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Protein

Transcriptional regulator ATRX

Gene

ATRX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).9 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri170 – 20637GATA-type; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri217 – 27256PHD-type; atypicalPROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi1594 – 16018ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: Ensembl
  • chromo shadow domain binding Source: BHF-UCL
  • DNA binding Source: UniProtKB-KW
  • DNA helicase activity Source: ProtInc
  • DNA translocase activity Source: UniProtKB
  • helicase activity Source: ProtInc
  • histone binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • methylated histone binding Source: UniProtKB

GO - Biological processi

  • cellular response to hydroxyurea Source: UniProtKB
  • chromatin remodeling Source: UniProtKB
  • DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  • DNA methylation Source: ProtInc
  • DNA recombination Source: ProtInc
  • DNA repair Source: ProtInc
  • DNA replication-independent nucleosome assembly Source: UniProtKB
  • forebrain development Source: Ensembl
  • multicellular organism growth Source: Ensembl
  • negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric Source: BHF-UCL
  • negative regulation of telomeric RNA transcription from RNA pol II promoter Source: UniProtKB
  • nucleosome assembly Source: UniProtKB
  • positive regulation of nuclear cell cycle DNA replication Source: UniProtKB
  • positive regulation of telomere maintenance Source: UniProtKB
  • positive regulation of telomeric RNA transcription from RNA pol II promoter Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • post-embryonic forelimb morphogenesis Source: Ensembl
  • protein localization to chromosome, telomeric region Source: BHF-UCL
  • regulation of transcription, DNA-templated Source: ProtInc
  • replication fork processing Source: UniProtKB
  • seminiferous tubule development Source: Ensembl
  • Sertoli cell development Source: Ensembl
  • spermatogenesis Source: Ensembl
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

SIGNORiP46100.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional regulator ATRX (EC:3.6.4.12)
Alternative name(s):
ATP-dependent helicase ATRX
X-linked helicase II
X-linked nuclear protein
Short name:
XNP
Znf-HX
Gene namesi
Name:ATRX
Synonyms:RAD54L, XH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:886. ATRX.

Subcellular locationi

  • Nucleus
  • Chromosometelomere
  • NucleusPML 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).By similarity

GO - Cellular componenti

  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear heterochromatin Source: ProtInc
  • nuclear subtelomeric heterochromatin Source: BHF-UCL
  • nucleus Source: HPA
  • pericentric heterochromatin Source: BHF-UCL
  • PML body Source: BHF-UCL
  • SWI/SNF superfamily-type complex Source: UniProtKB
  • telomeric heterochromatin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Involvement in diseasei

Alpha-thalassemia mental retardation syndrome, X-linked (ATRX)10 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by severe psychomotor retardation, facial dysmorphism, urogenital abnormalities, and alpha-thalassemia. An essential phenotypic trait are hemoglobin H erythrocyte inclusions.
See also OMIM:301040
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti175 – 1751G → E in ATRX. 1 Publication
VAR_012113
Natural varianti178 – 19821Missing in ATRX. 1 Publication
VAR_012114Add
BLAST
Natural varianti179 – 1791N → S in ATRX. 1 Publication
VAR_012115
Natural varianti190 – 1901P → A in ATRX; impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci. 1 Publication
VAR_001226
Natural varianti190 – 1901P → L in ATRX. 1 Publication
VAR_012116
Natural varianti190 – 1901P → S in ATRX. 1 Publication
VAR_012117
Natural varianti192 – 1921L → F in ATRX.
VAR_001227
Natural varianti194 – 1941V → I in ATRX. 1 Publication
VAR_012118
Natural varianti200 – 2001C → S in ATRX.
VAR_001228
Natural varianti219 – 2191Q → P in ATRX; greatly impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 3 Publications
VAR_012119
Natural varianti220 – 2201C → R in ATRX.
VAR_001229
Natural varianti222 – 2221W → S in ATRX.
VAR_001230
Natural varianti243 – 2431C → F in ATRX.
VAR_001231
Natural varianti246 – 2461R → C in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 4 Publications
VAR_001232
Natural varianti246 – 2461R → L in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). 3 Publications
VAR_010914
Natural varianti249 – 2491G → C in ATRX. 1 Publication
VAR_012120
Natural varianti249 – 2491G → D in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization. 1 Publication
VAR_001233
Natural varianti1538 – 15381V → G in ATRX; unknown pathological significance.
VAR_012121
Natural varianti1552 – 15521V → F in ATRX. 1 Publication
VAR_012122
Natural varianti1609 – 16091H → R in ATRX.
VAR_001234
Natural varianti1614 – 16141C → R in ATRX.
VAR_001235
Natural varianti1621 – 16211T → M in ATRX. 1 Publication
VAR_016916
Natural varianti1645 – 16451L → S in ATRX. 1 Publication
VAR_012123
Natural varianti1650 – 16501K → N in ATRX.
VAR_001236
Natural varianti1713 – 17131P → S in ATRX; without alpha-thalassemia. 1 Publication
VAR_012124
Natural varianti1742 – 17421R → K in ATRX; atypical; patients presents spastic paraplegia at birth. 1 Publication
VAR_012125
Natural varianti1847 – 18471Y → C in ATRX. 1 Publication
VAR_012126
Natural varianti2035 – 20351D → V in ATRX; impairs ATPase activity. 1 Publication
VAR_001238
Natural varianti2084 – 20841Y → H in ATRX; impairs ATPase activity. 1 Publication
VAR_001239
Natural varianti2163 – 21631Y → C in ATRX.
VAR_001241
Mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:309580
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti220 – 2201C → Y in MRXSHF1. 1 Publication
VAR_032625
Natural varianti409 – 4091L → S in MRXSHF1. 1 Publication
VAR_032626
Natural varianti2050 – 20501I → T in MRXSHF1; originally reported as Carpenter-Waziri syndrome. 1 Publication
VAR_012127
Natural varianti2131 – 21311R → Q in MRXSHF1; originally reported as Juberg-Marsidi syndrome. 1 Publication
VAR_001240
Natural varianti2271 – 22711R → G in MRXSHF1. 1 Publication
VAR_032627
Alpha-thalassemia myelodysplasia syndrome (ATMDS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by hypochromic, microcytic red blood cells, hemoglobin H detected in peripheral blood, and multilineage myelodysplasia.
See also OMIM:300448

