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Protein

ATP-dependent RNA helicase A

Gene

DHX9

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>

<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

Multifunctional ATP-dependent nucleic acid helicase that unwinds DNA and RNA in a 3' to 5' direction and that plays important roles in many processes, such as DNA replication, transcriptional activation, post-transcriptional RNA regulation, mRNA translation and RNA-mediated gene silencing (PubMed:9111062, PubMed:11416126, PubMed:12711669, PubMed:15355351, PubMed:16680162, PubMed:17531811, PubMed:20669935, PubMed:21561811, PubMed:24049074, PubMed:25062910, PubMed:24990949, PubMed:28221134). Requires a 3'-single-stranded tail as entry site for acid nuclei unwinding activities as well as the binding and hydrolyzing of any of the four ribo- or deoxyribo-nucleotide triphosphates (NTPs) (PubMed:1537828). Unwinds numerous nucleic acid substrates such as double-stranded (ds) DNA and RNA, DNA:RNA hybrids, DNA and RNA forks composed of either partially complementary DNA duplexes or DNA:RNA hybrids, respectively, and also DNA and RNA displacement loops (D- and R-loops), triplex-helical DNA (H-DNA) structure and DNA and RNA-based G-quadruplexes (PubMed:20669935, PubMed:21561811, PubMed:24049074). Binds dsDNA, single-stranded DNA (ssDNA), dsRNA, ssRNA and poly(A)-containing RNA (PubMed:9111062, PubMed:10198287). Binds also to circular dsDNA or dsRNA of either linear and/or circular forms and stimulates the relaxation of supercoiled DNAs catalyzed by topoisomerase TOP2A (PubMed:12711669). Plays a role in DNA replication at origins of replication and cell cycle progression (PubMed:24990949). Plays a role as a transcriptional coactivator acting as a bridging factor between polymerase II holoenzyme and transcription factors or cofactors, such as BRCA1, CREBBP, RELA and SMN1 (PubMed:11149922, PubMed:9323138, PubMed:9662397, PubMed:11038348, PubMed:11416126, PubMed:15355351, PubMed:28221134). Binds to the CDKN2A promoter (PubMed:11038348). Plays several roles in post-transcriptional regulation of gene expression (PubMed:28221134, PubMed:28355180). In cooperation with NUP98, promotes pre-mRNA alternative splicing activities of a subset of genes (PubMed:11402034, PubMed:16680162, PubMed:28221134, PubMed:28355180). As component of a large PER complex, is involved in the negative regulation of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms (By similarity). Acts also as a nuclear resolvase that is able to bind and neutralize harmful massive secondary double-stranded RNA structures formed by inverted-repeat Alu retrotransposon elements that are inserted and transcribed as parts of genes during the process of gene transposition (PubMed:28355180). Involved in the positive regulation of nuclear export of constitutive transport element (CTE)-containing unspliced mRNA (PubMed:9162007, PubMed:10924507, PubMed:11402034). Component of the coding region determinant (CRD)-mediated complex that promotes cytoplasmic MYC mRNA stability (PubMed:19029303). Plays a role in mRNA translation (PubMed:28355180). Positively regulates translation of selected mRNAs through its binding to post-transcriptional control element (PCE) in the 5'-untranslated region (UTR) (PubMed:16680162). Involved with LARP6 in the translation stimulation of type I collagen mRNAs for CO1A1 and CO1A2 through binding of a specific stem-loop structure in their 5'-UTRs (PubMed:22190748). Stimulates LIN28A-dependent mRNA translation probably by facilitating ribonucleoprotein remodeling during the process of translation (PubMed:21247876). Plays also a role as a small interfering (siRNA)-loading factor involved in the RNA-induced silencing complex (RISC) loading complex (RLC) assembly, and hence functions in the RISC-mediated gene silencing process (PubMed:17531811). Binds preferentially to short double-stranded RNA, such as those produced during rotavirus intestinal infection (PubMed:28636595). This interaction may mediate NLRP9 inflammasome activation and trigger inflammatory response, including IL18 release and pyroptosis (PubMed:28636595). Finally, mediates the attachment of heterogeneous nuclear ribonucleoproteins (hnRNPs) to actin filaments in the nucleus (PubMed:11687588).By similarity27 Publications
(Microbial infection) Plays a role in HIV-1 replication and virion infectivity (PubMed:11096080, PubMed:19229320, PubMed:25149208, PubMed:27107641). Enhances HIV-1 transcription by facilitating the binding of RNA polymerase II holoenzyme to the proviral DNA (PubMed:11096080, PubMed:25149208). Binds (via DRBM domain 2) to the HIV-1 TAR RNA and stimulates HIV-1 transcription of transactivation response element (TAR)-containing mRNAs (PubMed:9892698, PubMed:11096080). Involved also in HIV-1 mRNA splicing and transport (PubMed:25149208). Positively regulates HIV-1 gag mRNA translation, through its binding to post-transcriptional control element (PCE) in the 5'-untranslated region (UTR) (PubMed:16680162). Binds (via DRBM domains) to a HIV-1 double-stranded RNA region of the primer binding site (PBS)-segment of the 5'-UTR, and hence stimulates DHX9 incorporation into virions and virion infectivity (PubMed:27107641). Plays also a role as a cytosolic viral MyD88-dependent DNA and RNA sensors in plasmacytoid dendritic cells (pDCs), and hence induce antiviral innate immune responses (PubMed:20696886, PubMed:21957149). Binds (via the OB-fold region) to viral single-stranded DNA unmethylated C-phosphate-G (CpG) oligonucleotide (PubMed:20696886).8 Publications

