ID THAP1_HUMAN Reviewed; 213 AA. AC Q9NVV9; A6NCB6; D3DSY5; H9KV49; Q53FQ1; Q6IA99; DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 24-JAN-2024, entry version 180. DE RecName: Full=THAP domain-containing protein 1; GN Name=THAP1; 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 [LARGE SCALE MRNA] (ISOFORM 1). 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT DYT6 RP ARG-89. RC TISSUE=Gastric mucosa; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Adipocyte; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] 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 [8] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PAWR. RX PubMed=12717420; DOI=10.1038/sj.onc.1206271; RA Roussigne M., Cayrol C., Clouaire T., Amalric F., Girard J.-P.; RT "THAP1 is a nuclear proapoptotic factor that links prostate-apoptosis- RT response-4 (Par-4) to PML nuclear bodies."; RL Oncogene 22:2432-2442(2003). RN [9] RP DNA-BINDING, ZINC-BINDING, AND MUTAGENESIS OF CYS-5; CYS-10; PRO-26; RP TRP-36; CYS-54; HIS-57; PHE-58 AND PRO-78. RX PubMed=15863623; DOI=10.1073/pnas.0406882102; RA Clouaire T., Roussigne M., Ecochard V., Mathe C., Amalric F., Girard J.-P.; RT "The THAP domain of THAP1 is a large C2CH module with zinc-dependent RT sequence-specific DNA-binding activity."; RL Proc. Natl. Acad. Sci. U.S.A. 102:6907-6912(2005). RN [10] RP FUNCTION, AND DNA-BINDING. RX PubMed=17003378; DOI=10.1182/blood-2006-03-012013; RA Cayrol C., Lacroix C., Mathe C., Ecochard V., Ceribelli M., Loreau E., RA Lazar V., Dessen P., Mantovani R., Aguilar L., Girard J.-P.; RT "The THAP-zinc finger protein THAP1 regulates endothelial cell RT proliferation through modulation of pRB/E2F cell-cycle target genes."; RL Blood 109:584-594(2007). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY IN A THAP1/THAP3-HCFC1-OGT COMPLEX, RP INTERACTION WITH HCFC1 AND OGT, TISSUE SPECIFICITY, AND FUNCTION. RX PubMed=20200153; DOI=10.1074/jbc.m109.072579; RA Mazars R., Gonzalez-de-Peredo A., Cayrol C., Lavigne A.C., Vogel J.L., RA Ortega N., Lacroix C., Gautier V., Huet G., Ray A., Monsarrat B., RA Kristie T.M., Girard J.P.; RT "The THAP-zinc finger protein THAP1 associates with coactivator HCF-1 and RT O-GlcNAc transferase: a link between DYT6 and DYT3 dystonias."; RL J. Biol. Chem. 285:13364-13371(2010). RN [12] RP DNA-BINDING. RX PubMed=20010837; DOI=10.1038/nsmb.1742; RA Sabogal A., Lyubimov A.Y., Corn J.E., Berger J.M., Rio D.C.; RT "THAP proteins target specific DNA sites through bipartite recognition of RT adjacent major and minor grooves."; RL Nat. Struct. Mol. Biol. 17:117-123(2010). RN [13] RP REVIEW ON VARIANTS. RX PubMed=21793105; DOI=10.1002/humu.21564; RA Blanchard A., Ea V., Roubertie A., Martin M., Coquart C., Claustres M., RA Beroud C., Collod-Beroud G.; RT "DYT6 dystonia: review of the literature and creation of the UMD Locus- RT Specific Database (LSDB) for mutations in the THAP1 gene."; RL Hum. Mutat. 32:1213-1224(2011). RN [14] RP STRUCTURE BY NMR OF 1-82, AND MUTAGENESIS OF SER-4; CYS-5; SER-6; TYR-8; RP CYS-10; LYS-11; LYS-16; LYS-24; PRO-26; LEU-27; THR-28; ARG-29; PRO-30; RP SER-31; LEU-32; CYS-33; LYS-34; GLU-35; TRP-36; GLU-37; VAL-40; ARG-41; RP ARG-42; LYS-43; ASN-44; PHE-45; LYS-46; PRO-47; THR-48; TYR-50; SER-51; RP SER-52; CYS-54; SER-55; HIS-57; PHE-58 AND PRO-78. RX PubMed=18073205; DOI=10.1074/jbc.m707537200; RA Bessiere D., Lacroix C., Campagne S., Ecochard V., Guillet V., Mourey L., RA Lopez F., Czaplicki J., Demange P., Milon A., Girard J.-P., Gervais V.; RT "Structure-function analysis of the THAP zinc finger of THAP1, a large C2CH RT DNA-binding module linked to Rb/E2F pathways."; RL J. Biol. Chem. 283:4352-4363(2008). RN [15] RP STRUCTURE BY NMR OF 1-82 IN COMPLEX WITH DNA. RX PubMed=20144952; DOI=10.1093/nar/gkq053; RA Campagne S., Saurel O., Gervais V., Milon A.; RT "Structural determinants of specific DNA-recognition by the THAP zinc RT finger."; RL Nucleic Acids Res. 38:3466-3476(2010). RN [16] RP VARIANTS DYT6 LYS-12; THR-21; PRO-29; THR-39; LEU-81 AND ARG-89. RX PubMed=19345147; DOI=10.1016/s1474-4422(09)70081-x; RA Bressman S.B., Raymond D., Fuchs T., Heiman G.A., Ozelius L.J., RA Saunders-Pullman R.; RT "Mutations in THAP1 (DYT6) in early-onset dystonia: a genetic screening RT study."; RL Lancet Neurol. 8:441-446(2009). RN [17] RP VARIANT DYT6 ARG-170. RX PubMed=19908325; DOI=10.1002/mds.22861; RA Bonetti M., Barzaghi C., Brancati F., Ferraris A., Bellacchio E., RA Giovanetti A., Ialongo T., Zorzi G., Piano C., Petracca M., Albanese A., RA Nardocci N., Dallapiccola B., Bentivoglio A.R., Garavaglia B., RA Valente E.M.; RT "Mutation screening of the DYT6/THAP1 gene in Italy."; RL Mov. Disord. 