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi189 – 1891H → N: Impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci. 1 Publication
Mutagenesisi203 – 2031Y → A or K: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization. 3 Publications
Mutagenesisi204 – 2041Y → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 2 Publications
Mutagenesisi207 – 2071D → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci.
Mutagenesisi209 – 2091I → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). 1 Publication
Mutagenesisi214 – 2141D → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). 1 Publication
Mutagenesisi217 – 2171D → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization. 2 Publications
Mutagenesisi218 – 2181E → A: Impairs interaction with histone H3 peptides unmethylated at 'Lys-5' (H3K4me0); reduces pericentromeric localization. 1 Publication
Mutagenesisi252 – 2521E → L: Impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci. 1 Publication
Mutagenesisi1600 – 16001K → R: Abolishes ATPAse activity, no effect on pericentromeric heterochromatin localization. 2 Publications

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MalaCardsiATRX.
MIMi300448. phenotype.
301040. phenotype.
309580. phenotype.
Orphaneti231401. Alpha-thalassemia - myelodysplastic syndrome.
847. Alpha-thalassemia - X-linked intellectual disability syndrome.
93973. Carpenter-Waziri syndrome.
93971. Chudley-Lowry-Hoar syndrome.
93970. Holmes-Gang syndrome.
93972. Juberg-Marsidi syndrome.
93974. Smith-Fineman-Myers syndrome.
PharmGKBiPA25179.

Polymorphism and mutation databases

DMDMi311033500.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24922492Transcriptional regulator ATRXPRO_0000074301Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251PhosphoserineCombined sources
Modified residuei34 – 341PhosphoserineCombined sources
Modified residuei89 – 891PhosphotyrosineCombined sources
Modified residuei92 – 921PhosphoserineCombined sources
Modified residuei112 – 1121PhosphoserineCombined sources
Modified residuei213 – 2131PhosphoserineBy similarity
Cross-linki299 – 299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei316 – 3161PhosphoserineCombined sources
Cross-linki438 – 438Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei591 – 5911PhosphothreonineCombined sources
Modified residuei594 – 5941PhosphoserineCombined sources
Modified residuei598 – 5981PhosphoserineCombined sources
Cross-linki623 – 623Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki623 – 623Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei634 – 6341PhosphoserineCombined sources
Modified residuei674 – 6741PhosphothreonineCombined sources
Modified residuei675 – 6751PhosphoserineCombined sources
Modified residuei677 – 6771PhosphoserineCombined sources
Modified residuei729 – 7291PhosphoserineCombined sources
Modified residuei731 – 7311PhosphoserineCombined sources
Modified residuei784 – 7841PhosphoserineBy similarity
Modified residuei819 – 8191PhosphoserineCombined sources
Modified residuei849 – 8491PhosphoserineCombined sources
Modified residuei850 – 8501PhosphoserineCombined sources
Modified residuei875 – 8751PhosphoserineCombined sources
Modified residuei876 – 8761PhosphoserineCombined sources
Modified residuei889 – 8891PhosphoserineCombined sources
Modified residuei962 – 9621PhosphoserineCombined sources
Modified residuei967 – 9671N6-acetyllysineCombined sources
Modified residuei974 – 9741PhosphoserineCombined sources
Modified residuei977 – 9771PhosphothreonineCombined sources
Cross-linki1004 – 1004Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1011 – 10111PhosphoserineBy similarity
Modified residuei1012 – 10121PhosphoserineBy similarity
Modified residuei1013 – 10131PhosphoserineBy similarity
Modified residuei1061 – 10611PhosphoserineCombined sources
Modified residuei1063 – 10631PhosphotyrosineCombined sources
Modified residuei1244 – 12441PhosphoserineBy similarity
Modified residuei1245 – 12451PhosphoserineBy similarity
Modified residuei1253 – 12531PhosphoserineBy similarity
Modified residuei1322 – 13221PhosphoserineCombined sources
Modified residuei1324 – 13241PhosphoserineCombined sources
Modified residuei1326 – 13261PhosphoserineCombined sources
Modified residuei1348 – 13481PhosphoserineCombined sources
Modified residuei1352 – 13521PhosphoserineCombined sources
Cross-linki1488 – 1488Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1527 – 15271PhosphoserineCombined sources
Modified residuei1529 – 15291PhosphothreonineCombined sources
Modified residuei1906 – 19061PhosphoserineBy similarity
Modified residuei1913 – 19131PhosphoserineBy similarity
Cross-linki1982 – 1982Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki1982 – 1982Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1992 – 19921PhosphoserineCombined sources
Modified residuei1996 – 19961PhosphoserineCombined sources
Modified residuei2220 – 22201PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated at serine residues during mitose. Phosphorylation may promote the release from the nuclear matrix and progression to mitosis.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP46100.
MaxQBiP46100.
PaxDbiP46100.
PeptideAtlasiP46100.
PRIDEiP46100.

PTM databases

iPTMnetiP46100.
PhosphoSiteiP46100.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiP46100.
CleanExiHS_RAD54L.
ExpressionAtlasiP46100. baseline and differential.
GenevisibleiP46100. HS.

Organism-specific databases

HPAiCAB009372.
CAB068176.
HPA001906.
HPA064684.

Interactioni

Subunit structurei

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, MRE11A 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).12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBX5P459732EBI-396461,EBI-78219
DAXXQ9UER77EBI-396461,EBI-77321
EZH2Q159102EBI-396461,EBI-530054
H2AFYO75367-22EBI-396461,EBI-6249599
Mecp2Q005666EBI-396461,EBI-9396907From a different organism.
RAD50Q928785EBI-396461,EBI-495494

GO - Molecular functioni

  • chromo shadow domain binding Source: BHF-UCL
  • histone binding Source: UniProtKB
  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107028. 59 interactions.
DIPiDIP-31532N.
IntActiP46100. 30 interactions.
MINTiMINT-1186201.
STRINGi9606.ENSP00000362441.

Structurei

Secondary structure

1
2492
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni172 – 1743Combined sources
Beta strandi176 – 1783Combined sources
Turni179 – 1813Combined sources
Turni183 – 1853Combined sources
Beta strandi186 – 1883Combined sources
Turni190 – 1923Combined sources
Beta strandi195 – 1973Combined sources
Helixi198 – 2069Combined sources
Beta strandi210 – 2123Combined sources
Turni213 – 2153Combined sources
Beta strandi217 – 2193Combined sources
Turni221 – 2233Combined sources
Beta strandi227 – 2315Combined sources
Beta strandi233 – 2364Combined sources
Beta strandi238 – 2403Combined sources
Helixi241 – 2477Combined sources
Helixi250 – 2567Combined sources
Beta strandi258 – 2614Combined sources
Turni266 – 2683Combined sources
Helixi271 – 2733Combined sources
Helixi274 – 28411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JM1NMR-A159-296[»]
2LBMNMR-A163-296[»]
2LD1NMR-A163-296[»]
3QL9X-ray0.93A167-289[»]
3QLAX-ray1.60A/D167-289[»]
3QLCX-ray2.50A/B167-289[»]
3QLNX-ray1.90A/B167-289[»]
4W5AX-ray2.60A/B/E167-289[»]
ProteinModelPortaliP46100.
SMRiP46100. Positions 159-296.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46100.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini159 – 296138ADDPROSITE-ProRule annotationAdd
BLAST
Domaini1581 – 1768188Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2025 – 2205181Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1189 – 1326138Interaction with DAXXAdd
BLAST
Regioni2010 – 2280271Interaction with MECP2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi581 – 59414PxVxL motifAdd
BLAST
Motifi1719 – 17224DEGH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi745 – 7506Poly-Ser
Compositional biasi1151 – 11566Poly-Ser
Compositional biasi1166 – 11694Poly-Lys
Compositional biasi1202 – 12065Poly-Ser
Compositional biasi1259 – 12668Poly-Asp
Compositional biasi1443 – 146624Poly-GluAdd
BLAST
Compositional biasi1499 – 15024Poly-Glu
Compositional biasi1929 – 193911Poly-LysAdd
BLAST
Compositional biasi1941 – 19488Poly-Ser
Compositional biasi2222 – 22254Poly-Lys
Compositional biasi2262 – 22654Poly-Glu
Compositional biasi2420 – 24256Poly-Gln

Domaini

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.1 Publication
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.1 Publication

