Rosenfeld MG, Lunyak VV, Glass CK.; ''Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response.''; PubMed Europe PMC Scholia
  128. Lee MH, Kim YJ, Yoon WJ, Kim JI, Kim BG, Hwang YS, Wozney JM, Chi XZ, Bae SC, Choi KY, Cho JY, Choi JY, Ryoo HM.; ''Dlx5 specifically regulates Runx2 type II expression by binding to homeodomain-response elements in the Runx2 distal promoter.''; PubMed Europe PMC Scholia
  129. Näär AM, Lemon BD, Tjian R.; ''Transcriptional coactivator complexes.''; PubMed Europe PMC Scholia
  130. Bialek P, Kern B, Yang X, Schrock M, Sosic D, Hong N, Wu H, Yu K, Ornitz DM, Olson EN, Justice MJ, Karsenty G.; ''A twist code determines the onset of osteoblast differentiation.''; PubMed Europe PMC Scholia
  131. Bamforth SD, Bragança J, Eloranta JJ, Murdoch JN, Marques FI, Kranc KR, Farza H, Henderson DJ, Hurst HC, Bhattacharya S.; ''Cardiac malformations, adrenal agenesis, neural crest defects and exencephaly in mice lacking Cited2, a new Tfap2 co-activator.''; PubMed Europe PMC Scholia
  132. Barolo S, Posakony JW.; ''Three habits of highly effective signaling pathways: principles of transcriptional control by developmental cell signaling.''; PubMed Europe PMC Scholia
  133. Li XQ, Du X, Li DM, Kong PZ, Sun Y, Liu PF, Wang QS, Feng YM.; ''ITGBL1 Is a Runx2 Transcriptional Target and Promotes Breast Cancer Bone Metastasis by Activating the TGFβ Signaling Pathway.''; PubMed Europe PMC Scholia
  134. Turner BC, Zhang J, Gumbs AA, Maher MG, Kaplan L, Carter D, Glazer PM, Hurst HC, Haffty BG, Williams T.; ''Expression of AP-2 transcription factors in human breast cancer correlates with the regulation of multiple growth factor signalling pathways.''; PubMed Europe PMC Scholia
  135. Ducy P, Karsenty G.; ''Two distinct osteoblast-specific cis-acting elements control expression of a mouse osteocalcin gene.''; PubMed Europe PMC Scholia
  136. Gaubatz S, Wood JG, Livingston DM.; ''Unusual proliferation arrest and transcriptional control properties of a newly discovered E2F family member, E2F-6.''; PubMed Europe PMC Scholia
  137. Kaddoum L, Panayotis N, Mazarguil H, Giglia-Mari G, Roux JC, Joly E.; ''Isoform-specific anti-MeCP2 antibodies confirm that expression of the e1 isoform strongly predominates in the brain.''; PubMed Europe PMC Scholia
  138. deConinck EC, McPherson LA, Weigel RJ.; ''Transcriptional regulation of estrogen receptor in breast carcinomas.''; PubMed Europe PMC Scholia
  139. Roca H, Phimphilai M, Gopalakrishnan R, Xiao G, Franceschi RT.; ''Cooperative interactions between RUNX2 and homeodomain protein-binding sites are critical for the osteoblast-specific expression of the bone sialoprotein gene.''; PubMed Europe PMC Scholia
  140. Leong WY, Lim ZH, Korzh V, Pietri T, Goh EL.; ''Methyl-CpG Binding Protein 2 (Mecp2) Regulates Sensory Function Through Sema5b and Robo2.''; PubMed Europe PMC Scholia
  141. Louvi A, Artavanis-Tsakonas S.; ''Notch signalling in vertebrate neural development.''; PubMed Europe PMC Scholia
  142. Dhillon VS, Shahid M, Husain SA.; ''CpG methylation of the FHIT, FANCF, cyclin-D2, BRCA2 and RUNX3 genes in Granulosa cell tumors (GCTs) of ovarian origin.''; PubMed Europe PMC Scholia
  143. Dupont S, Mamidi A, Cordenonsi M, Montagner M, Zacchigna L, Adorno M, Martello G, Stinchfield MJ, Soligo S, Morsut L, Inui M, Moro S, Modena N, Argenton F, Newfeld SJ, Piccolo S.; ''FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling, controls Smad4 monoubiquitination.''; PubMed Europe PMC Scholia
  144. Calnan DR, Brunet A.; ''The FoxO code.''; PubMed Europe PMC Scholia
  145. Ryan RF, Schultz DC, Ayyanathan K, Singh PB, Friedman JR, Fredericks WJ, Rauscher FJ.; ''KAP-1 corepressor protein interacts and colocalizes with heterochromatic and euchromatic HP1 proteins: a potential role for Krüppel-associated box-zinc finger proteins in heterochromatin-mediated gene silencing.''; PubMed Europe PMC Scholia
  146. Nan X, Ng HH, Johnson CA, Laherty CD, Turner BM, Eisenman RN, Bird A.; ''Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex.''; PubMed Europe PMC Scholia
  147. Wong PP, Miranda F, Chan KV, Berlato C, Hurst HC, Scibetta AG.; ''Histone demethylase KDM5B collaborates with TFAP2C and Myc to repress the cell cycle inhibitor p21(cip) (CDKN1A).''; PubMed Europe PMC Scholia
  148. De Andrade JP, Park JM, Gu VW, Woodfield GW, Kulak MV, Lorenzen AW, Wu VT, Van Dorin SE, Spanheimer PM, Weigel RJ.; ''EGFR Is Regulated by TFAP2C in Luminal Breast Cancer and Is a Target for Vandetanib.''; PubMed Europe PMC Scholia
  149. Mangan JK, Speck NA.; ''RUNX1 mutations in clonal myeloid disorders: from conventional cytogenetics to next generation sequencing, a story 40 years in the making.''; PubMed Europe PMC Scholia
  150. Chao HT, Chen H, Samaco RC, Xue M, Chahrour M, Yoo J, Neul JL, Gong S, Lu HC, Heintz N, Ekker M, Rubenstein JL, Noebels JL, Rosenmund C, Zoghbi HY.; ''Dysfunction in GABA signalling mediates autism-like stereotypies and Rett syndrome phenotypes.''; PubMed Europe PMC Scholia
  151. Scerbo P, Girardot F, Vivien C, Markov GV, Luxardi G, Demeneix B, Kodjabachian L, Coen L.; ''Ventx factors function as Nanog-like guardians of developmental potential in Xenopus.''; PubMed Europe PMC Scholia
  152. Degano AL, Pasterkamp RJ, Ronnett GV.; ''MeCP2 deficiency disrupts axonal guidance, fasciculation, and targeting by altering Semaphorin 3F function.''; PubMed Europe PMC Scholia
  153. Kramer I, Sigrist M, de Nooij JC, Taniuchi I, Jessell TM, Arber S.; ''A role for Runx transcription factor signaling in dorsal root ganglion sensory neuron diversification.''; PubMed Europe PMC Scholia
  154. Tribioli C, Lufkin T.; ''The murine Bapx1 homeobox gene plays a critical role in embryonic development of the axial skeleton and spleen.''; PubMed Europe PMC Scholia
  155. Kruiswijk F, Labuschagne CF, Vousden KH.; ''p53 in survival, death and metabolic health: a lifeguard with a licence to kill.''; PubMed Europe PMC Scholia
  156. Li Q, Pan H, Guan L, Su D, Ma X.; ''CITED2 mutation links congenital heart defects to dysregulation of the cardiac gene VEGF and PITX2C expression.''; PubMed Europe PMC Scholia
  157. Ducy P, Starbuck M, Priemel M, Shen J, Pinero G, Geoffroy V, Amling M, Karsenty G.; ''A Cbfa1-dependent genetic pathway controls bone formation beyond embryonic development.''; PubMed Europe PMC Scholia
  158. Chen CR, Kang Y, Siegel PM, Massagué J.; ''E2F4/5 and p107 as Smad cofactors linking the TGFbeta receptor to c-myc repression.''; PubMed Europe PMC Scholia
  159. Karsenty G.; ''Transcriptional control of skeletogenesis.''; PubMed Europe PMC Scholia
  160. Chen CL, Broom DC, Liu Y, de Nooij JC, Li Z, Cen C, Samad OA, Jessell TM, Woolf CJ, Ma Q.; ''Runx1 determines nociceptive sensory neuron phenotype and is required for thermal and neuropathic pain.''; PubMed Europe PMC Scholia
  161. Levkovitz L, Yosef N, Gershengorn MC, Ruppin E, Sharan R, Oron Y.; ''A novel HMM-based method for detecting enriched transcription factor binding sites reveals RUNX3 as a potential target in pancreatic cancer biology.''; PubMed Europe PMC Scholia
  162. Arman M, Aguilera-Montilla N, Mas V, Puig-Kröger A, Pignatelli M, Guigó R, Corbí AL, Lozano F.; ''The human CD6 gene is transcriptionally regulated by RUNX and Ets transcription factors in T cells.''; PubMed Europe PMC Scholia
  163. Hwang CK, Song KY, Kim CS, Choi HS, Guo XH, Law PY, Wei LN, Loh HH.; ''Epigenetic programming of mu-opioid receptor gene in mouse brain is regulated by MeCP2 and Brg1 chromatin remodelling factor.''; PubMed Europe PMC Scholia
  164. Huang S, Jean D, Luca M, Tainsky MA, Bar-Eli M.; ''Loss of AP-2 results in downregulation of c-KIT and enhancement of melanoma tumorigenicity and metastasis.''; PubMed Europe PMC Scholia
  165. Lioy DT, Garg SK, Monaghan CE, Raber J, Foust KD, Kaspar BK, Hirrlinger PG, Kirchhoff F, Bissonnette JM, Ballas N, Mandel G.; ''A role for glia in the progression of Rett's syndrome.''; PubMed Europe PMC Scholia
  166. Le Y, Gao H, Bleday R, Zhu Z.; ''The homeobox protein VentX reverts immune suppression in the tumor microenvironment.''; PubMed Europe PMC Scholia
  167. Kadonaga JT.; ''Regulation of RNA polymerase II transcription by sequence-specific DNA binding factors.''; PubMed Europe PMC Scholia
  168. Mnatzakanian GN, Lohi H, Munteanu I, Alfred SE, Yamada T, MacLeod PJ, Jones JR, Scherer SW, Schanen NC, Friez MJ, Vincent JB, Minassian BA.; ''A previously unidentified MECP2 open reading frame defines a new protein isoform relevant to Rett syndrome.''; PubMed Europe PMC Scholia
  169. Bäckström S, Wolf-Watz M, Grundström C, Härd T, Grundström T, Sauer UH.; ''The RUNX1 Runt domain at 1.25A resolution: a structural switch and specifically bound chloride ions modulate DNA binding.''; PubMed Europe PMC Scholia
  170. Dykes IM, Tempest L, Lee SI, Turner EE.; ''Brn3a and Islet1 act epistatically to regulate the gene expression program of sensory differentiation.''; PubMed Europe PMC Scholia
  171. Collins AL, Levenson JM, Vilaythong AP, Richman R, Armstrong DL, Noebels JL, David Sweatt J, Zoghbi HY.; ''Mild overexpression of MeCP2 causes a progressive neurological disorder in mice.''; PubMed Europe PMC Scholia
  172. Zhang L, Lukasik SM, Speck NA, Bushweller JH.; ''Structural and functional characterization of Runx1, CBF beta, and CBF beta-SMMHC.''; PubMed Europe PMC Scholia
  173. Bamforth SD, Bragança J, Farthing CR, Schneider JE, Broadbent C, Michell AC, Clarke K, Neubauer S, Norris D, Brown NA, Anderson RH, Bhattacharya S.; ''Cited2 controls left-right patterning and heart development through a Nodal-Pitx2c pathway.''; PubMed Europe PMC Scholia
  174. Ichikawa M, Yoshimi A, Nakagawa M, Nishimoto N, Watanabe-Okochi N, Kurokawa M.; ''A role for RUNX1 in hematopoiesis and myeloid leukemia.''; PubMed Europe PMC Scholia
  175. Teplyuk NM, Galindo M, Teplyuk VI, Pratap J, Young DW, Lapointe D, Javed A, Stein JL, Lian JB, Stein GS, van Wijnen AJ.; ''Runx2 regulates G protein-coupled signaling pathways to control growth of osteoblast progenitors.''; PubMed Europe PMC Scholia
  176. Chahrour M, Jung SY, Shaw C, Zhou X, Wong ST, Qin J, Zoghbi HY.; ''MeCP2, a key contributor to neurological disease, activates and represses transcription.''; PubMed Europe PMC Scholia
  177. Begon DY, Delacroix L, Vernimmen D, Jackers P, Winkler R.; ''Yin Yang 1 cooperates with activator protein 2 to stimulate ERBB2 gene expression in mammary cancer cells.''; PubMed Europe PMC Scholia
  178. Rogers CD, Archer TC, Cunningham DD, Grammer TC, Casey EM.; ''Sox3 expression is maintained by FGF signaling and restricted to the neural plate by Vent proteins in the Xenopus embryo.''; PubMed Europe PMC Scholia
  179. Bragança J, Eloranta JJ, Bamforth SD, Ibbitt JC, Hurst HC, Bhattacharya S.; ''Physical and functional interactions among AP-2 transcription factors, p300/CREB-binding protein, and CITED2.''; PubMed Europe PMC Scholia
  180. Trojer P, Cao AR, Gao Z, Li Y, Zhang J, Xu X, Li G, Losson R, Erdjument-Bromage H, Tempst P, Farnham PJ, Reinberg D.; ''L3MBTL2 protein acts in concert with PcG protein-mediated monoubiquitination of H2A to establish a repressive chromatin structure.''; PubMed Europe PMC Scholia
  181. Chen L, Chen K, Lavery LA, Baker SA, Shaw CA, Li W, Zoghbi HY.; ''MeCP2 binds to non-CG methylated DNA as neurons mature, influencing transcription and the timing of onset for Rett syndrome.''; PubMed Europe PMC Scholia
  182. Landry JR, Kinston S, Knezevic K, de Bruijn MF, Wilson N, Nottingham WT, Peitz M, Edenhofer F, Pimanda JE, Ottersbach K, Göttgens B.; ''Runx genes are direct targets of Scl/Tal1 in the yolk sac and fetal liver.''; PubMed Europe PMC Scholia
  183. Guy J, Gan J, Selfridge J, Cobb S, Bird A.; ''Reversal of neurological defects in a mouse model of Rett syndrome.''; PubMed Europe PMC Scholia
  184. Kelleher RJ, Flanagan PM, Kornberg RD.; ''A novel mediator between activator proteins and the RNA polymerase II transcription apparatus.''; PubMed Europe PMC Scholia
  185. Cartwright P, Müller H, Wagener C, Holm K, Helin K.; ''E2F-6: a novel member of the E2F family is an inhibitor of E2F-dependent transcription.''; PubMed Europe PMC Scholia
  186. Trinh BQ, Barengo N, Kim SB, Lee JS, Zweidler-McKay PA, Naora H.; ''The homeobox gene DLX4 regulates erythro-megakaryocytic differentiation by stimulating IL-1β and NF-κB signaling.''; PubMed Europe PMC Scholia
  187. Lyst MJ, Ekiert R, Ebert DH, Merusi C, Nowak J, Selfridge J, Guy J, Kastan NR, Robinson ND, de Lima Alves F, Rappsilber J, Greenberg ME, Bird A.; ''Rett syndrome mutations abolish the interaction of MeCP2 with the NCoR/SMRT co-repressor.''; PubMed Europe PMC Scholia
