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P46100 (ATRX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ATRX
Synonyms:RAD54L, XH2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2492 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 (Ref.36) 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. Ref.15 Ref.16 Ref.25 Ref.27 Ref.28 Ref.33 Ref.34 Ref.36

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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. Ref.10 Ref.13 Ref.15 Ref.16 Ref.17 Ref.19 Ref.31 Ref.33 Ref.37

Subcellular location

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. Ref.11 Ref.15 Ref.16 Ref.25 Ref.39

Tissue specificity

Ubiquitous.

Domain

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. Ref.38

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. Ref.38

Post-translational modification

Phosphorylated at serine residues during mitose. Phosphorylation may promote the release from the nuclear matrix and progression to mitosis. Ref.13

Involvement in disease

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. Ref.1 Ref.9 Ref.16 Ref.28 Ref.31 Ref.39 Ref.40 Ref.41 Ref.43 Ref.44 Ref.45 Ref.47 Ref.48 Ref.50 Ref.53

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. Ref.12 Ref.42 Ref.46 Ref.49 Ref.51 Ref.52

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. Ref.14

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 1 ADD domain.

Contains 1 GATA-type zinc finger.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 PHD-type zinc finger.

Sequence caution

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.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Transcription
Transcription regulation
   Cellular componentChromosome
Nucleus
Telomere
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Mental retardation
   DomainZinc-finger
   LigandATP-binding
DNA-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionChromatin regulator
Helicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.15. Source: GOC

DNA damage response, signal transduction by p53 class mediator

Inferred from sequence or structural similarity. Source: UniProtKB

DNA duplex unwinding

Traceable author statement Ref.9. Source: GOC

DNA methylation

Traceable author statement PubMed 10742099. Source: ProtInc

DNA recombination

Traceable author statement Ref.9. Source: ProtInc

DNA repair

Traceable author statement Ref.9. Source: ProtInc

DNA replication-independent nucleosome assembly

Inferred from mutant phenotype Ref.33. Source: UniProtKB

cellular response to hydroxyurea

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin remodeling

Inferred from direct assay Ref.28. Source: UniProtKB

forebrain development

Inferred from electronic annotation. Source: Ensembl

negative regulation of telomeric RNA transcription from RNA pol II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

nucleosome assembly

Inferred from direct assay Ref.28. Source: UniProtKB

positive regulation of nuclear cell cycle DNA replication

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of telomere maintenance

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.33. Source: UniProtKB

regulation of transcription, DNA-templated

Traceable author statement Ref.9. Source: ProtInc

replication fork processing

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

SWI/SNF superfamily-type complex

Inferred from direct assay Ref.15. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

mitochondrion

Inferred from direct assay. Source: HPA

nuclear heterochromatin

Traceable author statement Ref.11. Source: ProtInc

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

telomeric heterochromatin

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA helicase activity

Traceable author statement Ref.9. Source: ProtInc

DNA translocase activity

Inferred from direct assay Ref.15. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: Ensembl

chromo shadow domain binding

Inferred from physical interaction Ref.17. Source: BHF-UCL

helicase activity

Traceable author statement Ref.7. Source: ProtInc

histone binding

Inferred from direct assay Ref.33. Source: UniProtKB

methylated histone binding

Inferred from direct assay Ref.31. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.33. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CBX5P459732EBI-396461,EBI-78219
DAXXQ9UER73EBI-396461,EBI-77321

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 4 (identifier: P46100-1)

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.
Isoform 1 (identifier: P46100-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-204: Missing.
Isoform 2 (identifier: P46100-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-117: Missing.
Isoform 3 (identifier: P46100-4)

The sequence of this isoform differs from the canonical sequence as follows:
     124-161: Missing.
Isoform 5 (identifier: P46100-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-117: Missing.
     124-161: Missing.
Isoform 6 (identifier: P46100-6)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24922492Transcriptional regulator ATRX
PRO_0000074301

