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Protein

Mediator of RNA polymerase II transcription subunit 1

Gene

MED1

Organism
Homo sapiens (Human)
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 (PubMed:10406464, PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447, PubMed:14636573, PubMed:15340084, PubMed:15471764, PubMed:15989967, PubMed:16574658, PubMed:9653119). Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781).12 Publications

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • chromatin DNA binding Source: Ensembl
  • core promoter binding Source: UniProtKB
  • estrogen receptor binding Source: UniProtKB
  • LBD domain binding Source: UniProtKB
  • ligand-dependent nuclear receptor binding Source: UniProtKB
  • ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  • mediator complex binding Source: UniProtKB
  • nuclear hormone receptor binding Source: UniProtKB
  • peroxisome proliferator activated receptor binding Source: UniProtKB
  • receptor activity Source: UniProtKB
  • retinoic acid receptor binding Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  • RNA polymerase II transcription cofactor activity Source: UniProtKB
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • thyroid hormone receptor binding Source: UniProtKB
  • thyroid hormone receptor coactivator activity Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB
  • transcription cofactor activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • ubiquitin protein ligase activity Source: Ensembl
  • vitamin D receptor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-1368082. RORA activates gene expression.
R-HSA-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-HSA-1989781. PPARA activates gene expression.
R-HSA-2032785. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
R-HSA-212436. Generic Transcription Pathway.
R-HSA-2151201. Transcriptional activation of mitochondrial biogenesis.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
R-HSA-383280. Nuclear Receptor transcription pathway.
R-HSA-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
R-HSA-400253. Circadian Clock.
SignaLinkiQ15648.
SIGNORiQ15648.

Names & Taxonomyi

Protein namesi
Recommended name:
Mediator of RNA polymerase II transcription subunit 1
Alternative name(s):
Activator-recruited cofactor 205 kDa component
Short name:
ARC205
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
Vitamin D receptor-interacting protein complex component DRIP205
p53 regulatory protein RB18A
Gene namesi
Name:MED1
Synonyms:ARC205, CRSP1, CRSP200, DRIP205, DRIP230, PBP, PPARBP, PPARGBP, RB18A, TRAP220, TRIP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:9234. MED1.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: Ensembl
  • mediator complex Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • protein-DNA complex Source: Ensembl
  • ubiquitin ligase complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi599 – 61214SQNPI…LQITG → EKHKILHRLLQDSS: Enhances interaction with ESR1. 1 PublicationAdd
BLAST
Mutagenesisi600 – 61213QNPIL…LQITG → RHKILHRLLQEGS: Enhances interaction with ESR1. 1 PublicationAdd
BLAST
Mutagenesisi604 – 6041L → A: Impairs interaction with ESR2; when associated with A-607; A-645 and A-648. 1 Publication
Mutagenesisi607 – 6082LL → AA: Impairs interaction with ESR1, PPARG, RXRA and THRB. Impairs interaction with THRA; when associated with 648-A-A-649. 6 Publications
Mutagenesisi607 – 6071L → A: Impairs interaction with ESR2; when associated with A-604; A-645 and A-648. 1 Publication
Mutagenesisi639 – 65315TKNHP…LKDNP → VSRHKILHRLLQEGS: Enhances interaction with ESR1. 1 PublicationAdd
BLAST
Mutagenesisi645 – 6451L → A: Impairs interaction with ESR2; when associated with A-604; A-607 and A-648. 1 Publication
Mutagenesisi648 – 6492LL → AA: Impairs interaction with ESR1, PPARG, THRB and VDR. Impairs interaction with THRA; when associated with 607-A-A-608. 6 Publications
Mutagenesisi648 – 6481L → A: Impairs interaction with ESR2; when associated with A-604; A-607 and A-645. 1 Publication
Mutagenesisi1032 – 10321T → A: Enhances protein stability; when associated with A-1457. 1 Publication
Mutagenesisi1457 – 14571T → A: Enhances protein stability; when associated with A-1032. 1 Publication

Organism-specific databases

PharmGKBiPA33556.

