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UniProtKB - Q28141 (DHX9_BOVIN)

Entry version 147 (07 Oct 2020)
Sequence version 1 (01 Nov 1997)
Previous versions | rss
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Protein

ATP-dependent RNA helicase A

Gene

DHX9

Organism
Bos taurus (Bovine)
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:7511411). 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:7511411). 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:7511411). Binds dsDNA, single-stranded DNA (ssDNA), dsRNA, ssRNA and poly(A)-containing RNA (PubMed:7511411). 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. Plays a role in DNA replication at origins of replication and cell cycle progression. 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. Binds to the CDKN2A promoter. Plays several roles in post-transcriptional regulation of gene expression. In cooperation with NUP98, promotes pre-mRNA alternative splicing activities of a subset of genes. 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. 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. Involved in the positive regulation of nuclear export of constitutive transport element (CTE)-containing unspliced mRNA. Component of the coding region determinant (CRD)-mediated complex that promotes cytoplasmic MYC mRNA stability. Plays a role in mRNA translation. Positively regulates translation of selected mRNAs through its binding to post-transcriptional control element (PCE) in the 5'-untranslated region (UTR). 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. Stimulates LIN28A-dependent mRNA translation probably by facilitating ribonucleoprotein remodeling during the process of translation. 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. Binds preferentially to short double-stranded RNA, such as those produced during rotavirus intestinal infection. This interaction may mediate NLRP9 inflammasome activation and trigger inflammatory response, including IL18 release and pyroptosis. Finally, mediates the attachment of heterogeneous nuclear ribonucleoproteins (hnRNPs) to actin filaments in the nucleus.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi415ManganeseBy similarity1
Metal bindingi509ManganeseBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi408 – 416ATPPROSITE-ProRule annotationBy similarity9

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

<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%5Fand%5Ftaxonomy%5Fsection">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 ABy similarity (EC:3.6.4.13By similarity)
Alternative name(s):
DEAH box protein 9By similarity
Nuclear DNA helicase IIBy similarity
Short name:
NDH IIBy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:DHX9By similarity
Synonyms:DDX9By similarity, NDH2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 16

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...VGNCi		VGNC:28060, DHX9

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000551561 – 1287ATP-dependent RNA helicase AAdd BLAST1287

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 residuei125PhosphoserineBy similarity1
Modified residuei143N6-acetyllysine; alternateBy similarity1
Modified residuei143N6-methyllysine; alternateBy similarity1
Modified residuei188N6-acetyllysineBy similarity1
Modified residuei196N6-acetyllysineBy similarity1
Modified residuei318PhosphoserineBy similarity1
Modified residuei446PhosphoserineBy similarity1
Modified residuei503PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki694Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1021N6-acetyllysineBy similarity1
Modified residuei1163Asymmetric dimethylarginineBy similarity1
Modified residuei1172Omega-N-methylarginineBy similarity1
Modified residuei1235Asymmetric dimethylarginineBy similarity1
Modified residuei1251Asymmetric dimethylarginineBy similarity1
Modified residuei1259Asymmetric dimethylarginineBy similarity1
Modified residuei1266Asymmetric dimethylarginineBy similarity1
Modified residuei1282Asymmetric dimethylarginineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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. PRMT1-mediated methylation of undefined Arg residues in the nuclear transport domain (NTD) is required for nuclear import of DHX9.By similarity
Phosphorylated by PRKDC; phosphorylation occurs in a RNA-dependent manner. Phosphorylated by EIF2AK2/PKR; this phosphorylation reduces its association with double-stranded RNA.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...PaxDbi		Q28141

PeptideAtlas

More...PeptideAtlasi		Q28141

PRoteomics IDEntifications database

More...PRIDEi		Q28141

<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

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q28141, baseline

<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%5Fsection">'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%5Fsection">'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.

Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1.

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active). Associates (via DRBM domains) with the RISC complex; this association occurs in a small interfering (siRNA)-dependent manner. Associates with the SMN complex; this association induces recruitment of DHX9 to the RNA polymerase II. Associates with polysomes in a LIN28A-dependent manner.

Interacts (via C-terminus) with ACTB; this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes.

Interacts with ADAR isoform 1; this interaction occurs in a RNA-independent manner.

Interacts (via DRBM domains) with AGO2 (via middle region); this interaction promotes active RISC assembly by promoting the association of siRNA with AGO2.

Interacts (via NTD domain) with AKAP8L (via N-terminus).

Interacts with BRCA1 (via C-terminus); this interaction is direct and links BRCA1 to the RNA polymerase II holoenzyme.

Interacts (via N-terminus) with CREBBP; this interaction mediates association with RNA polymerase II holoenzyme and stimulates CREB-dependent transcriptional activation.

Interacts (via N-terminus) with EIF2AK2/PKR; this interaction is dependent upon the activation of the kinase.

Interacts (via DRBM domains) with DICER1.

