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Entry version 118 (29 Sep 2021)
Sequence version 1 (01 Oct 2003)
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Protein

Transcriptional regulator ATRX

Gene

ATRX

Organism
Pongo pygmaeus (Bornean orangutan)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at transcript leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 telomeres. May be involved in transcriptional regulation of telomeric repeat-containing RNA (TERRA). Acts as negative regulator of chromatin incorporation of transcriptionally repressive histone MACROH2A1, 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. 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 (By similarity).

By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri170 – 206GATA-type; atypicalPROSITE-ProRule annotationAdd BLAST37
Zinc fingeri217 – 272PHD-type; atypicalPROSITE-ProRule annotationAdd BLAST56
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1594 – 1601ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChromatin regulator, DNA-binding, Helicase, Hydrolase
Biological processDNA damage, DNA repair, Transcription, Transcription regulation
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ATRX
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPongo pygmaeus (Bornean orangutan)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9600 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000743051 – 2492Transcriptional regulator ATRXAdd BLAST2492

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki10Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei25PhosphoserineBy similarity1
Modified residuei34PhosphoserineBy similarity1
Modified residuei89PhosphotyrosineBy similarity1
Modified residuei92PhosphoserineBy similarity1
Modified residuei112PhosphoserineBy similarity1
Cross-linki138Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei213PhosphoserineBy similarity1
Cross-linki299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei316PhosphoserineBy similarity1
Cross-linki438Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei591PhosphothreonineBy similarity1
Modified residuei594PhosphoserineBy similarity1
Modified residuei598PhosphoserineBy similarity1
Cross-linki623Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki623Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei634PhosphoserineBy similarity1
Modified residuei674PhosphothreonineBy similarity1
Modified residuei675PhosphoserineBy similarity1
Modified residuei677PhosphoserineBy similarity1
Modified residuei729PhosphoserineBy similarity1
Modified residuei731PhosphoserineBy similarity1
Modified residuei784PhosphoserineBy similarity1
Modified residuei819PhosphoserineBy similarity1
Modified residuei849PhosphoserineBy similarity1
Modified residuei850PhosphoserineBy similarity1
Modified residuei875PhosphoserineBy similarity1
Modified residuei876PhosphoserineBy similarity1
Modified residuei889PhosphoserineBy similarity1
Modified residuei962PhosphoserineBy similarity1
Modified residuei967N6-acetyllysineBy similarity1
Modified residuei974PhosphoserineBy similarity1
Modified residuei977PhosphothreonineBy similarity1
Cross-linki1004Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1011PhosphoserineBy similarity1
Modified residuei1012PhosphoserineBy similarity1
Modified residuei1013PhosphoserineBy similarity1
Modified residuei1061PhosphoserineBy similarity1
Modified residuei1063PhosphotyrosineBy similarity1
Modified residuei1244PhosphoserineBy similarity1
Modified residuei1245PhosphoserineBy similarity1
Modified residuei1253PhosphoserineBy similarity1
Modified residuei1322PhosphoserineBy similarity1
Modified residuei1324PhosphoserineBy similarity1
Modified residuei1326PhosphoserineBy similarity1
Modified residuei1348PhosphoserineBy similarity1
Modified residuei1352PhosphoserineBy similarity1
Cross-linki1488Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1527PhosphoserineBy similarity1
Modified residuei1529PhosphothreonineBy similarity1
Modified residuei1906PhosphoserineBy similarity1
Modified residuei1913PhosphoserineBy similarity1
Cross-linki1982Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki1982Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki1987Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1992PhosphoserineBy similarity1
Modified residuei1996PhosphoserineBy similarity1
Modified residuei2220PhosphoserineBy similarity1
Modified residuei2474Omega-N-methylarginineBy similarity1
Modified residuei2480Omega-N-methylarginineBy similarity1

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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, MRE11 and NBN; indicative for an association with the MRN complex.

Interacts with histone MACROH2A1.

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).

By similarity

GO - Molecular functioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
Q7YQM3

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>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
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 146DisorderedSequence analysisAdd BLAST146
Regioni457 – 581DisorderedSequence analysisAdd BLAST125
Regioni593 – 619DisorderedSequence analysisAdd BLAST27
Regioni652 – 949DisorderedSequence analysisAdd BLAST298
Regioni967 – 1479DisorderedSequence analysisAdd BLAST513
Regioni1189 – 1326Interaction with DAXXBy similarityAdd BLAST138
Regioni1913 – 2000DisorderedSequence analysisAdd BLAST88
Regioni2010 – 2280Interaction with MECP2By similarityAdd BLAST271
Regioni2462 – 2492DisorderedSequence analysisAdd BLAST31

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi581 – 594PxVxL motifAdd BLAST14
Motifi1719 – 1722DEGH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi32 – 61Polar residuesSequence analysisAdd BLAST30
Compositional biasi69 – 83Polar residuesSequence analysisAdd BLAST15
Compositional biasi109 – 124Polar residuesSequence analysisAdd BLAST16
Compositional biasi471 – 485Polar residuesSequence analysisAdd BLAST15
Compositional biasi486 – 506Basic and acidic residuesSequence analysisAdd BLAST21
Compositional biasi534 – 577Polar residuesSequence analysisAdd BLAST44
Compositional biasi663 – 679Polar residuesSequence analysisAdd BLAST17
Compositional biasi680 – 706Basic and acidic residuesSequence analysisAdd BLAST27
Compositional biasi707 – 731Polar residuesSequence analysisAdd BLAST25
Compositional biasi755 – 798Basic and acidic residuesSequence analysisAdd BLAST44
Compositional biasi811 – 829Basic and acidic residuesSequence analysisAdd BLAST19
Compositional biasi839 – 864Basic and acidic residuesSequence analysisAdd BLAST26
Compositional biasi871 – 912Basic and acidic residuesSequence analysisAdd BLAST42
Compositional biasi922 – 949Basic and acidic residuesSequence analysisAdd BLAST28
Compositional biasi967 – 1007Basic and acidic residuesSequence analysisAdd BLAST41
Compositional biasi1015 – 1030Basic and acidic residuesSequence analysisAdd BLAST16
Compositional biasi1037 – 1095Basic and acidic residuesSequence analysisAdd BLAST59
Compositional biasi1104 – 1144Basic and acidic residuesSequence analysisAdd BLAST41
Compositional biasi1170 – 1191Basic residuesSequence analysisAdd BLAST22
Compositional biasi1194 – 1210Polar residuesSequence analysisAdd BLAST17
Compositional biasi1226 – 1251Polar residuesSequence analysisAdd BLAST26
Compositional biasi1267 – 1288Basic and acidic residuesSequence analysisAdd BLAST22
Compositional biasi1295 – 1335Basic and acidic residuesSequence analysisAdd BLAST41
Compositional biasi1343 – 1362Basic and acidic residuesSequence analysisAdd BLAST20
Compositional biasi1394 – 1419Basic and acidic residuesSequence analysisAdd BLAST26
Compositional biasi1439 – 1468Acidic residuesSequence analysisAdd BLAST30
Compositional biasi1941 – 1955Polar residuesSequence analysisAdd BLAST15
Compositional biasi1969 – 1998Polar residuesSequence analysisAdd BLAST30
Compositional biasi2469 – 2483Pro residuesSequence analysisAdd BLAST15

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated

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

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.40.10, 1 hit
3.40.50.10810, 1 hit
3.40.50.300, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR025766, ADD
IPR041430, ADD_ATRX
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR027417, P-loop_NTPase
IPR038718, SNF2-like_sf
IPR000330, SNF2_N
IPR011011, Znf_FYVE_PHD
IPR013083, Znf_RING/FYVE/PHD

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF17981, ADD_ATRX, 1 hit
PF00271, Helicase_C, 1 hit
PF00176, SNF2_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540, SSF52540, 2 hits
SSF57903, SSF57903, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51533, ADD, 1 hit
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q7YQM3-1 [UniParc]FASTAAdd to basket
« 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 NSVFDNLEQL LQQNKKKIKV
310 320 330 340 350
DSEKSNKVYE HTSRFSPKKT SSNCNGEEKK LDDSCSGSVT YSYSALIVPK
360 370 380 390 400
EMIKKAKKLI ETTANMNSSY VKFLKQATDN SEINSATKLR QLKAFKSVLA
410 420 430 440 450
DIKKAHLALE EDLNSEFRAM DAVSKEKNTK EHKVIEAKFE TKARKGEKPC
460 470 480 490 500
ALEKKDISKS EAKLSRKQVD SEHMYQNVPT EEQRANKSTG GEHKKSDRKE
510 520 530 540 550
EPQYEPANTS EDLDMDIVSV PSSVPEDIFE NLETAMEVQS SVDHQGDGSS
560 570 580 590 600
GTEQEVESSS VKLSISSKDN RGGIKSKTTA KVTKELYVKL TPVSLSNSPI
610 620 630 640 650
KGADCQEVPQ DKDGYKSCGL NPKLEKCGLG QENSDNEHLV ENEVSLLLEE
660 670 680 690 700
SDLRRSPRVK TTPLRRQTET 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 RKQERENFSS AEGTVDKDTT
910 920 930 940 950
IMELRDRLPK KQQASASTDG VDKLSGKEEG FTSLEVRKVA ETKEKSKHLK
960 970 980 990 1000
TKICKKVQDG LSDITEKFLK KDQSDETSED DKKQSKKGTE EKKKTSDFKK
1010 1020 1030 1040 1050
KVIKMEQQYE SSSDGTEKLP EREEICHFPK GIKQIKNGTT DGEKKNKKIR
1060 1070 1080 1090 1100
DKTSKKKDEL SDYAEKSTGK GDSCDSSEDK KSKNGAYGRE KKRCTLLGKS
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):282,616
Last modified:October 1, 2003 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i48EC97106D0CEF20
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AB102643 mRNA Translation: BAC81112.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB102643 mRNA Translation: BAC81112.1

3D structure databases

BMRBiQ7YQM3
ModBaseiSearch...
SWISS-MODEL-WorkspaceiSubmit a new modelling project...

Family and domain databases

Gene3Di3.30.40.10, 1 hit
3.40.50.10810, 1 hit
3.40.50.300, 2 hits
InterProiView protein in InterPro
IPR025766, ADD
IPR041430, ADD_ATRX
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR027417, P-loop_NTPase
IPR038718, SNF2-like_sf
IPR000330, SNF2_N
IPR011011, Znf_FYVE_PHD
IPR013083, Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF17981, ADD_ATRX, 1 hit
PF00271, Helicase_C, 1 hit
PF00176, SNF2_N, 1 hit
SMARTiView protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit
SUPFAMiSSF52540, SSF52540, 2 hits
SSF57903, SSF57903, 1 hit
PROSITEiView protein in PROSITE
PS51533, ADD, 1 hit
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiATRX_PONPY
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q7YQM3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: October 1, 2003
Last modified: September 29, 2021
This is version 118 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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