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated
Contains 1 ADD domain.PROSITE-ProRule annotation
Contains 1 GATA-type zinc finger.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri170 – 20637GATA-type; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri217 – 27256PHD-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1015. Eukaryota.
COG0553. LUCA.
HOVERGENiHBG000104.
InParanoidiP46100.
KOiK10779.
OrthoDBiEOG7G4QDQ.
PhylomeDBiP46100.
TreeFamiTF313172.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR025766. ADD.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51533. ADD. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 4 (identifier: P46100-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTAEPMSESK LNTLVQKLHD FLAHSSEESE ETSSPPRLAM NQNTDKISGS
60 70 80 90 100
GSNSDMMENS KEEGTSSSEK SKSSGSSRSK RKPSIVTKYV ESDDEKPLDD
110 120 130 140 150
ETVNEDASNE NSENDITMQS LPKGTVIVQP EPVLNEDKDD FKGPEFRSRS
160 170 180 190 200
KMKTENLKKR GEDGLHGIVS CTACGQQVNH FQKDSIYRHP SLQVLICKNC
210 220 230 240 250
FKYYMSDDIS RDSDGMDEQC RWCAEGGNLI CCDFCHNAFC KKCILRNLGR
260 270 280 290 300
KELSTIMDEN NQWYCYICHP EPLLDLVTAC NSVFENLEQL LQQNKKKIKV
310 320 330 340 350
DSEKSNKVYE HTSRFSPKKT SSNCNGEEKK LDDSCSGSVT YSYSALIVPK
360 370 380 390 400
EMIKKAKKLI ETTANMNSSY VKFLKQATDN SEISSATKLR QLKAFKSVLA
410 420 430 440 450
DIKKAHLALE EDLNSEFRAM DAVNKEKNTK EHKVIDAKFE TKARKGEKPC
460 470 480 490 500
ALEKKDISKS EAKLSRKQVD SEHMHQNVPT EEQRTNKSTG GEHKKSDRKE
510 520 530 540 550
EPQYEPANTS EDLDMDIVSV PSSVPEDIFE NLETAMEVQS SVDHQGDGSS
560 570 580 590 600
GTEQEVESSS VKLNISSKDN RGGIKSKTTA KVTKELYVKL TPVSLSNSPI
610 620 630 640 650
KGADCQEVPQ DKDGYKSCGL NPKLEKCGLG QENSDNEHLV ENEVSLLLEE
660 670 680 690 700
SDLRRSPRVK TTPLRRPTET NPVTSNSDEE CNETVKEKQK LSVPVRKKDK
710 720 730 740 750
RNSSDSAIDN PKPNKLPKSK QSETVDQNSD SDEMLAILKE VSRMSHSSSS
760 770 780 790 800
DTDINEIHTN HKTLYDLKTQ AGKDDKGKRK RKSSTSGSDF DTKKGKSAKS
810 820 830 840 850
SIISKKKRQT QSESSNYDSE LEKEIKSMSK IGAARTTKKR IPNTKDFDSS
860 870 880 890 900
EDEKHSKKGM DNQGHKNLKT SQEGSSDDAE RKQERETFSS AEGTVDKDTT
910 920 930 940 950
IMELRDRLPK KQQASASTDG VDKLSGKEQS FTSLEVRKVA ETKEKSKHLK
960 970 980 990 1000
TKTCKKVQDG LSDIAEKFLK KDQSDETSED DKKQSKKGTE EKKKPSDFKK
1010 1020 1030 1040 1050
KVIKMEQQYE SSSDGTEKLP EREEICHFPK GIKQIKNGTT DGEKKSKKIR
1060 1070 1080 1090 1100
DKTSKKKDEL SDYAEKSTGK GDSCDSSEDK KSKNGAYGRE KKRCKLLGKS
1110 1120 1130 1140 1150
SRKRQDCSSS DTEKYSMKED GCNSSDKRLK RIELRERRNL SSKRNTKEIQ
1160 1170 1180 1190 1200
SGSSSSDAEE SSEDNKKKKQ RTSSKKKAVI VKEKKRNSLR TSTKRKQADI
1210 1220 1230 1240 1250
TSSSSSDIED DDQNSIGEGS SDEQKIKPVT ENLVLSSHTG FCQSSGDEAL
1260 1270 1280 1290 1300
SKSVPVTVDD DDDDNDPENR IAKKMLLEEI KANLSSDEDG SSDDEPEEGK
1310 1320 1330 1340 1350
KRTGKQNEEN PGDEEAKNQV NSESDSDSEE SKKPRYRHRL LRHKLTVSDG
1360 1370 1380 1390 1400
ESGEEKKTKP KEHKEVKGRN RRKVSSEDSE DSDFQESGVS EEVSESEDEQ
1410 1420 1430 1440 1450
RPRTRSAKKA ELEENQRSYK QKKKRRRIKV QEDSSSENKS NSEEEEEEKE
1460 1470 1480 1490 1500
EEEEEEEEEE EEEEDENDDS KSPGKGRKKI RKILKDDKLR TETQNALKEE
1510 1520 1530 1540 1550
EERRKRIAER EREREKLREV IEIEDASPTK CPITTKLVLD EDEETKEPLV
1560 1570 1580 1590 1600
QVHRNMVIKL KPHQVDGVQF MWDCCCESVK KTKKSPGSGC ILAHCMGLGK
1610 1620 1630 1640 1650
TLQVVSFLHT VLLCDKLDFS TALVVCPLNT ALNWMNEFEK WQEGLKDDEK
1660 1670 1680 1690 1700
LEVSELATVK RPQERSYMLQ RWQEDGGVMI IGYEMYRNLA QGRNVKSRKL
1710 1720 1730 1740 1750
KEIFNKALVD PGPDFVVCDE GHILKNEASA VSKAMNSIRS RRRIILTGTP
1760 1770 1780 1790 1800
LQNNLIEYHC MVNFIKENLL GSIKEFRNRF INPIQNGQCA DSTMVDVRVM
1810 1820 1830 1840 1850
KKRAHILYEM LAGCVQRKDY TALTKFLPPK HEYVLAVRMT SIQCKLYQYY
1860 1870 1880 1890 1900
LDHLTGVGNN SEGGRGKAGA KLFQDFQMLS RIWTHPWCLQ LDYISKENKG
1910 1920 1930 1940 1950
YFDEDSMDEF IASDSDETSM SLSSDDYTKK KKKGKKGKKD SSSSGSGSDN
1960 1970 1980 1990 2000
DVEVIKVWNS RSRGGGEGNV DETGNNPSVS LKLEESKATS SSNPSSPAPD
2010 2020 2030 2040 2050
WYKDFVTDAD AEVLEHSGKM VLLFEILRMA EEIGDKVLVF SQSLISLDLI
2060 2070 2080 2090 2100
EDFLELASRE KTEDKDKPLI YKGEGKWLRN IDYYRLDGST TAQSRKKWAE
2110 2120 2130 2140 2150
EFNDETNVRG RLFIISTKAG SLGINLVAAN RVIIFDASWN PSYDIQSIFR
2160 2170 2180 2190 2200
VYRFGQTKPV YVYRFLAQGT MEDKIYDRQV TKQSLSFRVV DQQQVERHFT
2210 2220 2230 2240 2250
MNELTELYTF EPDLLDDPNS EKKKKRDTPM LPKDTILAEL LQIHKEHIVG
2260 2270 2280 2290 2300
YHEHDSLLDH KEEEELTEEE RKAAWAEYEA EKKGLTMRFN IPTGTNLPPV
2310 2320 2330 2340 2350
SFNSQTPYIP FNLGALSAMS NQQLEDLINQ GREKVVEATN SVTAVRIQPL
2360 2370 2380 2390 2400
EDIISAVWKE NMNLSEAQVQ ALALSRQASQ ELDVKRREAI YNDVLTKQQM
2410 2420 2430 2440 2450
LISCVQRILM NRRLQQQYNQ QQQQQMTYQQ ATLGHLMMPK PPNLIMNPSN
2460 2470 2480 2490
YQQIDMRGMY QPVAGGMQPP PLQRAPPPMR SKNPGPSQGK SM
Length:2,492
Mass (Da):282,586
Last modified:November 2, 2010 - v5
Checksum:i637E341F6A4B29C6
GO
Isoform 1 (identifier: P46100-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-204: Missing.

Show »
Length:2,288
Mass (Da):259,843
Checksum:iAB2B948725F62D77
GO
Isoform 2 (identifier: P46100-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-117: Missing.

