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Q61687

- ATRX_MOUSE

UniProt

Q61687 - ATRX_MOUSE

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Protein

Transcriptional regulator ATRX

Gene

Atrx

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 (PubMed:20211137) 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; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri216 – 27156PHD-type; atypicalPROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi1579 – 15868ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. cellular response to hydroxyurea Source: UniProtKB
  2. chromatin remodeling Source: UniProtKB
  3. DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  4. DNA repair Source: UniProtKB-KW
  5. DNA replication-independent nucleosome assembly Source: UniProtKB
  6. forebrain development Source: MGI
  7. negative regulation of telomeric RNA transcription from RNA pol II promoter Source: UniProtKB
  8. nucleosome assembly Source: UniProtKB
  9. positive regulation of nuclear cell cycle DNA replication Source: UniProtKB
  10. positive regulation of telomere maintenance Source: UniProtKB
  11. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  12. replication fork processing Source: UniProtKB
  13. seminiferous tubule development Source: MGI
  14. Sertoli cell 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.By similarity

GO - Cellular componenti

  1. heterochromatin Source: MGI
  2. mitochondrion Source: Ensembl
  3. nuclear chromosome Source: MGI
  4. nucleolus Source: Ensembl
  5. nucleus Source: MGI
  6. SWI/SNF superfamily-type complex Source: UniProtKB
  7. 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 ATRXPRO_0000074303Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341PhosphoserineBy similarity
Modified residuei89 – 891Phosphotyrosine1 Publication
Modified residuei92 – 921Phosphoserine2 Publications
Modified residuei111 – 1111PhosphoserineBy similarity
Modified residuei583 – 5831PhosphothreonineBy similarity
Modified residuei586 – 5861PhosphoserineBy similarity
Modified residuei590 – 5901PhosphoserineBy similarity
Modified residuei626 – 6261PhosphoserineBy similarity
Modified residuei663 – 6631PhosphoserineBy similarity
Modified residuei665 – 6651PhosphoserineBy similarity
Modified residuei717 – 7171Phosphoserine1 Publication
Modified residuei719 – 7191Phosphoserine1 Publication
Modified residuei801 – 8011Phosphoserine1 Publication
Modified residuei854 – 8541PhosphoserineBy similarity
Modified residuei855 – 8551PhosphoserineBy similarity
Modified residuei871 – 8711PhosphoserineBy similarity
Modified residuei1041 – 10411PhosphoserineBy similarity
Modified residuei1063 – 10631Citrulline1 Publication
Modified residuei1309 – 13091PhosphoserineBy similarity
Modified residuei1311 – 13111PhosphoserineBy similarity
Modified residuei1313 – 13131PhosphoserineBy similarity
Modified residuei1335 – 13351PhosphoserineBy similarity
Modified residuei1339 – 13391Phosphoserine1 Publication
Modified residuei1512 – 15121PhosphoserineBy similarity
Modified residuei1975 – 19751PhosphoserineBy similarity
Modified residuei1979 – 19791PhosphoserineBy similarity
Modified residuei2203 – 22031PhosphoserineBy similarity

Post-translational modificationi

Citrullinated by PADI4.1 Publication

Keywords - PTMi

Citrullination, Phosphoprotein

Proteomic databases

MaxQBiQ61687.
PaxDbiQ61687.
PRIDEiQ61687.

PTM databases

PhosphoSiteiQ61687.

Expressioni

Gene expression databases

BgeeiQ61687.
ExpressionAtlasiQ61687. baseline and differential.
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.
DIPiDIP-55974N.
IntActiQ61687. 8 interactions.
MINTiMINT-4084315.

Structurei

3D structure databases

ProteinModelPortaliQ61687.
SMRiQ61687. Positions 158-295.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini158 – 295138ADDPROSITE-ProRule annotationAdd
BLAST
Domaini1566 – 1753188Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2008 – 2188181Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1169 – 1313145Interaction with DAXXBy similarityAdd
BLAST
Regioni1993 – 2263271Interaction with MECP2By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi573 – 58614PxVxL motifAdd
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).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

Belongs to the SNF2/RAD54 helicase family.Curated
Contains 1 ADD domain.PROSITE-ProRule annotation
Contains 1 GATA-type zinc finger.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri169 – 20537GATA-type; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri216 – 27156PHD-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0553.
GeneTreeiENSGT00550000074619.
HOGENOMiHOG000231302.
HOVERGENiHBG000104.
InParanoidiQ61687.
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

