Q15648 · MED1_HUMAN
- ProteinMediator of RNA polymerase II transcription subunit 1
- GeneMED1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1581 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the Mediator complex, 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. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (PubMed:10406464, PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447, PubMed:14636573, PubMed:15340084, PubMed:15471764, PubMed:15989967, PubMed:16574658, PubMed:9653119).
Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781).
Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMediator of RNA polymerase II transcription subunit 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ15648
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: A subset of the protein may enter the nucleolus subsequent to phosphorylation by MAPK1 or MAPK3.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 599-612 | Enhances interaction with ESR1. | ||||
Sequence: SQNPILTSLLQITG → EKHKILHRLLQDSS | ||||||
Mutagenesis | 600-612 | Enhances interaction with ESR1. | ||||
Sequence: QNPILTSLLQITG → RHKILHRLLQEGS | ||||||
Mutagenesis | 604 | Impairs interaction with ESR2; when associated with A-607; A-645 and A-648. | ||||
Sequence: L → A | ||||||
Mutagenesis | 607 | Impairs interaction with ESR2; when associated with A-604; A-645 and A-648. | ||||
Sequence: L → A | ||||||
Mutagenesis | 607-608 | Impairs interaction with ESR1, PPARG, RXRA and THRB. Impairs interaction with THRA; when associated with 648-A-A-649. | ||||
Sequence: LL → AA | ||||||
Mutagenesis | 639-653 | Enhances interaction with ESR1. | ||||
Sequence: TKNHPMLMNLLKDNP → VSRHKILHRLLQEGS | ||||||
Mutagenesis | 645 | Impairs interaction with ESR2; when associated with A-604; A-607 and A-648. | ||||
Sequence: L → A | ||||||
Mutagenesis | 648 | Impairs interaction with ESR2; when associated with A-604; A-607 and A-645. | ||||
Sequence: L → A | ||||||
Mutagenesis | 648-649 | Impairs interaction with ESR1, PPARG, THRB and VDR. Impairs interaction with THRA; when associated with 607-A-A-608. | ||||
Sequence: LL → AA | ||||||
Natural variant | VAR_053955 | 753 | in dbSNP:rs1139825 | |||
Sequence: P → T | ||||||
Mutagenesis | 886 | Increased interaction with PSIP1; when associated with D-887 or D-887 and D-889. | ||||
Sequence: S → D | ||||||
Mutagenesis | 887 | Phosphomimetic mutant. Increased interaction with PSIP1; when associated with D-886 or D-886 and D-889. | ||||
Sequence: S → D | ||||||
Mutagenesis | 889 | Increased interaction with PSIP1; when associated with D-886 and D-887. | ||||
Sequence: S → D | ||||||
Mutagenesis | 1032 | Enhances protein stability; when associated with A-1457. | ||||
Sequence: T → A | ||||||
Natural variant | VAR_034938 | 1240 | in dbSNP:rs35668211 | |||
Sequence: S → G | ||||||
Mutagenesis | 1457 | Enhances protein stability; when associated with A-1032. | ||||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,446 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000058552 | 1-1581 | UniProt | Mediator of RNA polymerase II transcription subunit 1 | |||
Sequence: MKAQGETEESEKLSKMSSLLERLHAKFNQNRPWSETIKLVRQVMEKRVVMSSGGHQHLVSCLETLQKALKVTSLPAMTDRLESIARQNGLGSHLSASGTECYITSDMFYVEVQLDPAGQLCDVKVAHHGENPVSCPELVQQLREKNFDEFSKHLKGLVNLYNLPGDNKLKTKMYLALQSLEQDLSKMAIMYWKATNAGPLDKILHGSVGYLTPRSGGHLMNLKYYVSPSDLLDDKTASPIILHENNVSRSLGMNASVTIEGTSAVYKLPIAPLIMGSHPVDNKWTPSFSSITSANSVDLPACFFLKFPQPIPVSRAFVQKLQNCTGIPLFETQPTYAPLYELITQFELSKDPDPIPLNHNMRFYAALPGQQHCYFLNKDAPLPDGRSLQGTLVSKITFQHPGRVPLILNLIRHQVAYNTLIGSCVKRTILKEDSPGLLQFEVCPLSESRFSVSFQHPVNDSLVCVVMDVQDSTHVSCKLYKGLSDALICTDDFIAKVVQRCMSIPVTMRAIRRKAETIQADTPALSLIAETVEDMVKKNLPPASSPGYGMTTGNNPMSGTTTPTNTFPGGPITTLFNMSMSIKDRHESVGHGEDFSKVSQNPILTSLLQITGNGGSTIGSSPTPPHHTPPPVSSMAGNTKNHPMLMNLLKDNPAQDFSTLYGSSPLERQNSSSGSPRMEICSGSNKTKKKKSSRLPPEKPKHQTEDDFQRELFSMDVDSQNPIFDVNMTADTLDTPHITPAPSQCSTPPTTYPQPVPHPQPSIQRMVRLSSSDSIGPDVTDILSDIAEEASKLPSTSDDCPAIGTPLRDSSSSGHSQSTLFDSDVFQTNNNENPYTDPADLIADAAGSPSSDSPTNHFFHDGVDFNPDLLNSQSQSGFGEEYFDESSQSGDNDDFKGFASQALNTLGVPMLGGDNGETKFKGNNQADTVDFSIISVAGKALAPADLMEHHSGSQGPLLTTGDLGKEKTQKRVKEGNGTSNSTLSGPGLDSKPGKRSRTPSNDGKSKDKPPKRKKADTEGKSPSHSSSNRPFTPPTSTGGSKSPGSAGRSQTPPGVATPPIPKITIQIPKGTVMVGKPSSHSQYTSSGSVSSSGSKSHHSHSSSSSSSASTSGKMKSSKSEGSSSSKLSSSMYSSQGSSGSSQSKNSSQSGGKPGSSPITKHGLSSGSSSTKMKPQGKPSSLMNPSLSKPNISPSHSRPPGGSDKLASPMKPVPGTPPSSKAKSPISSGSGGSHMSGTSSSSGMKSSSGLGSSGSLSQKTPPSSNSCTASSSSFSSSGSSMSSSQNQHGSSKGKSPSRNKKPSLTAVIDKLKHGVVTSGPGGEDPLDGQMGVSTNSSSHPMSSKHNMSGGEFQGKREKSDKDKSKVSTSGSSVDSSKKTSESKNVGSTGVAKIIISKHDGGSPSIKAKVTLQKPGESSGEGLRPQMASSKNYGSPLISGSTPKHERGSPSHSKSPAYTPQNLDSESESGSSIAEKSYQNSPSSDDGIRPLPEYSTEKHKKHKKEKKKVKDKDRDRDRDKDRDKKKSHSIKPESWSKSPISSDQSLSMTSNTILSADRPSRLSPDFMIGEEDDDLMDVALIGN | |||||||
Modified residue (large scale data) | 207 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 238 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 588 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 588 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 621 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 628 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 663 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 664 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 664 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 671 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 672 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 673 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 675 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 682 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 684 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 770 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 771 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 772 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 774 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 784 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 795 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 795 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 797 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 805 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 805 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 874 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 887 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 951 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 953 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 953 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1021 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1023 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1025 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1032 | UniProt | Phosphothreonine; by MAPK1 or MAPK3 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1032 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1042 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1045 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1049 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1051 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1051 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1057 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1057 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1088 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1092 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1129 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1138 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1149 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1155 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1156 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1156 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1159 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1177 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1192 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1202 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1207 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1207 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1215 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1215 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1218 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1219 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1223 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1223 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1226 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1229 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1247 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1251 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1252 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1254 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1302 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1302 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1347 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1347 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1368 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1374 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1401 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1403 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1431 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1433 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1433 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1437 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1439 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1440 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1440 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1447 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1449 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1453 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1456 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1457 | UniProt | Phosphothreonine; by MAPK1 or MAPK3 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1457 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1463 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1463 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1465 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1465 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1467 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1475 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1476 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1479 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1479 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1481 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1481 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1482 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1482 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1529 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1532 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1534 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1536 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by MAPK1 or MAPK3 during G2/M phase which may enhance protein stability and promote entry into the nucleolus (PubMed:16314496).
