Details for: ATRX

Gene ID: 546

Symbol: ATRX

Ensembl ID: ENSG00000085224

Description: ATRX chromatin remodeler

Associated with

Other Information

Genular Protein ID: 2420390440

Symbol: ATRX_HUMAN

Name: Transcriptional regulator ATRX

UniProtKB Accession Codes:

P46100 D3DTE2 P51068 Q15886 Q59FB5 Q59H31 Q5H9A2 Q5JWI4 Q7Z2J1 Q9H0Z1 Q9NTS3

Database IDs:

AGR 1 AlphaFoldDB 1 Antibodypedia 1 BMRB 1 Bgee 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 2 CDD 3 CORUM 1 CarbonylDB 1 ChEBI 6 ChiTaRS 1 DIP 1 DMDM 1 DNASU 1 DisGeNET 1 EC 2 EMBL 100 EPD 1 Ensembl 2 EvolutionaryTrace 1 ExpressionAtlas 1 GO 45 Gene3D 3 GeneCards 1 GeneReviews 1 GeneTree 1 GeneWiki 1 Genevisible 1 GenomeRNAi 1 GlyCosmos 1 GlyGen 1 HGNC 1 HOGENOM 1 HPA 1 IDEAL 1 InParanoid 1 IntAct 1 InterPro 9 MANE-Select 1 MIM 7 MINT 1 MalaCards 1 MassIVE 1 MaxQB 1 MetOSite 1 NCBI Taxonomy 1 OMA 1 OpenTargets 1 Orphanet 4 OrthoDB 1 PANTHER 2 PDB 16 PDBsum 12 PIR 2 PRO 1 PROSITE 3 PROSITE-ProRule 3 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 3 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 6 Pumba 1 RNAct 1 Reactome 3 RefSeq 2 Rhea 1 SAM 1 SIGNOR 1 SMART 2 SMR 1 STRING 1 SUPFAM 2 SignaLink 1 SwissPalm 1 TreeFam 1 UCSC 1 UniProtKB 2 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 8968741

Title: ATRX encodes a novel member of the SNF2 family of proteins: mutations point to a common mechanism underlying the ATR-X syndrome.

PubMed ID: 8968741

DOI: 10.1093/hmg/5.12.1899

PubMed ID: 9244431

Title: Determination of the genomic structure of the XNP/ATRX gene encoding a potential zinc finger helicase.

PubMed ID: 9244431

DOI: 10.1006/geno.1997.4793

PubMed ID: 12777533

Title: Gene diversity patterns at 10 X-chromosomal loci in humans and chimpanzees.

PubMed ID: 12777533

DOI: 10.1093/molbev/msg134

PubMed ID: 15772651

Title: The DNA sequence of the human X chromosome.

PubMed ID: 15772651

DOI: 10.1038/nature03440

PubMed ID: 7874112

Title: Cloning and characterization of a new human Xq13 gene, encoding a putative helicase.

PubMed ID: 7874112

DOI: 10.1093/hmg/3.11.1957

PubMed ID: 8162050

Title: Cloning and expression of the murine homologue of a putative human X-linked nuclear protein gene closely linked to PGK1 in Xq13.3.

PubMed ID: 8162050

DOI: 10.1093/hmg/3.1.39

PubMed ID: 7697714

Title: Mutations in a putative global transcriptional regulator cause X-linked mental retardation with alpha-thalassemia (ATR-X syndrome).

PubMed ID: 7697714

DOI: 10.1016/0092-8674(95)90287-2

PubMed ID: 9499421

Title: Specific interaction between the XNP/ATR-X gene product and the SET domain of the human EZH2 protein.

PubMed ID: 9499421

DOI: 10.1093/hmg/7.4.679

PubMed ID: 10570185

Title: Localization of a putative transcriptional regulator (ATRX) at pericentromeric heterochromatin and the short arms of acrocentric chromosomes.

PubMed ID: 10570185

DOI: 10.1073/pnas.96.24.13983

PubMed ID: 10751095

Title: Identification of a mutation in the XNP/ATR-X gene in a family reported as Smith-Fineman-Myers syndrome.

PubMed ID: 10751095

DOI: 10.1002/(sici)1096-8628(20000306)91:1<83::aid-ajmg15>3.3.co;2-e

PubMed ID: 10699177

Title: Cell cycle-dependent phosphorylation of the ATRX protein correlates with changes in nuclear matrix and chromatin association.

PubMed ID: 10699177

DOI: 10.1093/hmg/9.4.539

PubMed ID: 12858175

Title: Identification of acquired somatic mutations in the gene encoding chromatin-remodeling factor ATRX in the alpha-thalassemia myelodysplasia syndrome (ATMDS).

PubMed ID: 12858175

DOI: 10.1038/ng1213

PubMed ID: 12953102

Title: The ATRX syndrome protein forms a chromatin-remodeling complex with Daxx and localizes in promyelocytic leukemia nuclear bodies.

PubMed ID: 12953102

DOI: 10.1073/pnas.1937626100

PubMed ID: 14990586

Title: A novel transcription regulatory complex containing death domain-associated protein and the ATR-X syndrome protein.

PubMed ID: 14990586

DOI: 10.1074/jbc.m401321200

PubMed ID: 15882967

Title: The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain.

PubMed ID: 15882967

DOI: 10.1016/j.bbrc.2005.04.016

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 17296936

Title: Interaction between chromatin proteins MECP2 and ATRX is disrupted by mutations that cause inherited mental retardation.

PubMed ID: 17296936

DOI: 10.1073/pnas.0608056104

PubMed ID: 17525332

Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.

PubMed ID: 17525332

DOI: 10.1126/science.1140321

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 21029860

Title: ATR-X syndrome protein targets tandem repeats and influences allele-specific expression in a size-dependent manner.

PubMed ID: 21029860

DOI: 10.1016/j.cell.2010.09.023

PubMed ID: 20211137

Title: Distinct factors control histone variant H3.3 localization at specific genomic regions.

PubMed ID: 20211137

DOI: 10.1016/j.cell.2010.01.003

PubMed ID: 20504901

Title: The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3.

PubMed ID: 20504901

DOI: 10.1101/gad.566910

PubMed ID: 20651253

Title: Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres.

PubMed ID: 20651253

DOI: 10.1073/pnas.1008850107

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21421568

Title: The ATRX-ADD domain binds to H3 tail peptides and reads the combined methylation state of K4 and K9.

PubMed ID: 21421568

DOI: 10.1093/hmg/ddr107

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22391447

Title: ATRX-mediated chromatin association of histone variant macroH2A1 regulates alpha-globin expression.

PubMed ID: 22391447

DOI: 10.1101/gad.179416.111

PubMed ID: 22829774

Title: Loss of ATRX, genome instability, and an altered DNA damage response are hallmarks of the alternative lengthening of telomeres pathway.

PubMed ID: 22829774

DOI: 10.1371/journal.pgen.1002772

PubMed ID: 23222847

Title: DAXX-dependent supply of soluble (H3.3-H4) dimers to PML bodies pending deposition into chromatin.

PubMed ID: 23222847

DOI: 10.1101/gr.142703.112

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 24500201

Title: Alternative lengthening of telomeres is characterized by reduced compaction of telomeric chromatin.

PubMed ID: 24500201

DOI: 10.1093/nar/gku114

PubMed ID: 24651726

Title: ATRX dysfunction induces replication defects in primary mouse cells.

PubMed ID: 24651726

DOI: 10.1371/journal.pone.0092915

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 27029610

Title: ATRX binds to atypical chromatin domains at the 3' exons of zinc finger genes to preserve H3K9me3 enrichment.

PubMed ID: 27029610

DOI: 10.1080/15592294.2016.1169351

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 17609377

Title: Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX.

PubMed ID: 17609377

DOI: 10.1073/pnas.0704057104

PubMed ID: 21666679

Title: ATRX ADD domain links an atypical histone methylation recognition mechanism to human mental-retardation syndrome.

PubMed ID: 21666679

DOI: 10.1038/nsmb.2062

PubMed ID: 21666677

Title: Combinatorial readout of histone H3 modifications specifies localization of ATRX to heterochromatin.

PubMed ID: 21666677

DOI: 10.1038/nsmb.2070

PubMed ID: 9043863

Title: A point mutation in the XNP gene, associated with an ATR-X phenotype without alpha-thalassemia.

PubMed ID: 9043863

DOI: 10.1159/000472225

PubMed ID: 8630485

Title: XNP mutation in a large family with Juberg-Marsidi syndrome.

PubMed ID: 8630485

DOI: 10.1038/ng0496-359

PubMed ID: 9326931

Title: Mutations in transcriptional regulator ATRX establish the functional significance of a PHD-like domain.

PubMed ID: 9326931

DOI: 10.1038/ng1097-146

PubMed ID: 10660327

Title: New mutations in XNP/ATR-X gene: a further contribution to genotype/phenotype relationship in ATR/X syndrome.

PubMed ID: 10660327

PubMed ID: 10417298

Title: 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.

PubMed ID: 10417298

DOI: 10.1086/302499

PubMed ID: 10398237

Title: Carpenter-Waziri syndrome results from a mutation in XNP.

