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Transcriptional regulator ATRX (EC 3.6.4.12) (ATP-dependent helicase ATRX) (X-linked helicase II) (X-linked nuclear protein) (XNP) (Znf-HX)

 ATRX_HUMAN              Reviewed;        2492 AA.
P46100; D3DTE2; P51068; Q15886; Q59FB5; Q59H31; Q5H9A2; Q5JWI4;
Q7Z2J1; Q9H0Z1; Q9NTS3;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 5.
20-DEC-2017, entry version 201.
RecName: Full=Transcriptional regulator ATRX;
EC=3.6.4.12;
AltName: Full=ATP-dependent helicase ATRX;
AltName: Full=X-linked helicase II;
AltName: Full=X-linked nuclear protein;
Short=XNP;
AltName: Full=Znf-HX;
Name=ATRX; Synonyms=RAD54L, XH2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), VARIANT
SER-1860, AND VARIANTS ATRX.
PubMed=8968741; DOI=10.1093/hmg/5.12.1899;
Picketts D.J., Higgs D.R., Bachoo S., Blake D.J., Quarrell O.W.J.,
Gibbons R.J.;
"ATRX encodes a novel member of the SNF2 family of proteins: mutations
point to a common mechanism underlying the ATR-X syndrome.";
Hum. Mol. Genet. 5:1899-1907(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), AND VARIANTS PRO-596
AND GLY-740.
PubMed=9244431; DOI=10.1006/geno.1997.4793;
Villard L., Lossi A.-M., Cardoso C., Proud V., Chiaroni P.,
Colleaux L., Schwartz C., Fontes M.;
"Determination of the genomic structure of the XNP/ATRX gene encoding
a potential zinc finger helicase.";
Genomics 43:149-155(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF
163-198.
PubMed=12777533; DOI=10.1093/molbev/msg134;
Kitano T., Schwarz C., Nickel B., Paeaebo S.;
"Gene diversity patterns at 10 X-chromosomal loci in humans and
chimpanzees.";
Mol. Biol. Evol. 20:1281-1289(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 704-1927 (ISOFORMS 1/2/3/4/5), AND
VARIANT GLU-929.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 860-2492.
PubMed=7874112; DOI=10.1093/hmg/3.11.1957;
Stayton C.L., Dabovic B., Gulisano M., Gecz J., Broccoli V.,
Giovanazzi S., Bossolasco M., Monaco L., Rastan S., Boncinelli E.,
Bianchi M.E., Consalez G.G.;
"Cloning and characterization of a new human Xq13 gene, encoding a
putative helicase.";
Hum. Mol. Genet. 3:1957-1964(1994).
[8]
PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8162050; DOI=10.1093/hmg/3.1.39;
Gecz J., Pollard H., Consalez G., Villard L., Stayton C.L.,
Millasseau P., Khrestchatisky M., Fontes M.;
"Cloning and expression of the murine homologue of a putative human X-
linked nuclear protein gene closely linked to PGK1 in Xq13.3.";
Hum. Mol. Genet. 3:39-44(1994).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2401-2492, AND VARIANTS ATRX.
PubMed=7697714; DOI=10.1016/0092-8674(95)90287-2;
Gibbons R.J., Picketts D.J., Villard L., Higgs D.R.;
"Mutations in a putative global transcriptional regulator cause X-
linked mental retardation with alpha-thalassemia (ATR-X syndrome).";
Cell 80:837-845(1995).
[10]
INTERACTION WITH EZH2.
PubMed=9499421; DOI=10.1093/hmg/7.4.679;
Cardoso C., Timsit S., Villard L., Khrestchatisky M., Fontes M.,
Colleaux L.;
"Specific interaction between the XNP/ATR-X gene product and the SET
domain of the human EZH2 protein.";
Hum. Mol. Genet. 7:679-684(1998).
[11]
SUBCELLULAR LOCATION, AND ASSOCIATION WITH PERICENTROMERIC
HETEROCHROMATIN.
PubMed=10570185; DOI=10.1073/pnas.96.24.13983;
McDowell T.L., Gibbons R.J., Sutherland H., O'Rourke D.M.,
Bickmore W.A., Pombo A., Turley H., Gatter K., Picketts D.J.,
Buckle V.J., Chapman L., Rhodes D., Higgs D.R.;
"Localization of a putative transcriptional regulator (ATRX) at
pericentromeric heterochromatin and the short arms of acrocentric
chromosomes.";
Proc. Natl. Acad. Sci. U.S.A. 96:13983-13988(1999).
[12]
INVOLVEMENT IN MRXSHF1.
PubMed=10751095;
DOI=10.1002/(SICI)1096-8628(20000306)91:1<83::AID-AJMG15>3.0.CO;2-N;
Villard L., Fontes M., Ades L.C., Gecz J.;
"Identification of a mutation in the XNP/ATR-X gene in a family
reported as Smith-Fineman-Myers syndrome.";
Am. J. Med. Genet. 91:83-85(2000).
[13]
INTERACTION WITH CBX5, AND PHOSPHORYLATION.
PubMed=10699177; DOI=10.1093/hmg/9.4.539;
Berube N.G., Smeenk C.A., Picketts D.J.;
"Cell cycle-dependent phosphorylation of the ATRX protein correlates
with changes in nuclear matrix and chromatin association.";
Hum. Mol. Genet. 9:539-547(2000).
[14]
INVOLVEMENT IN ATMDS.
PubMed=12858175; DOI=10.1038/ng1213;
Gibbons R.J., Pellagatti A., Garrick D., Wood W.G., Malik N.,
Ayyub H., Langford C., Boultwood J., Wainscoat J.S., Higgs D.R.;
"Identification of acquired somatic mutations in the gene encoding
chromatin-remodeling factor ATRX in the alpha-thalassemia
myelodysplasia syndrome (ATMDS).";
Nat. Genet. 34:446-449(2003).
[15]
FUNCTION, INTERACTION WITH DAXX, AND SUBCELLULAR LOCATION.
PubMed=12953102; DOI=10.1073/pnas.1937626100;
Xue Y., Gibbons R., Yan Z., Yang D., McDowell T.L., Sechi S., Qin J.,
Zhou S., Higgs D., Wang W.;
"The ATRX syndrome protein forms a chromatin-remodeling complex with
Daxx and localizes in promyelocytic leukemia nuclear bodies.";
Proc. Natl. Acad. Sci. U.S.A. 100:10635-10640(2003).
[16]
FUNCTION, INTERACTION WITH DAXX, SUBCELLULAR LOCATION, MUTAGENESIS OF
LYS-1600, AND CHARACTERIZATION OF VARIANTS ATRX VAL-2035 AND HIS-2084.
PubMed=14990586; DOI=10.1074/jbc.M401321200;
Tang J., Wu S., Liu H., Stratt R., Barak O.G., Shiekhattar R.,
Picketts D.J., Yang X.;
"A novel transcription regulatory complex containing death domain-
associated protein and the ATR-X syndrome protein.";
J. Biol. Chem. 279:20369-20377(2004).
[17]
INTERACTION WITH CBX5.
PubMed=15882967; DOI=10.1016/j.bbrc.2005.04.016;
Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III;
"The mammalian heterochromatin protein 1 binds diverse nuclear
proteins through a common motif that targets the chromoshadow
domain.";
Biochem. Biophys. Res. Commun. 331:929-937(2005).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634 AND SER-1352, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[19]
INTERACTION WITH MECP2.
