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Q61687 (ATRX_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
HP1 alpha-interacting protein
HP1-BP38 protein
Heterochromatin protein 2
X-linked nuclear protein
Gene names
Name:Atrx
Synonyms:Hp1bp2, Xnp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2476 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 probably implying recruitment of CBX5 to telomers. Reports on the involvement in transcriptional regulation of telomeric repeat-containing RNA (TERRA) are conflicting; according (Ref.10) is required for its transcriptional repression in embryonic stem cells. Acts as negative regulator of chromatin incorporation of transcriptionally repressive histone H2AFY, particularily at telomeres. 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. Ref.9 Ref.10 Ref.15 Ref.16

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.6 Ref.14 Ref.15 Ref.16

Subcellular location

Nucleus. Chromosometelomere. NucleusPML body By similarity. 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 By similarity. In embryonic stem cells localized to telomeres; localization is reduced after 12 d of induction of cell differentiation. Colocalizes with cohesin (SMC1 and SMC3) and MECP2 at the maternal H19 ICR and the Gtl2/Dlk1 imprinted cluster in the brain. Ref.4 Ref.9 Ref.12 Ref.15

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 By similarity.

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.

Post-translational modification

Citrullinated by PADI4.

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.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Transcription
Transcription regulation
   Cellular componentChromosome
Nucleus
Telomere
   DomainZinc-finger
   LigandATP-binding
DNA-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionChromatin regulator
Helicase
Hydrolase
   PTMCitrullination
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator

Inferred from mutant phenotype Ref.16. Source: UniProtKB

DNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

DNA replication-independent nucleosome assembly

Inferred from sequence or structural similarity. Source: UniProtKB

Sertoli cell development

Inferred from mutant phenotype PubMed 21427128. Source: MGI

cellular response to hydroxyurea

Inferred from mutant phenotype Ref.16. Source: UniProtKB

chromatin remodeling

Inferred from sequence or structural similarity. Source: UniProtKB

forebrain development

Inferred from mutant phenotype PubMed 15668733. Source: MGI

negative regulation of telomeric RNA transcription from RNA pol II promoter

Inferred from mutant phenotype Ref.10. Source: UniProtKB

nucleosome assembly

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of nuclear cell cycle DNA replication

Inferred from mutant phenotype Ref.16. Source: UniProtKB

positive regulation of telomere maintenance

Inferred from mutant phenotype Ref.15. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 21427128. Source: MGI

replication fork processing

Inferred from mutant phenotype Ref.16. Source: UniProtKB

seminiferous tubule development

Inferred from mutant phenotype PubMed 21427128. Source: MGI

spermatogenesis

Inferred from mutant phenotype PubMed 21427128. Source: MGI

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 sequence or structural similarity. Source: UniProtKB

heterochromatin

Inferred from direct assay PubMed 14519686PubMed 15252119Ref.6. Source: MGI

nuclear chromosome

Inferred from direct assay PubMed 11555636. Source: MGI

nucleus

Inferred from direct assay Ref.6. Source: MGI

telomeric heterochromatin

Inferred from direct assay Ref.15. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from direct assay PubMed 15522233. Source: MGI

helicase activity

Inferred from electronic annotation. Source: UniProtKB-KW

histone binding

Inferred from direct assay Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.16. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24762476Transcriptional regulator ATRX
PRO_0000074303

Regions

Domain158 – 295138ADD
Domain1566 – 1753188Helicase ATP-binding
Domain2008 – 2188181Helicase C-terminal
Zinc finger169 – 20537GATA-type; atypical
Zinc finger216 – 27156PHD-type; atypical
Nucleotide binding1579 – 15868ATP Potential
Region1169 – 1313145Interaction with DAXX By similarity
Region1993 – 2263271Interaction with MECP2 By similarity
Motif573 – 58614PxVxL motif
Motif1704 – 17074DEGH box
Compositional bias319 – 3224Poly-Ser
Compositional bias735 – 7384Poly-Ser
Compositional bias1001 – 10044Poly-Glu
Compositional bias1130 – 11356Poly-Ser
Compositional bias1182 – 11854Poly-Ser
Compositional bias1238 – 12458Poly-Asp
Compositional bias1484 – 14874Poly-Glu
Compositional bias1924 – 19318Poly-Ser
Compositional bias2205 – 22084Poly-Lys
Compositional bias2245 – 22484Poly-Glu
Compositional bias2403 – 24086Poly-Gln

