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Q71SY5

- MED25_HUMAN

UniProt

Q71SY5 - MED25_HUMAN

Protein

Mediator of RNA polymerase II transcription subunit 25

Gene

MED25

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (02 Oct 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. Required for RARA/RXRA-mediated transcription.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. retinoic acid receptor binding Source: UniProtKB
    3. retinoid X receptor binding Source: UniProtKB
    4. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. gene expression Source: Reactome
    3. negative regulation of fibroblast proliferation Source: UniProtKB
    4. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    5. positive regulation of cell cycle arrest Source: UniProtKB
    6. positive regulation of chromatin binding Source: UniProtKB
    7. positive regulation of mediator complex assembly Source: UniProtKB
    8. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    9. transcription initiation from RNA polymerase II promoter Source: Reactome

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_116145. PPARA activates gene expression.
    REACT_12627. Generic Transcription Pathway.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mediator of RNA polymerase II transcription subunit 25
    Alternative name(s):
    Activator interaction domain-containing protein 1
    Activator-recruited cofactor 92 kDa component
    Short name:
    ARC92
    Mediator complex subunit 25
    p78
    Gene namesi
    Name:MED25
    Synonyms:ACID1, ARC92, PTOV2
    ORF Names:TCBAP0758
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:28845. MED25.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Charcot-Marie-Tooth disease 2B2 (CMT2B2) [MIM:605589]: A recessive axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti335 – 3351A → V in CMT2B2. 1 Publication
    Corresponds to variant rs145770066 [ dbSNP | Ensembl ].
    VAR_063521

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi646 – 6461L → A: Abrogates interaction with RARA. 1 Publication
    Mutagenesisi649 – 6502LL → AA: Abrogates interaction with RARA.

    Keywords - Diseasei

    Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

    Organism-specific databases

    MIMi605589. phenotype.
    Orphaneti101101. Charcot-Marie-Tooth disease type 2B2.
    PharmGKBiPA134984839.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 747747Mediator of RNA polymerase II transcription subunit 25PRO_0000304952Add
    BLAST

    Proteomic databases

    MaxQBiQ71SY5.
    PaxDbiQ71SY5.
    PRIDEiQ71SY5.

    PTM databases

    PhosphoSiteiQ71SY5.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Highest levels in brain, heart, kidney, peripheral leukocytes, placenta, skeletal muscle and spleen.2 Publications

    Gene expression databases

    ArrayExpressiQ71SY5.
    BgeeiQ71SY5.
    CleanExiHS_MED25.
    GenevestigatoriQ71SY5.

    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. Interacts with CREBBP. Interacts with ESR1, GR, RARA, RXRA and THRB in a ligand-dependent fashion. Binds the Herpes simplex virus activator VP16.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RARAP1027610EBI-394558,EBI-413374
    RXRAP197934EBI-394558,EBI-78598
    RxraP287003EBI-394558,EBI-346715From a different organism.

    Protein-protein interaction databases

    BioGridi123607. 43 interactions.
    DIPiDIP-31454N.
    IntActiQ71SY5. 15 interactions.
    MINTiMINT-5209896.

    Structurei

    Secondary structure

    1
    747
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi396 – 40914
    Beta strandi414 – 4174
    Beta strandi424 – 43411
    Helixi441 – 4433
    Beta strandi446 – 4549
    Helixi455 – 4617
    Helixi462 – 4654
    Beta strandi466 – 47510
    Beta strandi476 – 4783
    Helixi480 – 49314
    Beta strandi494 – 4996
    Beta strandi504 – 5074
    Beta strandi510 – 5156
    Turni517 – 5193
    Beta strandi521 – 5299
    Helixi530 – 54516

