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THAP domain-containing protein 1

 THAP1_HUMAN             Reviewed;         213 AA.
Q9NVV9; A6NCB6; D3DSY5; H9KV49; Q53FQ1; Q6IA99;
11-APR-2003, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 141.
RecName: Full=THAP domain-containing protein 1;
Name=THAP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT DYT6
ARG-89.
TISSUE=Gastric mucosa;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Adipocyte;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PAWR.
PubMed=12717420; DOI=10.1038/sj.onc.1206271;
Roussigne M., Cayrol C., Clouaire T., Amalric F., Girard J.-P.;
"THAP1 is a nuclear proapoptotic factor that links prostate-apoptosis-
response-4 (Par-4) to PML nuclear bodies.";
Oncogene 22:2432-2442(2003).
[9]
DNA-BINDING, ZINC-BINDING, AND MUTAGENESIS OF CYS-5; CYS-10; PRO-26;
TRP-36; CYS-54; HIS-57; PHE-58 AND PRO-78.
PubMed=15863623; DOI=10.1073/pnas.0406882102;
Clouaire T., Roussigne M., Ecochard V., Mathe C., Amalric F.,
Girard J.-P.;
"The THAP domain of THAP1 is a large C2CH module with zinc-dependent
sequence-specific DNA-binding activity.";
Proc. Natl. Acad. Sci. U.S.A. 102:6907-6912(2005).
[10]
FUNCTION, AND DNA-BINDING.
PubMed=17003378; DOI=10.1182/blood-2006-03-012013;
Cayrol C., Lacroix C., Mathe C., Ecochard V., Ceribelli M., Loreau E.,
Lazar V., Dessen P., Mantovani R., Aguilar L., Girard J.-P.;
"The THAP-zinc finger protein THAP1 regulates endothelial cell
proliferation through modulation of pRB/E2F cell-cycle target genes.";
Blood 109:584-594(2007).
[11]
IDENTIFICATION BY MASS SPECTROMETRY IN A THAP1/THAP3-HCFC1-OGT
COMPLEX, INTERACTION WITH HCFC1 AND OGT, TISSUE SPECIFICITY, AND
FUNCTION.
PubMed=20200153; DOI=10.1074/jbc.M109.072579;
Mazars R., Gonzalez-de-Peredo A., Cayrol C., Lavigne A.C., Vogel J.L.,
Ortega N., Lacroix C., Gautier V., Huet G., Ray A., Monsarrat B.,
Kristie T.M., Girard J.P.;
"The THAP-zinc finger protein THAP1 associates with coactivator HCF-1
and O-GlcNAc transferase: a link between DYT6 and DYT3 dystonias.";
J. Biol. Chem. 285:13364-13371(2010).
[12]
DNA-BINDING.
PubMed=20010837; DOI=10.1038/nsmb.1742;
Sabogal A., Lyubimov A.Y., Corn J.E., Berger J.M., Rio D.C.;
"THAP proteins target specific DNA sites through bipartite recognition
of adjacent major and minor grooves.";
Nat. Struct. Mol. Biol. 17:117-123(2010).
[13]
REVIEW ON VARIANTS.
PubMed=21793105; DOI=10.1002/humu.21564;
Blanchard A., Ea V., Roubertie A., Martin M., Coquart C.,
Claustres M., Beroud C., Collod-Beroud G.;
"DYT6 dystonia: review of the literature and creation of the UMD
Locus-Specific Database (LSDB) for mutations in the THAP1 gene.";
Hum. Mutat. 32:1213-1224(2011).
[14]
STRUCTURE BY NMR OF 1-82, AND MUTAGENESIS OF SER-4; CYS-5; SER-6;
TYR-8; CYS-10; LYS-11; LYS-16; LYS-24; PRO-26; LEU-27; THR-28; ARG-29;
PRO-30; SER-31; LEU-32; CYS-33; LYS-34; GLU-35; TRP-36; GLU-37;
VAL-40; ARG-41; ARG-42; LYS-43; ASN-44; PHE-45; LYS-46; PRO-47;
THR-48; TYR-50; SER-51; SER-52; CYS-54; SER-55; HIS-57; PHE-58 AND
PRO-78.
PubMed=18073205; DOI=10.1074/jbc.M707537200;
Bessiere D., Lacroix C., Campagne S., Ecochard V., Guillet V.,
Mourey L., Lopez F., Czaplicki J., Demange P., Milon A., Girard J.-P.,
Gervais V.;
"Structure-function analysis of the THAP zinc finger of THAP1, a large
C2CH DNA-binding module linked to Rb/E2F pathways.";
J. Biol. Chem. 283:4352-4363(2008).
[15]
STRUCTURE BY NMR OF 1-82 IN COMPLEX WITH DNA.
PubMed=20144952; DOI=10.1093/nar/gkq053;
Campagne S., Saurel O., Gervais V., Milon A.;
"Structural determinants of specific DNA-recognition by the THAP zinc
finger.";
Nucleic Acids Res. 38:3466-3476(2010).
