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Protein

Transcriptional regulator ATRX

Gene

ATRX

Organism
Homo sapiens (Human)
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 which probably implies recruitment of CBX5 to telomers. 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 telomers 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 negative regulator of chromatin incorporation of transcriptionally repressive histone H2AFY, 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 CTCTF within the H19 imprinting control region (ICR) and involved in esatblishment 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).9 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri170 – 206GATA-type; atypicalPROSITE-ProRule annotationAdd BLAST37
Zinc fingeri217 – 272PHD-type; atypicalPROSITE-ProRule annotationAdd BLAST56
Nucleotide bindingi1594 – 1601ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: UniProtKB
  • chromo shadow domain binding Source: BHF-UCL
  • DNA binding Source: UniProtKB-KW
  • DNA helicase activity Source: ProtInc
  • DNA translocase activity Source: UniProtKB
  • helicase activity Source: ProtInc
  • histone binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • methylated histone binding Source: UniProtKB

GO - Biological processi

  • cellular response to hydroxyurea Source: UniProtKB
  • chromatin modification Source: UniProtKB-KW
  • chromatin remodeling Source: UniProtKB
  • DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  • DNA methylation Source: ProtInc
  • DNA recombination Source: ProtInc
  • DNA repair Source: ProtInc
  • DNA replication-independent nucleosome assembly Source: UniProtKB
  • forebrain development Source: Ensembl
  • multicellular organism growth Source: Ensembl
  • negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric Source: BHF-UCL
  • negative regulation of telomeric RNA transcription from RNA pol II promoter Source: UniProtKB
  • nucleosome assembly Source: UniProtKB
  • positive regulation of nuclear cell cycle DNA replication Source: UniProtKB
  • positive regulation of telomere maintenance Source: UniProtKB
  • positive regulation of telomeric RNA transcription from RNA pol II promoter Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • post-embryonic forelimb morphogenesis Source: Ensembl
  • protein localization to chromosome, telomeric region Source: BHF-UCL
  • regulation of histone H3-K9 trimethylation Source: UniProtKB
  • regulation of transcription, DNA-templated Source: ProtInc
  • replication fork processing Source: UniProtKB
  • seminiferous tubule development Source: Ensembl
  • Sertoli cell development Source: Ensembl
  • spermatogenesis Source: Ensembl
  • 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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000085224-MONOMER.
SIGNORiP46100.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional regulator ATRX (EC:3.6.4.12)
Alternative name(s):
ATP-dependent helicase ATRX
X-linked helicase II
X-linked nuclear protein
Short name:
XNP
Znf-HX
Gene namesi
Name:ATRX
Synonyms:RAD54L, XH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:886. ATRX.

Subcellular locationi

  • Nucleus
  • Chromosometelomere
  • NucleusPML 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).By similarity

GO - Cellular componenti

  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear heterochromatin Source: ProtInc
  • nuclear subtelomeric heterochromatin Source: BHF-UCL
  • nucleus Source: HPA
  • pericentric heterochromatin Source: BHF-UCL
  • PML body Source: BHF-UCL
  • SWI/SNF superfamily-type complex Source: UniProtKB
  • telomeric heterochromatin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Involvement in diseasei

Alpha-thalassemia mental retardation syndrome, X-linked (ATRX)10 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by severe psychomotor retardation, facial dysmorphism, urogenital abnormalities, and alpha-thalassemia. An essential phenotypic trait are hemoglobin H erythrocyte inclusions.
See also OMIM:301040
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_012113175G → E in ATRX. 1 Publication1
Natural variantiVAR_012114178 – 198Missing in ATRX. 1 PublicationAdd BLAST21
Natural variantiVAR_012115179N → S in ATRX. 1 Publication1
Natural variantiVAR_001226190P → A in ATRX; impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci. 1 Publication1
Natural variantiVAR_012116190P → L in ATRX. 1 Publication1
Natural variantiVAR_012117190P → S in ATRX. 1 Publication1
Natural variantiVAR_001227192L → F in ATRX. 1
Natural variantiVAR_012118194V → I in ATRX. 1 Publication1
Natural variantiVAR_001228200C → S in ATRX. 1
Natural variantiVAR_012119219Q → P in ATRX; greatly impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 3 Publications1
Natural variantiVAR_001229220C → R in ATRX. 1
Natural variantiVAR_001230222W → S in ATRX. 1
Natural variantiVAR_001231243C → F in ATRX. 1
Natural variantiVAR_001232246R → C in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 4 Publications1
Natural variantiVAR_010914246R → L in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). 3 Publications1
Natural variantiVAR_012120249G → C in ATRX. 1 Publication1
Natural variantiVAR_001233249G → D in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization. 1 Publication1
Natural variantiVAR_0121211538V → G in ATRX; unknown pathological significance. 1
Natural variantiVAR_0121221552V → F in ATRX. 1 Publication1
Natural variantiVAR_0012341609H → R in ATRX. 1
Natural variantiVAR_0012351614C → R in ATRX. 1
Natural variantiVAR_0169161621T → M in ATRX. 1 Publication1
Natural variantiVAR_0121231645L → S in ATRX. 1 Publication1
Natural variantiVAR_0012361650K → N in ATRX. 1
Natural variantiVAR_0121241713P → S in ATRX; without alpha-thalassemia. 1 Publication1
Natural variantiVAR_0121251742R → K in ATRX; atypical; patients presents spastic paraplegia at birth. 1 Publication1
Natural variantiVAR_0121261847Y → C in ATRX. 1 Publication1
Natural variantiVAR_0012382035D → V in ATRX; impairs ATPase activity. 1 Publication1
Natural variantiVAR_0012392084Y → H in ATRX; impairs ATPase activity. 1 Publication1
Natural variantiVAR_0012412163Y → C in ATRX. 1
Mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXSHF1 is a syndromic mental retardation. Clinical features include severe mental retardation, 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.
See also OMIM:309580
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_032625220C → Y in MRXSHF1. 1 Publication1
Natural variantiVAR_032626409L → S in MRXSHF1. 1 Publication1
Natural variantiVAR_0121272050I → T in MRXSHF1; originally reported as Carpenter-Waziri syndrome. 1 Publication1
Natural variantiVAR_0012402131R → Q in MRXSHF1; originally reported as Juberg-Marsidi syndrome. 1 Publication1
Natural variantiVAR_0326272271R → G in MRXSHF1. 1 Publication1
Alpha-thalassemia myelodysplasia syndrome (ATMDS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by hypochromic, microcytic red blood cells, hemoglobin H detected in peripheral blood, and multilineage myelodysplasia.
See also OMIM:300448

