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Protein

ATP-dependent RNA helicase A

Gene

Dhx9

Organism
Mus musculus (Mouse)
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. 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). 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. Binds dsDNA, single-stranded DNA (ssDNA), dsRNA, ssRNA and poly(A)-containing RNA. 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 (By similarity). 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 (PubMed:22767893). 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. 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 (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 (By similarity).By similarity3 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 bindingi420ManganeseBy similarity1
Metal bindingi514ManganeseBy similarity1

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 bindingi413 – 421ATPPROSITE-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

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, 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, 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_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 ABy similarity (EC:3.6.4.13By similarity)
Alternative name(s):
DEAH box protein 91 Publication
Short name:
mHEL-51 Publication
Nuclear DNA helicase IIBy similarity
Short name:
NDH IIBy similarity
RNA helicase A1 Publication
Short name:
RHA1 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:Ddx9By similarity
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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: Unplaced

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:108177 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; 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000551581 – 1380ATP-dependent RNA helicase AAdd BLAST1380

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 residuei127PhosphoserineBy similarity1
Modified residuei136PhosphoserineCombined sources1
Modified residuei148N6-acetyllysine; alternateCombined sources1
Modified residuei148N6-methyllysine; alternateBy similarity1
Modified residuei193N6-acetyllysineBy similarity1
Modified residuei201N6-acetyllysineBy similarity1
Modified residuei323PhosphoserineBy similarity1
Modified residuei451PhosphoserineBy similarity1
Modified residuei508PhosphoserineBy similarity1
<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-linki699Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1026N6-acetyllysineBy similarity1
Modified residuei1167Asymmetric dimethylarginineCombined sources1
Modified residuei1176Omega-N-methylarginineBy similarity1
Modified residuei1312Asymmetric dimethylarginineCombined sources1
Modified residuei1323Asymmetric dimethylarginineCombined sources1
Modified residuei1339Asymmetric dimethylarginineCombined sources1
Modified residuei1346Asymmetric dimethylarginineCombined sources1
Modified residuei1353Asymmetric dimethylarginineCombined sources1
Modified residuei1361Asymmetric dimethylarginineCombined sources1
Modified residuei1372Asymmetric dimethylarginineCombined sources1
Isoform 2 (identifier: O70133-2)
Modified residuei137PhosphoserineCombined sources1

<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. 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

Encyclopedia of Proteome Dynamics

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EPDi
O70133

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O70133

MaxQB - The MaxQuant DataBase

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MaxQBi
O70133

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

More...
PaxDbi
O70133

PeptideAtlas

More...
PeptideAtlasi
O70133

PRoteomics IDEntifications database

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PRIDEi
O70133

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O70133

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

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PhosphoSitePlusi
O70133

SwissPalm database of S-palmitoylation events

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SwissPalmi
O70133

<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

CleanEx database of gene expression profiles

More...
CleanExi
MM_DHX9

<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. 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 (By similarity). The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active) (PubMed:22767893). 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 (By similarity). 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. 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 (By similarity). 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. 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. 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 (By similarity). 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. 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 (By similarity). Interacts with ZIC2 (via C2H2-type domain 3) (PubMed:17251188).By similarity5 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
199088, 10 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1089 CRD-mediated mRNA stability complex

Protein interaction database and analysis system

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IntActi
O70133, 11 interactors

Molecular INTeraction database

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MINTi
O70133

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000038135

<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

11380
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UILNMR-A163-262[»]
1WHQNMR-A4-89[»]
2RS6NMR-A4-89[»]
2RS7NMR-A163-262[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O70133

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

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SMRi
O70133

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
O70133

<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 annotationBy similarityAdd BLAST69
Domaini182 – 254DRBM 2PROSITE-ProRule annotationBy similarityAdd BLAST73
Domaini400 – 566Helicase ATP-bindingPROSITE-ProRule annotationBy similarityAdd BLAST167
Domaini638 – 811Helicase 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 – 252Interaction with CREBBPBy similarityAdd BLAST252
Regioni5 – 9siRNA-bindingBy similarity5
Regioni53 – 55siRNA-bindingBy similarity3
Regioni184 – 188siRNA-bindingBy similarity5
Regioni232 – 327Interaction with BRCA1By similarityAdd BLAST96
Regioni236 – 238siRNA-bindingBy similarity3
Regioni257 – 666Necessary for interaction with RNA polymerase II holoenzymeBy similarityAdd BLAST410
Regioni315 – 954Necessary for interaction with H2AFXBy similarityAdd BLAST640
Regioni333 – 382MTADBy similarityAdd BLAST50
Regioni400 – 811Core helicaseBy similarityAdd BLAST412
Regioni833 – 921HA2By similarityAdd BLAST89
Regioni960 – 1076OB-foldBy similarityAdd BLAST117
Regioni1151 – 1366NTD regionBy similarityAdd BLAST216
Regioni1152 – 1380RGGBy similarityAdd BLAST229

