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Q61687

- ATRX_MOUSE

UniProt

Q61687 - ATRX_MOUSE

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Protein
Transcriptional regulator ATRX
Gene
Atrx, Hp1bp2, Xnp
Organism
Mus musculus (Mouse)
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 probably implying recruitment of CBX5 to telomers. Reports on the involvement in transcriptional regulation of telomeric repeat-containing RNA (TERRA) are conflicting; according (1 Publication) 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.4 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri169 – 20537GATA-type; atypical
Add
BLAST
Zinc fingeri216 – 27156PHD-type; atypical
Add
BLAST
Nucleotide bindingi1579 – 15868ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. chromatin binding Source: MGI
  4. helicase activity Source: UniProtKB-KW
  5. histone binding Source: UniProtKB
  6. protein binding Source: UniProtKB
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  2. DNA repair Source: UniProtKB-KW
  3. DNA replication-independent nucleosome assembly Source: UniProtKB
  4. Sertoli cell development Source: MGI
  5. cellular response to hydroxyurea Source: UniProtKB
  6. chromatin remodeling Source: UniProtKB
  7. forebrain development Source: MGI
  8. negative regulation of telomeric RNA transcription from RNA pol II promoter Source: UniProtKB
  9. nucleosome assembly Source: UniProtKB
  10. positive regulation of nuclear cell cycle DNA replication Source: UniProtKB
  11. positive regulation of telomere maintenance Source: UniProtKB
  12. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  13. replication fork processing Source: UniProtKB
  14. seminiferous tubule development Source: MGI
  15. spermatogenesis Source: MGI
  16. 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
HP1 alpha-interacting protein
HP1-BP38 protein
Heterochromatin protein 2
X-linked nuclear protein
Gene namesi
Name:Atrx
Synonyms:Hp1bp2, Xnp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:103067. Atrx.

Subcellular locationi

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.4 Publications

GO - Cellular componenti

  1. PML body Source: UniProtKB-SubCell
  2. SWI/SNF superfamily-type complex Source: UniProtKB
  3. heterochromatin Source: MGI
  4. nuclear chromosome Source: MGI
  5. nucleus Source: MGI
  6. telomeric heterochromatin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi239 – 2391C → G: Reduces pericentromeric localization. Abolishes pericentromeric localization; when associated with E-580. 1 Publication
Mutagenesisi580 – 5801V → E: Reduces pericentromeric localization. Abolishes pericentromeric localization; when associated with G-239. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24762476Transcriptional regulator ATRX
PRO_0000074303Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341Phosphoserine By similarity
Modified residuei89 – 891Phosphotyrosine1 Publication
Modified residuei92 – 921Phosphoserine2 Publications
Modified residuei111 – 1111Phosphoserine By similarity
Modified residuei583 – 5831Phosphothreonine By similarity
Modified residuei586 – 5861Phosphoserine By similarity
Modified residuei590 – 5901Phosphoserine By similarity
Modified residuei626 – 6261Phosphoserine By similarity
Modified residuei663 – 6631Phosphoserine By similarity
Modified residuei665 – 6651Phosphoserine By similarity
Modified residuei717 – 7171Phosphoserine1 Publication
Modified residuei719 – 7191Phosphoserine1 Publication
Modified residuei801 – 8011Phosphoserine1 Publication
Modified residuei854 – 8541Phosphoserine By similarity
Modified residuei855 – 8551Phosphoserine By similarity
Modified residuei871 – 8711Phosphoserine By similarity
Modified residuei1041 – 10411Phosphoserine By similarity
Modified residuei1063 – 10631Citrulline
Modified residuei1309 – 13091Phosphoserine By similarity
Modified residuei1311 – 13111Phosphoserine By similarity
Modified residuei1313 – 13131Phosphoserine By similarity
Modified residuei1335 – 13351Phosphoserine By similarity
Modified residuei1339 – 13391Phosphoserine1 Publication
Modified residuei1512 – 15121Phosphoserine By similarity
Modified residuei1975 – 19751Phosphoserine By similarity
Modified residuei1979 – 19791Phosphoserine By similarity
Modified residuei2203 – 22031Phosphoserine By similarity

Post-translational modificationi

Citrullinated by PADI4.

