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14  structures 752  species 9  interactions 866  sequences 8  architectures

Family: Med17 (PF10156)

Summary: Subunit 17 of Mediator complex

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "MED17". More...

MED17 Edit Wikipedia article

MED17
Identifiers
AliasesMED17, CRSP6, CRSP77, DRIP80, TRAP80, mediator complex subunit 17, SRB4
External IDsOMIM: 603810 MGI: 2182585 HomoloGene: 3151 GeneCards: MED17
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for MED17
Genomic location for MED17
Band11q21Start93,784,227 bp[1]
End93,814,963 bp[1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004268

NM_144933
NM_001364533

RefSeq (protein)

NP_004259

NP_659182
NP_001351462

Location (UCSC)Chr 11: 93.78 – 93.81 MbChr 9: 15.26 – 15.28 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Mediator of RNA polymerase II transcription subunit 17 is an enzyme that in humans is encoded by the MED17 gene.[5][6][7]

The activation of gene transcription is a multistep process that is triggered by factors that recognize transcriptional enhancer sites in DNA. These factors work with co-activators to direct transcriptional initiation by the RNA polymerase II apparatus. The protein encoded by this gene is a subunit of the CRSP (cofactor required for SP1 activation) complex, which, along with TFIID, is required for efficient activation by SP1. This protein is also a component of other multisubunit complexes e.g. thyroid hormone receptor-(TR-) associated proteins which interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors.[7]

Interactions

MED17 has been shown to interact with PPARGC1A,[8] Cyclin-dependent kinase 8[6][9] and BRCA1.[10][11][12]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000042429 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031935 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Ryu S, Zhou S, Ladurner AG, Tjian R (Feb 1999). "The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Sp1". Nature. 397 (6718): 446–50. Bibcode:1999Natur.397..446R. doi:10.1038/17141. PMID 9989412.
  6. ^ a b Ito M, Yuan CX, Malik S, Gu W, Fondell JD, Yamamura S, Fu ZY, Zhang X, Qin J, Roeder RG (Apr 1999). "Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators". Mol Cell. 3 (3): 361–70. doi:10.1016/S1097-2765(00)80463-3. PMID 10198638.
  7. ^ a b "Entrez Gene: CRSP6 cofactor required for Sp1 transcriptional activation, subunit 6, 77kDa".
  8. ^ Wallberg, Annika E; Yamamura Soichiro; Malik Sohail; Spiegelman Bruce M; Roeder Robert G (Nov 2003). "Coordination of p300-mediated chromatin remodeling and TRAP/mediator function through coactivator PGC-1alpha". Mol. Cell. United States. 12 (5): 1137–49. doi:10.1016/S1097-2765(03)00391-5. ISSN 1097-2765. PMID 14636573.
  9. ^ Kang, Yun Kyoung; Guermah Mohamed; Yuan Chao-Xing; Roeder Robert G (Mar 2002). "The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro". Proc. Natl. Acad. Sci. U.S.A. United States. 99 (5): 2642–7. Bibcode:2002PNAS...99.2642K. doi:10.1073/pnas.261715899. ISSN 0027-8424. PMC 122401. PMID 11867769.
  10. ^ Chiba, N; Parvin J D (Oct 2001). "Redistribution of BRCA1 among four different protein complexes following replication blockage". J. Biol. Chem. United States. 276 (42): 38549–54. doi:10.1074/jbc.M105227200. ISSN 0021-9258. PMID 11504724.
  11. ^ Wada, Osamu; Oishi Hajime; Takada Ichiro; Yanagisawa Junn; Yano Tetsu; Kato Shigeaki (Aug 2004). "BRCA1 function mediates a TRAP/DRIP complex through direct interaction with TRAP220". Oncogene. England. 23 (35): 6000–5. doi:10.1038/sj.onc.1207786. ISSN 0950-9232. PMID 15208681.
  12. ^ Chiba, Natsuko; Parvin Jeffrey D (Aug 2002). "The BRCA1 and BARD1 association with the RNA polymerase II holoenzyme". Cancer Res. United States. 62 (15): 4222–8. ISSN 0008-5472. PMID 12154023.

Further reading


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This is the Wikipedia entry entitled "Mediator (coactivator)". More...

Mediator (coactivator) Edit Wikipedia article

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Subunit 17 of Mediator complex Provide feedback

This Mediator complex subunit was formerly known as Srb4 in yeasts or Trap80 in Drosophila and human. The Med17 subunit is located within the head domain and is essential for cell viability to the extent that a mutant strain of cerevisiae lacking it shows all RNA polymerase II-dependent transcription ceasing at non-permissive temperatures.

Literature references

  1. 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, , Mol Cell. 2004;14:553-557.: A unified nomenclature for protein subunits of mediator complexes linking transcriptional regulators to RNA polymerase II. PUBMED:15175151 EPMC:15175151

  2. Spahr H, Samuelsen CO, Baraznenok V, Ernest I, Huylebroeck D, Remacle JE, Samuelsson T, Kieselbach T, Holmberg S, Gustafsson CM; , Proc Natl Acad Sci U S A 2001;98:11985-11990.: Analysis of Schizosaccharomyces pombe mediator reveals a set of essential subunits conserved between yeast and metazoan cells. PUBMED:11572939 EPMC:11572939

  3. Linder T, Zhu X, Baraznenok V, Gustafsson CM; , Biochem Biophys Res Commun. 2006;349:948-953.: The classical srb4-138 mutant allele causes dissociation of yeast Mediator. PUBMED:16962561 EPMC:16962561


This tab holds annotation information from the InterPro database.

InterPro entry IPR019313

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.

This entry represents subunit Med17 of the Mediator complex. The Med17 subunit is located within the head domain and is essential for cell viability to the extent that a mutant strain of Saccharomyces cerevisiae (Baker's yeast) lacking it shows all RNA polymerase II-dependent transcription ceasing at non-permissive temperatures.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

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Alignments

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  Seed
(27)
Full
(866)
Representative proteomes UniProt
(1240)
NCBI
(1485)
Meta
(0)
RP15
(175)
RP35
(410)
RP55
(625)
RP75
(791)
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  Seed
(27)
Full
(866)
Representative proteomes UniProt
(1240)
NCBI
(1485)
Meta
(0)
RP15
(175)
RP35
(410)
RP55
(625)
RP75
(791)
Alignment:
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  Seed
(27)
Full
(866)
Representative proteomes UniProt
(1240)
NCBI
(1485)
Meta
(0)
RP15
(175)
RP35
(410)
RP55
(625)
RP75
(791)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: KOGs (KOG4512)
Previous IDs: DUF2364;
Type: Family
Sequence Ontology: SO:0100021
Author: KOGs, Finn RD , Coggill P
Number in seed: 27
Number in full: 866
Average length of the domain: 373.50 aa
Average identity of full alignment: 19 %
Average coverage of the sequence by the domain: 60.85 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 19.4 19.4
Trusted cut-off 19.4 19.4
Noise cut-off 19.3 19.3
Model length: 462
Family (HMM) version: 9
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 9 interactions for this family. More...

Med18 Med6 Med8 Med6 Med20 Med8 RNA_pol_Rpb1_R Med11 Med22

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Med17 domain has been found. There are 14 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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