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Mediator of RNA polymerase II transcription subunit 25 (Activator interaction domain-containing protein 1) (Activator-recruited cofactor 92 kDa component) (ARC92) (Mediator complex subunit 25) (p78)

 MED25_HUMAN             Reviewed;         747 AA.
Q71SY5; A8K095; B9TX30; O95783; Q6P143; Q6QMH5; Q707U4; Q8TB55;
Q9H0L5; Q9HB34;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
02-OCT-2007, sequence version 2.
20-JUN-2018, entry version 112.
RecName: Full=Mediator of RNA polymerase II transcription subunit 25;
AltName: Full=Activator interaction domain-containing protein 1;
AltName: Full=Activator-recruited cofactor 92 kDa component;
Short=ARC92;
AltName: Full=Mediator complex subunit 25;
AltName: Full=p78;
Name=MED25; Synonyms=ACID1, ARC92, PTOV2; ORFNames=TCBAP0758;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=12163014; DOI=10.1016/S0006-291X(02)00872-0;
Wang C., McCarty I.M., Balazs L., Li Y., Steiner M.S.;
"A prostate-derived cDNA that is mapped to human chromosome 19 encodes
a novel protein.";
Biochem. Biophys. Res. Commun. 296:281-287(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE,
FUNCTION, IDENTIFICATION IN THE MEDIATOR COMPLEX, INTERACTION WITH
VP16, ASSOCIATION WITH PROMOTER REGIONS, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=14657022; DOI=10.1093/emboj/cdg619;
Mittler G., Stuehler T., Santolin L., Uhlmann T., Kremmer E.,
Lottspeich F., Berti L., Meisterernst M.;
"A novel docking site on Mediator is critical for activation by VP16
in mammalian cells.";
EMBO J. 22:6494-6504(2003).
[3]
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, AND TISSUE SPECIFICITY.
PubMed=14983011; DOI=10.1073/pnas.0308676100;
Yang F., DeBeaumont R., Zhou S., Naeaer A.M.;
"The activator-recruited cofactor/Mediator coactivator subunit ARC92
is a functionally important target of the VP16 transcriptional
activator.";
Proc. Natl. Acad. Sci. U.S.A. 101:2339-2344(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), AND ALTERNATIVE SPLICING.
Kivil A., Kazantseva A., Vinkel K.J.M., Sadam H., Neuman T., Palm K.;
"Alternative splicing as a prevalent mechanism in regulating mammalian
mediator tail subcomplex activity.";
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
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.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 159-747 (ISOFORM 5).
TISSUE=Eye, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 178-747 (ISOFORM 4).
TISSUE=Leukocyte;
Villalon D.K., Luna R.A., Margolin J.K., Tsang Y.T.M., Hale S.M.,
Mei G., Bouck J., Gibbs R.A.;
"Pediatric leukemia cDNA sequencing project.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[11]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
MEDIATOR COMPLEX.
PubMed=15175163; DOI=10.1016/j.molcel.2004.05.006;
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.;
"A set of consensus mammalian mediator subunits identified by
multidimensional protein identification technology.";
Mol. Cell 14:685-691(2004).
[12]
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
COMPLEX, AND ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE
II.
PubMed=15989967; DOI=10.1016/j.molcel.2005.05.015;
Zhang X., Krutchinsky A., Fukuda A., Chen W., Yamamura S., Chait B.T.,
Roeder R.G.;
"MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation
enriched in RNA polymerase II and is required for ER-mediated
transcription.";
Mol. Cell 19:89-100(2005).
[13]
FUNCTION, ASSOCIATION WITH PROMOTER REGIONS, INTERACTION WITH CREBBP;
ESR1; GR; MED1; MED6; RARA; RXRA AND THRB, AND MUTAGENESIS OF LEU-646
AND 649-LEU-LEU-650.
PubMed=17641689; DOI=10.1038/sj.emboj.7601797;
Lee H.-K., Park U.-H., Kim E.-J., Um S.-J.;
"MED25 is distinct from TRAP220/MED1 in cooperating with CBP for
retinoid receptor activation.";
EMBO J. 26:3545-3557(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[15]
STRUCTURE BY NMR OF 391-548.
