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Protein

Mediator of RNA polymerase II transcription subunit 23

Gene

MED23

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

Functioni

Required for transcriptional activation subsequent to the assembly of the pre-initiation complex (By similarity). 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 pre-initiation complex with RNA polymerase II and the general transcription factors. Required for transcriptional activation by adenovirus E1A protein. Required for ELK1-dependent transcriptional activation in response to activated Ras signaling.By similarity3 Publications

GO - Molecular functioni

  • transcription coactivator activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Mediator of RNA polymerase II transcription subunit 23
Alternative name(s):
Activator-recruited cofactor 130 kDa component
Short name:
ARC130
Cofactor required for Sp1 transcriptional activation subunit 3
Short name:
CRSP complex subunit 3
Mediator complex subunit 23
Protein sur-2 homolog
Short name:
hSur-2
Transcriptional coactivator CRSP130
Vitamin D3 receptor-interacting protein complex 130 kDa component
Short name:
DRIP130
Gene namesi
Name:MED23
Synonyms:ARC130, CRSP3, DRIP130, KIAA1216, SUR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:2372. MED23.

Subcellular locationi

GO - Cellular componenti

  • mediator complex Source: Ensembl
  • nucleoplasm Source: Reactome
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Mental retardation, autosomal recessive 18 (MRT18)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.

See also OMIM:614249
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti617 – 6171P → Q in MRT18; specifically impairs the response of JUN and FOS immediate early genes to serum mitogens by altering the interaction between enhancer-bound transcription factors (TCF7L2 and ELK1 respectively) and Mediator complex. 1 Publication
VAR_066596

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi614249. phenotype.
Orphaneti88616. Autosomal recessive non-syndromic intellectual disability.
PharmGKBiPA162395499.

Polymorphism and mutation databases

BioMutaiMED23.
DMDMi28558074.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13681368Mediator of RNA polymerase II transcription subunit 23PRO_0000079358Add
BLAST

Proteomic databases

MaxQBiQ9ULK4.
PaxDbiQ9ULK4.
PRIDEiQ9ULK4.

PTM databases

PhosphoSiteiQ9ULK4.

Expressioni

Gene expression databases

BgeeiQ9ULK4.
ExpressionAtlasiQ9ULK4. baseline and differential.
GenevestigatoriQ9ULK4.

Interactioni

Subunit structurei

Interacts with ELK1 (By similarity). 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 CEBPB (when not methylated), CTNNB1, and GLI3. Interacts with the adenovirus E1A protein.By similarity12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MED14O602442EBI-311161,EBI-394489
MED16Q9Y2X02EBI-311161,EBI-394541

Protein-protein interaction databases

BioGridi114829. 52 interactions.
DIPiDIP-31461N.
IntActiQ9ULK4. 23 interactions.
MINTiMINT-4719443.

Structurei

3D structure databases

ProteinModelPortaliQ9ULK4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Mediator complex subunit 23 family.Curated

Phylogenomic databases

eggNOGiNOG305557.
GeneTreeiENSGT00390000010380.
HOGENOMiHOG000043810.
HOVERGENiHBG051122.
InParanoidiQ9ULK4.
KOiK15166.
OrthoDBiEOG7CCBQ5.
PhylomeDBiQ9ULK4.
TreeFamiTF324163.

Family and domain databases

InterProiIPR021629. Mediator_Med23.
[Graphical view]
PfamiPF11573. Med23. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q9ULK4-1) [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
METQLQSIFE EVVKTEVIEE AFPGMFMDTP EDEKTKLISC LGAFRQFWGG
60 70 80 90 100
LSQESHEQCI QWIVKFIHGQ HSPKRISFLY DCLAMAVETG LLPPRLVCES
110 120 130 140 150
LINSDTLEWE RTQLWALTFK LVRKIIGGVD YKGVRDLLKV ILEKILTIPN
160 170 180 190 200
TVSSAVVQQL LAAREVIAYI LERNACLLPA YFAVTEIRKL YPEGKLPHWL
210 220 230 240 250
LGNLVSDFVD TFRPTARINS ICGRCSLLPV VNNSGAICNS WKLDPATLRF
260 270 280 290 300
PLKGLLPYDK DLFEPQTALL RYVLEQPYSR DMVCNMLGLN KQHKQRCPVL
310 320 330 340 350
EDQLVDLVVY AMERSETEEK FDDGGTSQLL WQHLSSQLIF FVLFQFASFP
360 370 380 390 400
HMVLSLHQKL AGRGLIKGRD HLMWVLLQFI SGSIQKNALA DFLPVMKLFD
410 420 430 440 450
LLYPEKEYIP VPDINKPQST HAFAMTCIWI HLNRKAQNDN SKLQIPIPHS
460 470 480 490 500
LRLHHEFLQQ SLRNKSLQMN DYKIALLCNA YSTNSECFTL PMGALVETIY
510 520 530 540 550
GNGIMRIPLP GTNCMASGSI TPLPMNLLDS LTVHAKMSLI HSIATRVIKL
560 570 580 590 600
AHAKSSVALA PALVETYSRL LVYMEIESLG IKGFISQLLP TVFKSHAWGI
610 620 630 640 650
LHTLLEMFSY RMHHIQPHYR VQLLSHLHTL AAVAQTNQNQ LHLCVESTAL
660 670 680 690 700
RLITALGSSE VQPQFTRFLS DPKTVLSAES EELNRALILT LARATHVTDF
710 720 730 740 750
FTGSDSIQGT WCKDILQTIM SFTPHNWASH TLSCFPGPLQ AFFKQNNVPQ
760 770 780 790 800
ESRFNLKKNV EEEYRKWKSM SNENDIITHF SMQGSPPLFL CLLWKMLLET
810 820 830 840 850
DHINQIGYRV LERIGARALV AHVRTFADFL VYEFSTSAGG QQLNKCIEIL
860 870 880 890 900
NDMVWKYNIV TLDRLILCLA MRSHEGNEAQ VCYFIIQLLL LKPNDFRNRV
910 920 930 940 950
SDFVKENSPE HWLQNDWHTK HMNYHKKYPE KLYFEGLAEQ VDPPVQIQSP
960 970 980 990 1000
YLPIYFGNVC LRFLPVFDIV IHRFLELLPV SKSLETLLDH LGGLYKFHDR
1010 1020 1030 1040 1050
PVTYLYNTLH YYEMHLRDRA FLKRKLVHAI IGSLKDNRPQ GWCLSDTYLK
1060 1070 1080 1090 1100
CAMNAREENP WVPDDTYYCR LIGRLVDTMA GKSPGPFPNC DWRFNEFPNP
1110 1120 1130 1140 1150
AAHALHVTCV ELMALAVSGK EVGNALLNVV LKSQPLVPRE NITAWMNAIG
1160 1170 1180 1190 1200
LIITALPEPY WIVLHDRIVS VISSPSLTSE TEWVGYPFRL FDFTACHQSY
1210 1220 1230 1240 1250
SEMSCSYTLA LAHAVWHHSS IGQLSLIPKF LTEVLLPIVK TEFQLLYVYH
1260 1270 1280 1290 1300
LVGPFLQRFQ QERTRCMIEI GVAFYDMLLN VDQCSTHLNY MDPICDFLYH
1310 1320 1330 1340 1350
MKYMFTGDSV KEQVEKIICN LKPALKLRLR FITHISKMEP AAVPPQAMNS
1360
GSPAPQSNQV PVSLPVTQ
Length:1,368
Mass (Da):156,474
Last modified:February 22, 2003 - v2
Checksum:i2BEE9FF5E328477D
GO
Isoform 2 (identifier: Q9ULK4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     292-292: Q → QTLNIAQ
     870-880: AMRSHEGNEAQ → VRINTFLSLFS
     881-1368: Missing.

Show »
Length:886
Mass (Da):100,834
Checksum:iF1461C27AF9D7817
GO
Isoform 3 (identifier: Q9ULK4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     292-292: Q → QTLNIAQ
     1360-1368: Missing.

Show »
Length:1,365
Mass (Da):156,194
Checksum:i8F401B9FF90878C3
GO
Isoform 4 (identifier: Q9ULK4-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1360-1368: Missing.

Show »
Length:1,359
Mass (Da):155,553
Checksum:iE6EB563FEBC111DE
GO
Isoform 5 (identifier: Q9ULK4-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1361-1368: PVSLPVTQ → DTLT

Show »
Length:1,364
Mass (Da):156,082
Checksum:i55BAD400A566EB56
GO
Isoform 6 (identifier: Q9ULK4-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     457-475: FLQQSLRNKSLQMNDYKIA → SAFANCFQITCMGDLTHTP
     476-1368: Missing.

Show »
Length:475
Mass (Da):54,314
Checksum:i3621AC3036B0F0B5
GO

Sequence cautioni

The sequence AAD12724.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAD31729.1 differs from that shown. Reason: Frameshift at positions 945 and 950. Curated
The sequence BAA86530.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591C → W in AAH60759 (PubMed:15489334).Curated
Sequence conflicti131 – 1311Y → N in AAD31729 (PubMed:10235266).Curated
Sequence conflicti208 – 2081F → V in AAD30202 (PubMed:10353252).Curated
Sequence conflicti230 – 2301V → E in AAD30202 (PubMed:10353252).Curated
Sequence conflicti464 – 4641N → H in AAD30202 (PubMed:10353252).Curated
Sequence conflicti488 – 4881F → V in AAD30202 (PubMed:10353252).Curated
Sequence conflicti507 – 5071I → L in AAD30202 (PubMed:10353252).Curated
Sequence conflicti518 – 5181G → A in AAD30202 (PubMed:10353252).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti617 – 6171P → Q in MRT18; specifically impairs the response of JUN and FOS immediate early genes to serum mitogens by altering the interaction between enhancer-bound transcription factors (TCF7L2 and ELK1 respectively) and Mediator complex. 1 Publication
VAR_066596

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei292 – 2921Q → QTLNIAQ in isoform 2 and isoform 3. 2 PublicationsVSP_004034
Alternative sequencei457 – 47519FLQQS…DYKIA → SAFANCFQITCMGDLTHTP in isoform 6. 1 PublicationVSP_047860Add
BLAST
Alternative sequencei476 – 1368893Missing in isoform 6. 1 PublicationVSP_047861Add
BLAST
Alternative sequencei870 – 88011AMRSHEGNEAQ → VRINTFLSLFS in isoform 2. 1 PublicationVSP_004036Add
BLAST
Alternative sequencei881 – 1368488Missing in isoform 2. 1 PublicationVSP_004037Add
BLAST
Alternative sequencei1360 – 13689Missing in isoform 3 and isoform 4. 2 PublicationsVSP_004035
Alternative sequencei1361 – 13688PVSLPVTQ → DTLT in isoform 5. 1 PublicationVSP_028380

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF105332 mRNA. Translation: AAD31729.1. Frameshift.
AF135022 mRNA. Translation: AAD30202.1.
AF104255 mRNA. Translation: AAD12724.1. Different initiation.
EU392526 mRNA. Translation: ACB88854.1.
AB033042 mRNA. Translation: BAA86530.1. Different initiation.
AL136776 mRNA. Translation: CAB66710.1.
AL121575 Genomic DNA. Translation: CAB92072.1.
AL121575 Genomic DNA. Translation: CAB92073.1.
AL121575 Genomic DNA. Translation: CAI23319.1.
AL121575 Genomic DNA. Translation: CAI23320.1.
CH471051 Genomic DNA. Translation: EAW48052.1.
BC060759 mRNA. Translation: AAH60759.1.
CCDSiCCDS5146.1. [Q9ULK4-3]
CCDS5147.1. [Q9ULK4-1]
CCDS59039.1. [Q9ULK4-5]
RefSeqiNP_001257450.1. NM_001270521.1. [Q9ULK4-4]
NP_001257451.1. NM_001270522.1. [Q9ULK4-5]
NP_004821.2. NM_004830.3. [Q9ULK4-1]
NP_057063.2. NM_015979.3. [Q9ULK4-3]
UniGeneiHs.29679.

Genome annotation databases

EnsembliENST00000354577; ENSP00000346588; ENSG00000112282. [Q9ULK4-3]
ENST00000368053; ENSP00000357032; ENSG00000112282. [Q9ULK4-2]
ENST00000368060; ENSP00000357039; ENSG00000112282. [Q9ULK4-5]
ENST00000368068; ENSP00000357047; ENSG00000112282. [Q9ULK4-1]
ENST00000539158; ENSP00000445072; ENSG00000112282. [Q9ULK4-6]
GeneIDi9439.
KEGGihsa:9439.
UCSCiuc003qcq.4. human. [Q9ULK4-3]
uc003qcs.2. human. [Q9ULK4-1]
uc003qct.2. human. [Q9ULK4-2]
uc031spr.1. human. [Q9ULK4-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF105332 mRNA. Translation: AAD31729.1. Frameshift.
AF135022 mRNA. Translation: AAD30202.1.
AF104255 mRNA. Translation: AAD12724.1. Different initiation.
EU392526 mRNA. Translation: ACB88854.1.
AB033042 mRNA. Translation: BAA86530.1. Different initiation.
AL136776 mRNA. Translation: CAB66710.1.
AL121575 Genomic DNA. Translation: CAB92072.1.
AL121575 Genomic DNA. Translation: CAB92073.1.
AL121575 Genomic DNA. Translation: CAI23319.1.
AL121575 Genomic DNA. Translation: CAI23320.1.
CH471051 Genomic DNA. Translation: EAW48052.1.
BC060759 mRNA. Translation: AAH60759.1.
CCDSiCCDS5146.1. [Q9ULK4-3]
CCDS5147.1. [Q9ULK4-1]
CCDS59039.1. [Q9ULK4-5]
RefSeqiNP_001257450.1. NM_001270521.1. [Q9ULK4-4]
NP_001257451.1. NM_001270522.1. [Q9ULK4-5]
NP_004821.2. NM_004830.3. [Q9ULK4-1]
NP_057063.2. NM_015979.3. [Q9ULK4-3]
UniGeneiHs.29679.

3D structure databases

ProteinModelPortaliQ9ULK4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114829. 52 interactions.
DIPiDIP-31461N.
IntActiQ9ULK4. 23 interactions.
MINTiMINT-4719443.

Chemistry

BindingDBiQ9ULK4.
ChEMBLiCHEMBL2111426.

PTM databases

PhosphoSiteiQ9ULK4.

Polymorphism and mutation databases

BioMutaiMED23.
DMDMi28558074.

Proteomic databases

MaxQBiQ9ULK4.
PaxDbiQ9ULK4.
PRIDEiQ9ULK4.

Protocols and materials databases

DNASUi9439.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354577; ENSP00000346588; ENSG00000112282. [Q9ULK4-3]
ENST00000368053; ENSP00000357032; ENSG00000112282. [Q9ULK4-2]
ENST00000368060; ENSP00000357039; ENSG00000112282. [Q9ULK4-5]
ENST00000368068; ENSP00000357047; ENSG00000112282. [Q9ULK4-1]
ENST00000539158; ENSP00000445072; ENSG00000112282. [Q9ULK4-6]
GeneIDi9439.
KEGGihsa:9439.
UCSCiuc003qcq.4. human. [Q9ULK4-3]
uc003qcs.2. human. [Q9ULK4-1]
uc003qct.2. human. [Q9ULK4-2]
uc031spr.1. human. [Q9ULK4-5]

Organism-specific databases

CTDi9439.
GeneCardsiGC06M131895.
HGNCiHGNC:2372. MED23.
MIMi605042. gene.
614249. phenotype.
neXtProtiNX_Q9ULK4.
Orphaneti88616. Autosomal recessive non-syndromic intellectual disability.
PharmGKBiPA162395499.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG305557.
GeneTreeiENSGT00390000010380.
HOGENOMiHOG000043810.
HOVERGENiHBG051122.
InParanoidiQ9ULK4.
KOiK15166.
OrthoDBiEOG7CCBQ5.
PhylomeDBiQ9ULK4.
TreeFamiTF324163.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiMED23. human.
GeneWikiiCRSP3.
GenomeRNAii9439.
NextBioi35344.
PROiQ9ULK4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ULK4.
ExpressionAtlasiQ9ULK4. baseline and differential.
GenevestigatoriQ9ULK4.

Family and domain databases

InterProiIPR021629. Mediator_Med23.
[Graphical view]
PfamiPF11573. Med23. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 254-280; 1317-1326 AND 1331-1337, IDENTIFICATION IN ARC COMPLEX.
    Tissue: Cervix carcinoma.
  2. "Mammalian Srb/Mediator complex is targeted by adenovirus E1A protein."
    Boyer T.G., Martin M.E.D., Lees E., Ricciardi R.P., Berk A.J.
    Nature 399:276-279(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INTERACTION WITH E1A AND CDK8.
  3. "The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Sp1."
    Ryu S., Zhou S., Ladurner A.G., Tjian R.
    Nature 397:446-450(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), IDENTIFICATION IN THE CRSP COMPLEX.
  4. "Alternative splicing as a prevalent mechanism in regulating mammalian mediator tail subcomplex activity."
    Kivil A., Kazantseva A., Vinkel K.J.M., Sadam H., Neuman T., Palm K.
    Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
  5. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
    DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Testis.
  7. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Placenta.
  10. "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: IDENTIFICATION IN THE ARC COMPLEX, PROTEIN SEQUENCE OF 465-473 AND 1302-1311.
  11. "TFIIH is negatively regulated by cdk8-containing mediator complexes."
    Akoulitchev S., Chuikov S., Reinberg D.
    Nature 407:102-106(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MED6.
  12. "The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro."
    Kang Y.K., Guermah M., Yuan C.-X., Roeder R.G.
    Proc. Natl. Acad. Sci. U.S.A. 99:2642-2647(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX.
  13. "Ras induces mediator complex exchange on C/EBP beta."
    Mo X., Kowenz-Leutz E., Xu H., Leutz A.
    Mol. Cell 13:241-250(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CEBPB.
  14. "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.
  15. "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 AND MED10, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
  16. "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: INTERACTION WITH CDK8; CTNNB1 AND GLI3.
  17. "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.
  18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Crosstalk between C/EBPbeta phosphorylation, arginine methylation, and SWI/SNF/Mediator implies an indexing transcription factor code."
    Kowenz-Leutz E., Pless O., Dittmar G., Knoblich M., Leutz A.
    EMBO J. 29:1105-1115(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CEBPB.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "MED23 mutation links intellectual disability to dysregulation of immediate early gene expression."
    Hashimoto S., Boissel S., Zarhrate M., Rio M., Munnich A., Egly J.M., Colleaux L.
    Science 333:1161-1163(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MRT18 GLN-617, CHARACTERIZATION OF VARIANT MRT18 GLN-617.

Entry informationi

Entry nameiMED23_HUMAN
AccessioniPrimary (citable) accession number: Q9ULK4
Secondary accession number(s): B9TX55
, O95403, Q5JWT3, Q5JWT4, Q6P9H6, Q9H0J2, Q9NTT9, Q9NTU0, Q9Y5P7, Q9Y667
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2003
Last sequence update: February 22, 2003
Last modified: May 27, 2015
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.