Q15648 (MED1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	MED1
Synonyms:	ARC205, CRSP1, CRSP200, DRIP205, DRIP230, PBP, PPARBP, PPARGBP, RB18A, TRAP220, TRIP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1581 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.2 Ref.12 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.27
Subunit structure	Interacts with GATA1 and YWHAH By similarity. 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, RXRA, RXRG, THRA, THRB and VDR. Interacts with CTNNB1, GABPA, GLI3, PPARGC1A and TP53. Binds DNA. Ref.1 Ref.2 Ref.6 Ref.7 Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.27 Ref.28
Subcellular location	Nucleus. Note: A subset of the protein may enter the nucleolus subsequent to phosphorylation by MAPK1 or MAPK3. Ref.21 Ref.25 Ref.27
Tissue specificity	Ubiquitously expressed. Ref.1 Ref.2
Post-translational modification	Phosphorylated by MAPK1 or MAPK3 during G2/M phase which may enhance protein stability and promote entry into the nucleolus. Ref.25
Sequence similarities	Belongs to the Mediator complex subunit 1 family.
Sequence caution	The sequence AAC39854.1 differs from that shown. Reason: Frameshift at positions 543 and 545. The sequence AAH06517.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence CAA73867.1 differs from that shown. Reason: Frameshift at position 4.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	DNA-binding
Molecular function	Activator
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: Compara ERK1 and ERK2 cascade Inferred from direct assay PubMed 18391015. Source: UniProtKB androgen biosynthetic process Inferred from mutant phenotype PubMed 19497978. Source: UniProtKB androgen receptor signaling pathway Inferred from direct assay Ref.15. Source: UniProtKB angiogenesis Inferred from sequence or structural similarity. Source: UniProtKB brain development Inferred from electronic annotation. Source: Compara cell morphogenesis Inferred from mutant phenotype PubMed 17223341. Source: UniProtKB cellular lipid metabolic process Traceable author statement. Source: Reactome cellular response to epidermal growth factor stimulus Inferred from direct assay Ref.25. Source: UniProtKB cellular response to hepatocyte growth factor stimulus Inferred from electronic annotation. Source: Compara cellular response to steroid hormone stimulus Inferred from direct assay PubMed 18391015. Source: UniProtKB cellular response to thyroid hormone stimulus Inferred from direct assay PubMed 18391015. Source: UniProtKB embryonic heart tube development Inferred from electronic annotation. Source: Compara embryonic hemopoiesis Inferred from electronic annotation. Source: Compara embryonic hindlimb morphogenesis Inferred from electronic annotation. Source: Compara embryonic placenta development Inferred from electronic annotation. Source: Compara enucleate erythrocyte development Inferred from electronic annotation. Source: Compara epithelial cell proliferation involved in mammary gland duct elongation Inferred from electronic annotation. Source: Compara erythrocyte development Inferred from sequence or structural similarity. Source: UniProtKB fat cell differentiation Inferred from direct assay Ref.16. Source: MGI keratinocyte differentiation Inferred from mutant phenotype PubMed 17223341. Source: UniProtKB lactation Inferred from electronic annotation. Source: Compara lens development in camera-type eye Inferred from sequence or structural similarity. Source: UniProtKB liver development Inferred from electronic annotation. Source: Compara mRNA transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB mammary gland branching involved in pregnancy Inferred from electronic annotation. Source: Compara mammary gland branching involved in thelarche Inferred from electronic annotation. Source: Compara megakaryocyte development Inferred from sequence or structural similarity. Source: UniProtKB monocyte differentiation Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of keratinocyte proliferation Inferred from mutant phenotype PubMed 17223341. Source: UniProtKB negative regulation of neuron differentiation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB organ regeneration Inferred from electronic annotation. Source: Compara peroxisome proliferator activated receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of G0 to G1 transition Inferred from electronic annotation. Source: Compara positive regulation of hepatocyte proliferation Inferred from electronic annotation. Source: Compara positive regulation of interferon-gamma-mediated signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of intracellular estrogen receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of keratinocyte differentiation Inferred from mutant phenotype PubMed 17082781. Source: UniProtKB positive regulation of mammary gland epithelial cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of protein import into nucleus, translocation Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 17827210PubMed 19497978Ref.2. Source: UniProtKB regulation of cell cycle Non-traceable author statement Ref.25. Source: UniProtKB regulation of transcription from RNA polymerase I promoter Inferred from direct assay Ref.25. Source: UniProtKB regulation of vitamin D receptor signaling pathway Inferred from electronic annotation. Source: Compara retinal pigment epithelium development Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome thyroid hormone generation Inferred from electronic annotation. Source: Compara thyroid hormone mediated signaling pathway Inferred from mutant phenotype Ref.25. Source: UniProtKB transcription initiation from RNA polymerase II promoter Inferred from direct assay Ref.15. Source: UniProtKB ventricular trabecula myocardium morphogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	mediator complex Inferred from direct assay PubMed 10198638. Source: UniProtKB nucleolus Inferred from direct assay Ref.25. Source: UniProtKB
Molecular_function	RNA polymerase II transcription cofactor activity Inferred from direct assay PubMed 10198638. Source: UniProtKB chromatin binding Inferred from mutant phenotype PubMed 17641689. Source: UniProtKB core promoter binding Inferred from direct assay PubMed 17641689. Source: UniProtKB ligand-dependent nuclear receptor binding Inferred from direct assay PubMed 18391015. Source: UniProtKB mediator complex binding Inferred from direct assay PubMed 18391015. Source: UniProtKB receptor activity Inferred from direct assay Ref.15. Source: UniProtKB sequence-specific DNA binding RNA polymerase II transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB thyroid hormone receptor binding Inferred from direct assay PubMed 10198638. Source: UniProtKB thyroid hormone receptor coactivator activity Inferred from mutant phenotype PubMed 18391015. Source: UniProtKB vitamin D receptor binding Non-traceable author statement Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RARA	P10276	2	EBI-394459,EBI-413374
THRA	P10827	5	EBI-394459,EBI-286285