Amino acid modifications

Modified residue341Phosphoserine By similarity
Modified residue891Phosphotyrosine Ref.5
Modified residue921Phosphoserine Ref.7 Ref.8
Modified residue1111Phosphoserine By similarity
Modified residue5831Phosphothreonine By similarity
Modified residue5861Phosphoserine By similarity
Modified residue5901Phosphoserine By similarity
Modified residue6261Phosphoserine By similarity
Modified residue6631Phosphoserine By similarity
Modified residue6651Phosphoserine By similarity
Modified residue7171Phosphoserine Ref.5
Modified residue7191Phosphoserine Ref.5
Modified residue8011Phosphoserine Ref.5
Modified residue8541Phosphoserine By similarity
Modified residue8551Phosphoserine By similarity
Modified residue8711Phosphoserine By similarity
Modified residue10411Phosphoserine By similarity
Modified residue10631Citrulline
Modified residue13091Phosphoserine By similarity
Modified residue13111Phosphoserine By similarity
Modified residue13131Phosphoserine By similarity
Modified residue13351Phosphoserine By similarity
Modified residue13391Phosphoserine Ref.5
Modified residue15121Phosphoserine By similarity
Modified residue19751Phosphoserine By similarity
Modified residue19791Phosphoserine By similarity
Modified residue22031Phosphoserine By similarity

Experimental info

Mutagenesis2391C → G: Reduces pericentromeric localization. Abolishes pericentromeric localization; when associated with E-580. Ref.12
Mutagenesis5801V → E: Reduces pericentromeric localization. Abolishes pericentromeric localization; when associated with G-239. Ref.12
Sequence conflict1571K → I in AAC08741. Ref.1
Sequence conflict19531V → M in AAC08741. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q61687 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: B2E2218B6CC791EC

FASTA2,476278,587
        10         20         30         40         50         60 
MTAEPMSGNK LSTLVQKLHD FLAHSSEESE ETCSSPRLVM NQSTDKICGS GLNSDMMENN 

        70         80         90        100        110        120 
KEEGASTSEK SRSSGSSRSK RKPSIVTKYV ESDDEKPTDE NVNEKAATEN SENDITMQSL 

       130        140        150        160        170        180 
PKGTVIVQPE PVLNEDKDDF KGPEFRSRSK MKADNLKKRG EDGLHGIVSC TACGQQVNHF 

       190        200        210        220        230        240 
QKDSIYRHPS LKVLICKNCF KYYMSDDISR DSDGMDEQCR WCAEGGNLIC CDFCHNAFCK 

       250        260        270        280        290        300 
KCILRNLGRK ELSTIMDENN QWYCYICQPE PLLDLVTACN SVFENLEQLL QQNKKKIKVD 

       310        320        330        340        350        360 
SEKTSKVCDQ TSKFSPKKSS SSCNGEEKKL EESCSGSVSS TYSHSALSVP KEMIKKTTKL 

       370        380        390        400        410        420 
IETTSNMNSS YIKFLKQAAD NSEMTSAMKL CQLKSFKSVL DDIKKAHLAL EEDLNSEIQA 

       430        440        450        460        470        480 
LDDVHKEKNT KDLKSTDAKS ETKLGKGEKS YSTEKREFLK LDARSSVKAI DGEEQRAHKS 

       490        500        510        520        530        540 
TSGEHKGSGR KDGSQYEPTN TPEDLDMDIV SVPSSVPEDI FDSLESAMEV QSSADYQGDG 

       550        560        570        580        590        600 
NSGTEPELES SSVKLNVSSK DSRGNIKSKV TAKVRKELFV KLTPVSLSNS PIKGVDCQEV 

       610        620        630        640        650        660 
SQEKNGRKSS GVARSSEKCR PREEISDHEN NVTILLEDSD LRRSPRVKTT PLRRQTESNP 

       670        680        690        700        710        720 
AMSNSDEESN GTMKEKQKMS GPIRKKDKRN SADCATDNPK PHKVPKAKQP VIGDQNSDSD 

       730        740        750        760        770        780 
EMLAVLKEAS QMGHSSSSDT DINEPQMNHK GKTGKDDNGK RKRKNSTSGS DFDTKKGKST 

       790        800        810        820        830        840 
ETSIISKKKR QNYSESSNYD SELEREIKTM SRIGAARKSV PEKKEEDSSE DEKQGKKVVD 