Phosphorylation increases its interaction with PSIP1 (PubMed:29997176).
Phosphorylation increases its interaction with PSIP1 (PubMed:29997176).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitously expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Component of the Mediator complex, which is composed of 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 MED12, MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8 module. Mediator containing the CDK8 module is less active than Mediator lacking this module in supporting transcriptional activation. Individual preparations of the Mediator complex lacking one or more distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. This subunit specifically interacts with a number of nuclear receptors in a ligand-dependent fashion including AR, ESR1, ESR2, PPARA, PPARG, RORA, RXRA, RXRG, THRA, THRB and VDR. Interacts with CTNNB1, GABPA, GLI3, PPARGC1A and TP53. Interacts with YWHAH. Interacts with CLOCK; this interaction requires the presence of THRAP3 (By similarity).
Interacts with GATA1 and CCAR1. Interacts with NR4A3 (By similarity).
Interacts (via IBM motif) with PSIP1 (via IBD domain); phosphorylation increases its affinity for PSIP1 (PubMed:29997176).
Interacts with USP22 (By similarity).
Interacts with GATA1 and CCAR1. Interacts with NR4A3 (By similarity).
Interacts (via IBM motif) with PSIP1 (via IBD domain); phosphorylation increases its affinity for PSIP1 (PubMed:29997176).
Interacts with USP22 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q15648 | ESR1 P03372 | 3 | EBI-394459, EBI-78473 | |
BINARY | Q15648 | GATA1 P15976 | 6 | EBI-394459, EBI-3909284 | |
BINARY | Q15648 | MED21 Q13503 | 7 | EBI-394459, EBI-394678 | |
BINARY | Q15648 | MED7 O43513 | 8 | EBI-394459, EBI-394632 | |
BINARY | Q15648 | RARA P10276 | 6 | EBI-394459, EBI-413374 | |
BINARY | Q15648 | RXRA P19793 | 6 | EBI-394459, EBI-78598 | |
BINARY | Q15648 | THRA P10827 | 4 | EBI-394459, EBI-286285 | |
BINARY | Q15648 | VDR P11473 | 4 | EBI-394459, EBI-286357 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-670 | Interaction with the Mediator complex and THRA | ||||
