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Q93074

- MED12_HUMAN

UniProt

Q93074 - MED12_HUMAN

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Protein

Mediator of RNA polymerase II transcription subunit 12

Gene

MED12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. This subunit may specifically regulate transcription of targets of the Wnt signaling pathway and SHH signaling pathway.3 Publications

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  3. protein C-terminus binding Source: UniProtKB
  4. protein domain specific binding Source: UniProtKB
  5. receptor activity Source: UniProtKB
  6. RNA polymerase II distal enhancer sequence-specific DNA binding Source: Ensembl
  7. RNA polymerase II transcription cofactor activity Source: UniProtKB
  8. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  9. thyroid hormone receptor binding Source: UniProtKB
  10. transcription coactivator activity Source: MGI
  11. transcription cofactor activity Source: UniProtKB
  12. vitamin D receptor binding Source: UniProtKB

GO - Biological processi

  1. androgen receptor signaling pathway Source: UniProtKB
  2. axis elongation involved in somitogenesis Source: Ensembl
  3. canonical Wnt signaling pathway Source: Ensembl
  4. gene expression Source: Reactome
  5. heart development Source: Ensembl
  6. intracellular steroid hormone receptor signaling pathway Source: UniProtKB
  7. negative regulation of Wnt signaling pathway Source: UniProtKB
  8. neural tube closure Source: Ensembl
  9. oligodendrocyte development Source: Ensembl
  10. positive regulation of transcription, DNA-templated Source: UniProtKB
  11. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  12. Schwann cell development Source: Ensembl
  13. stem cell maintenance Source: Ensembl
  14. transcription initiation from RNA polymerase II promoter Source: UniProtKB
  15. Wnt signaling pathway, planar cell polarity pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

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.
SignaLinkiQ93074.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:MED12
Synonyms:ARC240, CAGH45, HOPA, KIAA0192, TNRC11, TRAP230
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:11957. MED12.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. mediator complex Source: UniProtKB
  2. membrane Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Opitz-Kaveggia syndrome (OKS) [MIM:305450]: X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti961 – 9611R → W in OKS. 1 Publication
VAR_033112
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1007 – 10071N → S in LUJFRYS. 1 Publication
VAR_037534
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1148 – 11481R → H in OHDOX. 1 Publication
VAR_069770
Natural varianti1165 – 11651S → P in OHDOX. 1 Publication
VAR_069771
Natural varianti1729 – 17291H → N in OHDOX. 1 Publication
VAR_069772

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi300895. phenotype.
305450. phenotype.
309520. phenotype.
Orphaneti293707. Blepharophimosis-intellectual disability syndrome, MKB type.
93932. FG syndrome type 1.
776. X-linked intellectual disability with marfanoid habitus.
777. X-linked non-syndromic intellectual disability.
PharmGKBiPA36645.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21772177Mediator of RNA polymerase II transcription subunit 12PRO_0000096359Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei80 – 801N6-acetyllysineBy similarity
Modified residuei166 – 1661Phosphotyrosine1 Publication
Modified residuei635 – 6351Phosphoserine4 Publications
Modified residuei1258 – 12581Phosphoserine2 Publications
Modified residuei1269 – 12691Phosphoserine1 Publication
Modified residuei1798 – 17981N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ93074.
PaxDbiQ93074.
PRIDEiQ93074.

PTM databases

PhosphoSiteiQ93074.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ93074.
CleanExiHS_MED12.
ExpressionAtlasiQ93074. baseline and differential.
GenevestigatoriQ93074.

Organism-specific databases

HPAiHPA003184.
HPA003185.

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. Also interacts with CTNNB1 and GLI3.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APLP1P516932EBI-394357,EBI-74648
APLP2Q064812EBI-394357,EBI-79306
APPP050672EBI-394357,EBI-77613
MED4Q9NPJ65EBI-394357,EBI-394607
TGFBR2P371733EBI-394357,EBI-296151

Protein-protein interaction databases

BioGridi115293. 64 interactions.
DIPiDIP-31459N.
IntActiQ93074. 27 interactions.
STRINGi9606.ENSP00000363193.

