SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9ULK4

- MED23_HUMAN

UniProt

Q9ULK4 - MED23_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Mediator of RNA polymerase II transcription subunit 23
Gene
MED23, ARC130, CRSP3, DRIP130, KIAA1216, SUR2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Required for transcriptional activation subsequent to the assembly of the preinitiation 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 preinitiation 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.3 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. transcription coactivator activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. gene expression Source: Reactome
  2. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  3. regulation of transcription, DNA-templated Source: MGI
  4. transcription initiation from RNA polymerase II promoter Source: Reactome
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: Chromosome 6

Organism-specific databases

HGNCiHGNC:2372. MED23.

Subcellular locationi

Nucleus Inferred

GO - Cellular componenti

  1. mediator complex Source: Ensembl
  2. nucleoplasm Source: Reactome
  3. transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Mental retardation, autosomal recessive 18 (MRT18) [MIM:614249]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 nonsyndromic intellectual disability.
PharmGKBiPA162395499.

PTM / Processingi

Molecule processing

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

Proteomic databases

MaxQBiQ9ULK4.
PaxDbiQ9ULK4.
PRIDEiQ9ULK4.

PTM databases

PhosphoSiteiQ9ULK4.

Expressioni

Gene expression databases

ArrayExpressiQ9ULK4.
BgeeiQ9ULK4.
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, CTNNB1, and GLI3. Interacts with the adenovirus E1A protein.11 Publications

Protein-protein interaction databases

BioGridi114829. 47 interactions.
DIPiDIP-31461N.
IntActiQ9ULK4. 20 interactions.
MINTiMINT-4719443.

Structurei

3D structure databases

ProteinModelPortaliQ9ULK4.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG305557.
HOVERGENiHBG051122.
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. Align

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

METQLQSIFE EVVKTEVIEE AFPGMFMDTP EDEKTKLISC LGAFRQFWGG     50
LSQESHEQCI QWIVKFIHGQ HSPKRISFLY DCLAMAVETG LLPPRLVCES 100
LINSDTLEWE RTQLWALTFK LVRKIIGGVD YKGVRDLLKV ILEKILTIPN 150
TVSSAVVQQL LAAREVIAYI LERNACLLPA YFAVTEIRKL YPEGKLPHWL 200
LGNLVSDFVD TFRPTARINS ICGRCSLLPV VNNSGAICNS WKLDPATLRF 250
PLKGLLPYDK DLFEPQTALL RYVLEQPYSR DMVCNMLGLN KQHKQRCPVL 300
EDQLVDLVVY AMERSETEEK FDDGGTSQLL WQHLSSQLIF FVLFQFASFP 350
HMVLSLHQKL AGRGLIKGRD HLMWVLLQFI SGSIQKNALA DFLPVMKLFD 400
LLYPEKEYIP VPDINKPQST HAFAMTCIWI HLNRKAQNDN SKLQIPIPHS 450
LRLHHEFLQQ SLRNKSLQMN DYKIALLCNA YSTNSECFTL PMGALVETIY 500
GNGIMRIPLP GTNCMASGSI TPLPMNLLDS LTVHAKMSLI HSIATRVIKL 550
AHAKSSVALA PALVETYSRL LVYMEIESLG IKGFISQLLP TVFKSHAWGI 600
LHTLLEMFSY RMHHIQPHYR VQLLSHLHTL AAVAQTNQNQ LHLCVESTAL 650
RLITALGSSE VQPQFTRFLS DPKTVLSAES EELNRALILT LARATHVTDF 700
FTGSDSIQGT WCKDILQTIM SFTPHNWASH TLSCFPGPLQ AFFKQNNVPQ 750
ESRFNLKKNV EEEYRKWKSM SNENDIITHF SMQGSPPLFL CLLWKMLLET 800
DHINQIGYRV LERIGARALV AHVRTFADFL VYEFSTSAGG QQLNKCIEIL 850
NDMVWKYNIV TLDRLILCLA MRSHEGNEAQ VCYFIIQLLL LKPNDFRNRV 900
SDFVKENSPE HWLQNDWHTK HMNYHKKYPE KLYFEGLAEQ VDPPVQIQSP 950
YLPIYFGNVC LRFLPVFDIV IHRFLELLPV SKSLETLLDH LGGLYKFHDR 1000
PVTYLYNTLH YYEMHLRDRA FLKRKLVHAI IGSLKDNRPQ GWCLSDTYLK 1050
CAMNAREENP WVPDDTYYCR LIGRLVDTMA GKSPGPFPNC DWRFNEFPNP 1100
AAHALHVTCV ELMALAVSGK EVGNALLNVV LKSQPLVPRE NITAWMNAIG 1150
LIITALPEPY WIVLHDRIVS VISSPSLTSE TEWVGYPFRL FDFTACHQSY 1200
SEMSCSYTLA LAHAVWHHSS IGQLSLIPKF LTEVLLPIVK TEFQLLYVYH 1250
LVGPFLQRFQ QERTRCMIEI GVAFYDMLLN VDQCSTHLNY MDPICDFLYH 1300
MKYMFTGDSV KEQVEKIICN LKPALKLRLR FITHISKMEP AAVPPQAMNS 1350
GSPAPQSNQV PVSLPVTQ 1368
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 AAD31729.1 differs from that shown. Reason: Frameshift at positions 945 and 950.
The sequence AAD12724.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence BAA86530.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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.
VSP_004034
Alternative sequencei457 – 47519FLQQS…DYKIA → SAFANCFQITCMGDLTHTP in isoform 6.
VSP_047860Add
BLAST
Alternative sequencei476 – 1368893Missing in isoform 6.
VSP_047861Add
BLAST
Alternative sequencei870 – 88011AMRSHEGNEAQ → VRINTFLSLFS in isoform 2.
VSP_004036Add
BLAST
Alternative sequencei881 – 1368488Missing in isoform 2.
VSP_004037Add
BLAST
Alternative sequencei1360 – 13689Missing in isoform 3 and isoform 4.
VSP_004035
Alternative sequencei1361 – 13688PVSLPVTQ → DTLT in isoform 5.
VSP_028380

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591C → W in AAH60759. 1 Publication
Sequence conflicti131 – 1311Y → N in AAD31729. 1 Publication
Sequence conflicti208 – 2081F → V in AAD30202. 1 Publication
Sequence conflicti230 – 2301V → E in AAD30202. 1 Publication
Sequence conflicti464 – 4641N → H in AAD30202. 1 Publication
Sequence conflicti488 – 4881F → V in AAD30202. 1 Publication
Sequence conflicti507 – 5071I → L in AAD30202. 1 Publication
Sequence conflicti518 – 5181G → A in AAD30202. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]

Polymorphism databases

DMDMi28558074.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS5146.1. [Q9ULK4-3 ]
CCDS5147.1. [Q9ULK4-1 ]
CCDS59039.1. [Q9ULK4-5 ]
RefSeqi NP_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 ]
UniGenei Hs.29679.

3D structure databases

ProteinModelPortali Q9ULK4.
ModBasei Search...

Protein-protein interaction databases

BioGridi 114829. 47 interactions.
DIPi DIP-31461N.
IntActi Q9ULK4. 20 interactions.
MINTi MINT-4719443.

Chemistry

BindingDBi Q9ULK4.
ChEMBLi CHEMBL4146.

PTM databases

PhosphoSitei Q9ULK4.

Polymorphism databases

DMDMi 28558074.

Proteomic databases

MaxQBi Q9ULK4.
PaxDbi Q9ULK4.
PRIDEi Q9ULK4.

Protocols and materials databases

DNASUi 9439.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000354577 ; ENSP00000346588 ; ENSG00000112282 . [Q9ULK4-3 ]
ENST00000368053 ; ENSP00000357032 ; ENSG00000112282 . [Q9ULK4-2 ]
ENST00000368060 ; ENSP00000357039 ; ENSG00000112282 . [Q9ULK4-5 ]
ENST00000368068 ; ENSP00000357047 ; ENSG00000112282 . [Q9ULK4-1 ]
ENST00000539158 ; ENSP00000445072 ; ENSG00000112282 . [Q9ULK4-6 ]
GeneIDi 9439.
KEGGi hsa:9439.
UCSCi uc003qcq.4. human. [Q9ULK4-3 ]
uc003qcs.2. human. [Q9ULK4-1 ]
uc003qct.2. human. [Q9ULK4-2 ]
uc031spr.1. human. [Q9ULK4-5 ]

Organism-specific databases

CTDi 9439.
GeneCardsi GC06M131895.
HGNCi HGNC:2372. MED23.
MIMi 605042. gene.
614249. phenotype.
neXtProti NX_Q9ULK4.
Orphaneti 88616. Autosomal recessive nonsyndromic intellectual disability.
PharmGKBi PA162395499.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG305557.
HOVERGENi HBG051122.
KOi K15166.
OrthoDBi EOG7CCBQ5.
PhylomeDBi Q9ULK4.
TreeFami TF324163.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi MED23. human.
GeneWikii CRSP3.
GenomeRNAii 9439.
NextBioi 35344.
PROi Q9ULK4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9ULK4.
Bgeei Q9ULK4.
Genevestigatori Q9ULK4.

Family and domain databases

InterProi IPR021629. Mediator_Med23.
[Graphical view ]
Pfami PF11573. Med23. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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: September 3, 2014
This is version 119 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