ATRX_HUMAN
ID ATRX_HUMAN Reviewed; 2492 AA.
AC P46100; D3DTE2; P51068; Q15886; Q59FB5; Q59H31; Q5H9A2; Q5JWI4; Q7Z2J1;
AC Q9H0Z1; Q9NTS3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 6.
DT 03-AUG-2022, entry version 234.
DE RecName: Full=Transcriptional regulator ATRX;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase ATRX;
DE AltName: Full=X-linked helicase II;
DE AltName: Full=X-linked nuclear protein;
DE Short=XNP;
DE AltName: Full=Znf-HX;
GN Name=ATRX; Synonyms=RAD54L, XH2;
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] (ISOFORMS 1; 2; 3; 4 AND 5), VARIANT SER-1860,
RP AND VARIANTS ATRX.
RX PubMed=8968741; DOI=10.1093/hmg/5.12.1899;
RA Picketts D.J., Higgs D.R., Bachoo S., Blake D.J., Quarrell O.W.J.,
RA Gibbons R.J.;
RT "ATRX encodes a novel member of the SNF2 family of proteins: mutations
RT point to a common mechanism underlying the ATR-X syndrome.";
RL Hum. Mol. Genet. 5:1899-1907(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), AND VARIANTS PRO-596 AND
RP GLY-740.
RX PubMed=9244431; DOI=10.1006/geno.1997.4793;
RA Villard L., Lossi A.-M., Cardoso C., Proud V., Chiaroni P., Colleaux L.,
RA Schwartz C., Fontes M.;
RT "Determination of the genomic structure of the XNP/ATRX gene encoding a
RT potential zinc finger helicase.";
RL Genomics 43:149-155(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF
RP 163-198.
RX PubMed=12777533; DOI=10.1093/molbev/msg134;
RA Kitano T., Schwarz C., Nickel B., Paeaebo S.;
RT "Gene diversity patterns at 10 X-chromosomal loci in humans and
RT chimpanzees.";
RL Mol. Biol. Evol. 20:1281-1289(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 704-1927 (ISOFORMS 1/2/3/4/5).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
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 [MRNA] OF 860-2492.
RX PubMed=7874112; DOI=10.1093/hmg/3.11.1957;
RA Stayton C.L., Dabovic B., Gulisano M., Gecz J., Broccoli V., Giovanazzi S.,
RA Bossolasco M., Monaco L., Rastan S., Boncinelli E., Bianchi M.E.,
RA Consalez G.G.;
RT "Cloning and characterization of a new human Xq13 gene, encoding a putative
RT helicase.";
RL Hum. Mol. Genet. 3:1957-1964(1994).
RN [8]
RP PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8162050; DOI=10.1093/hmg/3.1.39;
RA Gecz J., Pollard H., Consalez G., Villard L., Stayton C.L., Millasseau P.,
RA Khrestchatisky M., Fontes M.;
RT "Cloning and expression of the murine homologue of a putative human X-
RT linked nuclear protein gene closely linked to PGK1 in Xq13.3.";
RL Hum. Mol. Genet. 3:39-44(1994).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2401-2492, AND VARIANTS ATRX.
RX PubMed=7697714; DOI=10.1016/0092-8674(95)90287-2;
RA Gibbons R.J., Picketts D.J., Villard L., Higgs D.R.;
RT "Mutations in a putative global transcriptional regulator cause X-linked
RT mental retardation with alpha-thalassemia (ATR-X syndrome).";
RL Cell 80:837-845(1995).
RN [10]
RP INTERACTION WITH EZH2.
RX PubMed=9499421; DOI=10.1093/hmg/7.4.679;
RA Cardoso C., Timsit S., Villard L., Khrestchatisky M., Fontes M.,
RA Colleaux L.;
RT "Specific interaction between the XNP/ATR-X gene product and the SET domain
RT of the human EZH2 protein.";
RL Hum. Mol. Genet. 7:679-684(1998).
RN [11]
RP SUBCELLULAR LOCATION, AND ASSOCIATION WITH PERICENTROMERIC HETEROCHROMATIN.
RX PubMed=10570185; DOI=10.1073/pnas.96.24.13983;
RA McDowell T.L., Gibbons R.J., Sutherland H., O'Rourke D.M., Bickmore W.A.,
RA Pombo A., Turley H., Gatter K., Picketts D.J., Buckle V.J., Chapman L.,
RA Rhodes D., Higgs D.R.;
RT "Localization of a putative transcriptional regulator (ATRX) at
RT pericentromeric heterochromatin and the short arms of acrocentric
RT chromosomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13983-13988(1999).
RN [12]
RP INVOLVEMENT IN MRXHF1.
RX PubMed=10751095;
RX DOI=10.1002/(sici)1096-8628(20000306)91:1<83::aid-ajmg15>3.0.co;2-n;
RA Villard L., Fontes M., Ades L.C., Gecz J.;
RT "Identification of a mutation in the XNP/ATR-X gene in a family reported as
RT Smith-Fineman-Myers syndrome.";
RL Am. J. Med. Genet. 91:83-85(2000).
RN [13]
RP INTERACTION WITH CBX5, AND PHOSPHORYLATION.
RX PubMed=10699177; DOI=10.1093/hmg/9.4.539;
RA Berube N.G., Smeenk C.A., Picketts D.J.;
RT "Cell cycle-dependent phosphorylation of the ATRX protein correlates with
RT changes in nuclear matrix and chromatin association.";
RL Hum. Mol. Genet. 9:539-547(2000).
RN [14]
RP INVOLVEMENT IN ATMDS.
RX PubMed=12858175; DOI=10.1038/ng1213;
RA Gibbons R.J., Pellagatti A., Garrick D., Wood W.G., Malik N., Ayyub H.,
RA Langford C., Boultwood J., Wainscoat J.S., Higgs D.R.;
RT "Identification of acquired somatic mutations in the gene encoding
RT chromatin-remodeling factor ATRX in the alpha-thalassemia myelodysplasia
RT syndrome (ATMDS).";
RL Nat. Genet. 34:446-449(2003).
RN [15]
RP FUNCTION, INTERACTION WITH DAXX, AND SUBCELLULAR LOCATION.
RX PubMed=12953102; DOI=10.1073/pnas.1937626100;
RA Xue Y., Gibbons R., Yan Z., Yang D., McDowell T.L., Sechi S., Qin J.,
RA Zhou S., Higgs D., Wang W.;
RT "The ATRX syndrome protein forms a chromatin-remodeling complex with Daxx
RT and localizes in promyelocytic leukemia nuclear bodies.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10635-10640(2003).
RN [16]
RP FUNCTION, INTERACTION WITH DAXX, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP LYS-1600, AND CHARACTERIZATION OF VARIANTS ATRX VAL-2035 AND HIS-2084.
RX PubMed=14990586; DOI=10.1074/jbc.m401321200;
RA Tang J., Wu S., Liu H., Stratt R., Barak O.G., Shiekhattar R.,
RA Picketts D.J., Yang X.;
RT "A novel transcription regulatory complex containing death domain-
RT associated protein and the ATR-X syndrome protein.";
RL J. Biol. Chem. 279:20369-20377(2004).
RN [17]
RP INTERACTION WITH CBX5.
RX PubMed=15882967; DOI=10.1016/j.bbrc.2005.04.016;
RA Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III;
RT "The mammalian heterochromatin protein 1 binds diverse nuclear proteins
RT through a common motif that targets the chromoshadow domain.";
RL Biochem. Biophys. Res. Commun. 331:929-937(2005).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634 AND SER-1352, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [19]
RP INTERACTION WITH MECP2.
RX PubMed=17296936; DOI=10.1073/pnas.0608056104;
RA Nan X., Hou J., Maclean A., Nasir J., Lafuente M.J., Shu X.,
RA Kriaucionis S., Bird A.;
RT "Interaction between chromatin proteins MECP2 and ATRX is disrupted by
RT mutations that cause inherited mental retardation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2709-2714(2007).
