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Q925J9

- MED1_MOUSE

UniProt

Q925J9 - MED1_MOUSE

Protein

Mediator of RNA polymerase II transcription subunit 1

Gene

Med1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    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. Essential for embryogenesis, including development of the central nervous system, heart, liver and placenta and for erythropoiesis. Also required for normal transcriptional control of thyroid-stimulating hormone beta (TSHB) in the pituitary.10 Publications

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. chromatin DNA binding Source: Ensembl
    3. core promoter binding Source: UniProtKB
    4. DNA binding Source: MGI
    5. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    6. nuclear hormone receptor binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. protein complex binding Source: MGI
    9. receptor activity Source: UniProtKB
    10. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
    11. RNA polymerase II transcription cofactor activity Source: UniProtKB
    12. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
    13. thyroid hormone receptor binding Source: UniProtKB
    14. thyroid hormone receptor coactivator activity Source: Ensembl
    15. transcription coactivator activity Source: MGI
    16. transcription factor binding Source: BHF-UCL

    GO - Biological processi

    1. androgen biosynthetic process Source: UniProtKB
    2. androgen receptor signaling pathway Source: UniProtKB
    3. angiogenesis Source: BHF-UCL
    4. brain development Source: MGI
    5. camera-type eye development Source: MGI
    6. cell morphogenesis Source: UniProtKB
    7. cellular response to epidermal growth factor stimulus Source: UniProtKB
    8. cellular response to hepatocyte growth factor stimulus Source: MGI
    9. cellular response to steroid hormone stimulus Source: Ensembl
    10. cellular response to thyroid hormone stimulus Source: Ensembl
    11. embryonic heart tube development Source: MGI
    12. embryonic hemopoiesis Source: MGI
    13. embryonic hindlimb morphogenesis Source: MGI
    14. embryonic placenta development Source: MGI
    15. enucleate erythrocyte development Source: MGI
    16. epithelial cell proliferation involved in mammary gland duct elongation Source: MGI
    17. ERK1 and ERK2 cascade Source: Ensembl
    18. erythrocyte development Source: BHF-UCL
    19. fat cell differentiation Source: MGI
    20. heart development Source: MGI
    21. intracellular steroid hormone receptor signaling pathway Source: UniProtKB
    22. in utero embryonic development Source: MGI
    23. keratinocyte differentiation Source: UniProtKB
    24. lactation Source: MGI
    25. lens development in camera-type eye Source: BHF-UCL
    26. liver development Source: MGI
    27. mammary gland branching involved in pregnancy Source: MGI
    28. mammary gland branching involved in thelarche Source: MGI
    29. mammary gland epithelial cell proliferation Source: MGI
    30. megakaryocyte development Source: BHF-UCL
    31. monocyte differentiation Source: MGI
    32. mRNA transcription from RNA polymerase II promoter Source: UniProtKB
    33. multicellular organismal development Source: MGI
    34. negative regulation of apoptotic process Source: UniProtKB
    35. negative regulation of keratinocyte proliferation Source: UniProtKB
    36. negative regulation of neuron differentiation Source: UniProtKB
    37. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    38. organ morphogenesis Source: MGI
    39. organ regeneration Source: MGI
    40. peroxisome proliferator activated receptor signaling pathway Source: MGI
    41. positive regulation of cell proliferation Source: MGI
    42. positive regulation of G0 to G1 transition Source: MGI
    43. positive regulation of gene expression Source: UniProtKB
    44. positive regulation of hepatocyte proliferation Source: MGI
    45. positive regulation of interferon-gamma-mediated signaling pathway Source: MGI
    46. positive regulation of intracellular estrogen receptor signaling pathway Source: MGI
    47. positive regulation of keratinocyte differentiation Source: UniProtKB
    48. positive regulation of mammary gland epithelial cell proliferation Source: MGI
    49. positive regulation of protein import into nucleus, translocation Source: MGI
    50. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    51. regulation of RNA biosynthetic process Source: UniProtKB
    52. regulation of transcription, DNA-templated Source: MGI
    53. regulation of transcription from RNA polymerase I promoter Source: UniProtKB
    54. regulation of vitamin D receptor signaling pathway Source: MGI
    55. retinal pigment epithelium development Source: BHF-UCL
    56. thyroid hormone generation Source: MGI
    57. thyroid hormone mediated signaling pathway Source: UniProtKB
    58. transcription from RNA polymerase II promoter Source: MGI
    59. transcription initiation from RNA polymerase II promoter Source: UniProtKB
    60. ventricular trabecula myocardium morphogenesis Source: BHF-UCL