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>Motifi513 – 516DEAH box4
Motifi588 – 597Nuclear localization signal (NLS1)Sequence analysis10
Motifi1156 – 1174Nuclear localization signal (NLS2)By similarityAdd BLAST19

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1171 – 1380Arg/Gly/Ser/Tyr-richAdd BLAST210

<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

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0920 Eukaryota
COG1643 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000247063

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG039429

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O70133

KEGG Orthology (KO)

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KOi
K13184

Database of Orthologous Groups

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OrthoDBi
278674at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O70133

Family and domain databases

Conserved Domains Database

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CDDi
cd00048 DSRM, 2 hits
cd00079 HELICc, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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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

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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

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SUPFAMi
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

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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 (3+)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 3 <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

This entry has 3 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O70133-1) [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
MGDIKNFLYA WCGKRKMTPA YEIRAVGNKN RQKFMCEVRV EGFNYAGMGN
60 70 80 90 100
STNKKDAQSN AARDFVNYLV RINEVKSEEV PAVGIVPPPP ILSDTSDSTA
110 120 130 140 150
SAAEGLPAPM GGPLPPHLAL KAEENNSGVE SSGYGSPGPT WDRGANLKDY
160 170 180 190 200
YSRKEEQEVQ ATLESEEVDL NAGLHGNWTL ENAKARLNQY FQKEKIQGEY
210 220 230 240 250
KYTQVGPDHN RSFIAEMTIY IKQLGRRIFA REHGSNKKLA AQSCALSLVR
260 270 280 290 300
QLYHLGVIEA YSGLTKKKEG ERVEPYKVFL SPDLELQLQN VVQELDLEIV
310 320 330 340 350
PPPVDPSMPV ILNIGKLAHF EPSQRQNAVG VVPWSPPQSN WNPWTSSNID
360 370 380 390 400
EGPLAYASTE QISMDLKNEL TYQMEQDHNL QSVLQERELL PVKKFEAEIL
410 420 430 440 450
EAISSNSVVI IRGATGCGKT TQVPQYILDD FIQNDRAAEC NIVVTQPRRI
460 470 480 490 500
SAVAVAERVA YERGEEPGKS CGYSVRFESI LPRPHASIMF CTVGVLLRKL
510 520 530 540 550
EAGIRGISHV IVDEIHERDI NTDFLLVVLR DVVLAYPEVR IVLMSATIDT
560 570 580 590 600
TMFCEYFFNC PIIEVYGRTF PVQEYFLEDC IQMTQFIPPP KDKKKKDKED
610 620 630 640 650
DGGEDDDANC NLICGDEYGP ETKLSMSQLN EKETPFELIE ALLKYIETLN
660 670 680 690 700
VPGAVLVFLP GWNLIYTMQK HLENNSHFGS HRYQILPLHS QIPREEQRKV
710 720 730 740 750
FDPVPDGVTK VILSTNIAET SITINDVVYV IDSCKQKVKL FTAHNNMTNY
760 770 780 790 800
ATVWASKTNL EQRKGRAGRV RPGFCFHLCS RARFDRLETH MTPEMFRTPL
810 820 830 840 850
HEIALSIKLL RLGGIGQFLA KAIEPPPLDA IIEAEHTLRE LDALDANDEL
860 870 880 890 900
TPLGRILAKL PIEPRFGKMM IMGCIFYVGD AVCTISAATC FPEPFISEGK
910 920 930 940 950
RLGYIHRNFA GNRFSDHVAL LSVFQAWDDA RMSGEEAEIR FCEQKRLNMA
960 970 980 990 1000
TLRMTWEAKV QLKEILINSG FPEDCLLTQV FTNTGPDNNL DVVISLLAFG
1010 1020 1030 1040 1050
VYPNVCYHKE KRKILTTEGR NALIHKSSVN CPFSSQDMKY PSPFFVFGEK
1060 1070 1080 1090 1100
IRTRAISAKG MTLVTPLQLL LFASKKVQSD GQIVFIDDWI RLQISHEAAA
1110 1120 1130 1140 1150
CITIRAAMEA LVVEVSKQPN IISQLDPVNE HMLNTIRQIS RPSAAGINLM
1160 1170 1180 1190 1200
IGSVRYGDGP RPPKMARYDN GSGYRRGYGG GGYGGGGYGG GYGSGGFGGG
1210 1220 1230 1240 1250
FGSGGGFGGG FNSGGGGFGS GGGGFGSGGG GFGGGGGGFS GGGGGGFGGG
1260 1270 1280 1290 1300
RGGGGGGFGG SGGFGNGGGG YGVGGGGYGG GGGGGYGGGS GGYGGGGYGG
1310 1320 1330 1340 1350
GEGYSISPNS YRGNYGGGGG GYRGGSQGGY RNNFGGDYRG SSGDYRGSGG
1360 1370 1380
GYRGSGGFQR RGYGGGYFGQ GRGGGGGGGY
Length:1,380
Mass (Da):149,475
Last modified:July 19, 2005 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i005D641CD9A4F0C9
GO
Isoform 2 (identifier: O70133-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     123-123: E → EA

Show »
Length:1,381
Mass (Da):149,546
Checksum:i0AB5502F91DEFB73
GO
Isoform 3 (identifier: O70133-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-216: Missing.

