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Transcriptional regulator ATRX (EC 3.6.4.12) (ATP-dependent helicase ATRX) (X-linked nuclear protein) (pABP-2) (Fragment)

 ATRX_RAT                Reviewed;         527 AA.
P70486;
02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
22-NOV-2017, entry version 98.
RecName: Full=Transcriptional regulator ATRX;
EC=3.6.4.12;
AltName: Full=ATP-dependent helicase ATRX;
AltName: Full=X-linked nuclear protein;
AltName: Full=pABP-2;
Flags: Fragment;
Name=Atrx;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
STRAIN=Wistar; TISSUE=Embryonic brain;
PubMed=8667030;
Ohsawa K., Imai Y., Ito D., Kohsaka S.;
"Molecular cloning and characterization of annexin V-binding proteins
with highly hydrophilic peptide structure.";
J. Neurochem. 67:89-97(1996).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-113; SER-114;
SER-162; SER-345 AND SER-346, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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. 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. Binds to zinc-finger coding genes with
atypical chromatin signatures and regulates its H3K9me3 levels.
Forms a complex with ZNF274, TRIM28 and SETDB1 to facilitate the
deposition and maintenance of H3K9me3 at the 3' exons of zinc-
finger genes (By similarity). {ECO:0000250|UniProtKB:P46100}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: 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, MRE11 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. Interacts with SETDB1, TRIM28 and ZNF274 (By similarity).
{ECO:0000250|UniProtKB:P46100}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere
{ECO:0000250}. Nucleus, PML body {ECO:0000250}. 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). {ECO:0000250}.
-!- 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).
{ECO:0000250}.
-!- DOMAIN: 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.
-!- PTM: Citrullinated by PADI4. {ECO:0000250}.
-!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
{ECO:0000305}.
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EMBL; D64059; BAA10936.1; -; mRNA.
UniGene; Rn.107838; -.
UniGene; Rn.226151; -.
IntAct; P70486; 1.
STRING; 10116.ENSRNOP00000041679; -.
iPTMnet; P70486; -.
PhosphoSitePlus; P70486; -.
PaxDb; P70486; -.
PRIDE; P70486; -.
UCSC; RGD:619795; rat.
RGD; 619795; Atrx.
eggNOG; ENOG410IQAR; Eukaryota.
eggNOG; ENOG4111V25; LUCA.
HOGENOM; HOG000231302; -.
HOVERGEN; HBG105806; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0000792; C:heterochromatin; ISO:RGD.
GO; GO:0000228; C:nuclear chromosome; ISO:RGD.
GO; GO:0000784; C:nuclear chromosome, telomeric region; ISO:RGD.
GO; GO:0031618; C:nuclear pericentric heterochromatin; ISO:RGD.
GO; GO:1990707; C:nuclear subtelomeric heterochromatin; ISO:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005721; C:pericentric heterochromatin; ISO:RGD.
GO; GO:0016605; C:PML body; ISO:RGD.
GO; GO:0070603; C:SWI/SNF superfamily-type complex; ISS:UniProtKB.
GO; GO:0031933; C:telomeric heterochromatin; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0070087; F:chromo shadow domain binding; ISO:RGD.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0015616; F:DNA translocase activity; ISO:RGD.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0042393; F:histone binding; ISS:UniProtKB.
GO; GO:0035064; F:methylated histone binding; ISO:RGD.
GO; GO:0072711; P:cellular response to hydroxyurea; ISS:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; ISO:RGD.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0006336; P:DNA replication-independent nucleosome assembly; ISS:UniProtKB.
GO; GO:0030900; P:forebrain development; ISO:RGD.
GO; GO:0000212; P:meiotic spindle organization; ISO:RGD.
GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
GO; GO:1904908; P:negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric; ISO:RGD.
GO; GO:1901581; P:negative regulation of telomeric RNA transcription from RNA pol II promoter; ISS:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; ISS:UniProtKB.
GO; GO:0032206; P:positive regulation of telomere maintenance; ISS:UniProtKB.
GO; GO:1901582; P:positive regulation of telomeric RNA transcription from RNA pol II promoter; ISO:RGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0035128; P:post-embryonic forelimb morphogenesis; ISO:RGD.
GO; GO:0070198; P:protein localization to chromosome, telomeric region; ISO:RGD.
GO; GO:1900112; P:regulation of histone H3-K9 trimethylation; ISS:UniProtKB.
GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
GO; GO:0072520; P:seminiferous tubule development; ISO:RGD.
GO; GO:0060009; P:Sertoli cell development; ISO:RGD.
GO; GO:0007283; P:spermatogenesis; ISO:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
1: Evidence at protein level;
ATP-binding; Chromatin regulator; Chromosome; Citrullination;
Complete proteome; DNA damage; DNA repair; DNA-binding; Helicase;
Hydrolase; Isopeptide bond; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Telomere; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN <1 >527 Transcriptional regulator ATRX.
/FTId=PRO_0000074306.
REGION 290 427 Interaction with DAXX. {ECO:0000250}.
COMPBIAS 251 256 Poly-Ser.
COMPBIAS 304 307 Poly-Ser.
COMPBIAS 360 367 Poly-Asp.
MOD_RES 62 62 Phosphoserine.
{ECO:0000250|UniProtKB:P46100}.
MOD_RES 74 74 Phosphoserine.
{ECO:0000250|UniProtKB:P46100}.
MOD_RES 112 112 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 113 113 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 184 184 Citrulline. {ECO:0000250}.
MOD_RES 345 345 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 346 346 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 354 354 Phosphoserine.
{ECO:0000250|UniProtKB:Q61687}.
MOD_RES 423 423 Phosphoserine.
{ECO:0000250|UniProtKB:P46100}.
MOD_RES 425 425 Phosphoserine.
{ECO:0000250|UniProtKB:P46100}.
MOD_RES 427 427 Phosphoserine.
{ECO:0000250|UniProtKB:P46100}.
MOD_RES 449 449 Phosphoserine.
{ECO:0000250|UniProtKB:P46100}.
MOD_RES 453 453 Phosphoserine.
{ECO:0000250|UniProtKB:P46100}.
CROSSLNK 105 105 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P46100}.
NON_TER 1 1
NON_TER 527 527
SEQUENCE 527 AA; 59259 MW; ABEF4B10C086D638 CRC64;
GRSVVEFGDM VCKRQQSAVS SAGSEKPSGK EENVHSPEDK RVTKSKEKSK HLRTRTGRKV
KSDVTDRFRK KEQSSESSEG EKKQGRQRTG TRGKKSTDLK EEKVKREREY ESSSDGTEKL
PEGEEIGLFS KGVKQNKNDT TDEAKKGKKW KDKSCEKKEE LSDSVDRLPV KGESCDSSED
KKTRNRVSLR EKKQFSLPAK SSGKRPECSS SDTERSVKGE CCDSTDKRVK RIDLRERRSS
NSKRSTKEVK SGSSSSDAEG SSEDAKKQKK QRMSAKKKNS NTKERKRKSL RATTTKRKQA
DITSSSSDIG DDDQNSAGEE SSDEQKIKPV TENLVLPSHT GFCQSSGDEA FSKSVPATVD
DDDDDNDPEN RIAKKMLLEE IKANLSSDED GSSDDEPKEG EKKRIGKQSE ETPGDDGSNQ
VNSESDSDSE ESKKPRYRHR LLRHKLSLSD GESGGEKKTK PKEHKETKGR NRRKVSSEDS
EDTDFQESGV SEEVSESEDE QRPRTRSAKK AELEENQRSY KQKKKRR


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