UniProtKB - Q9UER7 (DAXX_HUMAN)
(max 400 entries)x
Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
- BLAST>sp|Q9UER7|DAXX_HUMAN Death domain-associated protein 6 OS=Homo sapiens OX=9606 GN=DAXX PE=1 SV=2 MATANSIIVLDDDDEDEAAAQPGPSHPLPNAASPGAEAPSSSEPHGARGSSSSGGKKCYK LENEKLFEEFLELCKMQTADHPEVVPFLYNRQQRAHSLFLASAEFCNILSRVLSRARSRP AKLYVYINELCTVLKAHSAKKKLNLAPAATTSNEPSGNNPPTHLSLDPTNAENTASQSPR TRGSRRQIQRLEQLLALYVAEIRRLQEKELDLSELDDPDSAYLQEARLKRKLIRLFGRLC ELKDCSSLTGRVIEQRIPYRGTRYPEVNRRIERLINKPGPDTFPDYGDVLRAVEKAAARH SLGLPRQQLQLMAQDAFRDVGIRLQERRHLDLIYNFGCHLTDDYRPGVDPALSDPVLARR LRENRSLAMSRLDEVISKYAMLQDKSEEGERKKRRARLQGTSSHSADTPEASLDSGEGPS GMASQGCPSASRAETDDEDDEESDEEEEEEEEEEEEEATDSEEEEDLEQMQEGQEDDEEE DEEEEAAAGKDGDKSPMSSLQISNEKNLEPGKQISRSSGEQQNKGRIVSPSLLSEEPLAP SSIDAESNGEQPEELTLEEESPVSQLFELEIEALPLDTPSSVETDISSSRKQSEEPFTTV LENGAGMVSSTSFNGGVSPHNWGDSGPPCKKSRKEKKQTGSGPLGNSYVERQRSVHEKNG KKICTLPSPPSPLASLAPVADSSTRVDSPSHGLVTSSLCIPSPARLSQTPHSQPPRPGTC KTSVATQCDPEEIIVLSDSD
- Align
Protein
Death domain-associated protein 6
Gene
DAXX
Organism
Homo sapiens (Human)
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 protein 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>Select a section on the left to see content.
<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
Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as histone chaperone that facilitates deposition of histone H3.3. Acts as targeting 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. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. In case of overexpression of centromeric histone variant CENPA (as found in various tumors) is involved in its mislocalization to chromosomes; the ectopic localization involves a heterotypic tetramer containing CENPA, and histones H3.3 and H4 and decreases binding of CTCF to chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Shows restriction activity towards human cytomegalovirus (HCMV). Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (PubMed:15016915).12 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.22"Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek."
Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R., Grosveld G.
J. Cell Sci. 115:3319-3330(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH HDAC2; HISTONES AND DEK. - Ref.29"A novel transcription regulatory complex containing death domain-associated protein and the ATR-X syndrome protein."
Tang J., Wu S., Liu H., Stratt R., Barak O.G., Shiekhattar R., Picketts D.J., Yang X.
J. Biol. Chem. 279:20369-20377(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH ATRX, SUBCELLULAR LOCATION. - Ref.30"Negative regulation of p53 functions by Daxx and the involvement of MDM2."
Zhao L.Y., Liu J., Sidhu G.S., Niu Y., Liu Y., Wang R., Liao D.
J. Biol. Chem. 279:50566-50579(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH MDM2 AND TP53. - Ref.31"DAXX interacts with heat shock factor 1 during stress activation and enhances its transcriptional activity."
Boellmann F., Guettouche T., Guo Y., Fenna M., Mnayer L., Voellmy R.
Proc. Natl. Acad. Sci. U.S.A. 101:4100-4105(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH HSF1. - Ref.34"Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors."
Lin D.Y., Huang Y.S., Jeng J.C., Kuo H.Y., Chang C.C., Chao T.T., Ho C.C., Chen Y.C., Lin T.P., Fang H.I., Hung C.C., Suen C.S., Hwang M.J., Chang K.S., Maul G.G., Shih H.M.
Mol. Cell 24:341-354(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION, SUMO INTERACTION MOTIF, MUTAGENESIS OF 733-ILE--ASP-740. - Ref.36"Critical role for Daxx in regulating Mdm2."
Tang J., Qu L.K., Zhang J., Wang W., Michaelson J.S., Degenhardt Y.Y., El-Deiry W.S., Yang X.
Nat. Cell Biol. 8:855-862(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH MDM2 AND USP7, INTERACTION WITH MDM2; TP53 AND USP7, SUBCELLULAR LOCATION. - Ref.40"Nuclear domain 10 components promyelocytic leukemia protein and hDaxx independently contribute to an intrinsic antiviral defense against human cytomegalovirus infection."
Tavalai N., Papior P., Rechter S., Stamminger T.
J. Virol. 82:126-137(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN HCMV RESTRICTION. - Ref.47"The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3."
Drane P., Ouararhni K., Depaux A., Shuaib M., Hamiche A.
Genes Dev. 24:1253-1265(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS HISTONE CHAPERONE, FUNCTION OF THE ATRX:DAXX COMPLEX, INTERACTION WITH HISTONE H3.3. - Ref.49"Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres."
Lewis P.W., Elsaesser S.J., Noh K.M., Stadler S.C., Allis C.D.
Proc. Natl. Acad. Sci. U.S.A. 107:14075-14080(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS HISTONE H3.3 CHAPERONE, INTERACTION WITH HISTONE H3.3. - Ref.53"DAXX-dependent supply of soluble (H3.3-H4) dimers to PML bodies pending deposition into chromatin."
Delbarre E., Ivanauskiene K., Kuntziger T., Collas P.
Genome Res. 23:440-451(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.55"Dynamics of histone H3.3 deposition in proliferating and senescent cells reveals a DAXX-dependent targeting to PML-NBs important for pericentromeric heterochromatin organization."
Corpet A., Olbrich T., Gwerder M., Fink D., Stucki M.
Cell Cycle 13:249-267(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.58"Mislocalization of the centromeric histone variant CenH3/CENP-A in human cells depends on the chaperone DAXX."
Lacoste N., Woolfe A., Tachiwana H., Garea A.V., Barth T., Cantaloube S., Kurumizaka H., Imhof A., Almouzni G.
Mol. Cell 53:631-644(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.
<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
- androgen receptor binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- enzyme binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- heat shock protein binding Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- histone binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- p53 binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein heterodimerization activity Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein homodimerization activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein kinase activator activity Source: ParkinsonsUK-UCL <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- protein kinase binding Source: ParkinsonsUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein N-terminus binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- SUMO binding Source: CAFA <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- transcription coactivator activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transcription corepressor activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transcription factor binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ubiquitin protein ligase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
<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 - Biological processi
- activation of JUN kinase activity Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- androgen receptor signaling pathway Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- apoptotic process Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- cellular response to cadmium ion Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cellular response to copper ion Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cellular response to diamide Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cellular response to heat Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cellular response to sodium arsenite Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cellular response to unfolded protein Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- chromatin remodeling Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- extrinsic apoptotic signaling pathway via death domain receptors Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- negative regulation of transcription, DNA-templated Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nucleosome assembly Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of neuron death Source: ParkinsonsUK-UCL <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- positive regulation of protein kinase activity Source: ParkinsonsUK-UCL <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- positive regulation of protein phosphorylation Source: ParkinsonsUK-UCL <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- regulation of protein ubiquitination Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of transcription, DNA-templated Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transcription, DNA-templated Source: UniProtKB-KW
- viral process Source: UniProtKB-KW
<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 function | Chaperone, Chromatin regulator, Repressor |
| Biological process | Apoptosis, Host-virus interaction, Transcription, Transcription regulation |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.7.7.19 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-6804757 Regulation of TP53 Degradation |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q9UER7 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q9UER7 |
<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: Death domain-associated protein 6Alternative name(s): Daxx Short name: hDaxx ETS1-associated protein 1 Short name: EAP1 Fas death domain-associated protein |
| <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:DAXX Synonyms:BING2, DAP6 |
| <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>Organismi | Homo sapiens (Human) |
| <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 identifieri | 9606 [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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000204209.10 |
Human Gene Nomenclature Database More...HGNCi | HGNC:2681 DAXX |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 603186 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9UER7 |
<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
Nucleus
- nucleoplasm 5 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"Cloning and expression of primate Daxx cDNAs and mapping of the human gene to chromosome 6p21.3 in the MHC region."
Kiriakidou M., Driscoll D.A., Lopez-Guisa J.M., Strauss J.F. III
DNA Cell Biol. 16:1289-1298(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION. - Ref.15"Sequestration and inhibition of Daxx-mediated transcriptional repression by PML."
Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D.
Mol. Cell. Biol. 20:1784-1796(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SUMOYLATED PML; HDAC1; HDAC2 AND HDAC3, SUBCELLULAR LOCATION. - Ref.36"Critical role for Daxx in regulating Mdm2."
Tang J., Qu L.K., Zhang J., Wang W., Michaelson J.S., Degenhardt Y.Y., El-Deiry W.S., Yang X.
Nat. Cell Biol. 8:855-862(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH MDM2 AND USP7, INTERACTION WITH MDM2; TP53 AND USP7, SUBCELLULAR LOCATION. - Ref.38"The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex."
Song M.S., Song S.J., Kim S.Y., Oh H.J., Lim D.S.
EMBO J. 27:1863-1874(2008) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A COMPLEX WITH MDM2; RASSF1 AND USP7, INTERACTION WITH RASSF1; USP7 AND MDM2, SUBCELLULAR LOCATION. - Ref.53"DAXX-dependent supply of soluble (H3.3-H4) dimers to PML bodies pending deposition into chromatin."
Delbarre E., Ivanauskiene K., Kuntziger T., Collas P.
Genome Res. 23:440-451(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
- PML body 8 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"Daxx-beta and Daxx-gamma, two novel splice variants of the transcriptional co-repressor Daxx."
Wethkamp N., Hanenberg H., Funke S., Suschek C.V., Wetzel W., Heikaus S., Grinstein E., Ramp U., Engers R., Gabbert H.E., Mahotka C.
J. Biol. Chem. 286:19576-19588(2011) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA), SUBCELLULAR LOCATION (ISOFORMS BETA AND GAMMA), ALTERNATIVE SPLICING. - Ref.15"Sequestration and inhibition of Daxx-mediated transcriptional repression by PML."
Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D.
Mol. Cell. Biol. 20:1784-1796(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SUMOYLATED PML; HDAC1; HDAC2 AND HDAC3, SUBCELLULAR LOCATION. - Ref.20"The insulin-sensitive glucose transporter, GLUT4, interacts physically with Daxx. Two proteins with capacity to bind Ubc9 and conjugated to SUMO1."
Lalioti V.S., Vergarajauregui S., Pulido D., Sandoval I.V.
J. Biol. Chem. 277:19783-19791(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SLC2A4 AND UBE2I, SUMOYLATION, SUBCELLULAR LOCATION. - Ref.29"A novel transcription regulatory complex containing death domain-associated protein and the ATR-X syndrome protein."
Tang J., Wu S., Liu H., Stratt R., Barak O.G., Shiekhattar R., Picketts D.J., Yang X.
J. Biol. Chem. 279:20369-20377(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH ATRX, SUBCELLULAR LOCATION. - Ref.34"Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors."
Lin D.Y., Huang Y.S., Jeng J.C., Kuo H.Y., Chang C.C., Chao T.T., Ho C.C., Chen Y.C., Lin T.P., Fang H.I., Hung C.C., Suen C.S., Hwang M.J., Chang K.S., Maul G.G., Shih H.M.
Mol. Cell 24:341-354(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION, SUMO INTERACTION MOTIF, MUTAGENESIS OF 733-ILE--ASP-740. - Ref.53"DAXX-dependent supply of soluble (H3.3-H4) dimers to PML bodies pending deposition into chromatin."
Delbarre E., Ivanauskiene K., Kuntziger T., Collas P.
Genome Res. 23:440-451(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.55"Dynamics of histone H3.3 deposition in proliferating and senescent cells reveals a DAXX-dependent targeting to PML-NBs important for pericentromeric heterochromatin organization."
Corpet A., Olbrich T., Gwerder M., Fink D., Stucki M.
Cell Cycle 13:249-267(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.57"Viral reprogramming of the Daxx histone H3.3 chaperone during early Epstein-Barr virus infection."
Tsai K., Chan L., Gibeault R., Conn K., Dheekollu J., Domsic J., Marmorstein R., Schang L.M., Lieberman P.M.
J. Virol. 88:14350-14363(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS PROTEIN BNRF1, SUBCELLULAR LOCATION.
- nucleolus 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.53"DAXX-dependent supply of soluble (H3.3-H4) dimers to PML bodies pending deposition into chromatin."
Delbarre E., Ivanauskiene K., Kuntziger T., Collas P.
Genome Res. 23:440-451(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
- nucleoplasm 5 Publications
Other locations
- Cytoplasm 4 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"Cloning and expression of primate Daxx cDNAs and mapping of the human gene to chromosome 6p21.3 in the MHC region."
Kiriakidou M., Driscoll D.A., Lopez-Guisa J.M., Strauss J.F. III
DNA Cell Biol. 16:1289-1298(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION. - Ref.17"Apoptosis signal-regulating kinase 1 controls the proapoptotic function of death-associated protein (Daxx) in the cytoplasm."
Ko Y.-G., Kang Y.-S., Park H., Seol W., Kim J., Kim T., Park H.-S., Choi E.-J., Kim S.
J. Biol. Chem. 276:39103-39106(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MAP3K5, SUBCELLULAR LOCATION. - Ref.20"The insulin-sensitive glucose transporter, GLUT4, interacts physically with Daxx. Two proteins with capacity to bind Ubc9 and conjugated to SUMO1."
Lalioti V.S., Vergarajauregui S., Pulido D., Sandoval I.V.
J. Biol. Chem. 277:19783-19791(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SLC2A4 AND UBE2I, SUMOYLATION, SUBCELLULAR LOCATION. - Ref.24"Role of the ASK1-SEK1-JNK1-HIPK1 signal in Daxx trafficking and ASK1 oligomerization."
Song J.J., Lee Y.J.
J. Biol. Chem. 278:47245-47252(2003) [PubMed] [Europe PMC] [Abstract]Cited for: OLIGOMERIZATION, SUBCELLULAR LOCATION, INTERACTION WITH MAP3K5, MUTAGENESIS OF SER-668 AND SER-671, PHOSPHORYLATION AT SER-668.
- centromere 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.3"Interphase-specific association of intrinsic centromere protein CENP-C with HDaxx, a death domain-binding protein implicated in Fas-mediated cell death."
Pluta A.F., Earnshaw W.C., Goldberg I.G.
J. Cell Sci. 111:2029-2041(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CENPC, SUBCELLULAR LOCATION. - Ref.55"Dynamics of histone H3.3 deposition in proliferating and senescent cells reveals a DAXX-dependent targeting to PML-NBs important for pericentromeric heterochromatin organization."
Corpet A., Olbrich T., Gwerder M., Fink D., Stucki M.
Cell Cycle 13:249-267(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
Note: Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli (Probable). Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at PML-nuclear bodies (PubMed:12953102, PubMed:14990586, PubMed:23222847, PubMed:24200965). Colocalizes with a subset of interphase centromeres, but is absent from mitotic centromeres (PubMed:9645950). Detected in cytoplasmic punctate structures (PubMed:11842083). Translocates from the nucleus to the cytoplasm upon glucose deprivation or oxidative stress (PubMed:12968034). Colocalizes with RASSF1 in the nucleus (PubMed:18566590). Colocalizes with USP7 in nucleoplasma with accumulation in speckled structures (PubMed:16845383).1 Publication- Cytoplasm 4 Publications
- Ref.15"Sequestration and inhibition of Daxx-mediated transcriptional repression by PML."
Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D.
Mol. Cell. Biol. 20:1784-1796(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SUMOYLATED PML; HDAC1; HDAC2 AND HDAC3, SUBCELLULAR LOCATION. - Ref.3"Interphase-specific association of intrinsic centromere protein CENP-C with HDaxx, a death domain-binding protein implicated in Fas-mediated cell death."
Pluta A.F., Earnshaw W.C., Goldberg I.G.
J. Cell Sci. 111:2029-2041(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CENPC, SUBCELLULAR LOCATION. - Ref.20"The insulin-sensitive glucose transporter, GLUT4, interacts physically with Daxx. Two proteins with capacity to bind Ubc9 and conjugated to SUMO1."
