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Q93074 (MED12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mediator of RNA polymerase II transcription subunit 12
Alternative name(s):
Activator-recruited cofactor 240 kDa component
Short name=ARC240
CAG repeat protein 45
Mediator complex subunit 12
OPA-containing protein
Thyroid hormone receptor-associated protein complex 230 kDa component
Short name=Trap230
Trinucleotide repeat-containing gene 11 protein
Gene names
Name:MED12
Synonyms:ARC240, CAGH45, HOPA, KIAA0192, TNRC11, TRAP230
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2177 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. This subunit may specifically regulate transcription of targets of the Wnt signaling pathway and SHH signaling pathway. Ref.12 Ref.13 Ref.14

Subunit structure

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. Ref.1 Ref.6 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14

Subcellular location

Nucleus Probable.

Tissue specificity

Ubiquitous. Ref.1

Involvement in disease

Opitz-Kaveggia syndrome (OKS) [MIM:305450]: X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22

Sequence similarities

Belongs to the Mediator complex subunit 12 family.

Sequence caution

The sequence AAD22033.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Mental retardation
   Molecular functionActivator
Repressor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processSchwann cell development

Inferred from electronic annotation. Source: Ensembl

Wnt signaling pathway, planar cell polarity pathway

Inferred from electronic annotation. Source: Ensembl

androgen receptor signaling pathway

Inferred from direct assay PubMed 12218053. Source: UniProtKB

axis elongation involved in somitogenesis

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

heart development

Inferred from electronic annotation. Source: Ensembl

intracellular steroid hormone receptor signaling pathway

Inferred from direct assay PubMed 11867769. Source: UniProtKB

negative regulation of Wnt signaling pathway

Inferred from mutant phenotype Ref.14. Source: UniProtKB

neural tube closure

Inferred from electronic annotation. Source: Ensembl

oligodendrocyte development

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12037571. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: UniProtKB

stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

transcription initiation from RNA polymerase II promoter

Inferred from direct assay PubMed 12218053. Source: UniProtKB

   Cellular_componentmediator complex

Inferred from direct assay Ref.1. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.8Ref.14. Source: UniProtKB

   Molecular_functionRNA polymerase II distal enhancer sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II transcription cofactor activity

Inferred from direct assay Ref.1. Source: UniProtKB

RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from electronic annotation. Source: Ensembl

ligand-dependent nuclear receptor transcription coactivator activity

Non-traceable author statement Ref.6. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction Ref.14. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 11984006. Source: UniProtKB

receptor activity

Inferred from direct assay PubMed 12218053. Source: UniProtKB

thyroid hormone receptor binding

Inferred from direct assay Ref.1. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay PubMed 12037571. Source: MGI

transcription cofactor activity

Inferred from direct assay PubMed 12218053. Source: UniProtKB

vitamin D receptor binding

Non-traceable author statement Ref.6. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q93074-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q93074-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1916-1916: Q → QAKI
Isoform 3 (identifier: Q93074-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1916-1916: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21772177Mediator of RNA polymerase II transcription subunit 12
PRO_0000096359

Regions

Region1616 – 2051436Interaction with CTNNB1 and GLI3
Compositional bias1732 – 177746Pro-rich
Compositional bias1900 – 2168269Gln-rich

Amino acid modifications

Modified residue801N6-acetyllysine By similarity
Modified residue1661Phosphotyrosine Ref.16
Modified residue6351Phosphoserine Ref.11 Ref.15 Ref.17 Ref.18
Modified residue12581Phosphoserine Ref.15 Ref.17
Modified residue12691Phosphoserine Ref.17
Modified residue17981N6-acetyllysine By similarity

Natural variations

Alternative sequence19161Q → QAKI in isoform 2.
VSP_035520
Alternative sequence19161Missing in isoform 3.
VSP_035521
Natural variant9611R → W in OKS. Ref.21
VAR_033112
Natural variant10071N → S in LUJFRYS. Ref.20
VAR_037534
Natural variant11481R → H in OHDOX. Ref.22
VAR_069770
Natural variant11651S → P in OHDOX. Ref.22
VAR_069771
Natural variant13921Q → R. Ref.1 Ref.3
Corresponds to variant rs1139013 [ dbSNP | Ensembl ].
VAR_046672
Natural variant17291H → N in OHDOX. Ref.22
VAR_069772

Experimental info

Sequence conflict161R → RPR in AAD22033. Ref.1
Sequence conflict3971Missing AA sequence Ref.6
Sequence conflict11661E → V in AAD44162. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 14, 2008. Version 4.
Checksum: 7492B07BA0F6EA9D