RN [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594; THR-674; SER-675;
RP SER-677; SER-729; SER-731; SER-875; SER-876; SER-1348; SER-1352; SER-1996
RP AND SER-2220, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; TYR-89; SER-112 AND
RP SER-1996, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-967, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [25]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21029860; DOI=10.1016/j.cell.2010.09.023;
RA Law M.J., Lower K.M., Voon H.P., Hughes J.R., Garrick D., Viprakasit V.,
RA Mitson M., De Gobbi M., Marra M., Morris A., Abbott A., Wilder S.P.,
RA Taylor S., Santos G.M., Cross J., Ayyub H., Jones S., Ragoussis J.,
RA Rhodes D., Dunham I., Higgs D.R., Gibbons R.J.;
RT "ATR-X syndrome protein targets tandem repeats and influences allele-
RT specific expression in a size-dependent manner.";
RL Cell 143:367-378(2010).
RN [26]
RP ASSOCIATION WITH HISTONE H3.3.
RX PubMed=20211137; DOI=10.1016/j.cell.2010.01.003;
RA Goldberg A.D., Banaszynski L.A., Noh K.M., Lewis P.W., Elsaesser S.J.,
RA Stadler S., Dewell S., Law M., Guo X., Li X., Wen D., Chapgier A.,
RA DeKelver R.C., Miller J.C., Lee Y.L., Boydston E.A., Holmes M.C.,
RA Gregory P.D., Greally J.M., Rafii S., Yang C., Scambler P.J., Garrick D.,
RA Gibbons R.J., Higgs D.R., Cristea I.M., Urnov F.D., Zheng D., Allis C.D.;
RT "Distinct factors control histone variant H3.3 localization at specific
RT genomic regions.";
RL Cell 140:678-691(2010).
RN [27]
RP FUNCTION.
RX PubMed=20504901; DOI=10.1101/gad.566910;
RA Drane P., Ouararhni K., Depaux A., Shuaib M., Hamiche A.;
RT "The death-associated protein DAXX is a novel histone chaperone involved in
RT the replication-independent deposition of H3.3.";
RL Genes Dev. 24:1253-1265(2010).
RN [28]
RP FUNCTION OF THE ATRX:DAXX COMPLEX.
RX PubMed=20651253; DOI=10.1073/pnas.1008850107;
RA Lewis P.W., Elsaesser S.J., Noh K.M., Stadler S.C., Allis C.D.;
RT "Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in
RT replication-independent chromatin assembly at telomeres.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:14075-14080(2010).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; THR-591; SER-598;
RP SER-1061; TYR-1063; SER-1348; SER-1352; SER-1527; SER-1992; SER-1996 AND
RP SER-2220, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [31]
RP INTERACTION WITH TRIMETHYLATED HISTONE H3 'LYS-9', CHARACTERIZATION OF
RP VARIANTS ATRX CYS-246; LEU-246 AND ASP-249, AND MUTAGENESIS OF TYR-203;
RP TYR-204; ILE-209; ASP-214 AND ASP-217.
RX PubMed=21421568; DOI=10.1093/hmg/ddr107;
RA Dhayalan A., Tamas R., Bock I., Tattermusch A., Dimitrova E.,
RA Kudithipudi S., Ragozin S., Jeltsch A.;
RT "The ATRX-ADD domain binds to H3 tail peptides and reads the combined
RT methylation state of K4 and K9.";
RL Hum. Mol. Genet. 20:2195-2203(2011).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598; SER-889; SER-1061;
RP SER-1322; SER-1324; SER-1326; SER-1348 AND SER-1352, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [33]
RP FUNCTION, AND INTERACTION WITH HISTONE MACROH2A1.
RX PubMed=22391447; DOI=10.1101/gad.179416.111;
RA Ratnakumar K., Duarte L.F., LeRoy G., Hasson D., Smeets D., Vardabasso C.,
RA Bonisch C., Zeng T., Xiang B., Zhang D.Y., Li H., Wang X., Hake S.B.,
RA Schermelleh L., Garcia B.A., Bernstein E.;
RT "ATRX-mediated chromatin association of histone variant macroH2A1 regulates
RT alpha-globin expression.";
RL Genes Dev. 26:433-438(2012).
RN [34]
RP FUNCTION.
RX PubMed=22829774; DOI=10.1371/journal.pgen.1002772;
RA Lovejoy C.A., Li W., Reisenweber S., Thongthip S., Bruno J., de Lange T.,
RA De S., Petrini J.H., Sung P.A., Jasin M., Rosenbluh J., Zwang Y.,
RA Weir B.A., Hatton C., Ivanova E., Macconaill L., Hanna M., Hahn W.C.,
RA Lue N.F., Reddel R.R., Jiao Y., Kinzler K., Vogelstein B., Papadopoulos N.,
RA Meeker A.K.;
RT "Loss of ATRX, genome instability, and an altered DNA damage response are
RT hallmarks of the alternative lengthening of telomeres pathway.";
RL PLoS Genet. 8:E1002772-E1002772(2012).
RN [35]
RP SUBCELLULAR LOCATION.
RX PubMed=23222847; DOI=10.1101/gr.142703.112;
RA Delbarre E., Ivanauskiene K., Kuntziger T., Collas P.;
RT "DAXX-dependent supply of soluble (H3.3-H4) dimers to PML bodies pending
RT deposition into chromatin.";
RL Genome Res. 23:440-451(2013).
RN [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-34; SER-316; SER-677;
RP SER-729; SER-731; SER-819; SER-849; SER-850; SER-889; SER-962; SER-1061;
RP SER-1348; SER-1352; SER-1527 AND THR-1529, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-598; SER-675; SER-974
RP AND THR-977, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [38]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-299; LYS-438; LYS-1004; LYS-1488
RP AND LYS-1982, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [39]
RP FUNCTION.
RX PubMed=24500201; DOI=10.1093/nar/gku114;
RA Episkopou H., Draskovic I., Van Beneden A., Tilman G., Mattiussi M.,
RA Gobin M., Arnoult N., Londono-Vallejo A., Decottignies A.;
RT "Alternative lengthening of telomeres is characterized by reduced
RT compaction of telomeric chromatin.";
RL Nucleic Acids Res. 42:4391-4405(2014).
RN [40]
RP INTERACTION WITH RAD50; MRE11 AND NBN.
RX PubMed=24651726; DOI=10.1371/journal.pone.0092915;
RA Clynes D., Jelinska C., Xella B., Ayyub H., Taylor S., Mitson M.,
RA Bachrati C.Z., Higgs D.R., Gibbons R.J.;
RT "ATRX dysfunction induces replication defects in primary mouse cells.";
RL PLoS ONE 9:E92915-E92915(2014).
RN [41]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-623 AND LYS-1982, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [42]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1004 AND LYS-1982, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [43]
RP FUNCTION, AND INTERACTION WITH DAXX; SETDB1; TRIM28 AND ZNF274.
RX PubMed=27029610; DOI=10.1080/15592294.2016.1169351;
RA Valle-Garcia D., Qadeer Z.A., McHugh D.S., Ghiraldini F.G., Chowdhury A.H.,
RA Hasson D., Dyer M.A., Recillas-Targa F., Bernstein E.;
RT "ATRX binds to atypical chromatin domains at the 3' exons of zinc finger
RT genes to preserve H3K9me3 enrichment.";
RL Epigenetics 11:398-414(2016).
RN [44]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-138; LYS-142; LYS-438;
RP LYS-623; LYS-1004; LYS-1488; LYS-1982 AND LYS-1987, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [45]
RP STRUCTURE BY NMR OF 159-296, AND DOMAIN GATA-TYPE ZINC-FINGER.
RX PubMed=17609377; DOI=10.1073/pnas.0704057104;
RA Argentaro A., Yang J.C., Chapman L., Kowalczyk M.S., Gibbons R.J.,
RA Higgs D.R., Neuhaus D., Rhodes D.;
RT "Structural consequences of disease-causing mutations in the ATRX-DNMT3-
RT DNMT3L (ADD) domain of the chromatin-associated protein ATRX.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:11939-11944(2007).
RN [46]
RP X-RAY CRYSTALLOGRAPHY (0.93 ANGSTROMS) OF 167-289 IN COMPLEX WITH HISTONE
RP H3K9ME3 PEPTIDE, SUBCELLULAR LOCATION, CHARACTERIZATION OF ATRX VARIANTS
RP ALA-190; PRO-219 AND CYS-246, AND MUTAGENESIS OF HIS-189; TYR-203; TYR-204;
RP ASP-217; GLU-252 AND LYS-1600.