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi189H → N: Impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci. 1 Publication1
Mutagenesisi203Y → A or K: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization. 3 Publications1
Mutagenesisi204Y → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 2 Publications1
Mutagenesisi207D → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 1
Mutagenesisi209I → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). 1 Publication1
Mutagenesisi214D → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). 1 Publication1
Mutagenesisi217D → A: Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization. 2 Publications1
Mutagenesisi218E → A: Impairs interaction with histone H3 peptides unmethylated at 'Lys-5' (H3K4me0); reduces pericentromeric localization. 1 Publication1
Mutagenesisi252E → L: Impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci. 1 Publication1
Mutagenesisi1600K → R: Abolishes ATPAse activity, no effect on pericentromeric heterochromatin localization. 2 Publications1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi546.
MalaCardsiATRX.
MIMi300448. phenotype.
301040. phenotype.
309580. phenotype.
Orphaneti231401. Alpha-thalassemia - myelodysplastic syndrome.
847. Alpha-thalassemia - X-linked intellectual disability syndrome.
93973. Carpenter-Waziri syndrome.
93971. Chudley-Lowry-Hoar syndrome.
93970. Holmes-Gang syndrome.
93972. Juberg-Marsidi syndrome.
93974. Smith-Fineman-Myers syndrome.
PharmGKBiPA25179.

Polymorphism and mutation databases

DMDMi311033500.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000743011 – 2492Transcriptional regulator ATRXAdd BLAST2492

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei25PhosphoserineCombined sources1
Modified residuei34PhosphoserineCombined sources1
Modified residuei89PhosphotyrosineCombined sources1
Modified residuei92PhosphoserineCombined sources1
Modified residuei112PhosphoserineCombined sources1
Modified residuei213PhosphoserineBy similarity1
Cross-linki299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei316PhosphoserineCombined sources1
Cross-linki438Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei591PhosphothreonineCombined sources1
Modified residuei594PhosphoserineCombined sources1
Modified residuei598PhosphoserineCombined sources1
Cross-linki623Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki623Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei634PhosphoserineCombined sources1
Modified residuei674PhosphothreonineCombined sources1
Modified residuei675PhosphoserineCombined sources1
Modified residuei677PhosphoserineCombined sources1
Modified residuei729PhosphoserineCombined sources1
Modified residuei731PhosphoserineCombined sources1
Modified residuei784PhosphoserineBy similarity1
Modified residuei819PhosphoserineCombined sources1
Modified residuei849PhosphoserineCombined sources1
Modified residuei850PhosphoserineCombined sources1
Modified residuei875PhosphoserineCombined sources1
Modified residuei876PhosphoserineCombined sources1
Modified residuei889PhosphoserineCombined sources1
Modified residuei962PhosphoserineCombined sources1
Modified residuei967N6-acetyllysineCombined sources1
Modified residuei974PhosphoserineCombined sources1
Modified residuei977PhosphothreonineCombined sources1
Cross-linki1004Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1011PhosphoserineBy similarity1
Modified residuei1012PhosphoserineBy similarity1
Modified residuei1013PhosphoserineBy similarity1
Modified residuei1061PhosphoserineCombined sources1
Modified residuei1063PhosphotyrosineCombined sources1
Modified residuei1244PhosphoserineBy similarity1
Modified residuei1245PhosphoserineBy similarity1
Modified residuei1253PhosphoserineBy similarity1
Modified residuei1322PhosphoserineCombined sources1
Modified residuei1324PhosphoserineCombined sources1
Modified residuei1326PhosphoserineCombined sources1
Modified residuei1348PhosphoserineCombined sources1
Modified residuei1352PhosphoserineCombined sources1
Cross-linki1488Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1527PhosphoserineCombined sources1
Modified residuei1529PhosphothreonineCombined sources1
Modified residuei1906PhosphoserineBy similarity1
Modified residuei1913PhosphoserineBy similarity1
Cross-linki1982Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki1982Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1992PhosphoserineCombined sources1
Modified residuei1996PhosphoserineCombined sources1
Modified residuei2220PhosphoserineCombined sources1
Modified residuei2474Omega-N-methylarginineBy similarity1
Modified residuei2480Omega-N-methylarginineBy similarity1