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi418ManganeseCombined sources1 Publication1
Metal bindingi512ManganeseCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi411 – 419ATPCombined sources2 Publications9

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

GO - Biological processi

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

Molecular functionActivator, DNA-binding, Helicase, Hydrolase, RNA-binding
Biological processBiological rhythms, DNA replication, Immunity, Inflammatory response, Innate immunity, mRNA processing, mRNA splicing, mRNA transport, RNA-mediated gene silencing, Transcription, Transcription regulation, Transcription termination, Translation regulation, Transport
LigandATP-binding, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.6.4.13 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1810476 RIP-mediated NFkB activation via ZBP1
R-HSA-3134963 DEx/H-box helicases activate type I IFN and inflammatory cytokines production
R-HSA-72163 mRNA Splicing - Major Pathway

<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:
ATP-dependent RNA helicase ACurated (EC:3.6.4.137 Publications)
Alternative name(s):
DEAH box protein 9
DExH-box helicase 9Imported
Leukophysin1 Publication
Short name:
LKP1 Publication
Nuclear DNA helicase II3 Publications
Short name:
NDH II2 Publications
RNA helicase A1 Publication
<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:DHX9Imported
Synonyms:DDX9Imported, LKP, NDH2
<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>OrganismiHomo 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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000135829.16

Human Gene Nomenclature Database

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HGNCi
HGNC:2750 DHX9

Online Mendelian Inheritance in Man (OMIM)

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MIMi
603115 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q08211