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KY6NMR-A391-553[»]
    2L23NMR-A391-548[»]
    2L6UNMR-A391-543[»]
    2XNFNMR-A394-543[»]
    ProteinModelPortaliQ71SY5.
    SMRiQ71SY5. Positions 391-553.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ71SY5.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 226226Interaction with the Mediator complexAdd
    BLAST
    Regioni389 – 543155Interaction with VP16Add
    BLAST
    Regioni395 – 545151Interaction with CREBBPAdd
    BLAST
    Regioni564 – 65390Interaction with RARAAdd
    BLAST
    Regioni640 – 70768Interaction with RARAAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi646 – 6505LXXLL motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi200 – 381182Pro-richAdd
    BLAST
    Compositional biasi565 – 735171Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Mediator complex subunit 25 family.Curated

    Phylogenomic databases

    eggNOGiNOG79607.
    HOVERGENiHBG108127.
    KOiK15168.
    OMAiPGQMLLS.
    OrthoDBiEOG78H3SP.
    PhylomeDBiQ71SY5.
    TreeFamiTF329598.

    Family and domain databases

    InterProiIPR021394. Mediator_Med25.
    IPR021406. Mediator_Med25_NR-box.
    IPR021397. Mediator_Med25_SD1.
    IPR021419. Mediator_Med25_VWA.
    IPR002035. VWF_A.
    [Graphical view]
    PfamiPF11232. Med25. 1 hit.
    PF11244. Med25_NR-box. 1 hit.
    PF11235. Med25_SD1. 1 hit.
    PF11265. Med25_VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF53300. SSF53300. 1 hit.

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q71SY5-1) [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

    MVPGSEGPAR AGSVVADVVF VIEGTANLGP YFEGLRKHYL LPAIEYFNGG    50
    PPAETDFGGD YGGTQYSLVV FNTVDCAPES YVQCHAPTSS AYEFVTWLDG 100
    IKFMGGGGES CSLIAEGLST ALQLFDDFKK MREQIGQTHR VCLLICNSPP 150
    YLLPAVESTT YSGCTTENLV QQIGERGIHF SIVSPRKLPA LRLLFEKAAP 200
    PALLEPLQPP TDVSQDPRHM VLVRGLVLPV GGGSAPGPLQ SKQPVPLPPA 250
    APSGATLSAA PQQPLPPVPP QYQVPGNLSA AQVAAQNAVE AAKNQKAGLG 300
    PRFSPITPLQ QAAPGVGPPF SQAPAPQLPP GPPGAPKPPP ASQPSLVSTV 350
    APGSGLAPTA QPGAPSMAGT VAPGGVSGPS PAQLGAPALG GQQSVSNKLL 400
    AWSGVLEWQE KPKPASVDAN TKLTRSLPCQ VYVNHGENLK TEQWPQKLIM 450
    QLIPQQLLTT LGPLFRNSRM VQFHFTNKDL ESLKGLYRIM GNGFAGCVHF 500
    PHTAPCEVRV LMLLYSSKKK IFMGLIPYDQ SGFVNGIRQV ITNHKQVQQQ 550
    KLEQQQRGMG GQQAPPGLGP ILEDQARPSQ NLLQLRPPQP QPQGTVGASG 600
    ATGQPQPQGT AQPPPGAPQG PPGAASGPPP PGPILRPQNP GANPQLRSLL 650
    LNPPPPQTGV PPPQASLHHL QPPGAPALLP PPHQGLGQPQ LGPPLLHPPP 700
    AQSWPAQLPP RAPLPGQMLL SGGPRGPVPQ PGLQPSVMED DILMDLI 747
    Length:747
    Mass (Da):78,171
    Last modified:October 2, 2007 - v2
    Checksum:i6FE13FB45786402D
    GO
    Isoform 2 (identifier: Q71SY5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         671-747: QPPGAPALLP...MEDDILMDLI → PSPGPHNFPL...ESPTPNKVPF

    Show »
    Length:754
    Mass (Da):78,882
    Checksum:i0E8022B21685A1EE
    GO
    Isoform 3 (identifier: Q71SY5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         701-747: AQSWPAQLPP...MEDDILMDLI → PATRGSCAAA...VERIQPETPL

    Note: No experimental confirmation available.