Sequence: MKAQGETEESEKLSKMSSLLERLHAKFNQNRPWSETIKLVRQVMEKRVVMSSGGHQHLVSCLETLQKALKVTSLPAMTDRLESIARQNGLGSHLSASGTECYITSDMFYVEVQLDPAGQLCDVKVAHHGENPVSCPELVQQLREKNFDEFSKHLKGLVNLYNLPGDNKLKTKMYLALQSLEQDLSKMAIMYWKATNAGPLDKILHGSVGYLTPRSGGHLMNLKYYVSPSDLLDDKTASPIILHENNVSRSLGMNASVTIEGTSAVYKLPIAPLIMGSHPVDNKWTPSFSSITSANSVDLPACFFLKFPQPIPVSRAFVQKLQNCTGIPLFETQPTYAPLYELITQFELSKDPDPIPLNHNMRFYAALPGQQHCYFLNKDAPLPDGRSLQGTLVSKITFQHPGRVPLILNLIRHQVAYNTLIGSCVKRTILKEDSPGLLQFEVCPLSESRFSVSFQHPVNDSLVCVVMDVQDSTHVSCKLYKGLSDALICTDDFIAKVVQRCMSIPVTMRAIRRKAETIQADTPALSLIAETVEDMVKKNLPPASSPGYGMTTGNNPMSGTTTPTNTFPGGPITTLFNMSMSIKDRHESVGHGEDFSKVSQNPILTSLLQITGNGGSTIGSSPTPPHHTPPPVSSMAGNTKNHPMLMNLLKDNPAQDFSTLYGSSPLERQN | ||||||
Region | 16-590 | Interaction with ESR1 | ||||
Sequence: MSSLLERLHAKFNQNRPWSETIKLVRQVMEKRVVMSSGGHQHLVSCLETLQKALKVTSLPAMTDRLESIARQNGLGSHLSASGTECYITSDMFYVEVQLDPAGQLCDVKVAHHGENPVSCPELVQQLREKNFDEFSKHLKGLVNLYNLPGDNKLKTKMYLALQSLEQDLSKMAIMYWKATNAGPLDKILHGSVGYLTPRSGGHLMNLKYYVSPSDLLDDKTASPIILHENNVSRSLGMNASVTIEGTSAVYKLPIAPLIMGSHPVDNKWTPSFSSITSANSVDLPACFFLKFPQPIPVSRAFVQKLQNCTGIPLFETQPTYAPLYELITQFELSKDPDPIPLNHNMRFYAALPGQQHCYFLNKDAPLPDGRSLQGTLVSKITFQHPGRVPLILNLIRHQVAYNTLIGSCVKRTILKEDSPGLLQFEVCPLSESRFSVSFQHPVNDSLVCVVMDVQDSTHVSCKLYKGLSDALICTDDFIAKVVQRCMSIPVTMRAIRRKAETIQADTPALSLIAETVEDMVKKNLPPASSPGYGMTTGNNPMSGTTTPTNTFPGGPITTLFNMSMSIKDRHESVG | ||||||
Region | 108-212 | Interaction with the Mediator complex | ||||
Sequence: FYVEVQLDPAGQLCDVKVAHHGENPVSCPELVQQLREKNFDEFSKHLKGLVNLYNLPGDNKLKTKMYLALQSLEQDLSKMAIMYWKATNAGPLDKILHGSVGYLT | ||||||
Region | 215-390 | Interaction with the Mediator complex | ||||
Sequence: SGGHLMNLKYYVSPSDLLDDKTASPIILHENNVSRSLGMNASVTIEGTSAVYKLPIAPLIMGSHPVDNKWTPSFSSITSANSVDLPACFFLKFPQPIPVSRAFVQKLQNCTGIPLFETQPTYAPLYELITQFELSKDPDPIPLNHNMRFYAALPGQQHCYFLNKDAPLPDGRSLQG | ||||||
Region | 405-644 | Interaction with THRA | ||||
Sequence: PLILNLIRHQVAYNTLIGSCVKRTILKEDSPGLLQFEVCPLSESRFSVSFQHPVNDSLVCVVMDVQDSTHVSCKLYKGLSDALICTDDFIAKVVQRCMSIPVTMRAIRRKAETIQADTPALSLIAETVEDMVKKNLPPASSPGYGMTTGNNPMSGTTTPTNTFPGGPITTLFNMSMSIKDRHESVGHGEDFSKVSQNPILTSLLQITGNGGSTIGSSPTPPHHTPPPVSSMAGNTKNHPM | ||||||
Region | 542-789 | Interaction with VDR | ||||
Sequence: PASSPGYGMTTGNNPMSGTTTPTNTFPGGPITTLFNMSMSIKDRHESVGHGEDFSKVSQNPILTSLLQITGNGGSTIGSSPTPPHHTPPPVSSMAGNTKNHPMLMNLLKDNPAQDFSTLYGSSPLERQNSSSGSPRMEICSGSNKTKKKKSSRLPPEKPKHQTEDDFQRELFSMDVDSQNPIFDVNMTADTLDTPHITPAPSQCSTPPTTYPQPVPHPQPSIQRMVRLSSSDSIGPDVTDILSDIAEE | ||||||
Motif | 604-608 | LXXLL motif 1 | ||||
Sequence: LTSLL | ||||||
Region | 609-705 | Disordered | ||||
Sequence: QITGNGGSTIGSSPTPPHHTPPPVSSMAGNTKNHPMLMNLLKDNPAQDFSTLYGSSPLERQNSSSGSPRMEICSGSNKTKKKKSSRLPPEKPKHQTE | ||||||
Region | 622-701 | Interaction with PPARGC1A and THRA | ||||
Sequence: PTPPHHTPPPVSSMAGNTKNHPMLMNLLKDNPAQDFSTLYGSSPLERQNSSSGSPRMEICSGSNKTKKKKSSRLPPEKPK | ||||||
Motif | 645-649 | LXXLL motif 2 | ||||
Sequence: LMNLL | ||||||
Compositional bias | 652-682 | Polar residues | ||||
Sequence: NPAQDFSTLYGSSPLERQNSSSGSPRMEICS | ||||||
Region | 656-1066 | Interaction with ESR1 | ||||
Sequence: DFSTLYGSSPLERQNSSSGSPRMEICSGSNKTKKKKSSRLPPEKPKHQTEDDFQRELFSMDVDSQNPIFDVNMTADTLDTPHITPAPSQCSTPPTTYPQPVPHPQPSIQRMVRLSSSDSIGPDVTDILSDIAEEASKLPSTSDDCPAIGTPLRDSSSSGHSQSTLFDSDVFQTNNNENPYTDPADLIADAAGSPSSDSPTNHFFHDGVDFNPDLLNSQSQSGFGEEYFDESSQSGDNDDFKGFASQALNTLGVPMLGGDNGETKFKGNNQADTVDFSIISVAGKALAPADLMEHHSGSQGPLLTTGDLGKEKTQKRVKEGNGTSNSTLSGPGLDSKPGKRSRTPSNDGKSKDKPPKRKKADTEGKSPSHSSSNRPFTPPTSTGGSKSPGSAGRSQTPPGVATPPIPKITIQ | ||||||
Region | 681-715 | Interaction with GATA1 | ||||
Sequence: CSGSNKTKKKKSSRLPPEKPKHQTEDDFQRELFSM | ||||||
Region | 792-820 | Disordered | ||||
Sequence: KLPSTSDDCPAIGTPLRDSSSSGHSQSTL | ||||||
Compositional bias | 806-820 | Polar residues | ||||
Sequence: PLRDSSSSGHSQSTL | ||||||
Region | 874-893 | Disordered | ||||
Sequence: SQSGFGEEYFDESSQSGDND | ||||||
Motif | 875-902 | Integrase domain-binding motif (IBM) | ||||
Sequence: QSGFGEEYFDESSQSGDNDDFKGFASQA | ||||||
Region | 948-1566 | Disordered | ||||
Sequence: EHHSGSQGPLLTTGDLGKEKTQKRVKEGNGTSNSTLSGPGLDSKPGKRSRTPSNDGKSKDKPPKRKKADTEGKSPSHSSSNRPFTPPTSTGGSKSPGSAGRSQTPPGVATPPIPKITIQIPKGTVMVGKPSSHSQYTSSGSVSSSGSKSHHSHSSSSSSSASTSGKMKSSKSEGSSSSKLSSSMYSSQGSSGSSQSKNSSQSGGKPGSSPITKHGLSSGSSSTKMKPQGKPSSLMNPSLSKPNISPSHSRPPGGSDKLASPMKPVPGTPPSSKAKSPISSGSGGSHMSGTSSSSGMKSSSGLGSSGSLSQKTPPSSNSCTASSSSFSSSGSSMSSSQNQHGSSKGKSPSRNKKPSLTAVIDKLKHGVVTSGPGGEDPLDGQMGVSTNSSSHPMSSKHNMSGGEFQGKREKSDKDKSKVSTSGSSVDSSKKTSESKNVGSTGVAKIIISKHDGGSPSIKAKVTLQKPGESSGEGLRPQMASSKNYGSPLISGSTPKHERGSPSHSKSPAYTPQNLDSESESGSSIAEKSYQNSPSSDDGIRPLPEYSTEKHKKHKKEKKKVKDKDRDRDRDKDRDKKKSHSIKPESWSKSPISSDQSLSMTSNTILSADRPSRLSPDFMI | ||||||
Compositional bias | 995-1020 | Basic and acidic residues | ||||
Sequence: RSRTPSNDGKSKDKPPKRKKADTEGK | ||||||
Compositional bias | 1021-1052 | Polar residues | ||||
Sequence: SPSHSSSNRPFTPPTSTGGSKSPGSAGRSQTP | ||||||
Compositional bias | 1075-1197 | Polar residues | ||||
Sequence: GKPSSHSQYTSSGSVSSSGSKSHHSHSSSSSSSASTSGKMKSSKSEGSSSSKLSSSMYSSQGSSGSSQSKNSSQSGGKPGSSPITKHGLSSGSSSTKMKPQGKPSSLMNPSLSKPNISPSHSR | ||||||
Compositional bias | 1219-1301 | Polar residues | ||||
Sequence: SKAKSPISSGSGGSHMSGTSSSSGMKSSSGLGSSGSLSQKTPPSSNSCTASSSSFSSSGSSMSSSQNQHGSSKGKSPSRNKKP | ||||||
Region | 1249-1421 | Interaction with TP53 | ||||
Sequence: LGSSGSLSQKTPPSSNSCTASSSSFSSSGSSMSSSQNQHGSSKGKSPSRNKKPSLTAVIDKLKHGVVTSGPGGEDPLDGQMGVSTNSSSHPMSSKHNMSGGEFQGKREKSDKDKSKVSTSGSSVDSSKKTSESKNVGSTGVAKIIISKHDGGSPSIKAKVTLQKPGESSGEGL | ||||||
Compositional bias | 1328-1348 | Polar residues | ||||
Sequence: QMGVSTNSSSHPMSSKHNMSG | ||||||
Compositional bias | 1349-1366 | Basic and acidic residues | ||||
Sequence: GEFQGKREKSDKDKSKVS | ||||||
Compositional bias | 1367-1388 | Polar residues | ||||
Sequence: TSGSSVDSSKKTSESKNVGSTG | ||||||
Compositional bias | 1421-1484 | Polar residues | ||||
Sequence: LRPQMASSKNYGSPLISGSTPKHERGSPSHSKSPAYTPQNLDSESESGSSIAEKSYQNSPSSDD | ||||||
Compositional bias | 1508-1530 | Basic and acidic residues | ||||
Sequence: KDKDRDRDRDKDRDKKKSHSIKP | ||||||
Compositional bias | 1531-1556 | Polar residues | ||||
Sequence: ESWSKSPISSDQSLSMTSNTILSADR |
Sequence similarities
Belongs to the Mediator complex subunit 1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q15648-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,581
- Mass (Da)168,478
- Last updated2007-09-11 v4
- ChecksumFCE0FE87EF08B887
Q15648-3
- Name2
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 86 | in Ref. 1; CAA73867 | ||||
Sequence: R → G | ||||||
Sequence conflict | 147 | in Ref. 1; CAA73867 | ||||
Sequence: F → S | ||||||
Sequence conflict | 471-472 | in Ref. 1; CAA73867 | ||||
Sequence: DS → GL | ||||||
Alternative sequence | VSP_027906 | 548-556 | in isoform 2 | |||
Sequence: YGMTTGNNP → SKNPELGSG | ||||||
Alternative sequence | VSP_027907 | 557-1581 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 563 | in Ref. 1; CAA73867 and 7; AAF98352 | ||||
Sequence: P → S | ||||||
Sequence conflict | 573 | in Ref. 1; CAA73867 and 7; AAF98352 | ||||
Sequence: T → A | ||||||
Sequence conflict | 651 | in Ref. 5; AAH06517 | ||||
Sequence: D → N | ||||||
Compositional bias | 652-682 | Polar residues | ||||
Sequence: NPAQDFSTLYGSSPLERQNSSSGSPRMEICS | ||||||
Sequence conflict | 673 | in Ref. 9; AAC41736 | ||||
Sequence: S → F | ||||||
Sequence conflict | 702-708 | in Ref. 9; AAC41736 | ||||
Sequence: Missing | ||||||