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15648-1)

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.

Isoform 2 (identifier: Q15648-3)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1581

1581

Mediator of RNA polymerase II transcription subunit 1

PRO_0000058552

Regions

Region

1 – 670

670

Interaction with the Mediator complex and THRA

Region

16 – 590

575

Interaction with ESR1

Region

108 – 212

105

Interaction with the Mediator complex

Region

215 – 390

176

Interaction with the Mediator complex

Region

405 – 644

240

Interaction with THRA

Region

542 – 789

248

Interaction with VDR

Region

622 – 701

80

Interaction with PPARGC1A and THRA

Region

637 – 716

80

Interaction with GATA1 By similarity

Region

656 – 1066

411

Interaction with ESR1

Region

1249 – 1421

173

Interaction with TP53

Motif

604 – 608

5

LXXLL motif 1

Motif

645 – 649

5

LXXLL motif 2

Compositional bias

1078 – 1482

405

Ser-rich

Compositional bias

1496 – 1529

34

Lys-rich

Amino acid modifications

Modified residue

664

1

Phosphoserine Ref.32 Ref.34 Ref.36

Modified residue

795

1

Phosphoserine Ref.29

Modified residue

805

1

Phosphothreonine Ref.29 Ref.31 Ref.33 Ref.36

Modified residue

953

1

Phosphoserine By similarity

Modified residue

1032

1

Phosphothreonine; by MAPK1 or MAPK3 Ref.25

Modified residue

1051

1

Phosphothreonine Ref.32 Ref.34 Ref.38

Modified residue

1057

1

Phosphothreonine Ref.29 Ref.31 Ref.32 Ref.34 Ref.36

Modified residue

1156

1

Phosphoserine Ref.38

Modified residue

1177

1

N6-acetyllysine Ref.35

Modified residue

1207

1

Phosphoserine Ref.31 Ref.32 Ref.36 Ref.38

Modified residue

1215

1

Phosphothreonine Ref.31 Ref.32 Ref.33 Ref.36 Ref.38

Modified residue

1223

1

Phosphoserine Ref.38

Modified residue

1347

1

Phosphoserine Ref.36

Modified residue

1403

1

Phosphoserine Ref.36

Modified residue

1433

1

Phosphoserine Ref.36

Modified residue

1457

1

Phosphothreonine; by MAPK1 or MAPK3 Ref.25

Modified residue

1463

1

Phosphoserine Ref.32 Ref.34

Modified residue

1479

1

Phosphoserine Ref.32 Ref.34 Ref.38

Modified residue

1481

1

Phosphoserine Ref.32 Ref.34

Modified residue

1482

1

Phosphoserine Ref.32 Ref.34

Modified residue

1529

1

N6-acetyllysine Ref.35

Natural variations

Alternative sequence

548 – 556

9

YGMTTGNNP → SKNPELGSG in isoform 2.