Show »
Length:1,164
Mass (Da):125,615
Checksum:iDA64E679A88D87C2
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WPL5A0A087WPL5_MOUSE
ATP-dependent RNA helicase A
Dhx9
1,383Annotation 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>
E9QNN1E9QNN1_MOUSE
ATP-dependent RNA helicase A
Dhx9
1,384Annotation score:

Annotation score:1 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>
Q3UR42Q3UR42_MOUSE
ATP-dependent RNA helicase A
Dhx9
735Annotation score:

Annotation score:1 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>
A0A0R4J2C3A0A0R4J2C3_MOUSE
ATP-dependent RNA helicase A
Dhx9
459Annotation score:

Annotation score:1 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>
A0A087WRT3A0A087WRT3_MOUSE
ATP-dependent RNA helicase A
Dhx9
47Annotation score:

Annotation score:1 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH89159 differs from that shown. Reason: Frameshift at positions 447 and 448.Curated
The sequence AAR87796 differs from that shown. Intron retention.Curated

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 conflicti46A → R in AAC05725 (PubMed:9480750).Curated1
Sequence conflicti136S → A in AAC05725 (PubMed:9480750).Curated1
Sequence conflicti136S → A in AAC05301 (PubMed:9480750).Curated1
Sequence conflicti187L → V (PubMed:14691545).Curated1
Sequence conflicti189Q → H in AAC05725 (PubMed:9480750).Curated1
Sequence conflicti211R → G in BAB28848 (PubMed:16141072).Curated1
Sequence conflicti235S → C in AAC05725 (PubMed:9480750).Curated1
Sequence conflicti257V → C in AAC05725 (PubMed:9480750).Curated1
Sequence conflicti281S → P in AAC05725 (PubMed:9480750).Curated1
Sequence conflicti674N → M in AAB72087 (Ref. 5) Curated1
Sequence conflicti748T → I in AAB72087 (Ref. 5) Curated1
Sequence conflicti831I → V in AAB72087 (Ref. 5) Curated1

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_0147781 – 216Missing in isoform 3. 1 PublicationAdd BLAST216
Alternative sequenceiVSP_014779123E → EA in isoform 2. 1 Publication1

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
U91922 mRNA Translation: AAC05725.1
AF023530 Genomic DNA Translation: AAC05301.1
AY512925 mRNA Translation: AAR87796.1 Sequence problems.
BC089159 mRNA Translation: AAH89159.1 Sequence problems.
AK013423 mRNA Translation: BAB28848.1
U92080 mRNA Translation: AAB72087.1

NCBI Reference Sequences

More...
RefSeqi
NP_031868.2, NM_007842.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.20000

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
13211

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:13211

Keywords - Coding sequence diversityi

Alternative splicing

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

<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
U91922 mRNA Translation: AAC05725.1
AF023530 Genomic DNA Translation: AAC05301.1
AY512925 mRNA Translation: AAR87796.1 Sequence problems.
BC089159 mRNA Translation: AAH89159.1 Sequence problems.
AK013423 mRNA Translation: BAB28848.1
U92080 mRNA Translation: AAB72087.1
RefSeqiNP_031868.2, NM_007842.2
UniGeneiMm.20000

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UILNMR-A163-262[»]
1WHQNMR-A4-89[»]
2RS6NMR-A4-89[»]
2RS7NMR-A163-262[»]
ProteinModelPortaliO70133
SMRiO70133
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199088, 10 interactors
ComplexPortaliCPX-1089 CRD-mediated mRNA stability complex
IntActiO70133, 11 interactors
MINTiO70133
STRINGi10090.ENSMUSP00000038135

PTM databases

iPTMnetiO70133
PhosphoSitePlusiO70133
SwissPalmiO70133

Proteomic databases

EPDiO70133
jPOSTiO70133
MaxQBiO70133
PaxDbiO70133
PeptideAtlasiO70133
PRIDEiO70133

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi13211
KEGGimmu:13211

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1660
MGIiMGI:108177 Dhx9

Phylogenomic databases

eggNOGiKOG0920 Eukaryota
COG1643 LUCA
HOGENOMiHOG000247063
HOVERGENiHBG039429
InParanoidiO70133
KOiK13184
OrthoDBi278674at2759
PhylomeDBiO70133

Miscellaneous databases

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

More...
ChiTaRSi
Dhx9 mouse
EvolutionaryTraceiO70133

Protein Ontology

More...
PROi
PR:O70133

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

CleanExiMM_DHX9

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

More...
ProtoNeti
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDHX9_MOUSE
<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: O70133
Secondary accession number(s): O35931
, O54703, Q5FWY1, Q6R5F7, Q9CSA2
<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: December 15, 1998
Last sequence update: July 19, 2005
Last modified: January 16, 2019
This is version 172 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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