ATRX_MOUSE
ID ATRX_MOUSE Reviewed; 2476 AA.
AC Q61687; A2ADH4;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Transcriptional regulator ATRX;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase ATRX;
DE AltName: Full=HP1 alpha-interacting protein;
DE AltName: Full=HP1-BP38 protein;
DE AltName: Full=Heterochromatin protein 2;
DE AltName: Full=X-linked nuclear protein;
GN Name=Atrx; Synonyms=Hp1bp2, Xnp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9545503; DOI=10.1007/s003359900781;
RA Picketts D.J., Tastan A.O., Higgs D.R., Gibbons R.J.;
RT "Comparison of the human and murine ATRX gene identifies highly conserved,
RT functionally important domains.";
RL Mamm. Genome 9:400-403(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 325-1176.
RX PubMed=8978696;
RA le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F.,
RA Losson R., Chambon P.;
RT "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic
RT control of transcription by nuclear receptors.";
RL EMBO J. 15:6701-6715(1996).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89; SER-717; SER-801 AND
RP SER-1339, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89; SER-92; SER-212; SER-315;
RP SER-626; SER-663; SER-665; SER-717; SER-766; SER-801; SER-854; SER-855;
RP SER-1223; SER-1224; SER-1232; SER-1339; SER-1891; SER-1898; SER-1975 AND
RP SER-1979, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
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 [11]
RP FUNCTION, AND 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 [12]
RP ASSOCIATION WITH HISTONE H3.3.
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 [13]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-239 AND VAL-580.
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 [14]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-2457 AND ARG-2464, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [15]
RP CITRULLINATION AT ARG-1063.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
RN [16]
RP INTERACTION WITH MECP2; SMC1 AND SMC3.
RX PubMed=20159591; DOI=10.1016/j.devcel.2009.12.017;
RA Kernohan K.D., Jiang Y., Tremblay D.C., Bonvissuto A.C., Eubanks J.H.,
RA Mann M.R., Berube N.G.;
RT "ATRX partners with cohesin and MeCP2 and contributes to developmental
RT silencing of imprinted genes in the brain.";
RL Dev. Cell 18:191-202(2010).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HISTONE H3.3.
RX PubMed=20110566; DOI=10.1101/gr.101477.109;
RA Wong L.H., McGhie J.D., Sim M., Anderson M.A., Ahn S., Hannan R.D.,
RA George A.J., Morgan K.A., Mann J.R., Choo K.H.;
RT "ATRX interacts with H3.3 in maintaining telomere structural integrity in
RT pluripotent embryonic stem cells.";
RL Genome Res. 20:351-360(2010).
RN [18]
RP FUNCTION, AND 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).
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 probably implying recruitment of CBX5 to
CC telomeres. Reports on the involvement in transcriptional regulation of
CC telomeric repeat-containing RNA (TERRA) are conflicting; according
CC (PubMed:20211137) is required for its transcriptional repression in
CC embryonic stem cells. Acts as negative regulator of chromatin
CC incorporation of transcriptionally repressive histone MACROH2A1,
CC particularily at telomeres. Participates in the allele-specific gene
CC expression at the imprinted IGF2/H19 gene locus. On the maternal
CC allele, required for the chromatin occupancy of SMC1 and CTCTF within
CC the H19 imprinting control region (ICR) and involved in esatblishment
CC of histone tails modifications in the ICR. Binds to zinc-finger coding
CC genes with atypical chromatin signatures and regulates its H3K9me3
CC levels. Forms a complex with ZNF274, TRIM28 and SETDB1 to facilitate
CC the deposition and maintenance of H3K9me3 at the 3' exons of zinc-
CC finger genes (By similarity). {ECO:0000250|UniProtKB:P46100,
CC ECO:0000269|PubMed:20110566, ECO:0000269|PubMed:20211137,
CC ECO:0000269|PubMed:21029860, ECO:0000269|PubMed:24651726}.
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 (By
CC similarity). {ECO:0000250|UniProtKB:P46100,
CC ECO:0000269|PubMed:17296936, ECO:0000269|PubMed:20110566,
CC ECO:0000269|PubMed:20159591, ECO:0000269|PubMed:24651726}.