Keywords - PTMi

Citrullination, Phosphoprotein

Proteomic databases

MaxQBiQ61687.
PaxDbiQ61687.
PRIDEiQ61687.

PTM databases

PhosphoSiteiQ61687.

Expressioni

Gene expression databases

ArrayExpressiQ61687.
BgeeiQ61687.
GenevestigatoriQ61687.

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 SMC3.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Mecp2Q9Z2D63EBI-2657527,EBI-1188816
Smc1aQ9CU624EBI-2657527,EBI-2550016

Protein-protein interaction databases

BioGridi204603. 5 interactions.
IntActiQ61687. 8 interactions.
MINTiMINT-4084315.

Structurei

3D structure databases

ProteinModelPortaliQ61687.
SMRiQ61687. Positions 158-295.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini158 – 295138ADD
Add
BLAST
Domaini1566 – 1753188Helicase ATP-binding
Add
BLAST
Domaini2008 – 2188181Helicase C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1169 – 1313145Interaction with DAXX By similarity
Add
BLAST
Regioni1993 – 2263271Interaction with MECP2 By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi573 – 58614PxVxL motif
Add
BLAST
Motifi1704 – 17074DEGH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi319 – 3224Poly-Ser
Compositional biasi735 – 7384Poly-Ser
Compositional biasi1001 – 10044Poly-Glu
Compositional biasi1130 – 11356Poly-Ser
Compositional biasi1182 – 11854Poly-Ser
Compositional biasi1238 – 12458Poly-Asp
Compositional biasi1484 – 14874Poly-Glu
Compositional biasi1924 – 19318Poly-Ser
Compositional biasi2205 – 22084Poly-Lys
Compositional biasi2245 – 22484Poly-Glu
Compositional biasi2403 – 24086Poly-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 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.

Sequence similaritiesi

Contains 1 ADD domain.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0553.
GeneTreeiENSGT00550000074619.
HOGENOMiHOG000231302.
HOVERGENiHBG000104.
InParanoidiA2ADH4.
KOiK10779.
OMAiDQRPRTR.
OrthoDBiEOG7G4QDQ.
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]

Sequencei

Sequence statusi: Complete.

Q61687-1 [UniParc]FASTAAdd to Basket

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MTAEPMSGNK LSTLVQKLHD FLAHSSEESE ETCSSPRLVM NQSTDKICGS     50
GLNSDMMENN KEEGASTSEK SRSSGSSRSK RKPSIVTKYV ESDDEKPTDE 100
NVNEKAATEN SENDITMQSL PKGTVIVQPE PVLNEDKDDF KGPEFRSRSK 150
MKADNLKKRG EDGLHGIVSC TACGQQVNHF QKDSIYRHPS LKVLICKNCF 200
KYYMSDDISR DSDGMDEQCR WCAEGGNLIC CDFCHNAFCK KCILRNLGRK 250
ELSTIMDENN QWYCYICQPE PLLDLVTACN SVFENLEQLL QQNKKKIKVD 300
SEKTSKVCDQ TSKFSPKKSS SSCNGEEKKL EESCSGSVSS TYSHSALSVP 350
KEMIKKTTKL IETTSNMNSS YIKFLKQAAD NSEMTSAMKL CQLKSFKSVL 400
DDIKKAHLAL EEDLNSEIQA LDDVHKEKNT KDLKSTDAKS ETKLGKGEKS 450
YSTEKREFLK LDARSSVKAI DGEEQRAHKS TSGEHKGSGR KDGSQYEPTN 500
TPEDLDMDIV SVPSSVPEDI FDSLESAMEV QSSADYQGDG NSGTEPELES 550
SSVKLNVSSK DSRGNIKSKV TAKVRKELFV KLTPVSLSNS PIKGVDCQEV 600
SQEKNGRKSS GVARSSEKCR PREEISDHEN NVTILLEDSD LRRSPRVKTT 650
PLRRQTESNP AMSNSDEESN GTMKEKQKMS GPIRKKDKRN SADCATDNPK 700
PHKVPKAKQP VIGDQNSDSD EMLAVLKEAS QMGHSSSSDT DINEPQMNHK 750
GKTGKDDNGK RKRKNSTSGS DFDTKKGKST ETSIISKKKR QNYSESSNYD 800
SELEREIKTM SRIGAARKSV PEKKEEDSSE DEKQGKKVVD NGGHERAKTT 850
QEGSSADDTG DTEGRQGGSC SIAGGSIEKV RSGVEFREML CKPGVSSDGA 900
EKPSVKEENV NSPEDKRVSK TKEKTKHLRS RQSRKGKGGS SDGTDRFPKK 950
EQSDESSEGE KKQSRQRPGT KGKKAPDLKG ETLKREQEWD SSSDGTERLP 1000
EEEEIGPFSK GIKQSKTDTA GGEKKGKKWK DKSCEKKEEL SDSVDKLPGK 1050
GDSCDSSEDK KTRNRVSLRE KKRFSLPAKS PGKRPECSSS DTEKSLKGQC 1100
CDSTEKRPKR IDLRERRNSS SKRNTKEVKS ASSSSDAEGS SEDNKKQKKQ 1150
RTSAKKKTGN TKEKKRNSLR ATPKRKQVDI TSSSSDIGDD DQNSAGEESS 1200
DEQKIKPVTE NLVLPSHTGF CQSSGDEALS KSVPATVDDD DDDNDPENRI 1250
AKKMLLEEIK ANLSSDEDGS SDDEPDGGGK KRIGKQSEES PADDGELRRE 1300
QLAVNQVNSE SDSDSEESKK PRYRHRLLRH KLTLSDGESG EEKPTKPKEH 1350
KEAKGRNRRK VSSEDSEDTD FQESGVSEEV SESEDEQRPR TRSAKKAELE 1400
ENQRSYKQKK KRRRIKVQED SSSENKSHSE EDKKEGDEED EEDEDEDEED 1450
ENDDSKSPGK GRKKIRKILK DDKLRTETQN ALKEEEERRK RIAERERERE 1500
KLREVIEIED ASPTKCPITT KLVLDENEET KEPLVQVHRN MVIKLKPHQV 1550
DGVQFMWDCC CESVEKTKKS PGSGCILAHC MGLGKTLQVV SFLHTVLLCD 1600
KLDFSTALVV CPLNTALNWM NEFEKWQEGL NDNEKLEVSE LATVKRPQER 1650
SYMLQRWQED GGVMIIGYEM YRNLAQGRNV KSRKLKDIFN KALVDPGPDF 1700
VVCDEGHILK NEASAVSKAM NSIKSRRRII LTGTPLQNNL IEYHCMVNFI 1750
KENLLGSIKE FRNRFINPIQ NGQCADSTMV DVRVMKKRAH ILYEMLAGCV 1800
QRKDYTALTK FLPPKHEYVL AVRMTAIQCK LYQYYLDHLT GVGNSTEGGR 1850
GKAGAKLFQD FQMLSRIWTH PWCLQLDYIS KENKGYFDED SMDEFIASDS 1900
DETSKSLSSD EKKKPKGKKG KKDSSSSGSG SDNDVEVIKV WNSRSRGGGD 1950
GNVDDTGNNP SVSLKLDESK TTSTSNPSSP APDWYKDFVT DTDAEVLEHS 2000
GKMVLLFEIL RMAEEIGDKV LVFSQSLISL DLIEDFLELA SREKTEDKEK 2050
PLIYKGEGKW IRNIDYYRLD GSTNAQSRKK WAEEFNDETN VRGRLFIIST 2100
KAGSLGINLV AANRVIIFDA SWNPSYDIQS IFRVYRFGQT KPVYVYRFLA 2150
QGTMEDKIYD RQVTKQSLSF RVVDQQQVER HFTMNELTEL YTFEPDLLDD 2200
PNSEKKKKRD TPMLPKDTIL AELLQIHKEH IVGYHEHDSL LDHKEEEELT 2250
EEERKAAWAE YEAEKKGLTM RFNIPTGTNL PPVTFTSQTP YIPFNLGALS 2300
AMSNQQLEDL INQGREKVVE ATNSMTAVRI QPLEDIISTV WKENMNLSEA 2350
QVQALALSRQ ASQELDVKRR EAIYNDVLTK QQMLINCVQR ILMNRRLQQQ 2400
YTQQQQQQLT YQQATLSHLM MPKPPNLIMT PSNYQQIDMR GMYQSVAGGM 2450
QPPPLQRAPP PTVRSKNPGP SPGKSM 2476
Length:2,476
Mass (Da):278,587
Last modified:July 27, 2011 - v3
Checksum:iB2E2218B6CC791EC
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1571K → I in AAC08741. 1 Publication
Sequence conflicti1953 – 19531V → M in AAC08741. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF026032 mRNA. Translation: AAC08741.1.
AL671893, AL670660 Genomic DNA. Translation: CAM16251.1.
AL670660, AL671893 Genomic DNA. Translation: CAM19070.1.
X99643 mRNA. Translation: CAA67962.1.
CCDSiCCDS41095.1.
RefSeqiNP_033556.2. NM_009530.2.
UniGeneiMm.10141.

Genome annotation databases

EnsembliENSMUST00000113573; ENSMUSP00000109203; ENSMUSG00000031229.
GeneIDi22589.
KEGGimmu:22589.
UCSCiuc009ubb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF026032 mRNA. Translation: AAC08741.1 .
AL671893 , AL670660 Genomic DNA. Translation: CAM16251.1 .
AL670660 , AL671893 Genomic DNA. Translation: CAM19070.1 .
X99643 mRNA. Translation: CAA67962.1 .
CCDSi CCDS41095.1.
RefSeqi NP_033556.2. NM_009530.2.
UniGenei Mm.10141.

3D structure databases

ProteinModelPortali Q61687.
SMRi Q61687. Positions 158-295.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204603. 5 interactions.
IntActi Q61687. 8 interactions.
MINTi MINT-4084315.

PTM databases

PhosphoSitei Q61687.

Proteomic databases

MaxQBi Q61687.
PaxDbi Q61687.
PRIDEi Q61687.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000113573 ; ENSMUSP00000109203 ; ENSMUSG00000031229 .
GeneIDi 22589.
KEGGi mmu:22589.
UCSCi uc009ubb.2. mouse.

Organism-specific databases

CTDi 546.
MGIi MGI:103067. Atrx.

Phylogenomic databases

eggNOGi COG0553.
GeneTreei ENSGT00550000074619.
HOGENOMi HOG000231302.
HOVERGENi HBG000104.
InParanoidi A2ADH4.
KOi K10779.
OMAi DQRPRTR.
OrthoDBi EOG7G4QDQ.
TreeFami TF313172.

Miscellaneous databases

NextBioi 302925.
PROi Q61687.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q61687.
Bgeei Q61687.
Genevestigatori Q61687.

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. "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. 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. 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. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. 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. 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. Cited for: FUNCTION, INTERACTION WITH RAD50; MRE11A AND NBN.

Entry informationi

Entry nameiATRX_MOUSE
AccessioniPrimary (citable) accession number: Q61687
Secondary accession number(s): A2ADH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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