PubMed=20974256; DOI=10.1016/j.jsb.2010.10.011;
Bontems F., Verger A., Dewitte F., Lens Z., Baert J.L., Ferreira E.,
Launoit Y.D., Sizun C., Guittet E., Villeret V., Monte D.;
"NMR structure of the human Mediator MED25 ACID domain.";
J. Struct. Biol. 174:245-251(2011).
[16]
VARIANT CMT2B2 VAL-335.
PubMed=19290556; DOI=10.1007/s10048-009-0183-3;
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.;
"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.";
Neurogenetics 10:275-287(2009).
[17]
ERRATUM.
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 10:375-376(2009).
[18]
INVOLVEMENT IN BVSYS, VARIANT BVSYS CYS-39, AND CHARACTERIZATION OF
VARIANT BVSYS CYS-39.
PubMed=25792360; DOI=10.1007/s00439-015-1541-x;
Basel-Vanagaite L., Smirin-Yosef P., Essakow J.L., Tzur S.,
Lagovsky I., Maya I., Pasmanik-Chor M., Yeheskel A., Konen O.,
Orenstein N., Weisz Hubshman M., Drasinover V., Magal N.,
Peretz Amit G., Zalzstein Y., Zeharia A., Shohat M., Straussberg R.,
Monte D., Salmon-Divon M., Behar D.M.;
"Homozygous MED25 mutation implicated in eye-intellectual disability
syndrome.";
Hum. Genet. 134:577-587(2015).
[19]
VARIANT TRP-140.
PubMed=25527630; DOI=10.1136/jmedgenet-2014-102793;
Figueiredo T., Melo U.S., Pessoa A.L., Nobrega P.R., Kitajima J.P.,
Correa I., Zatz M., Kok F., Santos S.;
"Homozygous missense mutation in MED25 segregates with syndromic
intellectual disability in a large consanguineous family.";
J. Med. Genet. 52:123-127(2015).
-!- 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. Required for RARA/RXRA-mediated
transcription. {ECO:0000269|PubMed:14657022,
ECO:0000269|PubMed:14983011, ECO:0000269|PubMed:17641689}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:14657022,
ECO:0000269|PubMed:14983011, ECO:0000269|PubMed:15175163,
ECO:0000269|PubMed:15989967, ECO:0000269|PubMed:17641689}.
-!- INTERACTION:
Q6NXG1:ESRP1; NbExp=4; IntAct=EBI-394558, EBI-10213520;
Q96RN5:MED15; NbExp=2; IntAct=EBI-394558, EBI-394506;
Q9Y2X0:MED16; NbExp=2; IntAct=EBI-394558, EBI-394541;
P10276:RARA; NbExp=10; IntAct=EBI-394558, EBI-413374;
P19793:RXRA; NbExp=4; IntAct=EBI-394558, EBI-78598;
P28700:Rxra (xeno); NbExp=3; IntAct=EBI-394558, EBI-346715;
G8HBG2:UL48 (xeno); NbExp=5; IntAct=EBI-394558, EBI-15844956;
Q9NZC7-5:WWOX; NbExp=4; IntAct=EBI-394558, EBI-12040603;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14657022}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q71SY5-1; Sequence=Displayed;
Name=2;
IsoId=Q71SY5-2; Sequence=VSP_028144;
Name=3;
IsoId=Q71SY5-3; Sequence=VSP_028145;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q71SY5-4; Sequence=VSP_028146;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q71SY5-5; Sequence=VSP_028143;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q71SY5-6; Sequence=VSP_047570;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Highest levels in
brain, heart, kidney, peripheral leukocytes, placenta, skeletal
muscle and spleen. {ECO:0000269|PubMed:14657022,
ECO:0000269|PubMed:14983011}.
-!- DISEASE: 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. {ECO:0000269|PubMed:19290556}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Basel-Vanagaite-Smirin-Yosef syndrome (BVSYS)
[MIM:616449]: An autosomal recessive syndrome characterized by
eye, brain, cardiac and palatal abnormalities as well as growth
retardation, microcephaly and severe intellectual disability.
{ECO:0000269|PubMed:25792360}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the Mediator complex subunit 25 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG15589.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAB66680.1; Type=Frameshift; Positions=567; Evidence={ECO:0000305};
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EMBL; AF261072; AAM20739.1; -; mRNA.