    Keywords - Molecular functioni

    Activator, Developmental protein

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_118837. Rora activates circadian gene expression.
    REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_198351. RORA activates circadian gene expression.
    REACT_198352. REV-ERBA represses gene expression.
    REACT_198602. PPARA activates gene expression.
    REACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_205251. Transcriptional activation of mitochondrial biogenesis.
    REACT_206529. Generic Transcription Pathway.
    REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mediator of RNA polymerase II transcription subunit 1
    Alternative name(s):
    Mediator complex subunit 1
    Peroxisome proliferator-activated receptor-binding protein
    Short name:
    PBP
    Short name:
    PPAR-binding protein
    Thyroid hormone receptor-associated protein complex 220 kDa component
    Short name:
    Trap220
    Thyroid receptor-interacting protein 2
    Short name:
    TR-interacting protein 2
    Short name:
    TRIP-2
    Gene namesi
    Name:Med1
    Synonyms:Crsp210, Drip205, Pbp, Pparbp, Trap220, Trip2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1100846. Med1.

    Subcellular locationi

    Nucleus 1 Publication
    Note: A subset of the protein may enter the nucleolus subsequent to phosphorylation by MAPK1 or MAPK3.By similarity

    GO - Cellular componenti

    1. chromatin Source: Ensembl
    2. mediator complex Source: MGI
    3. nucleolus Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: MGI
    6. protein-DNA complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15751575Mediator of RNA polymerase II transcription subunit 1PRO_0000058553Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei664 – 6641PhosphoserineBy similarity
    Modified residuei795 – 7951PhosphoserineBy similarity
    Modified residuei805 – 8051PhosphothreonineBy similarity
    Modified residuei953 – 9531Phosphoserine1 Publication
    Modified residuei955 – 9551Phosphoserine1 Publication
    Modified residuei1032 – 10321Phosphothreonine; by MAPK1 or MAPK3By similarity
    Modified residuei1051 – 10511PhosphothreonineBy similarity
    Modified residuei1057 – 10571PhosphothreonineBy similarity
    Modified residuei1158 – 11581PhosphoserineBy similarity
    Modified residuei1179 – 11791N6-acetyllysineBy similarity
    Modified residuei1209 – 12091PhosphoserineBy similarity
    Modified residuei1217 – 12171PhosphothreonineBy similarity
    Modified residuei1225 – 12251PhosphoserineBy similarity
    Modified residuei1349 – 13491PhosphoserineBy similarity
    Modified residuei1405 – 14051PhosphoserineBy similarity
    Modified residuei1435 – 14351PhosphoserineBy similarity
    Modified residuei1459 – 14591Phosphothreonine; by MAPK1 or MAPK3By similarity
    Modified residuei1465 – 14651PhosphoserineBy similarity
    Modified residuei1481 – 14811PhosphoserineBy similarity
    Modified residuei1483 – 14831PhosphoserineBy similarity
    Modified residuei1484 – 14841PhosphoserineBy similarity
    Modified residuei1523 – 15231N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylated by MAPK1 or MAPK3 during G2/M phase which may enhance protein stability and promote entry into the nucleolus.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ925J9.
    PaxDbiQ925J9.
    PRIDEiQ925J9.

    PTM databases

    PhosphoSiteiQ925J9.