Regions

Domain159 – 296138ADD
Domain1581 – 1768188Helicase ATP-binding
Domain2025 – 2205181Helicase C-terminal
Zinc finger170 – 20637GATA-type; atypical
Zinc finger217 – 27256PHD-type; atypical
Nucleotide binding1594 – 16018ATP Potential
Region1189 – 1326138Interaction with DAXX
Region2010 – 2280271Interaction with MECP2
Motif581 – 59414PxVxL motif
Motif1719 – 17224DEGH box
Compositional bias745 – 7506Poly-Ser
Compositional bias1151 – 11566Poly-Ser
Compositional bias1166 – 11694Poly-Lys
Compositional bias1202 – 12065Poly-Ser
Compositional bias1259 – 12668Poly-Asp
Compositional bias1443 – 146624Poly-Glu
Compositional bias1499 – 15024Poly-Glu
Compositional bias1929 – 193911Poly-Lys
Compositional bias1941 – 19488Poly-Ser
Compositional bias2222 – 22254Poly-Lys
Compositional bias2262 – 22654Poly-Glu
Compositional bias2420 – 24256Poly-Gln

Amino acid modifications

Modified residue341Phosphoserine Ref.23
Modified residue891Phosphotyrosine Ref.23
Modified residue921Phosphoserine Ref.29
Modified residue1121Phosphoserine Ref.23
Modified residue5911Phosphothreonine Ref.29
Modified residue5941Phosphoserine Ref.21
Modified residue5981Phosphoserine Ref.29 Ref.32
Modified residue6341Phosphoserine Ref.18
Modified residue6741Phosphothreonine Ref.21
Modified residue6751Phosphoserine Ref.21
Modified residue6771Phosphoserine Ref.21
Modified residue7291Phosphoserine Ref.21
Modified residue7311Phosphoserine Ref.21
Modified residue8191Phosphoserine By similarity
Modified residue8751Phosphoserine Ref.21
Modified residue8761Phosphoserine Ref.21
Modified residue8891Phosphoserine Ref.32
Modified residue9671N6-acetyllysine Ref.24
Modified residue10611Phosphoserine Ref.29 Ref.32
Modified residue10631Phosphotyrosine Ref.29
Modified residue13221Phosphoserine Ref.32
Modified residue13241Phosphoserine Ref.32
Modified residue13261Phosphoserine Ref.32
Modified residue13481Phosphoserine Ref.21 Ref.29 Ref.32
Modified residue13521Phosphoserine Ref.18 Ref.21 Ref.29 Ref.32
Modified residue15271Phosphoserine Ref.29
Modified residue19921Phosphoserine Ref.29
Modified residue19961Phosphoserine Ref.21 Ref.23 Ref.29
Modified residue22201Phosphoserine Ref.21 Ref.29

