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Mediator of RNA polymerase II transcription subunit 12 (Activator-recruited cofactor 240 kDa component) (ARC240) (CAG repeat protein 45) (Mediator complex subunit 12) (OPA-containing protein) (Thyroid hormone receptor-associated protein complex 230 kDa component) (Trap230) (Trinucleotide repeat-containing gene 11 protein)

 MED12_HUMAN             Reviewed;        2177 AA.
Q93074; O15410; O75557; Q9UHV6; Q9UND7;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
14-OCT-2008, sequence version 4.
22-NOV-2017, entry version 176.
RecName: Full=Mediator of RNA polymerase II transcription subunit 12;
AltName: Full=Activator-recruited cofactor 240 kDa component;
Short=ARC240;
AltName: Full=CAG repeat protein 45;
AltName: Full=Mediator complex subunit 12;
AltName: Full=OPA-containing protein;
AltName: Full=Thyroid hormone receptor-associated protein complex 230 kDa component;
Short=Trap230;
AltName: Full=Trinucleotide repeat-containing gene 11 protein;
Name=MED12; Synonyms=ARC240, CAGH45, HOPA, KIAA0192, TNRC11, TRAP230;
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), PROTEIN SEQUENCE OF 788-802
(ISOFORMS 1/2/3), IDENTIFICATION IN THE TRAP COMPLEX, TISSUE
SPECIFICITY, AND VARIANT ARG-1392.
TISSUE=Cervix carcinoma;
PubMed=10198638; DOI=10.1016/S1097-2765(00)80463-3;
Ito M., Yuan C.-X., Malik S., Gu W., Fondell J.D., Yamamura S.,
Fu Z.-Y., Zhang X., Qin J., Roeder R.G.;
"Identity between TRAP and SMCC complexes indicates novel pathways for
the function of nuclear receptors and diverse mammalian activators.";
Mol. Cell 3:361-370(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 54-2177 (ISOFORM 1), AND
VARIANT ARG-1392.
TISSUE=Bone marrow;
PubMed=8724849; DOI=10.1093/dnares/3.1.17;
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. V.
The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 3:17-24(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 154-2177 (ISOFORM 3).
PubMed=9702738; DOI=10.1038/sj.mp.4000442;
Philibert R.A., King B.H., Cook E.H., Lee Y.-H., Stubblefield B.,
Damschroder-Williams P., Dea C., Palotie A., Tengstrom C.,
Martin B.M., Ginns E.I.;
"Association of an X-chromosome dodecamer insertional variant allele
with mental retardation.";
Mol. Psychiatry 3:303-309(1998).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 154-2177 (ISOFORM 3).
PubMed=10480376; DOI=10.1007/s004399900084;
Philibert R.A., Winfield S.L., Damschroder-Williams P., Tengstrom C.,
Martin B.M., Ginns E.I.;
"The genomic structure and developmental expression patterns of the
human OPA-containing gene (HOPA).";
Hum. Genet. 105:174-178(1999).
[6]
PROTEIN SEQUENCE OF 386-418 (ISOFORMS 1/2/3), AND IDENTIFICATION IN
THE ARC COMPLEX.
TISSUE=Cervix carcinoma;
PubMed=10235266; DOI=10.1038/19783;
Rachez C., Lemon B.D., Suldan Z., Bromleigh V., Gamble M.,
Naeaer A.M., Erdjument-Bromage H., Tempst P., Freedman L.P.;
"Ligand-dependent transcription activation by nuclear receptors
requires the DRIP complex.";
Nature 398:824-828(1999).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1529-2177 (ISOFORM 2).
TISSUE=Brain;
PubMed=9225980; DOI=10.1007/s004390050476;
Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S.,
Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A.;
"cDNAs with long CAG trinucleotide repeats from human brain.";
Hum. Genet. 100:114-122(1997).
[8]
PROTEIN SEQUENCE OF 1674-1682 AND 1771-1782 (ISOFORMS 1/2/3), AND
IDENTIFICATION IN THE ARC COMPLEX.