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, 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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi5K → A: Reduces siRNA-binding and interaction with AGO2; when associated with A-6. 1 Publication1
Mutagenesisi6N → A: Reduces siRNA-binding; when associated with A-5. 1 Publication1
Mutagenesisi9Y → A: Inhibits siRNA-binding and interaction with AGO2. 1 Publication1
Mutagenesisi30N → A: Does not reduce siRNA-binding and interaction with AGO2. 1 Publication1
Mutagenesisi53N → A: Inhibits siRNA-binding and decreases interaction with AGO2; when associated with A-54 and A-55. 1 Publication1
Mutagenesisi54K → A: Inhibits siRNA-binding and decreases interaction with AGO2; when associated with A-53 and A-55. 1 Publication1
Mutagenesisi55K → A: Inhibits siRNA-binding and decreases interaction with AGO2; when associated with A-53 and A-54. 1 Publication1
Mutagenesisi182K → A: Reduces siRNA-binding and interaction with AGO2. 1 Publication1
Mutagenesisi186N → A: Reduces siRNA-binding and interaction with AGO2; when associated with A-187. 1 Publication1
Mutagenesisi187Q → A: Reduces siRNA-binding and interaction with AGO2; when associated with A-186. 1 Publication1
Mutagenesisi207H → A: Reduces siRNA-binding and interaction with AGO2. 1 Publication1
Mutagenesisi234N → A: Inhibits siRNA-binding and interaction with AGO2; when associated with A-235 and A-236. 1 Publication1
Mutagenesisi235K → A: Inhibits siRNA-binding and interaction with AGO2; when associated with A-234 and A-236. 1 Publication1
Mutagenesisi236K → A: Inhibits siRNA-binding and interaction with AGO2; when associated with A-234 and A-235. 1 Publication1
Mutagenesisi332W → A: Abrogates transcriptional activation by the MTAD region. No change in RNA polymerase II holoenzyme binding. 1 Publication1
Mutagenesisi339W → A: Abrogates transcriptional activation and RNA polymerase II binding by the MTAD region. No change in ATP binding and ATPase activities. 1 Publication1
Mutagenesisi342W → A: Abrogates transcriptional activation by the MTAD region. No change in RNA polymerase II holoenzyme binding. 1 Publication1
Mutagenesisi347I → A: Reduces NUP98-induced mRNA transcription and alternative splicing activities. 1 Publication1
Mutagenesisi417K → R or N: Inhibits interaction with AGO2, DICER1 and TARBP2. Abrogates helicase activity and transcriptional activation. Does not inhibit binding to origins of DNA replication. 4 Publications1
Mutagenesisi417K → R: Reduces NUP98-induced mRNA transcription and alternative splicing activities. 1 Publication1
Mutagenesisi511D → A: Does not inhibit binding to origins of DNA replication; when associated with A-512. 1 Publication1
Mutagenesisi512E → A: Does not inhibit binding to origins of DNA replication; when associated with A-511. 1 Publication1
Mutagenesisi543S → L: Does not inhibit binding to origins of DNA replication. 1 Publication1
Mutagenesisi1160R → A: Localizes in the nucleus and interacts with the importin complex. 1 Publication1
Mutagenesisi1163K → A: Localizes in the cytoplasm and does not interact with the importin complex. 1 Publication1
Mutagenesisi1163Missing : Abolishes nuclear localization. 1 Publication1
Mutagenesisi1166R → A: Localizes in the nucleus and the cytoplasm and interacts weakly with the importin complex. 1 Publication1
Mutagenesisi1166R → L: Abolishes nuclear localization. 1 Publication1
Mutagenesisi1166Missing : Abolishes nuclear localization. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
1660

Open Targets

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OpenTargetsi
ENSG00000135829

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27232

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
DHX9

Domain mapping of disease mutations (DMDM)

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DMDMi
116241330

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000551571 – 1270ATP-dependent RNA helicase AAdd BLAST1270

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei87PhosphoserineCombined sources1
Modified residuei125PhosphoserineCombined sources1
Modified residuei146N6-acetyllysine; alternateBy similarity1
Modified residuei146N6-methyllysine; alternateCombined sources1
Modified residuei191N6-acetyllysineCombined sources1
Modified residuei199N6-acetyllysineCombined sources1
Modified residuei321PhosphoserineCombined sources1
Modified residuei449PhosphoserineCombined sources1
Modified residuei506PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki697Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1024N6-acetyllysineCombined sources1
Modified residuei1166Asymmetric dimethylarginineBy similarity1
Modified residuei1175Omega-N-methylarginineCombined sources1
Modified residuei1219Asymmetric dimethylarginineBy similarity1
Modified residuei1235Asymmetric dimethylarginineBy similarity1
Modified residuei1242Asymmetric dimethylarginineBy similarity1
Modified residuei1249Asymmetric dimethylarginineBy similarity1
Modified residuei1265Asymmetric dimethylarginineBy similarity1

<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

Methylated (PubMed:15084609). PRMT1-mediated methylation of undefined Arg residues in the RGG region is required for nuclear import of DHX9 (PubMed:15084609).1 Publication
Phosphorylated by PRKDC; phosphorylation occurs in a RNA-dependent manner (PubMed:14704337). Phosphorylated by EIF2AK2/PKR; this phosphorylation reduces its association with double-stranded RNA (PubMed:19229320).2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q08211

MaxQB - The MaxQuant DataBase

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MaxQBi
Q08211

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q08211

PeptideAtlas

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PeptideAtlasi
Q08211

PRoteomics IDEntifications database

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PRIDEi
Q08211

ProteomicsDB human proteome resource

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ProteomicsDBi
58582
58583 [Q08211-2]