PubMed ID: 10398237

DOI: 10.1002/(sici)1096-8628(19990730)85:3<249::aid-ajmg12>3.0.co;2-u

PubMed ID: 10204841

Title: Evaluation of a mutation screening strategy for sporadic cases of ATR-X syndrome.

PubMed ID: 10204841

PubMed ID: 10995512

Title: Molecular genetic study of Japanese patients with X-linked alpha-thalassemia/mental retardation syndrome (ATR-X).

PubMed ID: 10995512

DOI: 10.1002/1096-8628(20000918)94:3<242::aid-ajmg11>3.3.co;2-b

PubMed ID: 11050622

Title: Holmes-Gang syndrome is allelic with XLMR-hypotonic face syndrome.

PubMed ID: 11050622

DOI: 10.1002/1096-8628(20001023)94:5<383::aid-ajmg7>3.0.co;2-7

PubMed ID: 12116232

Title: Expanding phenotype of XNP mutations: mild to moderate mental retardation.

PubMed ID: 12116232

DOI: 10.1002/ajmg.10446

PubMed ID: 16222662

Title: Asplenia in ATR-X syndrome: a second report.

PubMed ID: 16222662

DOI: 10.1002/ajmg.a.30990

PubMed ID: 15565397

Title: A missense mutation in the coiled-coil motif of the HP1-interacting domain of ATR-X in a family with X-linked mental retardation.

PubMed ID: 15565397

DOI: 10.1007/s10048-004-0190-3

PubMed ID: 16955409

Title: ATRX syndrome in a girl with a heterozygous mutation in the ATRX Zn finger domain and a totally skewed X-inactivation pattern.

PubMed ID: 16955409

DOI: 10.1002/ajmg.a.31400

Sequence Information:

