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Q15648

- MED1_HUMAN

UniProt

Q15648 - MED1_HUMAN

Protein

Mediator of RNA polymerase II transcription subunit 1

Gene

MED1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 4 (11 Sep 2007)
      Previous versions | rss
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    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.11 Publications

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. chromatin DNA binding Source: Ensembl
    3. core promoter binding Source: UniProtKB
    4. estrogen receptor binding Source: UniProtKB
    5. LBD domain binding Source: UniProtKB
    6. ligand-dependent nuclear receptor binding Source: UniProtKB
    7. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    8. mediator complex binding Source: UniProtKB
    9. nuclear hormone receptor binding Source: UniProtKB
    10. peroxisome proliferator activated receptor binding Source: UniProtKB
    11. protein binding Source: UniProtKB
    12. receptor activity Source: UniProtKB
    13. retinoic acid receptor binding Source: UniProtKB
    14. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
    15. RNA polymerase II transcription cofactor activity Source: UniProtKB
    16. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
    17. thyroid hormone receptor binding Source: UniProtKB
    18. thyroid hormone receptor coactivator activity Source: UniProtKB
    19. transcription coactivator activity Source: UniProtKB
    20. transcription cofactor activity Source: UniProtKB
    21. transcription factor binding Source: UniProtKB
    22. vitamin D receptor binding Source: UniProtKB

    GO - Biological processi

    1. androgen biosynthetic process Source: UniProtKB
    2. androgen receptor signaling pathway Source: UniProtKB
    3. angiogenesis Source: UniProtKB
    4. brain development Source: Ensembl
    5. cell morphogenesis Source: UniProtKB
    6. cellular lipid metabolic process Source: Reactome
    7. cellular response to epidermal growth factor stimulus Source: UniProtKB
    8. cellular response to hepatocyte growth factor stimulus Source: Ensembl
    9. cellular response to steroid hormone stimulus Source: UniProtKB
    10. cellular response to thyroid hormone stimulus Source: UniProtKB
    11. DNA replication Source: Ensembl
    12. embryonic heart tube development Source: Ensembl
    13. embryonic hemopoiesis Source: Ensembl
    14. embryonic hindlimb morphogenesis Source: Ensembl
    15. embryonic placenta development Source: Ensembl
    16. enucleate erythrocyte development Source: Ensembl
    17. epithelial cell proliferation involved in mammary gland duct elongation Source: Ensembl
    18. ERK1 and ERK2 cascade Source: UniProtKB
    19. erythrocyte development Source: UniProtKB
    20. fat cell differentiation Source: MGI
    21. gene expression Source: Reactome
    22. intracellular steroid hormone receptor signaling pathway Source: UniProtKB
    23. keratinocyte differentiation Source: UniProtKB
    24. lactation Source: Ensembl
    25. lens development in camera-type eye Source: UniProtKB
    26. liver development Source: Ensembl
    27. mammary gland branching involved in pregnancy Source: Ensembl
    28. mammary gland branching involved in thelarche Source: Ensembl
    29. megakaryocyte development Source: UniProtKB
    30. monocyte differentiation Source: Ensembl
    31. mRNA transcription from RNA polymerase II promoter Source: UniProtKB
    32. negative regulation of apoptotic process Source: UniProtKB
    33. negative regulation of keratinocyte proliferation Source: UniProtKB
    34. negative regulation of neuron differentiation Source: UniProtKB
    35. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    36. organ regeneration Source: Ensembl
    37. peroxisome proliferator activated receptor signaling pathway Source: Ensembl
    38. positive regulation of G0 to G1 transition Source: Ensembl
    39. positive regulation of gene expression Source: UniProtKB
    40. positive regulation of hepatocyte proliferation Source: Ensembl
    41. positive regulation of interferon-gamma-mediated signaling pathway Source: Ensembl
    42. positive regulation of intracellular estrogen receptor signaling pathway Source: Ensembl
    43. positive regulation of keratinocyte differentiation Source: UniProtKB
    44. positive regulation of mammary gland epithelial cell proliferation Source: Ensembl
    45. positive regulation of protein import into nucleus, translocation Source: Ensembl
    46. positive regulation of receptor activity Source: UniProtKB
    47. positive regulation of transcription, DNA-templated Source: UniProtKB
    48. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    49. regulation of cell cycle Source: UniProtKB
    50. regulation of RNA biosynthetic process Source: UniProtKB
    51. regulation of transcription from RNA polymerase I promoter Source: UniProtKB
    52. regulation of vitamin D receptor signaling pathway Source: Ensembl
    53. retinal pigment epithelium development Source: Ensembl
    54. small molecule metabolic process Source: Reactome
    55. thyroid hormone generation Source: Ensembl
    56. thyroid hormone mediated signaling pathway Source: UniProtKB
    57. transcription initiation from RNA polymerase II promoter Source: UniProtKB
    58. ventricular trabecula myocardium morphogenesis Source: Ensembl

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_12627. Generic Transcription Pathway.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_15525. Nuclear Receptor transcription pathway.
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_24941. Circadian Clock.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinkiQ15648.

    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
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9234. MED1.

    Subcellular locationi

    Nucleus 3 Publications
    Note: A subset of the protein may enter the nucleolus subsequent to phosphorylation by MAPK1 or MAPK3.

    GO - Cellular componenti

    1. chromatin Source: Ensembl
    2. mediator complex Source: UniProtKB
    3. membrane Source: UniProtKB
    4. nucleolus Source: UniProtKB
    5. nucleoplasm Source: Reactome
    6. nucleus Source: UniProtKB
    7. protein-DNA complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi599 – 61214SQNPI…LQITG → EKHKILHRLLQDSS: Enhances interaction with ESR1. Add
    BLAST
    Mutagenesisi600 – 61213QNPIL…LQITG → RHKILHRLLQEGS: Enhances interaction with ESR1. Add
    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. 1 Publication
    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. Add
    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. 1 Publication
    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.

    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 residuei664 – 6641Phosphoserine3 Publications
    Modified residuei795 – 7951Phosphoserine1 Publication
    Modified residuei805 – 8051Phosphothreonine4 Publications
    Modified residuei953 – 9531PhosphoserineBy similarity
    Modified residuei1032 – 10321Phosphothreonine; by MAPK1 or MAPK31 Publication
    Modified residuei1051 – 10511Phosphothreonine3 Publications
    Modified residuei1057 – 10571Phosphothreonine5 Publications
    Modified residuei1156 – 11561Phosphoserine1 Publication
    Modified residuei1177 – 11771N6-acetyllysine1 Publication
    Modified residuei1207 – 12071Phosphoserine4 Publications
    Modified residuei1215 – 12151Phosphothreonine5 Publications
    Modified residuei1223 – 12231Phosphoserine1 Publication
    Modified residuei1347 – 13471Phosphoserine1 Publication
    Modified residuei1403 – 14031Phosphoserine1 Publication
    Modified residuei1433 – 14331Phosphoserine1 Publication
    Modified residuei1457 – 14571Phosphothreonine; by MAPK1 or MAPK31 Publication
    Modified residuei1463 – 14631Phosphoserine2 Publications
    Modified residuei1479 – 14791Phosphoserine3 Publications
    Modified residuei1481 – 14811Phosphoserine2 Publications
    Modified residuei1482 – 14821Phosphoserine2 Publications
    Modified residuei1529 – 15291N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylated by MAPK1 or MAPK3 during G2/M phase which may enhance protein stability and promote entry into the nucleolus.8 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15648.
    PaxDbiQ15648.
    PRIDEiQ15648.

    PTM databases

    PhosphoSiteiQ15648.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.2 Publications

    Gene expression databases

    ArrayExpressiQ15648.
    BgeeiQ15648.
    CleanExiHS_MED1.
    GenevestigatoriQ15648.

    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 GATA1 and YWHAH.22 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RARAP102762EBI-394459,EBI-413374
    THRAP108275EBI-394459,EBI-286285

    Protein-protein interaction databases

    BioGridi111465. 91 interactions.
    DIPiDIP-24212N.
    IntActiQ15648. 25 interactions.
    MINTiMINT-1345780.
    STRINGi9606.ENSP00000300651.

    Structurei

    Secondary structure

    1
    1581
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi643 – 6497

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    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[»]
    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
    Regioni637 – 71680Interaction with GATA1By similarityAdd
    BLAST
    Regioni656 – 1066411Interaction with ESR1Add
    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

    eggNOGiNOG12793.
    HOVERGENiHBG101127.
    InParanoidiQ15648.
    KOiK15144.
    OMAiPKHQTED.
    OrthoDBiEOG7R830S.
    PhylomeDBiQ15648.
    TreeFamiTF324954.

    Family and domain databases

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

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    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

    MKAQGETEES EKLSKMSSLL ERLHAKFNQN RPWSETIKLV RQVMEKRVVM     50
    SSGGHQHLVS CLETLQKALK VTSLPAMTDR LESIARQNGL GSHLSASGTE 100
    CYITSDMFYV EVQLDPAGQL CDVKVAHHGE NPVSCPELVQ QLREKNFDEF 150
    SKHLKGLVNL YNLPGDNKLK TKMYLALQSL EQDLSKMAIM YWKATNAGPL 200
    DKILHGSVGY LTPRSGGHLM NLKYYVSPSD LLDDKTASPI ILHENNVSRS 250
    LGMNASVTIE GTSAVYKLPI APLIMGSHPV DNKWTPSFSS ITSANSVDLP 300
    ACFFLKFPQP IPVSRAFVQK LQNCTGIPLF ETQPTYAPLY ELITQFELSK 350
    DPDPIPLNHN MRFYAALPGQ QHCYFLNKDA PLPDGRSLQG TLVSKITFQH 400
    PGRVPLILNL IRHQVAYNTL IGSCVKRTIL KEDSPGLLQF EVCPLSESRF 450
    SVSFQHPVND SLVCVVMDVQ DSTHVSCKLY KGLSDALICT DDFIAKVVQR 500
    CMSIPVTMRA IRRKAETIQA DTPALSLIAE TVEDMVKKNL PPASSPGYGM 550
    TTGNNPMSGT TTPTNTFPGG PITTLFNMSM SIKDRHESVG HGEDFSKVSQ 600
    NPILTSLLQI TGNGGSTIGS SPTPPHHTPP PVSSMAGNTK NHPMLMNLLK 650
    DNPAQDFSTL YGSSPLERQN SSSGSPRMEI CSGSNKTKKK KSSRLPPEKP 700
    KHQTEDDFQR ELFSMDVDSQ NPIFDVNMTA DTLDTPHITP APSQCSTPPT 750
    TYPQPVPHPQ PSIQRMVRLS SSDSIGPDVT DILSDIAEEA SKLPSTSDDC 800
    PAIGTPLRDS SSSGHSQSTL FDSDVFQTNN NENPYTDPAD LIADAAGSPS 850
    SDSPTNHFFH DGVDFNPDLL NSQSQSGFGE EYFDESSQSG DNDDFKGFAS 900
    QALNTLGVPM LGGDNGETKF KGNNQADTVD FSIISVAGKA LAPADLMEHH 950
    SGSQGPLLTT GDLGKEKTQK RVKEGNGTSN STLSGPGLDS KPGKRSRTPS 1000
    NDGKSKDKPP KRKKADTEGK SPSHSSSNRP FTPPTSTGGS KSPGSAGRSQ 1050
    TPPGVATPPI PKITIQIPKG TVMVGKPSSH SQYTSSGSVS SSGSKSHHSH 1100
    SSSSSSSAST SGKMKSSKSE GSSSSKLSSS MYSSQGSSGS SQSKNSSQSG 1150
    GKPGSSPITK HGLSSGSSST KMKPQGKPSS LMNPSLSKPN ISPSHSRPPG 1200
    GSDKLASPMK PVPGTPPSSK AKSPISSGSG GSHMSGTSSS SGMKSSSGLG 1250
    SSGSLSQKTP PSSNSCTASS SSFSSSGSSM SSSQNQHGSS KGKSPSRNKK 1300
    PSLTAVIDKL KHGVVTSGPG GEDPLDGQMG VSTNSSSHPM SSKHNMSGGE 1350
    FQGKREKSDK DKSKVSTSGS SVDSSKKTSE SKNVGSTGVA KIIISKHDGG 1400
    SPSIKAKVTL QKPGESSGEG LRPQMASSKN YGSPLISGST PKHERGSPSH 1450
    SKSPAYTPQN LDSESESGSS IAEKSYQNSP SSDDGIRPLP EYSTEKHKKH 1500
    KKEKKKVKDK DRDRDRDKDR DKKKSHSIKP ESWSKSPISS DQSLSMTSNT 1550
    ILSADRPSRL SPDFMIGEED DDLMDVALIG N 1581
    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 AAH06517.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAC39854.1 differs from that shown. Reason: Frameshift at positions 543 and 545.
    The sequence CAA73867.1 differs from that shown. Reason: Frameshift at position 4.

    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:
    EMBL
    GenBank
    DDBJ
    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.2. human. [Q15648-3]
    uc002hrv.4. human. [Q15648-1]

    Polymorphism databases

    DMDMi158518535.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS11336.1. [Q15648-1 ]
    RefSeqi NP_004765.2. NM_004774.3. [Q15648-1 ]
    UniGenei Hs.643754.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    3W0G X-ray 1.94 C 640-652 [» ]
    3W0H X-ray 1.80 C 640-652 [» ]
    3W0I X-ray 1.90 C 640-652 [» ]
    3W0J X-ray 1.84 C 640-652 [» ]
    3W5P X-ray 1.90 C 640-652 [» ]
    3W5Q X-ray 1.90 C 640-652 [» ]
    3W5R X-ray 2.20 C 640-652 [» ]
    3W5T X-ray 2.29 C 640-652 [» ]
    3WT5 X-ray 1.90 C 640-652 [» ]
    3WT6 X-ray 2.00 C 640-652 [» ]
    3WT7 X-ray 2.40 C 640-652 [» ]
    ProteinModelPortali Q15648.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111465. 91 interactions.
    DIPi DIP-24212N.
    IntActi Q15648. 25 interactions.
    MINTi MINT-1345780.
    STRINGi 9606.ENSP00000300651.

    PTM databases

    PhosphoSitei Q15648.

    Polymorphism databases

    DMDMi 158518535.

    Proteomic databases

    MaxQBi Q15648.
    PaxDbi Q15648.
    PRIDEi Q15648.

    Protocols and materials databases

    DNASUi 5469.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300651 ; ENSP00000300651 ; ENSG00000125686 . [Q15648-1 ]
    ENST00000394287 ; ENSP00000377828 ; ENSG00000125686 . [Q15648-3 ]
    GeneIDi 5469.
    KEGGi hsa:5469.
    UCSCi uc002hru.2. human. [Q15648-3 ]
    uc002hrv.4. human. [Q15648-1 ]

    Organism-specific databases

    CTDi 5469.
    GeneCardsi GC17M037560.
    HGNCi HGNC:9234. MED1.
    HPAi CAB017696.
    HPA052818.
    MIMi 604311. gene.
    neXtProti NX_Q15648.
    PharmGKBi PA33556.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG101127.
    InParanoidi Q15648.
    KOi K15144.
    OMAi PKHQTED.
    OrthoDBi EOG7R830S.
    PhylomeDBi Q15648.
    TreeFami TF324954.

    Enzyme and pathway databases

    Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_12627. Generic Transcription Pathway.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_15525. Nuclear Receptor transcription pathway.
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_24941. Circadian Clock.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinki Q15648.

    Miscellaneous databases

    ChiTaRSi MED1. human.
    EvolutionaryTracei Q15648.
    GeneWikii MED1.
    GenomeRNAii 5469.
    NextBioi 21174.
    PROi Q15648.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15648.
    Bgeei Q15648.
    CleanExi HS_MED1.
    Genevestigatori Q15648.

    Family and domain databases

    InterProi IPR019680. Mediator_Med1_met/fun.
    [Graphical view ]
    Pfami PF10744. Med1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. "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.
    12. Cited for: INTERACTION WITH RORA.
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    30. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    32. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    33. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-805 AND THR-1215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    35. "The basic helix-loop-helix proteins differentiated embryo chondrocyte (DEC) 1 and DEC2 function as corepressors of retinoid X receptors."
      Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K., Kato Y., Makishima M.
      Mol. Pharmacol. 76:1360-1369(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RXRA.
    36. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    37. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    38. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    39. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    40. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    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: October 1, 2014
    This is version 145 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

    External Data

    Dasty 3