Show »
Length:2,375
Mass (Da):269,811
Checksum:i7314428AA21A9687
GO
Isoform 3 (identifier: P46100-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     124-161: Missing.

Show »
Length:2,454
Mass (Da):278,229
Checksum:iED9320A642E01E2A
GO
Isoform 5 (identifier: P46100-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-117: Missing.
     124-161: Missing.

Show »
Length:2,337
Mass (Da):265,454
Checksum:i437268E2C2817FEA
GO
Isoform 6 (identifier: P46100-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     124-162: Missing.
     573-601: Missing.
     1419-2492: Missing.

Note: No experimental confirmation available.
Show »
Length:1,350
Mass (Da):151,556
Checksum:iA67E6A155955371A
GO

Sequence cautioni

The sequence AAA20872.1 differs from that shown.Many frameshifts and conflits.Curated
The sequence AAC50069.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence BAD92165.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti879 – 8791A → R in AAC50069 (PubMed:7874112).Curated
Sequence conflicti1286 – 12861S → P in BAD92165 (Ref. 4) Curated
Sequence conflicti1627 – 16271P → L in AAC50069 (PubMed:7874112).Curated
Sequence conflicti1632 – 16321L → F in AAC50069 (PubMed:7874112).Curated
Sequence conflicti2280 – 22801A → G in AAC50069 (PubMed:7874112).Curated
Sequence conflicti2283 – 22842KG → RV in AAC50069 (PubMed:7874112).Curated
Sequence conflicti2436 – 24361L → H in AAC50069 (PubMed:7874112).Curated
Sequence conflicti2442 – 24421P → R in AAC50069 (PubMed:7874112).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti175 – 1751G → E in ATRX. 1 Publication
VAR_012113
Natural varianti178 – 19821Missing in ATRX. 1 Publication
VAR_012114Add
BLAST
Natural varianti179 – 1791N → S in ATRX. 1 Publication
VAR_012115
Natural varianti190 – 1901P → A in ATRX; impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci. 1 Publication
VAR_001226
Natural varianti190 – 1901P → L in ATRX. 1 Publication
VAR_012116
Natural varianti190 – 1901P → S in ATRX. 1 Publication
VAR_012117
Natural varianti192 – 1921L → F in ATRX.
VAR_001227
Natural varianti194 – 1941V → I in ATRX. 1 Publication
VAR_012118
Natural varianti200 – 2001C → S in ATRX.
VAR_001228
Natural varianti219 – 2191Q → P in ATRX; greatly impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 3 Publications
VAR_012119
Natural varianti220 – 2201C → R in ATRX.
VAR_001229
Natural varianti220 – 2201C → Y in MRXSHF1. 1 Publication
VAR_032625
Natural varianti222 – 2221W → S in ATRX.
VAR_001230
Natural varianti243 – 2431C → F in ATRX.
VAR_001231
Natural varianti246 – 2461R → C in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 4 Publications
VAR_001232
Natural varianti246 – 2461R → L in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). 3 Publications
VAR_010914
Natural varianti249 – 2491G → C in ATRX. 1 Publication
VAR_012120
Natural varianti249 – 2491G → D in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization. 1 Publication
VAR_001233
Natural varianti409 – 4091L → S in MRXSHF1. 1 Publication
VAR_032626
Natural varianti545 – 5451Q → E.
Corresponds to variant rs35738915 [ dbSNP | Ensembl ].
VAR_055939
Natural varianti596 – 5961S → P.1 Publication
Corresponds to variant rs1051678 [ dbSNP | Ensembl ].
VAR_016914
Natural varianti740 – 7401E → G.1 Publication
Corresponds to variant rs1051680 [ dbSNP | Ensembl ].
VAR_016915
Natural varianti929 – 9291Q → E.1 Publication
Corresponds to variant rs3088074 [ dbSNP | Ensembl ].
VAR_023438
Natural varianti1538 – 15381V → G in ATRX; unknown pathological significance.
VAR_012121
Natural varianti1552 – 15521V → F in ATRX. 1 Publication
VAR_012122
Natural varianti1609 – 16091H → R in ATRX.
VAR_001234
Natural varianti1614 – 16141C → R in ATRX.
VAR_001235
Natural varianti1621 – 16211T → M in ATRX. 1 Publication
VAR_016916
Natural varianti1645 – 16451L → S in ATRX. 1 Publication
VAR_012123
Natural varianti1650 – 16501K → N in ATRX.
VAR_001236
Natural varianti1713 – 17131P → S in ATRX; without alpha-thalassemia. 1 Publication
VAR_012124
Natural varianti1742 – 17421R → K in ATRX; atypical; patients presents spastic paraplegia at birth. 1 Publication
VAR_012125
Natural varianti1847 – 18471Y → C in ATRX. 1 Publication
VAR_012126
Natural varianti1860 – 18601N → S Rare polymorphism. 1 Publication
Corresponds to variant rs45439799 [ dbSNP | Ensembl ].
VAR_001237
Natural varianti2035 – 20351D → V in ATRX; impairs ATPase activity. 1 Publication
VAR_001238
Natural varianti2050 – 20501I → T in MRXSHF1; originally reported as Carpenter-Waziri syndrome. 1 Publication
VAR_012127
Natural varianti2084 – 20841Y → H in ATRX; impairs ATPase activity. 1 Publication
VAR_001239
Natural varianti2131 – 21311R → Q in MRXSHF1; originally reported as Juberg-Marsidi syndrome. 1 Publication
VAR_001240
Natural varianti2163 – 21631Y → C in ATRX.
VAR_001241
Natural varianti2271 – 22711R → G in MRXSHF1. 1 Publication
VAR_032627

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 204204Missing in isoform 1. 1 PublicationVSP_000575Add
BLAST
Alternative sequencei1 – 117117Missing in isoform 2 and isoform 5. 2 PublicationsVSP_000574Add
BLAST
Alternative sequencei124 – 16239Missing in isoform 6. 1 PublicationVSP_015499Add
BLAST
Alternative sequencei124 – 16138Missing in isoform 3 and isoform 5. 1 PublicationVSP_000576Add
BLAST
Alternative sequencei573 – 60129Missing in isoform 6. 1 PublicationVSP_015500Add
BLAST
Alternative sequencei1419 – 24921074Missing in isoform 6. 1 PublicationVSP_015501Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72937 mRNA. Translation: AAB49970.2.
U72938 mRNA. Translation: AAB49971.2.
U72935
, U72904, U72905, U72907, U72908, U72909, U72910, U72911, U72912, U72913, U72914, U72915, U72916, U72917, U72918, U72919, U72920, U72921, U72922, U72923, U72924, U72925, U72926, U72927, U72928, U72929, U72930, U72931, U72932, U72933, U72934 Genomic DNA. Translation: AAB40698.1.
U72935
, U72904, U72907, U72908, U72909, U72910, U72911, U72912, U72913, U72914, U72915, U72916, U72918, U72919, U72920, U72921, U72922, U72923, U72924, U72925, U72926, U72927, U72928, U72929, U72930, U72931, U72932, U72933, U72934 Genomic DNA. Translation: AAB40699.1.
U72936 mRNA. Translation: AAB49969.1.
U72935
, U72908, U72909, U72910, U72911, U72912, U72913, U72914, U72915, U72916, U72917, U72918, U72920, U72921, U72922, U72923, U72924, U72925, U72926, U72927, U72928, U72929, U72930, U72931, U72932, U72933, U72934 Genomic DNA. Translation: AAB40700.1.
U75653 Genomic DNA. Translation: AAC51655.1.
U97103
, AF000157, AF000158, AF000159, AF000160, U97080, U97081, U97082, U97083, U97084, U97085, U97086, U97087, U97088, U97089, U97090, U97091, U97092, U97093, U97094, U97095, U97096, U97097, U97098, U97099, U97100, U97101, U97102 Genomic DNA. Translation: AAC51657.1.
AB102641 mRNA. Translation: BAC81110.1.
AB101681 Genomic DNA. Translation: BAC80270.1.
AB101682 Genomic DNA. Translation: BAC80271.1.
AB101683 Genomic DNA. Translation: BAC80272.1.
AB101685 Genomic DNA. Translation: BAC80274.1.
AB101687 Genomic DNA. Translation: BAC80276.1.
AB101689 Genomic DNA. Translation: BAC80278.1.
AB101691 Genomic DNA. Translation: BAC80280.1.
AB101693 Genomic DNA. Translation: BAC80282.1.
AB101695 Genomic DNA. Translation: BAC80284.1.
AB101700 Genomic DNA. Translation: BAC80289.1.
AB101699 Genomic DNA. Translation: BAC80288.1.
AB101698 Genomic DNA. Translation: BAC80287.1.
AB101697 Genomic DNA. Translation: BAC80286.1.
AB101696 Genomic DNA. Translation: BAC80285.1.
AB101694 Genomic DNA. Translation: BAC80283.1.
AB101692 Genomic DNA. Translation: BAC80281.1.
AB101690 Genomic DNA. Translation: BAC80279.1.
AB101688 Genomic DNA. Translation: BAC80277.1.
AB101686 Genomic DNA. Translation: BAC80275.1.
AB101684 Genomic DNA. Translation: BAC80273.1.
AB208928 mRNA. Translation: BAD92165.1. Different initiation.
AB209545 mRNA. Translation: BAD92782.1.
AL121874 Genomic DNA. Translation: CAB90351.2.
AL121874, AL109753, Z84487 Genomic DNA. Translation: CAI40710.1.
Z84487, AL109753, AL121874 Genomic DNA. Translation: CAI42674.1.
Z84487, AL109753, AL121874 Genomic DNA. Translation: CAI42675.1.
AL109753, AL121874, Z84487 Genomic DNA. Translation: CAI43115.1.
AL109753, AL121874, Z84487 Genomic DNA. Translation: CAI43116.1.
CH471104 Genomic DNA. Translation: EAW98611.1.
CH471104 Genomic DNA. Translation: EAW98615.1.
U09820 mRNA. Translation: AAC50069.1. Frameshift.
L34363 Genomic DNA. Translation: AAA20872.1. Sequence problems.
X83753 Genomic DNA. Translation: CAA58711.1.
CCDSiCCDS14434.1. [P46100-1]
CCDS14435.1. [P46100-4]
PIRiI38614.
I54367.
RefSeqiNP_000480.3. NM_000489.4.
NP_612114.2. NM_138270.3.
UniGeneiHs.533526.
Hs.653797.