Interacts with H2AX; this interaction is direct, requires phosphorylation of histone H2AX by PRKDC and promotes binding of DHX9 to transcriptionally stalled sites on chromosomal DNA in response to genotoxic stress.

Interacts with HNRNPC; this interaction is direct, enhanced probably by their concomitant binding to RNA and mediates the attachment to actin filaments.

Interacts (via NTD domain) with PRMT1.

Interacts with IGF2BP1.

Interacts with IGF2BP2, IGF2BP3.

Interacts (via DRBM domains) with ILF3; this interaction occurs in a RNA-independent manner.

Interacts with Importin alpha/Importin beta receptor.

Interacts with LARP6 (via C-terminus); this interaction occurs in a mRNA-independent manner.

Interacts (via N- and C-terminus) with LIN28A (via C-terminus); this interaction occurs in a RNA-independent manner.

Interacts with LMX1B.

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.

Interacts with MBD2; this interaction stimulates transcriptional activation in a CREB-dependent manner.

Interacts (via H2A and OB-fold regions) with MYD88 (via TIR domain); this interaction is direct.

Interacts with NLRP9 upon rotavirus infection; this interaction may trigger NLRP9 inflammasome activation and inflammatory response.

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.

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.

Interacts with RELA; this interaction is direct and activates NF-kappa-B-mediated transcription.

Interacts (via MTAD region) with RNA polymerase II holoenzyme; this interaction stimulates transcription activation in a CREB-dependent manner.

Interacts (via RGG region) with SMN1; this interaction links SMN1 to the RNA polymerase II holoenzyme (ref.8).

Interacts with SP7.

Interacts (via DRBM domains) with TARBP2 (via DRBM first and second domains); this interaction occurs in a small interfering (siRNA)-dependent manner.

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.

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.

Interacts with XRCC5; this interaction occurs in a RNA-dependent manner.

Interacts with ZIC2 (via C2H2-type domain 3).

Interacts with MCM3AP (By similarity).

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		158477, 1 interactor

Protein interaction database and analysis system

More...IntActi		Q28141, 2 interactors

STRING: functional protein association networks

More...STRINGi		9913.ENSBTAP00000026409

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

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		Q28141

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

More...SMRi		Q28141

Database of comparative protein structure models

More...ModBasei		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%5Fand%5Fdomains%5Fsection">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 annotationBy similarityAdd BLAST69
Domaini177 – 249DRBM 2PROSITE-ProRule annotationBy similarityAdd BLAST73
Domaini395 – 561Helicase ATP-bindingPROSITE-ProRule annotationBy similarityAdd BLAST167
Domaini633 – 806Helicase 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 – 247Interaction with CREBBPBy similarityAdd BLAST247
Regioni5 – 9siRNA-bindingBy similarity5
Regioni53 – 55siRNA-bindingBy similarity3
Regioni179 – 183siRNA-bindingBy similarity5
Regioni227 – 322Interaction with BRCA1By similarityAdd BLAST96
Regioni231 – 233siRNA-bindingBy similarity3
Regioni252 – 661Necessary for interaction with RNA polymerase II holoenzymeBy similarityAdd BLAST410
Regioni310 – 949Necessary for interaction with H2AXBy similarityAdd BLAST640
Regioni328 – 377MTADBy similarityAdd BLAST50
Regioni395 – 806Core helicaseBy similarityAdd BLAST412
Regioni828 – 916HA2By similarityAdd BLAST89
Regioni955 – 1071OB-foldBy similarityAdd BLAST117
Regioni1147 – 1276NTD regionBy similarityAdd BLAST130
Regioni1148 – 1287RGGBy similarityAdd BLAST140

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>Motifi508 – 511DEIH box4
Motifi583 – 592Nuclear localization signal (NLS1)Sequence analysis10
Motifi1152 – 1170Nuclear localization signal (NLS2)By similarityAdd 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. The helicase-associated domain-2 (HA2) region is essential for the duplex RNA unwinding helicase activity. The minimal transactivation region (MTAD) mediates interaction with the RNA polymerase II holoenzyme and stimulates transcriptional activation in a CREB-dependent manner. 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. 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.By similarity

<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 DEAD box helicase family. DEAH subfamily.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0921, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155924

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q28141

KEGG Orthology (KO)