PubMed=17296936; DOI=10.1073/pnas.0608056104;
Nan X., Hou J., Maclean A., Nasir J., Lafuente M.J., Shu X.,
Kriaucionis S., Bird A.;
"Interaction between chromatin proteins MECP2 and ATRX is disrupted by
mutations that cause inherited mental retardation.";
Proc. Natl. Acad. Sci. U.S.A. 104:2709-2714(2007).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594; THR-674; SER-675;
SER-677; SER-729; SER-731; SER-875; SER-876; SER-1348; SER-1352;
SER-1996 AND SER-2220, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; TYR-89; SER-112 AND
SER-1996, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-967, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[25]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21029860; DOI=10.1016/j.cell.2010.09.023;
Law M.J., Lower K.M., Voon H.P., Hughes J.R., Garrick D.,
Viprakasit V., Mitson M., De Gobbi M., Marra M., Morris A., Abbott A.,
Wilder S.P., Taylor S., Santos G.M., Cross J., Ayyub H., Jones S.,
Ragoussis J., Rhodes D., Dunham I., Higgs D.R., Gibbons R.J.;
"ATR-X syndrome protein targets tandem repeats and influences allele-
specific expression in a size-dependent manner.";
Cell 143:367-378(2010).
[26]
ASSOCIATION WITH HISTONE H3.3.
PubMed=20211137; DOI=10.1016/j.cell.2010.01.003;
Goldberg A.D., Banaszynski L.A., Noh K.M., Lewis P.W., Elsaesser S.J.,
Stadler S., Dewell S., Law M., Guo X., Li X., Wen D., Chapgier A.,
DeKelver R.C., Miller J.C., Lee Y.L., Boydston E.A., Holmes M.C.,
Gregory P.D., Greally J.M., Rafii S., Yang C., Scambler P.J.,
Garrick D., Gibbons R.J., Higgs D.R., Cristea I.M., Urnov F.D.,
Zheng D., Allis C.D.;
"Distinct factors control histone variant H3.3 localization at
specific genomic regions.";
Cell 140:678-691(2010).
[27]
FUNCTION.
PubMed=20504901; DOI=10.1101/gad.566910;
Drane P., Ouararhni K., Depaux A., Shuaib M., Hamiche A.;
"The death-associated protein DAXX is a novel histone chaperone
involved in the replication-independent deposition of H3.3.";
Genes Dev. 24:1253-1265(2010).
[28]
FUNCTION OF THE ATRX:DAXX COMPLEX.
PubMed=20651253; DOI=10.1073/pnas.1008850107;
Lewis P.W., Elsaesser S.J., Noh K.M., Stadler S.C., Allis C.D.;
"Daxx is an H3.3-specific histone chaperone and cooperates with ATRX
in replication-independent chromatin assembly at telomeres.";
Proc. Natl. Acad. Sci. U.S.A. 107:14075-14080(2010).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; THR-591; SER-598;
SER-1061; TYR-1063; SER-1348; SER-1352; SER-1527; SER-1992; SER-1996
AND SER-2220, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[31]
INTERACTION WITH TRIMETHYLATED HISTONE H3 'LYS-9', CHARACTERIZATION OF
VARIANTS ATRX CYS-246; LEU-246 AND ASP-249, AND MUTAGENESIS OF
TYR-203; TYR-204; ILE-209; ASP-214 AND ASP-217.
PubMed=21421568; DOI=10.1093/hmg/ddr107;
Dhayalan A., Tamas R., Bock I., Tattermusch A., Dimitrova E.,
Kudithipudi S., Ragozin S., Jeltsch A.;
"The ATRX-ADD domain binds to H3 tail peptides and reads the combined
methylation state of K4 and K9.";
Hum. Mol. Genet. 20:2195-2203(2011).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598; SER-889; SER-1061;
SER-1322; SER-1324; SER-1326; SER-1348 AND SER-1352, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[33]
FUNCTION, AND INTERACTION WITH HISTONE H2AFY.
PubMed=22391447; DOI=10.1101/gad.179416.111;
Ratnakumar K., Duarte L.F., LeRoy G., Hasson D., Smeets D.,
Vardabasso C., Bonisch C., Zeng T., Xiang B., Zhang D.Y., Li H.,
Wang X., Hake S.B., Schermelleh L., Garcia B.A., Bernstein E.;
"ATRX-mediated chromatin association of histone variant macroH2A1
regulates alpha-globin expression.";
Genes Dev. 26:433-438(2012).
[34]
FUNCTION.
PubMed=22829774; DOI=10.1371/journal.pgen.1002772;
Lovejoy C.A., Li W., Reisenweber S., Thongthip S., Bruno J.,
de Lange T., De S., Petrini J.H., Sung P.A., Jasin M., Rosenbluh J.,
Zwang Y., Weir B.A., Hatton C., Ivanova E., Macconaill L., Hanna M.,
Hahn W.C., Lue N.F., Reddel R.R., Jiao Y., Kinzler K., Vogelstein B.,
Papadopoulos N., Meeker A.K.;
"Loss of ATRX, genome instability, and an altered DNA damage response
are hallmarks of the alternative lengthening of telomeres pathway.";
PLoS Genet. 8:E1002772-E1002772(2012).
[35]
SUBCELLULAR LOCATION.
PubMed=23222847; DOI=10.1101/gr.142703.112;
Delbarre E., Ivanauskiene K., Kuntziger T., Collas P.;
"DAXX-dependent supply of soluble (H3.3-H4) dimers to PML bodies
pending deposition into chromatin.";
Genome Res. 23:440-451(2013).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-34; SER-316;
SER-677; SER-729; SER-731; SER-819; SER-849; SER-850; SER-889;
SER-962; SER-1061; SER-1348; SER-1352; SER-1527 AND THR-1529, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-598; SER-675;
SER-974 AND THR-977, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-299; LYS-438; LYS-1004;
LYS-1488 AND LYS-1982, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[39]
FUNCTION.
PubMed=24500201; DOI=10.1093/nar/gku114;
Episkopou H., Draskovic I., Van Beneden A., Tilman G., Mattiussi M.,
Gobin M., Arnoult N., Londono-Vallejo A., Decottignies A.;
"Alternative lengthening of telomeres is characterized by reduced
compaction of telomeric chromatin.";
Nucleic Acids Res. 42:4391-4405(2014).
[40]
INTERACTION WITH RAD50; MRE11 AND NBN.
PubMed=24651726; DOI=10.1371/journal.pone.0092915;
Clynes D., Jelinska C., Xella B., Ayyub H., Taylor S., Mitson M.,
Bachrati C.Z., Higgs D.R., Gibbons R.J.;
"ATRX dysfunction induces replication defects in primary mouse
cells.";
PLoS ONE 9:E92915-E92915(2014).
[41]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-623 AND LYS-1982, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[42]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1004 AND LYS-1982, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[43]
FUNCTION, AND INTERACTION WITH DAXX; SETDB1; TRIM28 AND ZNF274.
PubMed=27029610; DOI=10.1080/15592294.2016.1169351;
Valle-Garcia D., Qadeer Z.A., McHugh D.S., Ghiraldini F.G.,
Chowdhury A.H., Hasson D., Dyer M.A., Recillas-Targa F., Bernstein E.;
"ATRX binds to atypical chromatin domains at the 3' exons of zinc
finger genes to preserve H3K9me3 enrichment.";
Epigenetics 11:398-414(2016).