Genome annotation databases

EnsembliENST00000373344; ENSP00000362441; ENSG00000085224.
ENST00000395603; ENSP00000378967; ENSG00000085224.
GeneIDi546.
KEGGihsa:546.
UCSCiuc004ecp.5. human. [P46100-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72937 mRNA. Translation: AAB49970.2.
U72938 mRNA. Translation: AAB49971.2.
U72935
, U72904, U72905, U72907, U72908, U72909, U72910, U72911, U72912, U72913, U72914, U72915, U72916, U72917, U72918, U72919, U72920, U72921, U72922, U72923, U72924, U72925, U72926, U72927, U72928, U72929, U72930, U72931, U72932, U72933, U72934 Genomic DNA. Translation: AAB40698.1.
U72935
, U72904, U72907, U72908, U72909, U72910, U72911, U72912, U72913, U72914, U72915, U72916, U72918, U72919, U72920, U72921, U72922, U72923, U72924, U72925, U72926, U72927, U72928, U72929, U72930, U72931, U72932, U72933, U72934 Genomic DNA. Translation: AAB40699.1.
U72936 mRNA. Translation: AAB49969.1.
U72935
, U72908, U72909, U72910, U72911, U72912, U72913, U72914, U72915, U72916, U72917, U72918, U72920, U72921, U72922, U72923, U72924, U72925, U72926, U72927, U72928, U72929, U72930, U72931, U72932, U72933, U72934 Genomic DNA. Translation: AAB40700.1.
U75653 Genomic DNA. Translation: AAC51655.1.
U97103
, AF000157, AF000158, AF000159, AF000160, U97080, U97081, U97082, U97083, U97084, U97085, U97086, U97087, U97088, U97089, U97090, U97091, U97092, U97093, U97094, U97095, U97096, U97097, U97098, U97099, U97100, U97101, U97102 Genomic DNA. Translation: AAC51657.1.
AB102641 mRNA. Translation: BAC81110.1.
AB101681 Genomic DNA. Translation: BAC80270.1.
AB101682 Genomic DNA. Translation: BAC80271.1.
AB101683 Genomic DNA. Translation: BAC80272.1.
AB101685 Genomic DNA. Translation: BAC80274.1.
AB101687 Genomic DNA. Translation: BAC80276.1.
AB101689 Genomic DNA. Translation: BAC80278.1.
AB101691 Genomic DNA. Translation: BAC80280.1.
AB101693 Genomic DNA. Translation: BAC80282.1.
AB101695 Genomic DNA. Translation: BAC80284.1.
AB101700 Genomic DNA. Translation: BAC80289.1.
AB101699 Genomic DNA. Translation: BAC80288.1.
AB101698 Genomic DNA. Translation: BAC80287.1.
AB101697 Genomic DNA. Translation: BAC80286.1.
AB101696 Genomic DNA. Translation: BAC80285.1.
AB101694 Genomic DNA. Translation: BAC80283.1.
AB101692 Genomic DNA. Translation: BAC80281.1.
AB101690 Genomic DNA. Translation: BAC80279.1.
AB101688 Genomic DNA. Translation: BAC80277.1.
AB101686 Genomic DNA. Translation: BAC80275.1.
AB101684 Genomic DNA. Translation: BAC80273.1.
AB208928 mRNA. Translation: BAD92165.1. Different initiation.
AB209545 mRNA. Translation: BAD92782.1.
AL121874 Genomic DNA. Translation: CAB90351.2.
AL121874, AL109753, Z84487 Genomic DNA. Translation: CAI40710.1.
Z84487, AL109753, AL121874 Genomic DNA. Translation: CAI42674.1.
Z84487, AL109753, AL121874 Genomic DNA. Translation: CAI42675.1.
AL109753, AL121874, Z84487 Genomic DNA. Translation: CAI43115.1.
AL109753, AL121874, Z84487 Genomic DNA. Translation: CAI43116.1.
CH471104 Genomic DNA. Translation: EAW98611.1.
CH471104 Genomic DNA. Translation: EAW98615.1.
U09820 mRNA. Translation: AAC50069.1. Frameshift.
L34363 Genomic DNA. Translation: AAA20872.1. Sequence problems.
X83753 Genomic DNA. Translation: CAA58711.1.
CCDSiCCDS14434.1. [P46100-1]
CCDS14435.1. [P46100-4]
PIRiI38614.
I54367.
RefSeqiNP_000480.3. NM_000489.4.
NP_612114.2. NM_138270.3.
UniGeneiHs.533526.
Hs.653797.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JM1NMR-A159-296[»]
2LBMNMR-A163-296[»]
2LD1NMR-A163-296[»]
3QL9X-ray0.93A167-289[»]
3QLAX-ray1.60A/D167-289[»]
3QLCX-ray2.50A/B167-289[»]
3QLNX-ray1.90A/B167-289[»]
4W5AX-ray2.60A/B/E167-289[»]
ProteinModelPortaliP46100.
SMRiP46100. Positions 159-296.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107028. 59 interactions.
DIPiDIP-31532N.
IntActiP46100. 30 interactions.
MINTiMINT-1186201.
STRINGi9606.ENSP00000362441.

PTM databases

iPTMnetiP46100.
PhosphoSiteiP46100.

Polymorphism and mutation databases

DMDMi311033500.

Proteomic databases

EPDiP46100.
MaxQBiP46100.
PaxDbiP46100.
PeptideAtlasiP46100.
PRIDEiP46100.

Protocols and materials databases

DNASUi546.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373344; ENSP00000362441; ENSG00000085224.
ENST00000395603; ENSP00000378967; ENSG00000085224.
GeneIDi546.
KEGGihsa:546.
UCSCiuc004ecp.5. human. [P46100-1]

Organism-specific databases

CTDi546.
GeneCardsiATRX.
GeneReviewsiATRX.
H-InvDBHIX0176765.
HGNCiHGNC:886. ATRX.
HPAiCAB009372.
CAB068176.
HPA001906.
HPA064684.
MalaCardsiATRX.
MIMi300032. gene.
300448. phenotype.
301040. phenotype.
309580. phenotype.
neXtProtiNX_P46100.
Orphaneti231401. Alpha-thalassemia - myelodysplastic syndrome.
847. Alpha-thalassemia - X-linked intellectual disability syndrome.
93973. Carpenter-Waziri syndrome.
93971. Chudley-Lowry-Hoar syndrome.
93970. Holmes-Gang syndrome.
93972. Juberg-Marsidi syndrome.
93974. Smith-Fineman-Myers syndrome.
PharmGKBiPA25179.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1015. Eukaryota.
COG0553. LUCA.
HOVERGENiHBG000104.
InParanoidiP46100.
KOiK10779.
OrthoDBiEOG7G4QDQ.
PhylomeDBiP46100.
TreeFamiTF313172.

Enzyme and pathway databases

SIGNORiP46100.

Miscellaneous databases

EvolutionaryTraceiP46100.
GeneWikiiATRX.
GenomeRNAii546.
PROiP46100.
SOURCEiSearch...

Gene expression databases

BgeeiP46100.
CleanExiHS_RAD54L.
ExpressionAtlasiP46100. baseline and differential.
GenevisibleiP46100. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR025766. ADD.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51533. ADD. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ATRX encodes a novel member of the SNF2 family of proteins: mutations point to a common mechanism underlying the ATR-X syndrome."
    Picketts D.J., Higgs D.R., Bachoo S., Blake D.J., Quarrell O.W.J., Gibbons R.J.
    Hum. Mol. Genet. 5:1899-1907(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), VARIANT SER-1860, VARIANTS ATRX.
  2. "Determination of the genomic structure of the XNP/ATRX gene encoding a potential zinc finger helicase."
    Villard L., Lossi A.-M., Cardoso C., Proud V., Chiaroni P., Colleaux L., Schwartz C., Fontes M.
    Genomics 43:149-155(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), VARIANTS PRO-596 AND GLY-740.
  3. "Gene diversity patterns at 10 X-chromosomal loci in humans and chimpanzees."
    Kitano T., Schwarz C., Nickel B., Paeaebo S.
    Mol. Biol. Evol. 20:1281-1289(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 163-198.
  4. 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
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 704-1927 (ISOFORMS 1/2/3/4/5), VARIANT GLU-929.
    Tissue: Brain.
  5. "The DNA sequence of the human X chromosome."
    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.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 860-2492.
  8. "Cloning and expression of the murine homologue of a putative human X-linked nuclear protein gene closely linked to PGK1 in Xq13.3."
    Gecz J., Pollard H., Consalez G., Villard L., Stayton C.L., Millasseau P., Khrestchatisky M., Fontes M.
    Hum. Mol. Genet. 3:39-44(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  9. "Mutations in a putative global transcriptional regulator cause X-linked mental retardation with alpha-thalassemia (ATR-X syndrome)."
    Gibbons R.J., Picketts D.J., Villard L., Higgs D.R.
    Cell 80:837-845(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2401-2492, VARIANTS ATRX.
  10. "Specific interaction between the XNP/ATR-X gene product and the SET domain of the human EZH2 protein."
    Cardoso C., Timsit S., Villard L., Khrestchatisky M., Fontes M., Colleaux L.
    Hum. Mol. Genet. 7:679-684(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EZH2.
  11. "Localization of a putative transcriptional regulator (ATRX) at pericentromeric heterochromatin and the short arms of acrocentric chromosomes."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 96:13983-13988(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH PERICENTROMERIC HETEROCHROMATIN.
  12. "Identification of a mutation in the XNP/ATR-X gene in a family reported as Smith-Fineman-Myers syndrome."
    Villard L., Fontes M., Ades L.C., Gecz J.
    Am. J. Med. Genet. 91:83-85(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MRXSHF1.
  13. "Cell cycle-dependent phosphorylation of the ATRX protein correlates with changes in nuclear matrix and chromatin association."
    Berube N.G., Smeenk C.A., Picketts D.J.
    Hum. Mol. Genet. 9:539-547(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBX5, PHOSPHORYLATION.
  14. "Identification of acquired somatic mutations in the gene encoding chromatin-remodeling factor ATRX in the alpha-thalassemia myelodysplasia syndrome (ATMDS)."
    Gibbons R.J., Pellagatti A., Garrick D., Wood W.G., Malik N., Ayyub H., Langford C., Boultwood J., Wainscoat J.S., Higgs D.R.
    Nat. Genet. 34:446-449(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ATMDS.
  15. "The ATRX syndrome protein forms a chromatin-remodeling complex with Daxx and localizes in promyelocytic leukemia nuclear bodies."
    Xue Y., Gibbons R., Yan Z., Yang D., McDowell T.L., Sechi S., Qin J., Zhou S., Higgs D., Wang W.
    Proc. Natl. Acad. Sci. U.S.A. 100:10635-10640(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DAXX, SUBCELLULAR LOCATION.
  16. "A novel transcription regulatory complex containing death domain-associated protein and the ATR-X syndrome protein."
    Tang J., Wu S., Liu H., Stratt R., Barak O.G., Shiekhattar R., Picketts D.J., Yang X.
    J. Biol. Chem. 279:20369-20377(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DAXX, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-1600, CHARACTERIZATION OF VARIANTS ATRX VAL-2035 AND HIS-2084.
  17. "The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain."
    Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III
    Biochem. Biophys. Res. Commun. 331:929-937(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBX5.
  18. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634 AND SER-1352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "Interaction between chromatin proteins MECP2 and ATRX is disrupted by mutations that cause inherited mental retardation."
    Nan X., Hou J., Maclean A., Nasir J., Lafuente M.J., Shu X., Kriaucionis S., Bird A.
    Proc. Natl. Acad. Sci. U.S.A. 104:2709-2714(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MECP2.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  21. Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; TYR-89; SER-112 AND SER-1996, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  24. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-967, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  26. Cited for: ASSOCIATION WITH HISTONE H3.3.
  27. "The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3."
    Drane P., Ouararhni K., Depaux A., Shuaib M., Hamiche A.
    Genes Dev. 24:1253-1265(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  28. "Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres."
    Lewis P.W., Elsaesser S.J., Noh K.M., Stadler S.C., Allis C.D.
    Proc. Natl. Acad. Sci. U.S.A. 107:14075-14080(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE ATRX:DAXX COMPLEX.
  29. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "The ATRX-ADD domain binds to H3 tail peptides and reads the combined methylation state of K4 and K9."
    Dhayalan A., Tamas R., Bock I., Tattermusch A., Dimitrova E., Kudithipudi S., Ragozin S., Jeltsch A.
    Hum. Mol. Genet. 20:2195-2203(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIMETHYLATED HISTONE H3 'LYS-9', CHARACTERIZATION OF VARIANTS ATR