VSP_027906

Alternative sequence

557 – 1581

1025

Missing in isoform 2.

VSP_027907

Natural variant

753

1

P → T.
Corresponds to variant rs1139825 [ dbSNP | Ensembl ].

VAR_053955

Natural variant

1240

1

S → G.
Corresponds to variant rs35668211 [ dbSNP | Ensembl ].

VAR_034938

Experimental info

Mutagenesis

599 – 612

14

SQNPI…LQITG → EKHKILHRLLQDSS: Enhances interaction with ESR1. Ref.2 Ref.7 Ref.13 Ref.14 Ref.20 Ref.23

Mutagenesis

600 – 612

13

QNPIL…LQITG → RHKILHRLLQEGS: Enhances interaction with ESR1. Ref.2 Ref.7 Ref.13 Ref.20 Ref.23

Mutagenesis

604

1

L → A: Impairs interaction with ESR2; when associated with A-607; A-645 and A-648. Ref.2 Ref.7 Ref.13 Ref.14 Ref.20 Ref.23

Mutagenesis

607 – 608

2

LL → AA: Impairs interaction with ESR1, PPARG, RXRA and THRB. Impairs interaction with THRA; when associated with 648-A-A-649. Ref.2 Ref.7 Ref.13 Ref.14 Ref.20 Ref.23

Mutagenesis

607

1

L → A: Impairs interaction with ESR2; when associated with A-604; A-645 and A-648. Ref.2 Ref.7 Ref.13 Ref.14 Ref.20 Ref.23

Mutagenesis

639 – 653

15

TKNHP…LKDNP → VSRHKILHRLLQEGS: Enhances interaction with ESR1. Ref.2 Ref.7 Ref.13 Ref.19 Ref.20 Ref.23

Mutagenesis

645

1

L → A: Impairs interaction with ESR2; when associated with A-604; A-607 and A-648. Ref.2 Ref.7 Ref.13 Ref.14 Ref.20 Ref.23

Mutagenesis

648 – 649

2

LL → AA: Impairs interaction with ESR1, PPARG, THRB and VDR. Impairs interaction with THRA; when associated with 607-A-A-608. Ref.2 Ref.7 Ref.13 Ref.14 Ref.20 Ref.23

Mutagenesis

648

1

L → A: Impairs interaction with ESR2; when associated with A-604; A-607 and A-645. Ref.2 Ref.7 Ref.13 Ref.14 Ref.20 Ref.23

Mutagenesis

1032

1

T → A: Enhances protein stability; when associated with A-1457. Ref.2 Ref.7 Ref.13 Ref.20 Ref.23 Ref.25

Mutagenesis

1457

1

T → A: Enhances protein stability; when associated with A-1032. Ref.2 Ref.7 Ref.13 Ref.20 Ref.23 Ref.25

Sequence conflict

86

1

R → G in CAA73867. Ref.1

Sequence conflict

147

1

F → S in CAA73867. Ref.1

Sequence conflict

471 – 472

2

DS → GL in CAA73867. Ref.1

Sequence conflict

563

1

P → S in CAA73867. Ref.1

Sequence conflict

563

1

P → S in AAF98352. Ref.7

Sequence conflict

573

1

T → A in CAA73867. Ref.1

Sequence conflict

573

1

T → A in AAF98352. Ref.7

Sequence conflict

651

1

D → N in AAH06517. Ref.5

Sequence conflict

673

1

S → F in AAC41736. Ref.9

Sequence conflict

702 – 708

7

Missing in AAC41736. Ref.9

Sequence conflict

721

1

N → K in AAC39854. Ref.2

Sequence conflict

728

1

M → R in AAF98352. Ref.7

Sequence conflict

756 – 761

6

VPHPQP → FYLTPQ in AAH06517. Ref.5

Sequence conflict

1388

1

G → S in AAC39854. Ref.2

Secondary structure

1

.

.

.

1581

Helix Strand Turn

Details...

Helix

643 – 649

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 11, 2007. Version 4. Checksum: FCE0FE87EF08B887	FASTA	1,581	168,478
	10 20 30 40 50 60 MKAQGETEES EKLSKMSSLL ERLHAKFNQN RPWSETIKLV RQVMEKRVVM SSGGHQHLVS 70 80 90 100 110 120 CLETLQKALK VTSLPAMTDR LESIARQNGL GSHLSASGTE CYITSDMFYV EVQLDPAGQL 130 140 150 160 170 180 CDVKVAHHGE NPVSCPELVQ QLREKNFDEF SKHLKGLVNL YNLPGDNKLK TKMYLALQSL 190 200 210 220 230 240 EQDLSKMAIM YWKATNAGPL DKILHGSVGY LTPRSGGHLM NLKYYVSPSD LLDDKTASPI 250 260 270 280 290 300 ILHENNVSRS LGMNASVTIE GTSAVYKLPI APLIMGSHPV DNKWTPSFSS ITSANSVDLP 310 320 330 340 350 360 ACFFLKFPQP IPVSRAFVQK LQNCTGIPLF ETQPTYAPLY ELITQFELSK DPDPIPLNHN 370 380 390 400 410 420 MRFYAALPGQ QHCYFLNKDA PLPDGRSLQG TLVSKITFQH PGRVPLILNL IRHQVAYNTL 430 440 450 460 470 480 IGSCVKRTIL KEDSPGLLQF EVCPLSESRF SVSFQHPVND SLVCVVMDVQ DSTHVSCKLY 490 500 510 520 530 540 KGLSDALICT DDFIAKVVQR CMSIPVTMRA IRRKAETIQA DTPALSLIAE TVEDMVKKNL 550 560 570 580 590 600 PPASSPGYGM TTGNNPMSGT TTPTNTFPGG PITTLFNMSM SIKDRHESVG HGEDFSKVSQ 610 620 630 640 650 660 NPILTSLLQI TGNGGSTIGS SPTPPHHTPP PVSSMAGNTK NHPMLMNLLK DNPAQDFSTL 670 680 690 700 710 720 YGSSPLERQN SSSGSPRMEI CSGSNKTKKK KSSRLPPEKP KHQTEDDFQR ELFSMDVDSQ 730 740 750 760 770 780 NPIFDVNMTA DTLDTPHITP APSQCSTPPT TYPQPVPHPQ PSIQRMVRLS SSDSIGPDVT 790 800 810 820 830 840 DILSDIAEEA SKLPSTSDDC PAIGTPLRDS SSSGHSQSTL FDSDVFQTNN NENPYTDPAD 850 860 870 880 890 900 LIADAAGSPS SDSPTNHFFH DGVDFNPDLL NSQSQSGFGE EYFDESSQSG DNDDFKGFAS 910 920 930 940 950 960 QALNTLGVPM LGGDNGETKF KGNNQADTVD FSIISVAGKA LAPADLMEHH SGSQGPLLTT 970 980 990 1000 1010 1020 GDLGKEKTQK RVKEGNGTSN STLSGPGLDS KPGKRSRTPS NDGKSKDKPP KRKKADTEGK 1030 1040 1050 1060 1070 1080 SPSHSSSNRP FTPPTSTGGS KSPGSAGRSQ TPPGVATPPI PKITIQIPKG TVMVGKPSSH 1090 1100 1110 1120 1130 1140 SQYTSSGSVS SSGSKSHHSH SSSSSSSAST SGKMKSSKSE GSSSSKLSSS MYSSQGSSGS 1150 1160 1170 1180 1190 1200 SQSKNSSQSG GKPGSSPITK HGLSSGSSST KMKPQGKPSS LMNPSLSKPN ISPSHSRPPG 1210 1220 1230 1240 1250 1260 GSDKLASPMK PVPGTPPSSK AKSPISSGSG GSHMSGTSSS SGMKSSSGLG SSGSLSQKTP 1270 1280 1290 1300 1310 1320 PSSNSCTASS SSFSSSGSSM SSSQNQHGSS KGKSPSRNKK PSLTAVIDKL KHGVVTSGPG 1330 1340 1350 1360 1370 1380 GEDPLDGQMG VSTNSSSHPM SSKHNMSGGE FQGKREKSDK DKSKVSTSGS SVDSSKKTSE 1390 1400 1410 1420 1430 1440 SKNVGSTGVA KIIISKHDGG SPSIKAKVTL QKPGESSGEG LRPQMASSKN YGSPLISGST 1450 1460 1470 1480 1490 1500 PKHERGSPSH SKSPAYTPQN LDSESESGSS IAEKSYQNSP SSDDGIRPLP EYSTEKHKKH 1510 1520 1530 1540 1550 1560 KKEKKKVKDK DRDRDRDKDR DKKKSHSIKP ESWSKSPISS DQSLSMTSNT ILSADRPSRL 1570 1580 SPDFMIGEED DDLMDVALIG N
	Isoform 2 [UniParc]. Checksum: 1E8BBE45A2629DB1	FASTA	556	61,563
	10 20 30 40 50 60 MKAQGETEES EKLSKMSSLL ERLHAKFNQN RPWSETIKLV RQVMEKRVVM SSGGHQHLVS 70 80 90 100 110 120 CLETLQKALK VTSLPAMTDR LESIARQNGL GSHLSASGTE CYITSDMFYV EVQLDPAGQL 130 140 150 160 170 180 CDVKVAHHGE NPVSCPELVQ QLREKNFDEF SKHLKGLVNL YNLPGDNKLK TKMYLALQSL 190 200 210 220 230 240 EQDLSKMAIM YWKATNAGPL DKILHGSVGY LTPRSGGHLM NLKYYVSPSD LLDDKTASPI 250 260 270 280 290 300 ILHENNVSRS LGMNASVTIE GTSAVYKLPI APLIMGSHPV DNKWTPSFSS ITSANSVDLP 310 320 330 340 350 360 ACFFLKFPQP IPVSRAFVQK LQNCTGIPLF ETQPTYAPLY ELITQFELSK DPDPIPLNHN 370 380 390 400 410 420 MRFYAALPGQ QHCYFLNKDA PLPDGRSLQG TLVSKITFQH PGRVPLILNL IRHQVAYNTL 430 440 450 460 470 480 IGSCVKRTIL KEDSPGLLQF EVCPLSESRF SVSFQHPVND SLVCVVMDVQ DSTHVSCKLY 490 500 510 520 530 540 KGLSDALICT DDFIAKVVQR CMSIPVTMRA IRRKAETIQA DTPALSLIAE TVEDMVKKNL 550 PPASSPGSKN PELGSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of RB18A, a 205 kDa new p53 regulatory protein which shares antigenic and functional properties with p53." Drane P., Barel M., Balbo M., Frade R. Oncogene 15:3013-3024(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DNA-BINDING, INTERACTION WITH TP53, TISSUE SPECIFICITY. Tissue: Heart.