[44]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-138; LYS-142;
LYS-438; LYS-623; LYS-1004; LYS-1488; LYS-1982 AND LYS-1987, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[45]
STRUCTURE BY NMR OF 159-296, AND DOMAIN GATA-TYPE ZINC-FINGER.
PubMed=17609377; DOI=10.1073/pnas.0704057104;
Argentaro A., Yang J.C., Chapman L., Kowalczyk M.S., Gibbons R.J.,
Higgs D.R., Neuhaus D., Rhodes D.;
"Structural consequences of disease-causing mutations in the ATRX-
DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX.";
Proc. Natl. Acad. Sci. U.S.A. 104:11939-11944(2007).
[46]
X-RAY CRYSTALLOGRAPHY (0.93 ANGSTROMS) OF 167-289 IN COMPLEX WITH
HISTONE H3K9ME3 PEPTIDE, SUBCELLULAR LOCATION, CHARACTERIZATION OF
ATRX VARIANTS ALA-190; PRO-219 AND CYS-246, AND MUTAGENESIS OF
HIS-189; TYR-203; TYR-204; ASP-217; GLU-252 AND LYS-1600.
PubMed=21666679; DOI=10.1038/nsmb.2062;
Iwase S., Xiang B., Ghosh S., Ren T., Lewis P.W., Cochrane J.C.,
Allis C.D., Picketts D.J., Patel D.J., Li H., Shi Y.;
"ATRX ADD domain links an atypical histone methylation recognition
mechanism to human mental-retardation syndrome.";
Nat. Struct. Mol. Biol. 18:769-776(2011).
[47]
STRUCTURE BY NMR OF 163-296 IN COMPLEX WITH HISTONE H3K9ME3 PEPTIDE,
CHARACTERIZATION OF ATRX VARIANT PRO-219, AND MUTAGENESIS OF TYR-203
AND GLU-218.
PubMed=21666677; DOI=10.1038/nsmb.2070;
Eustermann S., Yang J.C., Law M.J., Amos R., Chapman L.M.,
Jelinska C., Garrick D., Clynes D., Gibbons R.J., Rhodes D.,
Higgs D.R., Neuhaus D.;
"Combinatorial readout of histone H3 modifications specifies
localization of ATRX to heterochromatin.";
Nat. Struct. Mol. Biol. 18:777-782(2011).
[48]
VARIANT ATRX SER-1713.
PubMed=9043863;
Villard L., Lacombe D., Fontes M.;
"A point mutation in the XNP gene, associated with an ATR-X phenotype
without alpha-thalassemia.";
Eur. J. Hum. Genet. 4:316-320(1996).
[49]
VARIANT MRXSHF1 GLN-2131.
PubMed=8630485; DOI=10.1038/ng0496-359;
Villard L., Gecz J., Mattei J.-F., Fontes M., Saugier-Veber P.,
Munnich A., Lyonnet S.;
"XNP mutation in a large family with Juberg-Marsidi syndrome.";
Nat. Genet. 12:359-360(1996).
[50]
VARIANTS ATRX.
PubMed=9326931; DOI=10.1038/ng1097-146;
Gibbons R.J., Bachoo S., Picketts D.J., Aftimos S., Asenbauer B.,
Bergoffen J., Berry S.A., Dahl N., Fryer A., Keppler K., Kurosawa K.,
Levin M.L., Masuno M., Neri G., Pierpont M.E., Slaney S.F.,
Higgs D.R.;
"Mutations in transcriptional regulator ATRX establish the functional
significance of a PHD-like domain.";
Nat. Genet. 17:146-148(1997).
[51]
VARIANT ATRX LEU-246.
PubMed=10660327;
Fichera M., Romano C., Castiglia L., Failla P., Ruberto C., Amata S.,
Greco D., Cardoso C., Fontes M., Ragusa A.;
"New mutations in XNP/ATR-X gene: a further contribution to
genotype/phenotype relationship in ATR/X syndrome.";
Hum. Mutat. 12:214-214(1998).
[52]
VARIANT ATRX LYS-1742.
PubMed=10417298; DOI=10.1086/302499;
Lossi A.-M., Millan J.M., Villard L., Orellana C., Cardoso C.,
Prieto F., Fontes M., Martinez F.;
"Mutation of the XNP/ATR-X gene in a family with severe mental
retardation, spastic paraplegia and skewed pattern of X inactivation:
demonstration that the mutation is involved in the inactivation
bias.";
Am. J. Hum. Genet. 65:558-562(1999).
[53]
VARIANT MRXSHF1 THR-2050.
PubMed=10398237;
DOI=10.1002/(SICI)1096-8628(19990730)85:3<249::AID-AJMG12>3.0.CO;2-U;
Abidi F., Schwartz C.E., Carpenter N.J., Villard L., Fontes M.,
Curtis M.;
"Carpenter-Waziri syndrome results from a mutation in XNP.";
Am. J. Med. Genet. 85:249-251(1999).
[54]
VARIANTS ATRX GLU-175; 178-VAL--LYS-198 DEL; SER-190; PRO-219; LEU-246
AND CYS-249.
PubMed=10204841;
Villard L., Bonino M.-C., Abidi F., Ragusa A., Belougne J.,
Lossi A.-M., Seaver L., Bonnefont J.-P., Romano C., Fichera M.,
Lacombe D., Hanauer A., Philip N., Schwartz C.E., Fontes M.;
"Evaluation of a mutation screening strategy for sporadic cases of
ATR-X syndrome.";
J. Med. Genet. 36:183-186(1999).
[55]
VARIANTS ATRX SER-179; LEU-190; ILE-194; CYS-246; PHE-1552; SER-1645
AND CYS-1847.
PubMed=10995512;
DOI=10.1002/1096-8628(20000918)94:3<242::AID-AJMG11>3.3.CO;2-B;
Wada T., Kubota T., Fukushima Y., Saitoh S.;
"Molecular genetic study of Japanese patients with X-linked alpha-
thalassemia/mental retardation syndrome (ATR-X).";
Am. J. Med. Genet. 94:242-248(2000).
[56]
VARIANT MRXSHF1 TYR-220.
PubMed=11050622;
DOI=10.1002/1096-8628(20001023)94:5<383::AID-AJMG7>3.0.CO;2-7;
Stevenson R.E., Abidi F., Schwartz C.E., Lubs H.A., Holmes L.B.;
"Holmes-Gang syndrome is allelic with XLMR-hypotonic face syndrome.";
Am. J. Med. Genet. 94:383-385(2000).
[57]
VARIANT ATRX MET-1621.
PubMed=12116232; DOI=10.1002/ajmg.10446;
Yntema H.G., Poppelaars F.A., Derksen E., Oudakker A.R.,
van Roosmalen T., Jacobs A., Obbema H., Brunner H.G., Hamel B.C.J.,
van Bokhoven H.;
"Expanding phenotype of XNP mutations: mild to moderate mental
retardation.";
Am. J. Med. Genet. 110:243-247(2002).
[58]
VARIANT MRXSHF1 GLY-2271.
PubMed=16222662; DOI=10.1002/ajmg.a.30990;
Leahy R.T., Philip R.K., Gibbons R.J., Fisher C., Suri M., Reardon W.;
"Asplenia in ATR-X syndrome: a second report.";
Am. J. Med. Genet. A 139:37-39(2005).
[59]
VARIANT MRXSHF1 SER-409.
PubMed=15565397; DOI=10.1007/s10048-004-0190-3;
Wieland I., Sabathil J., Ostendorf A., Rittinger O., Roepke A.,
Winnepenninckx B., Kooy F., Holinski-Feder E., Wieacker P.;
"A missense mutation in the coiled-coil motif of the HP1-interacting
domain of ATR-X in a family with X-linked mental retardation.";
Neurogenetics 6:45-47(2005).
[60]
VARIANT ATRX CYS-246.
PubMed=16955409; DOI=10.1002/ajmg.a.31400;
Badens C., Martini N., Courrier S., DesPortes V., Touraine R.,
Levy N., Edery P.;
"ATRX syndrome in a girl with a heterozygous mutation in the ATRX Zn
finger domain and a totally skewed X-inactivation pattern.";
Am. J. Med. Genet. A 140:2212-2215(2006).
-!- FUNCTION: Involved in transcriptional regulation and chromatin
remodeling. Facilitates DNA replication in multiple cellular
environments and is required for efficient replication of a subset
of genomic loci. Binds to DNA tandem repeat sequences in both
telomeres and euchromatin and in vitro binds DNA quadruplex
structures. May help stabilizing G-rich regions into regular
chromatin structures by remodeling G4 DNA and incorporating H3.3-
containing nucleosomes. Catalytic component of the chromatin
remodeling complex ATRX:DAXX which has ATP-dependent DNA
translocase activity and catalyzes the replication-independent
deposition of histone H3.3 in pericentric DNA repeats outside S-
phase and telomeres, and the in vitro remodeling of H3.3-
containing nucleosomes. Its heterochromatin targeting is proposed
to involve a combinatorial readout of histone H3 modifications
(specifically methylation states of H3K9 and H3K4) and association
with CBX5. Involved in maintaining telomere structural integrity
in embryonic stem cells which probably implies recruitment of CBX5
to telomers. Reports on the involvement in transcriptional
regulation of telomeric repeat-containing RNA (TERRA) are
conflicting; according to a report, it is not sufficient to
decrease chromatin condensation at telomers nor to increase
expression of telomeric RNA in fibroblasts (PubMed:24500201). May
be involved in telomere maintenance via recombination in ALT
(alternative lengthening of telomeres) cell lines. Acts as
negative regulator of chromatin incorporation of transcriptionally
repressive histone H2AFY, particularily at telomeres and the
alpha-globin cluster in erythroleukemic cells. Participates in the
allele-specific gene expression at the imprinted IGF2/H19 gene
locus. On the maternal allele, required for the chromatin
occupancy of SMC1 and CTCTF within the H19 imprinting control
region (ICR) and involved in esatblishment of histone tails
modifications in the ICR. May be involved in brain development and
facial morphogenesis. Binds to zinc-finger coding genes with
atypical chromatin signatures and regulates its H3K9me3 levels.
Forms a complex with ZNF274, TRIM28 and SETDB1 to facilitate the
deposition and maintenance of H3K9me3 at the 3' exons of zinc-
finger genes (PubMed:27029610). {ECO:0000269|PubMed:12953102,
ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:20504901,
ECO:0000269|PubMed:20651253, ECO:0000269|PubMed:21029860,
ECO:0000269|PubMed:22391447, ECO:0000269|PubMed:22829774,
ECO:0000269|PubMed:24500201, ECO:0000269|PubMed:27029610}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Interacts with DAXX to form the chromatin remodeling
complex ATRX:DAXX. Probably binds EZH2. Binds annexin V in a
calcium and phosphatidylcholine/phosphatidylserine-dependent
manner. Interacts directly with CBX5 via the PxVxL motif.
Interacts with RAD50, MRE11 and NBN; indicative for an association
with the MRN complex. Interacts with histone H2AFY. Interacts with
histone H3 peptides methylated at 'Lys-10' with preferences
H3K9me3 > H3K9me2 > H3K9me1. Interacts with histone H3 peptides
unmethylated at 'Lys-5' (H3K4me0). Interacts with MECP2, SMC1 and
SMC3. Interacts with SETDB1, TRIM28 and ZNF274 (PubMed:27029610).
{ECO:0000269|PubMed:10699177, ECO:0000269|PubMed:12953102,
ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:15882967,
ECO:0000269|PubMed:17296936, ECO:0000269|PubMed:21421568,
ECO:0000269|PubMed:21666677, ECO:0000269|PubMed:21666679,
ECO:0000269|PubMed:22391447, ECO:0000269|PubMed:24651726,
ECO:0000269|PubMed:27029610, ECO:0000269|PubMed:9499421}.
-!- INTERACTION:
P45973:CBX5; NbExp=2; IntAct=EBI-396461, EBI-78219;
Q9UER7:DAXX; NbExp=7; IntAct=EBI-396461, EBI-77321;
Q15910:EZH2; NbExp=2; IntAct=EBI-396461, EBI-530054;
O75367-2:H2AFY; NbExp=2; IntAct=EBI-396461, EBI-6249599;
Q00566:Mecp2 (xeno); NbExp=6; IntAct=EBI-396461, EBI-9396907;
Q92878:RAD50; NbExp=5; IntAct=EBI-396461, EBI-495494;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. Nucleus, PML
body. Note=Associated with pericentromeric heterochromatin during
interphase and mitosis, probably by interacting with CBX5/HP1
alpha. Colocalizes with histone H3.3, DAXX, HIRA and ASF1A at PML-
nuclear bodies. Colocalizes with cohesin (SMC1 and SMC3) and MECP2
at the maternal H19 ICR (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=4;
IsoId=P46100-1; Sequence=Displayed;
Name=1;
IsoId=P46100-2; Sequence=VSP_000575;
Name=2;
IsoId=P46100-3; Sequence=VSP_000574;
Name=3;
IsoId=P46100-4; Sequence=VSP_000576;
Name=5;
IsoId=P46100-5; Sequence=VSP_000574, VSP_000576;
Name=6;
IsoId=P46100-6; Sequence=VSP_015499, VSP_015500, VSP_015501;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The ADD domain predominantly interacts with histone H3
trimethylated at 'Lys-10'(H3K9me3) (and to a lesser extent H3
mono-or dimethylated at 'Lys-10') and simultanously to histone H3
unmethylated at 'Lys-5' (H3K4me0). The interaction with H3K9me3 is
disrupted by the presence of H3K4me3 suggesting a readout of the
combined histone H3 methylation state.
{ECO:0000269|PubMed:17609377}.
-!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is
required for interaction with chromoshadow domains. This motif
requires additional residues -7, -6, +4 and +5 of the central Val
which contact the chromoshadow domain.
{ECO:0000269|PubMed:17609377}.
-!- PTM: Phosphorylated at serine residues during mitose.
Phosphorylation may promote the release from the nuclear matrix
and progression to mitosis. {ECO:0000269|PubMed:10699177}.
-!- DISEASE: Alpha-thalassemia mental retardation syndrome, X-linked
(ATRX) [MIM:301040]: A disorder characterized by severe
psychomotor retardation, facial dysmorphism, urogenital
abnormalities, and alpha-thalassemia. An essential phenotypic
trait are hemoglobin H erythrocyte inclusions.