RX PubMed=21666679; DOI=10.1038/nsmb.2062;
RA Iwase S., Xiang B., Ghosh S., Ren T., Lewis P.W., Cochrane J.C.,
RA Allis C.D., Picketts D.J., Patel D.J., Li H., Shi Y.;
RT "ATRX ADD domain links an atypical histone methylation recognition
RT mechanism to human mental-retardation syndrome.";
RL Nat. Struct. Mol. Biol. 18:769-776(2011).
RN [47]
RP STRUCTURE BY NMR OF 163-296 IN COMPLEX WITH HISTONE H3K9ME3 PEPTIDE,
RP CHARACTERIZATION OF ATRX VARIANT PRO-219, AND MUTAGENESIS OF TYR-203 AND
RP GLU-218.
RX PubMed=21666677; DOI=10.1038/nsmb.2070;
RA Eustermann S., Yang J.C., Law M.J., Amos R., Chapman L.M., Jelinska C.,
RA Garrick D., Clynes D., Gibbons R.J., Rhodes D., Higgs D.R., Neuhaus D.;
RT "Combinatorial readout of histone H3 modifications specifies localization
RT of ATRX to heterochromatin.";
RL Nat. Struct. Mol. Biol. 18:777-782(2011).
RN [48]
RP VARIANT ATRX SER-1713.
RX PubMed=9043863; DOI=10.1159/000472225;
RA Villard L., Lacombe D., Fontes M.;
RT "A point mutation in the XNP gene, associated with an ATR-X phenotype
RT without alpha-thalassemia.";
RL Eur. J. Hum. Genet. 4:316-320(1996).
RN [49]
RP VARIANT MRXHF1 GLN-2131.
RX PubMed=8630485; DOI=10.1038/ng0496-359;
RA Villard L., Gecz J., Mattei J.-F., Fontes M., Saugier-Veber P., Munnich A.,
RA Lyonnet S.;
RT "XNP mutation in a large family with Juberg-Marsidi syndrome.";
RL Nat. Genet. 12:359-360(1996).
RN [50]
RP VARIANTS ATRX.
RX PubMed=9326931; DOI=10.1038/ng1097-146;
RA Gibbons R.J., Bachoo S., Picketts D.J., Aftimos S., Asenbauer B.,
RA Bergoffen J., Berry S.A., Dahl N., Fryer A., Keppler K., Kurosawa K.,
RA Levin M.L., Masuno M., Neri G., Pierpont M.E., Slaney S.F., Higgs D.R.;
RT "Mutations in transcriptional regulator ATRX establish the functional
RT significance of a PHD-like domain.";
RL Nat. Genet. 17:146-148(1997).
RN [51]
RP VARIANT ATRX LEU-246.
RX PubMed=10660327;
RA Fichera M., Romano C., Castiglia L., Failla P., Ruberto C., Amata S.,
RA Greco D., Cardoso C., Fontes M., Ragusa A.;
RT "New mutations in XNP/ATR-X gene: a further contribution to
RT genotype/phenotype relationship in ATR/X syndrome.";
RL Hum. Mutat. 12:214-214(1998).
RN [52]
RP VARIANT ATRX LYS-1742.
RX PubMed=10417298; DOI=10.1086/302499;
RA Lossi A.-M., Millan J.M., Villard L., Orellana C., Cardoso C., Prieto F.,
RA Fontes M., Martinez F.;
RT "Mutation of the XNP/ATR-X gene in a family with severe mental retardation,
RT spastic paraplegia and skewed pattern of X inactivation: demonstration that
RT the mutation is involved in the inactivation bias.";
RL Am. J. Hum. Genet. 65:558-562(1999).
RN [53]
RP VARIANT MRXHF1 THR-2050.
RX PubMed=10398237;
RX DOI=10.1002/(sici)1096-8628(19990730)85:3<249::aid-ajmg12>3.0.co;2-u;
RA Abidi F., Schwartz C.E., Carpenter N.J., Villard L., Fontes M., Curtis M.;
RT "Carpenter-Waziri syndrome results from a mutation in XNP.";
RL Am. J. Med. Genet. 85:249-251(1999).
RN [54]
RP VARIANTS ATRX GLU-175; 178-VAL--LYS-198 DEL; SER-190; PRO-219; LEU-246 AND
RP CYS-249.
RX PubMed=10204841;
RA Villard L., Bonino M.-C., Abidi F., Ragusa A., Belougne J., Lossi A.-M.,
RA Seaver L., Bonnefont J.-P., Romano C., Fichera M., Lacombe D., Hanauer A.,
RA Philip N., Schwartz C.E., Fontes M.;
RT "Evaluation of a mutation screening strategy for sporadic cases of ATR-X
RT syndrome.";
RL J. Med. Genet. 36:183-186(1999).
RN [55]
RP VARIANTS ATRX SER-179; LEU-190; ILE-194; CYS-246; PHE-1552; SER-1645 AND
RP CYS-1847.
RX PubMed=10995512;
RX DOI=10.1002/1096-8628(20000918)94:3<242::aid-ajmg11>3.0.co;2-k;
RA Wada T., Kubota T., Fukushima Y., Saitoh S.;
RT "Molecular genetic study of Japanese patients with X-linked alpha-
RT thalassemia/mental retardation syndrome (ATR-X).";
RL Am. J. Med. Genet. 94:242-248(2000).
RN [56]
RP VARIANT MRXHF1 TYR-220.
RX PubMed=11050622;
RX DOI=10.1002/1096-8628(20001023)94:5<383::aid-ajmg7>3.0.co;2-7;
RA Stevenson R.E., Abidi F., Schwartz C.E., Lubs H.A., Holmes L.B.;
RT "Holmes-Gang syndrome is allelic with XLMR-hypotonic face syndrome.";
RL Am. J. Med. Genet. 94:383-385(2000).
RN [57]
RP VARIANT ATRX MET-1621.
RX PubMed=12116232; DOI=10.1002/ajmg.10446;
RA Yntema H.G., Poppelaars F.A., Derksen E., Oudakker A.R., van Roosmalen T.,
RA Jacobs A., Obbema H., Brunner H.G., Hamel B.C.J., van Bokhoven H.;
RT "Expanding phenotype of XNP mutations: mild to moderate mental
RT retardation.";
RL Am. J. Med. Genet. 110:243-247(2002).
RN [58]
RP VARIANT MRXHF1 GLY-2271.
RX PubMed=16222662; DOI=10.1002/ajmg.a.30990;
RA Leahy R.T., Philip R.K., Gibbons R.J., Fisher C., Suri M., Reardon W.;
RT "Asplenia in ATR-X syndrome: a second report.";
RL Am. J. Med. Genet. A 139:37-39(2005).
RN [59]
RP VARIANT MRXHF1 SER-409.
RX PubMed=15565397; DOI=10.1007/s10048-004-0190-3;
RA Wieland I., Sabathil J., Ostendorf A., Rittinger O., Roepke A.,
RA Winnepenninckx B., Kooy F., Holinski-Feder E., Wieacker P.;
RT "A missense mutation in the coiled-coil motif of the HP1-interacting domain
RT of ATR-X in a family with X-linked mental retardation.";
RL Neurogenetics 6:45-47(2005).
RN [60]
RP VARIANT ATRX CYS-246.
RX PubMed=16955409; DOI=10.1002/ajmg.a.31400;
RA Badens C., Martini N., Courrier S., DesPortes V., Touraine R., Levy N.,
RA Edery P.;
RT "ATRX syndrome in a girl with a heterozygous mutation in the ATRX Zn finger
RT domain and a totally skewed X-inactivation pattern.";
RL Am. J. Med. Genet. A 140:2212-2215(2006).
CC -!- FUNCTION: Involved in transcriptional regulation and chromatin
CC remodeling. Facilitates DNA replication in multiple cellular
CC environments and is required for efficient replication of a subset of
CC genomic loci. Binds to DNA tandem repeat sequences in both telomeres
CC and euchromatin and in vitro binds DNA quadruplex structures. May help
CC stabilizing G-rich regions into regular chromatin structures by
CC remodeling G4 DNA and incorporating H3.3-containing nucleosomes.