CC -!- INTERACTION:
CC Q61687; Q9Z2D6: Mecp2; NbExp=5; IntAct=EBI-2657527, EBI-1188816;
CC Q61687; Q9CU62: Smc1a; NbExp=4; IntAct=EBI-2657527, EBI-2550016;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. Nucleus, PML body
CC {ECO:0000250}. Note=Associated with pericentromeric heterochromatin
CC during interphase and mitosis, probably by interacting with CBX5/HP1
CC alpha. Colocalizes with histone H3.3, DAXX, HIRA and ASF1A at PML-
CC nuclear bodies (By similarity). In embryonic stem cells localized to
CC telomeres; localization is reduced after 12 d of induction of cell
CC differentiation. Colocalizes with cohesin (SMC1 and SMC3) and MECP2 at
CC the maternal H19 ICR and the Gtl2/Dlk1 imprinted cluster in the brain.
CC {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
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.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AF026032; AAC08741.1; -; mRNA.
DR EMBL; AL670660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL671893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X99643; CAA67962.1; -; mRNA.
DR CCDS; CCDS41095.1; -.
DR RefSeq; NP_033556.2; NM_009530.2.
DR AlphaFoldDB; Q61687; -.
DR BMRB; Q61687; -.
DR SMR; Q61687; -.
DR BioGRID; 204603; 37.
DR DIP; DIP-55974N; -.
DR IntAct; Q61687; 32.
DR MINT; Q61687; -.
DR STRING; 10090.ENSMUSP00000109203; -.
DR iPTMnet; Q61687; -.
DR PhosphoSitePlus; Q61687; -.
DR SwissPalm; Q61687; -.
DR EPD; Q61687; -.
DR jPOST; Q61687; -.
DR MaxQB; Q61687; -.
DR PaxDb; Q61687; -.
DR PeptideAtlas; Q61687; -.
DR PRIDE; Q61687; -.
DR ProteomicsDB; 265183; -.
DR Antibodypedia; 460; 417 antibodies from 36 providers.
DR DNASU; 22589; -.
DR Ensembl; ENSMUST00000113573; ENSMUSP00000109203; ENSMUSG00000031229.
DR GeneID; 22589; -.
DR KEGG; mmu:22589; -.
DR UCSC; uc009ubb.2; mouse.
DR CTD; 546; -.
DR MGI; MGI:103067; Atrx.
DR VEuPathDB; HostDB:ENSMUSG00000031229; -.
DR eggNOG; KOG1015; Eukaryota.
DR GeneTree; ENSGT00940000155902; -.
DR HOGENOM; CLU_000863_1_0_1; -.
DR InParanoid; Q61687; -.
DR OMA; QEMGGVM; -.
DR OrthoDB; 815681at2759; -.
DR PhylomeDB; Q61687; -.
DR TreeFam; TF313172; -.
DR Reactome; R-MMU-9670095; Inhibition of DNA recombination at telomere.
DR BioGRID-ORCS; 22589; 9 hits in 117 CRISPR screens.
DR ChiTaRS; Atrx; mouse.
DR PRO; PR:Q61687; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q61687; protein.
DR Bgee; ENSMUSG00000031229; Expressed in metanephric cortical collecting duct and 249 other tissues.
DR ExpressionAtlas; Q61687; baseline and differential.
DR Genevisible; Q61687; MM.
DR GO; GO:0099115; C:chromosome, subtelomeric region; ISO:MGI.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0000228; C:nuclear chromosome; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:BHF-UCL.
DR GO; GO:0016605; C:PML body; IDA: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:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0070087; F:chromo shadow domain binding; ISO:MGI.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0015616; F:DNA translocase activity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0072711; P:cellular response to hydroxyurea; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IMP:MGI.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; ISS:UniProtKB.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0000212; P:meiotic spindle organization; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:1904908; P:negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric; ISO:MGI.
DR GO; GO:1901581; P:negative regulation of telomeric RNA transcription from RNA pol II promoter; IMP:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IMP:UniProtKB.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; IMP:UniProtKB.
DR GO; GO:1901582; P:positive regulation of telomeric RNA transcription from RNA pol II promoter; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0035128; P:post-embryonic forelimb morphogenesis; IMP:MGI.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; IMP:BHF-UCL.