Post-translational modificationi

Phosphorylated at serine residues during mitose. Phosphorylation may promote the release from the nuclear matrix and progression to mitosis.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP46100.
MaxQBiP46100.
PaxDbiP46100.
PeptideAtlasiP46100.
PRIDEiP46100.

PTM databases

iPTMnetiP46100.
PhosphoSitePlusiP46100.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000085224.
CleanExiHS_RAD54L.
ExpressionAtlasiP46100. baseline and differential.
GenevisibleiP46100. HS.

Organism-specific databases

HPAiCAB009372.
CAB068176.
HPA001906.
HPA064684.

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. Interacts with SETDB1, TRIM28 and ZNF274 (PubMed:27029610).12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBX5P459732EBI-396461,EBI-78219
DAXXQ9UER77EBI-396461,EBI-77321
EZH2Q159102EBI-396461,EBI-530054
H2AFYO75367-22EBI-396461,EBI-6249599
Mecp2Q005666EBI-396461,EBI-9396907From a different organism.
RAD50Q928785EBI-396461,EBI-495494

GO - Molecular functioni

  • chromo shadow domain binding Source: BHF-UCL
  • histone binding Source: UniProtKB
  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107028. 59 interactors.
DIPiDIP-31532N.
IntActiP46100. 31 interactors.
MINTiMINT-1186201.
STRINGi9606.ENSP00000362441.

Structurei

Secondary structure

12492
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni172 – 174Combined sources3
Beta strandi176 – 178Combined sources3
Turni179 – 181Combined sources3
Turni183 – 185Combined sources3
Beta strandi186 – 188Combined sources3
Turni190 – 192Combined sources3
Beta strandi195 – 197Combined sources3
Helixi198 – 206Combined sources9
Beta strandi210 – 212Combined sources3
Turni213 – 215Combined sources3
Beta strandi217 – 219Combined sources3
Turni221 – 223Combined sources3
Beta strandi227 – 231Combined sources5
Beta strandi233 – 236Combined sources4
Beta strandi238 – 240Combined sources3
Helixi241 – 247Combined sources7
Helixi250 – 256Combined sources7
Beta strandi258 – 261Combined sources4
Turni266 – 268Combined sources3
Helixi271 – 273Combined sources3
Helixi274 – 284Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JM1NMR-A159-296[»]
2LBMNMR-A163-296[»]
2LD1NMR-A163-296[»]
3QL9X-ray0.93A167-289[»]
3QLAX-ray1.60A/D167-289[»]
3QLCX-ray2.50A/B167-289[»]
3QLNX-ray1.90A/B167-289[»]
4W5AX-ray2.60A/B/E167-289[»]
ProteinModelPortaliP46100.
SMRiP46100.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46100.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini159 – 296ADDPROSITE-ProRule annotationAdd BLAST138
Domaini1581 – 1768Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST188
Domaini2025 – 2205Helicase C-terminalPROSITE-ProRule annotationAdd BLAST181

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1189 – 1326Interaction with DAXXAdd BLAST138
Regioni2010 – 2280Interaction with MECP21 PublicationAdd BLAST271

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi581 – 594PxVxL motifAdd BLAST14
Motifi1719 – 1722DEGH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi745 – 750Poly-Ser6
Compositional biasi1151 – 1156Poly-Ser6
Compositional biasi1166 – 1169Poly-Lys4
Compositional biasi1202 – 1206Poly-Ser5
Compositional biasi1259 – 1266Poly-Asp8
Compositional biasi1443 – 1466Poly-GluAdd BLAST24
Compositional biasi1499 – 1502Poly-Glu4
Compositional biasi1929 – 1939Poly-LysAdd BLAST11
Compositional biasi1941 – 1948Poly-Ser8
Compositional biasi2222 – 2225Poly-Lys4
Compositional biasi2262 – 2265Poly-Glu4
Compositional biasi2420 – 2425Poly-Gln6

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.1 Publication
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.1 Publication

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)DescriptionActionsGraphical viewLength
Zinc fingeri170 – 206GATA-type; atypicalPROSITE-ProRule annotationAdd BLAST37
Zinc fingeri217 – 272PHD-type; atypicalPROSITE-ProRule annotationAdd BLAST56

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1015. Eukaryota.
COG0553. LUCA.
HOVERGENiHBG000104.
InParanoidiP46100.
KOiK10779.
OrthoDBiEOG091G01G9.
PhylomeDBiP46100.
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.
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.
[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]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 4 (identifier: P46100-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTAEPMSESK LNTLVQKLHD FLAHSSEESE ETSSPPRLAM NQNTDKISGS
60 70 80 90 100
GSNSDMMENS KEEGTSSSEK SKSSGSSRSK RKPSIVTKYV ESDDEKPLDD
110 120 130 140 150
ETVNEDASNE NSENDITMQS LPKGTVIVQP EPVLNEDKDD FKGPEFRSRS
160 170 180 190 200
KMKTENLKKR GEDGLHGIVS CTACGQQVNH FQKDSIYRHP SLQVLICKNC
210 220 230 240 250
FKYYMSDDIS RDSDGMDEQC RWCAEGGNLI CCDFCHNAFC KKCILRNLGR
260 270 280 290 300
KELSTIMDEN NQWYCYICHP EPLLDLVTAC NSVFENLEQL LQQNKKKIKV
310 320 330 340 350
DSEKSNKVYE HTSRFSPKKT SSNCNGEEKK LDDSCSGSVT YSYSALIVPK
360 370 380 390 400
EMIKKAKKLI ETTANMNSSY VKFLKQATDN SEISSATKLR QLKAFKSVLA
410 420 430 440 450
DIKKAHLALE EDLNSEFRAM DAVNKEKNTK EHKVIDAKFE TKARKGEKPC
460 470 480 490 500
ALEKKDISKS EAKLSRKQVD SEHMHQNVPT EEQRTNKSTG GEHKKSDRKE
510 520 530 540 550
EPQYEPANTS EDLDMDIVSV PSSVPEDIFE NLETAMEVQS SVDHQGDGSS
560 570 580 590 600
GTEQEVESSS VKLNISSKDN RGGIKSKTTA KVTKELYVKL TPVSLSNSPI
610 620 630 640 650
KGADCQEVPQ DKDGYKSCGL NPKLEKCGLG QENSDNEHLV ENEVSLLLEE
660 670 680 690 700
SDLRRSPRVK TTPLRRPTET NPVTSNSDEE CNETVKEKQK LSVPVRKKDK
710 720 730 740 750
RNSSDSAIDN PKPNKLPKSK QSETVDQNSD SDEMLAILKE VSRMSHSSSS
760 770 780 790 800
DTDINEIHTN HKTLYDLKTQ AGKDDKGKRK RKSSTSGSDF DTKKGKSAKS
810 820 830 840 850
SIISKKKRQT QSESSNYDSE LEKEIKSMSK IGAARTTKKR IPNTKDFDSS
860 870 880 890 900
EDEKHSKKGM DNQGHKNLKT SQEGSSDDAE RKQERETFSS AEGTVDKDTT
910 920 930 940 950
IMELRDRLPK KQQASASTDG VDKLSGKEQS FTSLEVRKVA ETKEKSKHLK
960 970 980 990 1000
TKTCKKVQDG LSDIAEKFLK KDQSDETSED DKKQSKKGTE EKKKPSDFKK
1010 1020 1030 1040 1050
KVIKMEQQYE SSSDGTEKLP EREEICHFPK GIKQIKNGTT DGEKKSKKIR
1060 1070 1080 1090 1100
DKTSKKKDEL SDYAEKSTGK GDSCDSSEDK KSKNGAYGRE KKRCKLLGKS
1110 1120 1130 1140 1150
SRKRQDCSSS DTEKYSMKED GCNSSDKRLK RIELRERRNL SSKRNTKEIQ
1160 1170 1180 1190 1200
SGSSSSDAEE SSEDNKKKKQ RTSSKKKAVI VKEKKRNSLR TSTKRKQADI
1210 1220 1230 1240 1250
TSSSSSDIED DDQNSIGEGS SDEQKIKPVT ENLVLSSHTG FCQSSGDEAL
1260 1270 1280 1290 1300
SKSVPVTVDD DDDDNDPENR IAKKMLLEEI KANLSSDEDG SSDDEPEEGK
1310 1320 1330 1340 1350
KRTGKQNEEN PGDEEAKNQV NSESDSDSEE SKKPRYRHRL LRHKLTVSDG
1360 1370 1380 1390 1400
ESGEEKKTKP KEHKEVKGRN RRKVSSEDSE DSDFQESGVS EEVSESEDEQ
1410 1420 1430 1440 1450
RPRTRSAKKA ELEENQRSYK QKKKRRRIKV QEDSSSENKS NSEEEEEEKE
1460 1470 1480 1490 1500
EEEEEEEEEE EEEEDENDDS KSPGKGRKKI RKILKDDKLR TETQNALKEE
1510 1520 1530 1540 1550
EERRKRIAER EREREKLREV IEIEDASPTK CPITTKLVLD EDEETKEPLV
1560 1570 1580 1590 1600
QVHRNMVIKL KPHQVDGVQF MWDCCCESVK KTKKSPGSGC ILAHCMGLGK
1610 1620 1630 1640 1650
TLQVVSFLHT VLLCDKLDFS TALVVCPLNT ALNWMNEFEK WQEGLKDDEK
1660 1670 1680 1690 1700
LEVSELATVK RPQERSYMLQ RWQEDGGVMI IGYEMYRNLA QGRNVKSRKL
1710 1720 1730 1740 1750
KEIFNKALVD PGPDFVVCDE GHILKNEASA VSKAMNSIRS RRRIILTGTP
1760 1770 1780 1790 1800
LQNNLIEYHC MVNFIKENLL GSIKEFRNRF INPIQNGQCA DSTMVDVRVM
1810 1820 1830 1840 1850
KKRAHILYEM LAGCVQRKDY TALTKFLPPK HEYVLAVRMT SIQCKLYQYY
1860 1870 1880 1890 1900
LDHLTGVGNN SEGGRGKAGA KLFQDFQMLS RIWTHPWCLQ LDYISKENKG
1910 1920 1930 1940 1950
YFDEDSMDEF IASDSDETSM SLSSDDYTKK KKKGKKGKKD SSSSGSGSDN
1960 1970 1980 1990 2000
DVEVIKVWNS RSRGGGEGNV DETGNNPSVS LKLEESKATS SSNPSSPAPD
2010 2020 2030 2040 2050
WYKDFVTDAD AEVLEHSGKM VLLFEILRMA EEIGDKVLVF SQSLISLDLI
2060 2070 2080 2090 2100
EDFLELASRE KTEDKDKPLI YKGEGKWLRN IDYYRLDGST TAQSRKKWAE
2110 2120 2130 2140 2150
EFNDETNVRG RLFIISTKAG SLGINLVAAN RVIIFDASWN PSYDIQSIFR
2160 2170 2180 2190 2200
VYRFGQTKPV YVYRFLAQGT MEDKIYDRQV TKQSLSFRVV DQQQVERHFT
2210 2220 2230 2240 2250
MNELTELYTF EPDLLDDPNS EKKKKRDTPM LPKDTILAEL LQIHKEHIVG
2260 2270 2280 2290 2300
YHEHDSLLDH KEEEELTEEE RKAAWAEYEA EKKGLTMRFN IPTGTNLPPV
2310 2320 2330 2340 2350
SFNSQTPYIP FNLGALSAMS NQQLEDLINQ GREKVVEATN SVTAVRIQPL
2360 2370 2380 2390 2400
EDIISAVWKE NMNLSEAQVQ ALALSRQASQ ELDVKRREAI YNDVLTKQQM
2410 2420 2430 2440 2450
LISCVQRILM NRRLQQQYNQ QQQQQMTYQQ ATLGHLMMPK PPNLIMNPSN
2460 2470 2480 2490
YQQIDMRGMY QPVAGGMQPP PLQRAPPPMR SKNPGPSQGK SM
Length:2,492
Mass (Da):282,586
Last modified:November 2, 2010 - v5
Checksum:i637E341F6A4B29C6
GO
Isoform 1 (identifier: P46100-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-204: Missing.

Show »
Length:2,288
Mass (Da):259,843
Checksum:iAB2B948725F62D77
GO
Isoform 2 (identifier: P46100-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-117: Missing.

Show »
Length:2,375
Mass (Da):269,811
Checksum:i7314428AA21A9687
GO
Isoform 3 (identifier: P46100-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     124-161: Missing.

Show »
Length:2,454
Mass (Da):278,229
Checksum:iED9320A642E01E2A
GO
Isoform 5 (identifier: P46100-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-117: Missing.
     124-161: Missing.

Show »
Length:2,337
Mass (Da):265,454
Checksum:i437268E2C2817FEA
GO
Isoform 6 (identifier: P46100-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     124-162: Missing.
     573-601: Missing.
     1419-2492: Missing.

Note: No experimental confirmation available.
Show »
Length:1,350
Mass (Da):151,556
Checksum:iA67E6A155955371A
GO

Sequence cautioni

The sequence AAA20872 differs from that shown. Many frameshifts and conflits.Curated
The sequence AAC50069 differs from that shown. Reason: Frameshift at several positions.Curated
The sequence BAD92165 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti879A → R in AAC50069 (PubMed:7874112).Curated1
Sequence conflicti1286S → P in BAD92165 (Ref. 4) Curated1
Sequence conflicti1627P → L in AAC50069 (PubMed:7874112).Curated1
Sequence conflicti1632L → F in AAC50069 (PubMed:7874112).Curated1
Sequence conflicti2280A → G in AAC50069 (PubMed:7874112).Curated1
Sequence conflicti2283 – 2284KG → RV in AAC50069 (PubMed:7874112).Curated2
Sequence conflicti2436L → H in AAC50069 (PubMed:7874112).Curated1
Sequence conflicti2442P → R in AAC50069 (PubMed:7874112).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_012113175G → E in ATRX. 1 Publication1
Natural variantiVAR_012114178 – 198Missing in ATRX. 1 PublicationAdd BLAST21
Natural variantiVAR_012115179N → S in ATRX. 1 Publication1
Natural variantiVAR_001226190P → A in ATRX; impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci. 1 Publication1
Natural variantiVAR_012116190P → L in ATRX. 1 Publication1
Natural variantiVAR_012117190P → S in ATRX. 1 Publication1
Natural variantiVAR_001227192L → F in ATRX. 1
Natural variantiVAR_012118194V → I in ATRX. 1 Publication1
Natural variantiVAR_001228200C → S in ATRX. 1
Natural variantiVAR_012119219Q → P in ATRX; greatly impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 3 Publications1
Natural variantiVAR_001229220C → R in ATRX. 1
Natural variantiVAR_032625220C → Y in MRXSHF1. 1 Publication1
Natural variantiVAR_001230222W → S in ATRX. 1
Natural variantiVAR_001231243C → F in ATRX. 1
Natural variantiVAR_001232246R → C in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci. 4 Publications1
Natural variantiVAR_010914246R → L in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3). 3 Publications1
Natural variantiVAR_012120249G → C in ATRX. 1 Publication1
Natural variantiVAR_001233249G → D in ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization. 1 Publication1
Natural variantiVAR_032626409L → S in MRXSHF1. 1 Publication1
Natural variantiVAR_055939545Q → E.Corresponds to variant rs35738915dbSNPEnsembl.1
Natural variantiVAR_016914596S → P.1 PublicationCorresponds to variant rs1051678dbSNPEnsembl.1
Natural variantiVAR_016915740E → G.1 PublicationCorresponds to variant rs1051680dbSNPEnsembl.1
Natural variantiVAR_023438929Q → E.1 PublicationCorresponds to variant rs3088074dbSNPEnsembl.1
Natural variantiVAR_0121211538V → G in ATRX; unknown pathological significance. 1
Natural variantiVAR_0121221552V → F in ATRX. 1 Publication1
Natural variantiVAR_0012341609H → R in ATRX. 1
Natural variantiVAR_0012351614C → R in ATRX. 1
Natural variantiVAR_0169161621T → M in ATRX. 1 Publication1
Natural variantiVAR_0121231645L → S in ATRX. 1 Publication1
Natural variantiVAR_0012361650K → N in ATRX. 1
Natural variantiVAR_0121241713P → S in ATRX; without alpha-thalassemia. 1 Publication1
Natural variantiVAR_0121251742R → K in ATRX; atypical; patients presents spastic paraplegia at birth. 1 Publication1
Natural variantiVAR_0121261847Y → C in ATRX. 1 Publication1
Natural variantiVAR_0012371860N → S Rare polymorphism. 1 PublicationCorresponds to variant rs45439799dbSNPEnsembl.1
Natural variantiVAR_0012382035D → V in ATRX; impairs ATPase activity. 1 Publication1
Natural variantiVAR_0121272050I → T in MRXSHF1; originally reported as Carpenter-Waziri syndrome. 1 Publication1
Natural variantiVAR_0012392084Y → H in ATRX; impairs ATPase activity. 1 Publication1
Natural variantiVAR_0012402131R → Q in MRXSHF1; originally reported as Juberg-Marsidi syndrome. 1 Publication1
Natural variantiVAR_0012412163Y → C in ATRX. 1
Natural variantiVAR_0326272271R → G in MRXSHF1. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0005751 – 204Missing in isoform 1. 1 PublicationAdd BLAST204
Alternative sequenceiVSP_0005741 – 117Missing in isoform 2 and isoform 5. 2 PublicationsAdd BLAST117
Alternative sequenceiVSP_015499124 – 162Missing in isoform 6. 1 PublicationAdd BLAST39
Alternative sequenceiVSP_000576124 – 161Missing in isoform 3 and isoform 5. 1 PublicationAdd BLAST38
Alternative sequenceiVSP_015500573 – 601Missing in isoform 6. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_0155011419 – 2492Missing in isoform 6. 1 PublicationAdd BLAST1074

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72937 mRNA. Translation: AAB49970.2.
U72938 mRNA. Translation: AAB49971.2.
U72935
, U72904, U72905, U72907, U72908, U72909, U72910, U72911, U72912, U72913, U72914, U72915, U72916, U72917, U72918, U72919, U72920, U72921, U72922, U72923, U72924, U72925, U72926, U72927, U72928, U72929, U72930, U72931, U72932, U72933, U72934 Genomic DNA. Translation: AAB40698.1.
U72935
, U72904, U72907, U72908, U72909, U72910, U72911, U72912, U72913, U72914, U72915, U72916, U72918, U72919, U72920, U72921, U72922, U72923, U72924, U72925, U72926, U72927, U72928, U72929, U72930, U72931, U72932, U72933, U72934 Genomic DNA. Translation: AAB40699.1.
U72936 mRNA. Translation: AAB49969.1.
U72935
, U72908, U72909, U72910, U72911, U72912, U72913, U72914, U72915, U72916, U72917, U72918, U72920, U72921, U72922, U72923, U72924, U72925, U72926, U72927, U72928, U72929, U72930, U72931, U72932, U72933, U72934 Genomic DNA. Translation: AAB40700.1.
U75653 Genomic DNA. Translation: AAC51655.1.
U97103
, AF000157, AF000158, AF000159, AF000160, U97080, U97081, U97082, U97083, U97084, U97085, U97086, U97087, U97088, U97089, U97090, U97091, U97092, U97093, U97094, U97095, U97096, U97097, U97098, U97099, U97100, U97101, U97102 Genomic DNA. Translation: AAC51657.1.
AB102641 mRNA. Translation: BAC81110.1.
AB101681 Genomic DNA. Translation: BAC80270.1.
AB101682 Genomic DNA. Translation: BAC80271.1.
AB101683 Genomic DNA. Translation: BAC80272.1.
AB101685 Genomic DNA. Translation: BAC80274.1.
AB101687 Genomic DNA. Translation: BAC80276.1.
AB101689 Genomic DNA. Translation: BAC80278.1.
AB101691 Genomic DNA. Translation: BAC80280.1.
AB101693 Genomic DNA. Translation: BAC80282.1.
AB101695 Genomic DNA. Translation: BAC80284.1.
AB101700 Genomic DNA. Translation: BAC80289.1.
AB101699 Genomic DNA. Translation: BAC80288.1.
AB101698 Genomic DNA. Translation: BAC80287.1.
AB101697 Genomic DNA. Translation: BAC80286.1.
AB101696 Genomic DNA. Translation: BAC80285.1.
AB101694 Genomic DNA. Translation: BAC80283.1.
AB101692 Genomic DNA. Translation: BAC80281.1.
AB101690 Genomic DNA. Translation: BAC80279.1.
AB101688 Genomic DNA. Translation: BAC80277.1.
AB101686 Genomic DNA. Translation: BAC80275.1.
AB101684 Genomic DNA. Translation: BAC80273.1.
AB208928 mRNA. Translation: BAD92165.1. Different initiation.
AB209545 mRNA. Translation: BAD92782.1.
AL121874 Genomic DNA. Translation: CAB90351.2.
AL121874, AL109753, Z84487 Genomic DNA. Translation: CAI40710.1.
Z84487, AL109753, AL121874 Genomic DNA. Translation: CAI42674.1.
Z84487, AL109753, AL121874 Genomic DNA. Translation: CAI42675.1.
AL109753, AL121874, Z84487 Genomic DNA. Translation: CAI43115.1.
AL109753, AL121874, Z84487 Genomic DNA. Translation: CAI43116.1.
CH471104 Genomic DNA. Translation: EAW98611.1.
CH471104 Genomic DNA. Translation: EAW98615.1.
U09820 mRNA. Translation: AAC50069.1. Frameshift.
L34363 Genomic DNA. Translation: AAA20872.1. Sequence problems.
X83753 Genomic DNA. Translation: CAA58711.1.
CCDSiCCDS14434.1. [P46100-1]
CCDS14435.1. [P46100-4]
PIRiI38614.
I54367.
RefSeqiNP_000480.3. NM_000489.4.
NP_612114.2. NM_138270.3.
UniGeneiHs.533526.
Hs.653797.

Genome annotation databases

EnsembliENST00000373344; ENSP00000362441; ENSG00000085224.
ENST00000395603; ENSP00000378967; ENSG00000085224.
GeneIDi546.
KEGGihsa:546.
UCSCiuc004ecp.5. human. [P46100-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72937 mRNA. Translation: AAB49970.2.
U72938 mRNA. Translation: AAB49971.2.
U72935
, U72904, U72905, U72907, U72908, U72909, U72910, U72911, U72912, U72913, U72914, U72915, U72916, U72917, U72918, U72919, U72920, U72921, U72922, U72923, U72924, U72925, U72926, U72927, U72928, U72929, U72930, U72931, U72932, U72933, U72934 Genomic DNA. Translation: AAB40698.1.
U72935
, U72904, U72907, U72908, U72909, U72910, U72911, U72912, U72913, U72914, U72915, U72916, U72918, U72919, U72920, U72921, U72922, U72923, U72924, U72925, U72926, U72927, U72928, U72929, U72930, U72931, U72932, U72933, U72934 Genomic DNA. Translation: AAB40699.1.
U72936 mRNA. Translation: AAB49969.1.
U72935
, U72908, U72909, U72910, U72911, U72912, U72913, U72914, U72915, U72916, U72917, U72918, U72920, U72921, U72922, U72923, U72924, U72925, U72926, U72927, U72928, U72929, U72930, U72931, U72932, U72933, U72934 Genomic DNA. Translation: AAB40700.1.
U75653 Genomic DNA. Translation: AAC51655.1.
U97103
, AF000157, AF000158, AF000159, AF000160, U97080, U97081, U97082, U97083, U97084, U97085, U97086, U97087, U97088, U97089, U97090, U97091, U97092, U97093, U97094, U97095, U97096, U97097, U97098, U97099, U97100, U97101, U97102 Genomic DNA. Translation: AAC51657.1.
AB102641 mRNA. Translation: BAC81110.1.
AB101681 Genomic DNA. Translation: BAC80270.1.
AB101682 Genomic DNA. Translation: BAC80271.1.
AB101683 Genomic DNA. Translation: BAC80272.1.
AB101685 Genomic DNA. Translation: BAC80274.1.
AB101687 Genomic DNA. Translation: BAC80276.1.
AB101689 Genomic DNA. Translation: BAC80278.1.
AB101691 Genomic DNA. Translation: BAC80280.1.
AB101693 Genomic DNA. Translation: BAC80282.1.
AB101695 Genomic DNA. Translation: BAC80284.1.
AB101700 Genomic DNA. Translation: BAC80289.1.
AB101699 Genomic DNA. Translation: BAC80288.1.
AB101698 Genomic DNA. Translation: BAC80287.1.
AB101697 Genomic DNA. Translation: BAC80286.1.
AB101696 Genomic DNA. Translation: BAC80285.1.
AB101694 Genomic DNA. Translation: BAC80283.1.
AB101692 Genomic DNA. Translation: BAC80281.1.
AB101690 Genomic DNA. Translation: BAC80279.1.
AB101688 Genomic DNA. Translation: BAC80277.1.
AB101686 Genomic DNA. Translation: BAC80275.1.
AB101684 Genomic DNA. Translation: BAC80273.1.
AB208928 mRNA. Translation: BAD92165.1. Different initiation.
AB209545 mRNA. Translation: BAD92782.1.
AL121874 Genomic DNA. Translation: CAB90351.2.
AL121874, AL109753, Z84487 Genomic DNA. Translation: CAI40710.1.
Z84487, AL109753, AL121874 Genomic DNA. Translation: CAI42674.1.
Z84487, AL109753, AL121874 Genomic DNA. Translation: CAI42675.1.
AL109753, AL121874, Z84487 Genomic DNA. Translation: CAI43115.1.
AL109753, AL121874, Z84487 Genomic DNA. Translation: CAI43116.1.
CH471104 Genomic DNA. Translation: EAW98611.1.
CH471104 Genomic DNA. Translation: EAW98615.1.
U09820 mRNA. Translation: AAC50069.1. Frameshift.
L34363 Genomic DNA. Translation: AAA20872.1. Sequence problems.
X83753 Genomic DNA. Translation: CAA58711.1.
CCDSiCCDS14434.1. [P46100-1]
CCDS14435.1. [P46100-4]
PIRiI38614.
I54367.
RefSeqiNP_000480.3. NM_000489.4.
NP_612114.2. NM_138270.3.
UniGeneiHs.533526.
Hs.653797.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JM1NMR-A159-296[»]
2LBMNMR-A163-296[»]
2LD1NMR-A163-296[»]
3QL9X-ray0.93A167-289[»]
3QLAX-ray1.60A/D167-289[»]
3QLCX-ray2.50A/B167-289[»]
3QLNX-ray1.90A/B167-289[»]
4W5AX-ray2.60A/B/E167-289[»]
ProteinModelPortaliP46100.
SMRiP46100.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107028. 59 interactors.
DIPiDIP-31532N.
IntActiP46100. 31 interactors.
MINTiMINT-1186201.
STRINGi9606.ENSP00000362441.

PTM databases

iPTMnetiP46100.
PhosphoSitePlusiP46100.

Polymorphism and mutation databases

DMDMi311033500.

Proteomic databases

EPDiP46100.
MaxQBiP46100.
PaxDbiP46100.
PeptideAtlasiP46100.
PRIDEiP46100.

Protocols and materials databases

DNASUi546.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373344; ENSP00000362441; ENSG00000085224.
ENST00000395603; ENSP00000378967; ENSG00000085224.
GeneIDi546.
KEGGihsa:546.
UCSCiuc004ecp.5. human. [P46100-1]

Organism-specific databases

CTDi546.
DisGeNETi546.
GeneCardsiATRX.
GeneReviewsiATRX.
H-InvDBHIX0176765.
HGNCiHGNC:886. ATRX.
HPAiCAB009372.
CAB068176.
HPA001906.
HPA064684.
MalaCardsiATRX.
MIMi300032. gene.
300448. phenotype.
301040. phenotype.
309580. phenotype.
neXtProtiNX_P46100.
Orphaneti231401. Alpha-thalassemia - myelodysplastic syndrome.
847. Alpha-thalassemia - X-linked intellectual disability syndrome.
93973. Carpenter-Waziri syndrome.
93971. Chudley-Lowry-Hoar syndrome.
93970. Holmes-Gang syndrome.
93972. Juberg-Marsidi syndrome.
93974. Smith-Fineman-Myers syndrome.
PharmGKBiPA25179.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1015. Eukaryota.
COG0553. LUCA.
HOVERGENiHBG000104.
InParanoidiP46100.
KOiK10779.
OrthoDBiEOG091G01G9.
PhylomeDBiP46100.
TreeFamiTF313172.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000085224-MONOMER.
SIGNORiP46100.

Miscellaneous databases

EvolutionaryTraceiP46100.
GeneWikiiATRX.
GenomeRNAii546.
PROiP46100.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000085224.
CleanExiHS_RAD54L.
ExpressionAtlasiP46100. baseline and differential.
GenevisibleiP46100. HS.

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.
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.
[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]
ProtoNetiSearch...

Entry informationi

Entry nameiATRX_HUMAN
AccessioniPrimary (citable) accession number: P46100
Secondary accession number(s): D3DTE2
, P51068, Q15886, Q59FB5, Q59H31, Q5H9A2, Q5JWI4, Q7Z2J1, Q9H0Z1, Q9NTS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 2, 2010
Last modified: November 2, 2016
This is version 190 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.