Structurei

3D structure databases

ProteinModelPortaliQ93074.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1616 – 2051436Interaction with CTNNB1 and GLI3Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1732 – 177746Pro-richAdd
BLAST
Compositional biasi1900 – 2168269Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the Mediator complex subunit 12 family.Curated

Phylogenomic databases

eggNOGiNOG319131.
GeneTreeiENSGT00440000037505.
HOGENOMiHOG000231423.
HOVERGENiHBG052447.
InParanoidiQ93074.
KOiK15162.
OMAiTVDMQSN.
OrthoDBiEOG7CRTNZ.
PhylomeDBiQ93074.
TreeFamiTF324178.

Family and domain databases

InterProiIPR019035. Mediator_Med12.
IPR021989. Mediator_Med12_catenin-bd.
IPR021990. Mediator_Med12_LCEWAV.
[Graphical view]
PfamiPF09497. Med12. 1 hit.
PF12145. Med12-LCEWAV. 1 hit.
PF12144. Med12-PQL. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q93074-1) [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

        10         20         30         40         50
MAAFGILSYE HRPLKRPRLG PPDVYPQDPK QKEDELTALN VKQGFNNQPA
60 70 80 90 100
VSGDEHGSAK NVSFNPAKIS SNFSSIIAEK LRCNTLPDTG RRKPQVNQKD
110 120 130 140 150
NFWLVTARSQ SAINTWFTDL AGTKPLTQLA KKVPIFSKKE EVFGYLAKYT
160 170 180 190 200
VPVMRAAWLI KMTCAYYAAI SETKVKKRHV DPFMEWTQII TKYLWEQLQK
210 220 230 240 250
MAEYYRPGPA GSGGCGSTIG PLPHDVEVAI RQWDYTEKLA MFMFQDGMLD
260 270 280 290 300
RHEFLTWVLE CFEKIRPGED ELLKLLLPLL LRYSGEFVQS AYLSRRLAYF
310 320 330 340 350
CTRRLALQLD GVSSHSSHVI SAQSTSTLPT TPAPQPPTSS TPSTPFSDLL
360 370 380 390 400
MCPQHRPLVF GLSCILQTIL LCCPSALVWH YSLTDSRIKT GSPLDHLPIA
410 420 430 440 450
PSNLPMPEGN SAFTQQVRAK LREIEQQIKE RGQAVEVRWS FDKCQEATAG
460 470 480 490 500
FTIGRVLHTL EVLDSHSFER SDFSNSLDSL CNRIFGLGPS KDGHEISSDD
510 520 530 540 550
DAVVSLLCEW AVSCKRSGRH RAMVVAKLLE KRQAEIEAER CGESEAADEK
560 570 580 590 600
GSIASGSLSA PSAPIFQDVL LQFLDTQAPM LTDPRSESER VEFFNLVLLF
610 620 630 640 650
CELIRHDVFS HNMYTCTLIS RGDLAFGAPG PRPPSPFDDP ADDPEHKEAE
660 670 680 690 700
GSSSSKLEDP GLSESMDIDP SSSVLFEDME KPDFSLFSPT MPCEGKGSPS
710 720 730 740 750
PEKPDVEKEV KPPPKEKIEG TLGVLYDQPR HVQYATHFPI PQEESCSHEC
760 770 780 790 800
NQRLVVLFGV GKQRDDARHA IKKITKDILK VLNRKGTAET DQLAPIVPLN
810 820 830 840 850
PGDLTFLGGE DGQKRRRNRP EAFPTAEDIF AKFQHLSHYD QHQVTAQVSR
860 870 880 890 900
NVLEQITSFA LGMSYHLPLV QHVQFIFDLM EYSLSISGLI DFAIQLLNEL
910 920 930 940 950
SVVEAELLLK SSDLVGSYTT SLCLCIVAVL RHYHACLILN QDQMAQVFEG
960 970 980 990 1000
LCGVVKHGMN RSDGSSAERC ILAYLYDLYT SCSHLKNKFG ELFSDFCSKV
1010 1020 1030 1040 1050
KNTIYCNVEP SESNMRWAPE FMIDTLENPA AHTFTYTGLG KSLSENPANR
1060 1070 1080 1090 1100
YSFVCNALMH VCVGHHDPDR VNDIAILCAE LTGYCKSLSA EWLGVLKALC
1110 1120 1130 1140 1150
CSSNNGTCGF NDLLCNVDVS DLSFHDSLAT FVAILIARQC LLLEDLIRCA
1160 1170 1180 1190 1200
AIPSLLNAAC SEQDSEPGAR LTCRILLHLF KTPQLNPCQS DGNKPTVGIR
1210 1220 1230 1240 1250
SSCDRHLLAA SQNRIVDGAV FAVLKAVFVL GDAELKGSGF TVTGGTEELP
1260 1270 1280 1290 1300
EEEGGGGSGG RRQGGRNISV ETASLDVYAK YVLRSICQQE WVGERCLKSL
1310 1320 1330 1340 1350
CEDSNDLQDP VLSSAQAQRL MQLICYPHRL LDNEDGENPQ RQRIKRILQN
1360 1370 1380 1390 1400
LDQWTMRQSS LELQLMIKQT PNNEMNSLLE NIAKATIEVF QQSAETGSSS
1410 1420 1430 1440 1450
GSTASNMPSS SKTKPVLSSL ERSGVWLVAP LIAKLPTSVQ GHVLKAAGEE
1460 1470 1480 1490 1500
LEKGQHLGSS SRKERDRQKQ KSMSLLSQQP FLSLVLTCLK GQDEQREGLL
1510 1520 1530 1540 1550
TSLYSQVHQI VNNWRDDQYL DDCKPKQLMH EALKLRLNLV GGMFDTVQRS
1560 1570 1580 1590 1600
TQQTTEWAML LLEIIISGTV DMQSNNELFT TVLDMLSVLI NGTLAADMSS
1610 1620 1630 1640 1650
ISQGSMEENK RAYMNLAKKL QKELGERQSD SLEKVRQLLP LPKQTRDVIT
1660 1670 1680 1690 1700
CEPQGSLIDT KGNKIAGFDS IFKKEGLQVS TKQKISPWDL FEGLKPSAPL
1710 1720 1730 1740 1750
SWGWFGTVRV DRRVARGEEQ QRLLLYHTHL RPRPRAYYLE PLPLPPEDEE
1760 1770 1780 1790 1800
PPAPTLLEPE KKAPEPPKTD KPGAAPPSTE ERKKKSTKGK KRSQPATKTE
1810 1820 1830 1840 1850
DYGMGPGRSG PYGVTVPPDL LHHPNPGSIT HLNYRQGSIG LYTQNQPLPA
1860 1870 1880 1890 1900
GGPRVDPYRP VRLPMQKLPT RPTYPGVLPT TMTGVMGLEP SSYKTSVYRQ
1910 1920 1930 1940 1950
QQPAVPQGQR LRQQLQQSQG MLGQSSVHQM TPSSSYGLQT SQGYTPYVSH
1960 1970 1980 1990 2000
VGLQQHTGPA GTMVPPSYSS QPYQSTHPST NPTLVDPTRH LQQRPSGYVH
2010 2020 2030 2040 2050
QQAPTYGHGL TSTQRFSHQT LQQTPMISTM TPMSAQGVQA GVRSTAILPE
2060 2070 2080 2090 2100
QQQQQQQQQQ QQQQQQQQQQ QQQQQQYHIR QQQQQQILRQ QQQQQQQQQQ
2110 2120 2130 2140 2150
QQQQQQQQQQ QQQQQHQQQQ QQQAAPPQPQ PQSQPQFQRQ GLQQTQQQQQ
2160 2170
TAALVRQLQQ QLSNTQPQPS TNIFGRY
Length:2,177
Mass (Da):243,081
Last modified:October 14, 2008 - v4
Checksum:i7492B07BA0F6EA9D
GO
Isoform 2 (identifier: Q93074-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1916-1916: Q → QAKI

