ID   MED17_HUMAN             Reviewed;         651 AA.
AC   Q9NVC6; B3KN07; Q9HA81; Q9UNP7; Q9Y2W0; Q9Y660;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   02-SEP-2026, entry version 190.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 17;
DE   AltName: Full=Activator-recruited cofactor 77 kDa component;
DE            Short=ARC77;
DE   AltName: Full=Cofactor required for Sp1 transcriptional activation subunit 6;
DE            Short=CRSP complex subunit 6;
DE   AltName: Full=Mediator complex subunit 17;
DE   AltName: Full=Thyroid hormone receptor-associated protein complex 80 kDa component;
DE            Short=Trap80;
DE   AltName: Full=Transcriptional coactivator CRSP77;
DE   AltName: Full=Vitamin D3 receptor-interacting protein complex 80 kDa component;
DE            Short=DRIP80;
GN   Name=MED17; Synonyms=ARC77, CRSP6, DRIP77, DRIP80, TRAP80;
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), PROTEIN SEQUENCE OF 306-319;
RP   405-415 AND 592-602, TISSUE SPECIFICITY, IDENTIFICATION IN TRAP COMPLEX,
RP   AND VARIANT ASP-69.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=10198638; DOI=10.1016/s1097-2765(00)80463-3;
RA   Ito M., Yuan C.-X., Malik S., Gu W., Fondell J.D., Yamamura S., Fu Z.-Y.,
RA   Zhang X., Qin J., Roeder R.G.;
RT   "Identity between TRAP and SMCC complexes indicates novel pathways for the
RT   function of nuclear receptors and diverse mammalian activators.";
RL   Mol. Cell 3:361-370(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 88-99 AND
RP   607-619, IDENTIFICATION IN ARC COMPLEX, AND VARIANT ASP-69.
RC   TISSUE=Cervix carcinoma;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   ASP-69.
RC   TISSUE=Embryo;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-69.
RC   TISSUE=Skin;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 269-651 (ISOFORM 1).
RX   PubMed=9989412; DOI=10.1038/17141;
RA   Ryu S., Zhou S., Ladurner A.G., Tjian R.;
RT   "The transcriptional cofactor complex CRSP is required for activity of the
RT   enhancer-binding protein Sp1.";
RL   Nature 397:446-450(1999).
RN   [7]
RP   IDENTIFICATION IN ARC COMPLEX, AND PROTEIN SEQUENCE OF 168-179 AND 355-361.
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   [8]
RP   INTERACTION WITH MED10.
RX   PubMed=12584197; DOI=10.1074/jbc.c300054200;
RA   Sato S., Tomomori-Sato C., Banks C.A.S., Sorokina I., Parmely T.J.,
RA   Kong S.E., Jin J., Cai Y., Lane W.S., Brower C.S., Conaway R.C.,
RA   Conaway J.W.;
RT   "Identification of mammalian Mediator subunits with similarities to yeast
RT   Mediator subunits Srb5, Srb6, Med11, and Rox3.";
RL   J. Biol. Chem. 278:15123-15127(2003).
RN   [9]
RP   INTERACTION WITH STAT2.
RX   PubMed=12509459; DOI=10.1128/mcb.23.2.620-628.2003;
RA   Lau J.F., Nusinzon I., Burakov D., Freedman L.P., Horvath C.M.;
RT   "Role of metazoan mediator proteins in interferon-responsive
RT   transcription.";
RL   Mol. Cell. Biol. 23:620-628(2003).
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   INTERACTION WITH MED1; MED10; MED18; MED21; MED28 AND MED30, IDENTIFICATION
RP   BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, AND
RP   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   FUNCTION, AND INTERACTION WITH MED1 AND MED10.
RX   PubMed=16595664; DOI=10.1074/jbc.m601983200;
RA   Baek H.J., Kang Y.K., Roeder R.G.;
RT   "Human Mediator enhances basal transcription by facilitating recruitment of
RT   transcription factor IIB during preinitiation complex assembly.";
RL   J. Biol. Chem. 281:15172-15181(2006).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [14]
RP   VARIANT [LARGE SCALE ANALYSIS] ASP-69, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [15]
RP   VARIANT [LARGE SCALE ANALYSIS] ASP-69, AND IDENTIFICATION BY MASS
RP   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   [16]
RP   VARIANT MCPHSBA PRO-371.
RX   PubMed=20950787; DOI=10.1016/j.ajhg.2010.09.016;
RA   Kaufmann R., Straussberg R., Mandel H., Fattal-Valevski A., Ben-Zeev B.,
RA   Naamati A., Shaag A., Zenvirt S., Konen O., Mimouni-Bloch A., Dobyns W.B.,
RA   Edvardson S., Pines O., Elpeleg O.;
RT   "Infantile cerebral and cerebellar atrophy is associated with a mutation in
RT   the MED17 subunit of the transcription preinitiation mediator complex.";
RL   Am. J. Hum. Genet. 87:667-670(2010).
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:16595664}.
CC   -!- SUBUNIT: Interacts with GATA1 and PPARG (By similarity). Component of
CC       the Mediator complex, which is composed of MED1, MED4, MED6, MED7,
CC       MED8, MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16,
CC       MED17, MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26,
CC       MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12,
CC       MED13, CCNC and CDK8 subunits form a distinct module termed the CDK8
CC       module. Mediator containing the CDK8 module is less active than
CC       Mediator lacking this module in supporting transcriptional activation.
CC       Individual preparations of the Mediator complex lacking one or more
CC       distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC
CC       and TRAP. Interacts with STAT2. {ECO:0000250,
CC       ECO:0000269|PubMed:10198638, ECO:0000269|PubMed:10235266,
CC       ECO:0000269|PubMed:10235267, ECO:0000269|PubMed:12509459,
CC       ECO:0000269|PubMed:12584197, ECO:0000269|PubMed:15175163,
CC       ECO:0000269|PubMed:15989967, ECO:0000269|PubMed:16595664}.
CC   -!- INTERACTION:
CC       Q9NVC6; Q9BUE0: MED18; NbExp=8; IntAct=EBI-394562, EBI-394640;
CC       Q9NVC6; Q15528: MED22; NbExp=8; IntAct=EBI-394562, EBI-394687;
CC       Q9NVC6; Q6P2C8: MED27; NbExp=8; IntAct=EBI-394562, EBI-394603;
CC       Q9NVC6; Q9H204: MED28; NbExp=7; IntAct=EBI-394562, EBI-514199;
CC       Q9NVC6; O75586: MED6; NbExp=6; IntAct=EBI-394562, EBI-394624;
CC       Q9NVC6; Q9D8C6: Med11; Xeno; NbExp=2; IntAct=EBI-394562, EBI-6260909;
CC       Q9NVC6; Q9CQI9: Med30; Xeno; NbExp=2; IntAct=EBI-394562, EBI-309220;
CC       Q9NVC6; Q9D7W5: Med8; Xeno; NbExp=2; IntAct=EBI-394562, EBI-7990252;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NVC6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NVC6-2; Sequence=VSP_028115, VSP_028116;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10198638}.
CC   -!- DISEASE: Microcephaly, postnatal progressive, with seizures and brain
CC       atrophy (MCPHSBA) [MIM:613668]: A disorder characterized by postnatal
CC       progressive microcephaly and severe developmental retardation
CC       associated with cerebral and cerebellar atrophy. Infants manifest
CC       swallowing difficulties leading to failure to thrive, jitteriness, poor
CC       visual fixation, truncal arching, seizures. There is no acquisition of
CC       developmental milestones and patients suffer from marked spasticity and
CC       profound retardation. Progressive microcephaly becomes evident few
CC       months after birth. {ECO:0000269|PubMed:20950787}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 17 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD30856.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF117657; AAD22031.2; -; mRNA.
DR   EMBL; AF105421; AAD30856.1; ALT_FRAME; mRNA.
DR   EMBL; AK001674; BAA91827.1; -; mRNA.
DR   EMBL; AK022156; BAB13973.1; -; mRNA.
DR   EMBL; AK023209; BAG51169.1; -; mRNA.
DR   EMBL; AC022150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC021101; AAH21101.1; -; mRNA.
DR   EMBL; AF104254; AAD12723.1; -; mRNA.
DR   CCDS; CCDS8295.1; -. [Q9NVC6-1]
DR   RefSeq; NP_004259.3; NM_004268.5. [Q9NVC6-1]
DR   PDB; 7EMF; EM; 3.50 A; Q=1-651.
DR   PDB; 7ENA; EM; 4.07 A; q=1-651.
DR   PDB; 7ENC; EM; 4.13 A; q=1-651.
DR   PDB; 7ENJ; EM; 4.40 A; Q=1-651.
DR   PDB; 7LBM; EM; 4.80 A; j=1-651.
DR   PDB; 7NVR; EM; 4.50 A; d=1-651.
DR   PDB; 8GXQ; EM; 5.04 A; q=1-651.
DR   PDB; 8GXS; EM; 4.16 A; q=1-651.
DR   PDB; 8T9D; EM; 4.66 A; L=1-651.
DR   PDB; 8TQW; EM; 8.20 A; Q=1-651.
DR   PDB; 8TRH; EM; 3.70 A; Q=1-651.
DR   AlphaFoldDB; Q9NVC6; -.
DR   EMDB; EMD-12610; -.
DR   EMDB; EMD-23255; -.
DR   EMDB; EMD-31191; -.
DR   EMDB; EMD-31204; -.
DR   EMDB; EMD-31207; -.
DR   EMDB; EMD-31211; -.
DR   EMDB; EMD-34359; -.
DR   EMDB; EMD-34360; -.
DR   EMDB; EMD-41107; -.
DR   EMDB; EMD-41565; -.
DR   EMDB; EMD-41580; -.
DR   SMR; Q9NVC6; -.
DR   BioGRID; 114830; 231.
DR   ComplexPortal; CPX-3227; Core mediator complex.
DR   CORUM; Q9NVC6; -.
DR   DIP; DIP-31451N; -.
DR   FunCoup; Q9NVC6; 4292.
DR   IntAct; Q9NVC6; 149.
DR   MINT; Q9NVC6; -.
DR   NDEx; IQUERY-CP-MED17; 1 NDEx IQuery Curated Pathway.
DR   STRING; 9606.ENSP00000251871; -.
DR   GlyGen; Q9NVC6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NVC6; -.
DR   PhosphoSitePlus; Q9NVC6; -.
DR   BioMuta; MED17; -.
DR   DMDM; 296437366; -.
DR   jPOST; Q9NVC6; -.
DR   MassIVE; Q9NVC6; -.
DR   PaxDb; 9606-ENSP00000251871; -.
DR   PeptideAtlas; Q9NVC6; -.
DR   ProteomicsDB; 82777; -. [Q9NVC6-1]
DR   ProteomicsDB; 82778; -. [Q9NVC6-2]
DR   Pumba; Q9NVC6; -.
DR   Antibodypedia; 17843; 287 antibodies from 36 providers.
DR   DNASU; 9440; -.
DR   Ensembl; ENST00000251871.9; ENSP00000251871.3; ENSG00000042429.13. [Q9NVC6-1]
DR   GeneID; 9440; -.
DR   KEGG; hsa:9440; -.
DR   MANE-Select; ENST00000251871.9; ENSP00000251871.3; NM_004268.5; NP_004259.3.
DR   UCSC; uc001pel.3; human. [Q9NVC6-1]
DR   AGR; HGNC:2375; -.
DR   ClinPGx; PA162395443; -.
DR   CTD; 9440; -.
DR   DisGeNET; 9440; -.
DR   GeneCards; MED17; -.
DR   HGNC; HGNC:2375; MED17.
DR   HPA; ENSG00000042429; Low tissue specificity.
DR   MalaCards; MED17; -.
DR   MIM; 603810; gene.
DR   MIM; 613668; phenotype.
DR   OpenTargets; ENSG00000042429; -.
DR   Orphanet; 402364; Infantile cerebral and cerebellar atrophy with postnatal progressive microcephaly.
DR   VEuPathDB; HostDB:ENSG00000042429; -.
DR   eggNOG; KOG4512; Eukaryota.
DR   GeneTree; ENSGT00390000011810; -.
DR   HOGENOM; CLU_028003_1_0_1; -.
DR   InParanoid; Q9NVC6; -.
DR   OMA; HMSYEPQ; -.
DR   OrthoDB; 10058398at2759; -.
DR   PAN-GO; Q9NVC6; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9NVC6; -.
DR   PathwayCommons; Q9NVC6; -.
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   Reactome; R-HSA-9833110; RSV-host interactions.
DR   Reactome; R-HSA-9841922; MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis.
DR   SignaLink; Q9NVC6; -.
DR   SIGNOR; Q9NVC6; -.
DR   Agora; ENSG00000042429; -.
DR   BioGRID-ORCS; 9440; 754 hits in 1168 CRISPR screens.
DR   ChiTaRS; MED17; human.
DR   GeneWiki; MED17; -.
DR   GenomeRNAi; 9440; -.
DR   Pharos; Q9NVC6; Tbio.
DR   PRO; PR:Q9NVC6; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9NVC6; protein.
DR   Bgee; ENSG00000042429; Expressed in sural nerve and 128 other cell types or tissues.
DR   ExpressionAtlas; Q9NVC6; baseline and differential.
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; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
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:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; NAS:ComplexPortal.
DR   GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; NAS:ComplexPortal.
DR   GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; TAS:ProtInc.
DR   InterPro; IPR063235; Med17_C.
DR   InterPro; IPR061954; Med17_M.
DR   InterPro; IPR063477; Med17_N.
DR   InterPro; IPR019313; Mediator_Med17.
DR   PANTHER; PTHR13114; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 17; 1.
DR   PANTHER; PTHR13114:SF7; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 17; 1.