EMBL; AJ617479; CAE84581.1; -; mRNA.
EMBL; AY533507; AAS45401.1; -; mRNA.
EMBL; AL136746; CAB66680.1; ALT_FRAME; mRNA.
EMBL; EU392500; ACB88862.1; -; mRNA.
EMBL; AK289460; BAF82149.1; -; mRNA.
EMBL; AC006942; AAD15565.1; -; Genomic_DNA.
EMBL; AC018766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471177; EAW52546.1; -; Genomic_DNA.
EMBL; BC024312; AAH24312.2; -; mRNA.
EMBL; BC065297; AAH65297.1; -; mRNA.
EMBL; AF283769; AAG15589.1; ALT_INIT; mRNA.
CCDS; CCDS33075.1; -. [Q71SY5-1]
RefSeq; NP_112235.2; NM_030973.3. [Q71SY5-1]
UniGene; Hs.656639; -.
UniGene; Hs.745568; -.
PDB; 2KY6; NMR; -; A=391-553.
PDB; 2L23; NMR; -; A=391-548.
PDB; 2L6U; NMR; -; A=391-543.
PDB; 2XNF; NMR; -; A=394-543.
PDBsum; 2KY6; -.
PDBsum; 2L23; -.
PDBsum; 2L6U; -.
PDBsum; 2XNF; -.
ProteinModelPortal; Q71SY5; -.
SMR; Q71SY5; -.
BioGrid; 123607; 47.
ComplexPortal; CPX-3227; Core mediator complex.
CORUM; Q71SY5; -.
DIP; DIP-31454N; -.
IntAct; Q71SY5; 48.
MINT; Q71SY5; -.
STRING; 9606.ENSP00000326767; -.
iPTMnet; Q71SY5; -.
PhosphoSitePlus; Q71SY5; -.
BioMuta; MED25; -.
DMDM; 158706143; -.
MaxQB; Q71SY5; -.
PaxDb; Q71SY5; -.
PeptideAtlas; Q71SY5; -.
PRIDE; Q71SY5; -.
ProteomicsDB; 68625; -.
ProteomicsDB; 68626; -. [Q71SY5-2]
ProteomicsDB; 68627; -. [Q71SY5-3]
ProteomicsDB; 68628; -. [Q71SY5-4]
ProteomicsDB; 68629; -. [Q71SY5-5]
DNASU; 81857; -.
Ensembl; ENST00000312865; ENSP00000326767; ENSG00000104973. [Q71SY5-1]
Ensembl; ENST00000538643; ENSP00000437496; ENSG00000104973. [Q71SY5-6]
GeneID; 81857; -.
KEGG; hsa:81857; -.
UCSC; uc002ppw.3; human. [Q71SY5-1]
CTD; 81857; -.
DisGeNET; 81857; -.
EuPathDB; HostDB:ENSG00000104973.14; -.
GeneCards; MED25; -.
GeneReviews; MED25; -.
H-InvDB; HIX0015345; -.
HGNC; HGNC:28845; MED25.
HPA; HPA068802; -.
MalaCards; MED25; -.
MIM; 605589; phenotype.
MIM; 610197; gene.
MIM; 616449; phenotype.
neXtProt; NX_Q71SY5; -.
OpenTargets; ENSG00000104973; -.
Orphanet; 101101; Charcot-Marie-Tooth disease type 2B2.
PharmGKB; PA134984839; -.
eggNOG; ENOG410IHD9; Eukaryota.
eggNOG; ENOG410Z0HI; LUCA.
GeneTree; ENSGT00520000055653; -.
HOVERGEN; HBG108127; -.
InParanoid; Q71SY5; -.
KO; K15168; -.
OMA; QPSVMED; -.
OrthoDB; EOG091G04LS; -.
PhylomeDB; Q71SY5; -.
TreeFam; TF329598; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-212436; Generic Transcription Pathway.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
ChiTaRS; MED25; human.
EvolutionaryTrace; Q71SY5; -.
GeneWiki; MED25; -.
GenomeRNAi; 81857; -.
PRO; PR:Q71SY5; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000104973; -.