[16]
VARIANTS DYT6 LYS-12; THR-21; PRO-29; THR-39; LEU-81 AND ARG-89.
PubMed=19345147; DOI=10.1016/S1474-4422(09)70081-X;
Bressman S.B., Raymond D., Fuchs T., Heiman G.A., Ozelius L.J.,
Saunders-Pullman R.;
"Mutations in THAP1 (DYT6) in early-onset dystonia: a genetic
screening study.";
Lancet Neurol. 8:441-446(2009).
[17]
VARIANT DYT6 ARG-170.
PubMed=19908325; DOI=10.1002/mds.22861;
Bonetti M., Barzaghi C., Brancati F., Ferraris A., Bellacchio E.,
Giovanetti A., Ialongo T., Zorzi G., Piano C., Petracca M.,
Albanese A., Nardocci N., Dallapiccola B., Bentivoglio A.R.,
Garavaglia B., Valente E.M.;
"Mutation screening of the DYT6/THAP1 gene in Italy.";
Mov. Disord. 24:2424-2427(2009).
[18]
VARIANT DYT6 GLN-29.
PubMed=19908320; DOI=10.1002/mds.22849;
Paisan-Ruiz C., Ruiz-Martinez J., Ruibal M., Mok K.Y., Indakoetxea B.,
Gorostidi A., Masso J.F.;
"Identification of a novel THAP1 mutation at R29 amino-acid residue in
sporadic patients with early-onset dystonia.";
Mov. Disord. 24:2428-2429(2009).
[19]
VARIANT DYT6 LEU-81, AND DNA-BINDING.
PubMed=19182804; DOI=10.1038/ng.304;
Fuchs T., Gavarini S., Saunders-Pullman R., Raymond D., Ehrlich M.E.,
Bressman S.B., Ozelius L.J.;
"Mutations in the THAP1 gene are responsible for DYT6 primary torsion
dystonia.";
Nat. Genet. 41:286-288(2009).
[20]
VARIANT DYT6 THR-149.
PubMed=20629133; DOI=10.1002/mds.23086;
Van Gerpen J.A., Ledoux M.S., Wszolek Z.K.;
"Adult-onset leg dystonia due to a missense mutation in THAP1.";
Mov. Disord. 25:1306-1307(2010).
[21]
VARIANTS DYT6 ASN-57; ARG-83; CYS-137; VAL-143 AND ASN-192.
PubMed=20669277; DOI=10.1002/mds.23207;
Sohn A.S., Glockle N., Doetzer A.D., Deuschl G., Felbor U.,
Topka H.R., Schols L., Riess O., Bauer P., Muller U., Grundmann K.;
"Prevalence of THAP1 sequence variants in German patients with primary
dystonia.";
Mov. Disord. 25:1982-1986(2010).
[22]
VARIANTS DYT6 ILE-59; ASN-69 DEL AND LYS-136.
PubMed=20687191; DOI=10.1002/mds.23285;
Groen J.L., Ritz K., Contarino M.F., van de Warrenburg B.P.,
Aramideh M., Foncke E.M., van Hilten J.J., Schuurman P.R.,
Speelman J.D., Koelman J.H., de Bie R.M., Baas F., Tijssen M.A.;
"DYT6 dystonia: mutation screening, phenotype, and response to deep
brain stimulation.";
Mov. Disord. 25:2420-2427(2010).
[23]
VARIANTS DYT6 CYS-9; GLY-17; SER-132; THR-149; THR-166 AND LYS-187.
PubMed=20083799; DOI=10.1212/WNL.0b013e3181ca00ca;
Xiao J., Zhao Y., Bastian R.W., Perlmutter J.S., Racette B.A.,
Tabbal S.D., Karimi M., Paniello R.C., Wszolek Z.K., Uitti R.J.,
Van Gerpen J.A., Simon D.K., Tarsy D., Hedera P., Truong D.D.,
Frei K.P., Dev Batish S., Blitzer A., Pfeiffer R.F., Gong S.,
LeDoux M.S.;
"Novel THAP1 sequence variants in primary dystonia.";
Neurology 74:229-238(2010).
[24]
VARIANTS DYT6 PHE-6; CYS-8; ARG-26; SER-136 AND GLN-169.
PubMed=20211909; DOI=10.1212/WNL.0b013e3181d5276d;
Houlden H., Schneider S.A., Paudel R., Melchers A., Schwingenschuh P.,
Edwards M., Hardy J., Bhatia K.P.;
"THAP1 mutations (DYT6) are an additional cause of early-onset
dystonia.";
Neurology 74:846-850(2010).
[25]
VARIANTS DYT6 HIS-13; GLU-16; PRO-23; GLU-24; LEU-26 AND VAL-80, AND
CHARACTERIZATION OF VARIANTS DYT6 HIS-13; GLU-16; PRO-23; GLU-24;
LEU-26 AND VAL-80.
