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Q925J9

- MED1_MOUSE

UniProt

Q925J9 - MED1_MOUSE

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Protein
Mediator of RNA polymerase II transcription subunit 1
Gene
Med1, Crsp210, Drip205, Pbp, Pparbp, Trap220, Trip2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. DNA binding Source: MGI
  2. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  3. RNA polymerase II transcription cofactor activity Source: UniProtKB
  4. chromatin DNA binding Source: Ensembl
  5. chromatin binding Source: MGI
  6. core promoter binding Source: UniProtKB
  7. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  8. nuclear hormone receptor binding Source: UniProtKB
  9. protein binding Source: UniProtKB
  10. protein complex binding Source: MGI
  11. receptor 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
Complete GO annotation...

GO - Biological processi

  1. ERK1 and ERK2 cascade Source: Ensembl
  2. androgen biosynthetic process Source: UniProtKB
  3. androgen receptor signaling pathway Source: UniProtKB
  4. angiogenesis Source: BHF-UCL
  5. brain development Source: MGI
  6. camera-type eye development Source: MGI
  7. cell morphogenesis Source: UniProtKB
  8. cellular response to epidermal growth factor stimulus Source: UniProtKB
  9. cellular response to hepatocyte growth factor stimulus Source: MGI
  10. cellular response to steroid hormone stimulus Source: Ensembl
  11. cellular response to thyroid hormone stimulus Source: Ensembl
  12. embryonic heart tube development Source: MGI
  13. embryonic hemopoiesis Source: MGI
  14. embryonic hindlimb morphogenesis Source: MGI
  15. embryonic placenta development Source: MGI
  16. enucleate erythrocyte development Source: MGI
  17. epithelial cell proliferation involved in mammary gland duct elongation Source: MGI
  18. erythrocyte development Source: BHF-UCL
  19. fat cell differentiation Source: MGI
  20. heart development Source: MGI
  21. in utero embryonic development Source: MGI
  22. intracellular steroid hormone receptor signaling pathway Source: UniProtKB
  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. mRNA transcription from RNA polymerase II promoter Source: UniProtKB
  28. mammary gland branching involved in pregnancy Source: MGI
  29. mammary gland branching involved in thelarche Source: MGI
  30. mammary gland epithelial cell proliferation Source: MGI
  31. megakaryocyte development Source: BHF-UCL
  32. monocyte differentiation Source: MGI
  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 G0 to G1 transition Source: MGI
  42. positive regulation of cell proliferation 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 from RNA polymerase I promoter Source: UniProtKB
  53. regulation of transcription, DNA-templated Source: MGI
  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
Complete GO annotation...

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

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
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei664 – 6641Phosphoserine By similarity
Modified residuei795 – 7951Phosphoserine By similarity
Modified residuei805 – 8051Phosphothreonine By similarityBy similarity
Modified residuei953 – 9531Phosphoserine1 Publication
Modified residuei955 – 9551Phosphoserine1 Publication
Modified residuei1032 – 10321Phosphothreonine; by MAPK1 or MAPK3 By similarity
Modified residuei1051 – 10511Phosphothreonine By similarityBy similarity
Modified residuei1057 – 10571Phosphothreonine By similarity
Modified residuei1158 – 11581Phosphoserine By similarity
Modified residuei1179 – 11791N6-acetyllysine By similarity
Modified residuei1209 – 12091Phosphoserine By similarity
Modified residuei1217 – 12171Phosphothreonine By similarity
Modified residuei1225 – 12251Phosphoserine By similarity
Modified residuei1349 – 13491Phosphoserine By similarity
Modified residuei1405 – 14051Phosphoserine By similarity
Modified residuei1435 – 14351Phosphoserine By similarity
Modified residuei1459 – 14591Phosphothreonine; by MAPK1 or MAPK3 By similarity
Modified residuei1465 – 14651Phosphoserine By similarity
Modified residuei1481 – 14811Phosphoserine By similarity
Modified residuei1483 – 14831Phosphoserine By similarity
Modified residuei1484 – 14841Phosphoserine By similarity
Modified residuei1523 – 15231N6-acetyllysine By 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.6 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ925J9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 670670Interaction with the Mediator complex and THRA By similarity
Add
BLAST
Regioni16 – 590575Interaction with ESR1 By similarity
Add
BLAST
Regioni108 – 212105Interaction with the Mediator complex By similarity
Add
BLAST
Regioni215 – 390176Interaction with the Mediator complex By similarity
Add
BLAST
Regioni405 – 644240Interaction with THRA By similarity
Add
BLAST
Regioni542 – 789248Interaction with VDR By similarity
Add
BLAST
Regioni622 – 70180Interaction with PPARGC1A and THRA By similarity
Add
BLAST
Regioni637 – 71680Interaction with GATA1
Add
BLAST
Regioni656 – 1066411Interaction with ESR1 By similarity
Add
BLAST
Regioni1251 – 1423173Interaction with TP53 By similarity
Add
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-rich
Add
BLAST
Compositional biasi1498 – 152326Lys-rich
Add
BLAST

Sequence similaritiesi

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.

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.

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.

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 Publications
VSP_051892Add
BLAST
Alternative sequencei548 – 63285YGMTT…TPPPV → VEEKRQDKPSLGHLPPIQVC SPSCLKDGKDMKSTCTYLLL LLLLLEFMVFCFFFFFLTYS SVFGLHVKGLWTKICSDVQE YFSVS in isoform 2. 1 Publication
VSP_051893Add
BLAST
Alternative sequencei548 – 5569YGMTTGNNP → SKNPELGSG in isoform 3. 2 Publications
VSP_051894
Alternative sequencei557 – 15751019Missing in isoform 3. 2 Publications
VSP_051895Add
BLAST
Alternative sequencei633 – 1575943Missing in isoform 2. 1 Publication
VSP_051896Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841I → L in AAC31118. 1 Publication
Sequence conflicti198 – 1981A → T in AAH21440. 1 Publication
Sequence conflicti211 – 2111L → H in BAE27757. 1 Publication
Sequence conflicti303 – 3031F → S in AAC31118. 1 Publication
Sequence conflicti382 – 3898LPDGQSLQ → VLPNKAVS in BAC35779. 1 Publication
Sequence conflicti948 – 9481E → K in BAC33607. 1 Publication
Sequence conflicti964 – 9641G → A in BAC33607. 1 Publication
Sequence conflicti1323 – 13231G → S in AAC31118. 1 Publication
Sequence conflicti1387 – 13871G → R in AAC31118. 1 Publication

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...

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

« Hide 'large scale' publications
  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: Liver.
  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: ILS and ISS.
  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/Ola.
  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/6J.
    Tissue: Embryonic stem cell and Ovary.
  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/6 and Czech II.
    Tissue: Brain and Mammary gland.
  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: September 3, 2014
This is version 106 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

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