Polymorphism and mutation databases

BioMutaiMED1.
DMDMi158518535.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15811581Mediator of RNA polymerase II transcription subunit 1PRO_0000058552Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei588 – 5881PhosphoserineCombined sources
Modified residuei664 – 6641PhosphoserineCombined sources
Modified residuei795 – 7951PhosphoserineCombined sources
Modified residuei805 – 8051PhosphothreonineCombined sources
Modified residuei953 – 9531PhosphoserineBy similarity
Modified residuei1032 – 10321Phosphothreonine; by MAPK1 or MAPK31 Publication
Modified residuei1051 – 10511PhosphothreonineCombined sources
Modified residuei1057 – 10571PhosphothreonineCombined sources
Modified residuei1156 – 11561PhosphoserineCombined sources
Modified residuei1177 – 11771N6-acetyllysineCombined sources
Modified residuei1207 – 12071PhosphoserineCombined sources
Modified residuei1215 – 12151PhosphothreonineCombined sources
Modified residuei1223 – 12231PhosphoserineCombined sources
Modified residuei1302 – 13021PhosphoserineCombined sources
Modified residuei1347 – 13471PhosphoserineCombined sources
Modified residuei1403 – 14031PhosphoserineCombined sources
Modified residuei1433 – 14331PhosphoserineCombined sources
Modified residuei1440 – 14401PhosphothreonineCombined sources
Modified residuei1457 – 14571Phosphothreonine; by MAPK1 or MAPK31 Publication
Modified residuei1463 – 14631PhosphoserineCombined sources
Modified residuei1465 – 14651PhosphoserineBy similarity
Modified residuei1479 – 14791PhosphoserineCombined sources
Modified residuei1481 – 14811PhosphoserineCombined sources
Modified residuei1482 – 14821PhosphoserineCombined sources
Modified residuei1529 – 15291N6-acetyllysineCombined sources

Post-translational modificationi

Phosphorylated by MAPK1 or MAPK3 during G2/M phase which may enhance protein stability and promote entry into the nucleolus.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ15648.
MaxQBiQ15648.
PaxDbiQ15648.
PeptideAtlasiQ15648.
PRIDEiQ15648.

PTM databases

iPTMnetiQ15648.
PhosphoSiteiQ15648.

Expressioni

Tissue specificityi

Ubiquitously expressed.2 Publications

Gene expression databases

BgeeiENSG00000125686.
CleanExiHS_MED1.
ExpressionAtlasiQ15648. baseline and differential.
GenevisibleiQ15648. HS.

Organism-specific databases

HPAiCAB017696.
HPA052818.

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 YWHAH. Interacts with CLOCK; this interaction requires the presence of THRAP3 (By similarity). Interacts with GATA1 and CCAR1. Interacts with NR4A3 (By similarity).By similarity23 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MED7O435134EBI-394459,EBI-394632
RARAP102763EBI-394459,EBI-413374
THRAP108275EBI-394459,EBI-286285

GO - Molecular functioni

  • estrogen receptor binding Source: UniProtKB
  • LBD domain binding Source: UniProtKB
  • ligand-dependent nuclear receptor binding Source: UniProtKB
  • mediator complex binding Source: UniProtKB
  • nuclear hormone receptor binding Source: UniProtKB
  • peroxisome proliferator activated receptor binding Source: UniProtKB
  • retinoic acid receptor binding Source: UniProtKB
  • thyroid hormone receptor binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • vitamin D receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111465. 101 interactions.
DIPiDIP-24212N.
IntActiQ15648. 38 interactions.
MINTiMINT-1345780.
STRINGi9606.ENSP00000300651.