    Expressioni

    Tissue specificityi

    Widely expressed in the adult, with high levels of expression in the liver, lung, intestinal mucosa, kidney cortex, thymic cortex, splenic follicle and seminiferous epithelium in testis. Also expressed in the adult heart, brain, spleen and skeletal muscle.2 Publications

    Developmental stagei

    Widely expressed during embryonic development; at stages E9.5-10.5, expression is strongest in neural tissues. At E11.5-E12.5, expression is abundant throughout embryonic tissues, being strongest in the developing liver, primitive gut, nasopharynx, and developing limb buds. Moderately expressed at this stage in the brain and optic stalk, branchial arch and urogential ridge. Expressed at a low level in the heart. By stage E13.5-E14.5, expression is abundant in the forebrain, vagus nerve, dorsal root ganglia, nasopharynx, kidney, liver, pancreas, intestine, gut, thymus, lung, genital tubercle, tongue and lower jaw. Moderately expressed in the midbrain and expressed at a low level in the heart and large blood vessels. In the developing placenta, expression is moderate in the giant and spongiotrophoblast cell layers and strongest in the labyrinthine portion throughout E9.5-E13.5.2 Publications

    Gene expression databases

    ArrayExpressiQ925J9.
    BgeeiQ925J9.
    CleanExiMM_MED1.
    GenevestigatoriQ925J9.

    Interactioni

    Subunit structurei

    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 GATA1 and YWHAH.7 Publications

    Protein-protein interaction databases

    BioGridi202318. 5 interactions.
    DIPiDIP-59232N.
    IntActiQ925J9. 8 interactions.
    MINTiMINT-4123213.

    Structurei

    Secondary structure

    1
    1575
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi643 – 6497

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XDKX-ray2.90C/D/G/H641-654[»]
    ProteinModelPortaliQ925J9.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ925J9.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 670670Interaction with the Mediator complex and THRABy similarityAdd
    BLAST
    Regioni16 – 590575Interaction with ESR1By similarityAdd
    BLAST
    Regioni108 – 212105Interaction with the Mediator complexBy similarityAdd
    BLAST
    Regioni215 – 390176Interaction with the Mediator complexBy similarityAdd
    BLAST
    Regioni405 – 644240Interaction with THRABy similarityAdd
    BLAST
    Regioni542 – 789248Interaction with VDRBy similarityAdd
    BLAST
    Regioni622 – 70180Interaction with PPARGC1A and THRABy similarityAdd
    BLAST
    Regioni637 – 71680Interaction with GATA1Add
    BLAST
    Regioni656 – 1066411Interaction with ESR1By similarityAdd
    BLAST
    Regioni1251 – 1423173Interaction with TP53By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi604 – 6085LXXLL motif 1
    Motifi645 – 6495LXXLL motif 2

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1078 – 1484407Ser-richSequence AnalysisAdd
    BLAST
    Compositional biasi1498 – 152326Lys-richSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Mediator complex subunit 1 family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG12793.
    GeneTreeiENSGT00660000095569.
    HOVERGENiHBG101127.
    InParanoidiQ925J9.
    KOiK15144.
    OMAiPKHQTED.
    PhylomeDBiQ925J9.
    TreeFamiTF324954.

