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Protein

Transcriptional regulator ATRX

Gene

Atrx

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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. May be involved in transcriptional regulation of telomeric repeat-containing RNA (TERRA). 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 (By similarity).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

GO - Molecular functioni

GO - Biological processi

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, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional regulator ATRX (EC:3.6.4.12)
Alternative name(s):
ATP-dependent helicase ATRX
X-linked nuclear protein
pABP-2
Gene namesi
Name:Atrx
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619795. Atrx.

Subcellular locationi

  • Nucleus By similarity
  • Chromosometelomere By similarity
  • 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).By similarity

GO - Cellular componenti

  • cytoplasm Source: RGD
  • nucleus Source: RGD
  • PML body Source: UniProtKB-SubCell
  • SWI/SNF superfamily-type complex Source: UniProtKB
  • telomeric heterochromatin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›527›527Transcriptional regulator ATRXPRO_0000074306Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741PhosphoserineBy similarity
Cross-linki105 – 105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei112 – 1121PhosphoserineCombined sources
Modified residuei113 – 1131PhosphoserineCombined sources
Modified residuei114 – 1141PhosphoserineCombined sources
Modified residuei162 – 1621PhosphoserineCombined sources
Modified residuei184 – 1841CitrullineBy similarity
Modified residuei345 – 3451PhosphoserineCombined sources
Modified residuei346 – 3461PhosphoserineCombined sources
Modified residuei354 – 3541PhosphoserineBy similarity
Modified residuei423 – 4231PhosphoserineBy similarity
Modified residuei425 – 4251PhosphoserineBy similarity
Modified residuei427 – 4271PhosphoserineBy similarity
Modified residuei449 – 4491PhosphoserineBy similarity
Modified residuei453 – 4531PhosphoserineBy similarity

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Citrullination, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP70486.
PRIDEiP70486.

PTM databases

iPTMnetiP70486.
PhosphoSiteiP70486.

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 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiP70486. 1 interaction.
STRINGi10116.ENSRNOP00000041679.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni290 – 427138Interaction with DAXXBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi251 – 2566Poly-Ser
Compositional biasi304 – 3074Poly-Ser
Compositional biasi360 – 3678Poly-Asp

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

Phylogenomic databases

eggNOGiENOG410IQAR. Eukaryota.
ENOG4111V25. LUCA.
HOGENOMiHOG000231302.
HOVERGENiHBG105806.

Sequencei

Sequence statusi: Fragment.

P70486-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GRSVVEFGDM VCKRQQSAVS SAGSEKPSGK EENVHSPEDK RVTKSKEKSK
60 70 80 90 100
HLRTRTGRKV KSDVTDRFRK KEQSSESSEG EKKQGRQRTG TRGKKSTDLK
110 120 130 140 150
EEKVKREREY ESSSDGTEKL PEGEEIGLFS KGVKQNKNDT TDEAKKGKKW
160 170 180 190 200
KDKSCEKKEE LSDSVDRLPV KGESCDSSED KKTRNRVSLR EKKQFSLPAK
210 220 230 240 250
SSGKRPECSS SDTERSVKGE CCDSTDKRVK RIDLRERRSS NSKRSTKEVK
260 270 280 290 300
SGSSSSDAEG SSEDAKKQKK QRMSAKKKNS NTKERKRKSL RATTTKRKQA
310 320 330 340 350
DITSSSSDIG DDDQNSAGEE SSDEQKIKPV TENLVLPSHT GFCQSSGDEA
360 370 380 390 400
FSKSVPATVD DDDDDNDPEN RIAKKMLLEE IKANLSSDED GSSDDEPKEG
410 420 430 440 450
EKKRIGKQSE ETPGDDGSNQ VNSESDSDSE ESKKPRYRHR LLRHKLSLSD
460 470 480 490 500
GESGGEKKTK PKEHKETKGR NRRKVSSEDS EDTDFQESGV SEEVSESEDE
510 520
QRPRTRSAKK AELEENQRSY KQKKKRR
Length:527
Mass (Da):59,259
Last modified:February 1, 1997 - v1
Checksum:iABEF4B10C086D638
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei527 – 5271

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D64059 mRNA. Translation: BAA10936.1.
UniGeneiRn.107838.
Rn.226151.

Genome annotation databases

UCSCiRGD:619795. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D64059 mRNA. Translation: BAA10936.1.
UniGeneiRn.107838.
Rn.226151.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP70486. 1 interaction.
STRINGi10116.ENSRNOP00000041679.

PTM databases

iPTMnetiP70486.
PhosphoSiteiP70486.

Proteomic databases

PaxDbiP70486.
PRIDEiP70486.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:619795. rat.

Organism-specific databases

RGDi619795. Atrx.

Phylogenomic databases

eggNOGiENOG410IQAR. Eukaryota.
ENOG4111V25. LUCA.
HOGENOMiHOG000231302.
HOVERGENiHBG105806.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of annexin V-binding proteins with highly hydrophilic peptide structure."
    Ohsawa K., Imai Y., Ito D., Kohsaka S.
    J. Neurochem. 67:89-97(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Strain: Wistar.
    Tissue: Embryonic brain.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-113; SER-114; SER-162; SER-345 AND SER-346, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATRX_RAT
AccessioniPrimary (citable) accession number: P70486
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: February 1, 1997
Last modified: June 8, 2016
This is version 90 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.