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Entry version 219 (16 Oct 2019)
Sequence version 5 (02 Nov 2010)
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Protein

Transcriptional regulator ATRX

Gene

ATRX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 telomeres. 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 telomeres 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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri170 – 206GATA-type; atypicalPROSITE-ProRule annotationAdd BLAST37
Zinc fingeri217 – 272PHD-type; atypicalPROSITE-ProRule annotationAdd BLAST56
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1594 – 1601ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChromatin regulator, DNA-binding, Helicase, Hydrolase
Biological processDNA damage, DNA repair, Transcription, Transcription regulation
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

SIGNOR Signaling Network Open Resource

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SIGNORi
P46100

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ATRX
Synonyms:RAD54L, XH2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:886 ATRX

Online Mendelian Inheritance in Man (OMIM)

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MIMi
300032 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P46100

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Alpha-thalassemia mental retardation syndrome, X-linked (ATRX)12 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_012113175G → E in ATRX. 1 Publication1
Natural variantiVAR_012114178 – 198Missing in ATRX. 1 PublicationAdd BLAST21
Natural variantiVAR_012115179N → S in ATRX. 1 PublicationCorresponds to variant dbSNP:rs398123425EnsemblClinVar.1
Natural variantiVAR_001226190P → A in ATRX; impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci. 1 PublicationCorresponds to variant dbSNP:rs122445103EnsemblClinVar.1
Natural variantiVAR_012116190P → L in ATRX. 1 PublicationCorresponds to variant dbSNP:rs1057518708EnsemblClinVar.1
Natural variantiVAR_012117190P → S in ATRX. 1 Publication1
Natural variantiVAR_001227192L → F in ATRX. 1
Natural variantiVAR_012118194V → I in ATRX. 1 Publication1
Natural variantiVAR_001228200C → S in ATRX. 1
Natural variantiVAR_012119219Q → P in ATRX; greatly impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 3 Publications1
Natural variantiVAR_001229220C → R in ATRX. 1
Natural variantiVAR_001230222W → S in ATRX. 1
Natural variantiVAR_001231243C → F in ATRX. 1
Natural variantiVAR_001232246R → C in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 4 PublicationsCorresponds to variant dbSNP:rs122445105EnsemblClinVar.1
Natural variantiVAR_010914246R → L in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). 3 Publications1
Natural variantiVAR_012120249G → C in ATRX. 1 Publication1
Natural variantiVAR_001233249G → D in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization. 1 Publication1
Natural variantiVAR_0121211538V → G in ATRX; unknown pathological significance. 1
Natural variantiVAR_0121221552V → F in ATRX. 1 Publication1
Natural variantiVAR_0012341609H → R in ATRX. Corresponds to variant dbSNP:rs122445093EnsemblClinVar.1
Natural variantiVAR_0012351614C → R in ATRX. Corresponds to variant dbSNP:rs122445094EnsemblClinVar.1
Natural variantiVAR_0169161621T → M in ATRX. 1 PublicationCorresponds to variant dbSNP:rs122445106EnsemblClinVar.1
Natural variantiVAR_0121231645L → S in ATRX. 1 Publication1
Natural variantiVAR_0012361650K → N in ATRX. Corresponds to variant dbSNP:rs122445095EnsemblClinVar.1
Natural variantiVAR_0121241713P → S in ATRX; without alpha-thalassemia. 1 Publication1
Natural variantiVAR_0121251742R → K in ATRX; atypical; patients presents spastic paraplegia at birth. 1 PublicationCorresponds to variant dbSNP:rs122445104EnsemblClinVar.1
Natural variantiVAR_0121261847Y → C in ATRX. 1 Publication1
Natural variantiVAR_0012382035D → V in ATRX; impairs ATPase activity. 1 PublicationCorresponds to variant dbSNP:rs122445096EnsemblClinVar.1
Natural variantiVAR_0012392084Y → H in ATRX; impairs ATPase activity. 1 PublicationCorresponds to variant dbSNP:rs122445097EnsemblClinVar.1
Natural variantiVAR_0012412163Y → C in ATRX. Corresponds to variant dbSNP:rs122445098EnsemblClinVar.1
Mental retardation-hypotonic facies syndrome, X-linked, 1 (MRXHF1)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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_032625220C → Y in MRXHF1. 1 PublicationCorresponds to variant dbSNP:rs122445111EnsemblClinVar.1
Natural variantiVAR_032626409L → S in MRXHF1. 1 PublicationCorresponds to variant dbSNP:rs122445109EnsemblClinVar.1
Natural variantiVAR_0121272050I → T in MRXHF1; originally reported as Carpenter-Waziri syndrome. 1 PublicationCorresponds to variant dbSNP:rs122445110EnsemblClinVar.1
Natural variantiVAR_0012402131R → Q in MRXHF1; originally reported as Juberg-Marsidi syndrome. 1 PublicationCorresponds to variant dbSNP:rs122445101EnsemblClinVar.1
Natural variantiVAR_0326272271R → G in MRXHF1. 1 PublicationCorresponds to variant dbSNP:rs122445112EnsemblClinVar.1
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.
Related information in OMIM