PubMed=10235267; DOI=10.1038/19789;
Naeaer A.M., Beaurang P.A., Zhou S., Abraham S., Solomon W.B.,
Tjian R.;
"Composite co-activator ARC mediates chromatin-directed
transcriptional activation.";
Nature 398:828-832(1999).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
COMPLEX, AND INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE
II.
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).
[10]
INTERACTION WITH MED1; MED18; MED21; MED28; MED29 AND MED30,
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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
FUNCTION, AND INTERACTION WITH CTNNB1 AND MED30.
PubMed=16565090; DOI=10.1074/jbc.M602696200;
Kim S., Xu X., Hecht A., Boyer T.G.;
"Mediator is a transducer of Wnt/beta-catenin signaling.";
J. Biol. Chem. 281:14066-14075(2006).
[13]
FUNCTION, AND INTERACTION WITH MED1 AND MED10.
PubMed=16595664; DOI=10.1074/jbc.M601983200;
Baek H.J., Kang Y.K., Roeder R.G.;
"Human Mediator enhances basal transcription by facilitating
recruitment of transcription factor IIB during preinitiation complex
assembly.";
J. Biol. Chem. 281:15172-15181(2006).
[14]
FUNCTION, AND INTERACTION WITH CDK8; CTNNB1 AND GLI3.
PubMed=17000779; DOI=10.1128/MCB.00443-06;
Zhou H., Kim S., Ishii S., Boyer T.G.;
"Mediator modulates Gli3-dependent Sonic hedgehog signaling.";
Mol. Cell. Biol. 26:8667-8682(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635 AND SER-1258, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-166, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635; SER-1258 AND
SER-1269, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635; SER-698 AND
SER-700, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635; SER-665 AND
SER-698, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1994 AND ARG-2015, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[23]
VARIANT LUJFRYS SER-1007.
PubMed=17369503; DOI=10.1136/jmg.2006.048637;
Schwartz C.E., Tarpey P.S., Lubs H.A., Verloes A., May M.M.,
Risheg H., Friez M.J., Futreal P.A., Edkins S., Teague J., Briault S.,
Skinner C., Bauer-Carlin A., Simensen R.J., Joseph S.M., Jones J.R.,
Gecz J., Stratton M.R., Raymond F.L., Stevenson R.E.;
"The original Lujan syndrome family has a novel missense mutation
(p.N1007S) in the MED12 gene.";
J. Med. Genet. 44:472-477(2007).
[24]
VARIANT OKS TRP-961.
PubMed=17334363; DOI=10.1038/ng1992;
Risheg H., Graham J.M. Jr., Clark R.D., Rogers R.C., Opitz J.M.,
Moeschler J.B., Peiffer A.P., May M., Joseph S.M., Jones J.R.,
Stevenson R.E., Schwartz C.E., Friez M.J.;
"A recurrent mutation in MED12 leading to R961W causes Opitz-Kaveggia
syndrome.";
Nat. Genet. 39:451-453(2007).
[25]
VARIANTS OHDOX HIS-1148; PRO-1165 AND ASN-1729.
PubMed=23395478; DOI=10.1016/j.ajhg.2013.01.007;
Vulto-van Silfhout A.T., de Vries B.B., van Bon B.W., Hoischen A.,
Ruiterkamp-Versteeg M., Gilissen C., Gao F., van Zwam M.,
Harteveld C.L., van Essen A.J., Hamel B.C., Kleefstra T.,
Willemsen M.A., Yntema H.G., van Bokhoven H., Brunner H.G.,
Boyer T.G., de Brouwer A.P.;
"Mutations in MED12 cause X-linked Ohdo syndrome.";
Am. J. Hum. Genet. 92:401-406(2013).
[26]
VARIANT HIS-1974.