« Hide

        10         20         30         40         50
MTAEPMSGNK LSTLVQKLHD FLAHSSEESE ETCSSPRLVM NQSTDKICGS
60 70 80 90 100
GLNSDMMENN KEEGASTSEK SRSSGSSRSK RKPSIVTKYV ESDDEKPTDE
110 120 130 140 150
NVNEKAATEN SENDITMQSL PKGTVIVQPE PVLNEDKDDF KGPEFRSRSK
160 170 180 190 200
MKADNLKKRG EDGLHGIVSC TACGQQVNHF QKDSIYRHPS LKVLICKNCF
210 220 230 240 250
KYYMSDDISR DSDGMDEQCR WCAEGGNLIC CDFCHNAFCK KCILRNLGRK
260 270 280 290 300
ELSTIMDENN QWYCYICQPE PLLDLVTACN SVFENLEQLL QQNKKKIKVD
310 320 330 340 350
SEKTSKVCDQ TSKFSPKKSS SSCNGEEKKL EESCSGSVSS TYSHSALSVP
360 370 380 390 400
KEMIKKTTKL IETTSNMNSS YIKFLKQAAD NSEMTSAMKL CQLKSFKSVL
410 420 430 440 450
DDIKKAHLAL EEDLNSEIQA LDDVHKEKNT KDLKSTDAKS ETKLGKGEKS
460 470 480 490 500
YSTEKREFLK LDARSSVKAI DGEEQRAHKS TSGEHKGSGR KDGSQYEPTN
510 520 530 540 550
TPEDLDMDIV SVPSSVPEDI FDSLESAMEV QSSADYQGDG NSGTEPELES
560 570 580 590 600
SSVKLNVSSK DSRGNIKSKV TAKVRKELFV KLTPVSLSNS PIKGVDCQEV
610 620 630 640 650
SQEKNGRKSS GVARSSEKCR PREEISDHEN NVTILLEDSD LRRSPRVKTT
660 670 680 690 700
PLRRQTESNP AMSNSDEESN GTMKEKQKMS GPIRKKDKRN SADCATDNPK
710 720 730 740 750
PHKVPKAKQP VIGDQNSDSD EMLAVLKEAS QMGHSSSSDT DINEPQMNHK
760 770 780 790 800
GKTGKDDNGK RKRKNSTSGS DFDTKKGKST ETSIISKKKR QNYSESSNYD
810 820 830 840 850
SELEREIKTM SRIGAARKSV PEKKEEDSSE DEKQGKKVVD NGGHERAKTT
860 870 880 890 900
QEGSSADDTG DTEGRQGGSC SIAGGSIEKV RSGVEFREML CKPGVSSDGA
910 920 930 940 950
EKPSVKEENV NSPEDKRVSK TKEKTKHLRS RQSRKGKGGS SDGTDRFPKK
960 970 980 990 1000
EQSDESSEGE KKQSRQRPGT KGKKAPDLKG ETLKREQEWD SSSDGTERLP
1010 1020 1030 1040 1050
EEEEIGPFSK GIKQSKTDTA GGEKKGKKWK DKSCEKKEEL SDSVDKLPGK
1060 1070 1080 1090 1100
GDSCDSSEDK KTRNRVSLRE KKRFSLPAKS PGKRPECSSS DTEKSLKGQC
1110 1120 1130 1140 1150
CDSTEKRPKR IDLRERRNSS SKRNTKEVKS ASSSSDAEGS SEDNKKQKKQ
1160 1170 1180 1190 1200
RTSAKKKTGN TKEKKRNSLR ATPKRKQVDI TSSSSDIGDD DQNSAGEESS
1210 1220 1230 1240 1250
DEQKIKPVTE NLVLPSHTGF CQSSGDEALS KSVPATVDDD DDDNDPENRI
1260 1270 1280 1290 1300
AKKMLLEEIK ANLSSDEDGS SDDEPDGGGK KRIGKQSEES PADDGELRRE
1310 1320 1330 1340 1350
QLAVNQVNSE SDSDSEESKK PRYRHRLLRH KLTLSDGESG EEKPTKPKEH
1360 1370 1380 1390 1400
KEAKGRNRRK VSSEDSEDTD FQESGVSEEV SESEDEQRPR TRSAKKAELE
1410 1420 1430 1440 1450
ENQRSYKQKK KRRRIKVQED SSSENKSHSE EDKKEGDEED EEDEDEDEED
1460 1470 1480 1490 1500
ENDDSKSPGK GRKKIRKILK DDKLRTETQN ALKEEEERRK RIAERERERE
1510 1520 1530 1540 1550
KLREVIEIED ASPTKCPITT KLVLDENEET KEPLVQVHRN MVIKLKPHQV
1560 1570 1580 1590 1600
DGVQFMWDCC CESVEKTKKS PGSGCILAHC MGLGKTLQVV SFLHTVLLCD
1610 1620 1630 1640 1650
KLDFSTALVV CPLNTALNWM NEFEKWQEGL NDNEKLEVSE LATVKRPQER
1660 1670 1680 1690 1700
SYMLQRWQED GGVMIIGYEM YRNLAQGRNV KSRKLKDIFN KALVDPGPDF
1710 1720 1730 1740 1750
VVCDEGHILK NEASAVSKAM NSIKSRRRII LTGTPLQNNL IEYHCMVNFI
1760 1770 1780 1790 1800
KENLLGSIKE FRNRFINPIQ NGQCADSTMV DVRVMKKRAH ILYEMLAGCV
1810 1820 1830 1840 1850
QRKDYTALTK FLPPKHEYVL AVRMTAIQCK LYQYYLDHLT GVGNSTEGGR
1860 1870 1880 1890 1900
GKAGAKLFQD FQMLSRIWTH PWCLQLDYIS KENKGYFDED SMDEFIASDS
1910 1920 1930 1940 1950
DETSKSLSSD EKKKPKGKKG KKDSSSSGSG SDNDVEVIKV WNSRSRGGGD
1960 1970 1980 1990 2000
GNVDDTGNNP SVSLKLDESK TTSTSNPSSP APDWYKDFVT DTDAEVLEHS
2010 2020 2030 2040 2050
GKMVLLFEIL RMAEEIGDKV LVFSQSLISL DLIEDFLELA SREKTEDKEK
2060 2070 2080 2090 2100
PLIYKGEGKW IRNIDYYRLD GSTNAQSRKK WAEEFNDETN VRGRLFIIST
2110 2120 2130 2140 2150
KAGSLGINLV AANRVIIFDA SWNPSYDIQS IFRVYRFGQT KPVYVYRFLA
2160 2170 2180 2190 2200
QGTMEDKIYD RQVTKQSLSF RVVDQQQVER HFTMNELTEL YTFEPDLLDD
2210 2220 2230 2240 2250
PNSEKKKKRD TPMLPKDTIL AELLQIHKEH IVGYHEHDSL LDHKEEEELT
2260 2270 2280 2290 2300
EEERKAAWAE YEAEKKGLTM RFNIPTGTNL PPVTFTSQTP YIPFNLGALS
2310 2320 2330 2340 2350
AMSNQQLEDL INQGREKVVE ATNSMTAVRI QPLEDIISTV WKENMNLSEA
2360 2370 2380 2390 2400
QVQALALSRQ ASQELDVKRR EAIYNDVLTK QQMLINCVQR ILMNRRLQQQ
2410 2420 2430 2440 2450
YTQQQQQQLT YQQATLSHLM MPKPPNLIMT PSNYQQIDMR GMYQSVAGGM
2460 2470
QPPPLQRAPP PTVRSKNPGP SPGKSM
Length:2,476
Mass (Da):278,587
Last modified:July 27, 2011 - v3
Checksum:iB2E2218B6CC791EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1571K → I in AAC08741. (PubMed:9545503)Curated
Sequence conflicti1953 – 19531V → M in AAC08741. (PubMed:9545503)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
DIPi DIP-55974N.
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 Q61687.
KOi K10779.
OMAi DQRPRTR.
OrthoDBi EOG7G4QDQ.
TreeFami TF313172.

Miscellaneous databases

NextBioi 302925.
PROi Q61687.
SOURCEi Search...

Gene expression databases

Bgeei Q61687.
ExpressionAtlasi Q61687. baseline and differential.
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: October 29, 2014
This is version 135 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