Lalioti V.S., Vergarajauregui S., Pulido D., Sandoval I.V.
J. Biol. Chem. 277:19783-19791(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SLC2A4 AND UBE2I, SUMOYLATION, SUBCELLULAR LOCATION. - Ref.24"Role of the ASK1-SEK1-JNK1-HIPK1 signal in Daxx trafficking and ASK1 oligomerization."
Song J.J., Lee Y.J.
J. Biol. Chem. 278:47245-47252(2003) [PubMed] [Europe PMC] [Abstract]Cited for: OLIGOMERIZATION, SUBCELLULAR LOCATION, INTERACTION WITH MAP3K5, MUTAGENESIS OF SER-668 AND SER-671, PHOSPHORYLATION AT SER-668. - Ref.26"The ATRX syndrome protein forms a chromatin-remodeling complex with Daxx and localizes in promyelocytic leukemia nuclear bodies."
Xue Y., Gibbons R., Yan Z., Yang D., McDowell T.L., Sechi S., Qin J., Zhou S., Higgs D., Wang W.
Proc. Natl. Acad. Sci. U.S.A. 100:10635-10640(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ATRX, SUBCELLULAR LOCATION. - Ref.29"A novel transcription regulatory complex containing death domain-associated protein and the ATR-X syndrome protein."
Tang J., Wu S., Liu H., Stratt R., Barak O.G., Shiekhattar R., Picketts D.J., Yang X.
J. Biol. Chem. 279:20369-20377(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH ATRX, SUBCELLULAR LOCATION. - Ref.36"Critical role for Daxx in regulating Mdm2."
Tang J., Qu L.K., Zhang J., Wang W., Michaelson J.S., Degenhardt Y.Y., El-Deiry W.S., Yang X.
Nat. Cell Biol. 8:855-862(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH MDM2 AND USP7, INTERACTION WITH MDM2; TP53 AND USP7, SUBCELLULAR LOCATION. - Ref.38"The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex."
Song M.S., Song S.J., Kim S.Y., Oh H.J., Lim D.S.
EMBO J. 27:1863-1874(2008) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A COMPLEX WITH MDM2; RASSF1 AND USP7, INTERACTION WITH RASSF1; USP7 AND MDM2, SUBCELLULAR LOCATION. - Ref.53"DAXX-dependent supply of soluble (H3.3-H4) dimers to PML bodies pending deposition into chromatin."
Delbarre E., Ivanauskiene K., Kuntziger T., Collas P.
Genome Res. 23:440-451(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.55"Dynamics of histone H3.3 deposition in proliferating and senescent cells reveals a DAXX-dependent targeting to PML-NBs important for pericentromeric heterochromatin organization."
Corpet A., Olbrich T., Gwerder M., Fink D., Stucki M.
Cell Cycle 13:249-267(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Isoform beta :
Nucleus
- Nucleus 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"Daxx-beta and Daxx-gamma, two novel splice variants of the transcriptional co-repressor Daxx."
Wethkamp N., Hanenberg H., Funke S., Suschek C.V., Wetzel W., Heikaus S., Grinstein E., Ramp U., Engers R., Gabbert H.E., Mahotka C.
J. Biol. Chem. 286:19576-19588(2011) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA), SUBCELLULAR LOCATION (ISOFORMS BETA AND GAMMA), ALTERNATIVE SPLICING.
Note: Diffuse nuclear distribution pattern and no comparable dot-like accumulation of isoform 1.1 Publication- Nucleus 1 Publication
- Ref.6"Daxx-beta and Daxx-gamma, two novel splice variants of the transcriptional co-repressor Daxx."
Wethkamp N., Hanenberg H., Funke S., Suschek C.V., Wetzel W., Heikaus S., Grinstein E., Ramp U., Engers R., Gabbert H.E., Mahotka C.
J. Biol. Chem. 286:19576-19588(2011) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA), SUBCELLULAR LOCATION (ISOFORMS BETA AND GAMMA), ALTERNATIVE SPLICING.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Isoform gamma :
Nucleus
- Nucleus 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"Daxx-beta and Daxx-gamma, two novel splice variants of the transcriptional co-repressor Daxx."
Wethkamp N., Hanenberg H., Funke S., Suschek C.V., Wetzel W., Heikaus S., Grinstein E., Ramp U., Engers R., Gabbert H.E., Mahotka C.
J. Biol. Chem. 286:19576-19588(2011) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA), SUBCELLULAR LOCATION (ISOFORMS BETA AND GAMMA), ALTERNATIVE SPLICING.
Note: Diffuse nuclear distribution pattern and no comparable dot-like accumulation of isoform 1.1 Publication- Nucleus 1 Publication
- Ref.6"Daxx-beta and Daxx-gamma, two novel splice variants of the transcriptional co-repressor Daxx."
Wethkamp N., Hanenberg H., Funke S., Suschek C.V., Wetzel W., Heikaus S., Grinstein E., Ramp U., Engers R., Gabbert H.E., Mahotka C.
J. Biol. Chem. 286:19576-19588(2011) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA), SUBCELLULAR LOCATION (ISOFORMS BETA AND GAMMA), ALTERNATIVE SPLICING.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Cytosol
- cytosol Source: UniProtKB
Nucleus
- nuclear body Source: HPA
- nucleolus Source: UniProtKB-SubCell
- nucleoplasm Source: Reactome
- nucleus Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- PML body Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- SWI/SNF superfamily-type complex Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
- chromosome, centromeric region Source: CACAO <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cytoplasm Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<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>Keywords - Cellular componenti
Centromere, Chromosome, Cytoplasm, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 206 | Q → L: Impairs interaction with histones H3 and H4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 220 | S → A: Abolishes interaction with histones H3 and H4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 222 | Y → A or S: Abolishes interaction with histones H3 and H4. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 222 | Y → E: Abolishes interaction with histone H3.3. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 225 | E → L: Impairs interaction with histones H3 and H4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 229 | K → A or L: Impairs interaction with histones H3 and H4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 251 | R → A: Abolishes interaction with histones H3 and H4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 317 | F → A: Abolishes interaction with histones H3 and H4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 328 | R → A: Abolishes interaction with histones H3 and H4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 331 | D → A: Abolishes interaction with histones H3 and H4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 630 | K → A: Abolishes sumoylation; when associated with A-631. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 631 | K → A: Abolishes sumoylation; when associated with A-630. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 668 | S → A: No translocation to the cytosol upon glucose deprivation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 671 | S → A: No effect on cytosol translocation. upon glucose deprivation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 733 – 740 | Missing : Abolishes sumoylation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 8 |
Organism-specific databases
DisGeNET More...DisGeNETi | 1616 |
MalaCards human disease database More...MalaCardsi | DAXX |
Open Targets More...OpenTargetsi | ENSG00000204209 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA27148 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | DAXX |
Domain mapping of disease mutations (DMDM) More...DMDMi | 24636785 |
<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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000151258 | 1 – 740 | Death domain-associated protein 6Add BLAST | 740 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 residuei | 25 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), 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-linki | 142 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <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 residuei | 178 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 213 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 412 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 424 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 459 | PhosphothreonineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <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 residuei | 495 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 498 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <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 residuei | 512 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 561 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <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 residuei | 580 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), 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-linki | 630 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), 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-linki | 631 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <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 residuei | 668 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 residuei | 671 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 688 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 702 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 737 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 739 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Sumoylated with SUMO1 on multiple lysine residues.3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.19"Modification of Daxx by small ubiquitin-related modifier-1."
Jang M.-S., Ryu S.-W., Kim E.
Biochem. Biophys. Res. Commun. 295:495-500(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUMOYLATION AT LYS-630 AND LYS-631, MUTAGENESIS OF LYS-630 AND LYS-631. - Ref.20"The insulin-sensitive glucose transporter, GLUT4, interacts physically with Daxx. Two proteins with capacity to bind Ubc9 and conjugated to SUMO1."
Lalioti V.S., Vergarajauregui S., Pulido D., Sandoval I.V.
J. Biol. Chem. 277:19783-19791(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SLC2A4 AND UBE2I, SUMOYLATION, SUBCELLULAR LOCATION. - Ref.34"Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors."
