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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
 
 
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