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi189H → N: Impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci. 1 Publication1
Mutagenesisi203Y → A or K: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization. 3 Publications1
Mutagenesisi204Y → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 2 Publications1
Mutagenesisi207D → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 1
Mutagenesisi209I → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). 1 Publication1
Mutagenesisi214D → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). 1 Publication1
Mutagenesisi217D → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization. 2 Publications1
Mutagenesisi218E → A: Impairs interaction with histone H3 peptides unmethylated at 'Lys-5' (H3K4me0); reduces pericentromeric localization. 1 Publication1
Mutagenesisi252E → L: Impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci. 1 Publication1
Mutagenesisi1600K → R: Abolishes ATPAse activity, no effect on pericentromeric heterochromatin localization. 2 Publications1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET

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DisGeNETi
546

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
ATRX

MalaCards human disease database

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MalaCardsi
ATRX
MIMi300448 phenotype
301040 phenotype
309580 phenotype

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
231401 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
100075 Neuroendocrine tumor of stomach
93974 Smith-Fineman-Myers syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA25179

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P46100

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
ATRX

Domain mapping of disease mutations (DMDM)

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DMDMi
311033500

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000743011 – 2492Transcriptional regulator ATRXAdd BLAST2492

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki10Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei25PhosphoserineCombined sources1
Modified residuei34PhosphoserineCombined sources1
Modified residuei89PhosphotyrosineCombined sources1
Modified residuei92PhosphoserineCombined sources1
Modified residuei112PhosphoserineCombined sources1
Cross-linki138Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei213PhosphoserineBy similarity1
Cross-linki299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei316PhosphoserineCombined sources1
Cross-linki438Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei591PhosphothreonineCombined sources1
Modified residuei594PhosphoserineCombined sources1
Modified residuei598PhosphoserineCombined sources1
Cross-linki623Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki623Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei634PhosphoserineCombined sources1
Modified residuei674PhosphothreonineCombined sources1
Modified residuei675PhosphoserineCombined sources1
Modified residuei677PhosphoserineCombined sources1
Modified residuei729PhosphoserineCombined sources1
Modified residuei731PhosphoserineCombined sources1
Modified residuei784PhosphoserineBy similarity1
Modified residuei819PhosphoserineCombined sources1
Modified residuei849PhosphoserineCombined sources1
Modified residuei850PhosphoserineCombined sources1
Modified residuei875PhosphoserineCombined sources1
Modified residuei876PhosphoserineCombined sources1
Modified residuei889PhosphoserineCombined sources1
Modified residuei962PhosphoserineCombined sources1
Modified residuei967N6-acetyllysineCombined sources1
Modified residuei974PhosphoserineCombined sources1
Modified residuei977PhosphothreonineCombined sources1
Cross-linki1004Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1011PhosphoserineBy similarity1
Modified residuei1012PhosphoserineBy similarity1
Modified residuei1013PhosphoserineBy similarity1
Modified residuei1061PhosphoserineCombined sources1
Modified residuei1063PhosphotyrosineCombined sources1
Modified residuei1244PhosphoserineBy similarity1
Modified residuei1245PhosphoserineBy similarity1
Modified residuei1253PhosphoserineBy similarity1
Modified residuei1322PhosphoserineCombined sources1
Modified residuei1324PhosphoserineCombined sources1
Modified residuei1326PhosphoserineCombined sources1
Modified residuei1348PhosphoserineCombined sources1
Modified residuei1352PhosphoserineCombined sources1
Cross-linki1488Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1527PhosphoserineCombined sources1
Modified residuei1529PhosphothreonineCombined sources1
Modified residuei1906PhosphoserineBy similarity1
Modified residuei1913PhosphoserineBy similarity1
Cross-linki1982Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki1982Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki1987Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1992PhosphoserineCombined sources1
Modified residuei1996PhosphoserineCombined sources1
Modified residuei2220PhosphoserineCombined sources1
Modified residuei2474Omega-N-methylarginineBy similarity1
Modified residuei2480Omega-N-methylarginineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P46100

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P46100

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P46100

MaxQB - The MaxQuant DataBase

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MaxQBi
P46100

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P46100

PeptideAtlas

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PeptideAtlasi
P46100

PRoteomics IDEntifications database

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PRIDEi
P46100

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
55726 [P46100-1]
55727 [P46100-2]
55728 [P46100-3]
55729 [P46100-4]
55730 [P46100-5]
55731 [P46100-6]

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P46100

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P46100

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P46100

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitous.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000085224 Expressed in 244 organ(s), highest expression level in frontal cortex

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P46100 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P46100 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB009372
CAB068176
HPA001906
HPA064684

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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, MRE11 and NBN; indicative for an association with the MRN complex.

Interacts with histone H2AFY.

Interacts with histone H3 peptides methylated at 'Lys-10' with preferences H3K9me3 > H3K9me2 > H3K9me1.

Interacts with histone H3 peptides unmethylated at 'Lys-5' (H3K4me0).

Interacts with MECP2, SMC1 and SMC3.

Interacts with SETDB1, TRIM28 and ZNF274 (PubMed:27029610).

12 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
107028, 83 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P46100

Database of interacting proteins

More...
DIPi
DIP-31532N

Protein interaction database and analysis system

More...
IntActi
P46100, 42 interactors

Molecular INTeraction database

More...
MINTi
P46100

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000362441

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

12492
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P46100

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P46100

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini159 – 296ADDPROSITE-ProRule annotationAdd BLAST138
Domaini1581 – 1768Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST188
Domaini2025 – 2205Helicase C-terminalPROSITE-ProRule annotationAdd BLAST181

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1189 – 1326Interaction with DAXXAdd BLAST138
Regioni2010 – 2280Interaction with MECP21 PublicationAdd BLAST271

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi581 – 594PxVxL motifAdd BLAST14
Motifi1719 – 1722DEGH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi745 – 750Poly-Ser6
Compositional biasi1151 – 1156Poly-Ser6
Compositional biasi1166 – 1169Poly-Lys4
Compositional biasi1202 – 1206Poly-Ser5
Compositional biasi1259 – 1266Poly-Asp8
Compositional biasi1443 – 1466Poly-GluAdd BLAST24
Compositional biasi1499 – 1502Poly-Glu4
Compositional biasi1929 – 1939Poly-LysAdd BLAST11
Compositional biasi1941 – 1948Poly-Ser8
Compositional biasi2222 – 2225Poly-Lys4
Compositional biasi2262 – 2265Poly-Glu4
Compositional biasi2420 – 2425Poly-Gln6

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri170 – 206GATA-type; atypicalPROSITE-ProRule annotationAdd BLAST37
Zinc fingeri217 – 272PHD-type; atypicalPROSITE-ProRule annotationAdd BLAST56

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1015 Eukaryota
COG0553 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P46100

KEGG Orthology (KO)

More...
KOi
K10779

Database of Orthologous Groups

More...
OrthoDBi
1258783at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P46100

TreeFam database of animal gene trees

More...
TreeFami
TF313172

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.40.10, 1 hit
3.40.50.10810, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR025766 ADD
IPR041430 ADD_ATRX
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase
IPR038718 SNF2-like_sf
IPR000330 SNF2_N
IPR011011 Znf_FYVE_PHD
IPR013083 Znf_RING/FYVE/PHD

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF17981 ADD_ATRX, 1 hit
PF00271 Helicase_C, 1 hit
PF00176 SNF2_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 2 hits
SSF57903 SSF57903, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51533 ADD, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (6+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 6 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 6 described isoforms and 11 potential isoforms that are computationally mapped.Show allAlign All

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

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 11 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A096LNL9A0A096LNL9_HUMAN
Transcriptional regulator ATRX
ATRX
1,351Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A096LNN3A0A096LNN3_HUMAN
Transcriptional regulator ATRX
ATRX
528Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A096LNW1A0A096LNW1_HUMAN
Transcriptional regulator ATRX
ATRX
954Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A096LNL6A0A096LNL6_HUMAN
Transcriptional regulator ATRX
ATRX
198Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A096LNL7A0A096LNL7_HUMAN
Transcriptional regulator ATRX
ATRX
108Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WWG0A0A087WWG0_HUMAN
Transcriptional regulator ATRX
ATRX
164Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A096LNR8A0A096LNR8_HUMAN
Transcriptional regulator ATRX
ATRX
66Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A096LP59A0A096LP59_HUMAN
Transcriptional regulator ATRX
ATRX
293Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A096LPG6A0A096LPG6_HUMAN
Transcriptional regulator ATRX
ATRX
47Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0Y3T0H0Y3T0_HUMAN
Transcriptional regulator ATRX
ATRX
198Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
There is more potential isoformShow all

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA20872 differs from that shown. Many frameshifts and conflits.Curated
The sequence AAC50069 differs from that shown. Reason: Frameshift.Curated
The sequence BAD92165 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti879A → R in AAC50069 (PubMed:7874112).Curated1
Sequence conflicti1286S → P in BAD92165 (Ref. 4) Curated1
Sequence conflicti1627P → L in AAC50069 (PubMed:7874112).Curated1
Sequence conflicti1632L → F in AAC50069 (PubMed:7874112).Curated1
Sequence conflicti2280A → G in AAC50069 (PubMed:7874112).Curated1
Sequence conflicti2283 – 2284KG → RV in AAC50069 (PubMed:7874112).Curated2
Sequence conflicti2436L → H in AAC50069 (PubMed:7874112).Curated1
Sequence conflicti2442P → R in AAC50069 (PubMed:7874112).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_012113175G → E in ATRX. 1 Publication1
Natural variantiVAR_012114178 – 198Missing in ATRX. 1 PublicationAdd BLAST21
Natural variantiVAR_012115179N → S in ATRX. 1 PublicationCorresponds to variant dbSNP:rs398123425EnsemblClinVar.1
Natural variantiVAR_001226190P → A in ATRX; impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci. 1 PublicationCorresponds to variant dbSNP:rs122445103EnsemblClinVar.1
Natural variantiVAR_012116190P → L in ATRX. 1 PublicationCorresponds to variant dbSNP:rs1057518708EnsemblClinVar.1
Natural variantiVAR_012117190P → S in ATRX. 1 Publication1
Natural variantiVAR_001227192L → F in ATRX. 1
Natural variantiVAR_012118194V → I in ATRX. 1 Publication1
Natural variantiVAR_001228200C → S in ATRX. 1
Natural variantiVAR_012119219Q → P in ATRX; greatly impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 3 Publications1
Natural variantiVAR_001229220C → R in ATRX. 1
Natural variantiVAR_032625220C → Y in MRXHF1. 1 PublicationCorresponds to variant dbSNP:rs122445111EnsemblClinVar.1
Natural variantiVAR_001230222W → S in ATRX. 1
Natural variantiVAR_001231243C → F in ATRX. 1
Natural variantiVAR_001232246R → C in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 4 PublicationsCorresponds to variant dbSNP:rs122445105EnsemblClinVar.1
Natural variantiVAR_010914246R → L in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). 3 Publications1
Natural variantiVAR_012120249G → C in ATRX. 1 Publication1
Natural variantiVAR_001233249G → D in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization. 1 Publication1
Natural variantiVAR_032626409L → S in MRXHF1. 1 PublicationCorresponds to variant dbSNP:rs122445109EnsemblClinVar.1
Natural variantiVAR_055939545Q → E. Corresponds to variant dbSNP:rs35738915EnsemblClinVar.1
Natural variantiVAR_016914596S → P1 PublicationCorresponds to variant dbSNP:rs1051678Ensembl.1
Natural variantiVAR_016915740E → G1 PublicationCorresponds to variant dbSNP:rs1051680Ensembl.1
Natural variantiVAR_023438929Q → E1 PublicationCorresponds to variant dbSNP:rs3088074Ensembl.1
Natural variantiVAR_0121211538V → G in ATRX; unknown pathological significance. 1
Natural variantiVAR_0121221552V → F in ATRX. 1 Publication1
Natural variantiVAR_0012341609H → R in ATRX. Corresponds to variant dbSNP:rs122445093EnsemblClinVar.1
Natural variantiVAR_0012351614C → R in ATRX. Corresponds to variant dbSNP:rs122445094EnsemblClinVar.1
Natural variantiVAR_0169161621T → M in ATRX. 1 PublicationCorresponds to variant dbSNP:rs122445106EnsemblClinVar.1
Natural variantiVAR_0121231645L → S in ATRX. 1 Publication1
Natural variantiVAR_0012361650K → N in ATRX. Corresponds to variant dbSNP:rs122445095EnsemblClinVar.1
Natural variantiVAR_0121241713P → S in ATRX; without alpha-thalassemia. 1 Publication1
Natural variantiVAR_0121251742R → K in ATRX; atypical; patients presents spastic paraplegia at birth. 1 PublicationCorresponds to variant dbSNP:rs122445104EnsemblClinVar.1
Natural variantiVAR_0121261847Y → C in ATRX. 1 Publication1
Natural variantiVAR_0012371860N → S Rare polymorphism. 1 PublicationCorresponds to variant dbSNP:rs45439799EnsemblClinVar.1
Natural variantiVAR_0012382035D → V in ATRX; impairs ATPase activity. 1 PublicationCorresponds to variant dbSNP:rs122445096EnsemblClinVar.1
Natural variantiVAR_0121272050I → T in MRXHF1; originally reported as Carpenter-Waziri syndrome. 1 PublicationCorresponds to variant dbSNP:rs122445110EnsemblClinVar.1
Natural variantiVAR_0012392084Y → H in ATRX; impairs ATPase activity. 1 PublicationCorresponds to variant dbSNP:rs122445097EnsemblClinVar.1
Natural variantiVAR_0012402131R → Q in MRXHF1; originally reported as Juberg-Marsidi syndrome. 1 PublicationCorresponds to variant dbSNP:rs122445101EnsemblClinVar.1
Natural variantiVAR_0012412163Y → C in ATRX. Corresponds to variant dbSNP:rs122445098EnsemblClinVar.1
Natural variantiVAR_0326272271R → G in MRXHF1. 1 PublicationCorresponds to variant dbSNP:rs122445112EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0005751 – 204Missing in isoform 1. 1 PublicationAdd BLAST204
Alternative sequenceiVSP_0005741 – 117Missing in isoform 2 and isoform 5. 2 PublicationsAdd BLAST117
Alternative sequenceiVSP_015499124 – 162Missing in isoform 6. 1 PublicationAdd BLAST39
Alternative sequenceiVSP_000576124 – 161Missing in isoform 3 and isoform 5. 1 PublicationAdd BLAST38
Alternative sequenceiVSP_015500573 – 601Missing in isoform 6. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_0155011419 – 2492Missing in isoform 6. 1 PublicationAdd BLAST1074

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS14434.1 [P46100-1]
CCDS14435.1 [P46100-4]

Protein sequence database of the Protein Information Resource

More...
PIRi
I38614
I54367

NCBI Reference Sequences

More...
RefSeqi
NP_000480.3, NM_000489.4
NP_612114.2, NM_138270.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000373344; ENSP00000362441; ENSG00000085224
ENST00000395603; ENSP00000378967; ENSG00000085224

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
546

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:546

UCSC genome browser

More...
UCSCi
uc004ecp.5 human [P46100-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB 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[»]
5GRQX-ray1.58C/D1256-1285[»]
5Y18X-ray2.20B1268-1289[»]
5Y6OX-ray3.10A/B/C/D/E/F/G/H/I1265-1288[»]
6G0OX-ray1.40B1027-1037[»]
SMRiP46100
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi107028, 83 interactors
CORUMiP46100
DIPiDIP-31532N
IntActiP46100, 42 interactors
MINTiP46100
STRINGi9606.ENSP00000362441

PTM databases

CarbonylDBiP46100
iPTMnetiP46100
PhosphoSitePlusiP46100

Polymorphism and mutation databases

BioMutaiATRX
DMDMi311033500

Proteomic databases

EPDiP46100
jPOSTiP46100
MassIVEiP46100
MaxQBiP46100
PaxDbiP46100
PeptideAtlasiP46100
PRIDEiP46100
ProteomicsDBi55726 [P46100-1]
55727 [P46100-2]
55728 [P46100-3]
55729 [P46100-4]
55730 [P46100-5]
55731 [P46100-6]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
546

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
546
DisGeNETi546

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ATRX
GeneReviewsiATRX
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
100075 Neuroendocrine tumor of stomach
93974 Smith-Fineman-Myers syndrome
PharmGKBiPA25179

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1015 Eukaryota
COG0553 LUCA
InParanoidiP46100
KOiK10779
OrthoDBi1258783at2759
PhylomeDBiP46100
TreeFamiTF313172

Enzyme and pathway databases

SIGNORiP46100

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
ATRX human
EvolutionaryTraceiP46100

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
ATRX

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
546
PharosiP46100

Protein Ontology

More...
PROi
PR:P46100

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000085224 Expressed in 244 organ(s), highest expression level in frontal cortex
ExpressionAtlasiP46100 baseline and differential
GenevisibleiP46100 HS

Family and domain databases

Gene3Di3.30.40.10, 1 hit
3.40.50.10810, 1 hit
InterProiView protein in InterPro
IPR025766 ADD
IPR041430 ADD_ATRX
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase
IPR038718 SNF2-like_sf
IPR000330 SNF2_N
IPR011011 Znf_FYVE_PHD
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF17981 ADD_ATRX, 1 hit
PF00271 Helicase_C, 1 hit
PF00176 SNF2_N, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF52540 SSF52540, 2 hits
SSF57903 SSF57903, 1 hit
PROSITEiView protein in PROSITE
PS51533 ADD, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiATRX_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P46100
Secondary accession number(s): D3DTE2
, P51068, Q15886, Q59FB5, Q59H31, Q5H9A2, Q5JWI4, Q7Z2J1, Q9H0Z1, Q9NTS3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 2, 2010
Last modified: October 16, 2019
This is version 219 of the entry and version 5 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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