Lin D.Y., Huang Y.S., Jeng J.C., Kuo H.Y., Chang C.C., Chao T.T., Ho C.C., Chen Y.C., Lin T.P., Fang H.I., Hung C.C., Suen C.S., Hwang M.J., Chang K.S., Maul G.G., Shih H.M.
Mol. Cell 24:341-354(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION, SUMO INTERACTION MOTIF, MUTAGENESIS OF 733-ILE--ASP-740.
Phosphorylated by HIPK1 upon glucose deprivation.3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.13"The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated repressor hDaxx."
Hollenbach A.D., Sublett J.E., McPherson C.J., Grosveld G.
EMBO J. 18:3702-3711(1999) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PAX3 AND PAX7, PHOSPHORYLATION. - Ref.22"Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek."
Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R., Grosveld G.
J. Cell Sci. 115:3319-3330(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH HDAC2; HISTONES AND DEK. - Ref.24"Role of the ASK1-SEK1-JNK1-HIPK1 signal in Daxx trafficking and ASK1 oligomerization."
Song J.J., Lee Y.J.
J. Biol. Chem. 278:47245-47252(2003) [PubMed] [Europe PMC] [Abstract]Cited for: OLIGOMERIZATION, SUBCELLULAR LOCATION, INTERACTION WITH MAP3K5, MUTAGENESIS OF SER-668 AND SER-671, PHOSPHORYLATION AT SER-668.
Polyubiquitinated; which is promoted by CUL3 and SPOP and results in proteasomal degradation. Ubiquitinated by MDM2; inducing its degradation. Deubiquitinated by USP7; leading to stabilize it.2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.33"BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase."
Kwon J.E., La M., Oh K.H., Oh Y.M., Kim G.R., Seol J.H., Baek S.H., Chiba T., Tanaka K., Bang O.S., Joe C.O., Chung C.H.
J. Biol. Chem. 281:12664-12672(2006) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A COMPLEX WITH CUL3 AND SPOP, UBIQUITINATION. - Ref.46"Daxx is reciprocally regulated by Mdm2 and Hausp."
Tang J., Qu L., Pang M., Yang X.
Biochem. Biophys. Res. Commun. 393:542-545(2010) [PubMed] [Europe PMC] [Abstract]Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP7.
<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>Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9UER7 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9UER7 |
PeptideAtlas More...PeptideAtlasi | Q9UER7 |
PRoteomics IDEntifications database More...PRIDEi | Q9UER7 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 84150 84151 [Q9UER7-2] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9UER7 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9UER7 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Ubiquitous.
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
Upon mitogenic stimulation by concanavalin-A.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000204209 |
CleanEx database of gene expression profiles More...CleanExi | HS_DAXX |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9UER7 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9UER7 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB002224 CAB025546 HPA008736 HPA008797 HPA065779 |
<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
Homomultimer. Interacts (via C-terminus) with TNFRSF6 (via death domain). Interacts with PAX5, SLC2A4/GLUT4, MAP3K5, TGFBR2, phosphorylated dimeric HSPB1/HSP27, CENPC, ETS1, sumoylated PML, UBE2I, MCRS1 and TP53. Interacts (via N-terminus) with HIPK2 and HIPK3. Interacts with HIPK1, which induces translocation from PML/POD/ND10 nuclear bodies to chromatin and enhances association with HDAC1. Interacts (non-phosphorylated) with PAX3, PAX7, DEK, HDAC1, HDAC2, HDAC3, acetylated histone H4 and histones H2A, H2B, H3, H3.3 and H4. Interacts with SPOP; mediating CUL3-dependent proteosomal degradation. Interacts with CBP; the interaction is dependent the sumoylation of CBP and suppresses CBP transcriptional activity via recruitment of HDAC2 directly in the complex with TP53 and HIPK2. Interacts with AXIN1; the interaction stimulates the interaction of DAXX with TP53, stimulates 'Ser-46' phosphorylation of TP53 on and induces cell death on UV irradiation. Interacts with MDM2; the interaction is direct. Interacts with USP7; the interaction is direct and independent of MDM2 and TP53. Part of a complex with DAXX, MDM2 and USP7 under non-stress conditions. Interacts (via N-terminus) with RASSF1 (via C-terminus); the interaction is independent of MDM2 and TP53; RASSF1 isoform A disrupts interactions among MDM2, DAXX and USP7, thus contributing to the efficient activation of TP53 by promoting MDM2 self-ubiquitination in cell-cycle checkpoint control in response to DNA damage. Interacts with ATRX to form the chromatin remodeling complex ATRX:DAXX. Interacts with human cytomegalovirus/HHV-5 tegument phosphoprotein pp71 and protein UL123. Interacts with Epstein-Barr virus protein BNRF1. Interacts with human adenovirus 5 E1B-55K protein; this interaction might alterate the normal interactions of DAXX, PML, and TP53, which may contribute to cell transformation (PubMed:14557665). Interacts with HSF1 (via homotrimeric form preferentially); this interaction relieves homotrimeric HSF1 from repression of its transcriptional activity by HSP90-dependent multichaperone complex upon heat shock (PubMed:15016915).31 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.3"Interphase-specific association of intrinsic centromere protein CENP-C with HDaxx, a death domain-binding protein implicated in Fas-mediated cell death."
Pluta A.F., Earnshaw W.C., Goldberg I.G.
J. Cell Sci. 111:2029-2041(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CENPC, SUBCELLULAR LOCATION. - Ref.13"The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated repressor hDaxx."
Hollenbach A.D., Sublett J.E., McPherson C.J., Grosveld G.
EMBO J. 18:3702-3711(1999) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PAX3 AND PAX7, PHOSPHORYLATION. - Ref.14"Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis."
Zhong S., Salomoni P., Ronchetti S., Guo A., Ruggero D., Pandolfi P.P.
J. Exp. Med. 191:631-640(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PML. - Ref.15"Sequestration and inhibition of Daxx-mediated transcriptional repression by PML."
Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D.
Mol. Cell. Biol. 20:1784-1796(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SUMOYLATED PML; HDAC1; HDAC2 AND HDAC3, SUBCELLULAR LOCATION. - Ref.16"Inhibition of Daxx-mediated apoptosis by heat shock protein 27."
Charette S.J., Lavoie J.N., Lambert H., Landry J.
Mol. Cell. Biol. 20:7602-7612(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HSPB1. - Ref.17"Apoptosis signal-regulating kinase 1 controls the proapoptotic function of death-associated protein (Daxx) in the cytoplasm."
Ko Y.-G., Kang Y.-S., Park H., Seol W., Kim J., Kim T., Park H.-S., Choi E.-J., Kim S.
J. Biol. Chem. 276:39103-39106(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MAP3K5, SUBCELLULAR LOCATION. - Ref.18"TGF-beta-induced apoptosis is mediated by the adapter protein Daxx that facilitates JNK activation."
Perlman R., Schiemann W.P., Brooks M.W., Lodish H.F., Weinberg R.A.
Nat. Cell Biol. 3:708-714(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TGFBR2. - Ref.20"The insulin-sensitive glucose transporter, GLUT4, interacts physically with Daxx. Two proteins with capacity to bind Ubc9 and conjugated to SUMO1."
Lalioti V.S., Vergarajauregui S., Pulido D., Sandoval I.V.
J. Biol. Chem. 277:19783-19791(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SLC2A4 AND UBE2I, SUMOYLATION, SUBCELLULAR LOCATION. - Ref.21"Essential role of the 58-kDa microspherule protein in the modulation of Daxx-dependent transcriptional repression as revealed by nucleolar sequestration."
Lin D.-Y., Shih H.-M.
J. Biol. Chem. 277:25446-25456(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MCRS1. - Ref.22"Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek."
Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R., Grosveld G.
J. Cell Sci. 115:3319-3330(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH HDAC2; HISTONES AND DEK. - Ref.23"HIPK2 regulates transforming growth factor-beta-induced c-Jun NH(2)-terminal kinase activation and apoptosis in human hepatoma cells."
Hofmann T.G., Stollberg N., Schmitz M.L., Will H.
Cancer Res. 63:8271-8277(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HIPK2. - Ref.24"Role of the ASK1-SEK1-JNK1-HIPK1 signal in Daxx trafficking and ASK1 oligomerization."
Song J.J., Lee Y.J.