Structurei

Secondary structure

1
1581
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
1RJKX-ray1.99C640-652[»]
1RK3X-ray2.20C640-652[»]
1RKGX-ray1.90C640-652[»]
1RKHX-ray2.28C640-652[»]
2O4JX-ray1.74C640-652[»]
2O4RX-ray1.98C640-652[»]
2ZFXX-ray1.99C640-652[»]
3A2HX-ray2.50B640-652[»]
3AUNX-ray1.81B640-652[»]
3VJSX-ray1.93C640-652[»]
3VJTX-ray2.00C640-652[»]
3VRTX-ray2.40C640-652[»]
3VRUX-ray2.00C640-652[»]
3VRVX-ray1.90C640-652[»]
3VRWX-ray2.40C640-652[»]
3W0GX-ray1.94C640-652[»]
3W0HX-ray1.80C640-652[»]
3W0IX-ray1.90C640-652[»]
3W0JX-ray1.84C640-652[»]
3W5PX-ray1.90C640-652[»]
3W5QX-ray1.90C640-652[»]
3W5RX-ray2.20C640-652[»]
3W5TX-ray2.29C640-652[»]
3WT5X-ray1.90C640-652[»]
3WT6X-ray2.00C640-652[»]
3WT7X-ray2.40C640-652[»]
3WTQX-ray2.10C640-652[»]
4YNKX-ray2.30C640-652[»]
5AWJX-ray2.20C640-652[»]
5AWKX-ray2.90C640-652[»]
ProteinModelPortaliQ15648.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15648.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 670670Interaction with the Mediator complex and THRAAdd
BLAST
Regioni16 – 590575Interaction with ESR1Add
BLAST
Regioni108 – 212105Interaction with the Mediator complexAdd
BLAST
Regioni215 – 390176Interaction with the Mediator complexAdd
BLAST
Regioni405 – 644240Interaction with THRAAdd
BLAST
Regioni542 – 789248Interaction with VDRAdd
BLAST
Regioni622 – 70180Interaction with PPARGC1A and THRAAdd
BLAST
Regioni656 – 1066411Interaction with ESR1Add
BLAST
Regioni681 – 71535Interaction with GATA11 PublicationAdd
BLAST
Regioni1249 – 1421173Interaction with TP53Add
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 – 1482405Ser-richAdd
BLAST
Compositional biasi1496 – 152934Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the Mediator complex subunit 1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IEFR. Eukaryota.
ENOG410XR2E. LUCA.
GeneTreeiENSGT00660000095569.
HOVERGENiHBG101127.
InParanoidiQ15648.
KOiK15144.
OMAiHGEDFSK.
OrthoDBiEOG091G035E.
PhylomeDBiQ15648.
TreeFamiTF324954.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15648-1) [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
MKAQGETEES EKLSKMSSLL ERLHAKFNQN RPWSETIKLV RQVMEKRVVM
60 70 80 90 100
SSGGHQHLVS CLETLQKALK VTSLPAMTDR LESIARQNGL GSHLSASGTE
110 120 130 140 150
CYITSDMFYV EVQLDPAGQL CDVKVAHHGE NPVSCPELVQ QLREKNFDEF
160 170 180 190 200
SKHLKGLVNL YNLPGDNKLK TKMYLALQSL EQDLSKMAIM YWKATNAGPL
210 220 230 240 250
DKILHGSVGY LTPRSGGHLM NLKYYVSPSD LLDDKTASPI ILHENNVSRS
260 270 280 290 300
LGMNASVTIE GTSAVYKLPI APLIMGSHPV DNKWTPSFSS ITSANSVDLP
310 320 330 340 350
ACFFLKFPQP IPVSRAFVQK LQNCTGIPLF ETQPTYAPLY ELITQFELSK
360 370 380 390 400
DPDPIPLNHN MRFYAALPGQ QHCYFLNKDA PLPDGRSLQG TLVSKITFQH
410 420 430 440 450
PGRVPLILNL 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 SSSGSPRMEI CSGSNKTKKK KSSRLPPEKP
710 720 730 740 750
KHQTEDDFQR ELFSMDVDSQ NPIFDVNMTA DTLDTPHITP APSQCSTPPT
760 770 780 790 800
TYPQPVPHPQ PSIQRMVRLS SSDSIGPDVT DILSDIAEEA SKLPSTSDDC
810 820 830 840 850
PAIGTPLRDS SSSGHSQSTL FDSDVFQTNN NENPYTDPAD LIADAAGSPS
860 870 880 890 900
SDSPTNHFFH DGVDFNPDLL NSQSQSGFGE EYFDESSQSG DNDDFKGFAS
910 920 930 940 950
QALNTLGVPM LGGDNGETKF KGNNQADTVD FSIISVAGKA LAPADLMEHH
960 970 980 990 1000
SGSQGPLLTT GDLGKEKTQK RVKEGNGTSN STLSGPGLDS KPGKRSRTPS
1010 1020 1030 1040 1050
NDGKSKDKPP KRKKADTEGK SPSHSSSNRP FTPPTSTGGS KSPGSAGRSQ
1060 1070 1080 1090 1100
TPPGVATPPI PKITIQIPKG TVMVGKPSSH SQYTSSGSVS SSGSKSHHSH
1110 1120 1130 1140 1150
SSSSSSSAST SGKMKSSKSE GSSSSKLSSS MYSSQGSSGS SQSKNSSQSG
1160 1170 1180 1190 1200
GKPGSSPITK HGLSSGSSST KMKPQGKPSS LMNPSLSKPN ISPSHSRPPG
1210 1220 1230 1240 1250
GSDKLASPMK PVPGTPPSSK AKSPISSGSG GSHMSGTSSS SGMKSSSGLG
1260 1270 1280 1290 1300
SSGSLSQKTP PSSNSCTASS SSFSSSGSSM SSSQNQHGSS KGKSPSRNKK
1310 1320 1330 1340 1350
PSLTAVIDKL KHGVVTSGPG GEDPLDGQMG VSTNSSSHPM SSKHNMSGGE
1360 1370 1380 1390 1400
FQGKREKSDK DKSKVSTSGS SVDSSKKTSE SKNVGSTGVA KIIISKHDGG
1410 1420 1430 1440 1450
SPSIKAKVTL QKPGESSGEG LRPQMASSKN YGSPLISGST PKHERGSPSH
1460 1470 1480 1490 1500
SKSPAYTPQN LDSESESGSS IAEKSYQNSP SSDDGIRPLP EYSTEKHKKH
1510 1520 1530 1540 1550
KKEKKKVKDK DRDRDRDKDR DKKKSHSIKP ESWSKSPISS DQSLSMTSNT
1560 1570 1580
ILSADRPSRL SPDFMIGEED DDLMDVALIG N
Length:1,581
Mass (Da):168,478
Last modified:September 11, 2007 - v4
Checksum:iFCE0FE87EF08B887
GO
Isoform 2 (identifier: Q15648-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     548-556: YGMTTGNNP → SKNPELGSG
     557-1581: Missing.