Consortium for Top Down Proteomics

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TopDownProteomicsi
Q08211-1 [Q08211-1]

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
Q08211

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q08211

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q08211

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q08211

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
Q08211

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000135829 Expressed in 237 organ(s), highest expression level in kidney

CleanEx database of gene expression profiles

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CleanExi
HS_DHX9

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q08211 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB011819
HPA028050
HPA055684

<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

Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1 (PubMed:19029303). Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1 (PubMed:19029303). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active) (By similarity). Associates (via DRBM domains) with the RISC complex; this association occurs in a small interfering (siRNA)-dependent manner (PubMed:17531811, PubMed:23361462). Associates with the SMN complex; this association induces recruitment of DHX9 to the RNA polymerase II (ref.8). Associates with polysomes in a LIN28A-dependent manner (PubMed:16680162, PubMed:21247876). Interacts (via C-terminus) with ACTB; this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes (PubMed:11687588). Interacts with ADAR isoform 1; this interaction occurs in a RNA-independent manner (PubMed:28355180). Interacts (via DRBM domains) with AGO2 (via middle region); this interaction promotes active RISC assembly by promoting the association of siRNA with AGO2 (PubMed:17531811, PubMed:23361462). Interacts (via RGG region) with AKAP8L (via N-terminus) (PubMed:11402034). Interacts with BRCA1 (via C-terminus); this interaction is direct and links BRCA1 to the RNA polymerase II holoenzyme (PubMed:9662397). Interacts (via N-terminus) with CREBBP; this interaction mediates association with RNA polymerase II holoenzyme and stimulates CREB-dependent transcriptional activation (PubMed:9323138). Interacts (via N-terminus) with EIF2AK2/PKR; this interaction is dependent upon the activation of the kinase (PubMed:19229320). Interacts (via DRBM domains) with DICER1 (PubMed:17531811). Interacts with H2AFX; this interaction is direct, requires phosphorylation of histone H2AFX on 'Ser-140' by PRKDC and promotes binding of DHX9 to transcriptionally stalled sites on chromosomal DNA in response to genotoxic stress (PubMed:15613478, PubMed:17498979). Interacts with HNRNPC; this interaction is direct, enhanced probably by their concomitant binding to RNA and mediates the attachment to actin filaments (PubMed:11687588). Interacts (via RGG region) with PRMT1 (PubMed:15084609). Interacts with IGF2BP1 (PubMed:17289661, PubMed:23640942). Interacts with IGF2BP2, IGF2BP3 (PubMed:23640942). Interacts (via DRBM domains) with ILF3; this interaction occurs in a RNA-independent manner (PubMed:12946349). Interacts with Importin alpha/Importin beta receptor (PubMed:16375861). Interacts with LARP6 (via C-terminus); this interaction occurs in a mRNA-independent manner (PubMed:22190748). Interacts (via N- and C-terminus) with LIN28A (via C-terminus); this interaction occurs in a RNA-independent manner (PubMed:21247876). Interacts with LMX1B (PubMed:23308148). Interacts (via helicase C-terminal domain, HA2 and OB-fold regions) with MAVS (via CARD domain); this interaction occurs in both resting and double-stranded RNA poly(I:C)-induced cells (PubMed:21957149). Interacts with MBD2; this interaction stimulates transcriptional activation in a CREB-dependent manner (PubMed:12665568). Interacts (via H2A and OB-fold regions) with MYD88 (via TIR domain); this interaction is direct (PubMed:20696886). Interacts with NLRP9 upon rotavirus infection; this interaction may trigger NLRP9 inflammasome activation and inflammatory response (PubMed:28636595). Interacts (via DRBM, OB-fold and RGG regions) with NUP98 (via N-terminus); this interaction occurs in a RNA-dependent manner and stimulates DHX9-mediated ATPase activity and regulates transcription and splicing of a subset of genes (PubMed:28221134). Interacts (via N-terminus) with NXF1 (via N-terminus); this interaction is direct and negatively regulates NXF1-mediated nuclear export of constitutive transport element (CTE)-containing cellular mRNAs (PubMed:10924507). Interacts with RELA; this interaction is direct and activates NF-kappa-B-mediated transcription (PubMed:15355351). Interacts (via MTAD region) with RNA polymerase II holoenzyme; this interaction stimulates transcription activation in a CREB-dependent manner (PubMed:11149922, PubMed:9323138, PubMed:11416126). Interacts (via RGG region) with SMN1; this interaction links SMN1 to the RNA polymerase II holoenzyme (PubMed:11149922). Interacts with SP7 (PubMed:17303075). Interacts (via DRBM domains) with TARBP2 (via DRBM first and second domains); this interaction occurs in a small interfering (siRNA)-dependent manner (PubMed:17531811, PubMed:23361462). Interacts with TOP2A; this interaction occurs in a E2 enzyme UBE2I- and RNA-dependent manner, negatively regulates DHX9-mediated double-stranded DNA and RNA duplex helicase activity and stimulates TOP2A-mediated supercoiled DNA relaxation activity (PubMed:12711669). Interacts (via DRBM domains and C-terminus) with WRN (via 3'-5' exonuclease domain); this interaction inhibits the DNA-dependent NTPase and DNA helicase activities of DHX9 and stimulates the 3'-5' exonuclease activity of WRN (PubMed:15995249). Interacts with XRCC5; this interaction occurs in a RNA-dependent manner (PubMed:14704337). Interacts with ZIC2 (via C2H2-type domain 3) (PubMed:17251188).By similarity34 Publications

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
108025, 248 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1080 CRD-mediated mRNA stability complex

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q08211

Database of interacting proteins

More...
DIPi
DIP-31504N

Protein interaction database and analysis system

More...
IntActi
Q08211, 83 interactors

Molecular INTeraction database

More...
MINTi
Q08211

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000356520

<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

11270
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q08211

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q08211

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini3 – 71DRBM 1PROSITE-ProRule annotation2 PublicationsAdd BLAST69
Domaini180 – 252DRBM 2PROSITE-ProRule annotation2 PublicationsAdd BLAST73
Domaini398 – 564Helicase ATP-bindingPROSITE-ProRule annotation1 PublicationAdd BLAST167
Domaini636 – 809Helicase C-terminalPROSITE-ProRule annotationAdd BLAST174

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 250Interaction with CREBBP1 PublicationAdd BLAST250
Regioni5 – 9siRNA-bindingCombined sources1 Publication5
Regioni53 – 55siRNA-bindingCombined sources1 Publication3
Regioni182 – 186siRNA-bindingCombined sources1 Publication5
Regioni230 – 325Interaction with BRCA11 PublicationAdd BLAST96
Regioni234 – 236siRNA-binding1 Publication3
Regioni255 – 664Necessary for interaction with RNA polymerase II holoenzyme1 PublicationAdd BLAST410
Regioni313 – 952Necessary for interaction with H2AFX1 PublicationAdd BLAST640
Regioni331 – 380MTAD1 PublicationAdd BLAST50
Regioni398 – 809Core helicase1 PublicationAdd BLAST412
Regioni831 – 919HA21 PublicationAdd BLAST89
Regioni958 – 1074OB-fold3 PublicationsAdd BLAST117
Regioni1150 – 1270RGG4 PublicationsAdd BLAST121

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi511 – 514DEIH box4
Motifi586 – 595Nuclear localization signal (NLS1)Sequence analysis10
Motifi1155 – 1173Nuclear localization signal (NLS2)1 PublicationAdd BLAST19

<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

DRBM domains cooperate for the binding to nucleic acid but not for unwinding helicase activity (PubMed:9111062, PubMed:25062910). The helicase-associated domain-2 (HA2) region is essential for the duplex RNA unwinding helicase activity (PubMed:25062910). The minimal transactivation region (MTAD) mediates interaction with the RNA polymerase II holoenzyme and stimulates transcriptional activation in a CREB-dependent manner (PubMed:11416126). The oligonucleotide- or oligosaccharide-binding (OB-fold) and the repeated arginine and glycine-glycine (RGG) regions are dispensable for both RNA-binding and unwinding helicase activities (PubMed:25062910). The RGG region contains both nuclear localization signal (NLS) and nuclear export signal (NES) and is necessary and sufficient for nucleocytoplasmic shuttling in a RNA-independent manner (PubMed:10207077, PubMed:11149922).5 Publications

<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

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0920 Eukaryota
COG1643 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155924

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000247063

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG039429

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q08211

KEGG Orthology (KO)

More...
KOi
K13184

Identification of Orthologs from Complete Genome Data

More...
OMAi
HARSFMA

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0PKT

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q08211

TreeFam database of animal gene trees

More...
TreeFami
TF313601

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00048 DSRM, 2 hits
cd00079 HELICc, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011545 DEAD/DEAH_box_helicase_dom
IPR002464 DNA/RNA_helicase_DEAH_CS
IPR014720 dsRBD_dom
IPR011709 DUF1605
IPR007502 Helicase-assoc_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00270 DEAD, 1 hit
PF00035 dsrm, 2 hits
PF04408 HA2, 1 hit
PF00271 Helicase_C, 1 hit
PF07717 OB_NTP_bind, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00487 DEXDc, 1 hit
SM00358 DSRM, 2 hits
SM00847 HA2, 1 hit
SM00490 HELICc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00690 DEAH_ATP_HELICASE, 1 hit
PS50137 DS_RBD, 2 hits
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)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 2 <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 basket
Isoform 1 (identifier: Q08211-1) [UniParc]FASTAAdd to basket

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

« Hide
        10         20         30         40         50
MGDVKNFLYA WCGKRKMTPS YEIRAVGNKN RQKFMCEVQV EGYNYTGMGN
60 70 80 90 100
STNKKDAQSN AARDFVNYLV RINEIKSEEV PAFGVASPPP LTDTPDTTAN
110 120 130 140 150
AEGDLPTTMG GPLPPHLALK AENNSEVGAS GYGVPGPTWD RGANLKDYYS
160 170 180 190 200
RKEEQEVQAT LESEEVDLNA GLHGNWTLEN AKARLNQYFQ KEKIQGEYKY
210 220 230 240 250
TQVGPDHNRS FIAEMTIYIK QLGRRIFARE HGSNKKLAAQ SCALSLVRQL
260 270 280 290 300
YHLGVVEAYS GLTKKKEGET VEPYKVNLSQ DLEHQLQNII QELNLEILPP
310 320 330 340 350
PEDPSVPVAL NIGKLAQFEP SQRQNQVGVV PWSPPQSNWN PWTSSNIDEG
360 370 380 390 400
PLAFATPEQI SMDLKNELMY QLEQDHDLQA ILQERELLPV KKFESEILEA
410 420 430 440 450
ISQNSVVIIR GATGCGKTTQ VPQFILDDFI QNDRAAECNI VVTQPRRISA
460 470 480 490 500
VSVAERVAFE RGEEPGKSCG YSVRFESILP RPHASIMFCT VGVLLRKLEA
510 520 530 540 550
GIRGISHVIV DEIHERDINT DFLLVVLRDV VQAYPEVRIV LMSATIDTSM
560 570 580 590 600
FCEYFFNCPI IEVYGRTYPV QEYFLEDCIQ MTHFVPPPKD KKKKDKDDDG
610 620 630 640 650
GEDDDANCNL ICGDEYGPET RLSMSQLNEK ETPFELIEAL LKYIETLNVP
660 670 680 690 700
GAVLVFLPGW NLIYTMQKHL EMNPHFGSHR YQILPLHSQI PREEQRKVFD
710 720 730 740 750
PVPVGVTKVI LSTNIAETSI TINDVVYVID SCKQKVKLFT AHNNMTNYAT
760 770 780 790 800
VWASKTNLEQ RKGRAGRVRP GFCFHLCSRA RFERLETHMT PEMFRTPLHE
810 820 830 840 850
IALSIKLLRL GGIGQFLAKA IEPPPLDAVI EAEHTLRELD ALDANDELTP
860 870 880 890 900
LGRILAKLPI EPRFGKMMIM GCIFYVGDAI CTIAAATCFP EPFINEGKRL
910 920 930 940 950
GYIHRNFAGN RFSDHVALLS VFQAWDDARM GGEEAEIRFC EHKRLNMATL
960 970 980 990 1000
RMTWEAKVQL KEILINSGFP EDCLLTQVFT NTGPDNNLDV VISLLAFGVY
1010 1020 1030 1040 1050
PNVCYHKEKR KILTTEGRNA LIHKSSVNCP FSSQDMKYPS PFFVFGEKIR
1060 1070 1080 1090 1100
TRAISAKGMT LVTPLQLLLF ASKKVQSDGQ IVLVDDWIKL QISHEAAACI
1110 1120 1130 1140 1150
TGLRAAMEAL VVEVTKQPAI ISQLDPVNER MLNMIRQISR PSAAGINLMI
1160 1170 1180 1190 1200
GSTRYGDGPR PPKMARYDNG SGYRRGGSSY SGGGYGGGYS SGGYGSGGYG
1210 1220 1230 1240 1250
GSANSFRAGY GAGVGGGYRG VSRGGFRGNS GGDYRGPSGG YRGSGGFQRG
1260 1270
GGRGAYGTGY FGQGRGGGGY
Length:1,270
Mass (Da):140,958
Last modified:October 17, 2006 - v4
<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:iA607DA8F4C4B217A
GO
Isoform 2 (identifier: Q08211-2) [UniParc]FASTAAdd to basket
Also known as: Leukophysin, LKP