J. Biol. Chem. 278:47245-47252(2003) [PubMed] [Europe PMC] [Abstract]Cited for: OLIGOMERIZATION, SUBCELLULAR LOCATION, INTERACTION WITH MAP3K5, MUTAGENESIS OF SER-668 AND SER-671, PHOSPHORYLATION AT SER-668. - Ref.25"Homeodomain-interacting protein kinase 1 modulates Daxx localization, phosphorylation, and transcriptional activity."
Ecsedy J.A., Michaelson J.S., Leder P.
Mol. Cell. Biol. 23:950-960(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HIPK1. - Ref.26"The ATRX syndrome protein forms a chromatin-remodeling complex with Daxx and localizes in promyelocytic leukemia nuclear bodies."
Xue Y., Gibbons R., Yan Z., Yang D., McDowell T.L., Sechi S., Qin J., Zhou S., Higgs D., Wang W.
Proc. Natl. Acad. Sci. U.S.A. 100:10635-10640(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ATRX, SUBCELLULAR LOCATION. - Ref.27"Adenovirus E1B 55-kilodalton oncoprotein binds to Daxx and eliminates enhancement of p53-dependent transcription by DAXX."
Zhao L.Y., Colosimo A.L., Liu Y., Wan Y., Liao D.
J. Virol. 77:11809-11821(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HADV5 E1B-55K. - Ref.28"Daxx-mediated transcriptional repression of MMP1 gene is reversed by SPOP."
La M., Kim K., Park J., Won J., Lee J.-H., Fu Y.M., Meadows G.G., Joe C.O.
Biochem. Biophys. Res. Commun. 320:760-765(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SPOP. - Ref.29"A novel transcription regulatory complex containing death domain-associated protein and the ATR-X syndrome protein."
Tang J., Wu S., Liu H., Stratt R., Barak O.G., Shiekhattar R., Picketts D.J., Yang X.
J. Biol. Chem. 279:20369-20377(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH ATRX, SUBCELLULAR LOCATION. - Ref.30"Negative regulation of p53 functions by Daxx and the involvement of MDM2."
Zhao L.Y., Liu J., Sidhu G.S., Niu Y., Liu Y., Wang R., Liao D.
J. Biol. Chem. 279:50566-50579(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH MDM2 AND TP53. - Ref.31"DAXX interacts with heat shock factor 1 during stress activation and enhances its transcriptional activity."
Boellmann F., Guettouche T., Guo Y., Fenna M., Mnayer L., Voellmy R.
Proc. Natl. Acad. Sci. U.S.A. 101:4100-4105(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH HSF1. - Ref.33"BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase."
Kwon J.E., La M., Oh K.H., Oh Y.M., Kim G.R., Seol J.H., Baek S.H., Chiba T., Tanaka K., Bang O.S., Joe C.O., Chung C.H.
J. Biol. Chem. 281:12664-12672(2006) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A COMPLEX WITH CUL3 AND SPOP, UBIQUITINATION. - Ref.36"Critical role for Daxx in regulating Mdm2."
Tang J., Qu L.K., Zhang J., Wang W., Michaelson J.S., Degenhardt Y.Y., El-Deiry W.S., Yang X.
Nat. Cell Biol. 8:855-862(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH MDM2 AND USP7, INTERACTION WITH MDM2; TP53 AND USP7, SUBCELLULAR LOCATION. - Ref.38"The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex."
Song M.S., Song S.J., Kim S.Y., Oh H.J., Lim D.S.
EMBO J. 27:1863-1874(2008) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A COMPLEX WITH MDM2; RASSF1 AND USP7, INTERACTION WITH RASSF1; USP7 AND MDM2, SUBCELLULAR LOCATION. - Ref.41"Human cytomegalovirus protein pp71 displaces the chromatin-associated factor ATRX from nuclear domain 10 at early stages of infection."
Lukashchuk V., McFarlane S., Everett R.D., Preston C.M.
J. Virol. 82:12543-12554(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HCMV PP71. - Ref.47"The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3."
Drane P., Ouararhni K., Depaux A., Shuaib M., Hamiche A.
Genes Dev. 24:1253-1265(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS HISTONE CHAPERONE, FUNCTION OF THE ATRX:DAXX COMPLEX, INTERACTION WITH HISTONE H3.3. - Ref.48"Human cytomegalovirus IE72 protein interacts with the transcriptional repressor hDaxx to regulate LUNA gene expression during lytic infection."
Reeves M., Woodhall D., Compton T., Sinclair J.
J. Virol. 84:7185-7194(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HHV-5 PROTEIN UL123. - Ref.49"Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres."
Lewis P.W., Elsaesser S.J., Noh K.M., Stadler S.C., Allis C.D.
Proc. Natl. Acad. Sci. U.S.A. 107:14075-14080(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS HISTONE H3.3 CHAPERONE, INTERACTION WITH HISTONE H3.3. - Ref.57"Viral reprogramming of the Daxx histone H3.3 chaperone during early Epstein-Barr virus infection."
Tsai K., Chan L., Gibeault R., Conn K., Dheekollu J., Domsic J., Marmorstein R., Schang L.M., Lieberman P.M.
J. Virol. 88:14350-14363(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS PROTEIN BNRF1, SUBCELLULAR LOCATION. - Ref.60"Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C."
Escobar-Cabrera E., Lau D.K., Giovinazzi S., Ishov A.M., McIntosh L.P.
Structure 18:1642-1653(2010) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 55-144 IN COMPLEX WITH RASSF1, INTERACTION WITH RASSF1. - Ref.62"Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX."
Liu C.P., Xiong C., Wang M., Yu Z., Yang N., Chen P., Zhang Z., Li G., Xu R.M.
Nat. Struct. Mol. Biol. 19:1287-1292(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 184-390 IN COMPLEX WITH HISTONE H3.3/H4 DIMER, MUTAGENESIS OF TYR-222. - Ref.63"DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition."
Elsasser S.J., Huang H., Lewis P.W., Chin J.W., Allis C.D., Patel D.J.
Nature 491:560-565(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 178-389 IN COMPLEX WITH HISTONE H3.3/H4 DIMER, MUTAGENESIS OF GLN-206; SER-220; TYR-222; GLU-225; LYS-229; ARG-251; PHE-317; ARG-328 AND ASP-331.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
<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
- androgen receptor binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- enzyme binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- heat shock protein binding Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- histone binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- p53 binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein heterodimerization activity Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein homodimerization activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein kinase binding Source: ParkinsonsUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein N-terminus binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- SUMO binding Source: CAFA <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- transcription factor binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ubiquitin protein ligase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 107985, 235 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q9UER7 |
Database of interacting proteins More...DIPi | DIP-27628N |
Protein interaction database and analysis system More...IntActi | Q9UER7, 124 interactors |
Molecular INTeraction database More...MINTi | Q9UER7 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000266000 |
<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
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 60 – 77 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 78 – 80 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 84 – 93 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 97 – 100 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 103 – 118 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 120 – 122 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 123 – 136 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 138 – 140 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 185 – 206 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 22 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 214 – 216 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 221 – 242 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 22 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 252 – 254 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 265 – 275 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 278 – 280 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 286 – 299 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 306 – 333 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 28 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 339 – 341 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 346 – 348 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 350 – 353 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 355 – 384 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 30 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2KQS | NMR | - | B | 721-740 | [»] | |
| 2KZS | NMR | - | A | 55-144 | [»] | |
| 2KZU | NMR | - | A | 55-144 | [»] | |
| 4H9N | X-ray | 1.95 | C | 178-389 | [»] | |
| 4H9O | X-ray | 2.05 | C | 178-389 | [»] | |
| 4H9P | X-ray | 2.20 | C | 178-389 | [»] | |
| 4H9Q | X-ray | 1.95 | C | 178-389 | [»] | |
| 4H9R | X-ray | 2.20 | C | 178-389 | [»] | |
| 4H9S | X-ray | 2.60 | E/F | 183-398 | [»] | |
| 4HGA | X-ray | 2.80 | A | 184-390 | [»] | |
| 5GRQ | X-ray | 1.58 | A | 55-144 | [»] | |
| B | 55-143 | [»] | ||||
| 5KDM | X-ray | 3.50 | C | 178-389 | [»] | |
| 5Y6O | X-ray | 3.10 | A/B/C/D/E/F/G/H/I | 50-144 | [»] | |
Database of protein disorder More...DisProti | DP00707 | |||||
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9UER7 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9UER7 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9UER7 |
<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
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Regioni | 1 – 160 | Necessary for interaction with USP7 and ATRXAdd BLAST | 160 | |
| <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>Regioni | 183 – 417 | Interaction with histone H3.3Add BLAST | 235 | |
| <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>Regioni | 347 – 570 | Necessary for interaction with USP7Add BLAST | 224 | |
| <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>Regioni | 501 – 625 | Interaction with MAP3K5Add BLAST | 125 | |
| <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>Regioni | 626 – 740 | Interaction with SPOP1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 115 | |
| <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>Regioni | 733 – 740 | Sumo interaction motif (SIM) | 8 |
Coiled coil
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 180 – 217 | Sequence analysisAdd BLAST | 38 | |
| <p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 358 – 399 | Sequence analysisAdd BLAST | 42 | |
| <p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 430 – 489 | Sequence analysisAdd BLAST | 60 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Motifi | 391 – 395 | Nuclear localization signalSequence analysis | 5 | |
| <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>Motifi | 628 – 634 | Nuclear localization signalSequence analysis | 7 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 11 – 16 | Poly-Asp | 6 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 434 – 572 | Asp/Glu-rich (acidic)Add BLAST | 139 |
<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 Sumo interaction motif mediates Sumo binding, and is required both for sumoylation and binding to sumoylated targets.
<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 DAXX family.Curated
<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>Keywords - Domaini
Coiled coilPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IGIP Eukaryota ENOG4111K0B LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000009448 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000112148 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG031495 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9UER7 |
KEGG Orthology (KO) More...KOi | K02308 |
Identification of Orthologs from Complete Genome Data More...OMAi | LCKTQTA |
Database of Orthologous Groups More...OrthoDBi | EOG09370P3D |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9UER7 |
TreeFam database of animal gene trees More...TreeFami | TF325803 |
Family and domain databases
Conserved Domains Database More...CDDi | cd13151 DAXX_helical_bundle, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.8.810, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR005012 Daxx IPR031333 Daxx_N IPR038298 Daxx_N_sf |
The PANTHER Classification System More...PANTHERi | PTHR12766 PTHR12766, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF03344 Daxx, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5)i
<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.
This entry describes 5 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
Isoform 1 (identifier: Q9UER7-1) [UniParc]FASTAAdd to basketAdded to basketShow »
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.
10 20 30 40 50
MATANSIIVL DDDDEDEAAA QPGPSHPLPN AASPGAEAPS SSEPHGARGS
60 70 80 90 100
SSSGGKKCYK LENEKLFEEF LELCKMQTAD HPEVVPFLYN RQQRAHSLFL
110 120 130 140 150
ASAEFCNILS RVLSRARSRP AKLYVYINEL CTVLKAHSAK KKLNLAPAAT
160 170 180 190 200
TSNEPSGNNP PTHLSLDPTN AENTASQSPR TRGSRRQIQR LEQLLALYVA
210 220 230 240 250
EIRRLQEKEL DLSELDDPDS AYLQEARLKR KLIRLFGRLC ELKDCSSLTG
260 270 280 290 300
RVIEQRIPYR GTRYPEVNRR IERLINKPGP DTFPDYGDVL RAVEKAAARH
310 320 330 340 350
SLGLPRQQLQ LMAQDAFRDV GIRLQERRHL DLIYNFGCHL TDDYRPGVDP
360 370 380 390 400
ALSDPVLARR LRENRSLAMS RLDEVISKYA MLQDKSEEGE RKKRRARLQG
410 420 430 440 450
TSSHSADTPE ASLDSGEGPS GMASQGCPSA SRAETDDEDD EESDEEEEEE
460 470 480 490 500
EEEEEEEATD SEEEEDLEQM QEGQEDDEEE DEEEEAAAGK DGDKSPMSSL
510 520 530 540 550
QISNEKNLEP GKQISRSSGE QQNKGRIVSP SLLSEEPLAP SSIDAESNGE
560 570 580 590 600
QPEELTLEEE SPVSQLFELE IEALPLDTPS SVETDISSSR KQSEEPFTTV
610 620 630 640 650
LENGAGMVSS TSFNGGVSPH NWGDSGPPCK KSRKEKKQTG SGPLGNSYVE
660 670 680 690 700
RQRSVHEKNG KKICTLPSPP SPLASLAPVA DSSTRVDSPS HGLVTSSLCI
710 720 730 740
PSPARLSQTP HSQPPRPGTC KTSVATQCDP EEIIVLSDSD
Length:740
Mass (Da):81,373
Last modified:November 1, 2002 - v2
<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:i1B309ADDAA878040
Isoform 2 (identifier: Q9UER7-2) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
696-740: SSLCIPSPARLSQTPHSQPPRPGTCKTSVATQCDPEEIIVLSDSD → PAKNLGRRRSKQDQG
10 20 30 40 50
MATANSIIVL DDDDEDEAAA QPGPSHPLPN AASPGAEAPS SSEPHGARGS
60 70 80 90 100
SSSGGKKCYK LENEKLFEEF LELCKMQTAD HPEVVPFLYN RQQRAHSLFL
110 120 130 140 150
ASAEFCNILS RVLSRARSRP AKLYVYINEL CTVLKAHSAK KKLNLAPAAT
160 170 180 190 200
TSNEPSGNNP PTHLSLDPTN AENTASQSPR TRGSRRQIQR LEQLLALYVA
210 220 230 240 250
EIRRLQEKEL DLSELDDPDS AYLQEARLKR KLIRLFGRLC ELKDCSSLTG
260 270 280 290 300
RVIEQRIPYR GTRYPEVNRR IERLINKPGP DTFPDYGDVL RAVEKAAARH
310 320 330 340 350
SLGLPRQQLQ LMAQDAFRDV GIRLQERRHL DLIYNFGCHL TDDYRPGVDP
360 370 380 390 400
ALSDPVLARR LRENRSLAMS RLDEVISKYA MLQDKSEEGE RKKRRARLQG
410 420 430 440 450
TSSHSADTPE ASLDSGEGPS GMASQGCPSA SRAETDDEDD EESDEEEEEE
460 470 480 490 500
EEEEEEEATD SEEEEDLEQM QEGQEDDEEE DEEEEAAAGK DGDKSPMSSL
510 520 530 540 550
QISNEKNLEP GKQISRSSGE QQNKGRIVSP SLLSEEPLAP SSIDAESNGE
560 570 580 590 600
QPEELTLEEE SPVSQLFELE IEALPLDTPS SVETDISSSR KQSEEPFTTV
610 620 630 640 650
LENGAGMVSS TSFNGGVSPH NWGDSGPPCK KSRKEKKQTG SGPLGNSYVE
660 670 680 690 700
RQRSVHEKNG KKICTLPSPP SPLASLAPVA DSSTRVDSPS HGLVTPAKNL
710
GRRRSKQDQG
Note: No experimental confirmation available.
Show »Length:710
Mass (Da):78,333
<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:i47E099676EB7315C
Isoform 3 (identifier: Q9UER7-3) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-75: Missing.
10 20 30 40 50
MQTADHPEVV PFLYNRQQRA HSLFLASAEF CNILSRVLSR ARSRPAKLYV
60 70 80 90 100
YINELCTVLK AHSAKKKLNL APAATTSNEP SGNNPPTHLS LDPTNAENTA
110 120 130 140 150
SQSPRTRGSR RQIQRLEQLL ALYVAEIRRL QEKELDLSEL DDPDSAYLQE
160 170 180 190 200
ARLKRKLIRL FGRLCELKDC SSLTGRVIEQ RIPYRGTRYP EVNRRIERLI
210 220 230 240 250
NKPGPDTFPD YGDVLRAVEK AAARHSLGLP RQQLQLMAQD AFRDVGIRLQ
260 270 280 290 300
ERRHLDLIYN FGCHLTDDYR PGVDPALSDP VLARRLRENR SLAMSRLDEV
310 320 330 340 350
ISKYAMLQDK SEEGERKKRR ARLQGTSSHS ADTPEASLDS GEGPSGMASQ
360 370 380 390 400
GCPSASRAET DDEDDEESDE EEEEEEEEEE EEATDSEEEE DLEQMQEGQE
410 420 430 440 450
DDEEEDEEEE AAAGKDGDKS PMSSLQISNE KNLEPGKQIS RSSGEQQNKG
460 470 480 490 500
RIVSPSLLSE EPLAPSSIDA ESNGEQPEEL TLEEESPVSQ LFELEIEALP
510 520 530 540 550
LDTPSSVETD ISSSRKQSEE PFTTVLENGA GMVSSTSFNG GVSPHNWGDS
560 570 580 590 600
GPPCKKSRKE KKQTGSGPLG NSYVERQRSV HEKNGKKICT LPSPPSPLAS
610 620 630 640 650
LAPVADSSTR VDSPSHGLVT SSLCIPSPAR LSQTPHSQPP RPGTCKTSVA
660
TQCDPEEIIV LSDSD
Note: No experimental confirmation available.
Show »Length:665
Mass (Da):73,589
<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:i11AF08F83A462073
Isoform beta (identifier: Q9UER7-4) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
653-688: RSVHEKNGKKICTLPSPPSPLASLAPVADSSTRVDS → SPAVPNPPFTASSAWYLQDKCGHTMRSRRDHRALRL
689-740: Missing.
10 20 30 40 50
MATANSIIVL DDDDEDEAAA QPGPSHPLPN AASPGAEAPS SSEPHGARGS
60 70 80 90 100
SSSGGKKCYK LENEKLFEEF LELCKMQTAD HPEVVPFLYN RQQRAHSLFL
110 120 130 140 150
ASAEFCNILS RVLSRARSRP AKLYVYINEL CTVLKAHSAK KKLNLAPAAT
160 170 180 190 200
TSNEPSGNNP PTHLSLDPTN AENTASQSPR TRGSRRQIQR LEQLLALYVA
210 220 230 240 250
EIRRLQEKEL DLSELDDPDS AYLQEARLKR KLIRLFGRLC ELKDCSSLTG
260 270 280 290 300
RVIEQRIPYR GTRYPEVNRR IERLINKPGP DTFPDYGDVL RAVEKAAARH
310 320 330 340 350
SLGLPRQQLQ LMAQDAFRDV GIRLQERRHL DLIYNFGCHL TDDYRPGVDP
360 370 380 390 400
ALSDPVLARR LRENRSLAMS RLDEVISKYA MLQDKSEEGE RKKRRARLQG
410 420 430 440 450
TSSHSADTPE ASLDSGEGPS GMASQGCPSA SRAETDDEDD EESDEEEEEE
460 470 480 490 500
EEEEEEEATD SEEEEDLEQM QEGQEDDEEE DEEEEAAAGK DGDKSPMSSL
510 520 530 540 550
QISNEKNLEP GKQISRSSGE QQNKGRIVSP SLLSEEPLAP SSIDAESNGE
560 570 580 590 600
QPEELTLEEE SPVSQLFELE IEALPLDTPS SVETDISSSR KQSEEPFTTV
610 620 630 640 650
LENGAGMVSS TSFNGGVSPH NWGDSGPPCK KSRKEKKQTG SGPLGNSYVE
660 670 680
RQSPAVPNPP FTASSAWYLQ DKCGHTMRSR RDHRALRL
Note: Markedly decreased affinity for PML and TP53/p53, unable to repress p53-mediated transcription.1 Publication
Show »<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"Daxx-beta and Daxx-gamma, two novel splice variants of the transcriptional co-repressor Daxx."
Wethkamp N., Hanenberg H., Funke S., Suschek C.V., Wetzel W., Heikaus S., Grinstein E., Ramp U., Engers R., Gabbert H.E., Mahotka C.
J. Biol. Chem. 286:19576-19588(2011) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA), SUBCELLULAR LOCATION (ISOFORMS BETA AND GAMMA), ALTERNATIVE SPLICING.
Length:688
Mass (Da):76,326
<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:i3835917DA2147821
Isoform gamma (identifier: Q9UER7-5) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
648-682: YVERQRSVHEKNGKKICTLPSPPSPLASLAPVADS → PAVPNPPFTASSAWYLQDKCGHTMRSRRDHRALRL
683-740: Missing.
10 20 30 40 50
MATANSIIVL DDDDEDEAAA QPGPSHPLPN AASPGAEAPS SSEPHGARGS
60 70 80 90 100
SSSGGKKCYK LENEKLFEEF LELCKMQTAD HPEVVPFLYN RQQRAHSLFL
110 120 130 140 150
ASAEFCNILS RVLSRARSRP AKLYVYINEL CTVLKAHSAK KKLNLAPAAT
160 170 180 190 200
TSNEPSGNNP PTHLSLDPTN AENTASQSPR TRGSRRQIQR LEQLLALYVA
210 220 230 240 250
EIRRLQEKEL DLSELDDPDS AYLQEARLKR KLIRLFGRLC ELKDCSSLTG
260 270 280 290 300
RVIEQRIPYR GTRYPEVNRR IERLINKPGP DTFPDYGDVL RAVEKAAARH
310 320 330 340 350
SLGLPRQQLQ LMAQDAFRDV GIRLQERRHL DLIYNFGCHL TDDYRPGVDP
360 370 380 390 400
ALSDPVLARR LRENRSLAMS RLDEVISKYA MLQDKSEEGE RKKRRARLQG
410 420 430 440 450
TSSHSADTPE ASLDSGEGPS GMASQGCPSA SRAETDDEDD EESDEEEEEE
460 470 480 490 500
EEEEEEEATD SEEEEDLEQM QEGQEDDEEE DEEEEAAAGK DGDKSPMSSL
510 520 530 540 550
QISNEKNLEP GKQISRSSGE QQNKGRIVSP SLLSEEPLAP SSIDAESNGE
560 570 580 590 600
QPEELTLEEE SPVSQLFELE IEALPLDTPS SVETDISSSR KQSEEPFTTV
610 620 630 640 650
LENGAGMVSS TSFNGGVSPH NWGDSGPPCK KSRKEKKQTG SGPLGNSPAV
660 670 680
PNPPFTASSA WYLQDKCGHT MRSRRDHRAL RL
Note: Markedly decreased affinity for PML and TP53/p53, unable to repress p53-mediated transcription.1 Publication
Show »<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"Daxx-beta and Daxx-gamma, two novel splice variants of the transcriptional co-repressor Daxx."
Wethkamp N., Hanenberg H., Funke S., Suschek C.V., Wetzel W., Heikaus S., Grinstein E., Ramp U., Engers R., Gabbert H.E., Mahotka C.
J. Biol. Chem. 286:19576-19588(2011) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA), SUBCELLULAR LOCATION (ISOFORMS BETA AND GAMMA), ALTERNATIVE SPLICING.
Length:682
Mass (Da):75,563
<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:i080438D150FCEF3A
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 177 | Q → R in AAB66585 (PubMed:9407001).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 263 | R → H in AAC72843 (PubMed:10698492).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 323 | R → W in AAB66585 (PubMed:9407001).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 365 | R → Q in AAB66585 (PubMed:9407001).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 382 | L → S in AAB66585 (PubMed:9407001).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 505 | E → G in BAG64795 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 647 | S → R in CAB09986 (PubMed:14574404).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 647 | S → R in CAB09989 (PubMed:14574404).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 722 | T → A in CAB09986 (PubMed:14574404).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 722 | T → A in CAB09989 (PubMed:14574404).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 731 – 732 | EE → KK in AAC72843 (PubMed:10698492).Curated | 2 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_045588 | 1 – 75 | Missing in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 75 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_057437 | 648 – 682 | YVERQ…PVADS → PAVPNPPFTASSAWYLQDKC GHTMRSRRDHRALRL in isoform gamma. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 35 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_057438 | 653 – 688 | RSVHE…TRVDS → SPAVPNPPFTASSAWYLQDK CGHTMRSRRDHRALRL in isoform beta. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 36 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_057439 | 683 – 740 | Missing in isoform gamma. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 58 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_057440 | 689 – 740 | Missing in isoform beta. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 52 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_001270 | 696 – 740 | SSLCI…LSDSD → PAKNLGRRRSKQDQG in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 45 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF039136 mRNA Translation: AAB92671.1 AF006041 mRNA Translation: AAB63043.1 AF015956 mRNA Translation: AAB66585.2 AF050179 mRNA Translation: AAC39853.1 AF097742 mRNA Translation: AAC72843.1 HQ436528 mRNA Translation: AEC33235.1 HQ436529 mRNA Translation: AEC33236.1 AB015051 mRNA Translation: BAA34295.1 AK303854 mRNA Translation: BAG64795.1 CR457085 mRNA Translation: CAG33366.1 AL662827 Genomic DNA Translation: CAI17527.1 AL662820 Genomic DNA Translation: CAI18124.1 BX248088 Genomic DNA Translation: CAI41788.1 CR759793 Genomic DNA No translation available. CR759817 Genomic DNA Translation: CAQ08035.1 CR759786 Genomic DNA Translation: CAQ08265.1 Z97183, Z97184 Genomic DNA Translation: CAB09986.2 Z97184, Z97183 Genomic DNA Translation: CAB09989.2 CH471081 Genomic DNA Translation: EAX03722.1 BC000220 mRNA Translation: AAH00220.1 BC109073 mRNA Translation: AAI09074.1 BC109074 mRNA Translation: AAI09075.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS4776.1 [Q9UER7-1] CCDS59008.1 [Q9UER7-3] |
Protein sequence database of the Protein Information Resource More...PIRi | T03847 |
NCBI Reference Sequences More...RefSeqi | NP_001135441.1, NM_001141969.1 [Q9UER7-1] NP_001241646.1, NM_001254717.1 [Q9UER7-3] NP_001341.1, NM_001350.4 [Q9UER7-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.336916 |
Genome annotation databases
<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>Keywords - Coding sequence diversityi
Alternative splicing<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
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9UER7 | DAXX | 740 | |||
| Uncharacterized protein | 824 | ||||
| Uncharacterized protein | 823 | ||||
| Death-domain associated protein | 754 | ||||
| UPI00083C067E | 752 | ||||
| +52 | |||||
| Q9UER7-4 | UPI00045DECD6 | 810 | |||
| Death domain associated protein | 750 | ||||
| UPI000533E1AF | 749 | ||||
| DAXX isoform 1 | 743 | ||||
| Death domain-associated protein 6 (Fragment) | 48 | ||||
| +12 | |||||
| Q9UER7-5 | UPI00045DECD6 | 810 | |||
| Death domain associated protein | 750 | ||||
| UPI000533E1AF | 749 | ||||
| DAXX isoform 1 | 743 | ||||
| Death domain-associated protein 6 (Fragment) | 48 | ||||
| +12 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9UER7 | DAXX | 740 | |||
| Uncharacterized protein | 824 | ||||
| Uncharacterized protein | 823 | ||||
| Death-domain associated protein | 754 | ||||
| UPI0005334F65 | 752 | ||||
| +203 | |||||
<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
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Atlas of Genetics and Cytogenetics in Oncology and Haematology |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF039136 mRNA Translation: AAB92671.1 AF006041 mRNA Translation: AAB63043.1 AF015956 mRNA Translation: AAB66585.2 AF050179 mRNA Translation: AAC39853.1 AF097742 mRNA Translation: AAC72843.1 HQ436528 mRNA Translation: AEC33235.1 HQ436529 mRNA Translation: AEC33236.1 AB015051 mRNA Translation: BAA34295.1 AK303854 mRNA Translation: BAG64795.1 CR457085 mRNA Translation: CAG33366.1 AL662827 Genomic DNA Translation: CAI17527.1 AL662820 Genomic DNA Translation: CAI18124.1 BX248088 Genomic DNA Translation: CAI41788.1 CR759793 Genomic DNA No translation available. CR759817 Genomic DNA Translation: CAQ08035.1 CR759786 Genomic DNA Translation: CAQ08265.1 Z97183, Z97184 Genomic DNA Translation: CAB09986.2 Z97184, Z97183 Genomic DNA Translation: CAB09989.2 CH471081 Genomic DNA Translation: EAX03722.1 BC000220 mRNA Translation: AAH00220.1 BC109073 mRNA Translation: AAI09074.1 BC109074 mRNA Translation: AAI09075.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS4776.1 [Q9UER7-1] CCDS59008.1 [Q9UER7-3] |
Protein sequence database of the Protein Information Resource More...PIRi | T03847 |
NCBI Reference Sequences More...RefSeqi | NP_001135441.1, NM_001141969.1 [Q9UER7-1] NP_001241646.1, NM_001254717.1 [Q9UER7-3] NP_001341.1, NM_001350.4 [Q9UER7-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.336916 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2KQS | NMR | - | B | 721-740 | [»] | |
| 2KZS | NMR | - | A | 55-144 | [»] | |
| 2KZU | NMR | - | A | 55-144 | [»] | |
| 4H9N | X-ray | 1.95 | C | 178-389 | [»] | |
| 4H9O | X-ray | 2.05 | C | 178-389 | [»] | |
| 4H9P | X-ray | 2.20 | C | 178-389 | [»] | |
| 4H9Q | X-ray | 1.95 | C | 178-389 | [»] | |
| 4H9R | X-ray | 2.20 | C | 178-389 | [»] | |
| 4H9S | X-ray | 2.60 | E/F | 183-398 | [»] | |
| 4HGA | X-ray | 2.80 | A | 184-390 | [»] | |
| 5GRQ | X-ray | 1.58 | A | 55-144 | [»] | |
| B | 55-143 | [»] | ||||
| 5KDM | X-ray | 3.50 | C | 178-389 | [»] | |
| 5Y6O | X-ray | 3.10 | A/B/C/D/E/F/G/H/I | 50-144 | [»] | |
Database of protein disorder More...DisProti | DP00707 | |||||
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9UER7 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9UER7 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 107985, 235 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q9UER7 |
Database of interacting proteins More...DIPi | DIP-27628N |
Protein interaction database and analysis system More...IntActi | Q9UER7, 124 interactors |
Molecular INTeraction database More...MINTi | Q9UER7 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000266000 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9UER7 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9UER7 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | DAXX |
Domain mapping of disease mutations (DMDM) More...DMDMi | 24636785 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9UER7 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9UER7 |
PeptideAtlas More...PeptideAtlasi | Q9UER7 |
PRoteomics IDEntifications database More...PRIDEi | Q9UER7 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 84150 84151 [Q9UER7-2] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 1616 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 1616 |
DisGeNET More...DisGeNETi | 1616 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000204209.10 |
GeneCards: human genes, protein and diseases More...GeneCardsi | DAXX |
Human Gene Nomenclature Database More...HGNCi | HGNC:2681 DAXX |
Human Protein Atlas More...HPAi | CAB002224 CAB025546 HPA008736 HPA008797 HPA065779 |
MalaCards human disease database More...MalaCardsi | DAXX |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 603186 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9UER7 |
Open Targets More...OpenTargetsi | ENSG00000204209 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA27148 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IGIP Eukaryota ENOG4111K0B LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000009448 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000112148 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG031495 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9UER7 |
KEGG Orthology (KO) More...KOi | K02308 |
Identification of Orthologs from Complete Genome Data More...OMAi | LCKTQTA |
Database of Orthologous Groups More...OrthoDBi | EOG09370P3D |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9UER7 |
TreeFam database of animal gene trees More...TreeFami | TF325803 |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.7.7.19 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-6804757 Regulation of TP53 Degradation |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q9UER7 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q9UER7 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | DAXX human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9UER7 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Death-associated_protein_6 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 1616 |
Protein Ontology More...PROi | PR:Q9UER7 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000204209 |
CleanEx database of gene expression profiles More...CleanExi | HS_DAXX |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9UER7 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9UER7 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd13151 DAXX_helical_bundle, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.8.810, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR005012 Daxx IPR031333 Daxx_N IPR038298 Daxx_N_sf |
The PANTHER Classification System More...PANTHERi | PTHR12766 PTHR12766, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF03344 Daxx, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | 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 namei | DAXX_HUMAN | |
| <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>Accessioni | Q9UER7Primary (citable) accession number: Q9UER7 Secondary accession number(s): B4E1I3 , F5ANJ6, F5ANJ7, F5H082, O14747, O15141, O15208, Q5STK9, Q9BWI3 | |
| <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 historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 2002 |
| Last sequence update: | November 1, 2002 | |
| Last modified: | June 20, 2018 | |
| This is version 183 of the entry and version 2 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 statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any 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. | |
<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
<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>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 6
Human chromosome 6: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