  188. Keita M, Bachvarova M, Morin C, Plante M, Gregoire J, Renaud MC, Sebastianelli A, Trinh XB, Bachvarov D.; ''The RUNX1 transcription factor is expressed in serous epithelial ovarian carcinoma and contributes to cell proliferation, migration and invasion.''; PubMed Europe PMC Scholia
  189. Stroschein SL, Wang W, Zhou S, Zhou Q, Luo K.; ''Negative feedback regulation of TGF-beta signaling by the SnoN oncoprotein.''; PubMed Europe PMC Scholia
  190. Pande S, Browne G, Padmanabhan S, Zaidi SK, Lian JB, van Wijnen AJ, Stein JL, Stein GS.; ''Oncogenic cooperation between PI3K/Akt signaling and transcription factor Runx2 promotes the invasive properties of metastatic breast cancer cells.''; PubMed Europe PMC Scholia
  191. Thomas DM, Carty SA, Piscopo DM, Lee JS, Wang WF, Forrester WC, Hinds PW.; ''The retinoblastoma protein acts as a transcriptional coactivator required for osteogenic differentiation.''; PubMed Europe PMC Scholia
  192. Fryer CJ, Lamar E, Turbachova I, Kintner C, Jones KA.; ''Mastermind mediates chromatin-specific transcription and turnover of the Notch enhancer complex.''; PubMed Europe PMC Scholia
  193. Baron VT, Pio R, Jia Z, Mercola D.; ''Early Growth Response 3 regulates genes of inflammation and directly activates IL6 and IL8 expression in prostate cancer.''; PubMed Europe PMC Scholia
  194. Nuber UA, Kriaucionis S, Roloff TC, Guy J, Selfridge J, Steinhoff C, Schulz R, Lipkowitz B, Ropers HH, Holmes MC, Bird A.; ''Up-regulation of glucocorticoid-regulated genes in a mouse model of Rett syndrome.''; PubMed Europe PMC Scholia
  195. Mellén M, Ayata P, Dewell S, Kriaucionis S, Heintz N.; ''MeCP2 binds to 5hmC enriched within active genes and accessible chromatin in the nervous system.''; PubMed Europe PMC Scholia
  196. Yoshida CA, Yamamoto H, Fujita T, Furuichi T, Ito K, Inoue K, Yamana K, Zanma A, Takada K, Ito Y, Komori T.; ''Runx2 and Runx3 are essential for chondrocyte maturation, and Runx2 regulates limb growth through induction of Indian hedgehog.''; PubMed Europe PMC Scholia
  197. Schweisguth F.; ''Regulation of notch signaling activity.''; PubMed Europe PMC Scholia
  198. Wu X, Gao H, Ke W, Giese RW, Zhu Z.; ''The homeobox transcription factor VentX controls human macrophage terminal differentiation and proinflammatory activation.''; PubMed Europe PMC Scholia
  199. Justice NJ, Jan YN.; ''Variations on the Notch pathway in neural development.''; PubMed Europe PMC Scholia
  200. Kobayashi A, Senzaki K, Ozaki S, Yoshikawa M, Shiga T.; ''Runx1 promotes neuronal differentiation in dorsal root ganglion.''; PubMed Europe PMC Scholia
  201. Chen AI, de Nooij JC, Jessell TM.; ''Graded activity of transcription factor Runx3 specifies the laminar termination pattern of sensory axons in the developing spinal cord.''; PubMed Europe PMC Scholia
  202. Rawat VP, Arseni N, Ahmed F, Mulaw MA, Thoene S, Heilmeier B, Sadlon T, D'Andrea RJ, Hiddemann W, Bohlander SK, Buske C, Feuring-Buske M.; ''The vent-like homeobox gene VENTX promotes human myeloid differentiation and is highly expressed in acute myeloid leukemia.''; PubMed Europe PMC Scholia
  203. Tandon M, Chen Z, Pratap J.; ''Runx2 activates PI3K/Akt signaling via mTORC2 regulation in invasive breast cancer cells.''; PubMed Europe PMC Scholia
  204. Vladimirova V, Waha A, Lückerath K, Pesheva P, Probstmeier R.; ''Runx2 is expressed in human glioma cells and mediates the expression of galectin-3.''; PubMed Europe PMC Scholia
  205. Murakami M, Nakagawa M, Olson EN, Nakagawa O.; ''A WW domain protein TAZ is a critical coactivator for TBX5, a transcription factor implicated in Holt-Oram syndrome.''; PubMed Europe PMC Scholia
  206. Ruiz M, Pettaway C, Song R, Stoeltzing O, Ellis L, Bar-Eli M.; ''Activator protein 2alpha inhibits tumorigenicity and represses vascular endothelial growth factor transcription in prostate cancer cells.''; PubMed Europe PMC Scholia
  207. Ichikawa M, Asai T, Chiba S, Kurokawa M, Ogawa S.; ''Runx1/AML-1 ranks as a master regulator of adult hematopoiesis.''; PubMed Europe PMC Scholia
  208. Wong WF, Kohu K, Chiba T, Sato T, Satake M.; ''Interplay of transcription factors in T-cell differentiation and function: the role of Runx.''; PubMed Europe PMC Scholia
  209. Friedman AD.; ''Cell cycle and developmental control of hematopoiesis by Runx1.''; PubMed Europe PMC Scholia
  210. Zeng YX, Somasundaram K, el-Deiry WS.; ''AP2 inhibits cancer cell growth and activates p21WAF1/CIP1 expression.''; PubMed Europe PMC Scholia
  211. Wu D, Ozaki T, Yoshihara Y, Kubo N, Nakagawara A.; ''Runt-related transcription factor 1 (RUNX1) stimulates tumor suppressor p53 protein in response to DNA damage through complex formation and acetylation.''; PubMed Europe PMC Scholia
  212. Zhang HY, Jin L, Stilling GA, Ruebel KH, Coonse K, Tanizaki Y, Raz A, Lloyd RV.; ''RUNX1 and RUNX2 upregulate Galectin-3 expression in human pituitary tumors.''; PubMed Europe PMC Scholia
  213. Karsenty G, Olson EN.; ''Bone and Muscle Endocrine Functions: Unexpected Paradigms of Inter-organ Communication.''; PubMed Europe PMC Scholia
  214. Malik S, Roeder RG.; ''Dynamic regulation of pol II transcription by the mammalian Mediator complex.''; PubMed Europe PMC Scholia
  215. Giangrande PH, Zhu W, Schlisio S, Sun X, Mori S, Gaubatz S, Nevins JR.; ''A role for E2F6 in distinguishing G1/S- and G2/M-specific transcription.''; PubMed Europe PMC Scholia
  216. Mumm JS, Kopan R.; ''Notch signaling: from the outside in.''; PubMed Europe PMC Scholia
  217. Li W, Pozzo-Miller L.; ''BDNF deregulation in Rett syndrome.''; PubMed Europe PMC Scholia
  218. Bragança J, Swingler T, Marques FI, Jones T, Eloranta JJ, Hurst HC, Shioda T, Bhattacharya S.; ''Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2.''; PubMed Europe PMC Scholia
  219. Gianakopoulos PJ, Zhang Y, Pencea N, Orlic-Milacic M, Mittal K, Windpassinger C, White SJ, Kroisel PM, Chow EW, Saunders CJ, Minassian BA, Vincent JB.; ''Mutations in MECP2 exon 1 in classical Rett patients disrupt MECP2_e1 transcription, but not transcription of MECP2_e2.''; PubMed Europe PMC Scholia
  220. Takeda S, Bonnamy JP, Owen MJ, Ducy P, Karsenty G.; ''Continuous expression of Cbfa1 in nonhypertrophic chondrocytes uncovers its ability to induce hypertrophic chondrocyte differentiation and partially rescues Cbfa1-deficient mice.''; PubMed Europe PMC Scholia
  221. Margolin JF, Friedman JR, Meyer WK, Vissing H, Thiesen HJ, Rauscher FJ.; ''Krüppel-associated boxes are potent transcriptional repression domains.''; PubMed Europe PMC Scholia
  222. Ebert DH, Greenberg ME.; ''Activity-dependent neuronal signalling and autism spectrum disorder.''; PubMed Europe PMC Scholia
  223. Qiu Z, Sylwestrak EL, Lieberman DN, Zhang Y, Liu XY, Ghosh A.; ''The Rett syndrome protein MeCP2 regulates synaptic scaling.''; PubMed Europe PMC Scholia
  224. Varelas X, Sakuma R, Samavarchi-Tehrani P, Peerani R, Rao BM, Dembowy J, Yaffe MB, Zandstra PW, Wrana JL.; ''TAZ controls Smad nucleocytoplasmic shuttling and regulates human embryonic stem-cell self-renewal.''; PubMed Europe PMC Scholia
  225. Luckey MA, Kimura MY, Waickman AT, Feigenbaum L, Singer A, Park JH.; ''The transcription factor ThPOK suppresses Runx3 and imposes CD4(+) lineage fate by inducing the SOCS suppressors of cytokine signaling.''; PubMed Europe PMC Scholia
  226. Urrutia R.; ''KRAB-containing zinc-finger repressor proteins.''; PubMed Europe PMC Scholia
  227. Huntley S, Baggott DM, Hamilton AT, Tran-Gyamfi M, Yang S, Kim J, Gordon L, Branscomb E, Stubbs L.; ''A comprehensive catalog of human KRAB-associated zinc finger genes: insights into the evolutionary history of a large family of transcriptional repressors.''; PubMed Europe PMC Scholia
  228. Gao H, Wu B, Le Y, Zhu Z.; ''Homeobox protein VentX induces p53-independent apoptosis in cancer cells.''; PubMed Europe PMC Scholia
  229. Boller S, Grosschedl R.; ''The regulatory network of B-cell differentiation: a focused view of early B-cell factor 1 function.''; PubMed Europe PMC Scholia
  230. Bosher JM, Totty NF, Hsuan JJ, Williams T, Hurst HC.; ''A family of AP-2 proteins regulates c-erbB-2 expression in mammary carcinoma.''; PubMed Europe PMC Scholia
  231. Wolff EM, Liang G, Cortez CC, Tsai YC, Castelao JE, Cortessis VK, Tsao-Wei DD, Groshen S, Jones PA.; ''RUNX3 methylation reveals that bladder tumors are older in patients with a history of smoking.''; PubMed Europe PMC Scholia
  232. Eloranta JJ, Hurst HC.; ''Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo.''; PubMed Europe PMC Scholia
  233. Luikenhuis S, Giacometti E, Beard CF, Jaenisch R.; ''Expression of MeCP2 in postmitotic neurons rescues Rett syndrome in mice.''; PubMed Europe PMC Scholia
  234. Conaway JW, Florens L, Sato S, Tomomori-Sato C, Parmely TJ, Yao T, Swanson SK, Banks CA, Washburn MP, Conaway RC.; ''The mammalian Mediator complex.''; PubMed Europe PMC Scholia
  235. Nagarajan RP, Patzel KA, Martin M, Yasui DH, Swanberg SE, Hertz-Picciotto I, Hansen RL, Van de Water J, Pessah IN, Jiang R, Robinson WP, LaSalle JM.; ''MECP2 promoter methylation and X chromosome inactivation in autism.''; PubMed Europe PMC Scholia
  236. Johnson W, Albanese C, Handwerger S, Williams T, Pestell RG, Jameson JL.; ''Regulation of the human chorionic gonadotropin alpha- and beta-subunit promoters by AP-2.''; PubMed Europe PMC Scholia
  237. Li XQ, Lu JT, Tan CC, Wang QS, Feng YM.; ''RUNX2 promotes breast cancer bone metastasis by increasing integrin α5-mediated colonization.''; PubMed Europe PMC Scholia
  238. Liyanage VR, Zachariah RM, Rastegar M.; ''Decitabine alters the expression of Mecp2 isoforms via dynamic DNA methylation at the Mecp2 regulatory elements in neural stem cells.''; PubMed Europe PMC Scholia
  239. Tahirov TH, Inoue-Bungo T, Morii H, Fujikawa A, Sasaki M, Kimura K, Shiina M, Sato K, Kumasaka T, Yamamoto M, Ishii S, Ogata K.; ''Structural analyses of DNA recognition by the AML1/Runx-1 Runt domain and its allosteric control by CBFbeta.''; PubMed Europe PMC Scholia
  240. Williams CM, Scibetta AG, Friedrich JK, Canosa M, Berlato C, Moss CH, Hurst HC.; ''AP-2gamma promotes proliferation in breast tumour cells by direct repression of the CDKN1A gene.''; PubMed Europe PMC Scholia
  241. Ricciardi S, Boggio EM, Grosso S, Lonetti G, Forlani G, Stefanelli G, Calcagno E, Morello N, Landsberger N, Biffo S, Pizzorusso T, Giustetto M, Broccoli V.; ''Reduced AKT/mTOR signaling and protein synthesis dysregulation in a Rett syndrome animal model.''; PubMed Europe PMC Scholia
  242. Wysokinski D, Blasiak J, Pawlowska E.; ''Role of RUNX2 in Breast Carcinogenesis.''; PubMed Europe PMC Scholia
  243. Nakamura S, Senzaki K, Yoshikawa M, Nishimura M, Inoue K, Ito Y, Ozaki S, Shiga T.; ''Dynamic regulation of the expression of neurotrophin receptors by Runx3.''; PubMed Europe PMC Scholia
  244. Kerr B, Soto C J, Saez M, Abrams A, Walz K, Young JI.; ''Transgenic complementation of MeCP2 deficiency: phenotypic rescue of Mecp2-null mice by isoform-specific transgenes.''; PubMed Europe PMC Scholia
  245. Goldfarb AN.; ''Megakaryocytic programming by a transcriptional regulatory loop: A circle connecting RUNX1, GATA-1, and P-TEFb.''; PubMed Europe PMC Scholia
  246. Moretti PA, Davidson AJ, Baker E, Lilley B, Zon LI, D'Andrea RJ.; ''Molecular cloning of a human Vent-like homeobox gene.''; PubMed Europe PMC Scholia
  247. Drissi H, Luc Q, Shakoori R, Chuva De Sousa Lopes S, Choi JY, Terry A, Hu M, Jones S, Neil JC, Lian JB, Stein JL, Van Wijnen AJ, Stein GS.; ''Transcriptional autoregulation of the bone related CBFA1/RUNX2 gene.''; PubMed Europe PMC Scholia
  248. Kriaucionis S, Bird A.; ''The major form of MeCP2 has a novel N-terminus generated by alternative splicing.''; PubMed Europe PMC Scholia
  249. Freedman LP.; ''Multimeric Coactivator Complexes for Steroid/Nuclear Receptors.''; PubMed Europe PMC Scholia
  250. Sato M, Morii E, Komori T, Kawahata H, Sugimoto M, Terai K, Shimizu H, Yasui T, Ogihara H, Yasui N, Ochi T, Kitamura Y, Ito Y, Nomura S.; ''Transcriptional regulation of osteopontin gene in vivo by PEBP2alphaA/CBFA1 and ETS1 in the skeletal tissues.''; PubMed Europe PMC Scholia
  251. Li H, Zhong X, Chau KF, Santistevan NJ, Guo W, Kong G, Li X, Kadakia M, Masliah J, Chi J, Jin P, Zhang J, Zhao X, Chang Q.; ''Cell cycle-linked MeCP2 phosphorylation modulates adult neurogenesis involving the Notch signalling pathway.''; PubMed Europe PMC Scholia
  252. Oswald F, Kostezka U, Astrahantseff K, Bourteele S, Dillinger K, Zechner U, Ludwig L, Wilda M, Hameister H, Knöchel W, Liptay S, Schmid RM.; ''SHARP is a novel component of the Notch/RBP-Jkappa signalling pathway.''; PubMed Europe PMC Scholia

