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P46100

- ATRX_HUMAN

UniProt

P46100 - ATRX_HUMAN

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Protein
Transcriptional regulator ATRX
Gene
ATRX, RAD54L, XH2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in transcriptional regulation and chromatin remodeling. Facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. Binds to DNA tandem repeat sequences in both telomeres and euchromatin and in vitro binds DNA quadruplex structures. May help stabilizing G-rich regions into regular chromatin structures by remodeling G4 DNA and incorporating H3.3-containing nucleosomes. Catalytic component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Its heterochromatin targeting is proposed to involve a combinatorial readout of histone H3 modifications (specifically methylation states of H3K9 and H3K4) and association with CBX5. Involved in maintaining telomere structural integrity in embryonic stem cells which probably implies recruitment of CBX5 to telomers. Reports on the involvement in transcriptional regulation of telomeric repeat-containing RNA (TERRA) are conflicting; according (1 Publication) 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; atypical
Add
BLAST
Zinc fingeri217 – 27256PHD-type; atypical
Add
BLAST
Nucleotide bindingi1594 – 16018ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. DNA helicase activity Source: ProtInc
  4. DNA translocase activity Source: UniProtKB
  5. chromatin binding Source: Ensembl
  6. chromo shadow domain binding Source: BHF-UCL
  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. DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  3. DNA duplex unwinding Source: GOC
  4. DNA methylation Source: ProtInc
  5. DNA recombination Source: ProtInc
  6. DNA repair Source: ProtInc
  7. DNA replication-independent nucleosome assembly Source: UniProtKB
  8. cellular response to hydroxyurea Source: UniProtKB
  9. chromatin remodeling 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
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

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

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.5 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Involvement in diseasei

Alpha-thalassemia mental retardation syndrome, X-linked (ATRX) [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.
Note: The disease is caused by mutations affecting the gene represented in this entry.15 Publications
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. 1 Publication
VAR_001226
Natural varianti190 – 1901P → L in ATRX. 1 Publication
VAR_012116
Natural varianti190 – 1901P → S in ATRX. 1 Publication
VAR_012117
Natural varianti192 – 1921L → F in ATRX.
VAR_001227
Natural varianti194 – 1941V → I in ATRX. 1 Publication
VAR_012118
Natural varianti200 – 2001C → S in ATRX.
VAR_001228
Natural varianti219 – 2191Q → P in ATRX; greatly impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 3 Publications
VAR_012119
Natural varianti220 – 2201C → R in ATRX.
VAR_001229
Natural varianti222 – 2221W → S in ATRX.
VAR_001230
Natural varianti243 – 2431C → F in ATRX.
VAR_001231
Natural varianti246 – 2461R → C in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 4 Publications
VAR_001232
Natural varianti246 – 2461R → L in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). 3 Publications
VAR_010914
Natural varianti249 – 2491G → C in ATRX. 1 Publication
VAR_012120
Natural varianti249 – 2491G → D in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization. 1 Publication
VAR_001233
Natural varianti1538 – 15381V → G in ATRX; unknown pathological significance.
VAR_012121
Natural varianti1552 – 15521V → F in ATRX. 1 Publication
VAR_012122
Natural varianti1609 – 16091H → R in ATRX.
VAR_001234
Natural varianti1614 – 16141C → R in ATRX.
VAR_001235
Natural varianti1621 – 16211T → M in ATRX. 1 Publication
VAR_016916
Natural varianti1645 – 16451L → S in ATRX. 1 Publication
VAR_012123
Natural varianti1650 – 16501K → N in ATRX.
VAR_001236
Natural varianti1713 – 17131P → S in ATRX; without alpha-thalassemia. 1 Publication
VAR_012124
Natural varianti1742 – 17421R → K in ATRX; atypical; patients presents spastic paraplegia at birth. 1 Publication
VAR_012125
Natural varianti1847 – 18471Y → C in ATRX. 1 Publication
VAR_012126
Natural varianti2035 – 20351D → V in ATRX; impairs ATPase activity. 1 Publication
VAR_001238
Natural varianti2084 – 20841Y → H in ATRX; impairs ATPase activity. 1 Publication
VAR_001239
Natural varianti2163 – 21631Y → C in ATRX.
VAR_001241
Mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1) [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.
Note: The disease is caused by mutations affecting the gene represented in this entry.6 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

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 ATRX
PRO_0000074301Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341Phosphoserine1 Publication
Modified residuei89 – 891Phosphotyrosine1 Publication
Modified residuei92 – 921Phosphoserine1 Publication
Modified residuei112 – 1121Phosphoserine1 Publication
Modified residuei591 – 5911Phosphothreonine1 Publication
Modified residuei594 – 5941Phosphoserine1 Publication
Modified residuei598 – 5981Phosphoserine2 Publications
Modified residuei634 – 6341Phosphoserine1 Publication
Modified residuei674 – 6741Phosphothreonine1 Publication
Modified residuei675 – 6751Phosphoserine1 Publication
Modified residuei677 – 6771Phosphoserine1 Publication
Modified residuei729 – 7291Phosphoserine1 Publication
Modified residuei731 – 7311Phosphoserine1 Publication
Modified residuei819 – 8191Phosphoserine By similarity
Modified residuei875 – 8751Phosphoserine1 Publication
Modified residuei876 – 8761Phosphoserine1 Publication
Modified residuei889 – 8891Phosphoserine1 Publication
Modified residuei967 – 9671N6-acetyllysine1 Publication
Modified residuei1061 – 10611Phosphoserine2 Publications
Modified residuei1063 – 10631Phosphotyrosine1 Publication
Modified residuei1322 – 13221Phosphoserine1 Publication
Modified residuei1324 – 13241Phosphoserine1 Publication
Modified residuei1326 – 13261Phosphoserine1 Publication
Modified residuei1348 – 13481Phosphoserine3 Publications
Modified residuei1352 – 13521Phosphoserine4 Publications
Modified residuei1527 – 15271Phosphoserine1 Publication
Modified residuei1992 – 19921Phosphoserine1 Publication
Modified residuei1996 – 19961Phosphoserine3 Publications
Modified residuei2220 – 22201Phosphoserine2 Publications

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, 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 SMC3.9 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

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.

Miscellaneous databases

EvolutionaryTraceiP46100.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini159 – 296138ADD
Add
BLAST
Domaini1581 – 1768188Helicase ATP-binding
Add
BLAST
Domaini2025 – 2205181Helicase C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1189 – 1326138Interaction with DAXX
Add
BLAST
Regioni2010 – 2280271Interaction with MECP2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi581 – 59414PxVxL motif
Add
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-Glu
Add
BLAST
Compositional biasi1499 – 15024Poly-Glu
Compositional biasi1929 – 193911Poly-Lys
Add
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

Contains 1 ADD domain.

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.

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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.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 204204Missing in isoform 1.
VSP_000575Add
BLAST
Alternative sequencei1 – 117117Missing in isoform 2 and isoform 5.
VSP_000574Add
BLAST
Alternative sequencei124 – 16239Missing in isoform 6.
VSP_015499Add
BLAST
Alternative sequencei124 – 16138Missing in isoform 3 and isoform 5.
VSP_000576Add
BLAST
Alternative sequencei573 – 60129Missing in isoform 6.
VSP_015500Add
BLAST
Alternative sequencei1419 – 24921074Missing in isoform 6.
VSP_015501Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti879 – 8791A → R in AAC50069. 1 Publication
Sequence conflicti1286 – 12861S → P in BAD92165. 1 Publication
Sequence conflicti1627 – 16271P → L in AAC50069. 1 Publication
Sequence conflicti1632 – 16321L → F in AAC50069. 1 Publication
Sequence conflicti2280 – 22801A → G in AAC50069. 1 Publication
Sequence conflicti2283 – 22842KG → RV in AAC50069. 1 Publication
Sequence conflicti2436 – 24361L → H in AAC50069. 1 Publication
Sequence conflicti2442 – 24421P → R in AAC50069. 1 Publication

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

« Hide 'large scale' publications
  1. "ATRX encodes a novel member of the SNF2 family of proteins: mutations point to a common mechanism underlying the ATR-X syndrome."
    Picketts D.J., Higgs D.R., Bachoo S., Blake D.J., Quarrell O.W.J., Gibbons R.J.
    Hum. Mol. Genet. 5:1899-1907(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), VARIANT SER-1860, VARIANTS ATRX.
  2. "Determination of the genomic structure of the XNP/ATRX gene encoding a potential zinc finger helicase."
    Villard L., Lossi A.-M., Cardoso C., Proud V., Chiaroni P., Colleaux L., Schwartz C., Fontes M.
    Genomics 43:149-155(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), VARIANTS PRO-596 AND GLY-740.
  3. "Gene diversity patterns at 10 X-chromosomal loci in humans and chimpanzees."
    Kitano T., Schwarz C., Nickel B., Paeaebo S.
    Mol. Biol. Evol. 20:1281-1289(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 163-198.
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 704-1927 (ISOFORMS 1/2/3/4/5), VARIANT GLU-929.
    Tissue: Brain.
  5. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 860-2492.
  8. "Cloning and expression of the murine homologue of a putative human X-linked nuclear protein gene closely linked to PGK1 in Xq13.3."
    Gecz J., Pollard H., Consalez G., Villard L., Stayton C.L., Millasseau P., Khrestchatisky M., Fontes M.
    Hum. Mol. Genet. 3:39-44(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  9. "Mutations in a putative global transcriptional regulator cause X-linked mental retardation with alpha-thalassemia (ATR-X syndrome)."
    Gibbons R.J., Picketts D.J., Villard L., Higgs D.R.
    Cell 80:837-845(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2401-2492, VARIANTS ATRX.
  10. "Specific interaction between the XNP/ATR-X gene product and the SET domain of the human EZH2 protein."
    Cardoso C., Timsit S., Villard L., Khrestchatisky M., Fontes M., Colleaux L.
    Hum. Mol. Genet. 7:679-684(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EZH2.
  11. "Localization of a putative transcriptional regulator (ATRX) at pericentromeric heterochromatin and the short arms of acrocentric chromosomes."
    McDowell T.L., Gibbons R.J., Sutherland H., O'Rourke D.M., Bickmore W.A., Pombo A., Turley H., Gatter K., Picketts D.J., Buckle V.J., Chapman L., Rhodes D., Higgs D.R.
    Proc. Natl. Acad. Sci. U.S.A. 96:13983-13988(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH PERICENTROMERIC HETEROCHROMATIN.
  12. "Identification of a mutation in the XNP/ATR-X gene in a family reported as Smith-Fineman-Myers syndrome."
    Villard L., Fontes M., Ades L.C., Gecz J.
    Am. J. Med. Genet. 91:83-85(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MRXSHF1.
  13. "Cell cycle-dependent phosphorylation of the ATRX protein correlates with changes in nuclear matrix and chromatin association."
    Berube N.G., Smeenk C.A., Picketts D.J.
    Hum. Mol. Genet. 9:539-547(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBX5, PHOSPHORYLATION.
  14. "Identification of acquired somatic mutations in the gene encoding chromatin-remodeling factor ATRX in the alpha-thalassemia myelodysplasia syndrome (ATMDS)."
    Gibbons R.J., Pellagatti A., Garrick D., Wood W.G., Malik N., Ayyub H., Langford C., Boultwood J., Wainscoat J.S., Higgs D.R.
    Nat. Genet. 34:446-449(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ATMDS.
  15. "The ATRX syndrome protein forms a chromatin-remodeling complex with Daxx and localizes in promyelocytic leukemia nuclear bodies."
    Xue Y., Gibbons R., Yan Z., Yang D., McDowell T.L., Sechi S., Qin J., Zhou S., Higgs D., Wang W.
    Proc. Natl. Acad. Sci. U.S.A. 100:10635-10640(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DAXX, SUBCELLULAR LOCATION.
  16. "A novel transcription regulatory complex containing death domain-associated protein and the ATR-X syndrome protein."
    Tang J., Wu S., Liu H., Stratt R., Barak O.G., Shiekhattar R., Picketts D.J., Yang X.
    J. Biol. Chem. 279:20369-20377(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DAXX, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-1600, CHARACTERIZATION OF VARIANTS ATRX VAL-2035 AND HIS-2084.
  17. "The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain."
    Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III
    Biochem. Biophys. Res. Commun. 331:929-937(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBX5.
  18. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634 AND SER-1352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "Interaction between chromatin proteins MECP2 and ATRX is disrupted by mutations that cause inherited mental retardation."
    Nan X., Hou J., Maclean A., Nasir J., Lafuente M.J., Shu X., Kriaucionis S., Bird A.
    Proc. Natl. Acad. Sci. U.S.A. 104:2709-2714(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MECP2.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594; THR-674; SER-675; SER-677; SER-729; SER-731; SER-875; SER-876; SER-1348; SER-1352; SER-1996 AND SER-2220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; TYR-89; SER-112 AND SER-1996, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  24. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-967, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  26. Cited for: ASSOCIATION WITH HISTONE H3.3.
  27. "The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3."
    Drane P., Ouararhni K., Depaux A., Shuaib M., Hamiche A.
    Genes Dev. 24:1253-1265(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  28. "Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres."
    Lewis P.W., Elsaesser S.J., Noh K.M., Stadler S.C., Allis C.D.
    Proc. Natl. Acad. Sci. U.S.A. 107:14075-14080(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE ATRX:DAXX COMPLEX.
  29. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; THR-591; SER-598; SER-1061; TYR-1063; SER-1348; SER-1352; SER-1527; SER-1992; SER-1996 AND SER-2220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "The ATRX-ADD domain binds to H3 tail peptides and reads the combined methylation state of K4 and K9."
    Dhayalan A., Tamas R., Bock I., Tattermusch A., Dimitrova E., Kudithipudi S., Ragozin S., Jeltsch A.
    Hum. Mol. Genet. 20:2195-2203(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIMETHYLATED HISTONE H3 'LYS-9', CHARACTERIZATION OF VARIANTS 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: September 3, 2014
This is version 167 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

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