PubMed=21847143; DOI=10.1038/ejhg.2011.159;
Lohmann K., Uflacker N., Erogullari A., Lohnau T., Winkler S.,
Dendorfer A., Schneider S.A., Osmanovic A., Svetel M., Ferbert A.,
Zittel S., Kuhn A.A., Schmidt A., Altenmuller E., Munchau A., Kamm C.,
Wittstock M., Kupsch A., Moro E., Volkmann J., Kostic V., Kaiser F.J.,
Klein C., Bruggemann N.;
"Identification and functional analysis of novel THAP1 mutations.";
Eur. J. Hum. Genet. 20:171-175(2012).
[26]
VARIANTS DYT6 ILE-75 AND PRO-150.
PubMed=20825472; DOI=10.1111/j.1468-1331.2010.03192.x;
Cheng F.B., Wan X.H., Feng J.C., Wang L., Yang Y.M., Cui L.Y.;
"Clinical and genetic evaluation of DYT1 and DYT6 primary dystonia in
China.";
Eur. J. Neurol. 18:497-503(2011).
[27]
VARIANTS DYT6 PHE-54; ILE-75; PRO-150 AND SER-180.
PubMed=21800139; DOI=10.1007/s00415-011-6196-5;
Cheng F.B., Ozelius L.J., Wan X.H., Feng J.C., Ma L.Y., Yang Y.M.,
Wang L.;
"THAP1/DYT6 sequence variants in non-DYT1 early-onset primary dystonia
in China and their effects on RNA expression.";
J. Neurol. 259:342-347(2012).
[28]
VARIANT DYT6 GLY-174.
PubMed=21839475; DOI=10.1016/j.jns.2011.07.023;
Song W., Chen Y., Huang R., Chen K., Pan P., Yang Y., Shang H.F.;
"Novel THAP1 gene mutations in patients with primary dystonia from
Southwest China.";
J. Neurol. Sci. 309:63-67(2011).
[29]
VARIANT DYT6 HIS-32, AND CHARACTERIZATION OF VARIANT DYT6 HIS-32.
PubMed=21425335; DOI=10.1002/mds.23561;
Schneider S.A., Ramirez A., Shafiee K., Kaiser F.J., Erogullari A.,
Bruggemann N., Winkler S., Bahman I., Osmanovic A., Shafa M.A.,
Bhatia K.P., Najmabadi H., Klein C., Lohmann K.;
"Homozygous THAP1 mutations as cause of early-onset generalized
dystonia.";
Mov. Disord. 26:858-861(2011).
[30]
VARIANT DYT6 ARG-30.
PubMed=21425341; DOI=10.1002/mds.23599;
Jech R., Bares M., Krepelova A., Urgosik D., Havrankova P.,
Ruzicka E.;
"DYT 6--a novel THAP1 mutation with excellent effect on pallidal
DBS.";
Mov. Disord. 26:924-925(2011).
[31]
VARIANTS DYT6 PRO-6; ASN-69 DEL AND ARG-72.
PubMed=21110056; DOI=10.1007/s10048-010-0264-3;
Clot F., Grabli D., Burbaud P., Aya M., Derkinderen P., Defebvre L.,
Damier P., Krystkowiak P., Pollak P., Leguern E., San C., Camuzat A.,
Roze E., Vidailhet M., Durr A., Brice A.;
"Screening of the THAP1 gene in patients with early-onset dystonia:
myoclonic jerks are part of the dystonia 6 phenotype.";
Neurogenetics 12:87-89(2011).
[32]
VARIANTS DYT6 ASP-7; GLU-16; CYS-21; GLN-29 AND VAL-80.
PubMed=22377579; DOI=10.1016/j.parkreldis.2012.02.001;
Ledoux M.S., Xiao J., Rudzinska M., Bastian R.W., Wszolek Z.K.,
Van Gerpen J.A., Puschmann A., Momcilovic D., Vemula S.R., Zhao Y.;
"Genotype-phenotype correlations in THAP1 dystonia: Molecular
foundations and description of new cases.";
Parkinsonism Relat. Disord. 18:414-425(2012).
[33]
VARIANT DYT6 GLY-56.
PubMed=25385508; DOI=10.3109/00207454.2014.981749;
Gajos A., Golanska E., Sieruta M., Szybka M., Liberski P.P.,
Bogucki A.;
"High variability of clinical symptoms in a Polish family with a novel
THAP1 mutation.";
Int. J. Neurosci. 125:755-759(2015).
[34]
SUBUNIT, REGION, VARIANTS DYT6 VAL-143; THR-149; PRO-150; THR-166;
GLN-169; ARG-170; GLY-174; PRO-177 AND SER-180, AND CHARACTERIZATION
OF VARIANTS DYT6 THR-149; PRO-150; THR-166; GLN-169; ARG-170; GLY-174;
PRO-177 AND SER-180.
PubMed=28299530; DOI=10.1007/s12031-017-0904-2;
Richter A., Hollstein R., Hebert E., Vulinovic F., Eckhold J.,
Osmanovic A., Depping R., Kaiser F.J., Lohmann K.;
"In-depth Characterization of the Homodimerization Domain of the
Transcription Factor THAP1 and Dystonia-Causing Mutations Therein.";
J. Mol. Neurosci. 62:11-16(2017).
-!- FUNCTION: DNA-binding transcription regulator that regulates
endothelial cell proliferation and G1/S cell-cycle progression.