Natural variations

Alternative sequence1 – 204204Missing in isoform 1.
VSP_000575
Alternative sequence1 – 117117Missing in isoform 2 and isoform 5.
VSP_000574
Alternative sequence124 – 16239Missing in isoform 6.
VSP_015499
Alternative sequence124 – 16138Missing in isoform 3 and isoform 5.
VSP_000576
Alternative sequence573 – 60129Missing in isoform 6.
VSP_015500
Alternative sequence1419 – 24921074Missing in isoform 6.
VSP_015501
Natural variant1751G → E in ATRX. Ref.47
VAR_012113
Natural variant178 – 19821Missing in ATRX.
VAR_012114
Natural variant1791N → S in ATRX. Ref.48
VAR_012115
Natural variant1901P → A in ATRX; impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci. Ref.39
VAR_001226
Natural variant1901P → L in ATRX. Ref.48
VAR_012116
Natural variant1901P → S in ATRX. Ref.47
VAR_012117
Natural variant1921L → F in ATRX.
VAR_001227
Natural variant1941V → I in ATRX. Ref.48
VAR_012118
Natural variant2001C → S in ATRX.
VAR_001228
Natural variant2191Q → P in ATRX; greatly impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. Ref.39 Ref.40 Ref.47
VAR_012119
Natural variant2201C → R in ATRX.
VAR_001229
Natural variant2201C → Y in MRXSHF1. Ref.49
VAR_032625
Natural variant2221W → S in ATRX.
VAR_001230
Natural variant2431C → F in ATRX.
VAR_001231
Natural variant2461R → C in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. Ref.31 Ref.39 Ref.48 Ref.53
VAR_001232
Natural variant2461R → L in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). Ref.31 Ref.44 Ref.47
VAR_010914
Natural variant2491G → C in ATRX. Ref.47
VAR_012120
Natural variant2491G → D in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization. Ref.31
VAR_001233
Natural variant4091L → S in MRXSHF1. Ref.52
VAR_032626
Natural variant5451Q → E.
Corresponds to variant rs35738915 [ dbSNP | Ensembl ].
VAR_055939
Natural variant5961S → P. Ref.2
Corresponds to variant rs1051678 [ dbSNP | Ensembl ].
VAR_016914
Natural variant7401E → G. Ref.2
Corresponds to variant rs1051680 [ dbSNP | Ensembl ].
VAR_016915
Natural variant9291Q → E. Ref.4
Corresponds to variant rs3088074 [ dbSNP | Ensembl ].
VAR_023438
Natural variant15381V → G in ATRX; unknown pathological significance.
VAR_012121
Natural variant15521V → F in ATRX. Ref.48
VAR_012122
Natural variant16091H → R in ATRX.
VAR_001234
Natural variant16141C → R in ATRX.
VAR_001235
Natural variant16211T → M in ATRX. Ref.50
VAR_016916
Natural variant16451L → S in ATRX. Ref.48
VAR_012123
Natural variant16501K → N in ATRX.
VAR_001236
Natural variant17131P → S in ATRX; without alpha-thalassemia. Ref.41
VAR_012124
Natural variant17421R → K in ATRX; atypical; patients presents spastic paraplegia at birth. Ref.45
VAR_012125
Natural variant18471Y → C in ATRX. Ref.48
VAR_012126
Natural variant18601N → S Rare polymorphism. Ref.1
Corresponds to variant rs45439799 [ dbSNP | Ensembl ].
VAR_001237
Natural variant20351D → V in ATRX; impairs ATPase activity. Ref.16
VAR_001238
Natural variant20501I → T in MRXSHF1; originally reported as Carpenter-Waziri syndrome. Ref.46
VAR_012127
Natural variant20841Y → H in ATRX; impairs ATPase activity. Ref.16
VAR_001239
Natural variant21311R → Q in MRXSHF1; originally reported as Juberg-Marsidi syndrome. Ref.42
VAR_001240
Natural variant21631Y → C in ATRX.
VAR_001241
Natural variant22711R → G in MRXSHF1. Ref.51
VAR_032627

Experimental info

Mutagenesis1891H → N: Impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci. Ref.39
Mutagenesis2031Y → A or K: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization. Ref.31 Ref.39 Ref.40
Mutagenesis2041Y → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. Ref.31 Ref.39
Mutagenesis2071D → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci.
Mutagenesis2091I → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). Ref.31
Mutagenesis2141D → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). Ref.31
Mutagenesis2171D → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization. Ref.31 Ref.39
Mutagenesis2181E → A: Impairs interaction with histone H3 peptides unmethylated at 'Lys-5' (H3K4me0); reduces pericentromeric localization. Ref.40
Mutagenesis2521E → L: Impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci. Ref.39
Mutagenesis16001K → R: Abolishes ATPAse activity, no effect on pericentromeric heterochromatin localization. Ref.16 Ref.39
Sequence conflict8791A → R in AAC50069. Ref.7
Sequence conflict12861S → P in BAD92165. Ref.4
Sequence conflict16271P → L in AAC50069. Ref.7
Sequence conflict16321L → F in AAC50069. Ref.7
Sequence conflict22801A → G in AAC50069. Ref.7
Sequence conflict2283 – 22842KG → RV in AAC50069. Ref.7
Sequence conflict24361L → H in AAC50069. Ref.7
Sequence conflict24421P → R in AAC50069. Ref.7

Secondary structure

..................................... 2492
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 4 [UniParc].

Last modified November 2, 2010. Version 5.
Checksum: 637E341F6A4B29C6

FASTA2,492282,586
        10         20         30         40         50         60 
MTAEPMSESK LNTLVQKLHD FLAHSSEESE ETSSPPRLAM NQNTDKISGS GSNSDMMENS 

        70         80         90        100        110        120 
KEEGTSSSEK SKSSGSSRSK RKPSIVTKYV ESDDEKPLDD ETVNEDASNE NSENDITMQS 

       130        140        150        160        170        180 
LPKGTVIVQP EPVLNEDKDD FKGPEFRSRS KMKTENLKKR GEDGLHGIVS CTACGQQVNH 

       190        200        210        220        230        240 
FQKDSIYRHP SLQVLICKNC FKYYMSDDIS RDSDGMDEQC RWCAEGGNLI CCDFCHNAFC 

       250        260        270        280        290        300 
KKCILRNLGR KELSTIMDEN NQWYCYICHP EPLLDLVTAC NSVFENLEQL LQQNKKKIKV 

       310        320        330        340        350        360 
DSEKSNKVYE HTSRFSPKKT SSNCNGEEKK LDDSCSGSVT YSYSALIVPK EMIKKAKKLI 

       370        380        390        400        410        420 
ETTANMNSSY VKFLKQATDN SEISSATKLR QLKAFKSVLA DIKKAHLALE EDLNSEFRAM 

       430        440        450        460        470        480 
DAVNKEKNTK EHKVIDAKFE TKARKGEKPC ALEKKDISKS EAKLSRKQVD SEHMHQNVPT 

       490        500        510        520        530        540 
EEQRTNKSTG GEHKKSDRKE EPQYEPANTS EDLDMDIVSV PSSVPEDIFE NLETAMEVQS 

       550        560        570        580        590        600 
SVDHQGDGSS GTEQEVESSS VKLNISSKDN RGGIKSKTTA KVTKELYVKL TPVSLSNSPI 

       610        620        630        640        650        660 
KGADCQEVPQ DKDGYKSCGL NPKLEKCGLG QENSDNEHLV ENEVSLLLEE SDLRRSPRVK 

       670        680        690        700        710        720 
TTPLRRPTET NPVTSNSDEE CNETVKEKQK LSVPVRKKDK RNSSDSAIDN PKPNKLPKSK 

       730        740        750        760        770        780 
QSETVDQNSD SDEMLAILKE VSRMSHSSSS DTDINEIHTN HKTLYDLKTQ AGKDDKGKRK 

       790        800        810        820        830        840 
RKSSTSGSDF DTKKGKSAKS SIISKKKRQT QSESSNYDSE LEKEIKSMSK IGAARTTKKR 

       850        860        870        880        890        900 
IPNTKDFDSS EDEKHSKKGM DNQGHKNLKT SQEGSSDDAE RKQERETFSS AEGTVDKDTT 

       910        920        930        940        950        960 
IMELRDRLPK KQQASASTDG VDKLSGKEQS FTSLEVRKVA ETKEKSKHLK TKTCKKVQDG 

       970        980        990       1000       1010       1020 
LSDIAEKFLK KDQSDETSED DKKQSKKGTE EKKKPSDFKK KVIKMEQQYE SSSDGTEKLP 

      1030       1040       1050       1060       1070       1080 
EREEICHFPK GIKQIKNGTT DGEKKSKKIR DKTSKKKDEL SDYAEKSTGK GDSCDSSEDK 

      1090       1100       1110       1120       1130       1140 
KSKNGAYGRE KKRCKLLGKS SRKRQDCSSS DTEKYSMKED GCNSSDKRLK RIELRERRNL 

      1150       1160       1170       1180       1190       1200 
SSKRNTKEIQ SGSSSSDAEE SSEDNKKKKQ RTSSKKKAVI VKEKKRNSLR TSTKRKQADI 