PubMed=26273451; DOI=10.1002/ccr3.301;
Bouazzi H., Lesca G., Trujillo C., Alwasiyah M.K., Munnich A.;
"Nonsyndromic X-linked intellectual deficiency in three brothers with
a novel MED12 missense mutation [c.5922G>T (p.Glu1974His)].";
Clin. Case Rep. 3:604-609(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. This subunit may specifically regulate
transcription of targets of the Wnt signaling pathway and SHH
signaling pathway. {ECO:0000269|PubMed:16565090,
ECO:0000269|PubMed:16595664, ECO:0000269|PubMed:17000779}.
-!- 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. Also interacts with CTNNB1 and GLI3.
{ECO:0000269|PubMed:10198638, ECO:0000269|PubMed:10235266,
ECO:0000269|PubMed:10235267, ECO:0000269|PubMed:15175163,
ECO:0000269|PubMed:15989967, ECO:0000269|PubMed:16565090,
ECO:0000269|PubMed:16595664, ECO:0000269|PubMed:17000779}.
-!- INTERACTION:
P51693:APLP1; NbExp=2; IntAct=EBI-394357, EBI-74648;
Q06481:APLP2; NbExp=2; IntAct=EBI-394357, EBI-79306;
P05067:APP; NbExp=2; IntAct=EBI-394357, EBI-77613;
Q9NPJ6:MED4; NbExp=6; IntAct=EBI-394357, EBI-394607;
P37173:TGFBR2; NbExp=3; IntAct=EBI-394357, EBI-296151;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q93074-1; Sequence=Displayed;
Name=2;
IsoId=Q93074-2; Sequence=VSP_035520;
Name=3;
IsoId=Q93074-3; Sequence=VSP_035521;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10198638}.
-!- DISEASE: Opitz-Kaveggia syndrome (OKS) [MIM:305450]: X-linked
disorder characterized by mental retardation, relative
macrocephaly, hypotonia and constipation.
{ECO:0000269|PubMed:17334363}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Lujan-Fryns syndrome (LUJFRYS) [MIM:309520]: Clinically,
Lujan-Fryns syndrome can be distinguished from Opitz-Kaveggia
syndrome by tall stature, hypernasal voice, hyperextensible digits
and high nasal root. {ECO:0000269|PubMed:17369503}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Ohdo syndrome, X-linked (OHDOX) [MIM:300895]: A syndrome
characterized by mental retardation, feeding problems, and
distinctive facial appearance with coarse facial features, severe
blepharophimosis, ptosis, a bulbous nose, micrognathia and a small
mouth. Dental hypoplasia and deafness can be considered as common
manifestations of the syndrome. Male patients show cryptorchidism
and scrotal hypoplasia. {ECO:0000269|PubMed:23395478}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the Mediator complex subunit 12 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD22033.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF117755; AAD22033.1; ALT_INIT; mRNA.
EMBL; AL590764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; D83783; BAA12112.1; -; mRNA.
EMBL; AF071309; AAC83163.1; -; mRNA.
EMBL; AF132033; AAD44162.1; -; Genomic_DNA.
EMBL; U80742; AAB91440.1; -; mRNA.
CCDS; CCDS43970.1; -. [Q93074-1]
RefSeq; NP_005111.2; NM_005120.2. [Q93074-1]
UniGene; Hs.409226; -.
ProteinModelPortal; Q93074; -.
BioGrid; 115293; 89.
CORUM; Q93074; -.
DIP; DIP-31459N; -.
IntAct; Q93074; 67.
STRING; 9606.ENSP00000363193; -.
iPTMnet; Q93074; -.
PhosphoSitePlus; Q93074; -.
BioMuta; MED12; -.
DMDM; 209572775; -.
EPD; Q93074; -.
MaxQB; Q93074; -.
PaxDb; Q93074; -.
PeptideAtlas; Q93074; -.
PRIDE; Q93074; -.
Ensembl; ENST00000374080; ENSP00000363193; ENSG00000184634. [Q93074-1]
Ensembl; ENST00000374102; ENSP00000363215; ENSG00000184634. [Q93074-3]
GeneID; 9968; -.
KEGG; hsa:9968; -.
UCSC; uc004dyy.4; human. [Q93074-1]
CTD; 9968; -.
DisGeNET; 9968; -.
EuPathDB; HostDB:ENSG00000184634.15; -.
GeneCards; MED12; -.
GeneReviews; MED12; -.
HGNC; HGNC:11957; MED12.
HPA; HPA003184; -.
HPA; HPA003185; -.
MalaCards; MED12; -.
MIM; 300188; gene.
MIM; 300895; phenotype.
MIM; 305450; phenotype.
MIM; 309520; phenotype.
neXtProt; NX_Q93074; -.
OpenTargets; ENSG00000184634; -.
Orphanet; 293707; Blepharophimosis-intellectual disability syndrome, MKB type.
Orphanet; 93932; FG syndrome type 1.
Orphanet; 776; X-linked intellectual disability with marfanoid habitus.
Orphanet; 777; X-linked non-syndromic intellectual disability.
PharmGKB; PA36645; -.
eggNOG; ENOG410ISJR; Eukaryota.
eggNOG; ENOG41119EY; LUCA.
GeneTree; ENSGT00440000037505; -.
HOGENOM; HOG000231423; -.
HOVERGEN; HBG052447; -.
InParanoid; Q93074; -.
KO; K15162; -.
OMA; MAQVFEG; -.
OrthoDB; EOG091G00I6; -.
PhylomeDB; Q93074; -.
TreeFam; TF324178; -.
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.
SignaLink; Q93074; -.
SIGNOR; Q93074; -.
ChiTaRS; MED12; human.
GeneWiki; MED12; -.
GenomeRNAi; 9968; -.
PRO; PR:Q93074; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000184634; -.
CleanEx; HS_MED12; -.
ExpressionAtlas; Q93074; baseline and differential.
Genevisible; Q93074; HS.
GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
GO; GO:0008013; F:beta-catenin binding; IEA:InterPro.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; NAS:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0004872; F:receptor activity; IDA:UniProtKB.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; IBA:GO_Central.
GO; GO:0001104; F:RNA polymerase II transcription cofactor activity; IDA:UniProtKB.
GO; GO:0046966; F:thyroid hormone receptor binding; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
GO; GO:0003712; F:transcription cofactor activity; IDA:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
GO; GO:0042809; F:vitamin D receptor binding; NAS:UniProtKB.
GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
GO; GO:0090245; P:axis elongation involved in somitogenesis; IEA:Ensembl.
GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:1990403; P:embryonic brain development; IEA:Ensembl.
GO; GO:0048702; P:embryonic neurocranium morphogenesis; IEA:Ensembl.
GO; GO:0007492; P:endoderm development; IEA:Ensembl.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IDA:UniProtKB.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0014003; P:oligodendrocyte development; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0036342; P:post-anal tail morphogenesis; IEA:Ensembl.
GO; GO:0014044; P:Schwann cell development; IEA:Ensembl.
GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IEA:Ensembl.
InterPro; IPR019035; Mediator_Med12.
InterPro; IPR021989; Mediator_Med12_catenin-bd.
InterPro; IPR021990; Mediator_Med12_LCEWAV.
Pfam; PF09497; Med12; 1.
Pfam; PF12145; Med12-LCEWAV; 1.
Pfam; PF12144; Med12-PQL; 1.
SMART; SM01281; Med12; 1.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Complete proteome;
Direct protein sequencing; Disease mutation; Mental retardation;
Methylation; Nucleus; Phosphoprotein; Reference proteome; Repressor;
Transcription; Transcription regulation.
CHAIN 1 2177 Mediator of RNA polymerase II
transcription subunit 12.
/FTId=PRO_0000096359.
REGION 1616 2051 Interaction with CTNNB1 and GLI3.
{ECO:0000269|PubMed:17000779}.
COMPBIAS 1732 1777 Pro-rich.
COMPBIAS 1900 2168 Gln-rich.
MOD_RES 80 80 N6-acetyllysine.
{ECO:0000250|UniProtKB:A2AGH6}.
MOD_RES 166 166 Phosphotyrosine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 635 635 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 665 665 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 698 698 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 700 700 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1258 1258 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 1269 1269 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 1798 1798 N6-acetyllysine.
{ECO:0000250|UniProtKB:A2AGH6}.
MOD_RES 1899 1899 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:A2AGH6}.
MOD_RES 1899 1899 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:A2AGH6}.
MOD_RES 1910 1910 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:A2AGH6}.
MOD_RES 1994 1994 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 2015 2015 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
VAR_SEQ 1916 1916 Q -> QAKI (in isoform 2).
{ECO:0000303|PubMed:9225980}.
/FTId=VSP_035520.
VAR_SEQ 1916 1916 Missing (in isoform 3).
{ECO:0000303|PubMed:10480376,
ECO:0000303|PubMed:9702738}.
/FTId=VSP_035521.
VARIANT 961 961 R -> W (in OKS; dbSNP:rs80338758).
{ECO:0000269|PubMed:17334363}.
/FTId=VAR_033112.
VARIANT 1007 1007 N -> S (in LUJFRYS; dbSNP:rs80338759).
{ECO:0000269|PubMed:17369503}.
/FTId=VAR_037534.
VARIANT 1148 1148 R -> H (in OHDOX; dbSNP:rs387907360).
{ECO:0000269|PubMed:23395478}.
/FTId=VAR_069770.
VARIANT 1165 1165 S -> P (in OHDOX; dbSNP:rs387907361).
{ECO:0000269|PubMed:23395478}.
/FTId=VAR_069771.
VARIANT 1392 1392 Q -> R (in dbSNP:rs1139013).
{ECO:0000269|PubMed:10198638,
ECO:0000269|PubMed:8724849}.
/FTId=VAR_046672.
VARIANT 1729 1729 H -> N (in OHDOX; dbSNP:rs387907362).
{ECO:0000269|PubMed:23395478}.
/FTId=VAR_069772.
VARIANT 1974 1974 Q -> H (found in a family with X-linked
intellectual disability; unknown
pathological significance;
dbSNP:rs879255528).
{ECO:0000269|PubMed:26273451}.
/FTId=VAR_074018.
CONFLICT 16 16 R -> RPR (in Ref. 1; AAD22033).
{ECO:0000305}.
CONFLICT 397 397 Missing (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 1166 1166 E -> V (in Ref. 5; AAD44162).
{ECO:0000305}.
SEQUENCE 2177 AA; 243081 MW; 7492B07BA0F6EA9D CRC64;
MAAFGILSYE HRPLKRPRLG PPDVYPQDPK QKEDELTALN VKQGFNNQPA VSGDEHGSAK
NVSFNPAKIS SNFSSIIAEK LRCNTLPDTG RRKPQVNQKD NFWLVTARSQ SAINTWFTDL
AGTKPLTQLA KKVPIFSKKE EVFGYLAKYT VPVMRAAWLI KMTCAYYAAI SETKVKKRHV
DPFMEWTQII TKYLWEQLQK MAEYYRPGPA GSGGCGSTIG PLPHDVEVAI RQWDYTEKLA
MFMFQDGMLD RHEFLTWVLE CFEKIRPGED ELLKLLLPLL LRYSGEFVQS AYLSRRLAYF
CTRRLALQLD GVSSHSSHVI SAQSTSTLPT TPAPQPPTSS TPSTPFSDLL MCPQHRPLVF
GLSCILQTIL LCCPSALVWH YSLTDSRIKT GSPLDHLPIA PSNLPMPEGN SAFTQQVRAK
LREIEQQIKE RGQAVEVRWS FDKCQEATAG FTIGRVLHTL EVLDSHSFER SDFSNSLDSL
CNRIFGLGPS KDGHEISSDD DAVVSLLCEW AVSCKRSGRH RAMVVAKLLE KRQAEIEAER
CGESEAADEK GSIASGSLSA PSAPIFQDVL LQFLDTQAPM LTDPRSESER VEFFNLVLLF
CELIRHDVFS HNMYTCTLIS RGDLAFGAPG PRPPSPFDDP ADDPEHKEAE GSSSSKLEDP
GLSESMDIDP SSSVLFEDME KPDFSLFSPT MPCEGKGSPS PEKPDVEKEV KPPPKEKIEG
TLGVLYDQPR HVQYATHFPI PQEESCSHEC NQRLVVLFGV GKQRDDARHA IKKITKDILK
VLNRKGTAET DQLAPIVPLN PGDLTFLGGE DGQKRRRNRP EAFPTAEDIF AKFQHLSHYD
QHQVTAQVSR NVLEQITSFA LGMSYHLPLV QHVQFIFDLM EYSLSISGLI DFAIQLLNEL
SVVEAELLLK SSDLVGSYTT SLCLCIVAVL RHYHACLILN QDQMAQVFEG LCGVVKHGMN
RSDGSSAERC ILAYLYDLYT SCSHLKNKFG ELFSDFCSKV KNTIYCNVEP SESNMRWAPE
FMIDTLENPA AHTFTYTGLG KSLSENPANR YSFVCNALMH VCVGHHDPDR VNDIAILCAE
LTGYCKSLSA EWLGVLKALC CSSNNGTCGF NDLLCNVDVS DLSFHDSLAT FVAILIARQC
LLLEDLIRCA AIPSLLNAAC SEQDSEPGAR LTCRILLHLF KTPQLNPCQS DGNKPTVGIR
SSCDRHLLAA SQNRIVDGAV FAVLKAVFVL GDAELKGSGF TVTGGTEELP EEEGGGGSGG
RRQGGRNISV ETASLDVYAK YVLRSICQQE WVGERCLKSL CEDSNDLQDP VLSSAQAQRL
MQLICYPHRL LDNEDGENPQ RQRIKRILQN LDQWTMRQSS LELQLMIKQT PNNEMNSLLE
NIAKATIEVF QQSAETGSSS GSTASNMPSS SKTKPVLSSL ERSGVWLVAP LIAKLPTSVQ
GHVLKAAGEE LEKGQHLGSS SRKERDRQKQ KSMSLLSQQP FLSLVLTCLK GQDEQREGLL
TSLYSQVHQI VNNWRDDQYL DDCKPKQLMH EALKLRLNLV GGMFDTVQRS TQQTTEWAML
LLEIIISGTV DMQSNNELFT TVLDMLSVLI NGTLAADMSS ISQGSMEENK RAYMNLAKKL
QKELGERQSD SLEKVRQLLP LPKQTRDVIT CEPQGSLIDT KGNKIAGFDS IFKKEGLQVS
TKQKISPWDL FEGLKPSAPL SWGWFGTVRV DRRVARGEEQ QRLLLYHTHL RPRPRAYYLE
PLPLPPEDEE PPAPTLLEPE KKAPEPPKTD KPGAAPPSTE ERKKKSTKGK KRSQPATKTE
DYGMGPGRSG PYGVTVPPDL LHHPNPGSIT HLNYRQGSIG LYTQNQPLPA GGPRVDPYRP
VRLPMQKLPT RPTYPGVLPT TMTGVMGLEP SSYKTSVYRQ QQPAVPQGQR LRQQLQQSQG
MLGQSSVHQM TPSSSYGLQT SQGYTPYVSH VGLQQHTGPA GTMVPPSYSS QPYQSTHPST
NPTLVDPTRH LQQRPSGYVH QQAPTYGHGL TSTQRFSHQT LQQTPMISTM TPMSAQGVQA
GVRSTAILPE QQQQQQQQQQ QQQQQQQQQQ QQQQQQYHIR QQQQQQILRQ QQQQQQQQQQ
QQQQQQQQQQ QQQQQHQQQQ QQQAAPPQPQ PQSQPQFQRQ GLQQTQQQQQ TAALVRQLQQ
QLSNTQPQPS TNIFGRY


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