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 27-MAR-2024, entry version 243. 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 GLY-1538; ARG-1609; ARG-1614; ASN-1650; VAL-2035; RP HIS-2084; GLN-2131 AND CYS-2163. 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 ARG-1609; RP ARG-1614; ASN-1650; SER-1860; VAL-2035; HIS-2084 AND CYS-2163. 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>3.3.co;2-e; 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 ALA-190; PHE-192; SER-200; ARG-220; SER-222; PHE-243; CYS-246 RP AND ASP-249. 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>3.3.co;2-b; 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 a 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/impaired intellectual development syndrome, CC X-linked (ATRX) [MIM:301040]: A disorder characterized by severe CC psychomotor retardation, facial dysmorphism, urogenital abnormalities, CC and alpha-thalassemia. An essential phenotypic trait are hemoglobin H CC erythrocyte inclusions. {ECO:0000269|PubMed:10204841, CC ECO:0000269|PubMed:10417298, ECO:0000269|PubMed:10660327, CC ECO:0000269|PubMed:10995512, ECO:0000269|PubMed:12116232, CC ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:16955409, CC ECO:0000269|PubMed:21421568, ECO:0000269|PubMed:7697714, CC ECO:0000269|PubMed:8968741, ECO:0000269|PubMed:9043863, CC ECO:0000269|PubMed:9326931}. Note=The disease is caused by variants CC affecting the gene represented in this 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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. [P46100-1] DR RefSeq; NP_612114.2; NM_138270.3. [P46100-4] 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; 254. DR CORUM; P46100; -. DR DIP; DIP-31532N; -. DR IntAct; P46100; 56. DR MINT; P46100; -. DR STRING; 9606.ENSP00000362441; -. DR CarbonylDB; P46100; -. DR GlyCosmos; P46100; 1 site, 1 glycan. DR GlyGen; P46100; 21 sites, 1 O-linked glycan (21 sites). DR iPTMnet; P46100; -. DR MetOSite; P46100; -. DR PhosphoSitePlus; P46100; -. DR SwissPalm; P46100; -. DR BioMuta; ATRX; -. DR DMDM; 311033500; -. DR EPD; P46100; -. DR jPOST; P46100; -. DR MassIVE; P46100; -. DR MaxQB; P46100; -. DR PaxDb; 9606-ENSP00000362441; -. DR PeptideAtlas; 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 Pumba; P46100; -. DR Antibodypedia; 460; 486 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 AGR; HGNC:886; -. 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; 96253; Cushing disease. 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 OMA; QEMGGVM; -. DR OrthoDB; 12329at2759; -. 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; 53 hits in 823 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 207 other cell types or tissues. DR ExpressionAtlas; P46100; baseline and differential. 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:0015616; F:DNA translocase activity; IDA:UniProtKB. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. 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:0006325; P:chromatin organization; IMP: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: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: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: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:0006355; P:regulation of DNA-templated transcription; 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:0031509; P:subtelomeric heterochromatin formation; IMP:BHF-UCL. DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl. DR CDD; cd11726; ADDz_ATRX; 1. DR CDD; cd18068; DEXHc_ATRX; 1. DR CDD; cd18793; SF2_C_SNF; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR049730; SNF2/RAD54-like_C. DR InterPro; IPR000330; SNF2_N. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR46357; TRANSCRIPTIONAL REGULATOR ATRX; 1. DR PANTHER; PTHR46357:SF1; TRANSCRIPTIONAL REGULATOR ATRX; 1. 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; SSF57903; FYVE/PHD zinc finger; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS51533; ADD; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR Genevisible; P46100; HS. 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 ECO:0000269|PubMed:9326931" 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 /evidence="ECO:0000269|PubMed:9326931" 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 /evidence="ECO:0000269|PubMed:9326931" 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 /evidence="ECO:0000269|PubMed:9326931" 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 /evidence="ECO:0000269|PubMed:9326931" FT /id="VAR_001230" FT VARIANT 243 FT /note="C -> F (in ATRX)" FT /evidence="ECO:0000269|PubMed:9326931" 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, ECO:0000269|PubMed:9326931" 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 dbSNP:rs1603226766)" 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 ECO:0000269|PubMed:9326931" 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; uncertain significance)" FT /evidence="ECO:0000269|PubMed:8968741" FT /id="VAR_012121" FT VARIANT 1552 FT /note="V -> F (in ATRX; dbSNP:rs1602995714)" FT /evidence="ECO:0000269|PubMed:10995512" FT /id="VAR_012122" FT VARIANT 1609 FT /note="H -> R (in ATRX; dbSNP:rs122445093)" FT /evidence="ECO:0000269|PubMed:7697714, FT ECO:0000269|PubMed:8968741" FT /id="VAR_001234" FT VARIANT 1614 FT /note="C -> R (in ATRX; dbSNP:rs122445094)" FT /evidence="ECO:0000269|PubMed:7697714, FT ECO:0000269|PubMed:8968741" 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 /evidence="ECO:0000269|PubMed:7697714, FT ECO:0000269|PubMed:8968741" 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 ATRX; dbSNP:rs45439799)" FT /evidence="ECO:0000269|PubMed:7697714, FT 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 ECO:0000269|PubMed:7697714, ECO:0000269|PubMed:8968741" FT /id="VAR_001238" FT VARIANT 2050 FT /note="I -> T (in MRXHF1; originally reported as FT Carpenter-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 ECO:0000269|PubMed:7697714, ECO:0000269|PubMed:8968741" FT /id="VAR_001239" FT VARIANT 2131 FT /note="R -> Q (in MRXHF1 and ATRX; originally reported as FT Juberg-Marsidi syndrome; dbSNP:rs122445101)" FT /evidence="ECO:0000269|PubMed:8630485, FT ECO:0000269|PubMed:8968741" FT /id="VAR_001240" FT VARIANT 2163 FT /note="Y -> C (in ATRX; dbSNP:rs122445098)" FT /evidence="ECO:0000269|PubMed:7697714, FT ECO:0000269|PubMed:8968741" 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 //