MED29_HUMAN
ID MED29_HUMAN Reviewed; 200 AA.
AC Q9NX70; B4DNQ6; M0R2E4; Q5XX09; Q9NTF4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 29;
DE AltName: Full=Intersex-like protein;
DE AltName: Full=Mediator complex subunit 29;
GN Name=MED29; Synonyms=IXL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Embryonic heart;
RX PubMed=15555573; DOI=10.1016/j.bbrc.2004.10.159;
RA Wang Y., Li Y., Zeng W., Zhu C., Xiao J., Yuan W., Wang Y., Cai Z.,
RA Zhou J., Liu M., Wu X.;
RT "IXL, a new subunit of the mammalian Mediator complex, functions as a
RT transcriptional suppressor.";
RL Biochem. Biophys. Res. Commun. 325:1330-1338(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Signet-ring cell carcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION IN THE TRAP/SMCC MEDIATOR COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND INTERACTION WITH MED18 AND MED20.
RX PubMed=14576168; DOI=10.1074/jbc.c300444200;
RA Sato S., Tomomori-Sato C., Banks C.A.S., Parmely T.J., Sorokina I.,
RA Brower C.S., Conaway R.C., Conaway J.W.;
RT "A mammalian homolog of Drosophila melanogaster transcriptional coactivator
RT intersex is a subunit of the mammalian Mediator complex.";
RL J. Biol. Chem. 278:49671-49674(2003).
RN [7]
RP IDENTIFICATION IN THE TRAP/SMCC MEDIATOR COMPLEX.
RX PubMed=14638676; DOI=10.1074/jbc.m312523200;
RA Tomomori-Sato C., Sato S., Parmely T.J., Banks C.A.S., Sorokina I.,
RA Florens L., Zybailov B., Washburn M.P., Brower C.S., Conaway R.C.,
RA Conaway J.W.;
RT "A mammalian mediator subunit that shares properties with Saccharomyces
RT cerevisiae mediator subunit Cse2.";
RL J. Biol. Chem. 279:5846-5851(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MEDIATOR
RP COMPLEX.
RX PubMed=15175163; DOI=10.1016/j.molcel.2004.05.006;
RA Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B.,
RA Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P., Conaway J.W.,
RA Conaway R.C.;
RT "A set of consensus mammalian mediator subunits identified by
RT multidimensional protein identification technology.";
RL Mol. Cell 14:685-691(2004).
RN [9]
RP INTERACTION WITH CCNC; MED1; MED12; MED13; MED17; MED20 AND MED21,
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
RP COMPLEX, AND ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
RX PubMed=15989967; DOI=10.1016/j.molcel.2005.05.015;
RA Zhang X., Krutchinsky A., Fukuda A., Chen W., Yamamura S., Chait B.T.,
RA Roeder R.G.;
RT "MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation
RT enriched in RNA polymerase II and is required for ER-mediated
RT transcription.";
RL Mol. Cell 19:89-100(2005).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC the regulated transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. Mediator is recruited to promoters by direct
CC interactions with regulatory proteins and serves as a scaffold for the
CC assembly of a functional preinitiation complex with RNA polymerase II
CC and the general transcription factors. {ECO:0000269|PubMed:15555573}.
CC -!- SUBUNIT: Component of the Mediator complex, which is composed of MED1,
CC MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L,
CC MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23,
CC MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and
CC CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct
CC module termed the CDK8 module. Mediator containing the CDK8 module is
CC less active than Mediator lacking this module in supporting
CC transcriptional activation. Individual preparations of the Mediator
CC complex lacking one or more distinct subunits have been variously
CC termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Associates with the
CC MED18/MED20 heteromer. {ECO:0000269|PubMed:14576168,
CC ECO:0000269|PubMed:14638676, ECO:0000269|PubMed:15175163,
CC ECO:0000269|PubMed:15989967}.
CC -!- INTERACTION:
CC Q9NX70; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-394656, EBI-11096309;
CC Q9NX70; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-394656, EBI-742038;
CC Q9NX70; O75934: BCAS2; NbExp=3; IntAct=EBI-394656, EBI-1050106;
CC Q9NX70; Q14232: EIF2B1; NbExp=3; IntAct=EBI-394656, EBI-491065;
CC Q9NX70; Q9BUE0: MED18; NbExp=6; IntAct=EBI-394656, EBI-394640;
CC Q9NX70; A0JLT2: MED19; NbExp=8; IntAct=EBI-394656, EBI-394430;
CC Q9NX70; Q9H944: MED20; NbExp=6; IntAct=EBI-394656, EBI-394644;
CC Q9NX70; Q15528: MED22; NbExp=4; IntAct=EBI-394656, EBI-394687;
CC Q9NX70; Q9H204: MED28; NbExp=3; IntAct=EBI-394656, EBI-514199;
CC Q9NX70; O75586: MED6; NbExp=3; IntAct=EBI-394656, EBI-394624;
CC Q9NX70; Q9H7Z3: NRDE2; NbExp=3; IntAct=EBI-394656, EBI-1042642;
CC Q9NX70; A1L4H1: SSC5D; NbExp=3; IntAct=EBI-394656, EBI-10172867;
CC Q9NX70; Q9D8C6: Med11; Xeno; NbExp=2; IntAct=EBI-394656, EBI-6260909;
CC Q9NX70; Q9R0X0: Med20; Xeno; NbExp=2; IntAct=EBI-394656, EBI-398698;
CC Q9NX70; Q9CQI9: Med30; Xeno; NbExp=2; IntAct=EBI-394656, EBI-309220;
CC Q9NX70; Q9D7W5: Med8; Xeno; NbExp=2; IntAct=EBI-394656, EBI-7990252;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15555573}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NX70-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NX70-2; Sequence=VSP_056133, VSP_056134;
CC -!- TISSUE SPECIFICITY: Widely expressed in embryo and adult.
CC {ECO:0000269|PubMed:15555573}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 29 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU43732.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY729650; AAU43732.1; ALT_INIT; mRNA.
DR EMBL; AK000411; BAA91147.1; -; mRNA.
DR EMBL; AK298014; BAG60318.1; -; mRNA.
DR EMBL; AL137304; CAB70687.2; -; mRNA.
DR EMBL; AC005239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019015; AAH19015.1; -; mRNA.
DR CCDS; CCDS33021.1; -. [Q9NX70-1]
DR PIR; T46497; T46497.
DR RefSeq; NP_001304699.1; NM_001317770.1. [Q9NX70-2]
DR RefSeq; NP_060062.1; NM_017592.2. [Q9NX70-1]
DR PDB; 7EMF; EM; 3.50 A; 2=1-200.
DR PDB; 7ENA; EM; 4.07 A; b=1-200.
DR PDB; 7ENC; EM; 4.13 A; b=1-200.
DR PDB; 7ENJ; EM; 4.40 A; 2=1-200.
DR PDB; 7LBM; EM; 4.80 A; p=1-200.
DR PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR AlphaFoldDB; Q9NX70; -.
DR SMR; Q9NX70; -.
DR BioGRID; 120734; 102.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; Q9NX70; -.
DR IntAct; Q9NX70; 104.
DR MINT; Q9NX70; -.
DR STRING; 9606.ENSP00000314343; -.
DR GlyGen; Q9NX70; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NX70; -.
DR PhosphoSitePlus; Q9NX70; -.
DR BioMuta; MED29; -.
DR DMDM; 74734688; -.
DR EPD; Q9NX70; -.
DR jPOST; Q9NX70; -.
DR MassIVE; Q9NX70; -.
DR MaxQB; Q9NX70; -.
DR PaxDb; Q9NX70; -.
DR PeptideAtlas; Q9NX70; -.
DR PRIDE; Q9NX70; -.
DR ProteomicsDB; 83050; -. [Q9NX70-1]
DR Antibodypedia; 30311; 63 antibodies from 19 providers.
DR DNASU; 55588; -.
DR Ensembl; ENST00000315588.11; ENSP00000314343.5; ENSG00000063322.15. [Q9NX70-1]
DR Ensembl; ENST00000594368.5; ENSP00000472501.2; ENSG00000063322.15. [Q9NX70-2]
DR GeneID; 55588; -.
DR KEGG; hsa:55588; -.
DR MANE-Select; ENST00000315588.11; ENSP00000314343.5; NM_017592.4; NP_060062.2.
DR UCSC; uc060ykk.1; human. [Q9NX70-1]
DR CTD; 55588; -.
DR DisGeNET; 55588; -.
DR GeneCards; MED29; -.
DR HGNC; HGNC:23074; MED29.
DR HPA; ENSG00000063322; Low tissue specificity.
DR MIM; 612914; gene.
DR neXtProt; NX_Q9NX70; -.
DR OpenTargets; ENSG00000063322; -.
DR PharmGKB; PA162395655; -.
DR VEuPathDB; HostDB:ENSG00000063322; -.
DR eggNOG; ENOG502QRNJ; Eukaryota.
DR GeneTree; ENSGT00390000007540; -.
DR HOGENOM; CLU_1312718_0_0_1; -.
DR InParanoid; Q9NX70; -.
DR OrthoDB; 1362864at2759; -.
DR PhylomeDB; Q9NX70; -.
DR TreeFam; TF326632; -.
DR PathwayCommons; Q9NX70; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; Q9NX70; -.
DR SIGNOR; Q9NX70; -.
DR BioGRID-ORCS; 55588; 414 hits in 1090 CRISPR screens.
DR ChiTaRS; MED29; human.
DR GenomeRNAi; 55588; -.
DR Pharos; Q9NX70; Tbio.
DR PRO; PR:Q9NX70; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NX70; protein.
DR Bgee; ENSG00000063322; Expressed in prefrontal cortex and 181 other tissues.
DR ExpressionAtlas; Q9NX70; baseline and differential.
DR Genevisible; Q9NX70; HS.
DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR InterPro; IPR021018; Mediator_Med29_met.
DR PANTHER; PTHR28314; PTHR28314; 1.
DR Pfam; PF11568; Med29; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..200
FT /note="Mediator of RNA polymerase II transcription subunit
FT 29"
FT /id="PRO_0000288058"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VAR_SEQ 121..196
FT /note="RLAHECLSQSCDSAKHSPTLVPTATKPDAVQPDSLPYPQYLAVIKAQISCAK
FT DIHTALLDCANKVTGKTPAPPAGP -> PPSPTQCSLTASPTHSTWRSSKPRFPVPRTF
FT TPPCWTVPTRSRARHPHHLLALGALCEVGDREWGRQWLVGGVQRE (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056133"
FT VAR_SEQ 197..200
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056134"
FT HELIX 56..89
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 102..135
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 157..185
FT /evidence="ECO:0007829|PDB:7EMF"
SQ SEQUENCE 200 AA; 21073 MW; E0CDA1DDD89635CA CRC64;
MAASQQQASA ASSAAGVSGP SSAGGPGPQQ QPQPPAQLVG PAQSGLLQQQ QQDFDPVQRY
KMLIPQLKES LQTLMKVAAQ NLIQNTNIDN GQKSSDGPIQ RFDKCLEEFY ALCDQLELCL
RLAHECLSQS CDSAKHSPTL VPTATKPDAV QPDSLPYPQY LAVIKAQISC AKDIHTALLD
CANKVTGKTP APPAGPGGTL