       850        860        870        880        890        900 
NGGHERAKTT QEGSSADDTG DTEGRQGGSC SIAGGSIEKV RSGVEFREML CKPGVSSDGA 

       910        920        930        940        950        960 
EKPSVKEENV NSPEDKRVSK TKEKTKHLRS RQSRKGKGGS SDGTDRFPKK EQSDESSEGE 

       970        980        990       1000       1010       1020 
KKQSRQRPGT KGKKAPDLKG ETLKREQEWD SSSDGTERLP EEEEIGPFSK GIKQSKTDTA 

      1030       1040       1050       1060       1070       1080 
GGEKKGKKWK DKSCEKKEEL SDSVDKLPGK GDSCDSSEDK KTRNRVSLRE KKRFSLPAKS 

      1090       1100       1110       1120       1130       1140 
PGKRPECSSS DTEKSLKGQC CDSTEKRPKR IDLRERRNSS SKRNTKEVKS ASSSSDAEGS 

      1150       1160       1170       1180       1190       1200 
SEDNKKQKKQ RTSAKKKTGN TKEKKRNSLR ATPKRKQVDI TSSSSDIGDD DQNSAGEESS 

      1210       1220       1230       1240       1250       1260 
DEQKIKPVTE NLVLPSHTGF CQSSGDEALS KSVPATVDDD DDDNDPENRI AKKMLLEEIK 

      1270       1280       1290       1300       1310       1320 
ANLSSDEDGS SDDEPDGGGK KRIGKQSEES PADDGELRRE QLAVNQVNSE SDSDSEESKK 

      1330       1340       1350       1360       1370       1380 
PRYRHRLLRH KLTLSDGESG EEKPTKPKEH KEAKGRNRRK VSSEDSEDTD FQESGVSEEV 

      1390       1400       1410       1420       1430       1440 
SESEDEQRPR TRSAKKAELE ENQRSYKQKK KRRRIKVQED SSSENKSHSE EDKKEGDEED 

      1450       1460       1470       1480       1490       1500 
EEDEDEDEED ENDDSKSPGK GRKKIRKILK DDKLRTETQN ALKEEEERRK RIAERERERE 

      1510       1520       1530       1540       1550       1560 
KLREVIEIED ASPTKCPITT KLVLDENEET KEPLVQVHRN MVIKLKPHQV DGVQFMWDCC 

      1570       1580       1590       1600       1610       1620 
CESVEKTKKS PGSGCILAHC MGLGKTLQVV SFLHTVLLCD KLDFSTALVV CPLNTALNWM 

      1630       1640       1650       1660       1670       1680 
NEFEKWQEGL NDNEKLEVSE LATVKRPQER SYMLQRWQED GGVMIIGYEM YRNLAQGRNV 

      1690       1700       1710       1720       1730       1740 
KSRKLKDIFN KALVDPGPDF VVCDEGHILK NEASAVSKAM NSIKSRRRII LTGTPLQNNL 

      1750       1760       1770       1780       1790       1800 
IEYHCMVNFI KENLLGSIKE FRNRFINPIQ NGQCADSTMV DVRVMKKRAH ILYEMLAGCV 

      1810       1820       1830       1840       1850       1860 
QRKDYTALTK FLPPKHEYVL AVRMTAIQCK LYQYYLDHLT GVGNSTEGGR GKAGAKLFQD 

      1870       1880       1890       1900       1910       1920 
FQMLSRIWTH PWCLQLDYIS KENKGYFDED SMDEFIASDS DETSKSLSSD EKKKPKGKKG 

      1930       1940       1950       1960       1970       1980 
KKDSSSSGSG SDNDVEVIKV WNSRSRGGGD GNVDDTGNNP SVSLKLDESK TTSTSNPSSP 

      1990       2000       2010       2020       2030       2040 
APDWYKDFVT DTDAEVLEHS GKMVLLFEIL RMAEEIGDKV LVFSQSLISL DLIEDFLELA 

      2050       2060       2070       2080       2090       2100 
SREKTEDKEK PLIYKGEGKW IRNIDYYRLD GSTNAQSRKK WAEEFNDETN VRGRLFIIST 

      2110       2120       2130       2140       2150       2160 
KAGSLGINLV AANRVIIFDA SWNPSYDIQS IFRVYRFGQT KPVYVYRFLA QGTMEDKIYD 