The sequence of this isoform differs from the canonical sequence as follows:
     1-1035: Missing.

Show »
Length:235
Mass (Da):24,336
Checksum:iB8A0D4E0C604A090
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 conflicti20S → T in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti108 – 109TM → HH in AAB48855 (PubMed:8344961).Curated2
Sequence conflicti114 – 116PPH → LHI in AAB48855 (PubMed:8344961).Curated3
Sequence conflicti186N → I in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti260S → T in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti478I → V in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti521D → S in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti541L → F in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti560 – 565IIEVYG → SLKLW in AAB48855 (PubMed:8344961).Curated6
Sequence conflicti590D → K in AAH25245 (PubMed:16710414).Curated1
Sequence conflicti749A → S in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti749A → S in CAA71668 (PubMed:9111062).Curated1
Sequence conflicti768 – 770VRP → STA in AAB48855 (PubMed:8344961).Curated3
Sequence conflicti768 – 770VRP → STA in CAA71668 (PubMed:9111062).Curated3
Sequence conflicti828A → G in AAI07882 (PubMed:16710414).Curated1
Sequence conflicti899R → Q in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti1037K → N in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti1063T → P in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti1063T → P in CAA71668 (PubMed:9111062).Curated1
Sequence conflicti1140R → E in AAB48855 (PubMed:8344961).Curated1
Sequence conflicti1204 – 1211NSFRAGYG → TPSGRIC in AAB48855 (PubMed:8344961).Curated8
Sequence conflicti1261 – 1270FGQGRGGGGY → LDIEEEVAAIKLGYVSSVCR Q in AAB48855 (PubMed:8344961).Curated10

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_052179894I → V1 PublicationCorresponds to variant dbSNP:rs1049264Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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_0423141 – 1035Missing in isoform 2. 2 PublicationsAdd BLAST1035

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L13848 mRNA Translation: AAB48855.1
U03643 mRNA Translation: AAA03571.1
Y10658 mRNA Translation: CAA71668.1
AB451248 mRNA Translation: BAG70062.1
AB451372 mRNA Translation: BAG70186.1
AL355999 Genomic DNA No translation available.
AL662837 Genomic DNA No translation available.
CH471067 Genomic DNA Translation: EAW91138.1
BC025245 mRNA Translation: AAH25245.1
BC058896 mRNA Translation: AAH58896.1
BC107881 mRNA Translation: AAI07882.1
BC137136 mRNA Translation: AAI37137.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS41444.1 [Q08211-1]

NCBI Reference Sequences

More...
RefSeqi
NP_001348.2, NM_001357.4 [Q08211-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.191518

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000367549; ENSP00000356520; ENSG00000135829 [Q08211-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1660

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1660

UCSC genome browser

More...
UCSCi
uc001gpr.4 human [Q08211-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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

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

<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:
EMBLi
GenBanki
DDBJi
Links Updated
L13848 mRNA Translation: AAB48855.1
U03643 mRNA Translation: AAA03571.1
Y10658 mRNA Translation: CAA71668.1
AB451248 mRNA Translation: BAG70062.1
AB451372 mRNA Translation: BAG70186.1
AL355999 Genomic DNA No translation available.
AL662837 Genomic DNA No translation available.
CH471067 Genomic DNA Translation: EAW91138.1
BC025245 mRNA Translation: AAH25245.1
BC058896 mRNA Translation: AAH58896.1
BC107881 mRNA Translation: AAI07882.1
BC137136 mRNA Translation: AAI37137.1
CCDSiCCDS41444.1 [Q08211-1]
RefSeqiNP_001348.2, NM_001357.4 [Q08211-1]
UniGeneiHs.191518

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LLMX-ray2.80A/B329-563[»]
3VYXX-ray2.29A152-264[»]
3VYYX-ray2.90A/B1-91[»]
ProteinModelPortaliQ08211
SMRiQ08211
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108025, 248 interactors
ComplexPortaliCPX-1080 CRD-mediated mRNA stability complex
CORUMiQ08211
DIPiDIP-31504N
IntActiQ08211, 83 interactors
MINTiQ08211
STRINGi9606.ENSP00000356520

PTM databases

iPTMnetiQ08211
PhosphoSitePlusiQ08211
SwissPalmiQ08211

Polymorphism and mutation databases

BioMutaiDHX9
DMDMi116241330

2D gel databases

SWISS-2DPAGEiQ08211

Proteomic databases

EPDiQ08211
MaxQBiQ08211
PaxDbiQ08211
PeptideAtlasiQ08211
PRIDEiQ08211
ProteomicsDBi58582
58583 [Q08211-2]
TopDownProteomicsiQ08211-1 [Q08211-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367549; ENSP00000356520; ENSG00000135829 [Q08211-1]
GeneIDi1660
KEGGihsa:1660
UCSCiuc001gpr.4 human [Q08211-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1660
DisGeNETi1660
EuPathDBiHostDB:ENSG00000135829.16

GeneCards: human genes, protein and diseases

More...
GeneCardsi
DHX9

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0001404
HIX0149309
HGNCiHGNC:2750 DHX9
HPAiCAB011819
HPA028050
HPA055684
MIMi603115 gene
neXtProtiNX_Q08211
OpenTargetsiENSG00000135829
PharmGKBiPA27232

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0920 Eukaryota
COG1643 LUCA
GeneTreeiENSGT00940000155924
HOGENOMiHOG000247063
HOVERGENiHBG039429
InParanoidiQ08211
KOiK13184
OMAiHARSFMA
OrthoDBiEOG091G0PKT
PhylomeDBiQ08211
TreeFamiTF313601

Enzyme and pathway databases

BRENDAi3.6.4.13 2681
ReactomeiR-HSA-1810476 RIP-mediated NFkB activation via ZBP1
R-HSA-3134963 DEx/H-box helicases activate type I IFN and inflammatory cytokines production
R-HSA-72163 mRNA Splicing - Major Pathway

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
DHX9 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
RNA_Helicase_A

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
1660
PMAP-CutDBiQ08211

Protein Ontology

More...
PROi
PR:Q08211

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000135829 Expressed in 237 organ(s), highest expression level in kidney
CleanExiHS_DHX9
GenevisibleiQ08211 HS

Family and domain databases

CDDicd00048 DSRM, 2 hits
cd00079 HELICc, 1 hit
InterProiView protein in InterPro
IPR011545 DEAD/DEAH_box_helicase_dom
IPR002464 DNA/RNA_helicase_DEAH_CS
IPR014720 dsRBD_dom
IPR011709 DUF1605
IPR007502 Helicase-assoc_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00270 DEAD, 1 hit
PF00035 dsrm, 2 hits
PF04408 HA2, 1 hit
PF00271 Helicase_C, 1 hit
PF07717 OB_NTP_bind, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00358 DSRM, 2 hits
SM00847 HA2, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00690 DEAH_ATP_HELICASE, 1 hit
PS50137 DS_RBD, 2 hits
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiDHX9_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>AccessioniPrimary (citable) accession number: Q08211
Secondary accession number(s): B2RNV4
, Q05CI5, Q12803, Q32Q22, Q5VY62, Q6PD69, Q99556
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 17, 2006
Last modified: December 5, 2018
This is version 207 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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