{ECO:0000269|PubMed:10204841, ECO:0000269|PubMed:10417298,
ECO:0000269|PubMed:10660327, ECO:0000269|PubMed:10995512,
ECO:0000269|PubMed:12116232, ECO:0000269|PubMed:14990586,
ECO:0000269|PubMed:16955409, ECO:0000269|PubMed:21421568,
ECO:0000269|PubMed:7697714, ECO:0000269|PubMed:8968741,
ECO:0000269|PubMed:9043863, ECO:0000269|PubMed:9326931}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Mental retardation, X-linked, syndromic, with hypotonic
facies 1 (MRXSHF1) [MIM:309580]: A disorder characterized by
significantly below average general intellectual functioning
associated with impairments in adaptive behavior and manifested
during the developmental period. MRXSHF1 is a syndromic mental
retardation. Clinical features include severe mental retardation,
dysmorphic facies, and a highly skewed X-inactivation pattern in
carrier women. Other more variable features include hypogonadism,
deafness, renal anomalies, and mild skeletal defects.
{ECO:0000269|PubMed:10398237, ECO:0000269|PubMed:10751095,
ECO:0000269|PubMed:11050622, ECO:0000269|PubMed:15565397,
ECO:0000269|PubMed:16222662, ECO:0000269|PubMed:8630485}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Alpha-thalassemia myelodysplasia syndrome (ATMDS)
[MIM:300448]: A disorder characterized by hypochromic, microcytic
red blood cells, hemoglobin H detected in peripheral blood, and
multilineage myelodysplasia. {ECO:0000269|PubMed:12858175}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA20872.1; Type=Miscellaneous discrepancy; Note=Many frameshifts and conflits.; Evidence={ECO:0000305};
Sequence=AAC50069.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=BAD92165.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U72937; AAB49970.2; -; mRNA.
EMBL; U72938; AAB49971.2; -; mRNA.
EMBL; U72935; AAB40698.1; -; Genomic_DNA.
EMBL; U72904; AAB40698.1; JOINED; Genomic_DNA.
EMBL; U72905; AAB40698.1; JOINED; Genomic_DNA.
EMBL; U72907; AAB40698.1; JOINED; Genomic_DNA.
EMBL; U72908; AAB40698.1; JOINED; Genomic_DNA.
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EMBL; U72936; AAB49969.1; -; mRNA.
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EMBL; U72924; AAB40700.1; JOINED; Genomic_DNA.
EMBL; U72925; AAB40700.1; JOINED; Genomic_DNA.
EMBL; U72926; AAB40700.1; JOINED; Genomic_DNA.
EMBL; U72927; AAB40700.1; JOINED; Genomic_DNA.
EMBL; U72928; AAB40700.1; JOINED; Genomic_DNA.
EMBL; U72929; AAB40700.1; JOINED; Genomic_DNA.
EMBL; U72930; AAB40700.1; JOINED; Genomic_DNA.
EMBL; U72931; AAB40700.1; JOINED; Genomic_DNA.
EMBL; U72932; AAB40700.1; JOINED; Genomic_DNA.
EMBL; U72933; AAB40700.1; JOINED; Genomic_DNA.
EMBL; U72934; AAB40700.1; JOINED; Genomic_DNA.
EMBL; U75653; AAC51655.1; -; Genomic_DNA.
EMBL; U97103; AAC51657.1; -; Genomic_DNA.
EMBL; AF000157; AAC51657.1; JOINED; Genomic_DNA.
EMBL; AF000158; AAC51657.1; JOINED; Genomic_DNA.
EMBL; AF000159; AAC51657.1; JOINED; Genomic_DNA.
EMBL; AF000160; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97080; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97081; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97082; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97083; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97084; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97085; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97086; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97087; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97088; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97089; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97090; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97091; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97092; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97093; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97094; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97095; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97096; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97097; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97098; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97099; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97100; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97101; AAC51657.1; JOINED; Genomic_DNA.
EMBL; U97102; AAC51657.1; JOINED; Genomic_DNA.
EMBL; AB102641; BAC81110.1; -; mRNA.
EMBL; AB101681; BAC80270.1; -; Genomic_DNA.
EMBL; AB101682; BAC80271.1; -; Genomic_DNA.
EMBL; AB101683; BAC80272.1; -; Genomic_DNA.
EMBL; AB101685; BAC80274.1; -; Genomic_DNA.
EMBL; AB101687; BAC80276.1; -; Genomic_DNA.
EMBL; AB101689; BAC80278.1; -; Genomic_DNA.
EMBL; AB101691; BAC80280.1; -; Genomic_DNA.
EMBL; AB101693; BAC80282.1; -; Genomic_DNA.
EMBL; AB101695; BAC80284.1; -; Genomic_DNA.
EMBL; AB101700; BAC80289.1; -; Genomic_DNA.
EMBL; AB101699; BAC80288.1; -; Genomic_DNA.
EMBL; AB101698; BAC80287.1; -; Genomic_DNA.
EMBL; AB101697; BAC80286.1; -; Genomic_DNA.
EMBL; AB101696; BAC80285.1; -; Genomic_DNA.
EMBL; AB101694; BAC80283.1; -; Genomic_DNA.
EMBL; AB101692; BAC80281.1; -; Genomic_DNA.
EMBL; AB101690; BAC80279.1; -; Genomic_DNA.
EMBL; AB101688; BAC80277.1; -; Genomic_DNA.
EMBL; AB101686; BAC80275.1; -; Genomic_DNA.
EMBL; AB101684; BAC80273.1; -; Genomic_DNA.
EMBL; AB208928; BAD92165.1; ALT_INIT; mRNA.
EMBL; AB209545; BAD92782.1; -; mRNA.
EMBL; AL121874; CAB90351.2; -; Genomic_DNA.
EMBL; AL121874; CAI40710.1; -; Genomic_DNA.
EMBL; AL109753; CAI40710.1; JOINED; Genomic_DNA.
EMBL; Z84487; CAI40710.1; JOINED; Genomic_DNA.
EMBL; Z84487; CAI42674.1; -; Genomic_DNA.
EMBL; AL109753; CAI42674.1; JOINED; Genomic_DNA.
EMBL; AL121874; CAI42674.1; JOINED; Genomic_DNA.
EMBL; Z84487; CAI42675.1; -; Genomic_DNA.
EMBL; AL109753; CAI42675.1; JOINED; Genomic_DNA.
EMBL; AL121874; CAI42675.1; JOINED; Genomic_DNA.
EMBL; AL109753; CAI43115.1; -; Genomic_DNA.
EMBL; AL121874; CAI43115.1; JOINED; Genomic_DNA.
EMBL; Z84487; CAI43115.1; JOINED; Genomic_DNA.
EMBL; AL109753; CAI43116.1; -; Genomic_DNA.
EMBL; AL121874; CAI43116.1; JOINED; Genomic_DNA.
EMBL; Z84487; CAI43116.1; JOINED; Genomic_DNA.
EMBL; CH471104; EAW98611.1; -; Genomic_DNA.
EMBL; CH471104; EAW98615.1; -; Genomic_DNA.
EMBL; U09820; AAC50069.1; ALT_FRAME; mRNA.
EMBL; L34363; AAA20872.1; ALT_SEQ; Genomic_DNA.
EMBL; X83753; CAA58711.1; -; Genomic_DNA.