FASTA2,177243,081
        10         20         30         40         50         60 
MAAFGILSYE HRPLKRPRLG PPDVYPQDPK QKEDELTALN VKQGFNNQPA VSGDEHGSAK 

        70         80         90        100        110        120 
NVSFNPAKIS SNFSSIIAEK LRCNTLPDTG RRKPQVNQKD NFWLVTARSQ SAINTWFTDL 

       130        140        150        160        170        180 
AGTKPLTQLA KKVPIFSKKE EVFGYLAKYT VPVMRAAWLI KMTCAYYAAI SETKVKKRHV 

       190        200        210        220        230        240 
DPFMEWTQII TKYLWEQLQK MAEYYRPGPA GSGGCGSTIG PLPHDVEVAI RQWDYTEKLA 

       250        260        270        280        290        300 
MFMFQDGMLD RHEFLTWVLE CFEKIRPGED ELLKLLLPLL LRYSGEFVQS AYLSRRLAYF 

       310        320        330        340        350        360 
CTRRLALQLD GVSSHSSHVI SAQSTSTLPT TPAPQPPTSS TPSTPFSDLL MCPQHRPLVF 

       370        380        390        400        410        420 
GLSCILQTIL LCCPSALVWH YSLTDSRIKT GSPLDHLPIA PSNLPMPEGN SAFTQQVRAK 

       430        440        450        460        470        480 
LREIEQQIKE RGQAVEVRWS FDKCQEATAG FTIGRVLHTL EVLDSHSFER SDFSNSLDSL 

       490        500        510        520        530        540 
CNRIFGLGPS KDGHEISSDD DAVVSLLCEW AVSCKRSGRH RAMVVAKLLE KRQAEIEAER 

       550        560        570        580        590        600 
CGESEAADEK GSIASGSLSA PSAPIFQDVL LQFLDTQAPM LTDPRSESER VEFFNLVLLF 

       610        620        630        640        650        660 
CELIRHDVFS HNMYTCTLIS RGDLAFGAPG PRPPSPFDDP ADDPEHKEAE GSSSSKLEDP 

       670        680        690        700        710        720 
GLSESMDIDP SSSVLFEDME KPDFSLFSPT MPCEGKGSPS PEKPDVEKEV KPPPKEKIEG 

       730        740        750        760        770        780 
TLGVLYDQPR HVQYATHFPI PQEESCSHEC NQRLVVLFGV GKQRDDARHA IKKITKDILK 

       790        800        810        820        830        840 
VLNRKGTAET DQLAPIVPLN PGDLTFLGGE DGQKRRRNRP EAFPTAEDIF AKFQHLSHYD 

       850        860        870        880        890        900 
QHQVTAQVSR NVLEQITSFA LGMSYHLPLV QHVQFIFDLM EYSLSISGLI DFAIQLLNEL 

       910        920        930        940        950        960 
SVVEAELLLK SSDLVGSYTT SLCLCIVAVL RHYHACLILN QDQMAQVFEG LCGVVKHGMN 

       970        980        990       1000       1010       1020 
RSDGSSAERC ILAYLYDLYT SCSHLKNKFG ELFSDFCSKV KNTIYCNVEP SESNMRWAPE 

      1030       1040       1050       1060       1070       1080 
FMIDTLENPA AHTFTYTGLG KSLSENPANR YSFVCNALMH VCVGHHDPDR VNDIAILCAE 

      1090       1100       1110       1120       1130       1140 
LTGYCKSLSA EWLGVLKALC CSSNNGTCGF NDLLCNVDVS DLSFHDSLAT FVAILIARQC 

      1150       1160       1170       1180       1190       1200 
LLLEDLIRCA AIPSLLNAAC SEQDSEPGAR LTCRILLHLF KTPQLNPCQS DGNKPTVGIR 

      1210       1220       1230       1240       1250       1260 
SSCDRHLLAA SQNRIVDGAV FAVLKAVFVL GDAELKGSGF TVTGGTEELP EEEGGGGSGG 

      1270       1280       1290       1300       1310       1320 
RRQGGRNISV ETASLDVYAK YVLRSICQQE WVGERCLKSL CEDSNDLQDP VLSSAQAQRL 

      1330       1340       1350       1360       1370       1380 
MQLICYPHRL LDNEDGENPQ RQRIKRILQN LDQWTMRQSS LELQLMIKQT PNNEMNSLLE 

      1390       1400       1410       1420       1430       1440 
NIAKATIEVF QQSAETGSSS GSTASNMPSS SKTKPVLSSL ERSGVWLVAP LIAKLPTSVQ 

      1450       1460       1470       1480       1490       1500 
GHVLKAAGEE LEKGQHLGSS SRKERDRQKQ KSMSLLSQQP FLSLVLTCLK GQDEQREGLL 

      1510       1520       1530       1540       1550       1560 
TSLYSQVHQI VNNWRDDQYL DDCKPKQLMH EALKLRLNLV GGMFDTVQRS TQQTTEWAML 

      1570       1580       1590       1600       1610       1620 
LLEIIISGTV DMQSNNELFT TVLDMLSVLI NGTLAADMSS ISQGSMEENK RAYMNLAKKL 

      1630       1640       1650       1660       1670       1680 
QKELGERQSD SLEKVRQLLP LPKQTRDVIT CEPQGSLIDT KGNKIAGFDS IFKKEGLQVS 

      1690       1700       1710       1720       1730       1740 
TKQKISPWDL FEGLKPSAPL SWGWFGTVRV DRRVARGEEQ QRLLLYHTHL RPRPRAYYLE 

      1750       1760       1770       1780       1790       1800 
PLPLPPEDEE PPAPTLLEPE KKAPEPPKTD KPGAAPPSTE ERKKKSTKGK KRSQPATKTE 

      1810       1820       1830       1840       1850       1860 
DYGMGPGRSG PYGVTVPPDL LHHPNPGSIT HLNYRQGSIG LYTQNQPLPA GGPRVDPYRP 

      1870       1880       1890       1900       1910       1920 
VRLPMQKLPT RPTYPGVLPT TMTGVMGLEP SSYKTSVYRQ QQPAVPQGQR LRQQLQQSQG 

      1930       1940       1950       1960       1970       1980 
MLGQSSVHQM TPSSSYGLQT SQGYTPYVSH VGLQQHTGPA GTMVPPSYSS QPYQSTHPST 

      1990       2000       2010       2020       2030       2040 
NPTLVDPTRH LQQRPSGYVH QQAPTYGHGL TSTQRFSHQT LQQTPMISTM TPMSAQGVQA 

      2050       2060       2070       2080       2090       2100 
GVRSTAILPE QQQQQQQQQQ QQQQQQQQQQ QQQQQQYHIR QQQQQQILRQ QQQQQQQQQQ 

      2110       2120       2130       2140       2150       2160 
QQQQQQQQQQ QQQQQHQQQQ QQQAAPPQPQ PQSQPQFQRQ GLQQTQQQQQ TAALVRQLQQ 

      2170 
QLSNTQPQPS TNIFGRY 

« Hide

Isoform 2 [UniParc].

Checksum: 22DB2ABC4A1CCA6B
Show »

FASTA2,180243,394
Isoform 3 [UniParc].

Checksum: 440A5E60BA3E7273
Show »

FASTA2,176242,953

References

« Hide 'large scale' references
[1]"Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators."
Ito M., Yuan C.-X., Malik S., Gu W., Fondell J.D., Yamamura S., Fu Z.-Y., Zhang X., Qin J., Roeder R.G.
Mol. Cell 3:361-370(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 788-802 (ISOFORMS 1/2/3), IDENTIFICATION IN THE TRAP COMPLEX, TISSUE SPECIFICITY, VARIANT ARG-1392.
Tissue: Cervix carcinoma.
[2]"The DNA sequence of the human X chromosome."
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. expand/collapse author list , 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.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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."
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 54-2177 (ISOFORM 1), VARIANT ARG-1392.
Tissue: Bone marrow.
[4]"Association of an X-chromosome dodecamer insertional variant allele with mental retardation."
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.
Mol. Psychiatry 3:303-309(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 154-2177 (ISOFORM 3).
[5]"The genomic structure and developmental expression patterns of the human OPA-containing gene (HOPA)."
Philibert R.A., Winfield S.L., Damschroder-Williams P., Tengstrom C., Martin B.M., Ginns E.I.
Hum. Genet. 105:174-178(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 154-2177 (ISOFORM 3).
[6]"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 386-418 (ISOFORMS 1/2/3), IDENTIFICATION IN THE ARC COMPLEX.
Tissue: Cervix carcinoma.
[7]"cDNAs with long CAG trinucleotide repeats from human brain."
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.
Hum. Genet. 100:114-122(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1529-2177 (ISOFORM 2).
Tissue: Brain.
[8]"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 1674-1682 AND 1771-1782 (ISOFORMS 1/2/3), IDENTIFICATION IN THE ARC COMPLEX.
[9]"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, INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
[10]"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: INTERACTION WITH MED1; MED18; MED21; MED28; MED29 AND MED30, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
[11]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Mediator is a transducer of Wnt/beta-catenin signaling."
Kim S., Xu X., Hecht A., Boyer T.G.
J. Biol. Chem. 281:14066-14075(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CTNNB1 AND MED30.
[13]"Human Mediator enhances basal transcription by facilitating recruitment of transcription factor IIB during preinitiation complex assembly."
Baek H.J., Kang Y.K., Roeder R.G.
J. Biol. Chem. 281:15172-15181(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MED1 AND MED10.
[14]"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: FUNCTION, INTERACTION WITH CDK8; CTNNB1 AND GLI3.
[15]"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 SER-635 AND SER-1258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635; SER-1258 AND SER-1269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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-635, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"The original Lujan syndrome family has a novel missense mutation (p.N1007S) in the MED12 gene."
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.
J. Med. Genet. 44:472-477(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LUJFRYS SER-1007.
[21]"A recurrent mutation in MED12 leading to R961W causes Opitz-Kaveggia syndrome."
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.
Nat. Genet. 39:451-453(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OKS TRP-961.
[22]"Mutations in MED12 cause X-linked Ohdo syndrome."
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.
Am. J. Hum. Genet. 92:401-406(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OHDOX HIS-1148; PRO-1165 AND ASN-1729.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF117755 mRNA. Translation: AAD22033.1. Different initiation.
AL590764 Genomic DNA. No translation available.
D83783 mRNA. Translation: BAA12112.1.
AF071309 mRNA. Translation: AAC83163.1.
AF132033 Genomic DNA. Translation: AAD44162.1.
U80742 mRNA. Translation: AAB91440.1.
RefSeqNP_005111.2. NM_005120.2.
XP_005262374.1. XM_005262317.1.
UniGeneHs.409226.

3D structure databases

ProteinModelPortalQ93074.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115293. 61 interactions.
DIPDIP-31459N.
IntActQ93074. 26 interactions.
STRING9606.ENSP00000363193.

PTM databases

PhosphoSiteQ93074.

Polymorphism databases

DMDM209572775.

Proteomic databases

PaxDbQ93074.
PRIDEQ93074.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000333646; ENSP00000333125; ENSG00000184634. [Q93074-2]
ENST00000374080; ENSP00000363193; ENSG00000184634. [Q93074-1]
ENST00000374102; ENSP00000363215; ENSG00000184634. [Q93074-3]
GeneID9968.
KEGGhsa:9968.
UCSCuc004dyy.3. human. [Q93074-1]
uc004dyz.3. human. [Q93074-3]

Organism-specific databases

CTD9968.
GeneCardsGC0XP070338.
HGNCHGNC:11957. MED12.
HPAHPA003184.
HPA003185.
MIM300188. gene.
300895. phenotype.
305450. phenotype.
309520. phenotype.
neXtProtNX_Q93074.
Orphanet293707. Blepharophimosis-intellectual deficit syndrome, MKB type.
93932. FG syndrome type 1.
776. X-linked intellectual deficit with marfanoid habitus.
777. X-linked non-syndromic intellectual deficit.
PharmGKBPA36645.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG319131.
HOGENOMHOG000231423.
HOVERGENHBG052447.
InParanoidQ93074.
KOK15162.
OMATVDMQSN.
OrthoDBEOG7CRTNZ.
PhylomeDBQ93074.
TreeFamTF324178.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_71. Gene Expression.
SignaLinkQ93074.

Gene expression databases

ArrayExpressQ93074.
BgeeQ93074.
CleanExHS_MED12.
GenevestigatorQ93074.

Family and domain databases

InterProIPR019035. Mediator_Med12.
IPR021989. Mediator_Med12_catenin-bd.
IPR021990. Mediator_Med12_LCEWAV.
[Graphical view]
PfamPF09497. Med12. 1 hit.
PF12145. Med12-LCEWAV. 1 hit.
PF12144. Med12-PQL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMED12. human.
GeneWikiMED12.
GenomeRNAi9968.
NextBio37618.
PROQ93074.
SOURCESearch...

Entry information

Entry nameMED12_HUMAN
AccessionPrimary (citable) accession number: Q93074
Secondary accession number(s): O15410 expand/collapse secondary AC list , O75557, Q9UHV6, Q9UND7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 14, 2008
Last modified: April 16, 2014
This is version 140 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM