MED17_HUMAN
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 03-AUG-2022, entry version 172.
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=3; IntAct=EBI-394562, EBI-394640;
CC Q9NVC6; Q15528: MED22; NbExp=4; IntAct=EBI-394562, EBI-394687;
CC Q9NVC6; Q6P2C8: MED27; NbExp=3; IntAct=EBI-394562, EBI-394603;
CC Q9NVC6; Q9H204: MED28; NbExp=2; IntAct=EBI-394562, EBI-514199;
CC Q9NVC6; O75586: MED6; NbExp=2; 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_004268.4. [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 PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR AlphaFoldDB; Q9NVC6; -.
DR SMR; Q9NVC6; -.
DR BioGRID; 114830; 207.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; Q9NVC6; -.
DR DIP; DIP-31451N; -.
DR IntAct; Q9NVC6; 67.
DR MINT; Q9NVC6; -.
DR STRING; 9606.ENSP00000251871; -.
DR iPTMnet; Q9NVC6; -.
DR PhosphoSitePlus; Q9NVC6; -.
DR BioMuta; MED17; -.
DR DMDM; 296437366; -.
DR EPD; Q9NVC6; -.
DR jPOST; Q9NVC6; -.
DR MassIVE; Q9NVC6; -.
DR MaxQB; Q9NVC6; -.
DR PaxDb; Q9NVC6; -.
DR PeptideAtlas; Q9NVC6; -.
DR PRIDE; Q9NVC6; -.
DR ProteomicsDB; 82777; -. [Q9NVC6-1]
DR ProteomicsDB; 82778; -. [Q9NVC6-2]
DR Antibodypedia; 17843; 294 antibodies from 33 providers.
DR DNASU; 9440; -.
DR Ensembl; ENST00000251871.9; ENSP00000251871.3; ENSG00000042429.12. [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 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 neXtProt; NX_Q9NVC6; -.
DR OpenTargets; ENSG00000042429; -.
DR Orphanet; 402364; Infantile cerebral and cerebellar atrophy with postnatal progressive microcephaly.
DR PharmGKB; PA162395443; -.
DR VEuPathDB; HostDB:ENSG00000042429; -.
DR eggNOG; KOG4512; Eukaryota.
DR GeneTree; ENSGT00390000011810; -.
DR HOGENOM; CLU_028003_1_0_1; -.
DR InParanoid; Q9NVC6; -.
DR OMA; CQIYQHQ; -.
DR OrthoDB; 976669at2759; -.
DR PhylomeDB; Q9NVC6; -.
DR TreeFam; TF323615; -.
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 SignaLink; Q9NVC6; -.
DR SIGNOR; Q9NVC6; -.
DR BioGRID-ORCS; 9440; 725 hits in 1087 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 126 other tissues.
DR ExpressionAtlas; Q9NVC6; baseline and differential.
DR Genevisible; Q9NVC6; 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; 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:0030374; F:nuclear receptor coactivator activity; IDA: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:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
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 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; IDA:MGI.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:ProtInc.
DR InterPro; IPR019313; Mediator_Med17.
DR PANTHER; PTHR13114; PTHR13114; 1.
DR Pfam; PF10156; Med17; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Direct protein sequencing;
KW Disease variant; Nucleus; Reference proteome; Transcription;
KW 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 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