      1210       1220       1230       1240       1250       1260 
TSSSSSDIED DDQNSIGEGS SDEQKIKPVT ENLVLSSHTG FCQSSGDEAL SKSVPVTVDD 

      1270       1280       1290       1300       1310       1320 
DDDDNDPENR IAKKMLLEEI KANLSSDEDG SSDDEPEEGK KRTGKQNEEN PGDEEAKNQV 

      1330       1340       1350       1360       1370       1380 
NSESDSDSEE SKKPRYRHRL LRHKLTVSDG ESGEEKKTKP KEHKEVKGRN RRKVSSEDSE 

      1390       1400       1410       1420       1430       1440 
DSDFQESGVS EEVSESEDEQ RPRTRSAKKA ELEENQRSYK QKKKRRRIKV QEDSSSENKS 

      1450       1460       1470       1480       1490       1500 
NSEEEEEEKE EEEEEEEEEE EEEEDENDDS KSPGKGRKKI RKILKDDKLR TETQNALKEE 

      1510       1520       1530       1540       1550       1560 
EERRKRIAER EREREKLREV IEIEDASPTK CPITTKLVLD EDEETKEPLV QVHRNMVIKL 

      1570       1580       1590       1600       1610       1620 
KPHQVDGVQF MWDCCCESVK KTKKSPGSGC ILAHCMGLGK TLQVVSFLHT VLLCDKLDFS 

      1630       1640       1650       1660       1670       1680 
TALVVCPLNT ALNWMNEFEK WQEGLKDDEK LEVSELATVK RPQERSYMLQ RWQEDGGVMI 

      1690       1700       1710       1720       1730       1740 
IGYEMYRNLA QGRNVKSRKL KEIFNKALVD PGPDFVVCDE GHILKNEASA VSKAMNSIRS 

      1750       1760       1770       1780       1790       1800 
RRRIILTGTP LQNNLIEYHC MVNFIKENLL GSIKEFRNRF INPIQNGQCA DSTMVDVRVM 

      1810       1820       1830       1840       1850       1860 
KKRAHILYEM LAGCVQRKDY TALTKFLPPK HEYVLAVRMT SIQCKLYQYY LDHLTGVGNN 

      1870       1880       1890       1900       1910       1920 
SEGGRGKAGA KLFQDFQMLS RIWTHPWCLQ LDYISKENKG YFDEDSMDEF IASDSDETSM 

      1930       1940       1950       1960       1970       1980 
SLSSDDYTKK KKKGKKGKKD SSSSGSGSDN DVEVIKVWNS RSRGGGEGNV DETGNNPSVS 

      1990       2000       2010       2020       2030       2040 
LKLEESKATS SSNPSSPAPD WYKDFVTDAD AEVLEHSGKM VLLFEILRMA EEIGDKVLVF 

      2050       2060       2070       2080       2090       2100 
SQSLISLDLI EDFLELASRE KTEDKDKPLI YKGEGKWLRN IDYYRLDGST TAQSRKKWAE 

      2110       2120       2130       2140       2150       2160 
EFNDETNVRG RLFIISTKAG SLGINLVAAN RVIIFDASWN PSYDIQSIFR VYRFGQTKPV 

      2170       2180       2190       2200       2210       2220 
YVYRFLAQGT MEDKIYDRQV TKQSLSFRVV DQQQVERHFT MNELTELYTF EPDLLDDPNS 

      2230       2240       2250       2260       2270       2280 
EKKKKRDTPM LPKDTILAEL LQIHKEHIVG YHEHDSLLDH KEEEELTEEE RKAAWAEYEA 

      2290       2300       2310       2320       2330       2340 
EKKGLTMRFN IPTGTNLPPV SFNSQTPYIP FNLGALSAMS NQQLEDLINQ GREKVVEATN 

      2350       2360       2370       2380       2390       2400 
SVTAVRIQPL EDIISAVWKE NMNLSEAQVQ ALALSRQASQ ELDVKRREAI YNDVLTKQQM 

      2410       2420       2430       2440       2450       2460 
LISCVQRILM NRRLQQQYNQ QQQQQMTYQQ ATLGHLMMPK PPNLIMNPSN YQQIDMRGMY 

      2470       2480       2490 
QPVAGGMQPP PLQRAPPPMR SKNPGPSQGK SM 

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Isoform 1 [UniParc].