Show »
Length:2,180
Mass (Da):243,394
Checksum:i22DB2ABC4A1CCA6B
GO
Isoform 3 (identifier: Q93074-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1916-1916: Missing.

Note: No experimental confirmation available.

Show »
Length:2,176
Mass (Da):242,953
Checksum:i440A5E60BA3E7273
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161R → RPR in AAD22033. (PubMed:10198638)Curated
Sequence conflicti397 – 3971Missing AA sequence (PubMed:10235266)Curated
Sequence conflicti1166 – 11661E → V in AAD44162. (PubMed:10480376)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti961 – 9611R → W in OKS. 1 Publication
VAR_033112
Natural varianti1007 – 10071N → S in LUJFRYS. 1 Publication
VAR_037534
Natural varianti1148 – 11481R → H in OHDOX. 1 Publication
VAR_069770
Natural varianti1165 – 11651S → P in OHDOX. 1 Publication
VAR_069771
Natural varianti1392 – 13921Q → R.2 Publications
Corresponds to variant rs1139013 [ dbSNP | Ensembl ].
VAR_046672
Natural varianti1729 – 17291H → N in OHDOX. 1 Publication
VAR_069772

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1916 – 19161Q → QAKI in isoform 2. 1 PublicationVSP_035520
Alternative sequencei1916 – 19161Missing in isoform 3. 2 PublicationsVSP_035521

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS43970.1. [Q93074-1]
RefSeqiNP_005111.2. NM_005120.2. [Q93074-1]
XP_005262374.1. XM_005262317.1. [Q93074-2]
UniGeneiHs.409226.

Genome annotation databases

EnsembliENST00000374080; ENSP00000363193; ENSG00000184634. [Q93074-1]
ENST00000374102; ENSP00000363215; ENSG00000184634. [Q93074-3]
GeneIDi9968.
KEGGihsa:9968.
UCSCiuc004dyy.3. human. [Q93074-1]
uc004dyz.3. human. [Q93074-3]

Polymorphism databases

DMDMi209572775.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS43970.1. [Q93074-1 ]
RefSeqi NP_005111.2. NM_005120.2. [Q93074-1 ]
XP_005262374.1. XM_005262317.1. [Q93074-2 ]
UniGenei Hs.409226.

3D structure databases

ProteinModelPortali Q93074.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115293. 64 interactions.
DIPi DIP-31459N.
IntActi Q93074. 27 interactions.
STRINGi 9606.ENSP00000363193.

PTM databases

PhosphoSitei Q93074.

Polymorphism databases

DMDMi 209572775.

Proteomic databases

MaxQBi Q93074.
PaxDbi Q93074.
PRIDEi Q93074.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374080 ; ENSP00000363193 ; ENSG00000184634 . [Q93074-1 ]
ENST00000374102 ; ENSP00000363215 ; ENSG00000184634 . [Q93074-3 ]
GeneIDi 9968.
KEGGi hsa:9968.
UCSCi uc004dyy.3. human. [Q93074-1 ]
uc004dyz.3. human. [Q93074-3 ]

Organism-specific databases

CTDi 9968.
GeneCardsi GC0XP070338.
GeneReviewsi MED12.
HGNCi HGNC:11957. MED12.
HPAi HPA003184.
HPA003185.
MIMi 300188. gene.
300895. phenotype.
305450. phenotype.
309520. phenotype.
neXtProti NX_Q93074.
Orphaneti 293707. Blepharophimosis-intellectual disability syndrome, MKB type.
93932. FG syndrome type 1.
776. X-linked intellectual disability with marfanoid habitus.
777. X-linked non-syndromic intellectual disability.
PharmGKBi PA36645.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG319131.
GeneTreei ENSGT00440000037505.
HOGENOMi HOG000231423.
HOVERGENi HBG052447.
InParanoidi Q93074.
KOi K15162.
OMAi TVDMQSN.
OrthoDBi EOG7CRTNZ.
PhylomeDBi Q93074.
TreeFami TF324178.

Enzyme and pathway databases

Reactomei REACT_116145. PPARA activates gene expression.
REACT_12627. Generic Transcription Pathway.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinki Q93074.

Miscellaneous databases

ChiTaRSi MED12. human.
GeneWikii MED12.
GenomeRNAii 9968.
NextBioi 37618.
PROi Q93074.
SOURCEi Search...

Gene expression databases

Bgeei Q93074.
CleanExi HS_MED12.
ExpressionAtlasi Q93074. baseline and differential.
Genevestigatori Q93074.

Family and domain databases

InterProi IPR019035. Mediator_Med12.
IPR021989. Mediator_Med12_catenin-bd.
IPR021990. Mediator_Med12_LCEWAV.
[Graphical view ]
Pfami PF09497. Med12. 1 hit.
PF12145. Med12-LCEWAV. 1 hit.
PF12144. Med12-PQL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: VARIANT LUJFRYS SER-1007.
  21. Cited for: VARIANT OKS TRP-961.
  22. Cited for: VARIANTS OHDOX HIS-1148; PRO-1165 AND ASN-1729.

Entry informationi

Entry nameiMED12_HUMAN
AccessioniPrimary (citable) accession number: Q93074
Secondary accession number(s): O15410
, O75557, Q9UHV6, Q9UND7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 14, 2008
Last modified: October 29, 2014
This is version 146 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3