    Family and domain databases

    InterProiIPR019680. Mediator_Med1_met/fun.
    [Graphical view]
    PfamiPF10744. Med1. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q925J9-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MKAQGETEDS ERLSKMSSLL ERLHAKFNQN RPWSETIKLV RQVMEKRVVM     50
    SSGGHQHLVS CLETLQKALK VTSLPAMTDR LESIARQNGL GSHLSASGTE 100
    CYITSDMFYV EVQLDPAGQL CDVKVAHHGE NPVSCPELVQ QLREKNFEEF 150
    SKHLKGLVNL YNLPGDNKLK TKMYLALQSL EQDLSKMAIM YWKATNAAPL 200
    DKILHGSVGY LTPRSGGHLM NMKYYASPSD LLDDKTASPI ILHEKNVPRS 250
    LGMNASVTIE GTSAMYKLPI APLIMGSHPA DNKWTPSFSA VTSANSVDLP 300
    ACFFLKFPQP IPVSKAFVQK LQNCTGIPLF ETPPTYLPLY ELITQFELSK 350
    DPDPLPLNHN MRFYAALPGQ QHCYFLNKDA PLPDGQSLQG TLVSKITFQH 400
    PGRVPLILNM IRHQVAYNTL IGSCVKRTIL KEDSPGLLQF EVCPLSESRF 450
    SVSFQHPVND SLVCVVMDVQ DSTHVSCKLY KGLSDALICT DDFIAKVVQR 500
    CMSIPVTMRA IRRKAETIQA DTPALSLIAE TVEDMVKKNL PPASSPGYGM 550
    TTGNNPMSGT TTPTNTFPGG PITTLFNMSM SIKDRHESVG HGEDFSKVSQ 600
    NPILTSLLQI TGNGGSTIGS SPTPPHHTPP PVSSMAGNTK NHPMLMNLLK 650
    DNPAQDFSTL YGSSPLERQN SSSGSPRMEM CSGSNKAKKK KSSRVPPDKP 700
    KHQTEDDFQR ELFSMDVDSQ NPMFDVSMTA DALDTPHITP APSQCSTPPA 750
    TYPQPVSHPQ PSIQRMVRLS SSDSIGPDVT DILSDIAEEA SKLPSTSDDC 800
    PPIGTPVRDS SSSGHSQSAL FDSDVFQTNN NENPYTDPAD LIADAAGSPN 850
    SDSPTNHFFP DGVDFNPDLL NSQSQSGFGE EYFDESSQSG DNDDFKGFAS 900
    QALNTLGMPM LGGDNGEPKF KGSSQADTVD FSIISVAGKA LGAADLMEHH 950
    SGSQSPLLTT GELGKEKTQK RVKEGNGTGA SSGSGPGSDS KPGKRSRTPS 1000
    NDGKSKDKPP KRKKADTEGK SPSHSSSNRP FTPPTSTGGS KSPGSSGRSQ 1050
    TPPGVATPPI PKITIQIPKG TVMVGKPSSH SQYTSSGSVS SSGSKSHHSH 1100
    SSSSSSLASA STSGKVKSSK SEGSSSSKLS GSMYASQGSS GSSQSKNSSQ 1150
    TGGKPGSSPI TKHGLSSGSS STKMKPQGKP SSLMNPSISK PNISPSHSRP 1200
    PGGSDKLASP MKPVPGTPPS SKAKSPISSG SSGSHVSGTS SSSGMKSSSG 1250
    SASSGSVSQK TPPASNSCTP SSSSFSSSGS SMSSSQNQHG SSKGKSPSRN 1300
    KKPSLTAVID KLKHGVVTSG PGGEDPIDSQ MGASTNSSNH PMSSKHNTSG 1350
    GEFQSKREKS DKDKSKVSAS GGSVDSSKKT SESKNVGSTG VAKIIISKHD 1400
    GGSPSIKAKV TLQKPGESGG DGLRPQIASS KNYGSPLISG STPKHERGSP 1450
    SHSKSPAYTP QNVDSESESG SSIAERSYQN SPSSEDGIRP LPEYSTEKHK 1500
    KHKKEKKKVR DKDRDKKKSH SMKPENWSKS PISSDPTASV TNNPILSADR 1550
    PSRLSPDFMI GEEDDDLMDV ALIGN 1575

    Note: No experimental confirmation available.Curated

    Length:1,575
    Mass (Da):167,141
    Last modified:December 6, 2005 - v2
    Checksum:iC3B8121A26003A22
    GO
    Isoform 21 Publication (identifier: Q925J9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         548-632: YGMTTGNNPM...TPPHHTPPPV → VEEKRQDKPS...SDVQEYFSVS
         633-1575: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:632
    Mass (Da):70,473
    Checksum:i21A6BD89B50EA9F2
    GO
    Isoform 31 Publication (identifier: Q925J9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         548-556: YGMTTGNNP → SKNPELGSG
         557-1575: Missing.

    Show »
    Length:556
    Mass (Da):61,566
    Checksum:i4E8E3E79087D4B3A
    GO
    Isoform 42 Publications (identifier: Q925J9-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-15: Missing.

    Show »
    Length:1,560
    Mass (Da):165,450
    Checksum:iC1408AE8196A6C76
    GO

    Sequence cautioni

    The sequence AAH21440.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti84 – 841I → L in AAC31118. (PubMed:9325263)Curated
    Sequence conflicti198 – 1981A → T in AAH21440. (PubMed:15489334)Curated
    Sequence conflicti211 – 2111L → H in BAE27757. (PubMed:16141072)Curated
    Sequence conflicti303 – 3031F → S in AAC31118. (PubMed:9325263)Curated
    Sequence conflicti382 – 3898LPDGQSLQ → VLPNKAVS in BAC35779. (PubMed:16141072)Curated
    Sequence conflicti948 – 9481E → K in BAC33607. (PubMed:16141072)Curated
    Sequence conflicti964 – 9641G → A in BAC33607. (PubMed:16141072)Curated
    Sequence conflicti1323 – 13231G → S in AAC31118. (PubMed:9325263)Curated
    Sequence conflicti1387 – 13871G → R in AAC31118. (PubMed:9325263)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti960 – 9601T → S in strain: ISS and 129/Ola. 2 Publications
    Natural varianti1348 – 13481T → M in strain: ISS and 129/Ola. 2 Publications

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1515Missing in isoform 4. 2 PublicationsVSP_051892Add
    BLAST
    Alternative sequencei548 – 63285YGMTT…TPPPV → VEEKRQDKPSLGHLPPIQVC SPSCLKDGKDMKSTCTYLLL LLLLLEFMVFCFFFFFLTYS SVFGLHVKGLWTKICSDVQE YFSVS in isoform 2. 1 PublicationVSP_051893Add
    BLAST
    Alternative sequencei548 – 5569YGMTTGNNP → SKNPELGSG in isoform 3. 2 PublicationsVSP_051894
    Alternative sequencei557 – 15751019Missing in isoform 3. 2 PublicationsVSP_051895Add
    BLAST
    Alternative sequencei633 – 1575943Missing in isoform 2. 1 PublicationVSP_051896Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF000294 mRNA. Translation: AAC31118.1.
    AF332073 mRNA. Translation: AAK56101.1.
    AF332074 mRNA. Translation: AAK56102.1.
    AY176046 Genomic DNA. Translation: AAN75014.1.
    AK049203 mRNA. Translation: BAC33607.2.
    AK054437 mRNA. Translation: BAC35779.2.
    AK147199 mRNA. Translation: BAE27757.1.
    AL591205 Genomic DNA. Translation: CAM21264.1.
    AL591205 Genomic DNA. Translation: CAM21266.1.
    BC021440 mRNA. Translation: AAH21440.1. Different initiation.
    BC079636 mRNA. Translation: AAH79636.1.
    CCDSiCCDS25341.1. [Q925J9-4]
    CCDS36300.1. [Q925J9-1]
    PIRiT02885.
    RefSeqiNP_001073587.1. NM_001080118.1. [Q925J9-1]
    NP_038662.2. NM_013634.2. [Q925J9-4]
    NP_598788.2. NM_134027.2. [Q925J9-3]
    UniGeneiMm.12926.