    Show »
    Length:796
    Mass (Da):82,972
    Checksum:i930FD1BDBEED7BA1
    GO
    Isoform 4 (identifier: Q71SY5-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         716-747: GQMLLSGGPRGPVPQPGLQPSVMEDDILMDLI → AAKRKREGEG...IRARPIWPDP

    Note: No experimental confirmation available.

    Show »
    Length:793
    Mass (Da):84,389
    Checksum:i4F9597470EB0E517
    GO
    Isoform 5 (identifier: Q71SY5-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         303-319: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:730
    Mass (Da):76,512
    Checksum:i70D41D4F28B8A709
    GO
    Isoform 6 (identifier: Q71SY5-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         61-273: Missing.

    Show »
    Length:534
    Mass (Da):55,456
    Checksum:iD49EA118755469AC
    GO

    Sequence cautioni

    The sequence CAB66680.1 differs from that shown. Reason: Frameshift at position 567.
    The sequence AAG15589.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 201F → S in AAM20739. (PubMed:12163014)Curated
    Sequence conflicti236 – 2361P → L in CAE84581. (PubMed:14657022)Curated
    Sequence conflicti236 – 2361P → L in CAB66680. 1 PublicationCurated
    Sequence conflicti268 – 2681V → I in AAM20739. (PubMed:12163014)Curated
    Sequence conflicti514 – 5141L → M in AAS45401. (PubMed:14983011)Curated
    Sequence conflicti536 – 5361G → D in AAS45401. (PubMed:14983011)Curated
    Sequence conflicti703 – 7031S → F in AAM20739. (PubMed:12163014)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti335 – 3351A → V in CMT2B2. 1 Publication
    Corresponds to variant rs145770066 [ dbSNP | Ensembl ].
    VAR_063521

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei61 – 273213Missing in isoform 6. 1 PublicationVSP_047570Add
    BLAST
    Alternative sequencei303 – 31917Missing in isoform 5. 1 PublicationVSP_028143Add
    BLAST
    Alternative sequencei671 – 74777QPPGA…LMDLI → PSPGPHNFPLGLHCQVRGPG GGQRSGLSVPAAPGLEHQDQ VLLGSKDIGSKNEGSPSRAC SPASWRTTSSWISSESPTPN KVPF in isoform 2. 2 PublicationsVSP_028144Add
    BLAST
    Alternative sequencei701 – 74747AQSWP…LMDLI → PATRGSCAAASAAPGPGAAP VGAPTPASTTCPVLARTTSP SGSTASGKTKERRRGPCVSR KMGASLFLCGSEEHAYVFNM QTNRVCVERIQPETPL in isoform 3. 1 PublicationVSP_028145Add
    BLAST
    Alternative sequencei716 – 74732GQMLL…LMDLI → AAKRKREGEGRVFREKWERA YFFVEVKSMPMCLICKQIVS VLKEYNLKRHYESKHSKSYD QYTEQTRRIRARPIWPDP in isoform 4. 1 PublicationVSP_028146Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF261072 mRNA. Translation: AAM20739.1.
    AJ617479 mRNA. Translation: CAE84581.1.
    AY533507 mRNA. Translation: AAS45401.1.
    AL136746 mRNA. Translation: CAB66680.1. Frameshift.
    EU392500 mRNA. Translation: ACB88862.1.
    AK289460 mRNA. Translation: BAF82149.1.
    AC006942 Genomic DNA. Translation: AAD15565.1.
    AC018766 Genomic DNA. No translation available.
    CH471177 Genomic DNA. Translation: EAW52546.1.
    BC024312 mRNA. Translation: AAH24312.2.
    BC065297 mRNA. Translation: AAH65297.1.
    AF283769 mRNA. Translation: AAG15589.1. Different initiation.
    CCDSiCCDS33075.1. [Q71SY5-1]
    RefSeqiNP_112235.2. NM_030973.3. [Q71SY5-1]
    UniGeneiHs.656639.
    Hs.745568.

    Genome annotation databases

    EnsembliENST00000312865; ENSP00000326767; ENSG00000104973. [Q71SY5-1]
    ENST00000538643; ENSP00000437496; ENSG00000104973. [Q71SY5-6]
    GeneIDi81857.
    KEGGihsa:81857.
    UCSCiuc002ppw.2. human. [Q71SY5-1]
    uc002ppx.1. human. [Q71SY5-4]

    Polymorphism databases

    DMDMi158706143.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF261072 mRNA. Translation: AAM20739.1 .
    AJ617479 mRNA. Translation: CAE84581.1 .
    AY533507 mRNA. Translation: AAS45401.1 .
    AL136746 mRNA. Translation: CAB66680.1 . Frameshift.
    EU392500 mRNA. Translation: ACB88862.1 .
    AK289460 mRNA. Translation: BAF82149.1 .
    AC006942 Genomic DNA. Translation: AAD15565.1 .
    AC018766 Genomic DNA. No translation available.
    CH471177 Genomic DNA. Translation: EAW52546.1 .
    BC024312 mRNA. Translation: AAH24312.2 .
    BC065297 mRNA. Translation: AAH65297.1 .
    AF283769 mRNA. Translation: AAG15589.1 . Different initiation.
    CCDSi CCDS33075.1. [Q71SY5-1 ]
    RefSeqi NP_112235.2. NM_030973.3. [Q71SY5-1 ]
    UniGenei Hs.656639.
    Hs.745568.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KY6 NMR - A 391-553 [» ]
    2L23 NMR - A 391-548 [» ]
    2L6U NMR - A 391-543 [» ]
    2XNF NMR - A 394-543 [» ]
    ProteinModelPortali Q71SY5.
    SMRi Q71SY5. Positions 391-553.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123607. 43 interactions.
    DIPi DIP-31454N.
    IntActi Q71SY5. 15 interactions.
    MINTi MINT-5209896.

    PTM databases

    PhosphoSitei Q71SY5.

    Polymorphism databases

    DMDMi 158706143.

    Proteomic databases

    MaxQBi Q71SY5.
    PaxDbi Q71SY5.
    PRIDEi Q71SY5.

    Protocols and materials databases

    DNASUi 81857.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000312865 ; ENSP00000326767 ; ENSG00000104973 . [Q71SY5-1 ]
    ENST00000538643 ; ENSP00000437496 ; ENSG00000104973 . [Q71SY5-6 ]
    GeneIDi 81857.
    KEGGi hsa:81857.
    UCSCi uc002ppw.2. human. [Q71SY5-1 ]
    uc002ppx.1. human. [Q71SY5-4 ]

    Organism-specific databases

    CTDi 81857.
    GeneCardsi GC19P050321.
    GeneReviewsi MED25.
    H-InvDB HIX0015345.
    HGNCi HGNC:28845. MED25.
    MIMi 605589. phenotype.
    610197. gene.
    neXtProti NX_Q71SY5.
    Orphaneti 101101. Charcot-Marie-Tooth disease type 2B2.
    PharmGKBi PA134984839.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG79607.
    HOVERGENi HBG108127.
    KOi K15168.
    OMAi PGQMLLS.
    OrthoDBi EOG78H3SP.
    PhylomeDBi Q71SY5.
    TreeFami TF329598.

    Enzyme and pathway databases

    Reactomei REACT_116145. PPARA activates gene expression.
    REACT_12627. Generic Transcription Pathway.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.

    Miscellaneous databases

    ChiTaRSi MED25. human.
    EvolutionaryTracei Q71SY5.
    GeneWikii MED25.
    GenomeRNAii 81857.
    NextBioi 35482117.
    PROi Q71SY5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q71SY5.
    Bgeei Q71SY5.
    CleanExi HS_MED25.
    Genevestigatori Q71SY5.