CC Catalytic component of the chromatin remodeling complex ATRX:DAXX which
CC has ATP-dependent DNA translocase activity and catalyzes the
CC replication-independent deposition of histone H3.3 in pericentric DNA
CC repeats outside S-phase and telomeres, and the in vitro remodeling of
CC H3.3-containing nucleosomes. Its heterochromatin targeting is proposed
CC to involve a combinatorial readout of histone H3 modifications
CC (specifically methylation states of H3K9 and H3K4) and association with
CC CBX5. Involved in maintaining telomere structural integrity in
CC embryonic stem cells which probably implies recruitment of CBX5 to
CC telomeres. Reports on the involvement in transcriptional regulation of
CC telomeric repeat-containing RNA (TERRA) are conflicting; according to a
CC report, it is not sufficient to decrease chromatin condensation at
CC telomeres nor to increase expression of telomeric RNA in fibroblasts
CC (PubMed:24500201). May be involved in telomere maintenance via
CC recombination in ALT (alternative lengthening of telomeres) cell lines.
CC Acts as negative regulator of chromatin incorporation of
CC transcriptionally repressive histone MACROH2A1, particularily at
CC telomeres and the alpha-globin cluster in erythroleukemic cells.
CC Participates in the allele-specific gene expression at the imprinted
CC IGF2/H19 gene locus. On the maternal allele, required for the chromatin
CC occupancy of SMC1 and CTCTF within the H19 imprinting control region
CC (ICR) and involved in esatblishment of histone tails modifications in
CC the ICR. May be involved in brain development and facial morphogenesis.
CC Binds to zinc-finger coding genes with atypical chromatin signatures
CC and regulates its H3K9me3 levels. Forms a complex with ZNF274, TRIM28
CC and SETDB1 to facilitate the deposition and maintenance of H3K9me3 at
CC the 3' exons of zinc-finger genes (PubMed:27029610).
CC {ECO:0000269|PubMed:12953102, ECO:0000269|PubMed:14990586,
CC ECO:0000269|PubMed:20504901, ECO:0000269|PubMed:20651253,
CC ECO:0000269|PubMed:21029860, ECO:0000269|PubMed:22391447,
CC ECO:0000269|PubMed:22829774, ECO:0000269|PubMed:24500201,
CC ECO:0000269|PubMed:27029610}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Interacts with DAXX to form the chromatin remodeling complex
CC ATRX:DAXX. Probably binds EZH2. Binds annexin V in a calcium and
CC phosphatidylcholine/phosphatidylserine-dependent manner. Interacts
CC directly with CBX5 via the PxVxL motif. Interacts with RAD50, MRE11 and
CC NBN; indicative for an association with the MRN complex. Interacts with
CC histone MACROH2A1. Interacts with histone H3 peptides methylated at
CC 'Lys-10' with preferences H3K9me3 > H3K9me2 > H3K9me1. Interacts with
CC histone H3 peptides unmethylated at 'Lys-5' (H3K4me0). Interacts with
CC MECP2, SMC1 and SMC3. Interacts with SETDB1, TRIM28 and ZNF274
CC (PubMed:27029610). {ECO:0000269|PubMed:10699177,
CC ECO:0000269|PubMed:12953102, ECO:0000269|PubMed:14990586,
CC ECO:0000269|PubMed:15882967, ECO:0000269|PubMed:17296936,
CC ECO:0000269|PubMed:21421568, ECO:0000269|PubMed:21666677,
CC ECO:0000269|PubMed:21666679, ECO:0000269|PubMed:22391447,
CC ECO:0000269|PubMed:24651726, ECO:0000269|PubMed:27029610,
CC ECO:0000269|PubMed:9499421}.
CC -!- INTERACTION:
CC P46100; P45973: CBX5; NbExp=2; IntAct=EBI-396461, EBI-78219;
CC P46100; Q9UER7: DAXX; NbExp=8; IntAct=EBI-396461, EBI-77321;
CC P46100; Q15910: EZH2; NbExp=2; IntAct=EBI-396461, EBI-530054;
CC P46100; O75367-2: MACROH2A1; NbExp=2; IntAct=EBI-396461, EBI-6249599;
CC P46100; Q92878: RAD50; NbExp=5; IntAct=EBI-396461, EBI-495494;
CC P46100; Q00566: Mecp2; Xeno; NbExp=5; IntAct=EBI-396461, EBI-9396907;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. Nucleus, PML body.
CC Note=Associated with pericentromeric heterochromatin during interphase
CC and mitosis, probably by interacting with CBX5/HP1 alpha. Colocalizes
CC with histone H3.3, DAXX, HIRA and ASF1A at PML-nuclear bodies.
CC Colocalizes with cohesin (SMC1 and SMC3) and MECP2 at the maternal H19
CC ICR (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=4;
CC IsoId=P46100-1; Sequence=Displayed;
CC Name=1;
CC IsoId=P46100-2; Sequence=VSP_000575;
CC Name=2;
CC IsoId=P46100-3; Sequence=VSP_000574;
CC Name=3;
CC IsoId=P46100-4; Sequence=VSP_000576;
CC Name=5;
CC IsoId=P46100-5; Sequence=VSP_000574, VSP_000576;
CC Name=6;
CC IsoId=P46100-6; Sequence=VSP_015499, VSP_015500, VSP_015501;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The ADD domain predominantly interacts with histone H3
CC trimethylated at 'Lys-10'(H3K9me3) (and to a lesser extent H3 mono- or
CC dimethylated at 'Lys-10') and simultanously to histone H3 unmethylated
CC at 'Lys-5' (H3K4me0). The interaction with H3K9me3 is disrupted by the
CC presence of H3K4me3 suggesting a readout of the combined histone H3
CC methylation state. {ECO:0000269|PubMed:17609377}.
CC -!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is
CC required for interaction with chromoshadow domains. This motif requires
CC additional residues -7, -6, +4 and +5 of the central Val which contact
CC the chromoshadow domain. {ECO:0000269|PubMed:17609377}.
CC -!- PTM: Phosphorylated at serine residues during mitose. Phosphorylation
CC may promote the release from the nuclear matrix and progression to
CC mitosis. {ECO:0000269|PubMed:10699177}.
CC -!- DISEASE: Alpha-thalassemia/intellectual disability syndrome, X-linked
CC (ATRX) [MIM:301040]: A disorder characterized by severe psychomotor
CC retardation, facial dysmorphism, urogenital abnormalities, and alpha-
CC thalassemia. An essential phenotypic trait are hemoglobin H erythrocyte
CC inclusions. {ECO:0000269|PubMed:10204841, ECO:0000269|PubMed:10417298,
CC ECO:0000269|PubMed:10660327, ECO:0000269|PubMed:10995512,
CC ECO:0000269|PubMed:12116232, ECO:0000269|PubMed:14990586,
CC ECO:0000269|PubMed:16955409, ECO:0000269|PubMed:21421568,
CC ECO:0000269|PubMed:7697714, ECO:0000269|PubMed:8968741,
CC ECO:0000269|PubMed:9043863, ECO:0000269|PubMed:9326931}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Intellectual disability-hypotonic facies syndrome, X-linked, 1
CC (MRXHF1) [MIM:309580]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC MRXSHF1 features include severe intellectual disability, dysmorphic
CC facies, and a highly skewed X-inactivation pattern in carrier women.
CC Other more variable features include hypogonadism, deafness, renal
CC anomalies, and mild skeletal defects. {ECO:0000269|PubMed:10398237,
CC ECO:0000269|PubMed:10751095, ECO:0000269|PubMed:11050622,
CC ECO:0000269|PubMed:15565397, ECO:0000269|PubMed:16222662,
CC ECO:0000269|PubMed:8630485}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Alpha-thalassemia myelodysplasia syndrome (ATMDS)
CC [MIM:300448]: A disorder characterized by hypochromic, microcytic red
CC blood cells, hemoglobin H detected in peripheral blood, and
CC multilineage myelodysplasia. {ECO:0000269|PubMed:12858175}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA20872.1; Type=Miscellaneous discrepancy; Note=Many frameshifts and conflits.; Evidence={ECO:0000305};
CC Sequence=AAC50069.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD92165.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U72937; AAB49970.2; -; mRNA.
