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Protein

Mediator of RNA polymerase II transcription subunit 1

Gene

Med1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (By similarity).By similarity10 Publications

GO - Molecular functioni

GO - Biological processi

  • androgen biosynthetic process Source: UniProtKB
  • androgen receptor signaling pathway Source: UniProtKB
  • angiogenesis Source: BHF-UCL
  • brain development Source: MGI
  • camera-type eye development Source: MGI
  • cell morphogenesis Source: UniProtKB
  • cellular response to epidermal growth factor stimulus Source: UniProtKB
  • cellular response to hepatocyte growth factor stimulus Source: MGI
  • cellular response to steroid hormone stimulus Source: MGI
  • cellular response to thyroid hormone stimulus Source: MGI
  • embryonic heart tube development Source: MGI
  • embryonic hemopoiesis Source: MGI
  • embryonic hindlimb morphogenesis Source: MGI
  • embryonic placenta development Source: MGI
  • enucleate erythrocyte development Source: MGI
  • epithelial cell proliferation involved in mammary gland duct elongation Source: MGI
  • ERK1 and ERK2 cascade Source: MGI
  • erythrocyte development Source: BHF-UCL
  • fat cell differentiation Source: MGI
  • heart development Source: MGI
  • intracellular steroid hormone receptor signaling pathway Source: UniProtKB
  • in utero embryonic development Source: MGI
  • keratinocyte differentiation Source: UniProtKB
  • lactation Source: MGI
  • lens development in camera-type eye Source: BHF-UCL
  • liver development Source: MGI
  • mammary gland branching involved in pregnancy Source: MGI
  • mammary gland branching involved in thelarche Source: MGI
  • mammary gland epithelial cell proliferation Source: MGI
  • megakaryocyte development Source: BHF-UCL
  • monocyte differentiation Source: MGI
  • mRNA transcription from RNA polymerase II promoter Source: UniProtKB
  • multicellular organismal development Source: MGI
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of keratinocyte proliferation Source: UniProtKB
  • negative regulation of neuron differentiation Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • organ morphogenesis Source: MGI
  • organ regeneration Source: MGI
  • peroxisome proliferator activated receptor signaling pathway Source: MGI
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of erythrocyte differentiation Source: UniProtKB
  • positive regulation of G0 to G1 transition Source: MGI
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of hepatocyte proliferation Source: MGI
  • positive regulation of interferon-gamma-mediated signaling pathway Source: MGI
  • positive regulation of intracellular estrogen receptor signaling pathway Source: MGI
  • positive regulation of keratinocyte differentiation Source: UniProtKB
  • positive regulation of mammary gland epithelial cell proliferation Source: MGI
  • positive regulation of protein import into nucleus, translocation Source: MGI
  • positive regulation of receptor activity Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • regulation of RNA biosynthetic process Source: UniProtKB
  • regulation of transcription, DNA-templated Source: MGI
  • regulation of transcription from RNA polymerase I promoter Source: UniProtKB
  • regulation of vitamin D receptor signaling pathway Source: MGI
  • retinal pigment epithelium development Source: BHF-UCL
  • thyroid hormone generation Source: MGI
  • thyroid hormone mediated signaling pathway Source: UniProtKB
  • transcription from RNA polymerase II promoter Source: MGI
  • transcription initiation from RNA polymerase II promoter Source: UniProtKB
  • 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_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
REACT_275829. Generic Transcription Pathway.
REACT_276696. Nuclear Receptor transcription pathway.
REACT_309805. Transcriptional regulation of white adipocyte differentiation.
REACT_332733. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).

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 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1100846. Med1.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: Ensembl
  • mediator complex Source: MGI
  • membrane Source: MGI
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • protein-DNA complex Source: Ensembl
  • ubiquitin ligase 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 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

BgeeiQ925J9.
CleanExiMM_MED1.
ExpressionAtlasiQ925J9. baseline and differential.
GenevisibleiQ925J9. MM.

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. Interacts with CLOCK; this interaction requires the presence of THRAP3. Interacts with CCAR1 (By similarity).By similarity8 Publications

Protein-protein interaction databases

BioGridi202318. 5 interactions.
DIPiDIP-59232N.
IntActiQ925J9. 8 interactions.
MINTiMINT-4123213.
STRINGi10090.ENSMUSP00000103169.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 GATA11 PublicationAdd
BLAST
Regioni622 – 70180Interaction with PPARGC1A and THRABy similarityAdd
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.
OMAiHGEDFSK.
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. AlignAdd to basket