24:2424-2427(2009). RN [18] RP VARIANT DYT6 GLN-29. RX PubMed=19908320; DOI=10.1002/mds.22849; RA Paisan-Ruiz C., Ruiz-Martinez J., Ruibal M., Mok K.Y., Indakoetxea B., RA Gorostidi A., Masso J.F.; RT "Identification of a novel THAP1 mutation at R29 amino-acid residue in RT sporadic patients with early-onset dystonia."; RL Mov. Disord. 24:2428-2429(2009). RN [19] RP VARIANT DYT6 LEU-81, AND DNA-BINDING. RX PubMed=19182804; DOI=10.1038/ng.304; RA Fuchs T., Gavarini S., Saunders-Pullman R., Raymond D., Ehrlich M.E., RA Bressman S.B., Ozelius L.J.; RT "Mutations in the THAP1 gene are responsible for DYT6 primary torsion RT dystonia."; RL Nat. Genet. 41:286-288(2009). RN [20] RP VARIANT DYT6 THR-149. RX PubMed=20629133; DOI=10.1002/mds.23086; RA Van Gerpen J.A., Ledoux M.S., Wszolek Z.K.; RT "Adult-onset leg dystonia due to a missense mutation in THAP1."; RL Mov. Disord. 25:1306-1307(2010). RN [21] RP VARIANTS DYT6 ASN-57; ARG-83; CYS-137; VAL-143 AND ASN-192. RX PubMed=20669277; DOI=10.1002/mds.23207; RA Sohn A.S., Glockle N., Doetzer A.D., Deuschl G., Felbor U., Topka H.R., RA Schols L., Riess O., Bauer P., Muller U., Grundmann K.; RT "Prevalence of THAP1 sequence variants in German patients with primary RT dystonia."; RL Mov. Disord. 25:1982-1986(2010). RN [22] RP VARIANTS DYT6 ILE-59; ASN-69 DEL AND LYS-136. RX PubMed=20687191; DOI=10.1002/mds.23285; RA Groen J.L., Ritz K., Contarino M.F., van de Warrenburg B.P., Aramideh M., RA Foncke E.M., van Hilten J.J., Schuurman P.R., Speelman J.D., Koelman J.H., RA de Bie R.M., Baas F., Tijssen M.A.; RT "DYT6 dystonia: mutation screening, phenotype, and response to deep brain RT stimulation."; RL Mov. Disord. 25:2420-2427(2010). RN [23] RP VARIANTS DYT6 CYS-9; GLY-17; SER-132; THR-149; THR-166 AND LYS-187. RX PubMed=20083799; DOI=10.1212/wnl.0b013e3181ca00ca; RA Xiao J., Zhao Y., Bastian R.W., Perlmutter J.S., Racette B.A., Tabbal S.D., RA Karimi M., Paniello R.C., Wszolek Z.K., Uitti R.J., Van Gerpen J.A., RA Simon D.K., Tarsy D., Hedera P., Truong D.D., Frei K.P., Dev Batish S., RA Blitzer A., Pfeiffer R.F., Gong S., LeDoux M.S.; RT "Novel THAP1 sequence variants in primary dystonia."; RL Neurology 74:229-238(2010). RN [24] RP VARIANTS DYT6 PHE-6; CYS-8; ARG-26; SER-136 AND GLN-169. RX PubMed=20211909; DOI=10.1212/wnl.0b013e3181d5276d; RA Houlden H., Schneider S.A., Paudel R., Melchers A., Schwingenschuh P., RA Edwards M., Hardy J., Bhatia K.P.; RT "THAP1 mutations (DYT6) are an additional cause of early-onset dystonia."; RL Neurology 74:846-850(2010). RN [25] RP VARIANTS DYT6 HIS-13; GLU-16; PRO-23; GLU-24; LEU-26 AND VAL-80, AND RP CHARACTERIZATION OF VARIANTS DYT6 HIS-13; GLU-16; PRO-23; GLU-24; LEU-26 RP AND VAL-80. RX PubMed=21847143; DOI=10.1038/ejhg.2011.159; RA Lohmann K., Uflacker N., Erogullari A., Lohnau T., Winkler S., RA Dendorfer A., Schneider S.A., Osmanovic A., Svetel M., Ferbert A., RA Zittel S., Kuhn A.A., Schmidt A., Altenmuller E., Munchau A., Kamm C., RA Wittstock M., Kupsch A., Moro E., Volkmann J., Kostic V., Kaiser F.J., RA Klein C., Bruggemann N.; RT "Identification and functional analysis of novel THAP1 mutations."; RL Eur. J. Hum. Genet. 20:171-175(2012). RN [26] RP VARIANTS DYT6 ILE-75 AND PRO-150. RX PubMed=20825472; DOI=10.1111/j.1468-1331.2010.03192.x; RA Cheng F.B., Wan X.H., Feng J.C., Wang L., Yang Y.M., Cui L.Y.; RT "Clinical and genetic evaluation of DYT1 and DYT6 primary dystonia in RT China."; RL Eur. J. Neurol. 18:497-503(2011). RN [27] RP VARIANTS DYT6 PHE-54; ILE-75; PRO-150 AND SER-180. RX PubMed=21800139; DOI=10.1007/s00415-011-6196-5; RA Cheng F.B., Ozelius L.J., Wan X.H., Feng J.C., Ma L.Y., Yang Y.M., Wang L.; RT "THAP1/DYT6 sequence variants in non-DYT1 early-onset primary dystonia in RT China and their effects on RNA expression."; RL J. Neurol. 259:342-347(2012). RN [28] RP VARIANT DYT6 GLY-174. RX PubMed=21839475; DOI=10.1016/j.jns.2011.07.023; RA Song W., Chen Y., Huang R., Chen K., Pan P., Yang Y., Shang H.F.; RT "Novel THAP1 gene mutations in patients with primary dystonia from RT Southwest China."; RL J. Neurol. Sci. 309:63-67(2011). RN [29] RP VARIANT DYT6 HIS-32, AND CHARACTERIZATION OF VARIANT DYT6 HIS-32. RX PubMed=21425335; DOI=10.1002/mds.23561; RA Schneider S.A., Ramirez A., Shafiee K., Kaiser F.J., Erogullari A., RA Bruggemann N., Winkler S., Bahman I., Osmanovic A., Shafa M.A., RA Bhatia K.P., Najmabadi H., Klein C., Lohmann K.; RT "Homozygous THAP1 mutations as cause of early-onset generalized dystonia."; RL Mov. Disord. 26:858-861(2011). RN [30] RP VARIANT DYT6 ARG-30. RX PubMed=21425341; DOI=10.1002/mds.23599; RA Jech R., Bares M., Krepelova A., Urgosik D., Havrankova P., Ruzicka E.; RT "DYT 6--a novel THAP1 mutation with excellent effect on pallidal DBS."; RL Mov. Disord. 26:924-925(2011). RN [31] RP VARIANTS DYT6 PRO-6; ASN-69 DEL AND ARG-72. RX PubMed=21110056; DOI=10.1007/s10048-010-0264-3; RA Clot F., Grabli D., Burbaud P., Aya M., Derkinderen P., Defebvre L., RA Damier P., Krystkowiak P., Pollak P., Leguern E., San C., Camuzat A., RA Roze E., Vidailhet M., Durr A., Brice A.; RT "Screening of the THAP1 gene in patients with early-onset dystonia: RT myoclonic jerks are part of the dystonia 6 phenotype."; RL Neurogenetics 12:87-89(2011). RN [32] RP VARIANTS DYT6 ASP-7; GLU-16; CYS-21; GLN-29 AND VAL-80. RX PubMed=22377579; DOI=10.1016/j.parkreldis.2012.02.001; RA Ledoux M.S., Xiao J., Rudzinska M., Bastian R.W., Wszolek Z.K., RA Van Gerpen J.A., Puschmann A., Momcilovic D., Vemula S.R., Zhao Y.; RT "Genotype-phenotype correlations in THAP1 dystonia: Molecular foundations RT and description of new cases."; RL Parkinsonism Relat. Disord. 18:414-425(2012). RN [33] RP VARIANT DYT6 GLY-56. RX PubMed=25385508; DOI=10.3109/00207454.2014.981749; RA Gajos A., Golanska E., Sieruta M., Szybka M., Liberski P.P., Bogucki A.; RT "High variability of clinical symptoms in a Polish family with a novel RT THAP1 mutation."; RL Int. J. Neurosci. 125:755-759(2015). RN [34] RP SUBUNIT, REGION, VARIANTS DYT6 VAL-143; THR-149; PRO-150; THR-166; GLN-169; RP ARG-170; GLY-174; PRO-177 AND SER-180, AND CHARACTERIZATION OF VARIANTS RP DYT6 THR-149; PRO-150; THR-166; GLN-169; ARG-170; GLY-174; PRO-177 AND RP SER-180. RX PubMed=28299530; DOI=10.1007/s12031-017-0904-2; RA Richter A., Hollstein R., Hebert E., Vulinovic F., Eckhold J., RA Osmanovic A., Depping R., Kaiser F.J., Lohmann K.; RT "In-depth Characterization of the Homodimerization Domain of the RT Transcription Factor THAP1 and Dystonia-Causing Mutations Therein."; RL J. Mol. Neurosci. 62:11-16(2017). CC -!- FUNCTION: DNA-binding transcription regulator that regulates CC endothelial cell proliferation and G1/S cell-cycle progression. CC Specifically binds the 5'-[AT]NTNN[GT]GGCA[AGT]-3' core DNA sequence CC and acts by modulating expression of pRB-E2F cell-cycle target genes, CC including RRM1. Component of a THAP1/THAP3-HCFC1-OGT complex that is CC required for the regulation of the transcriptional activity of RRM1. CC May also have pro-apoptotic activity by potentiating both serum- CC withdrawal and TNF-induced apoptosis. {ECO:0000269|PubMed:12717420, CC ECO:0000269|PubMed:17003378, ECO:0000269|PubMed:20200153}. CC -!- SUBUNIT: Homodimer (PubMed:28299530). Interacts with PAWR. Component of CC a THAP1/THAP3-HCFC1-OGT complex that contains, either THAP1 or THAP3, CC HCFC1 and OGT. Interacts with OGT. Interacts (via the HBM) with HCFC1 CC (via the Kelch-repeat domain); the interaction recruits HCFC1 to the CC RRM1 promoter (PubMed:12717420, PubMed:20144952, PubMed:20200153). CC {ECO:0000269|PubMed:12717420, ECO:0000269|PubMed:20144952, CC ECO:0000269|PubMed:20200153, ECO:0000269|PubMed:28299530}. CC -!- INTERACTION: CC Q9NVV9; A0A0S2Z645: ABCF3; NbExp=3; IntAct=EBI-741515, EBI-16432404; CC Q9NVV9; O00154: ACOT7; NbExp=3; IntAct=EBI-741515, EBI-948905; CC Q9NVV9; O00154-4: ACOT7; NbExp=3; IntAct=EBI-741515, EBI-12007918; CC Q9NVV9; Q02040: AKAP17A; NbExp=5; IntAct=EBI-741515, EBI-1042725; CC Q9NVV9; Q02040-3: AKAP17A; NbExp=3; IntAct=EBI-741515, EBI-10222656; CC Q9NVV9; Q99996-2: AKAP9; NbExp=3; IntAct=EBI-741515, EBI-9641546; CC Q9NVV9; P63010: AP2B1; NbExp=4; IntAct=EBI-741515, EBI-432924; CC Q9NVV9; Q66PJ3-3: ARL6IP4; NbExp=3; IntAct=EBI-741515, EBI-10248982; CC Q9NVV9; Q9UL15: BAG5; NbExp=7; IntAct=EBI-741515, EBI-356517; CC Q9NVV9; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-741515, EBI-10181188; CC Q9NVV9; Q13895: BYSL; NbExp=8; IntAct=EBI-741515, EBI-358049; CC Q9NVV9; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-741515, EBI-747505; CC Q9NVV9; Q9BRJ6: C7orf50; NbExp=6; IntAct=EBI-741515, EBI-751612; CC Q9NVV9; Q16543: CDC37; NbExp=3; IntAct=EBI-741515, EBI-295634; CC Q9NVV9; P46527: CDKN1B; NbExp=3; IntAct=EBI-741515, EBI-519280; CC Q9NVV9; P55273: CDKN2D; NbExp=3; IntAct=EBI-741515, EBI-745859; CC Q9NVV9; O14647: CHD2; NbExp=3; IntAct=EBI-741515, EBI-1210503; CC Q9NVV9; P68400: CSNK2A1; NbExp=7; IntAct=EBI-741515, EBI-347804; CC Q9NVV9; Q5TAQ9: DCAF8; NbExp=3; IntAct=EBI-741515, EBI-740686; CC Q9NVV9; Q86V42: FAM124A; NbExp=3; IntAct=EBI-741515, EBI-744506; CC Q9NVV9; Q8N9E0: FAM133A; NbExp=6; IntAct=EBI-741515, EBI-10268158; CC Q9NVV9; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-741515, EBI-8468186; CC Q9NVV9; O15520: FGF10; NbExp=3; IntAct=EBI-741515, EBI-1035684; CC Q9NVV9; Q92914: FGF11; NbExp=3; IntAct=EBI-741515, EBI-11987787; CC Q9NVV9; P61328-2: FGF12; NbExp=3; IntAct=EBI-741515, EBI-10699759; CC Q9NVV9; O95995: GAS8; NbExp=3; IntAct=EBI-741515, EBI-1052570; CC Q9NVV9; P14136: GFAP; NbExp=3; IntAct=EBI-741515, EBI-744302; CC Q9NVV9; Q9NWQ4: GPATCH2L; NbExp=3; IntAct=EBI-741515, EBI-5666657; CC Q9NVV9; Q9NWQ4-1: GPATCH2L; NbExp=5; IntAct=EBI-741515, EBI-11959863; CC Q9NVV9; P51610: HCFC1; NbExp=6; IntAct=EBI-741515, EBI-396176; CC Q9NVV9; A0A024RA76: hCG_1744368; NbExp=3; IntAct=EBI-741515, EBI-10180729; CC Q9NVV9; A0A024R5S0: hCG_2003792; NbExp=6; IntAct=EBI-741515, EBI-10188461; CC Q9NVV9; Q8WVV9: HNRNPLL; NbExp=3; IntAct=EBI-741515, EBI-535849; CC Q9NVV9; Q9C086: INO80B; NbExp=3; IntAct=EBI-741515, EBI-715611; CC Q9NVV9; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-741515, EBI-2556193; CC Q9NVV9; Q9Y4X4: KLF12; NbExp=3; IntAct=EBI-741515, EBI-750750; CC Q9NVV9; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-741515, EBI-10172290; CC Q9NVV9; Q969R5: L3MBTL2; NbExp=3; IntAct=EBI-741515, EBI-739909; CC Q9NVV9; Q14847: LASP1; NbExp=3; IntAct=EBI-741515, EBI-742828; CC Q9NVV9; Q03252: LMNB2; NbExp=3; IntAct=EBI-741515, EBI-2830427; CC Q9NVV9; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-741515, EBI-11742507; CC Q9NVV9; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-741515, EBI-739832; CC Q9NVV9; Q8N6R0: METTL13; NbExp=4; IntAct=EBI-741515, EBI-1053295; CC Q9NVV9; P55081: MFAP1; NbExp=3; IntAct=EBI-741515, EBI-1048159; CC Q9NVV9; Q9NYP9: MIS18A; NbExp=3; IntAct=EBI-741515, EBI-1104552; CC Q9NVV9; Q9BU76: MMTAG2; NbExp=9; IntAct=EBI-741515, EBI-742459; CC Q9NVV9; Q9UBU8: MORF4L1; NbExp=3; IntAct=EBI-741515, EBI-399246; CC Q9NVV9; Q15014: MORF4L2; NbExp=3; IntAct=EBI-741515, EBI-399257; CC Q9NVV9; Q9Y3B7: MRPL11; NbExp=4; IntAct=EBI-741515, EBI-5453723; CC Q9NVV9; Q96EL3: MRPL53; NbExp=3; IntAct=EBI-741515, EBI-2513715; CC Q9NVV9; O14561: NDUFAB1; NbExp=3; IntAct=EBI-741515, EBI-1246261; CC Q9NVV9; P19404: NDUFV2; NbExp=3; IntAct=EBI-741515, EBI-713665; CC Q9NVV9; Q6ZUT1: NKAPD1; NbExp=6; IntAct=EBI-741515, EBI-3920396; CC Q9NVV9; Q6ZUT1-2: NKAPD1; NbExp=3; IntAct=EBI-741515, EBI-10180231; CC Q9NVV9; P29474: NOS3; NbExp=3; IntAct=EBI-741515, EBI-1391623; CC Q9NVV9; Q96HA8: NTAQ1; NbExp=8; IntAct=EBI-741515, EBI-741158; CC Q9NVV9; P37198: NUP62; NbExp=12; IntAct=EBI-741515, EBI-347978; CC Q9NVV9; O43189: PHF1; NbExp=4; IntAct=EBI-741515, EBI-530034; CC Q9NVV9; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-741515, EBI-2339674; CC Q9NVV9; Q7Z2X4: PID1; NbExp=3; IntAct=EBI-741515, EBI-10256685; CC Q9NVV9; D3DTS7: PMP22; NbExp=3; IntAct=EBI-741515, EBI-25882629; CC Q9NVV9; Q96T60: PNKP; NbExp=3; IntAct=EBI-741515, EBI-1045072; CC Q9NVV9; P62875: POLR2L; NbExp=3; IntAct=EBI-741515, EBI-359527; CC Q9NVV9; P78424: POU6F2; NbExp=3; IntAct=EBI-741515, EBI-12029004; CC Q9NVV9; Q13427: PPIG; NbExp=3; IntAct=EBI-741515, EBI-396072; CC Q9NVV9; Q13131: PRKAA1; NbExp=3; IntAct=EBI-741515, EBI-1181405; CC Q9NVV9; P86479: PRR20C; NbExp=3; IntAct=EBI-741515, EBI-10172814; CC Q9NVV9; P86480: PRR20D; NbExp=3; IntAct=EBI-741515, EBI-12754095; CC Q9NVV9; Q9Y4B4: RAD54L2; NbExp=3; IntAct=EBI-741515, EBI-948156; CC Q9NVV9; Q53GL6: RALY; NbExp=3; IntAct=EBI-741515, EBI-9512693; CC Q9NVV9; Q86SE5: RALYL; NbExp=4; IntAct=EBI-741515, EBI-741520; CC Q9NVV9; Q86SE5-3: RALYL; NbExp=6; IntAct=EBI-741515, EBI-11526555; CC Q9NVV9; P98175: RBM10; NbExp=6; IntAct=EBI-741515, EBI-721525; CC Q9NVV9; Q14498: RBM39; NbExp=6; IntAct=EBI-741515, EBI-395290; CC Q9NVV9; Q0D2K3: RIPPLY1; NbExp=6; IntAct=EBI-741515, EBI-10226430; CC Q9NVV9; P78317: RNF4; NbExp=3; IntAct=EBI-741515, EBI-2340927; CC Q9NVV9; P35268: RPL22; NbExp=3; IntAct=EBI-741515, EBI-354533; CC Q9NVV9; P62851: RPS25; NbExp=3; IntAct=EBI-741515, EBI-353054; CC Q9NVV9; Q9UHR5: SAP30BP; NbExp=3; IntAct=EBI-741515, EBI-751683; CC Q9NVV9; O95391: SLU7; NbExp=3; IntAct=EBI-741515, EBI-750559; CC Q9NVV9; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-741515, EBI-12023934; CC Q9NVV9; Q96LM5: SPMIP2; NbExp=3; IntAct=EBI-741515, EBI-12020542; CC Q9NVV9; Q8N9Q2: SREK1IP1; NbExp=3; IntAct=EBI-741515, EBI-10268630; CC Q9NVV9; Q96SI9: STRBP; NbExp=7; IntAct=EBI-741515, EBI-740355; CC