[2]	"The TRAP220 component of a thyroid hormone receptor-associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion." Yuan C.-X., Ito M., Fondell J.D., Fu Z.-Y., Roeder R.G. Proc. Natl. Acad. Sci. U.S.A. 95:7939-7944(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 157-168; 943-952 AND 1432-1442, FUNCTION, INTERACTION WITH ESR1; PPARA; PPARG; RARA; RXRA; THRA AND VDR, TISSUE SPECIFICITY, MUTAGENESIS OF 607-LEU-LEU-608 AND 648-LEU-LEU-649.
[3]	Erratum Yuan C.-X., Ito M., Fondell J.D., Fu Z.-Y., Roeder R.G. Proc. Natl. Acad. Sci. U.S.A. 95:14584-14584(1998)
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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 1 AND 2). Tissue: Colon and Testis.
[6]	"Composite co-activator ARC mediates chromatin-directed transcriptional activation." Naeaer A.M., Beaurang P.A., Zhou S., Abraham S., Solomon W.B., Tjian R. Nature 398:828-832(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-13 AND 1452-1464, IDENTIFICATION IN THE ARC COMPLEX.
[7]	"The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes." Rachez C., Gamble M., Chang C.-P.B., Atkins G.B., Lazar M.A., Freedman L.P. Mol. Cell. Biol. 20:2718-2726(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-1581 (ISOFORM 1), INTERACTION WITH VDR, MUTAGENESIS OF 607-LEU-LEU-608 AND 648-LEU-LEU-649.
[8]	"Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex." Rachez C., Lemon B.D., Suldan Z., Bromleigh V., Gamble M., Naeaer A.M., Erdjument-Bromage H., Tempst P., Freedman L.P. Nature 398:824-828(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 307-315 AND 584-597, IDENTIFICATION IN THE DRIP COMPLEX, INTERACTION WITH VDR. Tissue: Cervix carcinoma.
[9]	"Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor." Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D. Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 622-711.
[10]	"A novel human SRB/MED-containing cofactor complex, SMCC, involved in transcription regulation." Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E., Qin J., Roeder R.G. Mol. Cell 3:97-108(1999) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SMCC COMPLEX.
[11]	Erratum Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E., Qin J., Roeder R.G. Mol. Cell 3:541-541(1999)
[12]	"Identification of mouse TRAP100: a transcriptional coregulatory factor for thyroid hormone and vitamin D receptors." Zhang J., Fondell J.D. Mol. Endocrinol. 13:1130-1140(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MED24; THRA; THRB AND VDR.
[13]	"Functional interactions between the estrogen receptor and DRIP205, a subunit of the heteromeric DRIP coactivator complex." Burakov D., Wong C.-W., Rachez C., Cheskis B.J., Freedman L.P. J. Biol. Chem. 275:20928-20934(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ESR1; ESR2 AND VDR, MUTAGENESIS OF 607-LEU-LEU-608 AND 648-LEU-LEU-649.
[14]	"Differential recruitment of the mammalian mediator subunit TRAP220 by estrogen receptors ERalpha and ERbeta." Waernmark A., Almloef T., Leers J., Gustafsson J.-A., Treuter E. J. Biol. Chem. 276:23397-23404(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ESR1 AND ESR2, MUTAGENESIS OF 599-SER--GLY-612; LEU-604; LEU-607; LEU-645 AND LEU-648.
[15]	"A coregulatory role for the TRAP-mediator complex in androgen receptor-mediated gene expression." Wang Q., Sharma D., Ren Y., Fondell J.D. J. Biol. Chem. 277:42852-42858(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH AR, ASSOCIATION WITH PROMOTER REGIONS.
[16]	"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, INTERACTION OF THE MEDIATOR COMPLEX WITH PPARG.
[17]	"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, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, INTERACTION OF THE MEDIATOR COMPLEX WITH ESR1 AND ESR2.
[18]	"Ordered recruitment of histone acetyltransferases and the TRAP/Mediator complex to thyroid hormone-responsive promoters in vivo." Sharma D., Fondell J.D. Proc. Natl. Acad. Sci. U.S.A. 99:7934-7939(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION WITH PROMOTER REGIONS.
[19]	"An extended LXXLL motif sequence determines the nuclear receptor binding specificity of TRAP220." Coulthard V.H., Matsuda S., Heery D.M. J. Biol. Chem. 278:10942-10951(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ESR1; PPARG; RARA; RXRA AND THRB, MUTAGENESIS OF 600-GLN--SER-612; 607-LEU-LEU-608; 639-THR--PRO-653 AND 648-LEU-LEU-649.
[20]	"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, MUTAGENESIS OF 607-LEU-LEU-608 AND 648-LEU-LEU-649.
[21]	"Vitamin D-interacting protein 205 (DRIP205) coactivation of estrogen receptor alpha (ERalpha) involves multiple domains of both proteins." Wu Q., Burghardt R., Safe S. J. Biol. Chem. 279:53602-53612(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ESR1, SUBCELLULAR LOCATION.
[22]	"A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology." Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B., Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P., Conaway J.W., Conaway R.C. Mol. Cell 14:685-691(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX.
[23]	"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, MUTAGENESIS OF 607-LEU-LEU-608 AND 648-LEU-LEU-649.
[24]	"MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation enriched in RNA polymerase II and is required for ER-mediated transcription." Zhang X., Krutchinsky A., Fukuda A., Chen W., Yamamura S., Chait B.T., Roeder R.G. Mol. Cell 19:89-100(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ASSOCIATION WITH PROMOTER REGIONS, INTERACTION WITH CCNC; MED6; MED10; MED11; MED12; MED13; MED14; MED15; MED16; MED17; MED18; MED19; MED20; MED21; MED23; MED24; MED25; MED26; MED28; MED29 AND MED30, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
[25]	"Activation of TRAP/mediator subunit TRAP220/Med1 is regulated by mitogen-activated protein kinase-dependent phosphorylation." Pandey P.K., Udayakumar T.S., Lin X., Sharma D., Shapiro P.S., Fondell J.D. Mol. Cell. Biol. 25:10695-10710(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-1032 AND THR-1457, MUTAGENESIS OF THR-1032 AND THR-1457.
[26]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[27]	"Regulation of Aurora-A kinase gene expression via GABP recruitment of TRAP220/MED1." Udayakumar T.S., Belakavadi M., Choi K.-H., Pandey P.K., Fondell J.D. J. Biol. Chem. 281:14691-14699(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH GABPA, ASSOCIATION WITH PROMOTER REGIONS, SUBCELLULAR LOCATION.
[28]	"Mediator modulates Gli3-dependent Sonic hedgehog signaling." Zhou H., Kim S., Ishii S., Boyer T.G. Mol. Cell. Biol. 26:8667-8682(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CDK8.
[29]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-795; THR-805 AND THR-1057, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[30]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[31]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-805; THR-1057; SER-1207 AND THR-1215, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[32]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; THR-1051; THR-1057; SER-1207; THR-1215; SER-1463; SER-1479; SER-1481 AND SER-1482, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[33]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-805 AND THR-1215, MASS SPECTROMETRY.
[34]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; THR-1051; THR-1057; SER-1463; SER-1479; SER-1481 AND SER-1482, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[35]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1177 AND LYS-1529, MASS SPECTROMETRY.
[36]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; THR-805; THR-1057; SER-1207; THR-1215; SER-1347; SER-1403 AND SER-1433, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[37]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1051; SER-1156; SER-1207; THR-1215; SER-1223 AND SER-1479, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00790747.
IPI00829826.