History

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CompareRevisionActionTimeUserComment
117732view12:37, 22 May 2021EweitzModified title
114974view16:50, 25 January 2021ReactomeTeamReactome version 75
113418view11:49, 2 November 2020ReactomeTeamReactome version 74
112620view16:00, 9 October 2020ReactomeTeamReactome version 73
101536view11:40, 1 November 2018ReactomeTeamreactome version 66
101071view21:22, 31 October 2018ReactomeTeamreactome version 65
100601view19:57, 31 October 2018ReactomeTeamreactome version 64
100152view16:42, 31 October 2018ReactomeTeamreactome version 63
99702view15:10, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
93811view13:37, 16 August 2017ReactomeTeamreactome version 61
93353view11:21, 9 August 2017ReactomeTeamreactome version 61
87152view18:57, 18 July 2016MkutmonOntology Term : 'transcription pathway' added !
86437view09:18, 11 July 2016ReactomeTeamreactome version 56
83195view10:19, 18 November 2015ReactomeTeamVersion54
81569view13:06, 21 August 2015ReactomeTeamVersion53
77033view08:33, 17 July 2014ReactomeTeamFixed remaining interactions
76738view12:10, 16 July 2014ReactomeTeamFixed remaining interactions
76063view10:12, 11 June 2014ReactomeTeamRe-fixing comment source
75773view11:28, 10 June 2014ReactomeTeamReactome 48 Update
75123view14:07, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74770view08:51, 30 April 2014ReactomeTeamReactome46
42045view21:52, 4 March 2011MaintBotAutomatic update
39848view05:52, 21 January 2011MaintBotNew pathway