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

        10         20         30         40         50
MKAQGETEDS ERLSKMSSLL ERLHAKFNQN RPWSETIKLV RQVMEKRVVM
60 70 80 90 100
SSGGHQHLVS CLETLQKALK VTSLPAMTDR LESIARQNGL GSHLSASGTE
110 120 130 140 150
CYITSDMFYV EVQLDPAGQL CDVKVAHHGE NPVSCPELVQ QLREKNFEEF
160 170 180 190 200
SKHLKGLVNL YNLPGDNKLK TKMYLALQSL EQDLSKMAIM YWKATNAAPL
210 220 230 240 250
DKILHGSVGY LTPRSGGHLM NMKYYASPSD LLDDKTASPI ILHEKNVPRS
260 270 280 290 300
LGMNASVTIE GTSAMYKLPI APLIMGSHPA DNKWTPSFSA VTSANSVDLP
310 320 330 340 350
ACFFLKFPQP IPVSKAFVQK LQNCTGIPLF ETPPTYLPLY ELITQFELSK
360 370 380 390 400
DPDPLPLNHN MRFYAALPGQ QHCYFLNKDA PLPDGQSLQG TLVSKITFQH
410 420 430 440 450
PGRVPLILNM IRHQVAYNTL IGSCVKRTIL KEDSPGLLQF EVCPLSESRF
460 470 480 490 500
SVSFQHPVND SLVCVVMDVQ DSTHVSCKLY KGLSDALICT DDFIAKVVQR
510 520 530 540 550
CMSIPVTMRA IRRKAETIQA DTPALSLIAE TVEDMVKKNL PPASSPGYGM
560 570 580 590 600
TTGNNPMSGT TTPTNTFPGG PITTLFNMSM SIKDRHESVG HGEDFSKVSQ
610 620 630 640 650
NPILTSLLQI TGNGGSTIGS SPTPPHHTPP PVSSMAGNTK NHPMLMNLLK
660 670 680 690 700
DNPAQDFSTL YGSSPLERQN SSSGSPRMEM CSGSNKAKKK KSSRVPPDKP
710 720 730 740 750
KHQTEDDFQR ELFSMDVDSQ NPMFDVSMTA DALDTPHITP APSQCSTPPA
760 770 780 790 800
TYPQPVSHPQ PSIQRMVRLS SSDSIGPDVT DILSDIAEEA SKLPSTSDDC
810 820 830 840 850
PPIGTPVRDS SSSGHSQSAL FDSDVFQTNN NENPYTDPAD LIADAAGSPN
860 870 880 890 900
SDSPTNHFFP DGVDFNPDLL NSQSQSGFGE EYFDESSQSG DNDDFKGFAS
910 920 930 940 950
QALNTLGMPM LGGDNGEPKF KGSSQADTVD FSIISVAGKA LGAADLMEHH
960 970 980 990 1000
SGSQSPLLTT GELGKEKTQK RVKEGNGTGA SSGSGPGSDS KPGKRSRTPS
1010 1020 1030 1040 1050
NDGKSKDKPP KRKKADTEGK SPSHSSSNRP FTPPTSTGGS KSPGSSGRSQ
1060 1070 1080 1090 1100
TPPGVATPPI PKITIQIPKG TVMVGKPSSH SQYTSSGSVS SSGSKSHHSH
1110 1120 1130 1140 1150
SSSSSSLASA STSGKVKSSK SEGSSSSKLS GSMYASQGSS GSSQSKNSSQ
1160 1170 1180 1190 1200
TGGKPGSSPI TKHGLSSGSS STKMKPQGKP SSLMNPSISK PNISPSHSRP
1210 1220 1230 1240 1250
PGGSDKLASP MKPVPGTPPS SKAKSPISSG SSGSHVSGTS SSSGMKSSSG
1260 1270 1280 1290 1300
SASSGSVSQK TPPASNSCTP SSSSFSSSGS SMSSSQNQHG SSKGKSPSRN
1310 1320 1330 1340 1350
KKPSLTAVID KLKHGVVTSG PGGEDPIDSQ MGASTNSSNH PMSSKHNTSG
1360 1370 1380 1390 1400
GEFQSKREKS DKDKSKVSAS GGSVDSSKKT SESKNVGSTG VAKIIISKHD
1410 1420 1430 1440 1450
GGSPSIKAKV TLQKPGESGG DGLRPQIASS KNYGSPLISG STPKHERGSP
1460 1470 1480 1490 1500
SHSKSPAYTP QNVDSESESG SSIAERSYQN SPSSEDGIRP LPEYSTEKHK
1510 1520 1530 1540 1550
KHKKEKKKVR DKDRDKKKSH SMKPENWSKS PISSDPTASV TNNPILSADR
1560 1570
PSRLSPDFMI GEEDDDLMDV ALIGN
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi202318. 5 interactions.
DIPiDIP-59232N.
IntActiQ925J9. 8 interactions.
MINTiMINT-4123213.
STRINGi10090.ENSMUSP00000103169.

PTM databases

PhosphoSiteiQ925J9.

Proteomic databases

MaxQBiQ925J9.
PaxDbiQ925J9.
PRIDEiQ925J9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi5469.
MGIiMGI:1100846. Med1.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
REACT_275829. Generic Transcription Pathway.
REACT_276696. Nuclear Receptor transcription pathway.
REACT_309805. Transcriptional regulation of white adipocyte differentiation.
REACT_332733. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).

Miscellaneous databases

EvolutionaryTraceiQ925J9.
NextBioi295432.
PROiQ925J9.
SOURCEiSearch...

Gene expression databases

BgeeiQ925J9.
CleanExiMM_MED1.
ExpressionAtlasiQ925J9. baseline and differential.
GenevisibleiQ925J9. MM.

Family and domain databases

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

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: 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. "A positive feedback loop links circadian clock factor CLOCK-BMAL1 to the basic transcriptional machinery."
    Lande-Diner L., Boyault C., Kim J.Y., Weitz C.J.
    Proc. Natl. Acad. Sci. U.S.A. 110:16021-16026(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLOCK.
  19. "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: July 22, 2015
This is version 116 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.