    Genome annotation databases

    EnsembliENSMUST00000018304; ENSMUSP00000018304; ENSMUSG00000018160. [Q925J9-4]
    ENSMUST00000107545; ENSMUSP00000103169; ENSMUSG00000018160. [Q925J9-1]
    GeneIDi19014.
    KEGGimmu:19014.
    UCSCiuc007lfo.1. mouse. [Q925J9-3]
    uc007lfp.1. mouse. [Q925J9-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF000294 mRNA. Translation: AAC31118.1 .
    AF332073 mRNA. Translation: AAK56101.1 .
    AF332074 mRNA. Translation: AAK56102.1 .
    AY176046 Genomic DNA. Translation: AAN75014.1 .
    AK049203 mRNA. Translation: BAC33607.2 .
    AK054437 mRNA. Translation: BAC35779.2 .
    AK147199 mRNA. Translation: BAE27757.1 .
    AL591205 Genomic DNA. Translation: CAM21264.1 .
    AL591205 Genomic DNA. Translation: CAM21266.1 .
    BC021440 mRNA. Translation: AAH21440.1 . Different initiation.
    BC079636 mRNA. Translation: AAH79636.1 .
    CCDSi CCDS25341.1. [Q925J9-4 ]
    CCDS36300.1. [Q925J9-1 ]
    PIRi T02885.
    RefSeqi NP_001073587.1. NM_001080118.1. [Q925J9-1 ]
    NP_038662.2. NM_013634.2. [Q925J9-4 ]
    NP_598788.2. NM_134027.2. [Q925J9-3 ]
    UniGenei Mm.12926.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XDK X-ray 2.90 C/D/G/H 641-654 [» ]
    ProteinModelPortali Q925J9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202318. 5 interactions.
    DIPi DIP-59232N.
    IntActi Q925J9. 8 interactions.
    MINTi MINT-4123213.

    PTM databases

    PhosphoSitei Q925J9.

    Proteomic databases

    MaxQBi Q925J9.
    PaxDbi Q925J9.
    PRIDEi Q925J9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000018304 ; ENSMUSP00000018304 ; ENSMUSG00000018160 . [Q925J9-4 ]
    ENSMUST00000107545 ; ENSMUSP00000103169 ; ENSMUSG00000018160 . [Q925J9-1 ]
    GeneIDi 19014.
    KEGGi mmu:19014.
    UCSCi uc007lfo.1. mouse. [Q925J9-3 ]
    uc007lfp.1. mouse. [Q925J9-1 ]

    Organism-specific databases

    CTDi 5469.
    MGIi MGI:1100846. Med1.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00660000095569.
    HOVERGENi HBG101127.
    InParanoidi Q925J9.
    KOi K15144.
    OMAi PKHQTED.
    PhylomeDBi Q925J9.
    TreeFami TF324954.

    Enzyme and pathway databases

    Reactomei REACT_118837. Rora activates circadian gene expression.
    REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_198351. RORA activates circadian gene expression.
    REACT_198352. REV-ERBA represses gene expression.
    REACT_198602. PPARA activates gene expression.
    REACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_205251. Transcriptional activation of mitochondrial biogenesis.
    REACT_206529. Generic Transcription Pathway.
    REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

    Miscellaneous databases

    EvolutionaryTracei Q925J9.
    NextBioi 295432.
    PROi Q925J9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q925J9.
    Bgeei Q925J9.
    CleanExi MM_MED1.
    Genevestigatori Q925J9.