DR EMBL; U72938; AAB49971.2; -; mRNA.
DR EMBL; U72935; AAB40698.1; -; Genomic_DNA.
DR EMBL; U72904; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72905; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72907; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72908; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72909; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72910; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72911; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72912; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72913; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72914; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72915; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72916; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72917; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72918; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72919; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72920; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72921; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72922; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72923; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72924; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72925; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72926; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72927; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72928; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72929; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72930; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72931; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72932; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72933; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72934; AAB40698.1; JOINED; Genomic_DNA.
DR EMBL; U72935; AAB40699.1; -; Genomic_DNA.
DR EMBL; U72904; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72907; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72908; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72909; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72910; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72911; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72912; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72913; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72914; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72915; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72916; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72918; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72919; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72920; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72921; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72922; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72923; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72924; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72925; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72926; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72927; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72928; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72929; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72930; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72931; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72932; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72933; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72934; AAB40699.1; JOINED; Genomic_DNA.
DR EMBL; U72936; AAB49969.1; -; mRNA.
DR EMBL; U72935; AAB40700.1; -; Genomic_DNA.
DR EMBL; U72908; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72909; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72910; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72911; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72912; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72913; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72914; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72915; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72916; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72917; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72918; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72920; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72921; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72922; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72923; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72924; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72925; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72926; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72927; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72928; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72929; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72930; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72931; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72932; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72933; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U72934; AAB40700.1; JOINED; Genomic_DNA.
DR EMBL; U75653; AAC51655.1; -; Genomic_DNA.
DR EMBL; U97103; AAC51657.1; -; Genomic_DNA.
DR EMBL; AF000157; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; AF000158; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; AF000159; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; AF000160; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97080; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97081; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97082; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97083; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97084; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97085; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97086; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97087; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97088; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97089; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97090; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97091; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97092; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97093; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97094; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97095; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97096; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97097; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97098; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97099; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97100; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97101; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; U97102; AAC51657.1; JOINED; Genomic_DNA.
DR EMBL; AB102641; BAC81110.1; -; mRNA.
DR EMBL; AB101681; BAC80270.1; -; Genomic_DNA.
DR EMBL; AB101682; BAC80271.1; -; Genomic_DNA.
DR EMBL; AB101683; BAC80272.1; -; Genomic_DNA.
DR EMBL; AB101685; BAC80274.1; -; Genomic_DNA.
DR EMBL; AB101687; BAC80276.1; -; Genomic_DNA.
DR EMBL; AB101689; BAC80278.1; -; Genomic_DNA.
DR EMBL; AB101691; BAC80280.1; -; Genomic_DNA.
DR EMBL; AB101693; BAC80282.1; -; Genomic_DNA.
DR EMBL; AB101695; BAC80284.1; -; Genomic_DNA.
DR EMBL; AB101700; BAC80289.1; -; Genomic_DNA.
DR EMBL; AB101699; BAC80288.1; -; Genomic_DNA.
DR EMBL; AB101698; BAC80287.1; -; Genomic_DNA.
DR EMBL; AB101697; BAC80286.1; -; Genomic_DNA.
DR EMBL; AB101696; BAC80285.1; -; Genomic_DNA.
DR EMBL; AB101694; BAC80283.1; -; Genomic_DNA.
DR EMBL; AB101692; BAC80281.1; -; Genomic_DNA.
DR EMBL; AB101690; BAC80279.1; -; Genomic_DNA.
DR EMBL; AB101688; BAC80277.1; -; Genomic_DNA.
DR EMBL; AB101686; BAC80275.1; -; Genomic_DNA.
DR EMBL; AB101684; BAC80273.1; -; Genomic_DNA.
DR EMBL; AB208928; BAD92165.1; ALT_INIT; mRNA.
DR EMBL; AB209545; BAD92782.1; -; mRNA.
DR EMBL; AL121874; CAB90351.2; -; Genomic_DNA.
DR EMBL; AL121874; CAI40710.1; -; Genomic_DNA.
DR EMBL; AL109753; CAI40710.1; JOINED; Genomic_DNA.
DR EMBL; Z84487; CAI40710.1; JOINED; Genomic_DNA.
DR EMBL; Z84487; CAI42674.1; -; Genomic_DNA.
DR EMBL; AL109753; CAI42674.1; JOINED; Genomic_DNA.
DR EMBL; AL121874; CAI42674.1; JOINED; Genomic_DNA.
DR EMBL; Z84487; CAI42675.1; -; Genomic_DNA.
DR EMBL; AL109753; CAI42675.1; JOINED; Genomic_DNA.
DR EMBL; AL121874; CAI42675.1; JOINED; Genomic_DNA.
DR EMBL; AL109753; CAI43115.1; -; Genomic_DNA.
DR EMBL; AL121874; CAI43115.1; JOINED; Genomic_DNA.
DR EMBL; Z84487; CAI43115.1; JOINED; Genomic_DNA.
DR EMBL; AL109753; CAI43116.1; -; Genomic_DNA.
DR EMBL; AL121874; CAI43116.1; JOINED; Genomic_DNA.
DR EMBL; Z84487; CAI43116.1; JOINED; Genomic_DNA.
DR EMBL; CH471104; EAW98611.1; -; Genomic_DNA.
DR EMBL; CH471104; EAW98615.1; -; Genomic_DNA.
DR EMBL; U09820; AAC50069.1; ALT_FRAME; mRNA.
DR EMBL; L34363; AAA20872.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X83753; CAA58711.1; -; Genomic_DNA.
DR CCDS; CCDS14434.1; -. [P46100-1]
DR CCDS; CCDS14435.1; -. [P46100-4]
DR PIR; I38614; I38614.
DR PIR; I54367; I54367.
DR RefSeq; NP_000480.3; NM_000489.4.
DR RefSeq; NP_612114.2; NM_138270.3.
DR PDB; 2JM1; NMR; -; A=159-296.
DR PDB; 2LBM; NMR; -; A=163-296.
DR PDB; 2LD1; NMR; -; A=163-296.
DR PDB; 3QL9; X-ray; 0.93 A; A=167-289.
DR PDB; 3QLA; X-ray; 1.60 A; A/D=167-289.
DR PDB; 3QLC; X-ray; 2.50 A; A/B=167-289.
DR PDB; 3QLN; X-ray; 1.90 A; A/B=167-289.
DR PDB; 4W5A; X-ray; 2.60 A; A/B/E=167-289.
DR PDB; 5GRQ; X-ray; 1.58 A; C/D=1256-1285.
DR PDB; 5Y18; X-ray; 2.20 A; B=1268-1289.
DR PDB; 5Y6O; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I=1265-1288.
DR PDB; 6G0O; X-ray; 1.40 A; B=1027-1037.
DR PDBsum; 2JM1; -.
DR PDBsum; 2LBM; -.
DR PDBsum; 2LD1; -.
DR PDBsum; 3QL9; -.
DR PDBsum; 3QLA; -.
DR PDBsum; 3QLC; -.
DR PDBsum; 3QLN; -.
DR PDBsum; 4W5A; -.
DR PDBsum; 5GRQ; -.
DR PDBsum; 5Y18; -.
DR PDBsum; 5Y6O; -.
DR PDBsum; 6G0O; -.
DR AlphaFoldDB; P46100; -.
DR BMRB; P46100; -.
DR SMR; P46100; -.
DR BioGRID; 107028; 209.
DR CORUM; P46100; -.
DR DIP; DIP-31532N; -.
DR IntAct; P46100; 51.
DR MINT; P46100; -.
DR STRING; 9606.ENSP00000362441; -.
DR CarbonylDB; P46100; -.
DR GlyGen; P46100; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P46100; -.
DR MetOSite; P46100; -.
DR PhosphoSitePlus; P46100; -.
DR BioMuta; ATRX; -.
DR DMDM; 311033500; -.
DR EPD; P46100; -.
DR jPOST; P46100; -.
DR MassIVE; P46100; -.
DR MaxQB; P46100; -.
DR PaxDb; P46100; -.
DR PeptideAtlas; P46100; -.
DR PRIDE; P46100; -.
DR ProteomicsDB; 55726; -. [P46100-1]
DR ProteomicsDB; 55727; -. [P46100-2]
DR ProteomicsDB; 55728; -. [P46100-3]
DR ProteomicsDB; 55729; -. [P46100-4]
DR ProteomicsDB; 55730; -. [P46100-5]
DR ProteomicsDB; 55731; -. [P46100-6]
DR Antibodypedia; 460; 417 antibodies from 36 providers.
DR DNASU; 546; -.
DR Ensembl; ENST00000373344.11; ENSP00000362441.4; ENSG00000085224.23. [P46100-1]
DR Ensembl; ENST00000395603.7; ENSP00000378967.3; ENSG00000085224.23. [P46100-4]
DR GeneID; 546; -.
DR KEGG; hsa:546; -.
DR MANE-Select; ENST00000373344.11; ENSP00000362441.4; NM_000489.6; NP_000480.3.
DR UCSC; uc004ecp.5; human. [P46100-1]
DR CTD; 546; -.
DR DisGeNET; 546; -.
DR GeneCards; ATRX; -.
DR GeneReviews; ATRX; -.
DR HGNC; HGNC:886; ATRX.
DR HPA; ENSG00000085224; Low tissue specificity.
DR MalaCards; ATRX; -.
DR MIM; 300032; gene.
DR MIM; 300448; phenotype.
DR MIM; 301040; phenotype.
DR MIM; 309580; phenotype.
DR neXtProt; NX_P46100; -.
DR OpenTargets; ENSG00000085224; -.
DR Orphanet; 231401; Alpha-thalassemia-myelodysplastic syndrome.
DR Orphanet; 847; Alpha-thalassemia-X-linked intellectual disability syndrome.
DR Orphanet; 100075; Neuroendocrine tumor of stomach.
DR PharmGKB; PA25179; -.
DR VEuPathDB; HostDB:ENSG00000085224; -.
DR eggNOG; KOG1015; Eukaryota.
DR GeneTree; ENSGT00940000155902; -.
DR HOGENOM; CLU_000863_1_0_1; -.
DR InParanoid; P46100; -.
DR OrthoDB; 815681at2759; -.
DR PhylomeDB; P46100; -.
DR TreeFam; TF313172; -.
DR PathwayCommons; P46100; -.
DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere.
DR Reactome; R-HSA-9670613; Defective Inhibition of DNA Recombination at Telomere Due to DAXX Mutations.
DR Reactome; R-HSA-9670615; Defective Inhibition of DNA Recombination at Telomere Due to ATRX Mutations.
DR SignaLink; P46100; -.
DR SIGNOR; P46100; -.
DR BioGRID-ORCS; 546; 49 hits in 735 CRISPR screens.
DR ChiTaRS; ATRX; human.
DR EvolutionaryTrace; P46100; -.
DR GeneWiki; ATRX; -.
DR GenomeRNAi; 546; -.
DR Pharos; P46100; Tbio.
DR PRO; PR:P46100; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P46100; protein.
DR Bgee; ENSG00000085224; Expressed in endothelial cell and 205 other tissues.
DR ExpressionAtlas; P46100; baseline and differential.
DR Genevisible; P46100; HS.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:BHF-UCL.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IEA:Ensembl.
DR GO; GO:0000792; C:heterochromatin; TAS:ProtInc.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0000228; C:nuclear chromosome; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005721; C:pericentric heterochromatin; ISS:BHF-UCL.
DR GO; GO:0016605; C:PML body; ISS:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0070087; F:chromo shadow domain binding; IPI:BHF-UCL.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0015616; F:DNA translocase activity; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0072711; P:cellular response to hydroxyurea; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IEA:Ensembl.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0006306; P:DNA methylation; TAS:ProtInc.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IMP:UniProtKB.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:0000212; P:meiotic spindle organization; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:1904908; P:negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric; IMP:BHF-UCL.
DR GO; GO:1901581; P:negative regulation of telomeric RNA transcription from RNA pol II promoter; ISS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; ISS:UniProtKB.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; ISS:UniProtKB.
DR GO; GO:1901582; P:positive regulation of telomeric RNA transcription from RNA pol II promoter; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0035128; P:post-embryonic forelimb morphogenesis; IEA:Ensembl.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; ISS:BHF-UCL.
DR GO; GO:1900112; P:regulation of histone H3-K9 trimethylation; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
DR GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
DR GO; GO:0060009; P:Sertoli cell development; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR IDEAL; IID00303; -.
DR InterPro; IPR025766; ADD.
DR InterPro; IPR041430; ADD_ATRX.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF17981; ADD_ATRX; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51533; ADD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Chromatin regulator; Chromosome; Disease variant; DNA damage; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Intellectual disability; Isopeptide bond;
KW Metal-binding; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Telomere; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..2492
FT /note="Transcriptional regulator ATRX"
FT /id="PRO_0000074301"
FT DOMAIN 159..296
FT /note="ADD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT DOMAIN 1581..1768
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 2025..2205
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 170..206
FT /note="GATA-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT ZN_FING 217..272
FT /note="PHD-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1326
FT /note="Interaction with DAXX"
FT REGION 1913..2000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2010..2280
FT /note="Interaction with MECP2"
FT /evidence="ECO:0000269|PubMed:17296936"
FT REGION 2462..2492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 581..594
FT /note="PxVxL motif"
FT MOTIF 1719..1722
FT /note="DEGH box"
FT COMPBIAS 32..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..829
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..1007
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1191
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1468
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1941..1955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1969..1998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2469..2483
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1594..1601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 89
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 591
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 674
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 849
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 889
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 967
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 977
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1011
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70486"
FT MOD_RES 1012
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70486"
FT MOD_RES 1013
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70486"
FT MOD_RES 1061
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1063
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT MOD_RES 1245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT MOD_RES 1253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT MOD_RES 1322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1529
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1906
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT MOD_RES 1913
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT MOD_RES 1992
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1996
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 2220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 2474
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT MOD_RES 2480
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61687"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 623
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 623
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1004
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 1488
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1982
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 1982
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 1987
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..204
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:8968741"
FT /id="VSP_000575"
FT VAR_SEQ 1..117
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:8968741,
FT ECO:0000303|PubMed:9244431"
FT /id="VSP_000574"
FT VAR_SEQ 124..162
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_015499"
FT VAR_SEQ 124..161
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:8968741"
FT /id="VSP_000576"
FT VAR_SEQ 573..601
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_015500"
FT VAR_SEQ 1419..2492
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_015501"
FT VARIANT 175
FT /note="G -> E (in ATRX)"
FT /evidence="ECO:0000269|PubMed:10204841"
FT /id="VAR_012113"
FT VARIANT 178..198
FT /note="Missing (in ATRX)"
FT /evidence="ECO:0000269|PubMed:10204841"
FT /id="VAR_012114"
FT VARIANT 179
FT /note="N -> S (in ATRX; dbSNP:rs398123425)"
FT /evidence="ECO:0000269|PubMed:10995512"
FT /id="VAR_012115"
FT VARIANT 190
FT /note="P -> A (in ATRX; impairs interaction with histone H3
FT peptides and reduces localization to pericentromeric
FT heterochromatin foci; dbSNP:rs122445103)"
FT /evidence="ECO:0000269|PubMed:21666679"
FT /id="VAR_001226"
FT VARIANT 190
FT /note="P -> L (in ATRX; dbSNP:rs1057518708)"
FT /evidence="ECO:0000269|PubMed:10995512"
FT /id="VAR_012116"
FT VARIANT 190
FT /note="P -> S (in ATRX)"
FT /evidence="ECO:0000269|PubMed:10204841"
FT /id="VAR_012117"
FT VARIANT 192
FT /note="L -> F (in ATRX)"
FT /id="VAR_001227"
FT VARIANT 194
FT /note="V -> I (in ATRX)"
FT /evidence="ECO:0000269|PubMed:10995512"
FT /id="VAR_012118"
FT VARIANT 200
FT /note="C -> S (in ATRX)"
FT /id="VAR_001228"
FT VARIANT 219
FT /note="Q -> P (in ATRX; greatly impairs interaction with
FT histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and
FT reduces localization to pericentromeric heterochromatin
FT foci)"
FT /evidence="ECO:0000269|PubMed:10204841,
FT ECO:0000269|PubMed:21666677, ECO:0000269|PubMed:21666679"
FT /id="VAR_012119"
FT VARIANT 220
FT /note="C -> R (in ATRX)"
FT /id="VAR_001229"
FT VARIANT 220
FT /note="C -> Y (in MRXHF1; dbSNP:rs122445111)"
FT /evidence="ECO:0000269|PubMed:11050622"
FT /id="VAR_032625"
FT VARIANT 222
FT /note="W -> S (in ATRX)"
FT /id="VAR_001230"
FT VARIANT 243
FT /note="C -> F (in ATRX)"
FT /id="VAR_001231"
FT VARIANT 246
FT /note="R -> C (in ATRX; impairs interaction with histone H3
FT peptides trimethylated at 'Lys-10' (H3K9me3) and reduces
FT localization to pericentromeric heterochromatin foci;
FT dbSNP:rs122445105)"
FT /evidence="ECO:0000269|PubMed:10995512,
FT ECO:0000269|PubMed:16955409, ECO:0000269|PubMed:21421568,
FT ECO:0000269|PubMed:21666679"
FT /id="VAR_001232"
FT VARIANT 246
FT /note="R -> L (in ATRX; impairs interaction with histone H3
FT peptides trimethylated at 'Lys-10' (H3K9me3))"
FT /evidence="ECO:0000269|PubMed:10204841,
FT ECO:0000269|PubMed:10660327, ECO:0000269|PubMed:21421568"
FT /id="VAR_010914"
FT VARIANT 249
FT /note="G -> C (in ATRX)"
FT /evidence="ECO:0000269|PubMed:10204841"
FT /id="VAR_012120"
FT VARIANT 249
FT /note="G -> D (in ATRX; impairs interaction with histone H3
FT peptides trimethylated at 'Lys-10' (H3K9me3); loss of
FT heterochromatic localization)"
FT /evidence="ECO:0000269|PubMed:21421568"
FT /id="VAR_001233"
FT VARIANT 409
FT /note="L -> S (in MRXHF1; dbSNP:rs122445109)"
FT /evidence="ECO:0000269|PubMed:15565397"
FT /id="VAR_032626"
FT VARIANT 545
FT /note="Q -> E (in dbSNP:rs35738915)"
FT /id="VAR_055939"
FT VARIANT 596
FT /note="S -> P (in dbSNP:rs1051678)"
FT /evidence="ECO:0000269|PubMed:9244431"
FT /id="VAR_016914"
FT VARIANT 740
FT /note="E -> G (in dbSNP:rs1051680)"
FT /evidence="ECO:0000269|PubMed:9244431"
FT /id="VAR_016915"
FT VARIANT 929
FT /note="E -> Q (in dbSNP:rs3088074)"
FT /id="VAR_023438"
FT VARIANT 1538
FT /note="V -> G (in ATRX; unknown pathological significance)"
FT /id="VAR_012121"
FT VARIANT 1552
FT /note="V -> F (in ATRX)"
FT /evidence="ECO:0000269|PubMed:10995512"
FT /id="VAR_012122"
FT VARIANT 1609
FT /note="H -> R (in ATRX; dbSNP:rs122445093)"
FT /id="VAR_001234"
FT VARIANT 1614
FT /note="C -> R (in ATRX; dbSNP:rs122445094)"
FT /id="VAR_001235"
FT VARIANT 1621
FT /note="T -> M (in ATRX; dbSNP:rs122445106)"
FT /evidence="ECO:0000269|PubMed:12116232"
FT /id="VAR_016916"
FT VARIANT 1645
FT /note="L -> S (in ATRX)"
FT /evidence="ECO:0000269|PubMed:10995512"
FT /id="VAR_012123"
FT VARIANT 1650
FT /note="K -> N (in ATRX; dbSNP:rs122445095)"
FT /id="VAR_001236"
FT VARIANT 1713
FT /note="P -> S (in ATRX; without alpha-thalassemia)"
FT /evidence="ECO:0000269|PubMed:9043863"
FT /id="VAR_012124"
FT VARIANT 1742
FT /note="R -> K (in ATRX; atypical; patients presents spastic
FT paraplegia at birth; dbSNP:rs122445104)"
FT /evidence="ECO:0000269|PubMed:10417298"
FT /id="VAR_012125"
FT VARIANT 1847
FT /note="Y -> C (in ATRX)"
FT /evidence="ECO:0000269|PubMed:10995512"
FT /id="VAR_012126"
FT VARIANT 1860
FT /note="N -> S (in dbSNP:rs45439799)"
FT /evidence="ECO:0000269|PubMed:8968741"
FT /id="VAR_001237"
FT VARIANT 2035
FT /note="D -> V (in ATRX; impairs ATPase activity;
FT dbSNP:rs122445096)"
FT /evidence="ECO:0000269|PubMed:14990586"
FT /id="VAR_001238"
FT VARIANT 2050
FT /note="I -> T (in MRXHF1; originally reported as Carpenter-
FT Waziri syndrome; dbSNP:rs122445110)"
FT /evidence="ECO:0000269|PubMed:10398237"
FT /id="VAR_012127"
FT VARIANT 2084
FT /note="Y -> H (in ATRX; impairs ATPase activity;
FT dbSNP:rs122445097)"
FT /evidence="ECO:0000269|PubMed:14990586"
FT /id="VAR_001239"
FT VARIANT 2131
FT /note="R -> Q (in MRXHF1; originally reported as Juberg-
FT Marsidi syndrome; dbSNP:rs122445101)"
FT /evidence="ECO:0000269|PubMed:8630485"
FT /id="VAR_001240"
FT VARIANT 2163
FT /note="Y -> C (in ATRX; dbSNP:rs122445098)"
FT /id="VAR_001241"
FT VARIANT 2271
FT /note="R -> G (in MRXHF1; dbSNP:rs122445112)"
FT /evidence="ECO:0000269|PubMed:16222662"
FT /id="VAR_032627"
FT MUTAGEN 189
FT /note="H->N: Impairs interaction with histone H3 peptides
FT and reduces localization to pericentromeric heterochromatin
FT foci."
FT /evidence="ECO:0000269|PubMed:21666679"
FT MUTAGEN 203
FT /note="Y->A,K: Impairs interaction with histone H3 peptides
FT trimethylated at 'Lys-10' (H3K9me3); loss of
FT heterochromatic localization."
FT /evidence="ECO:0000269|PubMed:21421568,
FT ECO:0000269|PubMed:21666677, ECO:0000269|PubMed:21666679"
FT MUTAGEN 204
FT /note="Y->A: Impairs interaction with histone H3 peptides
FT trimethylated at 'Lys-10' (H3K9me3) and reduces
FT localization to pericentromeric heterochromatin foci."
FT /evidence="ECO:0000269|PubMed:21421568,
FT ECO:0000269|PubMed:21666679"
FT MUTAGEN 207
FT /note="D->A: Impairs interaction with histone H3 peptides
FT trimethylated at 'Lys-10' (H3K9me3) and reduces
FT localization to pericentromeric heterochromatin foci."
FT MUTAGEN 209
FT /note="I->A: Impairs interaction with histone H3 peptides
FT trimethylated at 'Lys-10' (H3K9me3)."
FT /evidence="ECO:0000269|PubMed:21421568"
FT MUTAGEN 214
FT /note="D->A: Impairs interaction with histone H3 peptides
FT trimethylated at 'Lys-10' (H3K9me3)."
FT /evidence="ECO:0000269|PubMed:21421568"
FT MUTAGEN 217
FT /note="D->A: Impairs interaction with histone H3 peptides
FT trimethylated at 'Lys-10' (H3K9me3); loss of
FT heterochromatic localization."
FT /evidence="ECO:0000269|PubMed:21421568,
FT ECO:0000269|PubMed:21666679"
FT MUTAGEN 218
FT /note="E->A: Impairs interaction with histone H3 peptides
FT unmethylated at 'Lys-5' (H3K4me0); reduces pericentromeric
FT localization."
FT /evidence="ECO:0000269|PubMed:21666677"
FT MUTAGEN 252
FT /note="E->L: Impairs interaction with histone H3 peptides
FT and reduces localization to pericentromeric heterochromatin
FT foci."
FT /evidence="ECO:0000269|PubMed:21666679"
FT MUTAGEN 1600
FT /note="K->R: Abolishes ATPAse activity, no effect on
FT pericentromeric heterochromatin localization."
FT /evidence="ECO:0000269|PubMed:14990586,
FT ECO:0000269|PubMed:21666679"
FT CONFLICT 879
FT /note="A -> R (in Ref. 7; AAC50069)"
FT /evidence="ECO:0000305"
FT CONFLICT 1286
FT /note="S -> P (in Ref. 4; BAD92165)"
FT /evidence="ECO:0000305"
FT CONFLICT 1627
FT /note="P -> L (in Ref. 7; AAC50069)"
FT /evidence="ECO:0000305"
FT CONFLICT 1632
FT /note="L -> F (in Ref. 7; AAC50069)"
FT /evidence="ECO:0000305"
FT CONFLICT 2280
FT /note="A -> G (in Ref. 7; AAC50069)"
FT /evidence="ECO:0000305"
FT CONFLICT 2283..2284
FT /note="KG -> RV (in Ref. 7; AAC50069)"
FT /evidence="ECO:0000305"
FT CONFLICT 2436
FT /note="L -> H (in Ref. 7; AAC50069)"
FT /evidence="ECO:0000305"
FT CONFLICT 2442
FT /note="P -> R (in Ref. 7; AAC50069)"
FT /evidence="ECO:0000305"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:3QL9"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:2LBM"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:2LBM"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:3QL9"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:3QL9"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:3QL9"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:3QL9"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:3QL9"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:2JM1"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:2JM1"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3QL9"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:3QL9"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:3QL9"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:3QL9"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:3QL9"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:3QL9"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:3QL9"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:2JM1"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:3QL9"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:3QL9"
FT HELIX 274..284
FT /evidence="ECO:0007829|PDB:3QL9"
FT HELIX 1267..1282
FT /evidence="ECO:0007829|PDB:5GRQ"
SQ SEQUENCE 2492 AA; 282587 MW; 938F82D6D6F99805 CRC64;
MTAEPMSESK LNTLVQKLHD FLAHSSEESE ETSSPPRLAM NQNTDKISGS GSNSDMMENS
KEEGTSSSEK SKSSGSSRSK RKPSIVTKYV ESDDEKPLDD ETVNEDASNE NSENDITMQS
LPKGTVIVQP EPVLNEDKDD FKGPEFRSRS KMKTENLKKR GEDGLHGIVS CTACGQQVNH
FQKDSIYRHP SLQVLICKNC FKYYMSDDIS RDSDGMDEQC RWCAEGGNLI CCDFCHNAFC
KKCILRNLGR KELSTIMDEN NQWYCYICHP EPLLDLVTAC NSVFENLEQL LQQNKKKIKV
DSEKSNKVYE HTSRFSPKKT SSNCNGEEKK LDDSCSGSVT YSYSALIVPK EMIKKAKKLI
ETTANMNSSY VKFLKQATDN SEISSATKLR QLKAFKSVLA DIKKAHLALE EDLNSEFRAM
DAVNKEKNTK EHKVIDAKFE TKARKGEKPC ALEKKDISKS EAKLSRKQVD SEHMHQNVPT
EEQRTNKSTG GEHKKSDRKE EPQYEPANTS EDLDMDIVSV PSSVPEDIFE NLETAMEVQS
SVDHQGDGSS GTEQEVESSS VKLNISSKDN RGGIKSKTTA KVTKELYVKL TPVSLSNSPI
KGADCQEVPQ DKDGYKSCGL NPKLEKCGLG QENSDNEHLV ENEVSLLLEE SDLRRSPRVK
TTPLRRPTET NPVTSNSDEE CNETVKEKQK LSVPVRKKDK RNSSDSAIDN PKPNKLPKSK
QSETVDQNSD SDEMLAILKE VSRMSHSSSS DTDINEIHTN HKTLYDLKTQ AGKDDKGKRK
RKSSTSGSDF DTKKGKSAKS SIISKKKRQT QSESSNYDSE LEKEIKSMSK IGAARTTKKR
IPNTKDFDSS EDEKHSKKGM DNQGHKNLKT SQEGSSDDAE RKQERETFSS AEGTVDKDTT
IMELRDRLPK KQQASASTDG VDKLSGKEES FTSLEVRKVA ETKEKSKHLK TKTCKKVQDG
LSDIAEKFLK KDQSDETSED DKKQSKKGTE EKKKPSDFKK KVIKMEQQYE SSSDGTEKLP
EREEICHFPK GIKQIKNGTT DGEKKSKKIR DKTSKKKDEL SDYAEKSTGK GDSCDSSEDK
KSKNGAYGRE KKRCKLLGKS SRKRQDCSSS DTEKYSMKED GCNSSDKRLK RIELRERRNL
SSKRNTKEIQ SGSSSSDAEE SSEDNKKKKQ RTSSKKKAVI VKEKKRNSLR TSTKRKQADI
TSSSSSDIED DDQNSIGEGS SDEQKIKPVT ENLVLSSHTG FCQSSGDEAL SKSVPVTVDD
DDDDNDPENR IAKKMLLEEI KANLSSDEDG SSDDEPEEGK KRTGKQNEEN PGDEEAKNQV
NSESDSDSEE SKKPRYRHRL LRHKLTVSDG ESGEEKKTKP KEHKEVKGRN RRKVSSEDSE
DSDFQESGVS EEVSESEDEQ RPRTRSAKKA ELEENQRSYK QKKKRRRIKV QEDSSSENKS
NSEEEEEEKE EEEEEEEEEE EEEEDENDDS KSPGKGRKKI RKILKDDKLR TETQNALKEE
EERRKRIAER EREREKLREV IEIEDASPTK CPITTKLVLD EDEETKEPLV QVHRNMVIKL
KPHQVDGVQF MWDCCCESVK KTKKSPGSGC ILAHCMGLGK TLQVVSFLHT VLLCDKLDFS
TALVVCPLNT ALNWMNEFEK WQEGLKDDEK LEVSELATVK RPQERSYMLQ RWQEDGGVMI
IGYEMYRNLA QGRNVKSRKL KEIFNKALVD PGPDFVVCDE GHILKNEASA VSKAMNSIRS
RRRIILTGTP LQNNLIEYHC MVNFIKENLL GSIKEFRNRF INPIQNGQCA DSTMVDVRVM
KKRAHILYEM LAGCVQRKDY TALTKFLPPK HEYVLAVRMT SIQCKLYQYY LDHLTGVGNN
SEGGRGKAGA KLFQDFQMLS RIWTHPWCLQ LDYISKENKG YFDEDSMDEF IASDSDETSM
SLSSDDYTKK KKKGKKGKKD SSSSGSGSDN DVEVIKVWNS RSRGGGEGNV DETGNNPSVS
LKLEESKATS SSNPSSPAPD WYKDFVTDAD AEVLEHSGKM VLLFEILRMA EEIGDKVLVF
SQSLISLDLI EDFLELASRE KTEDKDKPLI YKGEGKWLRN IDYYRLDGST TAQSRKKWAE
EFNDETNVRG RLFIISTKAG SLGINLVAAN RVIIFDASWN PSYDIQSIFR VYRFGQTKPV
YVYRFLAQGT MEDKIYDRQV TKQSLSFRVV DQQQVERHFT MNELTELYTF EPDLLDDPNS
EKKKKRDTPM LPKDTILAEL LQIHKEHIVG YHEHDSLLDH KEEEELTEEE RKAAWAEYEA
EKKGLTMRFN IPTGTNLPPV SFNSQTPYIP FNLGALSAMS NQQLEDLINQ GREKVVEATN
SVTAVRIQPL EDIISAVWKE NMNLSEAQVQ ALALSRQASQ ELDVKRREAI YNDVLTKQQM
LISCVQRILM NRRLQQQYNQ QQQQQMTYQQ ATLGHLMMPK PPNLIMNPSN YQQIDMRGMY
QPVAGGMQPP PLQRAPPPMR SKNPGPSQGK SM