    Family and domain databases

    InterProi IPR021394. Mediator_Med25.
    IPR021406. Mediator_Med25_NR-box.
    IPR021397. Mediator_Med25_SD1.
    IPR021419. Mediator_Med25_VWA.
    IPR002035. VWF_A.
    [Graphical view ]
    Pfami PF11232. Med25. 1 hit.
    PF11244. Med25_NR-box. 1 hit.
    PF11235. Med25_SD1. 1 hit.
    PF11265. Med25_VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53300. SSF53300. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A prostate-derived cDNA that is mapped to human chromosome 19 encodes a novel protein."
      Wang C., McCarty I.M., Balazs L., Li Y., Steiner M.S.
      Biochem. Biophys. Res. Commun. 296:281-287(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "A novel docking site on Mediator is critical for activation by VP16 in mammalian cells."
      Mittler G., Stuehler T., Santolin L., Uhlmann T., Kremmer E., Lottspeich F., Berti L., Meisterernst M.
      EMBO J. 22:6494-6504(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE, FUNCTION, IDENTIFICATION IN THE MEDIATOR COMPLEX, INTERACTION WITH VP16, ASSOCIATION WITH PROMOTER REGIONS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Testis.
    3. "The activator-recruited cofactor/Mediator coactivator subunit ARC92 is a functionally important target of the VP16 transcriptional activator."
      Yang F., DeBeaumont R., Zhou S., Naeaer A.M.
      Proc. Natl. Acad. Sci. U.S.A. 101:2339-2344(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PROTEIN SEQUENCE OF 1-11; 197-207; 241-254; 398-446 AND 520-530, FUNCTION, IDENTIFICATION IN THE MEDIATOR COMPLEX, INTERACTION WITH VP16, TISSUE SPECIFICITY.
    4. "Alternative splicing as a prevalent mechanism in regulating mammalian mediator tail subcomplex activity."
      Kivil A., Kazantseva A., Vinkel K.J.M., Sadam H., Neuman T., Palm K.
      Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), ALTERNATIVE SPLICING.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 159-747 (ISOFORM 5).
      Tissue: Eye and Lung.
    10. "Pediatric leukemia cDNA sequencing project."
      Villalon D.K., Luna R.A., Margolin J.K., Tsang Y.T.M., Hale S.M., Mei G., Bouck J., Gibbs R.A.
      Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 178-747 (ISOFORM 4).
      Tissue: Leukocyte.
    11. "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.
    12. "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: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
    13. "MED25 is distinct from TRAP220/MED1 in cooperating with CBP for retinoid receptor activation."
      Lee H.-K., Park U.-H., Kim E.-J., Um S.-J.
      EMBO J. 26:3545-3557(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ASSOCIATION WITH PROMOTER REGIONS, INTERACTION WITH CREBBP; ESR1; GR; MED1; MED6; RARA; RXRA AND THRB, MUTAGENESIS OF LEU-646 AND 649-LEU-LEU-650.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: STRUCTURE BY NMR OF 391-548.
    16. "Identification of the variant Ala335Val of MED25 as responsible for CMT2B2: molecular data, functional studies of the SH3 recognition motif and correlation between wild-type MED25 and PMP22 RNA levels in CMT1A animal models."
      Leal A., Huehne K., Bauer F., Sticht H., Berger P., Suter U., Morera B., Del Valle G., Lupski J.R., Ekici A., Pasutto F., Endele S., Barrantes R., Berghoff C., Berghoff M., Neundoerfer B., Heuss D., Dorn T.
      , Young P., Santolin L., Uhlmann T., Meisterernst M., Sereda M.W., Sereda M., Stassart R.M., Zu Horste G.M., Nave K.A., Reis A., Rautenstrauss B.
      Neurogenetics 10:275-287(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMT2B2 VAL-335.

    Entry informationi

    Entry nameiMED25_HUMAN
    AccessioniPrimary (citable) accession number: Q71SY5
    Secondary accession number(s): A8K095
    , B9TX30, O95783, Q6P143, Q6QMH5, Q707U4, Q8TB55, Q9H0L5, Q9HB34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 2, 2007
    Last sequence update: October 2, 2007
    Last modified: October 1, 2014
    This is version 84 of the entry and version 2 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 19
      Human chromosome 19: 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