MED4_HUMAN
ID MED4_HUMAN Reviewed; 270 AA.
AC Q9NPJ6; B4DX67; Q53GB4; Q53H68; Q5T912; Q6FHC4; Q6IA79; Q9BS95; Q9NYR5;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 4;
DE AltName: Full=Activator-recruited cofactor 36 kDa component;
DE Short=ARC36;
DE AltName: Full=Mediator complex subunit 4;
DE AltName: Full=TRAP/SMCC/PC2 subunit p36 subunit;
DE AltName: Full=Vitamin D3 receptor-interacting protein complex 36 kDa component;
DE Short=DRIP36;
GN Name=MED4; Synonyms=ARC36, DRIP36, VDRIP; ORFNames=HSPC126;
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).
RX PubMed=10235266; DOI=10.1038/19783;
RA Rachez C., Lemon B.D., Suldan Z., Bromleigh V., Gamble M., Naeaer A.M.,
RA Erdjument-Bromage H., Tempst P., Freedman L.P.;
RT "Ligand-dependent transcription activation by nuclear receptors requires
RT the DRIP complex.";
RL Nature 398:824-828(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 14-27 AND
RP 30-42.
RX PubMed=10882111; DOI=10.1016/s1097-2765(00)80254-3;
RA Malik S., Gu W., Wu W., Qin J., Roeder R.G.;
RT "The USA-derived transcriptional coactivator PC2 is a submodule of
RT TRAP/SMCC and acts synergistically with other PCs.";
RL Mol. Cell 5:753-760(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Small intestine;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [8]
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 [9]
RP IDENTIFICATION IN ARC COMPLEX, AND PROTEIN SEQUENCE OF 81-88; 154-165 AND
RP 173-183.
RX PubMed=10235267; DOI=10.1038/19789;
RA Naeaer A.M., Beaurang P.A., Zhou S., Abraham S., Solomon W.B., Tjian R.;
RT "Composite co-activator ARC mediates chromatin-directed transcriptional
RT activation.";
RL Nature 398:828-832(1999).
RN [10]
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
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=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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.
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.
CC {ECO:0000269|PubMed:10235267, ECO:0000269|PubMed:15175163,
CC ECO:0000269|PubMed:15989967}.
CC -!- INTERACTION:
CC Q9NPJ6; A2BDD9: AMOT; NbExp=3; IntAct=EBI-394607, EBI-17286414;
CC Q9NPJ6; Q4VCS5-2: AMOT; NbExp=3; IntAct=EBI-394607, EBI-3891843;
CC Q9NPJ6; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-394607, EBI-747505;
CC Q9NPJ6; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-394607, EBI-10247802;
CC Q9NPJ6; Q8TD31-3: CCHCR1; NbExp=6; IntAct=EBI-394607, EBI-10175300;
CC Q9NPJ6; Q8WYA6: CTNNBL1; NbExp=3; IntAct=EBI-394607, EBI-748128;
CC Q9NPJ6; Q8NE31: FAM13C; NbExp=3; IntAct=EBI-394607, EBI-751248;
CC Q9NPJ6; Q96NE9: FRMD6; NbExp=3; IntAct=EBI-394607, EBI-741729;
CC Q9NPJ6; O95954: FTCD; NbExp=3; IntAct=EBI-394607, EBI-10192648;
CC Q9NPJ6; Q96CN9: GCC1; NbExp=3; IntAct=EBI-394607, EBI-746252;
CC Q9NPJ6; Q96CS2: HAUS1; NbExp=4; IntAct=EBI-394607, EBI-2514791;
CC Q9NPJ6; O14964: HGS; NbExp=3; IntAct=EBI-394607, EBI-740220;
CC Q9NPJ6; Q8IY31: IFT20; NbExp=4; IntAct=EBI-394607, EBI-744203;
CC Q9NPJ6; Q96PC2: IP6K3; NbExp=3; IntAct=EBI-394607, EBI-10990676;
CC Q9NPJ6; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-394607, EBI-2125614;
CC Q9NPJ6; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-394607, EBI-14069005;
CC Q9NPJ6; Q32MZ4-4: LRRFIP1; NbExp=3; IntAct=EBI-394607, EBI-10240044;
CC Q9NPJ6; Q8N8X9: MAB21L3; NbExp=3; IntAct=EBI-394607, EBI-10268010;
CC Q9NPJ6; Q96EZ8: MCRS1; NbExp=4; IntAct=EBI-394607, EBI-348259;
CC Q9NPJ6; Q93074: MED12; NbExp=8; IntAct=EBI-394607, EBI-394357;
CC Q9NPJ6; Q13503: MED21; NbExp=5; IntAct=EBI-394607, EBI-394678;
CC Q9NPJ6; O95402: MED26; NbExp=11; IntAct=EBI-394607, EBI-394392;
CC Q9NPJ6; Q9NWA0: MED9; NbExp=12; IntAct=EBI-394607, EBI-394653;
CC Q9NPJ6; O14777: NDC80; NbExp=4; IntAct=EBI-394607, EBI-715849;
CC Q9NPJ6; O43482: OIP5; NbExp=3; IntAct=EBI-394607, EBI-536879;
CC Q9NPJ6; O00560: SDCBP; NbExp=3; IntAct=EBI-394607, EBI-727004;
CC Q9NPJ6; Q96ES7: SGF29; NbExp=3; IntAct=EBI-394607, EBI-743117;
CC Q9NPJ6; Q96GM5: SMARCD1; NbExp=6; IntAct=EBI-394607, EBI-358489;
CC Q9NPJ6; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-394607, EBI-455078;
CC Q9NPJ6; Q99909: SSX3; NbExp=6; IntAct=EBI-394607, EBI-10295431;
CC Q9NPJ6; Q6PIF2: SYCE2; NbExp=3; IntAct=EBI-394607, EBI-11958386;
CC Q9NPJ6; Q08117: TLE5; NbExp=3; IntAct=EBI-394607, EBI-717810;
CC Q9NPJ6; O95379: TNFAIP8; NbExp=7; IntAct=EBI-394607, EBI-1049336;
CC Q9NPJ6; Q8WVP5: TNFAIP8L1; NbExp=3; IntAct=EBI-394607, EBI-752102;
CC Q9NPJ6; P40222: TXLNA; NbExp=8; IntAct=EBI-394607, EBI-359793;
CC Q9NPJ6; Q8N3L3: TXLNB; NbExp=4; IntAct=EBI-394607, EBI-6116822;
CC Q9NPJ6; Q8N6Y0: USHBP1; NbExp=6; IntAct=EBI-394607, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NPJ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NPJ6-2; Sequence=VSP_047072;
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 4 family.
CC {ECO:0000305}.
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DR EMBL; AF300618; AAG22542.1; -; mRNA.
DR EMBL; AF230381; AAF37289.1; -; mRNA.
DR EMBL; AF161475; AAF29090.1; -; mRNA.
DR EMBL; AK001934; BAA91987.1; -; mRNA.
DR EMBL; CR457276; CAG33557.1; -; mRNA.
DR EMBL; CR541830; CAG46629.1; -; mRNA.
DR EMBL; AK222713; BAD96433.1; -; mRNA.
DR EMBL; AK301835; BAG63279.1; -; mRNA.
DR EMBL; AK223017; BAD96737.1; -; mRNA.
DR EMBL; AL158196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005189; AAH05189.1; -; mRNA.
DR CCDS; CCDS59241.1; -. [Q9NPJ6-2]
DR CCDS; CCDS9408.1; -. [Q9NPJ6-1]
DR RefSeq; NP_001257558.1; NM_001270629.1. [Q9NPJ6-2]
DR RefSeq; NP_054885.1; NM_014166.3. [Q9NPJ6-1]
DR PDB; 7EMF; EM; 3.50 A; D=1-270.
DR PDB; 7ENA; EM; 4.07 A; d=1-270.
DR PDB; 7ENC; EM; 4.13 A; d=1-270.
DR PDB; 7ENJ; EM; 4.40 A; D=1-270.
DR PDB; 7LBM; EM; 4.80 A; s=1-270.
DR PDB; 7NVR; EM; 4.50 A; h=1-270.
DR PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR AlphaFoldDB; Q9NPJ6; -.
DR SMR; Q9NPJ6; -.
DR BioGRID; 118849; 443.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; Q9NPJ6; -.
DR IntAct; Q9NPJ6; 378.
DR MINT; Q9NPJ6; -.
DR STRING; 9606.ENSP00000258648; -.
DR GlyGen; Q9NPJ6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NPJ6; -.
DR PhosphoSitePlus; Q9NPJ6; -.
DR BioMuta; MED4; -.
DR DMDM; 29840770; -.
DR EPD; Q9NPJ6; -.
DR jPOST; Q9NPJ6; -.
DR MassIVE; Q9NPJ6; -.
DR MaxQB; Q9NPJ6; -.
DR PaxDb; Q9NPJ6; -.
DR PeptideAtlas; Q9NPJ6; -.
DR PRIDE; Q9NPJ6; -.
DR ProteomicsDB; 5415; -.
DR ProteomicsDB; 82028; -. [Q9NPJ6-1]
DR Antibodypedia; 1791; 219 antibodies from 34 providers.
DR DNASU; 29079; -.
DR Ensembl; ENST00000258648.7; ENSP00000258648.2; ENSG00000136146.15. [Q9NPJ6-1]
DR Ensembl; ENST00000378586.5; ENSP00000367849.1; ENSG00000136146.15. [Q9NPJ6-2]
DR GeneID; 29079; -.
DR KEGG; hsa:29079; -.
DR MANE-Select; ENST00000258648.7; ENSP00000258648.2; NM_014166.4; NP_054885.1.
DR UCSC; uc001vby.3; human. [Q9NPJ6-1]
DR CTD; 29079; -.
DR DisGeNET; 29079; -.
DR GeneCards; MED4; -.
DR HGNC; HGNC:17903; MED4.
DR HPA; ENSG00000136146; Low tissue specificity.
DR MIM; 605718; gene.
DR neXtProt; NX_Q9NPJ6; -.
DR OpenTargets; ENSG00000136146; -.
DR PharmGKB; PA134877001; -.
DR VEuPathDB; HostDB:ENSG00000136146; -.
DR eggNOG; KOG4552; Eukaryota.
DR GeneTree; ENSGT00390000012063; -.
DR HOGENOM; CLU_082233_0_0_1; -.
DR InParanoid; Q9NPJ6; -.
DR OMA; GEIHMSV; -.
DR PhylomeDB; Q9NPJ6; -.
DR TreeFam; TF324421; -.
DR PathwayCommons; Q9NPJ6; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; Q9NPJ6; -.
DR SIGNOR; Q9NPJ6; -.
DR BioGRID-ORCS; 29079; 736 hits in 1083 CRISPR screens.
DR ChiTaRS; MED4; human.
DR GeneWiki; MED4; -.
DR GenomeRNAi; 29079; -.
DR Pharos; Q9NPJ6; Tbio.
DR PRO; PR:Q9NPJ6; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9NPJ6; protein.
DR Bgee; ENSG00000136146; Expressed in gingival epithelium and 194 other tissues.
DR ExpressionAtlas; Q9NPJ6; baseline and differential.
DR Genevisible; Q9NPJ6; HS.
DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; NAS:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IDA:UniProtKB.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; NAS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
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 GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR InterPro; IPR019258; Mediator_Med4.
DR PANTHER; PTHR13208; PTHR13208; 1.
DR Pfam; PF10018; Med4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; Coiled coil;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..270
FT /note="Mediator of RNA polymerase II transcription subunit
FT 4"
FT /id="PRO_0000096383"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 24..48
FT /evidence="ECO:0000255"
FT COILED 90..131
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047072"
FT CONFLICT 105
FT /note="S -> G (in Ref. 8; AAH05189)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="I -> T (in Ref. 5; CAG46629)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="Q -> R (in Ref. 6; BAD96737)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="A -> P (in Ref. 5; CAG33557)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="R -> K (in Ref. 2; AAF37289)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="P -> S (in Ref. 6; BAD96433)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="N -> D (in Ref. 8; AAH05189)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="S -> T (in Ref. 2; AAF37289 and 5; CAG46629)"
FT /evidence="ECO:0000305"
FT HELIX 27..51
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 63..140
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 145..156
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:7EMF"
SQ SEQUENCE 270 AA; 29745 MW; 05641357EBFA85F4 CRC64;
MAASSSGEKE KERLGGGLGV AGGNSTRERL LSALEDLEVL SRELIEMLAI SRNQKLLQAG
EENQVLELLI HRDGEFQELM KLALNQGKIH HEMQVLEKEV EKRDSDIQQL QKQLKEAEQI
LATAVYQAKE KLKSIEKARK GAISSEEIIK YAHRISASNA VCAPLTWVPG DPRRPYPTDL
EMRSGLLGQM NNPSTNGVNG HLPGDALAAG RLPDVLAPQY PWQSNDMSMN MLPPNHSSDF
LLEPPGHNKE NEDDVEIMST DSSSSSSESD