Show »
Length:556
Mass (Da):61,563
Checksum:i1E8BBE45A2629DB1
GO

Sequence cautioni

The sequence AAC39854 differs from that shown. Reason: Frameshift at positions 543 and 545. Curated
The sequence AAH06517 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence CAA73867 differs from that shown. Reason: Frameshift at position 4. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861R → G in CAA73867 (PubMed:9444950).Curated
Sequence conflicti147 – 1471F → S in CAA73867 (PubMed:9444950).Curated
Sequence conflicti471 – 4722DS → GL in CAA73867 (PubMed:9444950).Curated
Sequence conflicti563 – 5631P → S in CAA73867 (PubMed:9444950).Curated
Sequence conflicti563 – 5631P → S in AAF98352 (PubMed:10733574).Curated
Sequence conflicti573 – 5731T → A in CAA73867 (PubMed:9444950).Curated
Sequence conflicti573 – 5731T → A in AAF98352 (PubMed:10733574).Curated
Sequence conflicti651 – 6511D → N in AAH06517 (PubMed:15489334).Curated
Sequence conflicti673 – 6731S → F in AAC41736 (PubMed:7776974).Curated
Sequence conflicti702 – 7087Missing in AAC41736 (PubMed:7776974).Curated
Sequence conflicti721 – 7211N → K in AAC39854 (PubMed:9653119).Curated
Sequence conflicti728 – 7281M → R in AAF98352 (PubMed:10733574).Curated
Sequence conflicti756 – 7616VPHPQP → FYLTPQ in AAH06517 (PubMed:15489334).Curated
Sequence conflicti1388 – 13881G → S in AAC39854 (PubMed:9653119).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti753 – 7531P → T.
Corresponds to variant rs1139825 [ dbSNP | Ensembl ].
VAR_053955
Natural varianti1240 – 12401S → G.
Corresponds to variant rs35668211 [ dbSNP | Ensembl ].
VAR_034938

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei548 – 5569YGMTTGNNP → SKNPELGSG in isoform 2. 1 PublicationVSP_027906
Alternative sequencei557 – 15811025Missing in isoform 2. 1 PublicationVSP_027907Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13467 mRNA. Translation: CAA73867.1. Frameshift.
AF055994 mRNA. Translation: AAC39854.1. Frameshift.
CH471152 Genomic DNA. Translation: EAW60575.1.
BC006517 mRNA. Translation: AAH06517.1. Different termination.
BC060758 mRNA. Translation: AAH60758.1.
BC131783 mRNA. Translation: AAI31784.1.
AF283812 mRNA. Translation: AAF98352.1.
L40366 mRNA. Translation: AAC41736.1.
CCDSiCCDS11336.1. [Q15648-1]
RefSeqiNP_004765.2. NM_004774.3. [Q15648-1]
UniGeneiHs.643754.

Genome annotation databases

EnsembliENST00000300651; ENSP00000300651; ENSG00000125686. [Q15648-1]
ENST00000394287; ENSP00000377828; ENSG00000125686. [Q15648-3]
GeneIDi5469.
KEGGihsa:5469.
UCSCiuc002hru.3. human. [Q15648-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13467 mRNA. Translation: CAA73867.1. Frameshift.
AF055994 mRNA. Translation: AAC39854.1. Frameshift.
CH471152 Genomic DNA. Translation: EAW60575.1.
BC006517 mRNA. Translation: AAH06517.1. Different termination.
BC060758 mRNA. Translation: AAH60758.1.
BC131783 mRNA. Translation: AAI31784.1.
AF283812 mRNA. Translation: AAF98352.1.
L40366 mRNA. Translation: AAC41736.1.
CCDSiCCDS11336.1. [Q15648-1]
RefSeqiNP_004765.2. NM_004774.3. [Q15648-1]
UniGeneiHs.643754.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RJKX-ray1.99C640-652[»]
1RK3X-ray2.20C640-652[»]
1RKGX-ray1.90C640-652[»]
1RKHX-ray2.28C640-652[»]
2O4JX-ray1.74C640-652[»]
2O4RX-ray1.98C640-652[»]
2ZFXX-ray1.99C640-652[»]
3A2HX-ray2.50B640-652[»]
3AUNX-ray1.81B640-652[»]
3VJSX-ray1.93C640-652[»]
3VJTX-ray2.00C640-652[»]
3VRTX-ray2.40C640-652[»]
3VRUX-ray2.00C640-652[»]
3VRVX-ray1.90C640-652[»]
3VRWX-ray2.40C640-652[»]
3W0GX-ray1.94C640-652[»]
3W0HX-ray1.80C640-652[»]
3W0IX-ray1.90C640-652[»]
3W0JX-ray1.84C640-652[»]
3W5PX-ray1.90C640-652[»]
3W5QX-ray1.90C640-652[»]
3W5RX-ray2.20C640-652[»]
3W5TX-ray2.29C640-652[»]
3WT5X-ray1.90C640-652[»]
3WT6X-ray2.00C640-652[»]
3WT7X-ray2.40C640-652[»]
3WTQX-ray2.10C640-652[»]
4YNKX-ray2.30C640-652[»]
5AWJX-ray2.20C640-652[»]
5AWKX-ray2.90C640-652[»]
ProteinModelPortaliQ15648.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111465. 101 interactions.
DIPiDIP-24212N.
IntActiQ15648. 38 interactions.
MINTiMINT-1345780.
STRINGi9606.ENSP00000300651.

PTM databases

iPTMnetiQ15648.
PhosphoSiteiQ15648.

Polymorphism and mutation databases

BioMutaiMED1.
DMDMi158518535.

Proteomic databases

EPDiQ15648.
MaxQBiQ15648.
PaxDbiQ15648.
PeptideAtlasiQ15648.
PRIDEiQ15648.

Protocols and materials databases

DNASUi5469.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000300651; ENSP00000300651; ENSG00000125686. [Q15648-1]
ENST00000394287; ENSP00000377828; ENSG00000125686. [Q15648-3]
GeneIDi5469.
KEGGihsa:5469.
UCSCiuc002hru.3. human. [Q15648-1]

Organism-specific databases

CTDi5469.
GeneCardsiMED1.
HGNCiHGNC:9234. MED1.
HPAiCAB017696.
HPA052818.
MIMi604311. gene.
neXtProtiNX_Q15648.
PharmGKBiPA33556.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IEFR. Eukaryota.
ENOG410XR2E. LUCA.
GeneTreeiENSGT00660000095569.
HOVERGENiHBG101127.
InParanoidiQ15648.
KOiK15144.
OMAiHGEDFSK.
OrthoDBiEOG091G035E.
PhylomeDBiQ15648.
TreeFamiTF324954.

Enzyme and pathway databases

ReactomeiR-HSA-1368082. RORA activates gene expression.
R-HSA-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-HSA-1989781. PPARA activates gene expression.
R-HSA-2032785. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
R-HSA-212436. Generic Transcription Pathway.
R-HSA-2151201. Transcriptional activation of mitochondrial biogenesis.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
R-HSA-383280. Nuclear Receptor transcription pathway.
R-HSA-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
R-HSA-400253. Circadian Clock.
SignaLinkiQ15648.
SIGNORiQ15648.

Miscellaneous databases

ChiTaRSiMED1. human.
EvolutionaryTraceiQ15648.
GeneWikiiMED1.
GenomeRNAii5469.
PROiQ15648.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000125686.
CleanExiHS_MED1.
ExpressionAtlasiQ15648. baseline and differential.
GenevisibleiQ15648. HS.

Family and domain databases

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

Entry informationi

Entry nameiMED1_HUMAN
AccessioniPrimary (citable) accession number: Q15648
Secondary accession number(s): A2RRQ6
, O43810, O75447, Q6P9H7, Q6PK58, Q9HD39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 11, 2007
Last modified: September 7, 2016
This is version 166 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.