      2170       2180       2190       2200       2210       2220 
RQVTKQSLSF RVVDQQQVER HFTMNELTEL YTFEPDLLDD PNSEKKKKRD TPMLPKDTIL 

      2230       2240       2250       2260       2270       2280 
AELLQIHKEH IVGYHEHDSL LDHKEEEELT EEERKAAWAE YEAEKKGLTM RFNIPTGTNL 

      2290       2300       2310       2320       2330       2340 
PPVTFTSQTP YIPFNLGALS AMSNQQLEDL INQGREKVVE ATNSMTAVRI QPLEDIISTV 

      2350       2360       2370       2380       2390       2400 
WKENMNLSEA QVQALALSRQ ASQELDVKRR EAIYNDVLTK QQMLINCVQR ILMNRRLQQQ 

      2410       2420       2430       2440       2450       2460 
YTQQQQQQLT YQQATLSHLM MPKPPNLIMT PSNYQQIDMR GMYQSVAGGM QPPPLQRAPP 

      2470 
PTVRSKNPGP SPGKSM 

« Hide

References

« Hide 'large scale' references
[1]"Comparison of the human and murine ATRX gene identifies highly conserved, functionally important domains."
Picketts D.J., Tastan A.O., Higgs D.R., Gibbons R.J.
Mamm. Genome 9:400-403(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors."
le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F., Losson R., Chambon P.
EMBO J. 15:6701-6715(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 325-1176.
[4]"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.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89; SER-717; SER-719; SER-801 AND SER-1339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"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.
[7]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[9]"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.
[10]"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: FUNCTION, ASSOCIATION WITH HISTONE H3.3.
[11]"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: ASSOCIATION WITH HISTONE H3.3.
[12]"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: SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-239 AND VAL-580.
[13]"Citrullination regulates pluripotency and histone H1 binding to chromatin."
Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S., Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C., Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.
Nature 507:104-108(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-1063.
[14]"ATRX partners with cohesin and MeCP2 and contributes to developmental silencing of imprinted genes in the brain."
Kernohan K.D., Jiang Y., Tremblay D.C., Bonvissuto A.C., Eubanks J.H., Mann M.R., Berube N.G.
Dev. Cell 18:191-202(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MECP2; SMC1 AND SMC3.
[15]"ATRX interacts with H3.3 in maintaining telomere structural integrity in pluripotent embryonic stem cells."
Wong L.H., McGhie J.D., Sim M., Anderson M.A., Ahn S., Hannan R.D., George A.J., Morgan K.A., Mann J.R., Choo K.H.
Genome Res. 20:351-360(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HISTONE H3.3.
[16]"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: FUNCTION, INTERACTION WITH RAD50; MRE11A AND NBN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF026032 mRNA. Translation: AAC08741.1.
AL671893, AL670660 Genomic DNA. Translation: CAM16251.1.
AL670660, AL671893 Genomic DNA. Translation: CAM19070.1.
X99643 mRNA. Translation: CAA67962.1.
CCDSCCDS41095.1.
RefSeqNP_033556.2. NM_009530.2.
UniGeneMm.10141.

3D structure databases

ProteinModelPortalQ61687.
SMRQ61687. Positions 158-295.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204603. 5 interactions.
IntActQ61687. 3 interactions.
MINTMINT-4084315.

PTM databases

PhosphoSiteQ61687.

Proteomic databases

MaxQBQ61687.
PaxDbQ61687.
PRIDEQ61687.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000113573; ENSMUSP00000109203; ENSMUSG00000031229.
GeneID22589.
KEGGmmu:22589.
UCSCuc009ubb.2. mouse.

Organism-specific databases

CTD546.
MGIMGI:103067. Atrx.

Phylogenomic databases

eggNOGCOG0553.
GeneTreeENSGT00550000074619.
HOGENOMHOG000231302.
HOVERGENHBG000104.
InParanoidA2ADH4.
KOK10779.
OMADQRPRTR.
OrthoDBEOG7G4QDQ.
TreeFamTF313172.

Gene expression databases

ArrayExpressQ61687.
BgeeQ61687.
GenevestigatorQ61687.

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

NextBio302925.
PROQ61687.
SOURCESearch...

Entry information

Entry nameATRX_MOUSE
AccessionPrimary (citable) accession number: Q61687
Secondary accession number(s): A2ADH4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot