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P46100

- ATRX_HUMAN

UniProt

P46100 - ATRX_HUMAN

Protein

Transcriptional regulator ATRX

Gene

ATRX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 5 (02 Nov 2010)
      Previous versions | rss
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    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 (PubMed:24500201) is not sufficient to decrease chromatin condensation at telomers nor to increase expression of telomeric RNA in fibroblasts. 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.8 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

    1. ATP binding Source: UniProtKB-KW
    2. chromatin binding Source: Ensembl
    3. chromo shadow domain binding Source: BHF-UCL
    4. DNA binding Source: UniProtKB-KW
    5. DNA helicase activity Source: ProtInc
    6. DNA translocase activity Source: UniProtKB
    7. helicase activity Source: ProtInc
    8. histone binding Source: UniProtKB
    9. methylated histone binding Source: UniProtKB
    10. protein binding Source: UniProtKB
    11. zinc ion binding Source: InterPro

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cellular response to hydroxyurea Source: UniProtKB
    3. chromatin remodeling Source: UniProtKB
    4. DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
    5. DNA duplex unwinding Source: GOC
    6. DNA methylation Source: ProtInc
    7. DNA recombination Source: ProtInc
    8. DNA repair Source: ProtInc
    9. DNA replication-independent nucleosome assembly Source: UniProtKB
    10. forebrain development Source: Ensembl
    11. negative regulation of telomeric RNA transcription from RNA pol II promoter Source: UniProtKB
    12. nucleosome assembly Source: UniProtKB
    13. positive regulation of nuclear cell cycle DNA replication Source: UniProtKB
    14. positive regulation of telomere maintenance Source: UniProtKB
    15. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    16. regulation of transcription, DNA-templated Source: ProtInc
    17. replication fork processing Source: UniProtKB
    18. transcription, DNA-templated Source: UniProtKB-KW

    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

    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
    ProteomesiUP000005640: 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

    1. cytoplasm Source: HPA
    2. mitochondrion Source: HPA
    3. nuclear heterochromatin Source: ProtInc
    4. nucleolus Source: HPA
    5. nucleus Source: HPA
    6. PML body Source: UniProtKB-SubCell
    7. SWI/SNF superfamily-type complex Source: UniProtKB
    8. telomeric heterochromatin Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus, Telomere

    Pathology & Biotechi

    Involvement in diseasei

    Alpha-thalassemia mental retardation syndrome, X-linked (ATRX) [MIM:301040]: A disorder characterized by severe psychomotor retardation, facial dysmorphism, urogenital abnormalities, and alpha-thalassemia. An essential phenotypic trait are hemoglobin H erythrocyte inclusions.10 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti175 – 1751G → E in ATRX. 1 Publication
    VAR_012113
    Natural varianti178 – 19821Missing in ATRX.
    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.
    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. 1 Publication
    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. 2 Publications
    VAR_001232
    Natural varianti246 – 2461R → L in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). 2 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.
    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.
    VAR_001238
    Natural varianti2084 – 20841Y → H in ATRX; impairs ATPase activity.
    VAR_001239
    Natural varianti2163 – 21631Y → C in ATRX.
    VAR_001241
    Mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1) [MIM:309580]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXSHF1 is a syndromic mental retardation. Clinical features include severe mental retardation, dysmorphic facies, and a highly skewed X-inactivation pattern in carrier women. Other more variable features include hypogonadism, deafness, renal anomalies, and mild skeletal defects.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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) [MIM:300448]: A disorder characterized by hypochromic, microcytic red blood cells, hemoglobin H detected in peripheral blood, and multilineage myelodysplasia.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    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

    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.

    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 residuei34 – 341Phosphoserine2 Publications
    Modified residuei89 – 891Phosphotyrosine2 Publications
    Modified residuei92 – 921Phosphoserine2 Publications
    Modified residuei112 – 1121Phosphoserine2 Publications
    Modified residuei591 – 5911Phosphothreonine2 Publications
    Modified residuei594 – 5941Phosphoserine2 Publications
    Modified residuei598 – 5981Phosphoserine3 Publications
    Modified residuei634 – 6341Phosphoserine2 Publications
    Modified residuei674 – 6741Phosphothreonine2 Publications
    Modified residuei675 – 6751Phosphoserine2 Publications
    Modified residuei677 – 6771Phosphoserine2 Publications
    Modified residuei729 – 7291Phosphoserine2 Publications
    Modified residuei731 – 7311Phosphoserine2 Publications
    Modified residuei819 – 8191PhosphoserineBy similarity
    Modified residuei875 – 8751Phosphoserine2 Publications
    Modified residuei876 – 8761Phosphoserine2 Publications
    Modified residuei889 – 8891Phosphoserine2 Publications
    Modified residuei967 – 9671N6-acetyllysine1 Publication
    Modified residuei1061 – 10611Phosphoserine3 Publications
    Modified residuei1063 – 10631Phosphotyrosine2 Publications
    Modified residuei1322 – 13221Phosphoserine2 Publications
    Modified residuei1324 – 13241Phosphoserine2 Publications
    Modified residuei1326 – 13261Phosphoserine2 Publications
    Modified residuei1348 – 13481Phosphoserine4 Publications
    Modified residuei1352 – 13521Phosphoserine5 Publications
    Modified residuei1527 – 15271Phosphoserine2 Publications
    Modified residuei1992 – 19921Phosphoserine2 Publications
    Modified residuei1996 – 19961Phosphoserine4 Publications
    Modified residuei2220 – 22201Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated at serine residues during mitose. Phosphorylation may promote the release from the nuclear matrix and progression to mitosis.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP46100.
    PaxDbiP46100.
    PRIDEiP46100.

    PTM databases

    PhosphoSiteiP46100.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiP46100.
    BgeeiP46100.
    CleanExiHS_RAD54L.
    GenevestigatoriP46100.

    Organism-specific databases

    HPAiCAB009372.
    HPA001906.

    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 SMC3.11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CBX5P459732EBI-396461,EBI-78219
    DAXXQ9UER75EBI-396461,EBI-77321
    RAD50Q928785EBI-396461,EBI-495494

    Protein-protein interaction databases

    BioGridi107028. 29 interactions.
    DIPiDIP-31532N.
    IntActiP46100. 18 interactions.
    MINTiMINT-1186201.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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

    eggNOGiCOG0553.
    HOVERGENiHBG000104.
    InParanoidiP46100.
    KOiK10779.
    OMAiNDPANIR.
    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.
    IPR001841. Znf_RING.
    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.
    SM00184. RING. 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. Align

    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

    MTAEPMSESK LNTLVQKLHD FLAHSSEESE ETSSPPRLAM NQNTDKISGS     50
    GSNSDMMENS KEEGTSSSEK SKSSGSSRSK RKPSIVTKYV ESDDEKPLDD 100
    ETVNEDASNE NSENDITMQS LPKGTVIVQP EPVLNEDKDD FKGPEFRSRS 150
    KMKTENLKKR GEDGLHGIVS CTACGQQVNH FQKDSIYRHP SLQVLICKNC 200
    FKYYMSDDIS RDSDGMDEQC RWCAEGGNLI CCDFCHNAFC KKCILRNLGR 250
    KELSTIMDEN NQWYCYICHP EPLLDLVTAC NSVFENLEQL LQQNKKKIKV 300
    DSEKSNKVYE HTSRFSPKKT SSNCNGEEKK LDDSCSGSVT YSYSALIVPK 350
    EMIKKAKKLI ETTANMNSSY VKFLKQATDN SEISSATKLR QLKAFKSVLA 400
    DIKKAHLALE EDLNSEFRAM DAVNKEKNTK EHKVIDAKFE TKARKGEKPC 450
    ALEKKDISKS EAKLSRKQVD SEHMHQNVPT EEQRTNKSTG GEHKKSDRKE 500
    EPQYEPANTS EDLDMDIVSV PSSVPEDIFE NLETAMEVQS SVDHQGDGSS 550
    GTEQEVESSS VKLNISSKDN RGGIKSKTTA KVTKELYVKL TPVSLSNSPI 600
    KGADCQEVPQ DKDGYKSCGL NPKLEKCGLG QENSDNEHLV ENEVSLLLEE 650
    SDLRRSPRVK TTPLRRPTET NPVTSNSDEE CNETVKEKQK LSVPVRKKDK 700
    RNSSDSAIDN PKPNKLPKSK QSETVDQNSD SDEMLAILKE VSRMSHSSSS 750
    DTDINEIHTN HKTLYDLKTQ AGKDDKGKRK RKSSTSGSDF DTKKGKSAKS 800
    SIISKKKRQT QSESSNYDSE LEKEIKSMSK IGAARTTKKR IPNTKDFDSS 850
    EDEKHSKKGM DNQGHKNLKT SQEGSSDDAE RKQERETFSS AEGTVDKDTT 900
    IMELRDRLPK KQQASASTDG VDKLSGKEQS FTSLEVRKVA ETKEKSKHLK 950
    TKTCKKVQDG LSDIAEKFLK KDQSDETSED DKKQSKKGTE EKKKPSDFKK 1000
    KVIKMEQQYE SSSDGTEKLP EREEICHFPK GIKQIKNGTT DGEKKSKKIR 1050
    DKTSKKKDEL SDYAEKSTGK GDSCDSSEDK KSKNGAYGRE KKRCKLLGKS 1100
    SRKRQDCSSS DTEKYSMKED GCNSSDKRLK RIELRERRNL SSKRNTKEIQ 1150
    SGSSSSDAEE SSEDNKKKKQ RTSSKKKAVI VKEKKRNSLR TSTKRKQADI 1200
    TSSSSSDIED DDQNSIGEGS SDEQKIKPVT ENLVLSSHTG FCQSSGDEAL 1250
    SKSVPVTVDD DDDDNDPENR IAKKMLLEEI KANLSSDEDG SSDDEPEEGK 1300
    KRTGKQNEEN PGDEEAKNQV NSESDSDSEE SKKPRYRHRL LRHKLTVSDG 1350
    ESGEEKKTKP KEHKEVKGRN RRKVSSEDSE DSDFQESGVS EEVSESEDEQ 1400
    RPRTRSAKKA ELEENQRSYK QKKKRRRIKV QEDSSSENKS NSEEEEEEKE 1450
    EEEEEEEEEE EEEEDENDDS KSPGKGRKKI RKILKDDKLR TETQNALKEE 1500
    EERRKRIAER EREREKLREV IEIEDASPTK CPITTKLVLD EDEETKEPLV 1550
    QVHRNMVIKL KPHQVDGVQF MWDCCCESVK KTKKSPGSGC ILAHCMGLGK 1600
    TLQVVSFLHT VLLCDKLDFS TALVVCPLNT ALNWMNEFEK WQEGLKDDEK 1650
    LEVSELATVK RPQERSYMLQ RWQEDGGVMI IGYEMYRNLA QGRNVKSRKL 1700
    KEIFNKALVD PGPDFVVCDE GHILKNEASA VSKAMNSIRS RRRIILTGTP 1750
    LQNNLIEYHC MVNFIKENLL GSIKEFRNRF INPIQNGQCA DSTMVDVRVM 1800
    KKRAHILYEM LAGCVQRKDY TALTKFLPPK HEYVLAVRMT SIQCKLYQYY 1850
    LDHLTGVGNN SEGGRGKAGA KLFQDFQMLS RIWTHPWCLQ LDYISKENKG 1900
    YFDEDSMDEF IASDSDETSM SLSSDDYTKK KKKGKKGKKD SSSSGSGSDN 1950
    DVEVIKVWNS RSRGGGEGNV DETGNNPSVS LKLEESKATS SSNPSSPAPD 2000
    WYKDFVTDAD AEVLEHSGKM VLLFEILRMA EEIGDKVLVF SQSLISLDLI 2050
    EDFLELASRE KTEDKDKPLI YKGEGKWLRN IDYYRLDGST TAQSRKKWAE 2100
    EFNDETNVRG RLFIISTKAG SLGINLVAAN RVIIFDASWN PSYDIQSIFR 2150
    VYRFGQTKPV YVYRFLAQGT MEDKIYDRQV TKQSLSFRVV DQQQVERHFT 2200
    MNELTELYTF EPDLLDDPNS EKKKKRDTPM LPKDTILAEL LQIHKEHIVG 2250
    YHEHDSLLDH KEEEELTEEE RKAAWAEYEA EKKGLTMRFN IPTGTNLPPV 2300
    SFNSQTPYIP FNLGALSAMS NQQLEDLINQ GREKVVEATN SVTAVRIQPL 2350
    EDIISAVWKE NMNLSEAQVQ ALALSRQASQ ELDVKRREAI YNDVLTKQQM 2400
    LISCVQRILM NRRLQQQYNQ QQQQQMTYQQ ATLGHLMMPK PPNLIMNPSN 2450
    YQQIDMRGMY QPVAGGMQPP PLQRAPPPMR SKNPGPSQGK SM 2492
    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. Reason: Many frameshifts and conflits.
    The sequence AAC50069.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence BAD92165.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti879 – 8791A → R in AAC50069. (PubMed:7874112)Curated
    Sequence conflicti1286 – 12861S → P in BAD92165. 1 PublicationCurated
    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.
    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.
    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. 1 Publication
    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. 2 Publications
    VAR_001232
    Natural varianti246 – 2461R → L in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). 2 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.
    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.
    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.
    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:
    EMBL
    GenBank
    DDBJ
    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. [P46100-1]
    ENST00000395603; ENSP00000378967; ENSG00000085224. [P46100-4]
    GeneIDi546.
    KEGGihsa:546.
    UCSCiuc004eco.4. human. [P46100-1]
    uc004ecq.4. human. [P46100-4]
    uc004ecr.2. human. [P46100-6]

    Polymorphism databases

    DMDMi311033500.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS14434.1. [P46100-1 ]
    CCDS14435.1. [P46100-4 ]
    PIRi I38614.
    I54367.
    RefSeqi NP_000480.3. NM_000489.4.
    NP_612114.2. NM_138270.3.
    UniGenei Hs.533526.
    Hs.653797.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JM1 NMR - A 159-296 [» ]
    2LBM NMR - A 163-296 [» ]
    2LD1 NMR - A 163-296 [» ]
    3QL9 X-ray 0.93 A 167-289 [» ]
    3QLA X-ray 1.60 A/D 167-289 [» ]
    3QLC X-ray 2.50 A/B 167-289 [» ]
    3QLN X-ray 1.90 A/B 167-289 [» ]
    ProteinModelPortali P46100.
    SMRi P46100. Positions 159-296.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107028. 29 interactions.
    DIPi DIP-31532N.
    IntActi P46100. 18 interactions.
    MINTi MINT-1186201.

    Chemistry

    DrugBanki DB00144. Phosphatidylserine.

    PTM databases

    PhosphoSitei P46100.

    Polymorphism databases

    DMDMi 311033500.

    Proteomic databases

    MaxQBi P46100.
    PaxDbi P46100.
    PRIDEi P46100.

    Protocols and materials databases

    DNASUi 546.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373344 ; ENSP00000362441 ; ENSG00000085224 . [P46100-1 ]
    ENST00000395603 ; ENSP00000378967 ; ENSG00000085224 . [P46100-4 ]
    GeneIDi 546.
    KEGGi hsa:546.
    UCSCi uc004eco.4. human. [P46100-1 ]
    uc004ecq.4. human. [P46100-4 ]
    uc004ecr.2. human. [P46100-6 ]

    Organism-specific databases

    CTDi 546.
    GeneCardsi GC0XM076760.
    GeneReviewsi ATRX.
    H-InvDB HIX0176765.
    HGNCi HGNC:886. ATRX.
    HPAi CAB009372.
    HPA001906.
    MIMi 300032. gene.
    300448. phenotype.
    301040. phenotype.
    309580. phenotype.
    neXtProti NX_P46100.
    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.
    93974. Smith-Fineman-Myers syndrome.
    PharmGKBi PA25179.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0553.
    HOVERGENi HBG000104.
    InParanoidi P46100.
    KOi K10779.
    OMAi NDPANIR.
    OrthoDBi EOG7G4QDQ.
    PhylomeDBi P46100.
    TreeFami TF313172.

    Miscellaneous databases

    EvolutionaryTracei P46100.
    GeneWikii ATRX.
    GenomeRNAii 546.
    NextBioi 2259.
    PROi P46100.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46100.
    Bgeei P46100.
    CleanExi HS_RAD54L.
    Genevestigatori P46100.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR025766. ADD.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    IPR011011. Znf_FYVE_PHD.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 3 hits.
    SSF57903. SSF57903. 1 hit.
    PROSITEi PS51533. ADD. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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 ATRX CYS-246; LEU-246 AND ASP-249, MUTAGENESIS OF TYR-203; TYR-204; ILE-209; ASP-214 AND ASP-217.
    32. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598; SER-889; SER-1061; SER-1322; SER-1324; SER-1326; SER-1348 AND SER-1352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "ATRX-mediated chromatin association of histone variant macroH2A1 regulates alpha-globin expression."
      Ratnakumar K., Duarte L.F., LeRoy G., Hasson D., Smeets D., Vardabasso C., Bonisch C., Zeng T., Xiang B., Zhang D.Y., Li H., Wang X., Hake S.B., Schermelleh L., Garcia B.A., Bernstein E.
      Genes Dev. 26:433-438(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HISTONE H2AFY.
    34. Cited for: FUNCTION.
    35. "DAXX-dependent supply of soluble (H3.3-H4) dimers to PML bodies pending deposition into chromatin."
      Delbarre E., Ivanauskiene K., Kuntziger T., Collas P.
      Genome Res. 23:440-451(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELULAR LOCATION.
    36. "Alternative lengthening of telomeres is characterized by reduced compaction of telomeric chromatin."
      Episkopou H., Draskovic I., Van Beneden A., Tilman G., Mattiussi M., Gobin M., Arnoult N., Londono-Vallejo A., Decottignies A.
      Nucleic Acids Res. 42:4391-4405(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    37. Cited for: INTERACTION WITH RAD50; MRE11A AND NBN.
    38. "Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX."
      Argentaro A., Yang J.C., Chapman L., Kowalczyk M.S., Gibbons R.J., Higgs D.R., Neuhaus D., Rhodes D.
      Proc. Natl. Acad. Sci. U.S.A. 104:11939-11944(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 159-296, DOMAIN GATA-TYPE ZINC-FINGER.
    39. "ATRX ADD domain links an atypical histone methylation recognition mechanism to human mental-retardation syndrome."
      Iwase S., Xiang B., Ghosh S., Ren T., Lewis P.W., Cochrane J.C., Allis C.D., Picketts D.J., Patel D.J., Li H., Shi Y.
      Nat. Struct. Mol. Biol. 18:769-776(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (0.93 ANGSTROMS) OF 167-289 IN COMPLEX WITH HISTONE H3K9ME3 PEPTIDE, SUBCELLULAR LOCATION, CHARACTERIZATION OF ATRX VARIANTS ALA-190; PRO-219 AND CYS-246, MUTAGENESIS OF HIS-189; TYR-203; TYR-204; ASP-217; GLU-252 AND LYS-1600.
    40. "Combinatorial readout of histone H3 modifications specifies localization of ATRX to heterochromatin."
      Eustermann S., Yang J.C., Law M.J., Amos R., Chapman L.M., Jelinska C., Garrick D., Clynes D., Gibbons R.J., Rhodes D., Higgs D.R., Neuhaus D.
      Nat. Struct. Mol. Biol. 18:777-782(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 163-296 IN COMPLEX WITH HISTONE H3K9ME3 PEPTIDE, CHARACTERIZATION OF ATRX VARIANT PRO-219, MUTAGENESIS OF TYR-203 AND GLU-218.
    41. "A point mutation in the XNP gene, associated with an ATR-X phenotype without alpha-thalassemia."
      Villard L., Lacombe D., Fontes M.
      Eur. J. Hum. Genet. 4:316-320(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ATRX SER-1713.
    42. Cited for: VARIANT MRXSHF1 GLN-2131.
    43. Cited for: VARIANTS ATRX.
    44. "New mutations in XNP/ATR-X gene: a further contribution to genotype/phenotype relationship in ATR/X syndrome."
      Fichera M., Romano C., Castiglia L., Failla P., Ruberto C., Amata S., Greco D., Cardoso C., Fontes M., Ragusa A.
      Hum. Mutat. 12:214-214(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ATRX LEU-246.
    45. "Mutation of the XNP/ATR-X gene in a family with severe mental retardation, spastic paraplegia and skewed pattern of X inactivation: demonstration that the mutation is involved in the inactivation bias."
      Lossi A.-M., Millan J.M., Villard L., Orellana C., Cardoso C., Prieto F., Fontes M., Martinez F.
      Am. J. Hum. Genet. 65:558-562(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ATRX LYS-1742.
    46. Cited for: VARIANT MRXSHF1 THR-2050.
    47. "Evaluation of a mutation screening strategy for sporadic cases of ATR-X syndrome."
      Villard L., Bonino M.-C., Abidi F., Ragusa A., Belougne J., Lossi A.-M., Seaver L., Bonnefont J.-P., Romano C., Fichera M., Lacombe D., Hanauer A., Philip N., Schwartz C.E., Fontes M.
      J. Med. Genet. 36:183-186(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ATRX GLU-175; 178-VAL--LYS-198 DEL; SER-190; PRO-219; LEU-246 AND CYS-249.
    48. "Molecular genetic study of Japanese patients with X-linked alpha-thalassemia/mental retardation syndrome (ATR-X)."
      Wada T., Kubota T., Fukushima Y., Saitoh S.
      Am. J. Med. Genet. 94:242-248(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ATRX SER-179; LEU-190; ILE-194; CYS-246; PHE-1552; SER-1645 AND CYS-1847.
    49. "Holmes-Gang syndrome is allelic with XLMR-hypotonic face syndrome."
      Stevenson R.E., Abidi F., Schwartz C.E., Lubs H.A., Holmes L.B.
      Am. J. Med. Genet. 94:383-385(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MRXSHF1 TYR-220.
    50. Cited for: VARIANT ATRX MET-1621.
    51. Cited for: VARIANT MRXSHF1 GLY-2271.
    52. "A missense mutation in the coiled-coil motif of the HP1-interacting domain of ATR-X in a family with X-linked mental retardation."
      Wieland I., Sabathil J., Ostendorf A., Rittinger O., Roepke A., Winnepenninckx B., Kooy F., Holinski-Feder E., Wieacker P.
      Neurogenetics 6:45-47(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MRXSHF1 SER-409.
    53. "ATRX syndrome in a girl with a heterozygous mutation in the ATRX Zn finger domain and a totally skewed X-inactivation pattern."
      Badens C., Martini N., Courrier S., DesPortes V., Touraine R., Levy N., Edery P.
      Am. J. Med. Genet. A 140:2212-2215(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ATRX CYS-246.

    Entry informationi

    Entry nameiATRX_HUMAN
    AccessioniPrimary (citable) accession number: P46100
    Secondary accession number(s): D3DTE2
    , P51068, Q15886, Q59FB5, Q59H31, Q5H9A2, Q5JWI4, Q7Z2J1, Q9H0Z1, Q9NTS3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 168 of the entry and version 5 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3