| Type |
Details |
Score |
| Publication |
| First Author: |
Brown JB |
| Year: |
2008 |
| Journal: |
Inflamm Bowel Dis |
| Title: |
Therapeutic benefit of pentostatin in severe IL-10-/- colitis. |
| Volume: |
14 |
| Issue: |
7 |
| Pages: |
880-7 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Blackburn MR |
| Year: |
2003 |
| Journal: |
J Clin Invest |
| Title: |
Adenosine mediates IL-13-induced inflammation and remodeling in the lung and interacts in an IL-13-adenosine amplification pathway. |
| Volume: |
112 |
| Issue: |
3 |
| Pages: |
332-44 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mohamedali KA |
| Year: |
1993 |
| Journal: |
J Biol Chem |
| Title: |
The highest levels of purine catabolic enzymes in mice are present in the proximal small intestine. |
| Volume: |
268 |
| Issue: |
31 |
| Pages: |
23728-33 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Orpinell M |
| Year: |
2010 |
| Journal: |
EMBO J |
| Title: |
The ATAC acetyl transferase complex controls mitotic progression by targeting non-histone substrates. |
| Volume: |
29 |
| Issue: |
14 |
| Pages: |
2381-94 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Apasov SG |
| Year: |
1999 |
| Journal: |
Int Immunol |
| Title: |
The extracellular versus intracellular mechanisms of inhibition of TCR-triggered activation in thymocytes by adenosine under conditions of inhibited adenosine deaminase. |
| Volume: |
11 |
| Issue: |
2 |
| Pages: |
179-89 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Stockinger EJ |
| Year: |
2001 |
| Journal: |
Nucleic Acids Res |
| Title: |
Transcriptional adaptor and histone acetyltransferase proteins in Arabidopsis and their interactions with CBF1, a transcriptional activator involved in cold-regulated gene expression. |
| Volume: |
29 |
| Issue: |
7 |
| Pages: |
1524-33 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Bieniasz PD |
| Year: |
1997 |
| Journal: |
EMBO J |
| Title: |
HIV-1-induced cell fusion is mediated by multiple regions within both the viral envelope and the CCR-5 co-receptor. |
| Volume: |
16 |
| Issue: |
10 |
| Pages: |
2599-609 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Maier EA |
| Year: |
2006 |
| Journal: |
J Biol Chem |
| Title: |
Temporal regulation of enhancer function in intestinal epithelium: a role for Onecut factors. |
| Volume: |
281 |
| Issue: |
43 |
| Pages: |
32263-71 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mistry D |
| Year: |
2006 |
| Journal: |
Osteoarthritis Cartilage |
| Title: |
The role of adenosine in chondrocyte death in murine osteoarthritis and in a murine chondrocyte cell line. |
| Volume: |
14 |
| Issue: |
5 |
| Pages: |
486-95 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Manalo JM |
| Year: |
2020 |
| Journal: |
FASEB J |
| Title: |
Adenosine A2B receptor: A pathogenic factor and a therapeutic target for sensorineural hearing loss. |
| Volume: |
34 |
| Issue: |
12 |
| Pages: |
15771-15787 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
473
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Strain |
| Attribute String: |
F1 hybrid, mutant stock |
|
•
•
•
•
•
|
| Strain |
| Attribute String: |
mutant stock |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Nascimento F |
| Year: |
2015 |
| Journal: |
Purinergic Signal |
| Title: |
Presymptomatic and symptomatic ALS SOD1(G93A) mice differ in adenosine A1 and A2A receptor-mediated tonic modulation of neuromuscular transmission. |
| Volume: |
11 |
| Issue: |
4 |
| Pages: |
471-80 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ishikawa T |
| Year: |
2001 |
| Journal: |
Mutat Res |
| Title: |
Importance of DNA repair in carcinogenesis: evidence from transgenic and gene targeting studies. |
| Volume: |
477 |
| Issue: |
1-2 |
| Pages: |
41-9 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Gupta MK |
| Year: |
2013 |
| Journal: |
J Mol Cell Cardiol |
| Title: |
Functional dissection of myosin binding protein C phosphorylation. |
| Volume: |
64 |
|
| Pages: |
39-50 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kulkarni AD |
| Year: |
1992 |
| Journal: |
Transplantation |
| Title: |
Immunohemopoietic effects of dietary nucleotide restriction in mice. |
| Volume: |
53 |
| Issue: |
2 |
| Pages: |
467-72 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Maier EA |
| Year: |
2005 |
| Journal: |
J Biol Chem |
| Title: |
Cdx binding determines the timing of enhancer activation in postnatal duodenum. |
| Volume: |
280 |
| Issue: |
13 |
| Pages: |
13195-202 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Wang L |
| Year: |
2014 |
| Journal: |
PLoS One |
| Title: |
Cardiac myosin binding protein C phosphorylation affects cross-bridge cycle's elementary steps in a site-specific manner. |
| Volume: |
9 |
| Issue: |
11 |
| Pages: |
e113417 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sakaguchi AY |
| Year: |
1984 |
| Journal: |
Cytogenet Cell Genet |
| Title: |
Mouse proto-oncogene assignments (Abstracts of meeting presentations: Human gene mapping 7, Los Angeles Conference (1983) Seventh International Workshop on Human Gene Mapping) |
| Volume: |
37 (1-4) |
|
| Pages: |
573-574 (Abstr.) (399-616) |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
813
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
830
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
829
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
830
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
833
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
813
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sterner DE |
| Year: |
2002 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription. |
| Volume: |
99 |
| Issue: |
18 |
| Pages: |
11622-7 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
The Mediator complex is a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. On recruitment the Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. The Mediator complex is composed of at least 31 subunits: MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The subunits form at least three structurally distinct submodules. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation.The head module contains: MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22. The middle module contains: MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31. CSE2/MED9 interacts directly with MED4. The tail module contains: MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The CDK8 module contains: MED12, MED13, CCNC and CDK8. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP.Regulation of mRNA synthesis requires intermediary proteins that transduce regulatory signals from upstream transcriptional activator proteins to basal transcription machinery at the core promoter. Three types of intermediary factors that enable the basal transcription machinery to respond to transcriptional activator proteins bound to regulatory DNA sequences have been identified: (i) TAFIIs, which associate with TATA-binding protein (TBP) to form TFIID; (ii) mediator, which associates with RNA polymerase II to form a holo-polymerase; and (iii) coactivators such as human upstream stimulatory activity (USA), mammalian CBP/P300, yeast ADA complex, and HMG proteins. The interaction of these multiprotein complexes with activators and general transcription factors is essential for transcriptional regulation. This family of proteins represent the transcriptional mediator protein that is required for activation of many RNA polymerase II promoters and which are conserved from yeast to humans [].This entry represents the Med6 subunit of the Mediator complex in fungi. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
The Mediator complex is a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. On recruitment the Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. The Mediator complex is composed of at least 31 subunits: MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The subunits form at least three structurally distinct submodules. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation.The head module contains: MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22. The middle module contains: MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31. CSE2/MED9 interacts directly with MED4. The tail module contains: MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The CDK8 module contains: MED12, MED13, CCNC and CDK8. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP.Regulation of mRNA synthesis requires intermediary proteins that transduce regulatory signals from upstream transcriptional activator proteins to basal transcription machinery at the core promoter. Three types of intermediary factors that enable the basal transcription machinery to respond to transcriptional activator proteins bound to regulatory DNA sequences have been identified: (i) TAFIIs, which associate with TATA-binding protein (TBP) to form TFIID; (ii) mediator, which associates with RNA polymerase II to form a holo-polymerase; and (iii) coactivators such as human upstream stimulatory activity (USA), mammalian CBP/P300, yeast ADA complex, and HMG proteins. The interaction of these multiprotein complexes with activators and general transcription factors is essential for transcriptional regulation.This family of proteins represent the transcriptional mediator protein subunit 6 that is required for activation of many RNA polymerase II promoters and which are conserved from yeast to humans []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
The Mediator complex is a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. On recruitment the Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. The Mediator complex is composed of at least 31 subunits: MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The subunits form at least three structurally distinct submodules. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation.The head module contains: MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22. The middle module contains: MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31. CSE2/MED9 interacts directly with MED4. The tail module contains: MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The CDK8 module contains: MED12, MED13, CCNC and CDK8. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP.Regulation of mRNA synthesis requires intermediary proteins that transduce regulatory signals from upstream transcriptional activator proteins to basal transcription machinery at the core promoter. Three types of intermediary factors that enable the basal transcription machinery to respond to transcriptional activator proteins bound to regulatory DNA sequences have been identified: (i) TAFIIs, which associate with TATA-binding protein (TBP) to form TFIID; (ii) mediator, which associates with RNA polymerase II to form a holo-polymerase; and (iii) coactivators such as human upstream stimulatory activity (USA), mammalian CBP/P300, yeast ADA complex, and HMG proteins. The interaction of these multiprotein complexes with activators and general transcription factors is essential for transcriptional regulation. This family of proteins represent the transcriptional mediator protein that is required for activation of many RNA polymerase II promoters and which are conserved from yeast to humans [].This group represents a RNA polymerase II mediator complex, subunit 6, metazoa/plant types. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lee YC |
| Year: |
1997 |
| Journal: |
Mol Cell Biol |
| Title: |
A transcriptional mediator protein that is required for activation of many RNA polymerase II promoters and is conserved from yeast to humans. |
| Volume: |
17 |
| Issue: |
8 |
| Pages: |
4622-32 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
181
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
132
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Pray-Grant MG |
| Year: |
2005 |
| Journal: |
Nature |
| Title: |
Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation. |
| Volume: |
433 |
| Issue: |
7024 |
| Pages: |
434-8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Pray-Grant MG |
| Year: |
2002 |
| Journal: |
Mol Cell Biol |
| Title: |
The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway. |
| Volume: |
22 |
| Issue: |
24 |
| Pages: |
8774-86 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Han Y |
| Year: |
2014 |
| Journal: |
EMBO J |
| Title: |
Architecture of the Saccharomyces cerevisiae SAGA transcription coactivator complex. |
| Volume: |
33 |
| Issue: |
21 |
| Pages: |
2534-46 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ogryzko VV |
| Year: |
1998 |
| Journal: |
Cell |
| Title: |
Histone-like TAFs within the PCAF histone acetylase complex. |
| Volume: |
94 |
| Issue: |
1 |
| Pages: |
35-44 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
246
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
195
 |
| Fragment?: |
false |
|
•
•
•
•
•
|