More...KOi		K13184

Database of Orthologous Groups

More...OrthoDBi		278674at2759

Family and domain databases

Conserved Domains Database

More...CDDi		cd00048, DSRM, 2 hits

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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q28141-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGDVKNFLYA WCGKRKMTPS YEIRAVGNKN RQKFMCEVRV EGYNYTGMGN 
        60         70         80         90        100
STNKKDAQSN AARDFVNYLV RINELKSEEV PAVGVAPPTP SATDSSDTTA 
       110        120        130        140        150
EDGGVPGNLG GPLPPHLTLQ AENNSGGGGS GYVPTWDRGA NLKDYYSRKE 
       160        170        180        190        200
EQEVQATLES EEVDLNAGLH GNWTLENAKA RLNQYFQKEK IQGEYKYTQV 
       210        220        230        240        250
GPDHNRSFIA EMTIYIKQIG RRIFAREHGS NKKLAAQSCA LSLVRQLYHL 
       260        270        280        290        300
GVIEPYSGLT KKKEGETVEP YKVNLSQDLE HQLQNIVQEL NLEIVPIPED 
       310        320        330        340        350
PSVPVALNLG KLAQFEPSQR QNPVGVVPWS PPQSNWNPWT SSNIDEGPLA 
       360        370        380        390        400
YATPEQISMD LKNELMYQLE QDRDLQAVLQ ERELLPVKKF ESEILEAISQ 
       410        420        430        440        450
NPVVIIRGAT GCGKTTQVPQ FILDDCIQND RAAECNIVVT QPRRISAVSV 
       460        470        480        490        500
AERVAYERGE EPGKSCGYSV RFESILPRPH ASIMFCTVGV LLRKLEAGIR 
       510        520        530        540        550
GISHVIVDEI HERDINTDFL LVVLRDVVQA YPEVRIVLMS ATIDTSMFCE 
       560        570        580        590        600
YFFNCPIIEV YGRTFPVQEY FLEDCIQMTH FVPPPKDKKK KDKDDDGGED 
       610        620        630        640        650
DDANCNLICG DEYGAETRIS MAQLNEKETP FELIEALLLY IETLNVPGAV 
       660        670        680        690        700
LVFLPGWNLI YTMQKHLEMN PHFGSHRYQI LPLHSQIPRE EQRKVFDPVP 
       710        720        730        740        750
SGVTKIILST NIAETSITIN DVVYVIDSCK QKVKLFTAHN NMTNYATVWA 
       760        770        780        790        800
SKTNLEQRKG RAGRVRPGFC FHLCSRARFE RLETHMTPEM FRTPLHEIAL 
       810        820        830        840        850
SIKLLRLGGI GQFLAKAIEP PPLDAVIEAE HTLRELDALD ANDELTPLGR 
       860        870        880        890        900
ILAKLPIEPR FGKMMIMGCI FYVGDAICTI SAATCFPEPF ISEGKRLGYI 
       910        920        930        940        950
HRNFAGNRFS DHVALLSVFQ AWDDARMGGE EAEIRFCEHK RLNMATLRMT 
       960        970        980        990       1000
WEAKVQLKEI LINSGFPEEC LLTQVFTNTG PDNNLDVVIS LLAFGVYPNV 
      1010       1020       1030       1040       1050
CYHKEKRKIL TTEGRNALIH KSSVNCPFSS QDMKYPSPFF VFGEKIRTRA 
      1060       1070       1080       1090       1100
ISAKGMTLVT PLQLLLFASK KVQSDGQLVL VDDWIRLQIS HEAAACITAL 
      1110       1120       1130       1140       1150
RAAMEALVVE VTKQPGIISQ LDPVNERMLN TIRQISRPSA AGINLMIGTT 
      1160       1170       1180       1190       1200
RYGDGPRPPK MARYDNGSGY RRGGSSYSGG GYGLGGYGTG GYGGGGGYGG 
      1210       1220       1230       1240       1250
RGGYSGGGYG GGSNSFRGSY VGGGGGVGGG GGGFRGLSRG GYRGMSGGDY 
      1260       1270       1280 
RGESGGGYRG SGGFQRGGGR GGYGGGYFGQ GRGGGGY
Length:1,287
Mass (Da):141,944
Last modified:November 1, 1997 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDC908095AB683ED4
GO

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
X82829 mRNA Translation: CAA58036.1

Protein sequence database of the Protein Information Resource

More...PIRi		I46032

NCBI Reference Sequences

More...RefSeqi		NP_776461.1, NM_174036.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSBTAT00000026409; ENSBTAP00000026409; ENSBTAG00000019821

Database of genes from NCBI RefSeq genomes

More...GeneIDi		281115

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bta:281115

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82829 mRNA Translation: CAA58036.1
PIRiI46032
RefSeqiNP_776461.1, NM_174036.2

3D structure databases

BMRBiQ28141
SMRiQ28141
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi158477, 1 interactor
IntActiQ28141, 2 interactors
STRINGi9913.ENSBTAP00000026409

Proteomic databases

PaxDbiQ28141
PeptideAtlasiQ28141
PRIDEiQ28141

Genome annotation databases

EnsembliENSBTAT00000026409; ENSBTAP00000026409; ENSBTAG00000019821
GeneIDi281115
KEGGibta:281115

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1660
VGNCiVGNC:28060, DHX9

Phylogenomic databases

eggNOGiKOG0921, Eukaryota
GeneTreeiENSGT00940000155924
InParanoidiQ28141
KOiK13184
OrthoDBi278674at2759

Gene expression databases

ExpressionAtlasiQ28141, baseline

Family and domain databases

CDDicd00048, DSRM, 2 hits
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

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDHX9_BOVIN
<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: Q28141
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 7, 2020
This is version 147 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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