Sequence conflict | 721 | in Ref. 2; AAC39854 | ||||
Sequence: N → K | ||||||
Sequence conflict | 728 | in Ref. 7; AAF98352 | ||||
Sequence: M → R | ||||||
Sequence conflict | 756-761 | in Ref. 5; AAH06517 | ||||
Sequence: VPHPQP → FYLTPQ | ||||||
Compositional bias | 806-820 | Polar residues | ||||
Sequence: PLRDSSSSGHSQSTL | ||||||
Compositional bias | 995-1020 | Basic and acidic residues | ||||
Sequence: RSRTPSNDGKSKDKPPKRKKADTEGK | ||||||
Compositional bias | 1021-1052 | Polar residues | ||||
Sequence: SPSHSSSNRPFTPPTSTGGSKSPGSAGRSQTP | ||||||
Compositional bias | 1075-1197 | Polar residues | ||||
Sequence: GKPSSHSQYTSSGSVSSSGSKSHHSHSSSSSSSASTSGKMKSSKSEGSSSSKLSSSMYSSQGSSGSSQSKNSSQSGGKPGSSPITKHGLSSGSSSTKMKPQGKPSSLMNPSLSKPNISPSHSR | ||||||
Compositional bias | 1219-1301 | Polar residues | ||||
Sequence: SKAKSPISSGSGGSHMSGTSSSSGMKSSSGLGSSGSLSQKTPPSSNSCTASSSSFSSSGSSMSSSQNQHGSSKGKSPSRNKKP | ||||||
Compositional bias | 1328-1348 | Polar residues | ||||
Sequence: QMGVSTNSSSHPMSSKHNMSG | ||||||
Compositional bias | 1349-1366 | Basic and acidic residues | ||||
Sequence: GEFQGKREKSDKDKSKVS | ||||||
Compositional bias | 1367-1388 | Polar residues | ||||
Sequence: TSGSSVDSSKKTSESKNVGSTG | ||||||
Sequence conflict | 1388 | in Ref. 2; AAC39854 | ||||
Sequence: G → S | ||||||
Compositional bias | 1421-1484 | Polar residues | ||||
Sequence: LRPQMASSKNYGSPLISGSTPKHERGSPSHSKSPAYTPQNLDSESESGSSIAEKSYQNSPSSDD | ||||||
Compositional bias | 1508-1530 | Basic and acidic residues | ||||
Sequence: KDKDRDRDRDKDRDKKKSHSIKP | ||||||
Compositional bias | 1531-1556 | Polar residues | ||||
Sequence: ESWSKSPISSDQSLSMTSNTILSADR |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y13467 EMBL· GenBank· DDBJ | CAA73867.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AF055994 EMBL· GenBank· DDBJ | AAC39854.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
CH471152 EMBL· GenBank· DDBJ | EAW60575.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC006517 EMBL· GenBank· DDBJ | AAH06517.1 EMBL· GenBank· DDBJ | mRNA | Different termination. | |
BC060758 EMBL· GenBank· DDBJ | AAH60758.1 EMBL· GenBank· DDBJ | mRNA | ||
BC131783 EMBL· GenBank· DDBJ | AAI31784.1 EMBL· GenBank· DDBJ | mRNA | ||
AF283812 EMBL· GenBank· DDBJ | AAF98352.1 EMBL· GenBank· DDBJ | mRNA | ||
L40366 EMBL· GenBank· DDBJ | AAC41736.1 EMBL· GenBank· DDBJ | mRNA |