Specifically binds the 5'-[AT]NTNN[GT]GGCA[AGT]-3' core DNA
sequence and acts by modulating expression of pRB-E2F cell-cycle
target genes, including RRM1. Component of a THAP1/THAP3-HCFC1-OGT
complex that is required for the regulation of the transcriptional
activity of RRM1. May also have pro-apoptopic activity by
potentiating both serum-withdrawal and TNF-induced apoptosis.
{ECO:0000269|PubMed:12717420, ECO:0000269|PubMed:17003378,
ECO:0000269|PubMed:20200153}.
-!- SUBUNIT: Homodimer (PubMed:28299530). Interacts with PAWR.
Component of a THAP1/THAP3-HCFC1-OGT complex that contains, either
THAP1 or THAP3, HCFC1 and OGT. Interacts with OGT. Interacts (via
the HBM) with HCFC1 (via the Kelch-repeat domain); the interaction
recruits HCFC1 to the RRM1 promoter (PubMed:12717420,
PubMed:20144952, PubMed:20200153). {ECO:0000269|PubMed:12717420,
ECO:0000269|PubMed:20144952, ECO:0000269|PubMed:20200153,
ECO:0000269|PubMed:28299530}.
-!- INTERACTION:
Self; NbExp=8; IntAct=EBI-741515, EBI-741515;
O00154:ACOT7; NbExp=3; IntAct=EBI-741515, EBI-948905;
Q02040-3:AKAP17A; NbExp=3; IntAct=EBI-741515, EBI-10222656;
Q99996-2:AKAP9; NbExp=3; IntAct=EBI-741515, EBI-9641546;
P63010:AP2B1; NbExp=4; IntAct=EBI-741515, EBI-432924;
Q66PJ3-3:ARL6IP4; NbExp=3; IntAct=EBI-741515, EBI-10248982;
Q9UL15:BAG5; NbExp=7; IntAct=EBI-741515, EBI-356517;
Q13895:BYSL; NbExp=7; IntAct=EBI-741515, EBI-358049;
Q6ZUT1:C11orf57; NbExp=5; IntAct=EBI-741515, EBI-3920396;
Q6ZUT1-2:C11orf57; NbExp=3; IntAct=EBI-741515, EBI-10180231;
Q9BRJ6:C7orf50; NbExp=5; IntAct=EBI-741515, EBI-751612;
P46527:CDKN1B; NbExp=3; IntAct=EBI-741515, EBI-519280;
O14647:CHD2; NbExp=3; IntAct=EBI-741515, EBI-1210503;
P68400:CSNK2A1; NbExp=5; IntAct=EBI-741515, EBI-347804;
Q5TAQ9:DCAF8; NbExp=3; IntAct=EBI-741515, EBI-740686;
Q86V42:FAM124A; NbExp=3; IntAct=EBI-741515, EBI-744506;
Q8N9E0:FAM133A; NbExp=5; IntAct=EBI-741515, EBI-10268158;
Q9NWQ4:GPATCH2L; NbExp=3; IntAct=EBI-741515, EBI-5666657;
A0A024RA76:hCG_1744368; NbExp=5; IntAct=EBI-741515, EBI-10180729;
A0A024R5S0:hCG_2003792; NbExp=5; IntAct=EBI-741515, EBI-10188461;
Q8WVV9:HNRNPLL; NbExp=3; IntAct=EBI-741515, EBI-535849;
Q9Y4X4:KLF12; NbExp=3; IntAct=EBI-741515, EBI-750750;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-741515, EBI-10172290;
Q14847:LASP1; NbExp=3; IntAct=EBI-741515, EBI-742828;
Q8N6R0:METTL13; NbExp=3; IntAct=EBI-741515, EBI-1053295;
Q9NYP9:MIS18A; NbExp=4; IntAct=EBI-741515, EBI-1104552;
Q9BU76:MMTAG2; NbExp=6; IntAct=EBI-741515, EBI-742459;
Q9UBU8:MORF4L1; NbExp=3; IntAct=EBI-741515, EBI-399246;
Q15014:MORF4L2; NbExp=3; IntAct=EBI-741515, EBI-399257;
Q9Y3B7:MRPL11; NbExp=3; IntAct=EBI-741515, EBI-5453723;
P37198:NUP62; NbExp=11; IntAct=EBI-741515, EBI-347978;
O43189:PHF1; NbExp=3; IntAct=EBI-741515, EBI-530034;
Q7Z2X4:PID1; NbExp=3; IntAct=EBI-741515, EBI-10256685;
Q96T60:PNKP; NbExp=4; IntAct=EBI-741515, EBI-1045072;
P62875:POLR2L; NbExp=3; IntAct=EBI-741515, EBI-359527;
P78424:POU6F2; NbExp=4; IntAct=EBI-741515, EBI-12029004;
Q13427:PPIG; NbExp=3; IntAct=EBI-741515, EBI-396072;
Q13131:PRKAA1; NbExp=3; IntAct=EBI-741515, EBI-1181405;
P86479:PRR20C; NbExp=3; IntAct=EBI-741515, EBI-10172814;
Q86SE5:RALYL; NbExp=4; IntAct=EBI-741515, EBI-741520;
Q86SE5-3:RALYL; NbExp=5; IntAct=EBI-741515, EBI-11526555;