DR GO; GO:1900112; P:regulation of histone H3-K9 trimethylation; ISS:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; IMP:UniProtKB.
DR GO; GO:0072520; P:seminiferous tubule development; IMP:MGI.
DR GO; GO:0060009; P:Sertoli cell development; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR025766; ADD.
DR InterPro; IPR041430; ADD_ATRX.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF17981; ADD_ATRX; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51533; ADD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; Chromosome; Citrullination; DNA damage;
KW DNA repair; DNA-binding; Helicase; Hydrolase; 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..2476
FT /note="Transcriptional regulator ATRX"
FT /id="PRO_0000074303"
FT DOMAIN 158..295
FT /note="ADD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT DOMAIN 1566..1753
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 2008..2188
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 169..205
FT /note="GATA-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT ZN_FING 216..271
FT /note="PHD-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT REGION 24..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1313
FT /note="Interaction with DAXX"
FT /evidence="ECO:0000250"
FT REGION 1898..1982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1993..2263
FT /note="Interaction with MECP2"
FT /evidence="ECO:0000250"
FT REGION 2445..2476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 573..586
FT /note="PxVxL motif"
FT MOTIF 1704..1707
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 84..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..852
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..1009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1079
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1171
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1453
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1898..1925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1952..1981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2453..2467
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1579..1586
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:0000250|UniProtKB:P46100"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 89
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 583
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 854
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 953
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70486"
FT MOD_RES 992
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70486"
FT MOD_RES 993
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70486"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1063
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 1223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1514
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 1891
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1898
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1975
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1979
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MOD_RES 2457
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2464
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 439
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 984
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 1473
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 1965
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 1965
