ATRX
entrez
546
canonical
uniprot
P46100
canonical
ensembl
ENSG00000085224
resolver
ensp
ENSP00000362441
resolver
ensp
ENSP00000378967
resolver
ensp
ENSP00000753407
resolver
genesymbol
ATRX
resolver
genesymbol_syn
RAD54L
resolver
genesymbol_syn
XH2
resolver
hgnc
HGNC:886
resolver
uniprot
B4DLW1
resolver
uniprot
D3DTE2
resolver
uniprot
P51068
resolver
uniprot
Q15886
resolver
uniprot
Q59FB5
resolver
uniprot
Q59H31
resolver
uniprot
Q5H9A2
resolver
uniprot
Q5JWI4
resolver
uniprot
Q7Z2J1
resolver
uniprot
Q9H0Z1
resolver
uniprot
Q9NTS3
resolver
uniprot_entry
ATRX_HUMAN
resolver
uniprot_entry
B4DLW1_HUMAN
resolver
uniprot_sec
D3DTE2
resolver
uniprot_sec
P51068
resolver
uniprot_sec
Q15886
resolver
uniprot_sec
Q59FB5
resolver
uniprot_sec
Q59H31
resolver
uniprot_sec
Q5H9A2
resolver
uniprot_sec
Q5JWI4
resolver
uniprot_sec
Q7Z2J1
resolver
uniprot_sec
Q9H0Z1
resolver
uniprot_sec
Q9NTS3
resolver
amino_acid_sequence
MTAEPMSESKLNTLVQKLHDFLAHSSEESEETSSPPRLAMNQNTDKISGSGSNSDMMENSKEEGTSSSEKSKSSGSSRSKRKPSIVTKYVESDDEKPLDDETVNEDASNENSENDITMQSLPKGTVIVQPEPVLNEDKDDFKGPEFRSRSKMKTENLKKRGEDGLHGIVSCTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDFCHNAFCKKCILRNLGRKELSTIMDENNQWYCYICHPEPLLDLVTACNSVFENLEQLLQQNKKKIKVDSEKSNKVYEHTSRFSPKKTSSNCNGEEKKLDDSCSGSVTYSYSALIVPKEMIKKAKKLIETTANMNSSYVKFLKQATDNSEISSATKLRQLKAFKSVLADIKKAHLALEEDLNSEFRAMDAVNKEKNTKEHKVIDAKFETKARKGEKPCALEKKDISKSEAKLSRKQVDSEHMHQNVPTEEQRTNKSTGGEHKKSDRKEEPQYEPANTSEDLDMDIVSVPSSVPEDIFENLETAMEVQSSVDHQGDGSSGTEQEVESSSVKLNISSKDNRGGIKSKTTAKVTKELYVKLTPVSLSNSPIKGADCQEVPQDKDGYKSCGLNPKLEKCGLGQENSDNEHLVENEVSLLLEESDLRRSPRVKTTPLRRPTETNPVTSNSDEECNETVKEKQKLSVPVRKKDKRNSSDSAIDNPKPNKLPKSKQSETVDQNSDSDEMLAILKEVSRMSHSSSSDTDINEIHTNHKTLYDLKTQAGKDDKGKRKRKSSTSGSDFDTKKGKSAKSSIISKKKRQTQSESSNYDSELEKEIKSMSKIGAARTTKKRIPNTKDFDSSEDEKHSKKGMDNQGHKNLKTSQEGSSDDAERKQERETFSSAEGTVDKDTTIMELRDRLPKKQQASASTDGVDKLSGKEESFTSLEVRKVAETKEKSKHLKTKTCKKVQDGLSDIAEKFLKKDQSDETSEDDKKQSKKGTEEKKKPSDFKKKVIKMEQQYESSSDGTEKLPEREEICHFPKGIKQIKNGTTDGEKKSKKIRDKTSKKKDELSDYAEKSTGKGDSCDSSEDKKSKNGAYGREKKRCKLLGKSSRKRQDCSSSDTEKYSMKEDGCNSSDKRLKRIELRERRNLSSKRNTKEIQSGSSSSDAEESSEDNKKKKQRTSSKKKAVIVKEKKRNSLRTSTKRKQADITSSSSSDIEDDDQNSIGEGSSDEQKIKPVTENLVLSSHTGFCQSSGDEALSKSVPVTVDDDDDDNDPENRIAKKMLLEEIKANLSSDEDGSSDDEPEEGKKRTGKQNEENPGDEEAKNQVNSESDSDSEESKKPRYRHRLLRHKLTVSDGESGEEKKTKPKEHKEVKGRNRRKVSSEDSEDSDFQESGVSEEVSESEDEQRPRTRSAKKAELEENQRSYKQKKKRRRIKVQEDSSSENKSNSEEEEEEKEEEEEEEEEEEEEEEDENDDSKSPGKGRKKIRKILKDDKLRTETQNALKEEEERRKRIAEREREREKLREVIEIEDASPTKCPITTKLVLDEDEETKEPLVQVHRNMVIKLKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDFSTALVVCPLNTALNWMNEFEKWQEGLKDDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSRKLKEIFNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDVRVMKKRAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTSIQCKLYQYYLDHLTGVGNNSEGGRGKAGAKLFQDFQMLSRIWTHPWCLQLDYISKENKGYFDEDSMDEFIASDSDETSMSLSSDDYTKKKKKGKKGKKDSSSSGSGSDNDVEVIKVWNSRSRGGGEGNVDETGNNPSVSLKLEESKATSSSNPSSPAPDWYKDFVTDADAEVLEHSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLELASREKTEDKDKPLIYKGEGKWLRNIDYYRLDGSTTAQSRKKWAEEFNDETNVRGRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTKQSLSFRVVDQQQVERHFTMNELTELYTFEPDLLDDPNSEKKKKRDTPMLPKDTILAELLQIHKEHIVGYHEHDSLLDHKEEEELTEEERKAAWAEYEAEKKGLTMRFNIPTGTNLPPVSFNSQTPYIPFNLGALSAMSNQQLEDLINQGREKVVEATNSVTAVRIQPLEDIISAVWKENMNLSEAQVQALALSRQASQELDVKRREAIYNDVLTKQQMLISCVQRILMNRRLQQQYNQQQQQQMTYQQATLGHLMMPKPPNLIMNPSNYQQIDMRGMYQPVAGGMQPPPLQRAPPPMRSKNPGPSQGKSM
uniprot
proteins
disease_involvement
DISEASE: Alpha-thalassemia/impaired intellectual development syndrome, X-linked (ATRX) [MIM:301040]: A disorder characterized by severe psychomotor retardation, facial dysmorphism, urogenital abnormalities, and alpha-thalassemia. An essential phenotypic trait are hemoglobin H erythrocyte inclusions. {ECO:0000269|PubMed:10204841, ECO:0000269|PubMed:10417298, ECO:0000269|PubMed:10660327, ECO:0000269|PubMed:10995512, ECO:0000269|PubMed:12116232, ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:16955409, ECO:0000269|PubMed:21421568, ECO:0000269|PubMed:7697714, ECO:0000269|PubMed:8968741, ECO:0000269|PubMed:9043863, ECO:0000269|PubMed:9326931}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Intellectual disability-hypotonic facies syndrome, X-linked, 1 (MRXHF1) [MIM:309580]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXSHF1 features include severe intellectual disability, dysmorphic facies, and a highly skewed X-inactivation pattern in carrier women. Other more variable features include hypogonadism, deafness, renal anomalies, and mild skeletal defects. {ECO:0000269|PubMed:10398237, ECO:0000269|PubMed:10751095, ECO:0000269|PubMed:11050622, ECO:0000269|PubMed:15565397, ECO:0000269|PubMed:16222662, ECO:0000269|PubMed:8630485}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Alpha-thalassemia myelodysplasia syndrome (ATMDS) [MIM:300448]: A disorder characterized by hypochromic, microcytic red blood cells, hemoglobin H detected in peripheral blood, and multilineage myelodysplasia. {ECO:0000269|PubMed:12858175}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.4.-
uniprot
proteins
function
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 which probably implies recruitment of CBX5 to telomeres. Reports on the involvement in transcriptional regulation of telomeric repeat-containing RNA (TERRA) are conflicting; according to a report, it is not sufficient to decrease chromatin condensation at telomeres nor to increase expression of telomeric RNA in fibroblasts (PubMed:24500201). May be involved in telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines. Acts as a negative regulator of chromatin incorporation of transcriptionally repressive histone MACROH2A1, particularily at telomeres and the alpha-globin cluster in erythroleukemic cells. 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 CTCF within the H19 imprinting control region (ICR) and involved in establishment of histone tails modifications in the ICR. May be involved in brain development and facial morphogenesis. 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 (PubMed:27029610). {ECO:0000269|PubMed:12953102, ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:20504901, ECO:0000269|PubMed:20651253, ECO:0000269|PubMed:21029860, ECO:0000269|PubMed:22391447, ECO:0000269|PubMed:22829774, ECO:0000269|PubMed:24500201, ECO:0000269|PubMed:27029610}.
uniprot
proteins
mass_dalton
282587
uniprot
proteins
mutagenesis
MUTAGEN 189; /note="H->N: Impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci."; /evidence="ECO:0000269|PubMed:21666679"; MUTAGEN 203; /note="Y->A,K: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization."; /evidence="ECO:0000269|PubMed:21421568, ECO:0000269|PubMed:21666677, ECO:0000269|PubMed:21666679"; MUTAGEN 204; /note="Y->A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci."; /evidence="ECO:0000269|PubMed:21421568, ECO:0000269|PubMed:21666679"; MUTAGEN 207; /note="D->A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci."; MUTAGEN 209; /note="I->A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3)."; /evidence="ECO:0000269|PubMed:21421568"; MUTAGEN 214; /note="D->A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3)."; /evidence="ECO:0000269|PubMed:21421568"; MUTAGEN 217; /note="D->A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization."; /evidence="ECO:0000269|PubMed:21421568, ECO:0000269|PubMed:21666679"; MUTAGEN 218; /note="E->A: Impairs interaction with histone H3 peptides unmethylated at 'Lys-5' (H3K4me0); reduces pericentromeric localization."; /evidence="ECO:0000269|PubMed:21666677"; MUTAGEN 252; /note="E->L: Impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci."; /evidence="ECO:0000269|PubMed:21666679"; MUTAGEN 1600; /note="K->R: Abolishes ATPAse activity, no effect on pericentromeric heterochromatin localization."; /evidence="ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:21666679
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at serine residues during mitose. Phosphorylation may promote the release from the nuclear matrix and progression to mitosis. {ECO:0000269|PubMed:10699177}.
uniprot
proteins
protein_family
SNF2/RAD54 helicase family
uniprot
proteins
pubmed
10204841
uniprot
proteins
pubmed
10398237
uniprot
proteins
pubmed
10417298
uniprot
proteins
pubmed
10570185
uniprot
proteins
pubmed
10660327
uniprot
proteins
pubmed
10699177
uniprot
proteins
pubmed
10751095
uniprot
proteins
pubmed
10995512
uniprot
proteins
pubmed
11050622
uniprot
proteins
pubmed
12116232
uniprot
proteins
pubmed
12777533
uniprot
proteins
pubmed
12858175
uniprot
proteins
pubmed
12953102
uniprot
proteins
pubmed
14990586
uniprot
proteins
pubmed
15565397
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
15882967
uniprot
proteins
pubmed
16222662
uniprot
proteins
pubmed
16955409
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17296936
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17609377
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20211137
uniprot
proteins
pubmed
20504901
uniprot
proteins
pubmed
20651253
uniprot
proteins
pubmed
21029860
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21421568
uniprot
proteins
pubmed
21666677
uniprot
proteins
pubmed
21666679
uniprot
proteins
pubmed
22391447
uniprot
proteins
pubmed
22829774
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23222847
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24500201
uniprot
proteins
pubmed
24651726
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
27029610
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
7697714
uniprot
proteins
pubmed
7874112
uniprot
proteins
pubmed
8162050
uniprot
proteins
pubmed
8630485
uniprot
proteins
pubmed
8968741
uniprot
proteins
pubmed
9043863
uniprot
proteins
pubmed
9244431
uniprot
proteins
pubmed
9326931
uniprot
proteins
pubmed
9499421
uniprot
proteins
sequence_length
2492
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. Nucleus, PML body. 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. Colocalizes with cohesin (SMC1 and SMC3) and MECP2 at the maternal H19 ICR (By similarity). {ECO:0000250}.
uniprot
proteins