CleanEx; HS_MED25; -.
ExpressionAtlas; Q71SY5; baseline and differential.
Genevisible; Q71SY5; HS.
GO; GO:0044798; C:nuclear transcription factor complex; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0042974; F:retinoic acid receptor binding; IPI:UniProtKB.
GO; GO:0046965; F:retinoid X receptor binding; IPI:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IMP:UniProtKB.
GO; GO:0035563; P:positive regulation of chromatin binding; IMP:UniProtKB.
GO; GO:2001178; P:positive regulation of mediator complex assembly; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
Gene3D; 2.40.290.30; -; 1.
InterPro; IPR021394; Med25_PTOV.
InterPro; IPR021406; Mediator_Med25_NR-box.
InterPro; IPR021397; Mediator_Med25_SD1.
InterPro; IPR021419; Mediator_Med25_VWA.
InterPro; IPR038196; PTOV_dom_sf.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF11232; Med25; 1.
Pfam; PF11244; Med25_NR-box; 1.
Pfam; PF11235; Med25_SD1; 1.
Pfam; PF11265; Med25_VWA; 1.
SUPFAM; SSF53300; SSF53300; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing;
Charcot-Marie-Tooth disease; Complete proteome;
Direct protein sequencing; Disease mutation; Mental retardation;
Methylation; Neurodegeneration; Neuropathy; Nucleus;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 747 Mediator of RNA polymerase II
transcription subunit 25.
/FTId=PRO_0000304952.
REGION 1 226 Interaction with the Mediator complex.
REGION 389 543 Interaction with VP16.
REGION 395 545 Interaction with CREBBP.
{ECO:0000269|PubMed:17641689}.
REGION 564 653 Interaction with RARA.
{ECO:0000269|PubMed:17641689}.
REGION 640 707 Interaction with RARA.
{ECO:0000269|PubMed:17641689}.
MOTIF 646 650 LXXLL motif.
COMPBIAS 200 381 Pro-rich.
COMPBIAS 565 735 Pro-rich.
MOD_RES 725 725 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q8VCB2}.
VAR_SEQ 61 273 Missing (in isoform 6).
{ECO:0000303|Ref.4}.
/FTId=VSP_047570.
VAR_SEQ 303 319 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_028143.
VAR_SEQ 671 747 QPPGAPALLPPPHQGLGQPQLGPPLLHPPPAQSWPAQLPPR
APLPGQMLLSGGPRGPVPQPGLQPSVMEDDILMDLI -> P
SPGPHNFPLGLHCQVRGPGGGQRSGLSVPAAPGLEHQDQVL
LGSKDIGSKNEGSPSRACSPASWRTTSSWISSESPTPNKVP
F (in isoform 2).
{ECO:0000303|PubMed:11230166,
ECO:0000303|PubMed:14657022}.
/FTId=VSP_028144.
VAR_SEQ 701 747 AQSWPAQLPPRAPLPGQMLLSGGPRGPVPQPGLQPSVMEDD
ILMDLI -> PATRGSCAAASAAPGPGAAPVGAPTPASTTC
PVLARTTSPSGSTASGKTKERRRGPCVSRKMGASLFLCGSE
EHAYVFNMQTNRVCVERIQPETPL (in isoform 3).
{ECO:0000303|PubMed:14983011}.
/FTId=VSP_028145.
VAR_SEQ 716 747 GQMLLSGGPRGPVPQPGLQPSVMEDDILMDLI -> AAKRK
REGEGRVFREKWERAYFFVEVKSMPMCLICKQIVSVLKEYN
LKRHYESKHSKSYDQYTEQTRRIRARPIWPDP (in
isoform 4). {ECO:0000303|Ref.10}.
/FTId=VSP_028146.
VARIANT 39 39 Y -> C (in BVSYS; the mutation impairs
interaction with the Mediator complex;
dbSNP:rs794729668).
{ECO:0000269|PubMed:25792360}.
/FTId=VAR_073949.
VARIANT 140 140 R -> W (found in a patient with syndromic
intellectual disability; unknown
pathological significance;
dbSNP:rs781140315).
{ECO:0000269|PubMed:25527630}.
/FTId=VAR_073950.