Q14498:RBM39; NbExp=5; IntAct=EBI-741515, EBI-395290;
Q0D2K3:RIPPLY1; NbExp=5; IntAct=EBI-741515, EBI-10226430;
P62851:RPS25; NbExp=3; IntAct=EBI-741515, EBI-353054;
Q9UHR5:SAP30BP; NbExp=3; IntAct=EBI-741515, EBI-751683;
O95391:SLU7; NbExp=3; IntAct=EBI-741515, EBI-750559;
Q96SI9:STRBP; NbExp=6; IntAct=EBI-741515, EBI-740355;
Q15560:TCEA2; NbExp=5; IntAct=EBI-741515, EBI-710310;
P06753:TPM3; NbExp=4; IntAct=EBI-741515, EBI-355607;
Q5VU62:TPM3; NbExp=3; IntAct=EBI-741515, EBI-10184033;
O00463:TRAF5; NbExp=5; IntAct=EBI-741515, EBI-523498;
Q12899:TRIM26; NbExp=5; IntAct=EBI-741515, EBI-2341136;
Q6ZVT0:TTLL10; NbExp=3; IntAct=EBI-741515, EBI-7844656;
P26368:U2AF2; NbExp=4; IntAct=EBI-741515, EBI-742339;
Q96HA8:WDYHV1; NbExp=6; IntAct=EBI-741515, EBI-741158;
P07947:YES1; NbExp=5; IntAct=EBI-741515, EBI-515331;
Q8TBK6:ZCCHC10; NbExp=6; IntAct=EBI-741515, EBI-597063;
Q66K41:ZNF385C; NbExp=3; IntAct=EBI-741515, EBI-10219231;
Q9H9D4:ZNF408; NbExp=5; IntAct=EBI-741515, EBI-347633;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000269|PubMed:12717420}. Nucleus, PML body
{ECO:0000269|PubMed:12717420}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NVV9-1; Sequence=Displayed;
Name=2;
IsoId=Q9NVV9-2; Sequence=VSP_044665, VSP_044666;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle,
kidney and liver. Weaker expression in brain and placenta.
{ECO:0000269|PubMed:20200153}.
-!- DISEASE: Dystonia 6, torsion (DYT6) [MIM:602629]: A primary
torsion dystonia. Dystonia is defined by the presence of sustained
involuntary muscle contractions, often leading to abnormal
postures. Dystonia type 6 is characterized by onset in early
adulthood, cranial or cervical involvement in about half of the
cases, and frequent progression to involve multiple body regions.
{ECO:0000269|PubMed:19182804, ECO:0000269|PubMed:19345147,
ECO:0000269|PubMed:19908320, ECO:0000269|PubMed:19908325,
ECO:0000269|PubMed:20083799, ECO:0000269|PubMed:20211909,
ECO:0000269|PubMed:20629133, ECO:0000269|PubMed:20669277,
ECO:0000269|PubMed:20687191, ECO:0000269|PubMed:20825472,
ECO:0000269|PubMed:21110056, ECO:0000269|PubMed:21425335,
ECO:0000269|PubMed:21425341, ECO:0000269|PubMed:21800139,
ECO:0000269|PubMed:21839475, ECO:0000269|PubMed:21847143,
ECO:0000269|PubMed:22377579, ECO:0000269|PubMed:25385508,
ECO:0000269|PubMed:28299530, ECO:0000269|Ref.3}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the THAP1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK001339; BAA91635.1; -; mRNA.
EMBL; CR457256; CAG33537.1; -; mRNA.
EMBL; AK223231; BAD96951.1; -; mRNA.
EMBL; AL832077; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC087533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471080; EAW63205.1; -; Genomic_DNA.
EMBL; CH471080; EAW63206.1; -; Genomic_DNA.
EMBL; BC021721; AAH21721.1; -; mRNA.
CCDS; CCDS6136.1; -. [Q9NVV9-1]
CCDS; CCDS6137.1; -. [Q9NVV9-2]
RefSeq; NP_060575.1; NM_018105.2. [Q9NVV9-1]
RefSeq; NP_945354.1; NM_199003.1. [Q9NVV9-2]
UniGene; Hs.7432; -.
PDB; 2JTG; NMR; -; A=1-81.
PDB; 2KO0; NMR; -; A=1-82.
PDB; 2L1G; NMR; -; A=1-82.
PDBsum; 2JTG; -.
PDBsum; 2KO0; -.
PDBsum; 2L1G; -.
ProteinModelPortal; Q9NVV9; -.
SMR; Q9NVV9; -.
BioGrid; 120448; 68.
ELM; Q9NVV9; -.
IntAct; Q9NVV9; 97.
MINT; MINT-1434025; -.
STRING; 9606.ENSP00000254250; -.
iPTMnet; Q9NVV9; -.
PhosphoSitePlus; Q9NVV9; -.
BioMuta; THAP1; -.
DMDM; 29839656; -.
EPD; Q9NVV9; -.
MaxQB; Q9NVV9; -.
PaxDb; Q9NVV9; -.
PeptideAtlas; Q9NVV9; -.
PRIDE; Q9NVV9; -.
DNASU; 55145; -.
Ensembl; ENST00000254250; ENSP00000254250; ENSG00000131931. [Q9NVV9-1]
Ensembl; ENST00000345117; ENSP00000344966; ENSG00000131931. [Q9NVV9-2]
GeneID; 55145; -.
KEGG; hsa:55145; -.
UCSC; uc003xpk.4; human. [Q9NVV9-1]
CTD; 55145; -.
DisGeNET; 55145; -.
EuPathDB; HostDB:ENSG00000131931.8; -.
GeneCards; THAP1; -.
HGNC; HGNC:20856; THAP1.
HPA; HPA071310; -.
MalaCards; THAP1; -.
MIM; 602629; phenotype.
MIM; 609520; gene.
neXtProt; NX_Q9NVV9; -.
OpenTargets; ENSG00000131931; -.
Orphanet; 98806; Primary dystonia, DYT6 type.
PharmGKB; PA134920361; -.
eggNOG; ENOG410IGDI; Eukaryota.
eggNOG; ENOG4111FGC; LUCA.
GeneTree; ENSGT00840000129785; -.
HOGENOM; HOG000231117; -.
HOVERGEN; HBG057457; -.
InParanoid; Q9NVV9; -.
OMA; HQRKRIQ; -.
OrthoDB; EOG091G034R; -.
PhylomeDB; Q9NVV9; -.
TreeFam; TF330127; -.
ChiTaRS; THAP1; human.
EvolutionaryTrace; Q9NVV9; -.
GeneWiki; THAP1; -.
GenomeRNAi; 55145; -.
PRO; PR:Q9NVV9; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000131931; -.
CleanEx; HS_THAP1; -.
ExpressionAtlas; Q9NVV9; baseline and differential.
Genevisible; Q9NVV9; HS.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IC:NTNU_SB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0001935; P:endothelial cell proliferation; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IMP:UniProtKB.
InterPro; IPR026516; THAP1.
InterPro; IPR006612; Znf_C2CH.
PANTHER; PTHR23080:SF85; PTHR23080:SF85; 1.
Pfam; PF05485; THAP; 1.
SMART; SM00692; DM3; 1.
SMART; SM00980; THAP; 1.
PROSITE; PS50950; ZF_THAP; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Coiled coil;
Complete proteome; Disease mutation; DNA-binding; Dystonia;
Metal-binding; Nucleus; Reference proteome; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 213 THAP domain-containing protein 1.
/FTId=PRO_0000068637.
ZN_FING 1 81 THAP-type. {ECO:0000255|PROSITE-
ProRule:PRU00309}.
REGION 139 185 Involved in homodimer formation.
{ECO:0000269|PubMed:28299530}.
COILED 139 190 {ECO:0000255}.
MOTIF 134 137 HCFC1-binding motif (HBM).
COMPBIAS 96 108 Pro-rich.
VAR_SEQ 25 53 FPLTRPSLCKEWEAAVRRKNFKPTKYSSI -> KKIFWSHR
NSFPHLLYRLLFPRLMLLLDY (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_044665.
VAR_SEQ 54 213 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_044666.
VARIANT 6 6 S -> F (in DYT6).
{ECO:0000269|PubMed:20211909}.
/FTId=VAR_066677.
VARIANT 6 6 S -> P (in DYT6).
{ECO:0000269|PubMed:21110056}.
/FTId=VAR_066678.
VARIANT 7 7 A -> D (in DYT6).
{ECO:0000269|PubMed:22377579}.
/FTId=VAR_067356.
VARIANT 8 8 Y -> C (in DYT6).
{ECO:0000269|PubMed:20211909}.
/FTId=VAR_066679.
VARIANT 9 9 G -> C (in DYT6; dbSNP:rs267607112).
{ECO:0000269|PubMed:20083799}.
/FTId=VAR_066680.
VARIANT 12 12 N -> K (in DYT6).
{ECO:0000269|PubMed:19345147}.
/FTId=VAR_065880.
VARIANT 13 13 R -> H (in DYT6).
{ECO:0000269|PubMed:21847143}.
/FTId=VAR_066681.
VARIANT 16 16 K -> E (in DYT6; lower activity than
wild-type). {ECO:0000269|PubMed:21847143,
ECO:0000269|PubMed:22377579}.
/FTId=VAR_066682.
VARIANT 17 17 D -> G (in DYT6; dbSNP:rs766483829).
{ECO:0000269|PubMed:20083799}.
/FTId=VAR_066683.
VARIANT 21 21 S -> C (in DYT6).
{ECO:0000269|PubMed:22377579}.
/FTId=VAR_067357.
VARIANT 21 21 S -> T (in DYT6).
{ECO:0000269|PubMed:19345147}.
/FTId=VAR_065881.
VARIANT 23 23 H -> P (in DYT6; lower activity than
wild-type; dbSNP:rs387907177).
{ECO:0000269|PubMed:21847143}.
/FTId=VAR_066684.
VARIANT 24 24 K -> E (in DYT6; lower activity than
wild-type; dbSNP:rs387907176).
{ECO:0000269|PubMed:21847143}.
/FTId=VAR_066685.
VARIANT 26 26 P -> L (in DYT6; lower activity than
wild-type).
{ECO:0000269|PubMed:21847143}.
/FTId=VAR_066686.
VARIANT 26 26 P -> R (in DYT6).
{ECO:0000269|PubMed:20211909}.
/FTId=VAR_066687.
VARIANT 29 29 R -> P (in DYT6).
{ECO:0000269|PubMed:19345147}.
/FTId=VAR_065882.
VARIANT 29 29 R -> Q (in DYT6; dbSNP:rs767952378).
{ECO:0000269|PubMed:19908320,
ECO:0000269|PubMed:22377579}.
/FTId=VAR_066688.
VARIANT 30 30 P -> R (in DYT6).
{ECO:0000269|PubMed:21425341}.
/FTId=VAR_066689.
VARIANT 32 32 L -> H (in DYT6; lower activity than
wild-type).
{ECO:0000269|PubMed:21425335}.
/FTId=VAR_066690.
VARIANT 39 39 A -> T (in DYT6).
{ECO:0000269|PubMed:19345147}.
/FTId=VAR_065883.
VARIANT 54 54 C -> F (in DYT6).
{ECO:0000269|PubMed:21800139}.
/FTId=VAR_066691.
VARIANT 56 56 E -> G (in DYT6).
{ECO:0000269|PubMed:25385508}.
/FTId=VAR_072272.
VARIANT 57 57 H -> N (in DYT6).
{ECO:0000269|PubMed:20669277}.
/FTId=VAR_066692.
VARIANT 59 59 T -> I (in DYT6).
{ECO:0000269|PubMed:20687191}.
/FTId=VAR_065884.
VARIANT 69 69 Missing (in DYT6).
{ECO:0000269|PubMed:20687191,
ECO:0000269|PubMed:21110056}.
/FTId=VAR_066693.
VARIANT 72 72 L -> R (in DYT6).
{ECO:0000269|PubMed:21110056}.
/FTId=VAR_066694.
VARIANT 75 75 N -> I (in DYT6).
{ECO:0000269|PubMed:20825472,
ECO:0000269|PubMed:21800139}.
/FTId=VAR_066695.
VARIANT 80 80 I -> V (in DYT6; mild phenotype; does not
affect activity; dbSNP:rs372080941).
{ECO:0000269|PubMed:21847143,
ECO:0000269|PubMed:22377579}.
/FTId=VAR_066696.
VARIANT 81 81 F -> L (in DYT6; affects DNA-binding;
dbSNP:rs118204013).
{ECO:0000269|PubMed:19182804,
ECO:0000269|PubMed:19345147}.
/FTId=VAR_054788.
VARIANT 83 83 C -> R (in DYT6; dbSNP:rs768017019).
{ECO:0000269|PubMed:20669277}.
/FTId=VAR_066697.
VARIANT 89 89 K -> R (in DYT6; dbSNP:rs267607111).
{ECO:0000269|PubMed:19345147,
ECO:0000269|Ref.3}.
/FTId=VAR_065885.
VARIANT 132 132 F -> S (in DYT6).
{ECO:0000269|PubMed:20083799}.
/FTId=VAR_066698.
VARIANT 136 136 N -> K (in DYT6).
{ECO:0000269|PubMed:20687191}.
/FTId=VAR_065886.
VARIANT 136 136 N -> S (in DYT6; dbSNP:rs769988455).
{ECO:0000269|PubMed:20211909}.
/FTId=VAR_066699.
VARIANT 137 137 Y -> C (in DYT6).
{ECO:0000269|PubMed:20669277}.
/FTId=VAR_066700.
VARIANT 143 143 M -> V (in DYT6; no effect on
dimerization; dbSNP:rs374512193).
{ECO:0000269|PubMed:20669277,
ECO:0000269|PubMed:28299530}.
/FTId=VAR_066701.
VARIANT 149 149 I -> T (in DYT6; no effect on
dimerization).
{ECO:0000269|PubMed:20083799,
ECO:0000269|PubMed:20629133,
ECO:0000269|PubMed:28299530}.
/FTId=VAR_066702.
VARIANT 150 150 H -> P (in DYT6; no effect on
dimerization).
{ECO:0000269|PubMed:20825472,
ECO:0000269|PubMed:21800139,
ECO:0000269|PubMed:28299530}.
/FTId=VAR_066703.
VARIANT 166 166 A -> T (in DYT6; no effect on
dimerization; dbSNP:rs138918468).
{ECO:0000269|PubMed:20083799,
ECO:0000269|PubMed:28299530}.
/FTId=VAR_066704.
VARIANT 169 169 R -> Q (in DYT6; no effect on
dimerization; dbSNP:rs767519301).
{ECO:0000269|PubMed:20211909,
ECO:0000269|PubMed:28299530}.
/FTId=VAR_066705.
VARIANT 170 170 C -> R (in DYT6; no effect on
dimerization).
{ECO:0000269|PubMed:19908325,
ECO:0000269|PubMed:28299530}.
/FTId=VAR_065887.
VARIANT 174 174 E -> G (in DYT6; no effect on
dimerization; dbSNP:rs759392096).
{ECO:0000269|PubMed:21839475,
ECO:0000269|PubMed:28299530}.
/FTId=VAR_066706.
VARIANT 177 177 L -> P (in DYT6; no effect on
dimerization).
{ECO:0000269|PubMed:28299530}.
/FTId=VAR_079366.
VARIANT 180 180 L -> S (in DYT6; no effect on
dimerization).
{ECO:0000269|PubMed:21800139,
ECO:0000269|PubMed:28299530}.
/FTId=VAR_066707.
VARIANT 187 187 Q -> K (in DYT6).
{ECO:0000269|PubMed:20083799}.
/FTId=VAR_066708.
VARIANT 192 192 D -> N (in DYT6; dbSNP:rs377725442).
{ECO:0000269|PubMed:20669277}.
/FTId=VAR_066709.
MUTAGEN 4 4 S->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 5 5 C->A: Abolishes DNA- and zinc-binding.
{ECO:0000269|PubMed:15863623,
ECO:0000269|PubMed:18073205}.
MUTAGEN 6 6 S->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 8 8 Y->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 10 10 C->A: Abolishes DNA- and zinc-binding.
{ECO:0000269|PubMed:15863623,
ECO:0000269|PubMed:18073205}.
MUTAGEN 11 11 K->A: Partially affects DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 16 16 K->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 24 24 K->A: Strongly affects DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 26 26 P->A: Abolishes DNA- and zinc-binding.
{ECO:0000269|PubMed:15863623,
ECO:0000269|PubMed:18073205}.
MUTAGEN 27 27 L->A: Partially affects DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 28 30 TRP->AAA: Strongly affects DNA-binding.
MUTAGEN 28 28 T->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 29 29 R->A: Strongly affects DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 30 30 P->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 31 31 S->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 32 32 L->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 33 33 C->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 34 34 K->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 35 35 E->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 36 36 W->A: Abolishes DNA- and zinc-binding.
{ECO:0000269|PubMed:15863623,
ECO:0000269|PubMed:18073205}.
MUTAGEN 37 37 E->A: Partially affects DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 40 40 V->A: Partially affects DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 41 43 RRK->AAA: Strongly affects DNA-binding.
MUTAGEN 41 41 R->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 42 42 R->A: Strongly affects DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 43 43 K->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 44 44 N->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 45 45 F->A: Strongly affects DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 46 46 K->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 47 49 PTK->AAA: Strongly affects DNA-binding.
MUTAGEN 47 47 P->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 48 48 T->A: Strongly affects DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 49 49 K->A: Does not affect DNA-binding.
MUTAGEN 50 52 YSS->AAA: Strongly affects DNA-binding.
MUTAGEN 50 50 Y->A: Partially affects DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 51 51 S->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 52 52 S->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 54 54 C->A: Abolishes DNA- and zinc-binding.
{ECO:0000269|PubMed:15863623,
ECO:0000269|PubMed:18073205}.
MUTAGEN 55 55 S->A: Does not affect DNA-binding.
{ECO:0000269|PubMed:18073205}.
MUTAGEN 57 57 H->A: Abolishes DNA- and zinc-binding.
{ECO:0000269|PubMed:15863623,
ECO:0000269|PubMed:18073205}.
MUTAGEN 58 58 F->A: Abolishes DNA- and zinc-binding.
{ECO:0000269|PubMed:15863623,
ECO:0000269|PubMed:18073205}.
MUTAGEN 78 78 P->A: Abolishes DNA- and zinc-binding.
{ECO:0000269|PubMed:15863623,
ECO:0000269|PubMed:18073205}.
CONFLICT 171 171 R -> G (in Ref. 2; CAG33537).
{ECO:0000305}.
CONFLICT 213 213 A -> T (in Ref. 3; BAD96951).
{ECO:0000305}.
STRAND 6 9 {ECO:0000244|PDB:2KO0}.
STRAND 16 18 {ECO:0000244|PDB:2JTG}.
STRAND 22 24 {ECO:0000244|PDB:2JTG}.
HELIX 33 40 {ECO:0000244|PDB:2JTG}.
STRAND 42 44 {ECO:0000244|PDB:2KO0}.
TURN 47 49 {ECO:0000244|PDB:2JTG}.
STRAND 51 54 {ECO:0000244|PDB:2JTG}.
HELIX 55 57 {ECO:0000244|PDB:2JTG}.
HELIX 60 63 {ECO:0000244|PDB:2JTG}.
STRAND 67 71 {ECO:0000244|PDB:2KO0}.
HELIX 79 81 {ECO:0000244|PDB:2JTG}.
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


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