External references

DataNodes

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NameTypeDatabase referenceComment
AR ProteinP10275 (Uniprot-TrEMBL)
ARC coactivator complexComplexR-HSA-212374 (Reactome) Summary: ARC co-activator complex and assembly The ARC coactivator complex is a subset of 19 proteins from the set of at least 31 Mediator proteins that, in different combinations, form "Adapter" complexes (Figure 1). Adapter complexes bridge between the basal transcription factors (including Pol II) and tisue-specific transcrption factors (TFs) bound to sites within upstream Proximal Promoter regions or distal Enhancer regions (reviewed in Maston, 2006 and Naar, 2001). The ARC complex contains the 15 components present in the DRIP complex, as well as 4 additional components (Rachez, 1999), These ARC-specific components are now called: MED8, MED15, MED25, and MED 26 in the unified nomenclature scheme (Bourbon, 2004). The 15 ARC complex components that are shared with the DRIP complex components, are also shared with the TRAP coactivator complex. However, the TRAP complex also has 4 additional, distinct components (Bourbon, 2004), which are now called: MED20, MED27, MED30, and MED 31 in the unified nomenclature scheme. The ARC complex was originally identified and named as a co-activator complex associated with transcription activator proteins (reviewed in Malik, 2005 and references therein). It was subsequently determined that all of the components of the DRIP complex are also in the ARC complex, and in the TRAP complex. In addition, these various transcription co-activator proteins identified in mammalian cells were found to be the orthologues or homologues of the Mediator complex proteins in yeast, first identified by Kornberg and colleagues (Kelleher, 1990). The unified nomenclature system for these adapter / co-activator proteins now labels them Mediator 1 through Mediator 31 (Bourbon, 2004). The order of addition of the ARC proteins during complex assembly is not fully determined, and may vary in different cell contexts. Therefore, ARC complex assembly is represented as a single reaction, in which all 19 components assemble simultaneously into the ARC co-activator complex.
CBPComplexR-HSA-212328 (Reactome)
CCNC ProteinP24863 (Uniprot-TrEMBL)
CCNCProteinP24863 (Uniprot-TrEMBL)
CDK8 ProteinP49336 (Uniprot-TrEMBL)
CDK8ProteinP49336 (Uniprot-TrEMBL)
CREBBP ProteinQ92793 (Uniprot-TrEMBL)
CSL NICD coactivator complexComplexR-HSA-212451 (Reactome)
DRIP coactivator complexComplexR-HSA-212340 (Reactome)
ESR1 ProteinP03372 (Uniprot-TrEMBL)
ESR2 ProteinQ92731 (Uniprot-TrEMBL)
ESRRA ProteinP11474 (Uniprot-TrEMBL)
ESRRB ProteinO95718 (Uniprot-TrEMBL)
ESRRG ProteinP62508 (Uniprot-TrEMBL)
HKR1 ProteinP10072 (Uniprot-TrEMBL)
HNF4A ProteinP41235 (Uniprot-TrEMBL)
HNF4G ProteinQ14541 (Uniprot-TrEMBL)
KAP (KRAB-Domain Associated Protein)ComplexR-HSA-975006 (Reactome)
KAT2A ProteinQ92830 (Uniprot-TrEMBL)
KAT2B ProteinQ92831 (Uniprot-TrEMBL)
KRAB-ZNF / KAP ComplexComplexR-HSA-975037 (Reactome)
KRAB-ZNFComplexR-HSA-974995 (Reactome)
KRBA1 ProteinA5PL33 (Uniprot-TrEMBL)
KRBOX4 ProteinQ5JUW0 (Uniprot-TrEMBL)
MAML1 ProteinQ92585 (Uniprot-TrEMBL)
MAML2 ProteinQ8IZL2 (Uniprot-TrEMBL)
MAML3 ProteinQ96JK9 (Uniprot-TrEMBL)
MAMLD1 ProteinQ13495 (Uniprot-TrEMBL)
MAMLComplexR-HSA-212357 (Reactome)
MED1 ProteinQ15648 (Uniprot-TrEMBL) MED1 is a component of each of the various Mediator complexes, that function as transcription co-activators. The MED1-containing compolexes include the DRIP, ARC, TRIP and CRSP compllexes.
MED10 ProteinQ9BTT4 (Uniprot-TrEMBL)
MED10ProteinQ9BTT4 (Uniprot-TrEMBL)
MED12 ProteinQ93074 (Uniprot-TrEMBL)
MED12ProteinQ93074 (Uniprot-TrEMBL)
MED13 ProteinQ9UHV7 (Uniprot-TrEMBL)
MED13ProteinQ9UHV7 (Uniprot-TrEMBL)
MED14 ProteinO60244 (Uniprot-TrEMBL)
MED14ProteinO60244 (Uniprot-TrEMBL)
MED15 ProteinQ96RN5 (Uniprot-TrEMBL)
MED15ProteinQ96RN5 (Uniprot-TrEMBL)
MED16 ProteinQ9Y2X0 (Uniprot-TrEMBL)
MED16ProteinQ9Y2X0 (Uniprot-TrEMBL)
MED17 ProteinQ9NVC6 (Uniprot-TrEMBL)
MED17ProteinQ9NVC6 (Uniprot-TrEMBL)
MED1ProteinQ15648 (Uniprot-TrEMBL) MED1 is a component of each of the various Mediator complexes, that function as transcription co-activators. The MED1-containing compolexes include the DRIP, ARC, TRIP and CRSP compllexes.
MED20 ProteinQ9H944 (Uniprot-TrEMBL)
MED20ProteinQ9H944 (Uniprot-TrEMBL)
MED23 ProteinQ9ULK4 (Uniprot-TrEMBL)
MED23ProteinQ9ULK4 (Uniprot-TrEMBL)
MED24 ProteinO75448 (Uniprot-TrEMBL)
MED24ProteinO75448 (Uniprot-TrEMBL)
MED25 ProteinQ71SY5 (Uniprot-TrEMBL)
MED25ProteinQ71SY5 (Uniprot-TrEMBL)
MED26 ProteinO95402 (Uniprot-TrEMBL)
MED26ProteinO95402 (Uniprot-TrEMBL)
MED27 ProteinQ6P2C8 (Uniprot-TrEMBL)
MED27ProteinQ6P2C8 (Uniprot-TrEMBL)
MED30 ProteinQ96HR3 (Uniprot-TrEMBL)
MED30ProteinQ96HR3 (Uniprot-TrEMBL)
MED31 ProteinQ9Y3C7 (Uniprot-TrEMBL)
MED31ProteinQ9Y3C7 (Uniprot-TrEMBL)
MED4 ProteinQ9NPJ6 (Uniprot-TrEMBL)
MED4ProteinQ9NPJ6 (Uniprot-TrEMBL)
MED6 ProteinO75586 (Uniprot-TrEMBL)
MED6ProteinO75586 (Uniprot-TrEMBL)
MED7 ProteinO43513 (Uniprot-TrEMBL)
MED7ProteinO43513 (Uniprot-TrEMBL)
MED8 ProteinQ96G25 (Uniprot-TrEMBL)
MED8ProteinQ96G25 (Uniprot-TrEMBL)
NICD1 ProteinP46531 (Uniprot-TrEMBL)
NICD2 ProteinQ04721 (Uniprot-TrEMBL)
NICD3 ProteinQ9UM47 (Uniprot-TrEMBL)
NICD4 ProteinQ99466 (Uniprot-TrEMBL)
NICDComplexR-HSA-212420 (Reactome)
NR-MED1 Coactivator ComplexComplexR-HSA-376420 (Reactome)
NR0B1-1 ProteinP51843-1 (Uniprot-TrEMBL)
NR0B1-2 ProteinP51843-2 (Uniprot-TrEMBL)
NR0B2 ProteinQ15466 (Uniprot-TrEMBL)
NR1D1 ProteinP20393 (Uniprot-TrEMBL)
NR1D2 ProteinQ14995 (Uniprot-TrEMBL)
NR1H2 ProteinP55055 (Uniprot-TrEMBL)
NR1H3-1 ProteinQ13133-1 (Uniprot-TrEMBL)
NR1H3-2 ProteinQ13133-2 (Uniprot-TrEMBL)
NR1H4-1 ProteinQ96RI1-1 (Uniprot-TrEMBL)
NR1H4-2 ProteinQ96RI1-2 (Uniprot-TrEMBL)
NR1H4-3 ProteinQ96RI1-3 (Uniprot-TrEMBL)
NR1H4-4 ProteinQ96RI1-4 (Uniprot-TrEMBL)
NR1I2-1 ProteinO75469-1 (Uniprot-TrEMBL)
NR1I2-2 ProteinO75469-2 (Uniprot-TrEMBL)
NR1I2-3 ProteinO75469-3 (Uniprot-TrEMBL)
NR1I2-4 ProteinO75469-4 (Uniprot-TrEMBL)
NR1I2-5 ProteinO75469-5 (Uniprot-TrEMBL)
NR1I2-6 ProteinO75469-6 (Uniprot-TrEMBL)
NR1I2-7 ProteinO75469-7 (Uniprot-TrEMBL)
NR1I3-1 ProteinQ14994-1 (Uniprot-TrEMBL)
NR1I3-2 ProteinQ14994-2 (Uniprot-TrEMBL)
NR2C1 ProteinP13056 (Uniprot-TrEMBL)
NR2C2 ProteinP49116 (Uniprot-TrEMBL)
NR2C2AP ProteinQ86WQ0 (Uniprot-TrEMBL)
NR2E1 ProteinQ9Y466 (Uniprot-TrEMBL)
NR2E3-1 ProteinQ9Y5X4-1 (Uniprot-TrEMBL)
NR2E3-2 ProteinQ9Y5X4-2 (Uniprot-TrEMBL)
NR2F1 ProteinP10589 (Uniprot-TrEMBL)
NR2F6 ProteinP10588 (Uniprot-TrEMBL)
NR3C1-1 ProteinP04150-1 (Uniprot-TrEMBL)
NR3C1-2 ProteinP04150-2 (Uniprot-TrEMBL)
NR3C1-3 ProteinP04150-3 (Uniprot-TrEMBL)
NR3C1-4 ProteinP04150-4 (Uniprot-TrEMBL)
NR3C1-5 ProteinP04150-5 (Uniprot-TrEMBL)
NR3C1-6 ProteinP04150-6 (Uniprot-TrEMBL)
NR3C1-7 ProteinP04150-7 (Uniprot-TrEMBL)
NR3C1-8 ProteinP04150-8 (Uniprot-TrEMBL)
NR3C1-9 ProteinP04150-9 (Uniprot-TrEMBL)
NR3C2-1 ProteinP08235-1 (Uniprot-TrEMBL)
NR3C2-2 ProteinP08235-2 (Uniprot-TrEMBL)
NR3C2-3 ProteinP08235-3 (Uniprot-TrEMBL)
NR3C2-4 ProteinP08235-4 (Uniprot-TrEMBL)
NR4A1 ProteinP22736 (Uniprot-TrEMBL)
NR4A2 ProteinP43354 (Uniprot-TrEMBL)
NR4A3-1 ProteinQ92570-1 (Uniprot-TrEMBL)
NR4A3-2 ProteinQ92570-2 (Uniprot-TrEMBL)
NR5A1 ProteinQ13285 (Uniprot-TrEMBL)
NR5A2-1 ProteinO00482-1 (Uniprot-TrEMBL)
NR5A2-2 ProteinO00482-2 (Uniprot-TrEMBL)
NR5A2-3 ProteinO00482-3 (Uniprot-TrEMBL)
NR6A1-1 ProteinQ15406-1 (Uniprot-TrEMBL)
NR6A1-2 ProteinQ15406-2 (Uniprot-TrEMBL)
NR6A1-3 ProteinQ15406-3 (Uniprot-TrEMBL)
NR6A1-4 ProteinQ15406-4 (Uniprot-TrEMBL)
NR6A1-5 ProteinQ15406-5 (Uniprot-TrEMBL)
NRBF2-1 ProteinQ96F24-1 (Uniprot-TrEMBL)
NRBF2-2 ProteinQ96F24-2 (Uniprot-TrEMBL)
NRBP1 ProteinQ9UHY1 (Uniprot-TrEMBL)
NRComplexR-HSA-376224 (Reactome) The proteins listed here have been divided into two groups based on the amount of data from direct experimental assy or detailed sequence analysis that is available to assign a receptor function to each. Those backed by more evidence have "member" status; ones backed by less have "candidate" status.
PCAFComplexR-HSA-350078 (Reactome)
PGR ProteinP06401 (Uniprot-TrEMBL)
PGR-2 ProteinP06401-2 (Uniprot-TrEMBL)
PPARA ProteinQ07869 (Uniprot-TrEMBL)
PPARD ProteinQ03181 (Uniprot-TrEMBL)
PPARG ProteinP37231 (Uniprot-TrEMBL)
PRDM7 ProteinQ9NQW5 (Uniprot-TrEMBL)
RARA ProteinP10276 (Uniprot-TrEMBL)
RARB ProteinP10826 (Uniprot-TrEMBL)
RARG ProteinP13631 (Uniprot-TrEMBL)
RBPJ ProteinQ06330 (Uniprot-TrEMBL)
RBPJProteinQ06330 (Uniprot-TrEMBL)
RORA ProteinP35398 (Uniprot-TrEMBL)
RORB ProteinQ92753 (Uniprot-TrEMBL)
RORC ProteinP51449 (Uniprot-TrEMBL)
RXRA ProteinP19793 (Uniprot-TrEMBL)
RXRB ProteinP28702 (Uniprot-TrEMBL)
RXRG ProteinP48443 (Uniprot-TrEMBL)
SNW1 ProteinQ13573 (Uniprot-TrEMBL)
SNWComplexR-HSA-212438 (Reactome)
THRA ProteinP10827 (Uniprot-TrEMBL)
THRB ProteinP10828 (Uniprot-TrEMBL)
TRAP coactivator complexComplexR-HSA-212379 (Reactome) DRIP co-activator complex and assembly

The DRIP co-activator complex is a subset of 14 proteins from the set of at least 31 Mediator proteins that, in different combinations, form "Adapter" complexes. Adapter complexes bridge between the basal transcription factors (including Pol II) and tissue-specific transcription factors (TFs) bound to sites within upstream Proximal Promoter regions or distal Enhancer regions (reviewed in Maston, 2006 and Naar, 2001).

The DRIP complex was originally identified and named as a co-activator complex associated with the Vitamin D Receptor member of the nuclear receptor family of transcription factors (Rachez, 1998). It was later determined that all of the components of the DRIP complex were also in the TRAP complex, and the ARC complex.

The DRIP complex contains the following 14 proteins, which also are common to the ARC and TRAP complexes: MED1, MED4, MED6, MED7, MED10, MED12, MED13, MED14, MED16, MED17, MED23, MED24, CDK8, CycC.

All of the DRIP adapter complex components are present in the ARC adapter complex, but the ARC complex also has 4 additional components (Rachez, 1999). These ARC-specific components are now called: MED8, MED15, MED25, and MED 26 in the unified nomenclature scheme (Bourbon, 2004).

Similarly, all 14 of the DRIP adapter complex components are present in the TRAP adapter complex, but the TRAP complex also has 4 additional components (Bourbon, 2004), These TRAP-specific components are now called: MED20, MED27, MED30, and MED 31 in the unified nomenclature scheme.

In addition, these various transcription co-activator proteins identified in mammalian cells were found to be the orthologues or homologues of the Mediator complex identified in yeast, first identified by Kornberg and colleagues (Kelleher, 1990).

TRIM28 ProteinQ13263 (Uniprot-TrEMBL)
Transcriptional Regulation by TP53PathwayR-HSA-3700989 (Reactome) TP53 regulates transcription of a number of genes involved in cellular metabolism, survival, senescence and DNA damage response. For a recent review, please refer to Vousden and Prives 2009.
Transcriptional

activity of SMAD2/SMAD3:SMAD4

heterotrimer		PathwayR-HSA-2173793 (Reactome) In the nucleus, SMAD2/3:SMAD4 heterotrimer complex acts as a transcriptional regulator. The activity of SMAD2/3 complex is regulated both positively and negatively by association with other transcription factors (Chen et al. 2002, Varelas et al. 2008, Stroschein et al. 1999, Wotton et al. 1999). In addition, the activity of SMAD2/3:SMAD4 complex can be inhibited by nuclear protein phosphatases and ubiquitin ligases (Lin et al. 2006, Dupont et al. 2009).
VDR ProteinP11473 (Uniprot-TrEMBL)
YAP1- and WWTR1

(TAZ)-stimulated

gene expression		PathwayR-HSA-2032785 (Reactome) YAP1 and WWTR1 (TAZ) are transcriptional co-activators, both homologues of the Drosophila Yorkie protein. They both interact with members of the TEAD family of transcription factors, and WWTR1 interacts as well with TBX5 and RUNX2, to promote gene expression. Their transcriptional targets include genes critical to regulation of cell proliferation and apoptosis. Their subcellular location is regulated by the Hippo signaling cascade: phosphorylation mediated by this cascade leads to the cytosolic sequestration of both proteins (Murakami et al. 2005; Oh and Irvine 2010).
ZFP1 ProteinQ6P2D0 (Uniprot-TrEMBL)
ZFP14 ProteinQ9HCL3 (Uniprot-TrEMBL)
ZFP2 ProteinQ6ZN57 (Uniprot-TrEMBL)
ZFP28 ProteinQ8NHY6 (Uniprot-TrEMBL)
ZFP30 ProteinQ9Y2G7 (Uniprot-TrEMBL)
ZFP37 ProteinQ9Y6Q3 (Uniprot-TrEMBL)
ZFP69 ProteinQ49AA0 (Uniprot-TrEMBL)
ZFP69B ProteinQ9UJL9 (Uniprot-TrEMBL)
ZFP90 ProteinQ8TF47 (Uniprot-TrEMBL)
ZIK1 ProteinQ3SY52 (Uniprot-TrEMBL)
ZIM2 ProteinQ9NZV7 (Uniprot-TrEMBL)
ZIM3 ProteinQ96PE6 (Uniprot-TrEMBL)
ZKSCAN1 ProteinP17029 (Uniprot-TrEMBL)
ZKSCAN3 ProteinQ9BRR0 (Uniprot-TrEMBL)
ZKSCAN4 ProteinQ969J2 (Uniprot-TrEMBL)
ZKSCAN5 ProteinQ9Y2L8 (Uniprot-TrEMBL)
ZKSCAN7 ProteinQ9P0L1 (Uniprot-TrEMBL)
ZKSCAN8 ProteinQ15776 (Uniprot-TrEMBL)
ZNF10 ProteinP21506 (Uniprot-TrEMBL)
ZNF100 ProteinQ8IYN0 (Uniprot-TrEMBL)
ZNF101 ProteinQ8IZC7 (Uniprot-TrEMBL)
ZNF112 ProteinQ9UJU3 (Uniprot-TrEMBL)
ZNF114 ProteinQ8NC26 (Uniprot-TrEMBL)
ZNF12(1-501) ProteinP17014 (Uniprot-TrEMBL)
ZNF124 ProteinQ15973 (Uniprot-TrEMBL)
ZNF133 ProteinP52736 (Uniprot-TrEMBL)
ZNF135 ProteinP52742 (Uniprot-TrEMBL)
ZNF136 ProteinP52737 (Uniprot-TrEMBL)
ZNF138 ProteinP52744 (Uniprot-TrEMBL)
ZNF14 ProteinP17017 (Uniprot-TrEMBL)
ZNF140 ProteinP52738 (Uniprot-TrEMBL)
ZNF141 ProteinQ15928 (Uniprot-TrEMBL)
ZNF154 ProteinQ13106 (Uniprot-TrEMBL)
ZNF155 ProteinQ12901 (Uniprot-TrEMBL)
ZNF157 ProteinP51786 (Uniprot-TrEMBL)
ZNF160 ProteinQ9HCG1 (Uniprot-TrEMBL)
ZNF169 ProteinQ14929 (Uniprot-TrEMBL)
ZNF17 ProteinP17021 (Uniprot-TrEMBL)
ZNF175 ProteinQ9Y473 (Uniprot-TrEMBL)
ZNF18 ProteinP17022 (Uniprot-TrEMBL)
ZNF180 ProteinQ9UJW8 (Uniprot-TrEMBL)
ZNF184 ProteinQ99676 (Uniprot-TrEMBL)
ZNF189 ProteinO75820 (Uniprot-TrEMBL)
ZNF19 ProteinP17023 (Uniprot-TrEMBL)
ZNF195 ProteinO14628 (Uniprot-TrEMBL)
ZNF197 ProteinO14709 (Uniprot-TrEMBL)
ZNF2 ProteinQ9BSG1 (Uniprot-TrEMBL)
ZNF20 ProteinP17024 (Uniprot-TrEMBL)
ZNF200 ProteinP98182 (Uniprot-TrEMBL)
ZNF202 ProteinO95125 (Uniprot-TrEMBL)
ZNF205 ProteinO95201 (Uniprot-TrEMBL)
ZNF208 ProteinO43345 (Uniprot-TrEMBL)
ZNF211 ProteinQ13398 (Uniprot-TrEMBL)
ZNF212 ProteinQ9UDV6 (Uniprot-TrEMBL)
ZNF213 ProteinO14771 (Uniprot-TrEMBL)
ZNF214 ProteinQ9UL59 (Uniprot-TrEMBL)
ZNF215 ProteinQ9UL58 (Uniprot-TrEMBL)
ZNF221 ProteinQ9UK13 (Uniprot-TrEMBL)
ZNF222 ProteinQ9UK12 (Uniprot-TrEMBL)
ZNF223 ProteinQ9UK11 (Uniprot-TrEMBL)
ZNF224 ProteinQ9NZL3 (Uniprot-TrEMBL)
ZNF225 ProteinQ9UK10 (Uniprot-TrEMBL)
ZNF226 ProteinQ9NYT6 (Uniprot-TrEMBL)
ZNF227 ProteinQ86WZ6 (Uniprot-TrEMBL)
ZNF23 ProteinP17027 (Uniprot-TrEMBL)
ZNF230 ProteinQ9UIE0 (Uniprot-TrEMBL)
ZNF233 ProteinA6NK53 (Uniprot-TrEMBL)
ZNF234 ProteinQ14588 (Uniprot-TrEMBL)
ZNF235 ProteinQ14590 (Uniprot-TrEMBL)
ZNF248 ProteinQ8NDW4 (Uniprot-TrEMBL)
ZNF25 ProteinP17030 (Uniprot-TrEMBL)
ZNF250 ProteinP15622 (Uniprot-TrEMBL)
ZNF253 ProteinO75346 (Uniprot-TrEMBL)
ZNF254 ProteinO75437 (Uniprot-TrEMBL)
ZNF256 ProteinQ9Y2P7 (Uniprot-TrEMBL)
ZNF257(1-535) ProteinQ9Y2Q1 (Uniprot-TrEMBL)
ZNF26 ProteinP17031 (Uniprot-TrEMBL)
ZNF263 ProteinO14978 (Uniprot-TrEMBL)
ZNF264 ProteinO43296 (Uniprot-TrEMBL)
ZNF266 ProteinQ14584 (Uniprot-TrEMBL)
ZNF267 ProteinQ14586 (Uniprot-TrEMBL)
ZNF268 ProteinQ14587 (Uniprot-TrEMBL)
ZNF273 ProteinQ14593 (Uniprot-TrEMBL)
ZNF274 ProteinQ96GC6 (Uniprot-TrEMBL)
ZNF28 ProteinP17035 (Uniprot-TrEMBL)
ZNF282 ProteinQ9UDV7 (Uniprot-TrEMBL)
ZNF285 ProteinQ96NJ3 (Uniprot-TrEMBL)
ZNF286A ProteinQ9HBT8 (Uniprot-TrEMBL)
ZNF287 ProteinQ9HBT7 (Uniprot-TrEMBL)
ZNF3 ProteinP17036 (Uniprot-TrEMBL)
ZNF30 ProteinP17039 (Uniprot-TrEMBL)
ZNF300 ProteinQ96RE9 (Uniprot-TrEMBL)
ZNF302 ProteinQ9NR11 (Uniprot-TrEMBL)
ZNF304 ProteinQ9HCX3 (Uniprot-TrEMBL)
ZNF311 ProteinQ5JNZ3 (Uniprot-TrEMBL)
ZNF317 ProteinQ96PQ6 (Uniprot-TrEMBL)
ZNF320 ProteinA2RRD8 (Uniprot-TrEMBL)
ZNF324 ProteinO75467 (Uniprot-TrEMBL)
ZNF324B ProteinQ6AW86 (Uniprot-TrEMBL)
ZNF331 ProteinQ9NQX6 (Uniprot-TrEMBL)
ZNF333 ProteinQ96JL9 (Uniprot-TrEMBL)
ZNF334 ProteinQ9HCZ1 (Uniprot-TrEMBL)
ZNF337 ProteinQ9Y3M9 (Uniprot-TrEMBL)
ZNF33A ProteinQ06730 (Uniprot-TrEMBL)
ZNF33B ProteinQ06732 (Uniprot-TrEMBL)
ZNF34 ProteinQ8IZ26 (Uniprot-TrEMBL)
ZNF343 ProteinQ6P1L6 (Uniprot-TrEMBL)
ZNF347 ProteinQ96SE7 (Uniprot-TrEMBL)
ZNF350 ProteinQ9GZX5 (Uniprot-TrEMBL)
ZNF354A ProteinO60765 (Uniprot-TrEMBL)
ZNF354B ProteinQ96LW1 (Uniprot-TrEMBL)
ZNF354C ProteinQ86Y25 (Uniprot-TrEMBL)
ZNF37A ProteinP17032 (Uniprot-TrEMBL)
ZNF382 ProteinQ96SR6 (Uniprot-TrEMBL)
ZNF383 ProteinQ8NA42 (Uniprot-TrEMBL)
ZNF394 ProteinQ53GI3 (Uniprot-TrEMBL)
ZNF398 ProteinQ8TD17 (Uniprot-TrEMBL)
ZNF41 ProteinP51814 (Uniprot-TrEMBL)
ZNF415 ProteinQ09FC8 (Uniprot-TrEMBL)
ZNF416 ProteinQ9BWM5 (Uniprot-TrEMBL)
ZNF417 ProteinQ8TAU3 (Uniprot-TrEMBL)
ZNF418 ProteinQ8TF45 (Uniprot-TrEMBL)
ZNF419 ProteinQ96HQ0 (Uniprot-TrEMBL)
ZNF420 ProteinQ8TAQ5 (Uniprot-TrEMBL)
ZNF425 ProteinQ6IV72 (Uniprot-TrEMBL)
ZNF426 ProteinQ9BUY5 (Uniprot-TrEMBL)
ZNF429 ProteinQ86V71 (Uniprot-TrEMBL)
ZNF43 ProteinP17038 (Uniprot-TrEMBL)
ZNF430 ProteinQ9H8G1 (Uniprot-TrEMBL)
ZNF431 ProteinQ8TF32 (Uniprot-TrEMBL)
ZNF432 ProteinO94892 (Uniprot-TrEMBL)
ZNF433 ProteinQ8N7K0 (Uniprot-TrEMBL)
ZNF436 ProteinQ9C0F3 (Uniprot-TrEMBL)
ZNF439 ProteinQ8NDP4 (Uniprot-TrEMBL)
ZNF440 ProteinQ8IYI8 (Uniprot-TrEMBL)
ZNF441 ProteinQ8N8Z8 (Uniprot-TrEMBL)
ZNF442 ProteinQ9H7R0 (Uniprot-TrEMBL)
ZNF443 ProteinQ9Y2A4 (Uniprot-TrEMBL)
ZNF445 ProteinP59923 (Uniprot-TrEMBL)
ZNF446 ProteinQ9NWS9 (Uniprot-TrEMBL)
ZNF45 ProteinQ02386 (Uniprot-TrEMBL)
ZNF454 ProteinQ8N9F8 (Uniprot-TrEMBL)
ZNF460 ProteinQ14592 (Uniprot-TrEMBL)
ZNF461 ProteinQ8TAF7 (Uniprot-TrEMBL)
ZNF468 ProteinQ5VIY5 (Uniprot-TrEMBL)
ZNF470 ProteinQ6ECI4 (Uniprot-TrEMBL)
ZNF471 ProteinQ9BX82 (Uniprot-TrEMBL)
ZNF473 ProteinQ8WTR7 (Uniprot-TrEMBL)
ZNF479 ProteinQ96JC4 (Uniprot-TrEMBL)
ZNF480 ProteinQ8WV37 (Uniprot-TrEMBL)
ZNF483 ProteinQ8TF39 (Uniprot-TrEMBL)
ZNF484 ProteinQ5JVG2 (Uniprot-TrEMBL)
ZNF485 ProteinQ8NCK3 (Uniprot-TrEMBL)
ZNF486 ProteinQ96H40 (Uniprot-TrEMBL)
ZNF490 ProteinQ9ULM2 (Uniprot-TrEMBL)
ZNF492 ProteinQ9P255 (Uniprot-TrEMBL)
ZNF493 ProteinQ6ZR52 (Uniprot-TrEMBL)
ZNF496 ProteinQ96IT1 (Uniprot-TrEMBL)
ZNF500 ProteinO60304 (Uniprot-TrEMBL)
ZNF506 ProteinQ5JVG8 (Uniprot-TrEMBL)
ZNF510 ProteinQ9Y2H8 (Uniprot-TrEMBL)
ZNF514 ProteinQ96K75 (Uniprot-TrEMBL)
ZNF517 ProteinQ6ZMY9 (Uniprot-TrEMBL)
ZNF519 ProteinQ8TB69 (Uniprot-TrEMBL)
ZNF528 ProteinQ3MIS6 (Uniprot-TrEMBL)
ZNF529 ProteinQ6P280 (Uniprot-TrEMBL)
ZNF530 ProteinQ6P9A1 (Uniprot-TrEMBL)
ZNF540 ProteinQ8NDQ6 (Uniprot-TrEMBL)
ZNF543 ProteinQ08ER8 (Uniprot-TrEMBL)
ZNF544 ProteinQ6NX49 (Uniprot-TrEMBL)
ZNF546 ProteinQ86UE3 (Uniprot-TrEMBL)
ZNF547 ProteinQ8IVP9 (Uniprot-TrEMBL)
ZNF548 ProteinQ8NEK5 (Uniprot-TrEMBL)
ZNF549 ProteinQ6P9A3 (Uniprot-TrEMBL)
ZNF550 ProteinQ7Z398 (Uniprot-TrEMBL)
ZNF551 ProteinQ7Z340 (Uniprot-TrEMBL)
ZNF552 ProteinQ9H707 (Uniprot-TrEMBL)
ZNF554 ProteinQ86TJ5 (Uniprot-TrEMBL)
ZNF555 ProteinQ8NEP9 (Uniprot-TrEMBL)
ZNF556 ProteinQ9HAH1 (Uniprot-TrEMBL)
ZNF557 ProteinQ8N988 (Uniprot-TrEMBL)
ZNF558 ProteinQ96NG5 (Uniprot-TrEMBL)
ZNF559 ProteinQ9BR84 (Uniprot-TrEMBL)
ZNF560 ProteinQ96MR9 (Uniprot-TrEMBL)
ZNF561 ProteinQ8N587 (Uniprot-TrEMBL)
ZNF562 ProteinQ6V9R5 (Uniprot-TrEMBL)
ZNF563 ProteinQ8TA94 (Uniprot-TrEMBL)
ZNF564 ProteinQ8TBZ8 (Uniprot-TrEMBL)
ZNF565 ProteinQ8N9K5 (Uniprot-TrEMBL)
ZNF566 ProteinQ969W8 (Uniprot-TrEMBL)
ZNF567 ProteinQ8N184 (Uniprot-TrEMBL)
ZNF568 ProteinQ3ZCX4 (Uniprot-TrEMBL)
ZNF569 ProteinQ5MCW4 (Uniprot-TrEMBL)
ZNF570 ProteinQ96NI8 (Uniprot-TrEMBL)
ZNF571 ProteinQ7Z3V5 (Uniprot-TrEMBL)
ZNF573 ProteinQ86YE8 (Uniprot-TrEMBL)
ZNF577 ProteinQ9BSK1 (Uniprot-TrEMBL)
ZNF582 ProteinQ96NG8 (Uniprot-TrEMBL)
ZNF583 ProteinQ96ND8 (Uniprot-TrEMBL)
ZNF584 ProteinQ8IVC4 (Uniprot-TrEMBL)
ZNF585A ProteinQ6P3V2 (Uniprot-TrEMBL)
ZNF585B ProteinQ52M93 (Uniprot-TrEMBL)
ZNF586 ProteinQ9NXT0 (Uniprot-TrEMBL)
ZNF587 ProteinQ96SQ5 (Uniprot-TrEMBL)
ZNF589 ProteinQ86UQ0 (Uniprot-TrEMBL)
ZNF595 ProteinQ8IYB9 (Uniprot-TrEMBL)
ZNF596 ProteinQ8TC21 (Uniprot-TrEMBL)
ZNF597 ProteinQ96LX8 (Uniprot-TrEMBL)
ZNF599 ProteinQ96NL3 (Uniprot-TrEMBL)
ZNF600 ProteinQ6ZNG1 (Uniprot-TrEMBL)
ZNF605 ProteinQ86T29 (Uniprot-TrEMBL)
ZNF606 ProteinQ8WXB4 (Uniprot-TrEMBL)
ZNF607 ProteinQ96SK3 (Uniprot-TrEMBL)
ZNF610 ProteinQ8N9Z0 (Uniprot-TrEMBL)
ZNF611 ProteinQ8N823 (Uniprot-TrEMBL)
ZNF613 ProteinQ6PF04 (Uniprot-TrEMBL)
ZNF614 ProteinQ8N883 (Uniprot-TrEMBL)
ZNF615 ProteinQ8N8J6 (Uniprot-TrEMBL)
ZNF616 ProteinQ08AN1 (Uniprot-TrEMBL)
ZNF619 ProteinQ8N2I2 (Uniprot-TrEMBL)
ZNF620 ProteinQ6ZNG0 (Uniprot-TrEMBL)
ZNF621 ProteinQ6ZSS3 (Uniprot-TrEMBL)
ZNF624 ProteinQ9P2J8 (Uniprot-TrEMBL)
ZNF625 ProteinQ96I27 (Uniprot-TrEMBL)
ZNF626 ProteinQ68DY1 (Uniprot-TrEMBL)
ZNF627 ProteinQ7L945 (Uniprot-TrEMBL)
ZNF641 ProteinQ96N77 (Uniprot-TrEMBL)
ZNF649 ProteinQ9BS31 (Uniprot-TrEMBL)
ZNF655 ProteinQ8N720 (Uniprot-TrEMBL)
ZNF658 ProteinQ5TYW1 (Uniprot-TrEMBL)
ZNF658B ProteinQ4V348 (Uniprot-TrEMBL)
ZNF660 ProteinQ6AZW8 (Uniprot-TrEMBL)
ZNF662 ProteinQ6ZS27 (Uniprot-TrEMBL)
ZNF664 ProteinQ8N3J9 (Uniprot-TrEMBL)
ZNF665 ProteinQ9H7R5 (Uniprot-TrEMBL)
ZNF667 ProteinQ5HYK9 (Uniprot-TrEMBL)
ZNF668 ProteinQ96K58 (Uniprot-TrEMBL)
ZNF669 ProteinQ96BR6 (Uniprot-TrEMBL)
ZNF670 ProteinQ9BS34 (Uniprot-TrEMBL)
ZNF671 ProteinQ8TAW3 (Uniprot-TrEMBL)
ZNF675 ProteinQ8TD23 (Uniprot-TrEMBL)
ZNF676 ProteinQ8N7Q3 (Uniprot-TrEMBL)
ZNF677 ProteinQ86XU0 (Uniprot-TrEMBL)
ZNF678 ProteinQ5SXM1 (Uniprot-TrEMBL)
ZNF679 ProteinQ8IYX0 (Uniprot-TrEMBL)
ZNF680 ProteinQ8NEM1 (Uniprot-TrEMBL)
ZNF681 ProteinQ96N22 (Uniprot-TrEMBL)
ZNF682 ProteinO95780 (Uniprot-TrEMBL)
ZNF684 ProteinQ5T5D7 (Uniprot-TrEMBL)
ZNF688 ProteinP0C7X2 (Uniprot-TrEMBL)
ZNF689 ProteinQ96CS4 (Uniprot-TrEMBL)
ZNF691 ProteinQ5VV52 (Uniprot-TrEMBL)
ZNF692 ProteinQ9BU19 (Uniprot-TrEMBL)
ZNF696 ProteinQ9H7X3 (Uniprot-TrEMBL)
ZNF697 ProteinQ5TEC3 (Uniprot-TrEMBL)
ZNF699 ProteinQ32M78 (Uniprot-TrEMBL)
ZNF70 ProteinQ9UC06 (Uniprot-TrEMBL)
ZNF700 ProteinQ9H0M5 (Uniprot-TrEMBL)
ZNF701 ProteinQ9NV72 (Uniprot-TrEMBL)
ZNF702P ProteinQ9H963 (Uniprot-TrEMBL)
ZNF703 ProteinQ9H7S9 (Uniprot-TrEMBL)
ZNF704 ProteinQ6ZNC4 (Uniprot-TrEMBL)
ZNF705A ProteinQ6ZN79 (Uniprot-TrEMBL)
ZNF705D ProteinP0CH99 (Uniprot-TrEMBL)
ZNF705E ProteinA8MWA4 (Uniprot-TrEMBL)
ZNF705F ProteinA8MVS1 (Uniprot-TrEMBL)
ZNF705G ProteinA8MUZ8 (Uniprot-TrEMBL)
ZNF706 ProteinQ9Y5V0 (Uniprot-TrEMBL)
ZNF707 ProteinQ96C28 (Uniprot-TrEMBL)
ZNF708 ProteinP17019 (Uniprot-TrEMBL)
ZNF709 ProteinQ8N972 (Uniprot-TrEMBL)
ZNF71 ProteinQ9NQZ8 (Uniprot-TrEMBL)
ZNF710 ProteinQ8N1W2 (Uniprot-TrEMBL)
ZNF711 ProteinQ9Y462 (Uniprot-TrEMBL)
ZNF713 ProteinQ8N859 (Uniprot-TrEMBL)
ZNF714 ProteinQ96N38 (Uniprot-TrEMBL)
ZNF716 ProteinA6NP11 (Uniprot-TrEMBL)
ZNF717 ProteinQ9BY31 (Uniprot-TrEMBL)
ZNF718 ProteinQ3SXZ3 (Uniprot-TrEMBL)
ZNF720 ProteinQ7Z2F6 (Uniprot-TrEMBL)
ZNF721 ProteinQ8TF20 (Uniprot-TrEMBL)
ZNF724P ProteinA8MTY0 (Uniprot-TrEMBL)
ZNF726 ProteinA6NNF4 (Uniprot-TrEMBL)
ZNF726P1 ProteinQ15940 (Uniprot-TrEMBL)
ZNF727 ProteinA8MUV8 (Uniprot-TrEMBL)
ZNF729 ProteinA6NN14 (Uniprot-TrEMBL)
ZNF730 ProteinQ6ZMV8 (Uniprot-TrEMBL)
ZNF732 ProteinB4DXR9 (Uniprot-TrEMBL)
ZNF735 ProteinP0CB33 (Uniprot-TrEMBL)
ZNF736 ProteinB4DX44 (Uniprot-TrEMBL)
ZNF737 ProteinO75373 (Uniprot-TrEMBL)
ZNF738 ProteinQ8NE65 (Uniprot-TrEMBL)
ZNF74 ProteinQ16587 (Uniprot-TrEMBL)
ZNF740 ProteinQ8NDX6 (Uniprot-TrEMBL)
ZNF746 ProteinQ6NUN9 (Uniprot-TrEMBL)
ZNF747 ProteinQ9BV97 (Uniprot-TrEMBL)
ZNF749 ProteinO43361 (Uniprot-TrEMBL)
ZNF750 ProteinQ32MQ0 (Uniprot-TrEMBL)
ZNF75A ProteinQ96N20 (Uniprot-TrEMBL)
ZNF75CP ProteinQ92670 (Uniprot-TrEMBL)
ZNF75D ProteinP51815 (Uniprot-TrEMBL)
ZNF761 ProteinQ86XN6 (Uniprot-TrEMBL)
ZNF764 ProteinQ96H86 (Uniprot-TrEMBL)
ZNF767 ProteinQ75MW2 (Uniprot-TrEMBL)
ZNF77 ProteinQ15935 (Uniprot-TrEMBL)
ZNF770 ProteinQ6IQ21 (Uniprot-TrEMBL)
ZNF771 ProteinQ7L3S4 (Uniprot-TrEMBL)
ZNF772 ProteinQ68DY9 (Uniprot-TrEMBL)
ZNF773 ProteinQ6PK81 (Uniprot-TrEMBL)
ZNF774 ProteinQ6NX45 (Uniprot-TrEMBL)
ZNF775 ProteinQ96BV0 (Uniprot-TrEMBL)
ZNF776 ProteinQ68DI1 (Uniprot-TrEMBL)
ZNF777 ProteinQ9ULD5 (Uniprot-TrEMBL)
ZNF778 ProteinQ96MU6 (Uniprot-TrEMBL)
ZNF782 ProteinQ6ZMW2 (Uniprot-TrEMBL)
ZNF785 ProteinA8K8V0 (Uniprot-TrEMBL)
ZNF786 ProteinQ8N393 (Uniprot-TrEMBL)
ZNF79 ProteinQ15937 (Uniprot-TrEMBL)
ZNF790 ProteinQ6PG37 (Uniprot-TrEMBL)
ZNF791 ProteinQ3KP31 (Uniprot-TrEMBL)
ZNF792 ProteinQ3KQV3 (Uniprot-TrEMBL)
ZNF793 ProteinQ6ZN11 (Uniprot-TrEMBL)
ZNF799 ProteinQ96GE5 (Uniprot-TrEMBL)
ZNF804B ProteinA4D1E1 (Uniprot-TrEMBL)
ZNF839 ProteinA8K0R7 (Uniprot-TrEMBL)
ZNF840 ProteinA6NDX5 (Uniprot-TrEMBL)
ZNF860 ProteinA6NHJ4 (Uniprot-TrEMBL)
ZNF92 ProteinQ03936 (Uniprot-TrEMBL)
ZNF99 ProteinA8MXY4 (Uniprot-TrEMBL)
ZSCAN25 ProteinQ6NSZ9 (Uniprot-TrEMBL)
ZSCAN32 ProteinQ9NX65 (Uniprot-TrEMBL)

Annotated Interactions

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SourceTargetTypeDatabase referenceComment
ARC coactivator complexArrowR-HSA-212352 (Reactome)
CBPR-HSA-212356 (Reactome)
CCNCR-HSA-212352 (Reactome)
CCNCR-HSA-212380 (Reactome)
CCNCR-HSA-212432 (Reactome)
CDK8R-HSA-212352 (Reactome)
CDK8R-HSA-212380 (Reactome)
CDK8R-HSA-212432 (Reactome)
CSL NICD coactivator complexArrowR-HSA-212356 (Reactome)
DRIP coactivator complexArrowR-HSA-212432 (Reactome)
KAP (KRAB-Domain Associated Protein)R-HSA-975040 (Reactome)
KRAB-ZNF / KAP ComplexArrowR-HSA-975040 (Reactome)
KRAB-ZNFR-HSA-975040 (Reactome)
MAMLR-HSA-212356 (Reactome)
MED10R-HSA-212352 (Reactome)
MED10R-HSA-212380 (Reactome)
MED10R-HSA-212432 (Reactome)
MED12R-HSA-212352 (Reactome)
MED12R-HSA-212380 (Reactome)
MED12R-HSA-212432 (Reactome)
MED13R-HSA-212352 (Reactome)
MED13R-HSA-212380 (Reactome)
MED13R-HSA-212432 (Reactome)
MED14R-HSA-212352 (Reactome)
MED14R-HSA-212380 (Reactome)
MED14R-HSA-212432 (Reactome)
MED15R-HSA-212352 (Reactome)
MED16R-HSA-212352 (Reactome)
MED16R-HSA-212380 (Reactome)
MED16R-HSA-212432 (Reactome)
MED17R-HSA-212352 (Reactome)
MED17R-HSA-212380 (Reactome)
MED17R-HSA-212432 (Reactome)
MED1R-HSA-212352 (Reactome)
MED1R-HSA-212380 (Reactome)
MED1R-HSA-212432 (Reactome)
MED1R-HSA-376419 (Reactome)
MED20R-HSA-212380 (Reactome)
MED23R-HSA-212352 (Reactome)
MED23R-HSA-212380 (Reactome)
MED23R-HSA-212432 (Reactome)
MED24R-HSA-212352 (Reactome)
MED24R-HSA-212380 (Reactome)
MED24R-HSA-212432 (Reactome)
MED25R-HSA-212352 (Reactome)
MED26R-HSA-212352 (Reactome)
MED27R-HSA-212380 (Reactome)
MED30R-HSA-212380 (Reactome)
MED31R-HSA-212380 (Reactome)
MED4R-HSA-212352 (Reactome)
MED4R-HSA-212380 (Reactome)
MED4R-HSA-212432 (Reactome)
MED6R-HSA-212352 (Reactome)
MED6R-HSA-212380 (Reactome)
MED6R-HSA-212432 (Reactome)
MED7R-HSA-212352 (Reactome)
MED7R-HSA-212380 (Reactome)
MED7R-HSA-212432 (Reactome)
MED8R-HSA-212352 (Reactome)
NICDR-HSA-212356 (Reactome)
NR-MED1 Coactivator ComplexArrowR-HSA-376419 (Reactome)
NRR-HSA-376419 (Reactome)
PCAFR-HSA-212356 (Reactome)
R-HSA-212352 (Reactome) ARC co-activator complex and assembly

The ARC co-activator complex is a subset of 18 proteins from the set of at least 31 Mediator proteins that, in different combinations, form "Adapter" complexes in human cells. Adapter complexes bridge between the basal transcription factors (including Pol II) and tissue-specific transcription factors (TFs) bound to sites within upstream Proximal Promoter regions or distal Enhancer regions (reviewed in Maston, 2006 and Naar, 2001).

The ARC complex was originally identified and named as a co-activator complex associated with transcription activator proteins (reviewed in Malik, 2005 and references therein). It was subsequently determined that many of the components of the ARC complex are also in the DRIP complex, and in the TRAP complex..

The ARC complex contains the following 14 proteins, which also are common to the DRIP and TRAP complexes: MED1, MED4, MED6, MED7, MED10, MED12, MED13, MED14, MED16, MED17, MED23, MED24, CDK8, CycC.

The ARC complex also contains 4 additional, ARC-specific components, which are now called: MED8, MED15, MED25, and MED 26 in the unified nomenclature scheme (Bourbon, 2004).

In addition, these various transcription co-activator proteins identified in mammalian cells were found to be the orthologues or homologues of the Mediator complex proteins in yeast, first identified by Kornberg and colleagues (Kelleher, 1990). The unified nomenclature system for these adapter / co-activator proteins now labels them Mediator 1 through Mediator 31 (Bourbon, 2004).

The order of addition of the ARC proteins during complex assembly is not fully determined, and may vary in different cell contexts. Therefore, ARC complex assembly is represented as a single reaction event, in which all 19 components assemble simultaneously into the ARC co-activator complex.


R-HSA-212356 (Reactome) Mammalian CSL Coactivator Complexes: Upon activation of Notch signaling, cleavage of the transmembrane Notch receptor releases the Notch Intracellular Domain (NICD), which translocates to the nucleus, where it binds to CSL and displaces the corepressor complex from CSL (reviewed in Mumm, 2000 and Kovall, 2007). The resulting CSL-NICD "binary complex" then recruits an additional coactivator, Mastermind (Mam), to form a ternary complex. The ternary complex then recruits additional, more general coactivators, such as CREB Binding Protein (CBP), or the related p300 coactivator, and a number of Histone Acetytransferase (HAT) proteins, including GCN5 and PCAF (Fryer, 2002). There is evidence that Mam also can subsequently recruit specific kinases that phosphorylate NICD, to downregulate its function and turn off Notch signaling (Fryer, 2004).
R-HSA-212380 (Reactome) TRAP co-activator complex and assembly

The TRAP co-activator complex is a subset of 18 proteins from the set of at least 31 Mediator proteins that, in different combinations and in different contexts, form specific co-activator or "Adapter" complexes in human cells. These complexes bridge between the basal transcription factors (including Pol II) and tissue-specific transcription factors (TFs) bound to sites within upstream Proximal Promoter regions or distal Enhancer regions (reviewed in Maston, 2006 and Naar, 2001).

The TRAP complex was originally identified and named as a co-activator complex associated with the Thyroid Hormone Receptor member of the nuclear receptor family of transcription factors (Yuan, 1998). It was later determined that many of the components of the TRAP complex are also in the DRIP complex, and in the ARC complex.

The TRAP complex contains the following 14 proteins, which also are common to the DRIP and ARC complexes: MED1, MED4, MED6, MED7, MED10, MED12, MED13, MED14, MED16, MED17, MED23, MED24, CDK8, CycC.

The TRAP complex also contains 4 additional components, which are now called: MED20, MED27, MED30, and MED 31 in the unified nomenclature scheme (Bourbon, 2004).

In addition, these various transcription co-activator proteins identified in mammalian cells were found to be the orthologues or homologues of the Mediator complex proteins in yeast, first identified by Kornberg and colleagues (Kelleher, 1990). The unified nomenclature system for these adapter / co-activator proteins now labels them Mediator 1 through Mediator 31 (Bourbon, 2004).

The order of addition of the TRAP proteins during complex assembly is not fully determined, and may vary in different cell contexts. Therefore, TRAP co-activator complex assembly is represented as a single reaction event, in which all 18 components assemble simultaneously into the TRAP co-activator complex.


R-HSA-212432 (Reactome) DRIP co-activator complex and assembly

The DRIP co-activator complex is a subset of 14 proteins from the set of at least 31 Mediator proteins that, in different combinations, form "Adapter" complexes. Adapter complexes bridge between the basal transcription factors (including Pol II) and tissue-specific transcription factors (TFs) bound to sites within upstream Proximal Promoter regions or distal Enhancer regions (reviewed in Maston, 2006 and Naar, 2001).

The DRIP complex was originally identified and named as a co-activator complex associated with the Vitamin D Receptor member of the nuclear receptor family of transcription factors (Rachez, 1998). It was later determined that all of the components of the DRIP complex were also in the TRAP complex, and the ARC complex.

The DRIP complex contains the following 14 proteins, which also are common to the ARC and TRAP complexes: MED1, MED4, MED6, MED7, MED10, MED12, MED13, MED14, MED16, MED17, MED23, MED24, CDK8, CycC.

All of the DRIP adapter complex components are present in the ARC adapter complex, but the ARC complex also has 4 additional components (Rachez, 1999). These ARC-specific components are now called: MED8, MED15, MED25, and MED 26 in the unified nomenclature scheme (Bourbon, 2004).

Similarly, all 14 of the DRIP adapter complex components are present in the TRAP adapter complex, but the TRAP complex also has 4 additional components (Bourbon, 2004), These TRAP-specific components are now called: MED20, MED27, MED30, and MED 31 in the unified nomenclature scheme.

In addition, these various transcription co-activator proteins identified in mammalian cells were found to be the orthologues or homologues of the Mediator complex identified in yeast, first identified by Kornberg and colleagues (Kelleher, 1990).


R-HSA-376419 (Reactome) THE NUCLEAR RECEPTOR-MED1 REACTION: The Nuclear Receptor (NR) proteins are a highly conserved family of DNA-binding transcription factors that bind certain hormones, vitamins, and other small, diffusible signaling molecules. The non-liganded NRs recruit specific corepressor complexes of the NCOR/SMRT type, to mediate transcriptional repression of the target genes to which they are bound. During signaling, ligand binding to a specific domain in the NR proteins induces a conformational change that results in the exchange of the associated corepressor complex, and its replacement by a specific coactivator complex of either the TRAP/DRIP/Mediator type, or the p160/SRC type. The Mediator coactivator complexes typically nucleate around the MED1 coactivator protein, which is directly bound to the NR transcription factor (reviewed in Freedman, 1999; Malik, 2005).

A general feature of the NR proteins is that they each contain a specific protein interaction domain (PID), or domains, that mediates the specific binding interactions with the MED1 proteins. In the ligand-bound state, NRs each take part in an NR-MED1 binding reaction to form an NR-MED1 complex. The bound MED1 then functions to nucleate the assembly of additional specific coactivator proteins, depending on the cell and DNA context, such as what specific target gene promoter or enhancer they are bound to, and in what cell type.

The formation of specific MED1-containing coactivator complexes on specific NR proteins has been well-characterized for a number of the human NR proteins. For example, binding of Vitamin D to the human Vitamin D3 Receptor was found to result in the recruitment of a specific complex of D Receptor Interacting Proteins - the DRIP coactivator complex (Rachez, 1998). Within the DRIP complex, the DRIP205 subunit was later renamed human "MED1", based on sequence similarities with yeast MED1 (reviewed in Bourbon, 2004).

Similarly, binding of thyroid hormone (TH) to the human TH Receptor (THRA or THRB) was found to result in the recruitment of a specific complex of Thyroid Receptor Associated Proteins - the TRAP coactivator complex (Yuan, 1998). The TRAP220 subunit was later identified to be the Mediator 1 (MED1) homologue (summarized in Bourbon, et al., 2004; Table 1).

The 48 human NR proteins each contain the PID(s) known to mediate interaction with the human MED1 protein. Direct NR-MED1 protein-protein interactions have been shown for a number of the NR proteins. The MED1-interacting PIDs are conserved in all of the human NRs. Therefore, each of the human NRs is known or expected to interact with MED1 in the appropriate cell context, depending on the cell type, the cell state, and the target gene regulatory region involved.
R-HSA-975040 (Reactome)

Formation of the KRAB ZNF / KAP1 Corepressor Complex:

Transcription factors which contain tandem copies of the C2H2 zinc finger DNA binding motif (ZNFs) are the most abundant class of TFs in the human proteome, comprising more than 1000 members. The KRAB ZNF proteins are the largest subset of these (with 423 members) and are defined by having an additional conserved domain, the KRAB domain (Bellefroid,1991, Margolin, 1994, Urrutia, 2003, Huntley, 2006). The Kruppel Associated Box (KRAB) domain is a transcription repression domain (Margolin, 1994) which mediates the recruitment of a specific and dedicated co repressor protein for the KRAB-ZNF family - KAP1 - which is required for transcriptional repression and gene silencing (Friedman, 1996).

The larger family of ZNF transcription factors are present in almost all metazoans and generally their DNA binding specificities and transcription regulation functions are conserved from Drosophila to humans. Although the biological functions of most ZNF TFs is not known, they often function biochemically as sequence specific DNA binding proteins and can be activators, or more oftenly observed, repressors of transcription, depending on cellular context. Transcriptional repression is mediated via specific protein protein interaction surfaces in the ZNF that function as repression domains, by recruiting specific co repressors, such as KAP1 in humans (Friedman, 1996), and dCTBP in Drosophila (Nibu, 1998).

In contrast to the larger ZNF family, the KRAB-ZNFs only appear much later in vertebrate evolution: genes encoding the primordial KRAB ZNF subfamily first arose in tetrapods and the family has been greatly expanded in numbers and complexity in mammals. Interestingly,a large fraction of KRAB-ZNFs are found only in primates. In addition to their rapid and dynamic evolutionary history, comparative genomics and expression studies of primate KRAB-ZNFs suggest that these genes have played a significant role in shaping primate specific traits (Huntley, 2006, Nowick, 2009).

The biochemical pathway utilized by KRAB-ZNFs is well defined and probably nearly identical for each member: All KRAB-ZNF proteins which have been studied in detail are repressors and utilize the KRAB domain to bind the KAP1 co-repressor. This interaction is direct, of high affinity, and is obligate for the KRAB-ZNF to function as a repressor when bound to DNA in vivo (Peng, 2000a,b).. The KAP1co-repressor appears to function as a scaffold protein to assemble and coordinate multiple enzymes (histone de-acetylases, histone methyltransferases and heterochromatin proteins) which target and modify chromatin structure thus leading to a compacted, silent state (Lechner, 2000; Schultz, 2001 Schultz, 2002 , Ayyanathan, 2003). The post-translational modification of KAP1 by SUMO controls its ability to assemble the enzymatic apparatus in chromatin (Ivanov, 2007; Zeng, 2008). It is formally possible that some KRAB ZNF proteins may have additional functional domains that recruit coactivators in specific contexts, given that such bifunctionality is common for many classes of DNA binding transcription factors,. However, there is no experimental evidence for this yet.

There also is good evidence that the KRAB ZNF-KAP1 complex proteins can have long range gene silencing functions, by nucleating chromatin complexes that inactivate transcription of large numbers of genes over large distances by assembling silent heterochromatin (Ayyanathan, 2003). Although KAP1 was originally identified as a mediator of specific gene transcription repression, subsequent studies have shown that KAP1 also is involved in the recruitment of homologues of the HP1 protein family (Ryan, 1999, Ayyanathan, 2003; Lechner, 2000). These nonhistone heterochromatin associated proteins were first shown to have an epigenetic gene silencing function in Drosophila and more recently in mammalian cells . These studies suggest that KRAB ZNF proteins and KAP1 may also be involved in large scale chromatin regulation and gene silencing, not just in gene specific transcriptional repression. Whether this is a general property of most or all KRAB ZNF proteins will require additional studies.

Finally, several KRAB containing ZNFs in mammals also contain a conserved SCAN domain which, like the KRAB domain also functions as a protein protein interaction domain. (Edelstein, 2005, Peng, 2000a,b). The SCAN domain does not participate in KAP1 binding but rather functions to mediate homodimerization, or selective heterodimerization with other SCAN containing proteins. However, the biochemical and biological functions of the SCAN domain in KRAB-ZNF mediated repression are not known.

Remaining Questions: The single most important unanswered question for KRAB-ZNFDs is to determine their biological functions. While the mechanism utilized by the KRAB ZNF / KAP1 protein complex to mediate gene specific transcription repression is well understood , much less known about the specific biological pathways they control. Preliminary evidence from recent whole genome analysis of the target genes for the KRAB- ZNF263 protein suggest that it can have both positive and negative effects on transcriptional regulation of its target genes (Frietze, 2010). Presumably, each KRAB-ZNF, via its array of zinc fingers can bind to specific DNA recognition sequences in target promoters. This, combined with highly tissue specific expression of each gene, makes the potential transcriptome controlled by the 423 KRAB-ZNFs extremely large.


RBPJR-HSA-212356 (Reactome)
SNWR-HSA-212356 (Reactome)
TRAP coactivator complexArrowR-HSA-212380 (Reactome)
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