Checksum: AB2B948725F62D77
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FASTA2,288259,843
Isoform 2 [UniParc].

Checksum: 7314428AA21A9687
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FASTA2,375269,811
Isoform 3 [UniParc].

Checksum: ED9320A642E01E2A
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FASTA2,454278,229
Isoform 5 [UniParc].

Checksum: 437268E2C2817FEA
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FASTA2,337265,454
Isoform 6 [UniParc].

Checksum: A67E6A155955371A
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FASTA1,350151,556

References

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[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"Cloning and characterization of a new human Xq13 gene, encoding a putative helicase."
Stayton C.L., Dabovic B., Gulisano M., Gecz J., Broccoli V., Giovanazzi S., Bossolasco M., Monaco L., Rastan S., Boncinelli E., Bianchi M.E., Consalez G.G.
Hum. Mol. Genet. 3:1957-1964(1994) [PubMed] [Europe PMC] [Abstract]
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[21]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"ATR-X syndrome protein targets tandem repeats and influences allele-specific expression in a size-dependent manner."
Law M.J., Lower K.M., Voon H.P., Hughes J.R., Garrick D., Viprakasit V., Mitson M., De Gobbi M., Marra M., Morris A., Abbott A., Wilder S.P., Taylor S., Santos G.M., Cross J., Ayyub H., Jones S., Ragoussis J. expand/collapse author list , Rhodes D., Dunham I., Higgs D.R., Gibbons R.J.
Cell 143:367-378(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[26]"Distinct factors control histone variant H3.3 localization at specific genomic regions."
Goldberg A.D., Banaszynski L.A., Noh K.M., Lewis P.W., Elsaesser S.J., Stadler S., Dewell S., Law M., Guo X., Li X., Wen D., Chapgier A., DeKelver R.C., Miller J.C., Lee Y.L., Boydston E.A., Holmes M.C., Gregory P.D. expand/collapse author list , Greally J.M., Rafii S., Yang C., Scambler P.J., Garrick D., Gibbons R.J., Higgs D.R., Cristea I.M., Urnov F.D., Zheng D., Allis C.D.
Cell 140:678-691(2010) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Loss of ATRX, genome instability, and an altered DNA damage response are hallmarks of the alternative lengthening of telomeres pathway."
Lovejoy C.A., Li W., Reisenweber S., Thongthip S., Bruno J., de Lange T., De S., Petrini J.H., Sung P.A., Jasin M., Rosenbluh J., Zwang Y., Weir B.A., Hatton C., Ivanova E., Macconaill L., Hanna M., Hahn W.C. expand/collapse author list , Lue N.F., Reddel R.R., Jiao Y., Kinzler K., Vogelstein B., Papadopoulos N., Meeker A.K.
PLoS Genet. 8:E1002772-E1002772(2012) [PubMed] [Europe PMC] [Abstract]
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]"ATRX dysfunction induces replication defects in primary mouse cells."
Clynes D., Jelinska C., Xella B., Ayyub H., Taylor S., Mitson M., Bachrati C.Z., Higgs D.R., Gibbons R.J.
PLoS ONE 9:E92915-E92915(2014) [PubMed] [Europe PMC] [Abstract]
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]"XNP mutation in a large family with Juberg-Marsidi syndrome."
Villard L., Gecz J., Mattei J.-F., Fontes M., Saugier-Veber P., Munnich A., Lyonnet S.
Nat. Genet. 12:359-360(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MRXSHF1 GLN-2131.
[43]"Mutations in transcriptional regulator ATRX establish the functional significance of a PHD-like domain."
Gibbons R.J., Bachoo S., Picketts D.J., Aftimos S., Asenbauer B., Bergoffen J., Berry S.A., Dahl N., Fryer A., Keppler K., Kurosawa K., Levin M.L., Masuno M., Neri G., Pierpont M.E., Slaney S.F., Higgs D.R.
Nat. Genet. 17:146-148(1997) [PubMed] [Europe PMC] [Abstract]
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]"Carpenter-Waziri syndrome results from a mutation in XNP."
Abidi F., Schwartz C.E., Carpenter N.J., Villard L., Fontes M., Curtis M.
Am. J. Med. Genet. 85:249-251(1999) [PubMed] [Europe PMC] [Abstract]
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]"Expanding phenotype of XNP mutations: mild to moderate mental retardation."
Yntema H.G., Poppelaars F.A., Derksen E., Oudakker A.R., van Roosmalen T., Jacobs A., Obbema H., Brunner H.G., Hamel B.C.J., van Bokhoven H.
Am. J. Med. Genet. 110:243-247(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ATRX MET-1621.
[51]"Asplenia in ATR-X syndrome: a second report."
Leahy R.T., Philip R.K., Gibbons R.J., Fisher C., Suri M., Reardon W.
Am. J. Med. Genet. A 139:37-39(2005) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U72937 mRNA. Translation: AAB49970.2.
U72938 mRNA. Translation: AAB49971.2.
U72935 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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.
CCDSCCDS14434.1. [P46100-1]
CCDS14435.1. [P46100-4]
PIRI38614.
I54367.
RefSeqNP_000480.3. NM_000489.4.
NP_612114.2. NM_138270.3.
UniGeneHs.533526.
Hs.653797.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP46100.
SMRP46100. Positions 159-296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107028. 29 interactions.
DIPDIP-31532N.
IntActP46100. 12 interactions.
MINTMINT-1186201.

Chemistry

DrugBankDB00144. Phosphatidylserine.

PTM databases

PhosphoSiteP46100.

Polymorphism databases

DMDM311033500.

Proteomic databases

MaxQBP46100.
PaxDbP46100.
PRIDEP46100.

Protocols and materials databases

DNASU546.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373344; ENSP00000362441; ENSG00000085224. [P46100-1]
ENST00000395603; ENSP00000378967; ENSG00000085224. [P46100-4]
GeneID546.
KEGGhsa:546.
UCSCuc004eco.4. human. [P46100-1]
uc004ecq.4. human. [P46100-4]
uc004ecr.2. human. [P46100-6]

Organism-specific databases

CTD546.
GeneCardsGC0XM076760.
GeneReviewsATRX.
H-InvDBHIX0176765.
HGNCHGNC:886. ATRX.
HPACAB009372.
HPA001906.
MIM300032. gene.
300448. phenotype.
301040. phenotype.
309580. phenotype.
neXtProtNX_P46100.
Orphanet231401. 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.
PharmGKBPA25179.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOVERGENHBG000104.
InParanoidP46100.
KOK10779.
OMANDPANIR.
OrthoDBEOG7G4QDQ.
PhylomeDBP46100.
TreeFamTF313172.

Gene expression databases

ArrayExpressP46100.
BgeeP46100.
CleanExHS_RAD54L.
GenevestigatorP46100.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR025766. 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]
PfamPF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 3 hits.
SSF57903. SSF57903. 1 hit.
PROSITEPS51533. ADD. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP46100.
GeneWikiATRX.
GenomeRNAi546.
NextBio2259.
PROP46100.
SOURCESearch...

Entry information

Entry nameATRX_HUMAN
AccessionPrimary (citable) accession number: P46100
Secondary accession number(s): D3DTE2 expand/collapse secondary AC list , P51068, Q15886, Q59FB5, Q59H31, Q5H9A2, Q5JWI4, Q7Z2J1, Q9H0Z1, Q9NTS3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 2, 2010
Last modified: July 9, 2014
This is version 166 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM