Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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
  • animal organ morphogenesis Source: MGI
  • animal organ regeneration Source: MGI
  • 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 organism 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
  • 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

ReactomeiR-MMU-212436. Generic Transcription Pathway.
R-MMU-381340. Transcriptional regulation of white adipocyte differentiation.
R-MMU-383280. Nuclear Receptor transcription pathway.
R-MMU-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
R-MMU-442533. 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
Proteomesi
  • UP000000589 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)DescriptionActionsGraphical viewLength
ChainiPRO_00000585531 – 1575Mediator of RNA polymerase II transcription subunit 1Add BLAST1575

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei588PhosphoserineBy similarity1
Modified residuei664PhosphoserineCombined sources1
Modified residuei795PhosphoserineBy similarity1
Modified residuei805PhosphothreonineCombined sources1
Modified residuei953PhosphoserineCombined sources1
Modified residuei955PhosphoserineCombined sources1
Modified residuei1032Phosphothreonine; by MAPK1 or MAPK3By similarity1
Modified residuei1051PhosphothreonineCombined sources1
Modified residuei1057PhosphothreonineCombined sources1
Modified residuei1158PhosphoserineCombined sources1
Modified residuei1179N6-acetyllysineBy similarity1
Modified residuei1209PhosphoserineCombined sources1
Modified residuei1217PhosphothreonineBy similarity1
Modified residuei1225PhosphoserineBy similarity1
Modified residuei1304PhosphoserineBy similarity1
Modified residuei1349PhosphoserineBy similarity1
Modified residuei1405PhosphoserineBy similarity1
Modified residuei1435PhosphoserineCombined sources1
Modified residuei1442PhosphothreonineCombined sources1
Modified residuei1459Phosphothreonine; by MAPK1 or MAPK3By similarity1
Modified residuei1465PhosphoserineCombined sources1
Modified residuei1467PhosphoserineCombined sources1
Modified residuei1481PhosphoserineCombined sources1
Modified residuei1483PhosphoserineBy similarity1
Modified residuei1484PhosphoserineCombined sources1
Modified residuei1523N6-acetyllysineBy similarity1

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

EPDiQ925J9.
PaxDbiQ925J9.
PeptideAtlasiQ925J9.
PRIDEiQ925J9.

PTM databases

iPTMnetiQ925J9.
PhosphoSitePlusiQ925J9.

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

BgeeiENSMUSG00000018160.
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). Interacts with NR4A3 (PubMed:12709428).By similarity9 Publications

GO - Molecular functioni

Protein-protein interaction databases

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

Structurei

Secondary structure

11575
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi643 – 649Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XDKX-ray2.90C/D/G/H641-654[»]
ProteinModelPortaliQ925J9.
SMRiQ925J9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ925J9.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 670Interaction with the Mediator complex and THRABy similarityAdd BLAST670
Regioni16 – 590Interaction with ESR1By similarityAdd BLAST575
Regioni108 – 212Interaction with the Mediator complexBy similarityAdd BLAST105
Regioni215 – 390Interaction with the Mediator complexBy similarityAdd BLAST176
Regioni405 – 644Interaction with THRABy similarityAdd BLAST240
Regioni542 – 789Interaction with VDRBy similarityAdd BLAST248
Regioni622 – 701Interaction with GATA11 PublicationAdd BLAST80
Regioni622 – 701Interaction with PPARGC1A and THRABy similarityAdd BLAST80
Regioni656 – 1066Interaction with ESR1By similarityAdd BLAST411
Regioni1251 – 1423Interaction with TP53By similarityAdd BLAST173

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi604 – 608LXXLL motif 15
Motifi645 – 649LXXLL motif 25

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1078 – 1484Ser-richSequence analysisAdd BLAST407
Compositional biasi1498 – 1523Lys-richSequence analysisAdd BLAST26

Sequence similaritiesi

Belongs to the Mediator complex subunit 1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IEFR. Eukaryota.
ENOG410XR2E. LUCA.
GeneTreeiENSGT00660000095569.
HOVERGENiHBG101127.
InParanoidiQ925J9.
KOiK15144.
OMAiHGEDFSK.
OrthoDBiEOG091G035E.
PhylomeDBiQ925J9.
TreeFamiTF324954.

Family and domain databases

InterProiIPR019680. Mediator_Med1.
[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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti84I → L in AAC31118 (PubMed:9325263).Curated1
Sequence conflicti198A → T in AAH21440 (PubMed:15489334).Curated1
Sequence conflicti211L → H in BAE27757 (PubMed:16141072).Curated1
Sequence conflicti303F → S in AAC31118 (PubMed:9325263).Curated1
Sequence conflicti382 – 389LPDGQSLQ → VLPNKAVS in BAC35779 (PubMed:16141072).Curated8
Sequence conflicti948E → K in BAC33607 (PubMed:16141072).Curated1
Sequence conflicti964G → A in BAC33607 (PubMed:16141072).Curated1
Sequence conflicti1323G → S in AAC31118 (PubMed:9325263).Curated1
Sequence conflicti1387G → R in AAC31118 (PubMed:9325263).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti960T → S in strain: ISS and 129/Ola. 2 Publications1
Natural varianti1348T → M in strain: ISS and 129/Ola. 2 Publications1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0518921 – 15Missing in isoform 4. 2 PublicationsAdd BLAST15
Alternative sequenceiVSP_051893548 – 632YGMTT…TPPPV → VEEKRQDKPSLGHLPPIQVC SPSCLKDGKDMKSTCTYLLL LLLLLEFMVFCFFFFFLTYS SVFGLHVKGLWTKICSDVQE YFSVS in isoform 2. 1 PublicationAdd BLAST85
Alternative sequenceiVSP_051894548 – 556YGMTTGNNP → SKNPELGSG in isoform 3. 2 Publications9
Alternative sequenceiVSP_051895557 – 1575Missing in isoform 3. 2 PublicationsAdd BLAST1019
Alternative sequenceiVSP_051896633 – 1575Missing in isoform 2. 1 PublicationAdd BLAST943

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XDKX-ray2.90C/D/G/H641-654[»]
ProteinModelPortaliQ925J9.
SMRiQ925J9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ925J9.
PhosphoSitePlusiQ925J9.

Proteomic databases

EPDiQ925J9.
PaxDbiQ925J9.
PeptideAtlasiQ925J9.
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

eggNOGiENOG410IEFR. Eukaryota.
ENOG410XR2E. LUCA.
GeneTreeiENSGT00660000095569.
HOVERGENiHBG101127.
InParanoidiQ925J9.
KOiK15144.
OMAiHGEDFSK.
OrthoDBiEOG091G035E.
PhylomeDBiQ925J9.
TreeFamiTF324954.

Enzyme and pathway databases

ReactomeiR-MMU-212436. Generic Transcription Pathway.
R-MMU-381340. Transcriptional regulation of white adipocyte differentiation.
R-MMU-383280. Nuclear Receptor transcription pathway.
R-MMU-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
R-MMU-442533. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Miscellaneous databases

EvolutionaryTraceiQ925J9.
PROiQ925J9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000018160.
CleanExiMM_MED1.
ExpressionAtlasiQ925J9. baseline and differential.
GenevisibleiQ925J9. MM.

Family and domain databases

InterProiIPR019680. Mediator_Med1.
[Graphical view]
PfamiPF10744. Med1. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 129 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

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 one 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.