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT CROSSLNK 1970
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46100"
FT MUTAGEN 239
FT /note="C->G: Reduces pericentromeric localization.
FT Abolishes pericentromeric localization; when associated
FT with E-580."
FT /evidence="ECO:0000269|PubMed:21666677"
FT MUTAGEN 580
FT /note="V->E: Reduces pericentromeric localization.
FT Abolishes pericentromeric localization; when associated
FT with G-239."
FT /evidence="ECO:0000269|PubMed:21666677"
FT CONFLICT 157
FT /note="K -> I (in Ref. 1; AAC08741)"
FT /evidence="ECO:0000305"
FT CONFLICT 1953
FT /note="V -> M (in Ref. 1; AAC08741)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2476 AA; 278587 MW; B2E2218B6CC791EC CRC64;
MTAEPMSGNK LSTLVQKLHD FLAHSSEESE ETCSSPRLVM NQSTDKICGS GLNSDMMENN
KEEGASTSEK SRSSGSSRSK RKPSIVTKYV ESDDEKPTDE NVNEKAATEN SENDITMQSL
PKGTVIVQPE PVLNEDKDDF KGPEFRSRSK MKADNLKKRG EDGLHGIVSC TACGQQVNHF
QKDSIYRHPS LKVLICKNCF KYYMSDDISR DSDGMDEQCR WCAEGGNLIC CDFCHNAFCK
KCILRNLGRK ELSTIMDENN QWYCYICQPE PLLDLVTACN SVFENLEQLL QQNKKKIKVD
SEKTSKVCDQ TSKFSPKKSS SSCNGEEKKL EESCSGSVSS TYSHSALSVP KEMIKKTTKL
IETTSNMNSS YIKFLKQAAD NSEMTSAMKL CQLKSFKSVL DDIKKAHLAL EEDLNSEIQA
LDDVHKEKNT KDLKSTDAKS ETKLGKGEKS YSTEKREFLK LDARSSVKAI DGEEQRAHKS
TSGEHKGSGR KDGSQYEPTN TPEDLDMDIV SVPSSVPEDI FDSLESAMEV QSSADYQGDG
NSGTEPELES SSVKLNVSSK DSRGNIKSKV TAKVRKELFV KLTPVSLSNS PIKGVDCQEV
SQEKNGRKSS GVARSSEKCR PREEISDHEN NVTILLEDSD LRRSPRVKTT PLRRQTESNP
AMSNSDEESN GTMKEKQKMS GPIRKKDKRN SADCATDNPK PHKVPKAKQP VIGDQNSDSD
EMLAVLKEAS QMGHSSSSDT DINEPQMNHK GKTGKDDNGK RKRKNSTSGS DFDTKKGKST
ETSIISKKKR QNYSESSNYD SELEREIKTM SRIGAARKSV PEKKEEDSSE DEKQGKKVVD
NGGHERAKTT QEGSSADDTG DTEGRQGGSC SIAGGSIEKV RSGVEFREML CKPGVSSDGA
EKPSVKEENV NSPEDKRVSK TKEKTKHLRS RQSRKGKGGS SDGTDRFPKK EQSDESSEGE
KKQSRQRPGT KGKKAPDLKG ETLKREQEWD SSSDGTERLP EEEEIGPFSK GIKQSKTDTA
GGEKKGKKWK DKSCEKKEEL SDSVDKLPGK GDSCDSSEDK KTRNRVSLRE KKRFSLPAKS
PGKRPECSSS DTEKSLKGQC CDSTEKRPKR IDLRERRNSS SKRNTKEVKS ASSSSDAEGS
SEDNKKQKKQ RTSAKKKTGN TKEKKRNSLR ATPKRKQVDI TSSSSDIGDD DQNSAGEESS
DEQKIKPVTE NLVLPSHTGF CQSSGDEALS KSVPATVDDD DDDNDPENRI AKKMLLEEIK
ANLSSDEDGS SDDEPDGGGK KRIGKQSEES PADDGELRRE QLAVNQVNSE SDSDSEESKK
PRYRHRLLRH KLTLSDGESG EEKPTKPKEH KEAKGRNRRK VSSEDSEDTD FQESGVSEEV
SESEDEQRPR TRSAKKAELE ENQRSYKQKK KRRRIKVQED SSSENKSHSE EDKKEGDEED
EEDEDEDEED ENDDSKSPGK GRKKIRKILK DDKLRTETQN ALKEEEERRK RIAERERERE
KLREVIEIED ASPTKCPITT KLVLDENEET KEPLVQVHRN MVIKLKPHQV DGVQFMWDCC
CESVEKTKKS PGSGCILAHC MGLGKTLQVV SFLHTVLLCD KLDFSTALVV CPLNTALNWM
NEFEKWQEGL NDNEKLEVSE LATVKRPQER SYMLQRWQED GGVMIIGYEM YRNLAQGRNV
KSRKLKDIFN KALVDPGPDF VVCDEGHILK NEASAVSKAM NSIKSRRRII LTGTPLQNNL
IEYHCMVNFI KENLLGSIKE FRNRFINPIQ NGQCADSTMV DVRVMKKRAH ILYEMLAGCV
QRKDYTALTK FLPPKHEYVL AVRMTAIQCK LYQYYLDHLT GVGNSTEGGR GKAGAKLFQD
FQMLSRIWTH PWCLQLDYIS KENKGYFDED SMDEFIASDS DETSKSLSSD EKKKPKGKKG
KKDSSSSGSG SDNDVEVIKV WNSRSRGGGD GNVDDTGNNP SVSLKLDESK TTSTSNPSSP
APDWYKDFVT DTDAEVLEHS GKMVLLFEIL RMAEEIGDKV LVFSQSLISL DLIEDFLELA
SREKTEDKEK PLIYKGEGKW IRNIDYYRLD GSTNAQSRKK WAEEFNDETN VRGRLFIIST
KAGSLGINLV AANRVIIFDA SWNPSYDIQS IFRVYRFGQT KPVYVYRFLA QGTMEDKIYD
RQVTKQSLSF RVVDQQQVER HFTMNELTEL YTFEPDLLDD PNSEKKKKRD TPMLPKDTIL
AELLQIHKEH IVGYHEHDSL LDHKEEEELT EEERKAAWAE YEAEKKGLTM RFNIPTGTNL
PPVTFTSQTP YIPFNLGALS AMSNQQLEDL INQGREKVVE ATNSMTAVRI QPLEDIISTV
WKENMNLSEA QVQALALSRQ ASQELDVKRR EAIYNDVLTK QQMLINCVQR ILMNRRLQQQ
YTQQQQQQLT YQQATLSHLM MPKPPNLIMT PSNYQQIDMR GMYQSVAGGM QPPPLQRAPP
PTVRSKNPGP SPGKSM