CCDS; CCDS14434.1; -. [P46100-1]
CCDS; CCDS14435.1; -. [P46100-4]
PIR; I38614; I38614.
PIR; I54367; I54367.
RefSeq; NP_000480.3; NM_000489.4.
RefSeq; NP_612114.2; NM_138270.3.
UniGene; Hs.533526; -.
UniGene; Hs.653797; -.
PDB; 2JM1; NMR; -; A=159-296.
PDB; 2LBM; NMR; -; A=163-296.
PDB; 2LD1; NMR; -; A=163-296.
PDB; 3QL9; X-ray; 0.93 A; A=167-289.
PDB; 3QLA; X-ray; 1.60 A; A/D=167-289.
PDB; 3QLC; X-ray; 2.50 A; A/B=167-289.
PDB; 3QLN; X-ray; 1.90 A; A/B=167-289.
PDB; 4W5A; X-ray; 2.60 A; A/B/E=167-289.
PDB; 5GRQ; X-ray; 1.58 A; C/D=1256-1285.
PDB; 5Y6O; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I=1265-1288.
PDBsum; 2JM1; -.
PDBsum; 2LBM; -.
PDBsum; 2LD1; -.
PDBsum; 3QL9; -.
PDBsum; 3QLA; -.
PDBsum; 3QLC; -.
PDBsum; 3QLN; -.
PDBsum; 4W5A; -.
PDBsum; 5GRQ; -.
PDBsum; 5Y6O; -.
ProteinModelPortal; P46100; -.
SMR; P46100; -.
BioGrid; 107028; 74.
CORUM; P46100; -.
DIP; DIP-31532N; -.
IntAct; P46100; 31.
MINT; MINT-1186201; -.
STRING; 9606.ENSP00000362441; -.
iPTMnet; P46100; -.
PhosphoSitePlus; P46100; -.
DMDM; 311033500; -.
EPD; P46100; -.
MaxQB; P46100; -.
PaxDb; P46100; -.
PeptideAtlas; P46100; -.
PRIDE; P46100; -.
DNASU; 546; -.
Ensembl; ENST00000373344; ENSP00000362441; ENSG00000085224.
Ensembl; ENST00000395603; ENSP00000378967; ENSG00000085224.
GeneID; 546; -.
KEGG; hsa:546; -.
UCSC; uc004ecp.5; human. [P46100-1]
CTD; 546; -.
DisGeNET; 546; -.
EuPathDB; HostDB:ENSG00000085224.20; -.
GeneCards; ATRX; -.
GeneReviews; ATRX; -.
H-InvDB; HIX0176765; -.
HGNC; HGNC:886; ATRX.
HPA; CAB009372; -.
HPA; CAB068176; -.
HPA; HPA001906; -.
HPA; HPA064684; -.
MalaCards; ATRX; -.
MIM; 300032; gene.
MIM; 300448; phenotype.
MIM; 301040; phenotype.
MIM; 309580; phenotype.
neXtProt; NX_P46100; -.
Orphanet; 231401; Alpha-thalassemia - myelodysplastic syndrome.
Orphanet; 847; Alpha-thalassemia - X-linked intellectual disability syndrome.
Orphanet; 93973; Carpenter-Waziri syndrome.
Orphanet; 93971; Chudley-Lowry-Hoar syndrome.
Orphanet; 93970; Holmes-Gang syndrome.
Orphanet; 93972; Juberg-Marsidi syndrome.
Orphanet; 93974; Smith-Fineman-Myers syndrome.
PharmGKB; PA25179; -.
eggNOG; KOG1015; Eukaryota.
eggNOG; COG0553; LUCA.
HOVERGEN; HBG000104; -.
InParanoid; P46100; -.
KO; K10779; -.
OrthoDB; EOG091G01G9; -.
PhylomeDB; P46100; -.
TreeFam; TF313172; -.
SIGNOR; P46100; -.
EvolutionaryTrace; P46100; -.
GeneWiki; ATRX; -.
GenomeRNAi; 546; -.
PRO; PR:P46100; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000085224; -.
CleanEx; HS_RAD54L; -.
ExpressionAtlas; P46100; baseline and differential.
Genevisible; P46100; HS.
GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IEA:Ensembl.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0000784; C:nuclear chromosome, telomeric region; ISS:BHF-UCL.
GO; GO:0005720; C:nuclear heterochromatin; TAS:ProtInc.
GO; GO:0031618; C:nuclear pericentric heterochromatin; IEA:Ensembl.
GO; GO:1990707; C:nuclear subtelomeric heterochromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0005721; C:pericentric heterochromatin; ISS:BHF-UCL.
GO; GO:0016605; C:PML body; ISS:BHF-UCL.
GO; GO:0070603; C:SWI/SNF superfamily-type complex; IDA:UniProtKB.
GO; GO:0031933; C:telomeric heterochromatin; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0070087; F:chromo shadow domain binding; IPI:BHF-UCL.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003678; F:DNA helicase activity; TAS:ProtInc.
GO; GO:0015616; F:DNA translocase activity; IDA:UniProtKB.
GO; GO:0004386; F:helicase activity; TAS:ProtInc.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0072711; P:cellular response to hydroxyurea; ISS:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IEA:Ensembl.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
GO; GO:0006306; P:DNA methylation; TAS:ProtInc.
GO; GO:0006310; P:DNA recombination; TAS:ProtInc.
GO; GO:0006281; P:DNA repair; TAS:ProtInc.
GO; GO:0006336; P:DNA replication-independent nucleosome assembly; IMP:UniProtKB.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0000212; P:meiotic spindle organization; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:1904908; P:negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric; IMP:BHF-UCL.
GO; GO:1901581; P:negative regulation of telomeric RNA transcription from RNA pol II promoter; ISS:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; ISS:UniProtKB.
GO; GO:0032206; P:positive regulation of telomere maintenance; ISS:UniProtKB.
GO; GO:1901582; P:positive regulation of telomeric RNA transcription from RNA pol II promoter; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0035128; P:post-embryonic forelimb morphogenesis; IEA:Ensembl.
GO; GO:0070198; P:protein localization to chromosome, telomeric region; ISS:BHF-UCL.
GO; GO:1900112; P:regulation of histone H3-K9 trimethylation; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
GO; GO:0060009; P:Sertoli cell development; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00079; HELICc; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR025766; ADD.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000330; SNF2_N.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF00176; SNF2_N; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 3.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS51533; ADD; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Chromatin regulator; Chromosome; Complete proteome; Disease mutation;
DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
Isopeptide bond; Mental retardation; Metal-binding; Methylation;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Telomere; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 2492 Transcriptional regulator ATRX.
/FTId=PRO_0000074301.
DOMAIN 159 296 ADD. {ECO:0000255|PROSITE-
ProRule:PRU00865}.
DOMAIN 1581 1768 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 2025 2205 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
ZN_FING 170 206 GATA-type; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00865}.
ZN_FING 217 272 PHD-type; atypical. {ECO:0000255|PROSITE-
ProRule:PRU00865}.
NP_BIND 1594 1601 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 1189 1326 Interaction with DAXX.
REGION 2010 2280 Interaction with MECP2.
{ECO:0000269|PubMed:17296936}.
MOTIF 581 594 PxVxL motif.
MOTIF 1719 1722 DEGH box.
COMPBIAS 745 750 Poly-Ser.
COMPBIAS 1151 1156 Poly-Ser.
COMPBIAS 1166 1169 Poly-Lys.
COMPBIAS 1202 1206 Poly-Ser.
COMPBIAS 1259 1266 Poly-Asp.
COMPBIAS 1443 1466 Poly-Glu.
COMPBIAS 1499 1502 Poly-Glu.
COMPBIAS 1929 1939 Poly-Lys.
COMPBIAS 1941 1948 Poly-Ser.
COMPBIAS 2222 2225 Poly-Lys.
COMPBIAS 2262 2265 Poly-Glu.
COMPBIAS 2420 2425 Poly-Gln.
MOD_RES 25 25 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 89 89 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 92 92 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 112 112 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000250|UniProtKB:Q61687}.
MOD_RES 316 316 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 591 591 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 594 594 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 598 598 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 634 634 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 674 674 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 675 675 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 677 677 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 729 729 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 731 731 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 784 784 Phosphoserine.
{ECO:0000250|UniProtKB:Q61687}.
MOD_RES 819 819 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 849 849 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 850 850 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 875 875 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 876 876 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 889 889 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 962 962 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 967 967 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 974 974 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 977 977 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1011 1011 Phosphoserine.
{ECO:0000250|UniProtKB:P70486}.
MOD_RES 1012 1012 Phosphoserine.
{ECO:0000250|UniProtKB:P70486}.
MOD_RES 1013 1013 Phosphoserine.
{ECO:0000250|UniProtKB:P70486}.
MOD_RES 1061 1061 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1063 1063 Phosphotyrosine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1244 1244 Phosphoserine.
{ECO:0000250|UniProtKB:Q61687}.
MOD_RES 1245 1245 Phosphoserine.
{ECO:0000250|UniProtKB:Q61687}.
MOD_RES 1253 1253 Phosphoserine.
{ECO:0000250|UniProtKB:Q61687}.
MOD_RES 1322 1322 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1324 1324 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1326 1326 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1348 1348 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1352 1352 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1527 1527 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1529 1529 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1906 1906 Phosphoserine.
{ECO:0000250|UniProtKB:Q61687}.
MOD_RES 1913 1913 Phosphoserine.
{ECO:0000250|UniProtKB:Q61687}.
MOD_RES 1992 1992 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1996 1996 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 2220 2220 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 2474 2474 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q61687}.
MOD_RES 2480 2480 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q61687}.
CROSSLNK 10 10 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 138 138 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 142 142 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 299 299 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 438 438 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 623 623 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 623 623 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1004 1004 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1488 1488 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1982 1982 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 1982 1982 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1987 1987 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 204 Missing (in isoform 1).
{ECO:0000303|PubMed:8968741}.
/FTId=VSP_000575.
VAR_SEQ 1 117 Missing (in isoform 2 and isoform 5).
{ECO:0000303|PubMed:8968741,
ECO:0000303|PubMed:9244431}.
/FTId=VSP_000574.
VAR_SEQ 124 162 Missing (in isoform 6).
{ECO:0000303|Ref.4}.
/FTId=VSP_015499.
VAR_SEQ 124 161 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:8968741}.
/FTId=VSP_000576.
VAR_SEQ 573 601 Missing (in isoform 6).
{ECO:0000303|Ref.4}.
/FTId=VSP_015500.
VAR_SEQ 1419 2492 Missing (in isoform 6).
{ECO:0000303|Ref.4}.
/FTId=VSP_015501.
VARIANT 175 175 G -> E (in ATRX).
{ECO:0000269|PubMed:10204841}.
/FTId=VAR_012113.
VARIANT 178 198 Missing (in ATRX).
{ECO:0000269|PubMed:10204841}.
/FTId=VAR_012114.
VARIANT 179 179 N -> S (in ATRX).
{ECO:0000269|PubMed:10995512}.
/FTId=VAR_012115.
VARIANT 190 190 P -> A (in ATRX; impairs interaction with
histone H3 peptides and reduces
localization to pericentromeric
heterochromatin foci).
{ECO:0000269|PubMed:21666679}.
/FTId=VAR_001226.
VARIANT 190 190 P -> L (in ATRX).
{ECO:0000269|PubMed:10995512}.
/FTId=VAR_012116.
VARIANT 190 190 P -> S (in ATRX).
{ECO:0000269|PubMed:10204841}.
/FTId=VAR_012117.
VARIANT 192 192 L -> F (in ATRX).
/FTId=VAR_001227.
VARIANT 194 194 V -> I (in ATRX).
{ECO:0000269|PubMed:10995512}.
/FTId=VAR_012118.
VARIANT 200 200 C -> S (in ATRX).
/FTId=VAR_001228.
VARIANT 219 219 Q -> P (in ATRX; greatly impairs
interaction with histone H3 peptides
trimethylated at 'Lys-10' (H3K9me3) and
reduces localization to pericentromeric
heterochromatin foci).
{ECO:0000269|PubMed:10204841,
ECO:0000269|PubMed:21666677,
ECO:0000269|PubMed:21666679}.
/FTId=VAR_012119.
VARIANT 220 220 C -> R (in ATRX).
/FTId=VAR_001229.
VARIANT 220 220 C -> Y (in MRXSHF1).
{ECO:0000269|PubMed:11050622}.
/FTId=VAR_032625.
VARIANT 222 222 W -> S (in ATRX).
/FTId=VAR_001230.
VARIANT 243 243 C -> F (in ATRX).
/FTId=VAR_001231.
VARIANT 246 246 R -> C (in ATRX; impairs interaction with
histone H3 peptides trimethylated at
'Lys-10' (H3K9me3) and reduces
localization to pericentromeric
heterochromatin foci).
{ECO:0000269|PubMed:10995512,
ECO:0000269|PubMed:16955409,
ECO:0000269|PubMed:21421568,
ECO:0000269|PubMed:21666679}.
/FTId=VAR_001232.
VARIANT 246 246 R -> L (in ATRX; impairs interaction with
histone H3 peptides trimethylated at
'Lys-10' (H3K9me3)).
{ECO:0000269|PubMed:10204841,
ECO:0000269|PubMed:10660327,
ECO:0000269|PubMed:21421568}.
/FTId=VAR_010914.
VARIANT 249 249 G -> C (in ATRX).
{ECO:0000269|PubMed:10204841}.
/FTId=VAR_012120.
VARIANT 249 249 G -> D (in ATRX; impairs interaction with
histone H3 peptides trimethylated at
'Lys-10' (H3K9me3); loss of
heterochromatic localization).
{ECO:0000269|PubMed:21421568}.
/FTId=VAR_001233.
VARIANT 409 409 L -> S (in MRXSHF1).
{ECO:0000269|PubMed:15565397}.
/FTId=VAR_032626.
VARIANT 545 545 Q -> E (in dbSNP:rs35738915).
/FTId=VAR_055939.
VARIANT 596 596 S -> P (in dbSNP:rs1051678).
{ECO:0000269|PubMed:9244431}.
/FTId=VAR_016914.
VARIANT 740 740 E -> G (in dbSNP:rs1051680).
{ECO:0000269|PubMed:9244431}.
/FTId=VAR_016915.
VARIANT 929 929 Q -> E (in dbSNP:rs3088074).
{ECO:0000269|Ref.4}.
/FTId=VAR_023438.