  • Length: 2492
  • Mass: 282587
  • Checksum: 938F82D6D6F99805
  • Sequence:
    • MTAEPMSESK LNTLVQKLHD FLAHSSEESE ETSSPPRLAM NQNTDKISGS GSNSDMMENS 
KEEGTSSSEK SKSSGSSRSK RKPSIVTKYV ESDDEKPLDD ETVNEDASNE NSENDITMQS 
LPKGTVIVQP EPVLNEDKDD FKGPEFRSRS KMKTENLKKR GEDGLHGIVS CTACGQQVNH 
FQKDSIYRHP SLQVLICKNC FKYYMSDDIS RDSDGMDEQC RWCAEGGNLI CCDFCHNAFC 
KKCILRNLGR KELSTIMDEN NQWYCYICHP EPLLDLVTAC NSVFENLEQL LQQNKKKIKV 
DSEKSNKVYE HTSRFSPKKT SSNCNGEEKK LDDSCSGSVT YSYSALIVPK EMIKKAKKLI 
ETTANMNSSY VKFLKQATDN SEISSATKLR QLKAFKSVLA DIKKAHLALE EDLNSEFRAM 
DAVNKEKNTK EHKVIDAKFE TKARKGEKPC ALEKKDISKS EAKLSRKQVD SEHMHQNVPT 
EEQRTNKSTG GEHKKSDRKE EPQYEPANTS EDLDMDIVSV PSSVPEDIFE NLETAMEVQS 
SVDHQGDGSS GTEQEVESSS VKLNISSKDN RGGIKSKTTA KVTKELYVKL TPVSLSNSPI 
KGADCQEVPQ DKDGYKSCGL NPKLEKCGLG QENSDNEHLV ENEVSLLLEE SDLRRSPRVK 
TTPLRRPTET NPVTSNSDEE CNETVKEKQK LSVPVRKKDK RNSSDSAIDN PKPNKLPKSK 
QSETVDQNSD SDEMLAILKE VSRMSHSSSS DTDINEIHTN HKTLYDLKTQ AGKDDKGKRK 
RKSSTSGSDF DTKKGKSAKS SIISKKKRQT QSESSNYDSE LEKEIKSMSK IGAARTTKKR 
IPNTKDFDSS EDEKHSKKGM DNQGHKNLKT SQEGSSDDAE RKQERETFSS AEGTVDKDTT 
IMELRDRLPK KQQASASTDG VDKLSGKEES FTSLEVRKVA ETKEKSKHLK TKTCKKVQDG 
LSDIAEKFLK KDQSDETSED DKKQSKKGTE EKKKPSDFKK KVIKMEQQYE SSSDGTEKLP 
EREEICHFPK GIKQIKNGTT DGEKKSKKIR DKTSKKKDEL SDYAEKSTGK GDSCDSSEDK 
KSKNGAYGRE KKRCKLLGKS SRKRQDCSSS DTEKYSMKED GCNSSDKRLK RIELRERRNL 
SSKRNTKEIQ SGSSSSDAEE SSEDNKKKKQ RTSSKKKAVI VKEKKRNSLR TSTKRKQADI 
TSSSSSDIED DDQNSIGEGS SDEQKIKPVT ENLVLSSHTG FCQSSGDEAL SKSVPVTVDD 
DDDDNDPENR IAKKMLLEEI KANLSSDEDG SSDDEPEEGK KRTGKQNEEN PGDEEAKNQV 
NSESDSDSEE SKKPRYRHRL LRHKLTVSDG ESGEEKKTKP KEHKEVKGRN RRKVSSEDSE 
DSDFQESGVS EEVSESEDEQ RPRTRSAKKA ELEENQRSYK QKKKRRRIKV QEDSSSENKS 
NSEEEEEEKE EEEEEEEEEE EEEEDENDDS KSPGKGRKKI RKILKDDKLR TETQNALKEE 
EERRKRIAER EREREKLREV IEIEDASPTK CPITTKLVLD EDEETKEPLV QVHRNMVIKL 
KPHQVDGVQF MWDCCCESVK KTKKSPGSGC ILAHCMGLGK TLQVVSFLHT VLLCDKLDFS 
TALVVCPLNT ALNWMNEFEK WQEGLKDDEK LEVSELATVK RPQERSYMLQ RWQEDGGVMI 
IGYEMYRNLA QGRNVKSRKL KEIFNKALVD PGPDFVVCDE GHILKNEASA VSKAMNSIRS 
RRRIILTGTP LQNNLIEYHC MVNFIKENLL GSIKEFRNRF INPIQNGQCA DSTMVDVRVM 
KKRAHILYEM LAGCVQRKDY TALTKFLPPK HEYVLAVRMT SIQCKLYQYY LDHLTGVGNN 
SEGGRGKAGA KLFQDFQMLS RIWTHPWCLQ LDYISKENKG YFDEDSMDEF IASDSDETSM 
SLSSDDYTKK KKKGKKGKKD SSSSGSGSDN DVEVIKVWNS RSRGGGEGNV DETGNNPSVS 
LKLEESKATS SSNPSSPAPD WYKDFVTDAD AEVLEHSGKM VLLFEILRMA EEIGDKVLVF 
SQSLISLDLI EDFLELASRE KTEDKDKPLI YKGEGKWLRN IDYYRLDGST TAQSRKKWAE 
EFNDETNVRG RLFIISTKAG SLGINLVAAN RVIIFDASWN PSYDIQSIFR VYRFGQTKPV 
YVYRFLAQGT MEDKIYDRQV TKQSLSFRVV DQQQVERHFT MNELTELYTF EPDLLDDPNS 
EKKKKRDTPM LPKDTILAEL LQIHKEHIVG YHEHDSLLDH KEEEELTEEE RKAAWAEYEA 
EKKGLTMRFN IPTGTNLPPV SFNSQTPYIP FNLGALSAMS NQQLEDLINQ GREKVVEATN 
SVTAVRIQPL EDIISAVWKE NMNLSEAQVQ ALALSRQASQ ELDVKRREAI YNDVLTKQQM 
LISCVQRILM NRRLQQQYNQ QQQQQMTYQQ ATLGHLMMPK PPNLIMNPSN YQQIDMRGMY 
QPVAGGMQPP PLQRAPPPMR SKNPGPSQGK SM

Genular Protein ID: 914767088

Symbol: B4DLW1_HUMAN

Name: N/A

UniProtKB Accession Codes:

B4DLW1

Database IDs:

ARBA 13 AlphaFoldDB 1 BioGRID-ORCS 1 ChEBI 5 DNASU 1 EC 1 EMBL 2 Gene3D 2 GenomeRNAi 1 InterPro 1 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PeptideAtlas 1 RefSeq 1 Rhea 1 SAM 1

Sequence Information:

  • Length: 322
  • Mass: 37129
  • Checksum: A7EEADA84098E0DC
  • Sequence:
    • MEDKIYDRQV TKQSLSFRVV DQQQVERHFT MNELTELYTF EPDLLDDPNS EKKKKRDTPM 
LPKDTILAEL LQIHKEHIVG YHEHDSLLDH KEEEELTEEE RKAAWAEYEA EKKGLTMRFN 
IPTGTNLPPV SFNSQTPYIP FNLGALSAMS NQQLEDLINQ GREKVVEATN SVTAVRIQPL 
EDIISAAWKE NMNLSEAQVQ ALALSRQASQ ELDVKRREAI YNDVLTKQQM LISCVQRILM 
NRRLQQQYNQ QQQQQMTYQQ ATLGHLMMPK PPNLIMNPSN YQQIDMRGMY QPVAGGMQPP 
PLQRAPPPMR SKNPGPSQGK SM

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.