Q9NVV9; Q15560: TCEA2; NbExp=6; IntAct=EBI-741515, EBI-710310; CC Q9NVV9; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-741515, EBI-11955057; CC Q9NVV9; Q9NVV9: THAP1; NbExp=9; IntAct=EBI-741515, EBI-741515; CC Q9NVV9; P06753: TPM3; NbExp=6; IntAct=EBI-741515, EBI-355607; CC Q9NVV9; Q5VU62: TPM3; NbExp=3; IntAct=EBI-741515, EBI-10184033; CC Q9NVV9; O00463: TRAF5; NbExp=6; IntAct=EBI-741515, EBI-523498; CC Q9NVV9; Q12899: TRIM26; NbExp=6; IntAct=EBI-741515, EBI-2341136; CC Q9NVV9; Q15642-2: TRIP10; NbExp=3; IntAct=EBI-741515, EBI-6550597; CC Q9NVV9; Q6ZVT0: TTLL10; NbExp=3; IntAct=EBI-741515, EBI-7844656; CC Q9NVV9; P26368: U2AF2; NbExp=4; IntAct=EBI-741515, EBI-742339; CC Q9NVV9; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-741515, EBI-10180829; CC Q9NVV9; Q3SXR9: VCX2; NbExp=3; IntAct=EBI-741515, EBI-11983741; CC Q9NVV9; P07947: YES1; NbExp=6; IntAct=EBI-741515, EBI-515331; CC Q9NVV9; P10074: ZBTB48; NbExp=3; IntAct=EBI-741515, EBI-744864; CC Q9NVV9; Q8TBK6: ZCCHC10; NbExp=10; IntAct=EBI-741515, EBI-597063; CC Q9NVV9; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-741515, EBI-10183064; CC Q9NVV9; Q66K41: ZNF385C; NbExp=4; IntAct=EBI-741515, EBI-8651919; CC Q9NVV9; Q66K41-2: ZNF385C; NbExp=3; IntAct=EBI-741515, EBI-12055653; CC Q9NVV9; Q9H9D4: ZNF408; NbExp=4; IntAct=EBI-741515, EBI-347633; CC Q9NVV9; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-741515, EBI-11035148; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm CC {ECO:0000269|PubMed:12717420}. Nucleus, PML body CC {ECO:0000269|PubMed:12717420}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NVV9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NVV9-2; Sequence=VSP_044665, VSP_044666; CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, kidney CC and liver. Weaker expression in brain and placenta. CC {ECO:0000269|PubMed:20200153}. CC -!- DISEASE: Dystonia 6, torsion (DYT6) [MIM:602629]: A primary torsion CC dystonia. Dystonia is defined by the presence of sustained involuntary CC muscle contractions, often leading to abnormal postures. Dystonia type CC 6 is characterized by onset in early adulthood, cranial or cervical CC involvement in about half of the cases, and frequent progression to CC involve multiple body regions. {ECO:0000269|PubMed:19182804, CC ECO:0000269|PubMed:19345147, ECO:0000269|PubMed:19908320, CC ECO:0000269|PubMed:19908325, ECO:0000269|PubMed:20083799, CC ECO:0000269|PubMed:20211909, ECO:0000269|PubMed:20629133, CC ECO:0000269|PubMed:20669277, ECO:0000269|PubMed:20687191, CC ECO:0000269|PubMed:20825472, ECO:0000269|PubMed:21110056, CC ECO:0000269|PubMed:21425335, ECO:0000269|PubMed:21425341, CC ECO:0000269|PubMed:21800139, ECO:0000269|PubMed:21839475, CC ECO:0000269|PubMed:21847143, ECO:0000269|PubMed:22377579, CC ECO:0000269|PubMed:25385508, ECO:0000269|PubMed:28299530, CC ECO:0000269|Ref.3}. Note=The disease is caused by variants affecting CC the gene represented in this entry. CC -!- SIMILARITY: Belongs to the THAP1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK001339; BAA91635.1; -; mRNA. DR EMBL; CR457256; CAG33537.1; -; mRNA. DR EMBL; AK223231; BAD96951.1; -; mRNA. DR EMBL; AL832077; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC087533; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471080; EAW63205.1; -; Genomic_DNA. DR EMBL; CH471080; EAW63206.1; -; Genomic_DNA. DR EMBL; BC021721; AAH21721.1; -; mRNA. DR CCDS; CCDS6136.1; -. [Q9NVV9-1] DR CCDS; CCDS6137.1; -. [Q9NVV9-2] DR RefSeq; NP_060575.1; NM_018105.2. [Q9NVV9-1] DR RefSeq; NP_945354.1; NM_199003.1. [Q9NVV9-2] DR PDB; 2JTG; NMR; -; A=1-81. DR PDB; 2KO0; NMR; -; A=1-82. DR PDB; 2L1G; NMR; -; A=1-82. DR PDBsum; 2JTG; -. DR PDBsum; 2KO0; -. DR PDBsum; 2L1G; -. DR AlphaFoldDB; Q9NVV9; -. DR BMRB; Q9NVV9; -. DR SMR; Q9NVV9; -. DR BioGRID; 120448; 128. DR ELM; Q9NVV9; -. DR IntAct; Q9NVV9; 110. DR MINT; Q9NVV9; -. DR STRING; 9606.ENSP00000254250; -. DR DrugCentral; Q9NVV9; -. DR iPTMnet; Q9NVV9; -. DR PhosphoSitePlus; Q9NVV9; -. DR BioMuta; THAP1; -. DR DMDM; 29839656; -. DR EPD; Q9NVV9; -. DR MassIVE; Q9NVV9; -. DR MaxQB; Q9NVV9; -. DR PaxDb; 9606-ENSP00000254250; -. DR PeptideAtlas; Q9NVV9; -. DR ProteomicsDB; 46208; -. DR ProteomicsDB; 82871; -. [Q9NVV9-1] DR ABCD; Q9NVV9; 1 sequenced antibody. DR Antibodypedia; 24159; 161 antibodies from 27 providers. DR DNASU; 55145; -. DR Ensembl; ENST00000254250.7; ENSP00000254250.3; ENSG00000131931.8. [Q9NVV9-1] DR Ensembl; ENST00000345117.2; ENSP00000344966.2; ENSG00000131931.8. [Q9NVV9-2] DR GeneID; 55145; -. DR KEGG; hsa:55145; -. DR MANE-Select; ENST00000254250.7; ENSP00000254250.3; NM_018105.3; NP_060575.1. DR UCSC; uc003xpk.4; human. [Q9NVV9-1] DR AGR; HGNC:20856; -. DR CTD; 55145; -. DR DisGeNET; 55145; -. DR GeneCards; THAP1; -. DR HGNC; HGNC:20856; THAP1. DR HPA; ENSG00000131931; Low tissue specificity. DR MalaCards; THAP1; -. DR MIM; 602629; phenotype. DR MIM; 609520; gene. DR neXtProt; NX_Q9NVV9; -. DR OpenTargets; ENSG00000131931; -. DR Orphanet; 98806; Primary dystonia, DYT6 type. DR PharmGKB; PA134920361; -. DR VEuPathDB; HostDB:ENSG00000131931; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000159383; -. DR HOGENOM; CLU_076186_2_1_1; -. DR InParanoid; Q9NVV9; -. DR OMA; KDCFKRE; -. DR OrthoDB; 5356539at2759; -. DR PhylomeDB; Q9NVV9; -. DR TreeFam; TF330127; -. DR PathwayCommons; Q9NVV9; -. DR SignaLink; Q9NVV9; -. DR BioGRID-ORCS; 55145; 694 hits in 1187 CRISPR screens. DR ChiTaRS; THAP1; human. DR EvolutionaryTrace; Q9NVV9; -. DR GeneWiki; THAP1; -. DR GenomeRNAi; 55145; -. DR Pharos; Q9NVV9; Tbio. DR PRO; PR:Q9NVV9; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q9NVV9; Protein. DR Bgee; ENSG00000131931; Expressed in secondary oocyte and 178 other cell types or tissues. DR ExpressionAtlas; Q9NVV9; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0006351; P:DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0001935; P:endothelial cell proliferation; IMP:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR Gene3D; 6.20.210.20; THAP domain; 1. DR InterPro; IPR026516; THAP1/10. DR InterPro; IPR006612; THAP_Znf. DR InterPro; IPR038441; THAP_Znf_sf. DR PANTHER; PTHR46600; THAP DOMAIN-CONTAINING; 1. DR PANTHER; PTHR46600:SF5; THAP DOMAIN-CONTAINING PROTEIN 1; 1. DR Pfam; PF05485; THAP; 1. DR SMART; SM00692; DM3; 1. DR SMART; SM00980; THAP; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR PROSITE; PS50950; ZF_THAP; 1. DR Genevisible; Q9NVV9; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell cycle; Coiled coil; KW Disease variant; DNA-binding; Dystonia; Metal-binding; Nucleus; KW Reference proteome; Transcription; Transcription regulation; Zinc; KW Zinc-finger. FT CHAIN 1..213 FT /note="THAP domain-containing protein 1" FT /id="PRO_0000068637" FT ZN_FING 1..81 FT /note="THAP-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00309" FT REGION 139..185 FT /note="Involved in homodimer formation" FT /evidence="ECO:0000269|PubMed:28299530" FT COILED 139..190 FT /evidence="ECO:0000255" FT MOTIF 134..137 FT /note="HCFC1-binding motif (HBM)" FT VAR_SEQ 25..53 FT /note="FPLTRPSLCKEWEAAVRRKNFKPTKYSSI -> KKIFWSHRNSFPHLLYRLL FT FPRLMLLLDY (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_044665" FT VAR_SEQ 54..213 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_044666" FT VARIANT 6 FT /note="S -> F (in DYT6)" FT /evidence="ECO:0000269|PubMed:20211909" FT /id="VAR_066677" FT VARIANT 6 FT /note="S -> P (in DYT6; dbSNP:rs1586459410)" FT /evidence="ECO:0000269|PubMed:21110056" FT /id="VAR_066678" FT VARIANT 7 FT /note="A -> D (in DYT6)" FT /evidence="ECO:0000269|PubMed:22377579" FT /id="VAR_067356" FT VARIANT 8 FT /note="Y -> C (in DYT6)" FT /evidence="ECO:0000269|PubMed:20211909" FT /id="VAR_066679" FT VARIANT 9 FT /note="G -> C (in DYT6; dbSNP:rs267607112)" FT /evidence="ECO:0000269|PubMed:20083799" FT /id="VAR_066680" FT VARIANT 12 FT /note="N -> K (in DYT6)" FT /evidence="ECO:0000269|PubMed:19345147" FT /id="VAR_065880" FT VARIANT 13 FT /note="R -> H (in DYT6)" FT /evidence="ECO:0000269|PubMed:21847143" FT /id="VAR_066681" FT VARIANT 16 FT /note="K -> E (in DYT6; lower activity than wild-type)" FT /evidence="ECO:0000269|PubMed:21847143, FT ECO:0000269|PubMed:22377579" FT /id="VAR_066682" FT VARIANT 17 FT /note="D -> G (in DYT6; dbSNP:rs766483829)" FT /evidence="ECO:0000269|PubMed:20083799" FT /id="VAR_066683" FT VARIANT 21 FT /note="S -> C (in DYT6)" FT /evidence="ECO:0000269|PubMed:22377579" FT /id="VAR_067357" FT VARIANT 21 FT /note="S -> T (in DYT6)" FT /evidence="ECO:0000269|PubMed:19345147" FT /id="VAR_065881" FT VARIANT 23 FT /note="H -> P (in DYT6; lower activity than wild-type; FT dbSNP:rs387907177)" FT /evidence="ECO:0000269|PubMed:21847143" FT /id="VAR_066684" FT VARIANT 24 FT /note="K -> E (in DYT6; lower activity than wild-type; FT dbSNP:rs387907176)" FT /evidence="ECO:0000269|PubMed:21847143" FT /id="VAR_066685" FT VARIANT 26 FT /note="P -> L (in DYT6; lower activity than wild-type; FT dbSNP:rs1802674870)" FT /evidence="ECO:0000269|PubMed:21847143" FT /id="VAR_066686" FT VARIANT 26 FT /note="P -> R (in DYT6)" FT /evidence="ECO:0000269|PubMed:20211909" FT /id="VAR_066687" FT VARIANT 29 FT /note="R -> P (in DYT6)" FT /evidence="ECO:0000269|PubMed:19345147" FT /id="VAR_065882" FT VARIANT 29 FT /note="R -> Q (in DYT6; dbSNP:rs767952378)" FT /evidence="ECO:0000269|PubMed:19908320, FT ECO:0000269|PubMed:22377579" FT /id="VAR_066688" FT VARIANT 30 FT /note="P -> R (in DYT6)" FT /evidence="ECO:0000269|PubMed:21425341" FT /id="VAR_066689" FT VARIANT 32 FT /note="L -> H (in DYT6; lower activity than wild-type)" FT /evidence="ECO:0000269|PubMed:21425335" FT /id="VAR_066690" FT VARIANT 39 FT /note="A -> T (in DYT6)" FT /evidence="ECO:0000269|PubMed:19345147" FT /id="VAR_065883" FT VARIANT 54 FT /note="C -> F (in DYT6)" FT /evidence="ECO:0000269|PubMed:21800139" FT /id="VAR_066691" FT VARIANT 56 FT /note="E -> G (in DYT6)" FT /evidence="ECO:0000269|PubMed:25385508" FT /id="VAR_072272" FT VARIANT 57 FT /note="H -> N (in DYT6)" FT /evidence="ECO:0000269|PubMed:20669277" FT /id="VAR_066692" FT VARIANT 59 FT /note="T -> I (in DYT6)" FT /evidence="ECO:0000269|PubMed:20687191" FT /id="VAR_065884" FT VARIANT 69 FT /note="Missing (in DYT6)" FT /evidence="ECO:0000269|PubMed:20687191, FT ECO:0000269|PubMed:21110056" FT /id="VAR_066693" FT VARIANT 72 FT /note="L -> R (in DYT6)" FT /evidence="ECO:0000269|PubMed:21110056" FT /id="VAR_066694" FT VARIANT 75 FT /note="N -> I (in DYT6)" FT /evidence="ECO:0000269|PubMed:20825472, FT ECO:0000269|PubMed:21800139" FT /id="VAR_066695" FT VARIANT 80 FT /note="I -> V (in DYT6; mild phenotype; does not affect FT activity; dbSNP:rs372080941)" FT /evidence="ECO:0000269|PubMed:21847143, FT ECO:0000269|PubMed:22377579" FT /id="VAR_066696" FT VARIANT 81 FT /note="F -> L (in DYT6; affects DNA-binding; FT dbSNP:rs118204013)" FT /evidence="ECO:0000269|PubMed:19182804, FT ECO:0000269|PubMed:19345147" FT /id="VAR_054788" FT VARIANT 83 FT /note="C -> R (in DYT6; dbSNP:rs768017019)" FT /evidence="ECO:0000269|PubMed:20669277" FT /id="VAR_066697" FT VARIANT 89 FT /note="K -> R (in DYT6; dbSNP:rs267607111)" FT /evidence="ECO:0000269|PubMed:19345147, ECO:0000269|Ref.3" FT /id="VAR_065885" FT VARIANT 132 FT /note="F -> S (in DYT6; dbSNP:rs950435041)" FT /evidence="ECO:0000269|PubMed:20083799" FT /id="VAR_066698" FT VARIANT 136 FT /note="N -> K (in DYT6)" FT /evidence="ECO:0000269|PubMed:20687191" FT /id="VAR_065886" FT VARIANT 136 FT /note="N -> S (in DYT6; dbSNP:rs769988455)" FT /evidence="ECO:0000269|PubMed:20211909" FT /id="VAR_066699" FT VARIANT 137 FT /note="Y -> C (in DYT6)" FT /evidence="ECO:0000269|PubMed:20669277" FT /id="VAR_066700" FT VARIANT 143 FT /note="M -> V (in DYT6; no effect on dimerization; FT dbSNP:rs374512193)" FT /evidence="ECO:0000269|PubMed:20669277, FT ECO:0000269|PubMed:28299530" FT /id="VAR_066701" FT VARIANT 149 FT /note="I -> T (in DYT6; no effect on dimerization)" FT /evidence="ECO:0000269|PubMed:20083799, FT ECO:0000269|PubMed:20629133, ECO:0000269|PubMed:28299530" FT /id="VAR_066702" FT VARIANT 150 FT /note="H -> P (in DYT6; no effect on dimerization)" FT /evidence="ECO:0000269|PubMed:20825472, FT ECO:0000269|PubMed:21800139, ECO:0000269|PubMed:28299530" FT /id="VAR_066703" FT VARIANT 166 FT /note="A -> T (in DYT6; no effect on dimerization; FT dbSNP:rs138918468)" FT /evidence="ECO:0000269|PubMed:20083799, FT ECO:0000269|PubMed:28299530" FT /id="VAR_066704" FT VARIANT 169 FT /note="R -> Q (in DYT6; no effect on dimerization; FT dbSNP:rs767519301)" FT /evidence="ECO:0000269|PubMed:20211909, FT ECO:0000269|PubMed:28299530" FT /id="VAR_066705" FT VARIANT 170 FT /note="C -> R (in DYT6; no effect on dimerization)" FT /evidence="ECO:0000269|PubMed:19908325, FT ECO:0000269|PubMed:28299530" FT /id="VAR_065887" FT VARIANT 174 FT /note="E -> G (in DYT6; no effect on dimerization; FT dbSNP:rs759392096)" FT /evidence="ECO:0000269|PubMed:21839475, FT ECO:0000269|PubMed:28299530" FT /id="VAR_066706" FT VARIANT 177 FT /note="L -> P (in DYT6; no effect on dimerization)" FT /evidence="ECO:0000269|PubMed:28299530" FT /id="VAR_079366" FT VARIANT 180 FT /note="L -> S (in DYT6; no effect on dimerization)" FT /evidence="ECO:0000269|PubMed:21800139, FT ECO:0000269|PubMed:28299530" FT /id="VAR_066707" FT VARIANT 187 FT /note="Q -> K (in DYT6)" FT /evidence="ECO:0000269|PubMed:20083799" FT /id="VAR_066708" FT VARIANT 192 FT /note="D -> N (in DYT6; dbSNP:rs377725442)" FT /evidence="ECO:0000269|PubMed:20669277" FT /id="VAR_066709" FT MUTAGEN 4 FT /note="S->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 5 FT /note="C->A: Abolishes DNA- and zinc-binding." FT /evidence="ECO:0000269|PubMed:15863623, FT ECO:0000269|PubMed:18073205" FT MUTAGEN 6 FT /note="S->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 8 FT /note="Y->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 10 FT /note="C->A: Abolishes DNA- and zinc-binding." FT /evidence="ECO:0000269|PubMed:15863623, FT ECO:0000269|PubMed:18073205" FT MUTAGEN 11 FT /note="K->A: Partially affects DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 16 FT /note="K->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 24 FT /note="K->A: Strongly affects DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 26 FT /note="P->A: Abolishes DNA- and zinc-binding." FT /evidence="ECO:0000269|PubMed:15863623, FT ECO:0000269|PubMed:18073205" FT MUTAGEN 27 FT /note="L->A: Partially affects DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 28..30 FT /note="TRP->AAA: Strongly affects DNA-binding." FT MUTAGEN 28 FT /note="T->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 29 FT /note="R->A: Strongly affects DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 30 FT /note="P->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 31 FT /note="S->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 32 FT /note="L->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 33 FT /note="C->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 34 FT /note="K->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 35 FT /note="E->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 36 FT /note="W->A: Abolishes DNA- and zinc-binding." FT /evidence="ECO:0000269|PubMed:15863623, FT ECO:0000269|PubMed:18073205" FT MUTAGEN 37 FT /note="E->A: Partially affects DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 40 FT /note="V->A: Partially affects DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 41..43 FT /note="RRK->AAA: Strongly affects DNA-binding." FT MUTAGEN 41 FT /note="R->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 42 FT /note="R->A: Strongly affects DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 43 FT /note="K->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 44 FT /note="N->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 45 FT /note="F->A: Strongly affects DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 46 FT /note="K->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 47..49 FT /note="PTK->AAA: Strongly affects DNA-binding." FT MUTAGEN 47 FT /note="P->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 48 FT /note="T->A: Strongly affects DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 49 FT /note="K->A: Does not affect DNA-binding." FT MUTAGEN 50..52 FT /note="YSS->AAA: Strongly affects DNA-binding." FT MUTAGEN 50 FT /note="Y->A: Partially affects DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 51 FT /note="S->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 52 FT /note="S->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 54 FT /note="C->A: Abolishes DNA- and zinc-binding." FT /evidence="ECO:0000269|PubMed:15863623, FT ECO:0000269|PubMed:18073205" FT MUTAGEN 55 FT /note="S->A: Does not affect DNA-binding." FT /evidence="ECO:0000269|PubMed:18073205" FT MUTAGEN 57 FT /note="H->A: Abolishes DNA- and zinc-binding." FT /evidence="ECO:0000269|PubMed:15863623, FT ECO:0000269|PubMed:18073205" FT MUTAGEN 58 FT /note="F->A: Abolishes DNA- and zinc-binding." FT /evidence="ECO:0000269|PubMed:15863623, FT ECO:0000269|PubMed:18073205" FT MUTAGEN 78 FT /note="P->A: Abolishes DNA- and zinc-binding." FT /evidence="ECO:0000269|PubMed:15863623, FT ECO:0000269|PubMed:18073205" FT CONFLICT 171 FT /note="R -> G (in Ref. 2; CAG33537)" FT /evidence="ECO:0000305" FT CONFLICT 213 FT /note="A -> T (in Ref. 3; BAD96951)" FT /evidence="ECO:0000305" FT STRAND 6..9 FT /evidence="ECO:0007829|PDB:2KO0" FT STRAND 16..18 FT /evidence="ECO:0007829|PDB:2JTG" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:2JTG" FT HELIX 33..40 FT /evidence="ECO:0007829|PDB:2JTG" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:2KO0" FT TURN 47..49 FT /evidence="ECO:0007829|PDB:2JTG" FT STRAND 51..54 FT /evidence="ECO:0007829|PDB:2JTG" FT HELIX 55..57 FT /evidence="ECO:0007829|PDB:2JTG" FT HELIX 60..63 FT /evidence="ECO:0007829|PDB:2JTG" FT STRAND 67..71 FT /evidence="ECO:0007829|PDB:2KO0" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:2JTG" SQ SEQUENCE 213 AA; 24944 MW; F3769B0F4CC56539 CRC64; MVQSCSAYGC KNRYDKDKPV SFHKFPLTRP SLCKEWEAAV RRKNFKPTKY SSICSEHFTP DCFKRECNNK LLKENAVPTI FLCTEPHDKK EDLLEPQEQL PPPPLPPPVS QVDAAIGLLM PPLQTPVNLS VFCDHNYTVE DTMHQRKRIH QLEQQVEKLR KKLKTAQQRC RRQERQLEKL KEVVHFQKEK DDVSERGYVI LPNDYFEIVE VPA //