VARIANT 1538 1538 V -> G (in ATRX; unknown pathological
significance).
/FTId=VAR_012121.
VARIANT 1552 1552 V -> F (in ATRX).
{ECO:0000269|PubMed:10995512}.
/FTId=VAR_012122.
VARIANT 1609 1609 H -> R (in ATRX).
/FTId=VAR_001234.
VARIANT 1614 1614 C -> R (in ATRX).
/FTId=VAR_001235.
VARIANT 1621 1621 T -> M (in ATRX).
{ECO:0000269|PubMed:12116232}.
/FTId=VAR_016916.
VARIANT 1645 1645 L -> S (in ATRX).
{ECO:0000269|PubMed:10995512}.
/FTId=VAR_012123.
VARIANT 1650 1650 K -> N (in ATRX).
/FTId=VAR_001236.
VARIANT 1713 1713 P -> S (in ATRX; without alpha-
thalassemia).
{ECO:0000269|PubMed:9043863}.
/FTId=VAR_012124.
VARIANT 1742 1742 R -> K (in ATRX; atypical; patients
presents spastic paraplegia at birth).
{ECO:0000269|PubMed:10417298}.
/FTId=VAR_012125.
VARIANT 1847 1847 Y -> C (in ATRX).
{ECO:0000269|PubMed:10995512}.
/FTId=VAR_012126.
VARIANT 1860 1860 N -> S (rare polymorphism;
dbSNP:rs45439799).
{ECO:0000269|PubMed:8968741}.
/FTId=VAR_001237.
VARIANT 2035 2035 D -> V (in ATRX; impairs ATPase
activity). {ECO:0000269|PubMed:14990586}.
/FTId=VAR_001238.
VARIANT 2050 2050 I -> T (in MRXSHF1; originally reported
as Carpenter-Waziri syndrome).
{ECO:0000269|PubMed:10398237}.
/FTId=VAR_012127.
VARIANT 2084 2084 Y -> H (in ATRX; impairs ATPase
activity). {ECO:0000269|PubMed:14990586}.
/FTId=VAR_001239.
VARIANT 2131 2131 R -> Q (in MRXSHF1; originally reported
as Juberg-Marsidi syndrome).
{ECO:0000269|PubMed:8630485}.
/FTId=VAR_001240.
VARIANT 2163 2163 Y -> C (in ATRX).
/FTId=VAR_001241.
VARIANT 2271 2271 R -> G (in MRXSHF1).
{ECO:0000269|PubMed:16222662}.
/FTId=VAR_032627.
MUTAGEN 189 189 H->N: Impairs interaction with histone H3
peptides and reduces localization to
pericentromeric heterochromatin foci.
{ECO:0000269|PubMed:21666679}.
MUTAGEN 203 203 Y->A,K: Impairs interaction with histone
H3 peptides trimethylated at 'Lys-10'
(H3K9me3); loss of heterochromatic
localization.
{ECO:0000269|PubMed:21421568,
ECO:0000269|PubMed:21666677,
ECO:0000269|PubMed:21666679}.
MUTAGEN 204 204 Y->A: Impairs interaction with histone H3
peptides trimethylated at 'Lys-10'
(H3K9me3) and reduces localization to
pericentromeric heterochromatin foci.
{ECO:0000269|PubMed:21421568,
ECO:0000269|PubMed:21666679}.
MUTAGEN 207 207 D->A: Impairs interaction with histone H3
peptides trimethylated at 'Lys-10'
(H3K9me3) and reduces localization to
pericentromeric heterochromatin foci.
MUTAGEN 209 209 I->A: Impairs interaction with histone H3
peptides trimethylated at 'Lys-10'
(H3K9me3). {ECO:0000269|PubMed:21421568}.
MUTAGEN 214 214 D->A: Impairs interaction with histone H3
peptides trimethylated at 'Lys-10'
(H3K9me3). {ECO:0000269|PubMed:21421568}.
MUTAGEN 217 217 D->A: Impairs interaction with histone H3
peptides trimethylated at 'Lys-10'
(H3K9me3); loss of heterochromatic
localization.
{ECO:0000269|PubMed:21421568,
ECO:0000269|PubMed:21666679}.
MUTAGEN 218 218 E->A: Impairs interaction with histone H3
peptides unmethylated at 'Lys-5'
(H3K4me0); reduces pericentromeric
localization.
{ECO:0000269|PubMed:21666677}.
MUTAGEN 252 252 E->L: Impairs interaction with histone H3
peptides and reduces localization to
pericentromeric heterochromatin foci.
{ECO:0000269|PubMed:21666679}.
MUTAGEN 1600 1600 K->R: Abolishes ATPAse activity, no
effect on pericentromeric heterochromatin
localization.
{ECO:0000269|PubMed:14990586,
ECO:0000269|PubMed:21666679}.
CONFLICT 879 879 A -> R (in Ref. 7; AAC50069).
{ECO:0000305}.
CONFLICT 1286 1286 S -> P (in Ref. 4; BAD92165).
{ECO:0000305}.
CONFLICT 1627 1627 P -> L (in Ref. 7; AAC50069).
{ECO:0000305}.
CONFLICT 1632 1632 L -> F (in Ref. 7; AAC50069).
{ECO:0000305}.
CONFLICT 2280 2280 A -> G (in Ref. 7; AAC50069).
{ECO:0000305}.
CONFLICT 2283 2284 KG -> RV (in Ref. 7; AAC50069).
{ECO:0000305}.
CONFLICT 2436 2436 L -> H (in Ref. 7; AAC50069).
{ECO:0000305}.
CONFLICT 2442 2442 P -> R (in Ref. 7; AAC50069).
{ECO:0000305}.
TURN 172 174 {ECO:0000244|PDB:3QL9}.
STRAND 176 178 {ECO:0000244|PDB:2LBM}.
TURN 179 181 {ECO:0000244|PDB:2LBM}.
TURN 183 185 {ECO:0000244|PDB:3QL9}.
STRAND 186 188 {ECO:0000244|PDB:3QL9}.
TURN 190 192 {ECO:0000244|PDB:3QL9}.
STRAND 195 197 {ECO:0000244|PDB:3QL9}.
HELIX 198 206 {ECO:0000244|PDB:3QL9}.
STRAND 210 212 {ECO:0000244|PDB:2JM1}.
TURN 213 215 {ECO:0000244|PDB:2JM1}.
STRAND 217 219 {ECO:0000244|PDB:3QL9}.
TURN 221 223 {ECO:0000244|PDB:3QL9}.
STRAND 227 231 {ECO:0000244|PDB:3QL9}.
STRAND 233 236 {ECO:0000244|PDB:3QL9}.
STRAND 238 240 {ECO:0000244|PDB:3QL9}.
HELIX 241 247 {ECO:0000244|PDB:3QL9}.
HELIX 250 256 {ECO:0000244|PDB:3QL9}.
STRAND 258 261 {ECO:0000244|PDB:2JM1}.
TURN 266 268 {ECO:0000244|PDB:3QL9}.
HELIX 271 273 {ECO:0000244|PDB:3QL9}.
HELIX 274 284 {ECO:0000244|PDB:3QL9}.
HELIX 1267 1282 {ECO:0000244|PDB:5GRQ}.
SEQUENCE 2492 AA; 282586 MW; 637E341F6A4B29C6 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 VDKLSGKEQS 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


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