VARIANT 335 335 A -> V (in CMT2B2; dbSNP:rs145770066).
{ECO:0000269|PubMed:19290556}.
/FTId=VAR_063521.
MUTAGEN 646 646 L->A: Abrogates interaction with RARA.
{ECO:0000269|PubMed:17641689}.
MUTAGEN 649 650 LL->AA: Abrogates interaction with RARA.
{ECO:0000269|PubMed:17641689}.
CONFLICT 20 20 F -> S (in Ref. 1; AAM20739).
{ECO:0000305}.
CONFLICT 236 236 P -> L (in Ref. 2; CAE84581 and 4;
CAB66680). {ECO:0000305}.
CONFLICT 268 268 V -> I (in Ref. 1; AAM20739).
{ECO:0000305}.
CONFLICT 514 514 L -> M (in Ref. 3; AAS45401).
{ECO:0000305}.
CONFLICT 536 536 G -> D (in Ref. 3; AAS45401).
{ECO:0000305}.
CONFLICT 703 703 S -> F (in Ref. 1; AAM20739).
{ECO:0000305}.
STRAND 396 409 {ECO:0000244|PDB:2KY6}.
STRAND 414 417 {ECO:0000244|PDB:2KY6}.
STRAND 424 434 {ECO:0000244|PDB:2KY6}.
HELIX 441 443 {ECO:0000244|PDB:2KY6}.
STRAND 446 454 {ECO:0000244|PDB:2KY6}.
HELIX 455 461 {ECO:0000244|PDB:2KY6}.
HELIX 462 465 {ECO:0000244|PDB:2KY6}.
STRAND 466 475 {ECO:0000244|PDB:2KY6}.
STRAND 476 478 {ECO:0000244|PDB:2L6U}.
HELIX 480 493 {ECO:0000244|PDB:2KY6}.
STRAND 494 499 {ECO:0000244|PDB:2KY6}.
STRAND 502 504 {ECO:0000244|PDB:2L23}.
STRAND 510 515 {ECO:0000244|PDB:2KY6}.
TURN 517 519 {ECO:0000244|PDB:2KY6}.
STRAND 521 529 {ECO:0000244|PDB:2KY6}.
HELIX 530 545 {ECO:0000244|PDB:2KY6}.
SEQUENCE 747 AA; 78171 MW; 6FE13FB45786402D CRC64;
MVPGSEGPAR AGSVVADVVF VIEGTANLGP YFEGLRKHYL LPAIEYFNGG PPAETDFGGD
YGGTQYSLVV FNTVDCAPES YVQCHAPTSS AYEFVTWLDG IKFMGGGGES CSLIAEGLST
ALQLFDDFKK MREQIGQTHR VCLLICNSPP YLLPAVESTT YSGCTTENLV QQIGERGIHF
SIVSPRKLPA LRLLFEKAAP PALLEPLQPP TDVSQDPRHM VLVRGLVLPV GGGSAPGPLQ
SKQPVPLPPA APSGATLSAA PQQPLPPVPP QYQVPGNLSA AQVAAQNAVE AAKNQKAGLG
PRFSPITPLQ QAAPGVGPPF SQAPAPQLPP GPPGAPKPPP ASQPSLVSTV APGSGLAPTA
QPGAPSMAGT VAPGGVSGPS PAQLGAPALG GQQSVSNKLL AWSGVLEWQE KPKPASVDAN
TKLTRSLPCQ VYVNHGENLK TEQWPQKLIM QLIPQQLLTT LGPLFRNSRM VQFHFTNKDL
ESLKGLYRIM GNGFAGCVHF PHTAPCEVRV LMLLYSSKKK IFMGLIPYDQ SGFVNGIRQV
ITNHKQVQQQ KLEQQQRGMG GQQAPPGLGP ILEDQARPSQ NLLQLRPPQP QPQGTVGASG
ATGQPQPQGT AQPPPGAPQG PPGAASGPPP PGPILRPQNP GANPQLRSLL LNPPPPQTGV
PPPQASLHHL QPPGAPALLP PPHQGLGQPQ LGPPLLHPPP AQSWPAQLPP RAPLPGQMLL
SGGPRGPVPQ PGLQPSVMED DILMDLI


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