    Family and domain databases

    InterProi IPR019680. Mediator_Med1_met/fun.
    [Graphical view ]
    Pfami PF10744. Med1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor."
      Zhu Y., Qi C., Jain S., Rao M.S., Reddy J.K.
      J. Biol. Chem. 272:25500-25506(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH PPARA; PPARG; RARA; RXRA AND THRB.
      Tissue: Liver1 Publication.
    2. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
      Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
      Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANTS SER-960 AND MET-1348.
      Strain: ILSImported and ISSImported.
    3. "The thyroid hormone receptor-associated protein TRAP220 is required at distinct embryonic stages in placental, cardiac, and hepatic development."
      Landles C., Chalk S., Steel J.H., Rosewell I., Spencer-Dene B., Lalani E.-N., Parker M.G.
      Mol. Endocrinol. 17:2418-2435(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANTS SER-960 AND MET-1348.
      Strain: 129/OlaImported.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-389 (ISOFORMS 1/4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-964 (ISOFORM 1).
      Strain: C57BL/6JImported.
      Tissue: Embryonic stem cell1 Publication and OvaryImported.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
      Strain: C57BL/6Imported and Czech IIImported.
      Tissue: Brain1 Publication and Mammary gland1 Publication.
    7. "Involvement of the TRAP220 component of the TRAP/SMCC coactivator complex in embryonic development and thyroid hormone action."
      Ito M., Yuan C.-X., Okano H.J., Darnell R.B., Roeder R.G.
      Mol. Cell 5:683-693(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE.
    8. "Regulation of glucocorticoid receptor activity by 14-3-3-dependent intracellular relocalization of the corepressor RIP140."
      Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E., Gustafsson J.-A.
      Mol. Endocrinol. 15:501-511(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YWHAH.
    9. "Transcription coactivator TRAP220 is required for PPAR gamma 2-stimulated adipogenesis."
      Ge K., Guermah M., Yuan C.-X., Ito M., Wallberg A.E., Spiegelman B.M., Roeder R.G.
      Nature 417:563-567(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "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."
      Kang Y.K., Guermah M., Yuan C.-X., Roeder R.G.
      Proc. Natl. Acad. Sci. U.S.A. 99:2642-2647(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION OF THE MEDIATOR COMPLEX WITH ESR1 AND ESR2.
    11. "Coordination of p300-mediated chromatin remodeling and TRAP/mediator function through coactivator PGC-1alpha."
      Wallberg A.E., Yamamura S., Malik S., Spiegelman B.M., Roeder R.G.
      Mol. Cell 12:1137-1149(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PPARGC1A.
    12. "Transcription coactivator PBP, the peroxisome proliferator-activated receptor (PPAR)-binding protein, is required for PPARalpha-regulated gene expression in liver."
      Jia Y., Qi C., Kashireddy P., Surapureddi S., Zhu Y.-J., Rao M.S., Le Roith D., Chambon P., Gonzalez F.J., Reddy J.K.
      J. Biol. Chem. 279:24427-24434(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "Structural and functional organization of TRAP220, the TRAP/mediator subunit that is targeted by nuclear receptors."
      Malik S., Guermah M., Yuan C.-X., Wu W., Yamamura S., Roeder R.G.
      Mol. Cell. Biol. 24:8244-8254(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION OF THE MEDIATOR COMPLEX WITH THRA.
    14. "Thyroid hormone-induced juxtaposition of regulatory elements/factors and chromatin remodeling of Crabp1 dependent on MED1/TRAP220."
      Park S.W., Li G., Lin Y.-P., Barrero M.J., Ge K., Roeder R.G., Wei L.-N.
      Mol. Cell 19:643-653(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ASSOCIATION WITH PROMOTER REGIONS.
    15. "The mediator complex functions as a coactivator for GATA-1 in erythropoiesis via subunit Med1/TRAP220."
      Stumpf M., Waskow C., Kroetschel M., van Essen D., Rodriguez P., Zhang X., Guyot B., Roeder R.G., Borggrefe T.
      Proc. Natl. Acad. Sci. U.S.A. 103:18504-18509(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GATA1, ASSOCIATION WITH PROMOTER REGIONS.
    16. Erratum
      Stumpf M., Waskow C., Kroetschel M., van Essen D., Rodriguez P., Zhang X., Guyot B., Roeder R.G., Borggrefe T.
      Proc. Natl. Acad. Sci. U.S.A. 104:1442-1442(2007)
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-953 AND SER-955, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    18. "Characterization of the interaction between retinoic acid receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional coactivators through structural and fluorescence anisotropy studies."
      Pogenberg V., Guichou J.F., Vivat-Hannah V., Kammerer S., Perez E., Germain P., de Lera A.R., Gronemeyer H., Royer C.A., Bourguet W.
      J. Biol. Chem. 280:1625-1633(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 641-654 IN COMPLEX WITH RARB AND RXRA.

    Entry informationi

    Entry nameiMED1_MOUSE
    AccessioniPrimary (citable) accession number: Q925J9
    Secondary accession number(s): A2A526
    , A2A528, O88323, Q3UHV0, Q6AXD5, Q8BW37, Q8BX19, Q8VDQ7, Q925K0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3