Q8VCD5
PR
Gene name |
Med17 (Crsp6, Trap80) |
Protein name |
Mediator of RNA polymerase II transcription subunit 17 |
Names |
Cofactor required for Sp1 transcriptional activation subunit 6, CRSP complex subunit 6, Mediator complex subunit 17, Thyroid hormone receptor-associated protein complex 80 kDa component |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:234959 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
2 structures for Q8VCD5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 6W1S | EM | 402 A | L | 15-645 | PDB |
| AF-Q8VCD5-F1 | Predicted | AlphaFoldDB |
23 variants for Q8VCD5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389005552 | 24 | L>H | No | EVA | |
| rs3389029855 | 63 | P>S | No | EVA | |
| rs3389024793 | 80 | E>K | No | EVA | |
| rs3399310236 | 167 | K>* | No | EVA | |
| rs3399955767 | 167 | K>R | No | EVA | |
| rs3399849949 | 184 | E>A | No | EVA | |
| rs3388974625 | 196 | K>N | No | EVA | |
| rs3389027214 | 207 | Y>* | No | EVA | |
| rs3389022317 | 211 | G>D | No | EVA | |
| rs3389022279 | 245 | I>N | No | EVA | |
| rs3389029831 | 275 | F>L | No | EVA | |
| rs3412951754 | 283 | K>T | No | EVA | |
| rs3388999471 | 298 | N>I | No | EVA | |
| rs228108877 | 357 | A>T | No | EVA | |
| rs3389022336 | 390 | M>I | No | EVA | |
| rs3389032285 | 448 | S>C | No | EVA | |
| rs3389025794 | 496 | G>VSDG* | No | EVA | |
| rs3389018197 | 516 | E>G | No | EVA | |
| rs3399511787 | 529 | Q>L | No | EVA | |
| rs3399921482 | 530 | H>N | No | EVA | |
| rs3399940794 | 531 | Q>H | No | EVA | |
| rs3399885700 | 532 | V>G | No | EVA | |
| rs3399511816 | 634 | V>I | No | EVA |
No associated diseases with Q8VCD5
No regional properties for Q8VCD5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q8VCD5 | |||
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| core mediator complex | A protein complex that interacts with the carboxy-terminal domain of the largest subunit of RNA polymerase II and plays an active role in transducing the signal from a transcription factor to the transcriptional machinery. The core mediator complex has a stimulatory effect on basal transcription, and contains most of the same subdomains as the larger form of mediator complex -- a head domain comprising proteins known in Saccharomyces as Srb2, -4, and -5, Med6, -8, and -11, and Rox3 proteins; a middle domain comprising Med1, -4, and -7, Nut1 and -2, Cse2, Rgr1, Soh1, and Srb7 proteins; and a tail consisting of Gal11p, Med2p, Pgd1p, and Sin4p -- but lacks the regulatory subcomplex comprising Ssn2, -3, and -8, and Srb8 proteins. Metazoan core mediator complexes have similar modular structures and include homologs of yeast Srb and Med proteins. |
| mediator complex | A protein complex that interacts with the carboxy-terminal domain of the largest subunit of RNA polymerase II and plays an active role in transducing the signal from a transcription factor to the transcriptional machinery. The mediator complex is required for activation of transcription of most protein-coding genes, but can also act as a transcriptional corepressor. The Saccharomyces complex contains several identifiable subcomplexes: a head domain comprising Srb2, -4, and -5, Med6, -8, and -11, and Rox3 proteins; a middle domain comprising Med1, -4, and -7, Nut1 and -2, Cse2, Rgr1, Soh1, and Srb7 proteins; a tail consisting of Gal11p, Med2p, Pgd1p, and Sin4p; and a regulatory subcomplex comprising Ssn2, -3, and -8, and Srb8 proteins. Metazoan mediator complexes have similar modular structures and include homologs of yeast Srb and Med proteins. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
| transcription regulator complex | A protein complex that is capable of associating with DNA by direct binding, or via other DNA-binding proteins or complexes, and regulating transcription. |
| ubiquitin ligase complex | A protein complex that includes a ubiquitin-protein ligase and enables ubiquitin protein ligase activity. The complex also contains other proteins that may confer substrate specificity on the complex. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| nuclear receptor coactivator activity | A transcription coactivator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound nuclear receptor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator. |
| nuclear thyroid hormone receptor binding | Binding to a nuclear thyroid hormone receptor. |
| transcription coactivator activity | A transcription coregulator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coactivators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator. |
| transcription coregulator activity | A transcription regulator activity that modulates the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coregulators often act by altering chromatin structure and modifications. For example, one class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. |
| ubiquitin protein ligase activity | Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues. |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| positive regulation of DNA-templated transcription | Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription. |
| positive regulation of transcription by RNA polymerase II | Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter. |
| positive regulation of transcription elongation by RNA polymerase II | Any process that activates or increases the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides, catalyzed by RNA polymerase II. |
| positive regulation of transcription initiation by RNA polymerase II | Any process that increases the rate, frequency or extent of a process involved in starting transcription from an RNA polymerase II promoter. |
| protein ubiquitination | The process in which one or more ubiquitin groups are added to a protein. |
| regulation of transcription by RNA polymerase II | Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II. |
| RNA polymerase II preinitiation complex assembly | The aggregation, arrangement and bonding together of proteins on an RNA polymerase II promoter DNA to form the transcriptional preinitiation complex (PIC), the formation of which is a prerequisite for transcription by RNA polymerase. |
| somatic stem cell population maintenance | Any process by which an organism retains a population of somatic stem cells, undifferentiated cells in the embryo or adult which can undergo unlimited division and give rise to cell types of the body other than those of the germ-line. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSGVRAVRIS | IESACEKQVQ | EVGLDGTETY | LQPLSMSQNL | ARLAQRIDFS | QGSGSEEEEA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AGPDGDAPDW | GGAGADQDDE | EGLVKFQPSL | WPWDSVRNNL | RSALTEMCVL | YDVLSIVRDK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KFMTLDPVSQ | DALPPKQSPQ | TLQLISKKKS | LAGAAQILLK | GAERLTKSVA | ENQENKLQRD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FNSELLRLRQ | HWKLRKVGDK | ILGDLSYRSA | GSLFPHHGTF | EVIKNTDIDL | DKKIPEDYCP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LDVQIPSDLE | GSAYIKVSIQ | KQAPDIGDLG | TVNLFKRPLP | KSKPGSPHWQ | TKLEAAQNVL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LCKEIFAQLS | REAVQIKSQI | PHIVVKNQII | SQPFPSLQLS | ISLCHSSDDK | KSQKCAAEKP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GQEDHLYVLE | HNLHLLIREF | HKQTLSSIVM | PHPASAPFGH | KRMRLSGPQA | FDKNEINSIQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| STEGLLEKII | KQAKHIFLRS | RTAATIDSLA | SRIEDPQIQA | HWSNINDVYE | SSVKVLITSQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GYEQICKSIQ | LQLNIGVEQV | RVVHRDGRVI | MLSHQEQELQ | DFLLSQMSQH | QVHAVQQLAK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VMGWQVLSFS | NHVGLGPIES | IGNASAITVA | SPSGDYAISV | RNGPESGSKI | MVQFPRNQCK |
| 610 | 620 | 630 | 640 | ||
| DLPKSDVLQD | SKWSHLRGPF | KEVQWNKMEG | RNFVYKMELL | MSALSPCLL |