RefSeq

NP_004765.2. NM_004774.3.

UniGene

Hs.643754.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RJK	X-ray	1.99	C	640-652	[»]
1RK3	X-ray	2.20	C	640-652	[»]
1RKG	X-ray	1.90	C	640-652	[»]
1RKH	X-ray	2.28	C	640-652	[»]
2O4J	X-ray	1.74	C	640-652	[»]
2O4R	X-ray	1.98	C	640-652	[»]
2ZFX	X-ray	1.99	C	640-652	[»]
3A2H	X-ray	2.50	B	640-652	[»]
3AUN	X-ray	1.81	B	640-652	[»]
3VJS	X-ray	1.93	C	640-652	[»]
3VJT	X-ray	2.00	C	640-652	[»]
3VRT	X-ray	2.40	C	640-652	[»]
3VRU	X-ray	2.00	C	640-652	[»]
3VRV	X-ray	1.90	C	640-652	[»]
3VRW	X-ray	2.40	C	640-652	[»]

ProteinModelPortal

Q15648.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24212N.

IntAct

Q15648. 21 interactions.

MINT

MINT-1345780.

STRING

9606.ENSP00000300651.

PTM databases

PhosphoSite

Q15648.

Polymorphism databases

DMDM

158518535.

Proteomic databases

PaxDb

Q15648.

PRIDE

Q15648.

Protocols and materials databases

DNASU

5469.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000300651; ENSP00000300651; ENSG00000125686.
ENST00000394287; ENSP00000377828; ENSG00000125686.

GeneID

5469.

KEGG

hsa:5469.

UCSC

uc002hru.2. human.
uc002hrv.4. human.

Organism-specific databases

CTD

5469.

GeneCards

GC17M037560.

HGNC

HGNC:9234. MED1.

HPA

CAB017696.

MIM

604311. gene.

neXtProt

NX_Q15648.

PharmGKB

PA33556.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG12793.

HOVERGEN

HBG101127.

InParanoid

Q15648.

KO

K15144.

OMA

PKHQTED.

PhylomeDB

Q15648.

Enzyme and pathway databases

Pathway_Interaction_DB

rxr_vdr_pathway. RXR and RAR hetrodimerization with other nuclear receptor.

Reactome

REACT_111045. Developmental Biology.
REACT_111217. Metabolism.
REACT_71. Gene Expression.

Gene expression databases

Bgee

Q15648.

CleanEx

HS_MED1.

Genevestigator

Q15648.

GermOnline

ENSG00000125686. Homo sapiens.

Family and domain databases

InterPro

IPR019680. Mediator_Med1_met/fun.
[Graphical view]

Pfam

PF10744. Med1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

MED1. human.

EvolutionaryTrace

Q15648.

GenomeRNAi

5469.

NextBio

21174.

SOURCE

Search...

Entry information

Entry name

MED1_HUMAN

Accession

Primary (citable) accession number: Q15648
Secondary accession number(s): A2RRQ6 , O43810, O75447, Q6P9H7, Q6PK58, Q9HD39

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	September 11, 2007
Last modified:	April 3, 2013
This is version 130 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.