DR   Pfam; PF10156; Med17; 1.
DR   Pfam; PF30532; Med17_C; 1.
DR   Pfam; PF30534; Med17_M; 1.
DR   PDBsum; 7EMF; -.
DR   PDBsum; 7ENA; -.
DR   PDBsum; 7ENC; -.
DR   PDBsum; 7ENJ; -.
DR   PDBsum; 7LBM; -.
DR   PDBsum; 7NVR; -.
DR   PDBsum; 8GXQ; -.
DR   PDBsum; 8GXS; -.
DR   PDBsum; 8T9D; -.
DR   PDBsum; 8TQW; -.
DR   PDBsum; 8TRH; -.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Direct protein sequencing;
KW   Disease variant; Nucleus; Proteomics identification; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..651
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   17"
FT                   /id="PRO_0000079359"
FT   REGION          51..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         140..145
FT                   /note="NPQTLQ -> VFVDFN (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_028115"
FT   VAR_SEQ         146..651
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_028116"
FT   VARIANT         69
FT                   /note="E -> D (in dbSNP:rs2848477)"
FT                   /evidence="ECO:0000269|PubMed:10198638,
FT                   ECO:0000269|PubMed:10235266, ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:19369195"
FT                   /id="VAR_063126"
FT   VARIANT         357
FT                   /note="F -> L (in dbSNP:rs35313315)"
FT                   /id="VAR_057781"
FT   VARIANT         371
FT                   /note="L -> P (in MCPHSBA; dbSNP:rs267607232)"
FT                   /evidence="ECO:0000269|PubMed:20950787"
FT                   /id="VAR_065066"
FT   CONFLICT        21
FT                   /note="E -> G (in Ref. 3; BAB13973)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        58
FT                   /note="E -> G (in Ref. 3; BAB13973)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        356
FT                   /note="K -> N (in Ref. 2; AAD30856)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        409
FT                   /note="G -> Q (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        531
FT                   /note="Q -> H (in Ref. 6; AAD12723)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..6
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   HELIX           11..13
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   HELIX           37..46
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   HELIX           97..120
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          126..129
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   HELIX           140..171
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   HELIX           183..193
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          194..199
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          202..206
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   TURN            209..213
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          221..226
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          243..246
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          255..263
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   HELIX           290..317
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          328..333
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          340..347
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   HELIX           369..386
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   HELIX           389..391
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          394..398
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   HELIX           403..407
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   TURN            408..412
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   HELIX           415..421
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   HELIX           427..454
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   TURN            485..487
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          492..497
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          502..506
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          511..514
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   HELIX           520..543
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          547..555
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          557..559
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          562..564
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          566..573
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          576..584
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          586..588
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          591..595
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          602..604
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   HELIX           614..616
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          622..625
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   STRAND          633..635
FT                   /evidence="ECO:0007829|PDB:7EMF"
FT   HELIX           636..645
FT                   /evidence="ECO:0007829|PDB:7EMF"
SQ   SEQUENCE   651 AA;  72890 MW;  47011210952D287B CRC64;
     MSGVRAVRIS IESACEKQVH EVGLDGTETY LPPLSMSQNL ARLAQRIDFS QGSGSEEEEA
     AGTEGDAQEW PGAGSSADQD DEEGVVKFQP SLWPWDSVRN NLRSALTEMC VLYDVLSIVR
     DKKFMTLDPV SQDALPPKQN PQTLQLISKK KSLAGAAQIL LKGAERLTKS VTENQENKLQ
     RDFNSELLRL RQHWKLRKVG DKILGDLSYR SAGSLFPHHG TFEVIKNTDL DLDKKIPEDY
     CPLDVQIPSD LEGSAYIKVS IQKQAPDIGD LGTVNLFKRP LPKSKPGSPH WQTKLEAAQN
     VLLCKEIFAQ LSREAVQIKS QVPHIVVKNQ IISQPFPSLQ LSISLCHSSN DKKSQKFATE
     KQCPEDHLYV LEHNLHLLIR EFHKQTLSSI MMPHPASAPF GHKRMRLSGP QAFDKNEINS
     LQSSEGLLEK IIKQAKHIFL RSRAAATIDS LASRIEDPQI QAHWSNINDV YESSVKVLIT
     SQGYEQICKS IQLQLNIGVE QIRVVHRDGR VITLSYQEQE LQDFLLSQMS QHQVHAVQQL
     AKVMGWQVLS FSNHVGLGPI ESIGNASAIT VASPSGDYAI SVRNGPESGS KIMVQFPRNQ
     CKDLPKSDVL QDNKWSHLRG PFKEVQWNKM EGRNFVYKME LLMSALSPCL L
//