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Entry version 101 (16 Oct 2019)
Sequence version 1 (14 Nov 2006)
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Protein

ATP-dependent DNA/RNA helicase DHX36

Gene

DHX36

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 helicase that unwinds G-quadruplex (G4) structures (PubMed:29899445). Plays a role in many biological processes such as genomic integrity, gene expression regulations and as a sensor to initiate antiviral responses (By similarity). G4 structures correspond to helical structures containing guanine tetrads (PubMed:29899445). Binds with high affinity to and unwinds G4 structures that are formed in nucleic acids (G4-ADN and G4-RNA) (PubMed:29899445) (By similarity). Plays a role in genomic integrity. Converts the G4-RNA structure present in telomerase RNA template component (TREC) into a double-stranded RNA to promote P1 helix formation that acts as a template boundary ensuring accurate reverse transcription (By similarity). Plays a role in transcriptional regulation. Resolves G4-DNA structures in promoters of genes, such as YY1, KIT/c-kit and ALPL and positively regulates their expression (By similarity). Plays a role in post-transcriptional regulation. Unwinds a G4-RNA structure located in the 3'-UTR polyadenylation site of the pre-mRNA TP53 and stimulates TP53 pre-mRNA 3'-end processing in response to ultraviolet (UV)-induced DNA damage (By similarity). Binds to the precursor-microRNA-134 (pre-miR-134) terminal loop and regulates its transport into the synapto-dendritic compartment (By similarity). Involved in the pre-miR-134-dependent inhibition of target gene expression and the control of dendritic spine size (By similarity). Plays a role in the regulation of cytoplasmic mRNA translation and mRNA stability (By similarity). Binds to both G4-RNA structures and alternative non-quadruplex-forming sequence within the 3'-UTR of the PITX1 mRNA regulating negatively PITX1 protein expression (By similarity). Binds to both G4-RNA structure in the 5'-UTR and AU-rich elements (AREs) localized in the 3'-UTR of NKX2-5 mRNA to either stimulate protein translation or induce mRNA decay in an ELAVL1-dependent manner, respectively (By similarity). Binds also to ARE sequences present in several mRNAs mediating exosome-mediated 3'-5' mRNA degradation (By similarity). Involved in cytoplasmic urokinase-type plasminogen activator (uPA) mRNA decay (By similarity). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of proinflammatory cytokines via the adapter molecule TICAM1 (By similarity). Required for the early embryonic development and hematopoiesis. Involved in the regulation of cardioblast differentiation and proliferation during heart development. Involved in spermatogonia differentiation. May play a role in ossification (By similarity).By similarity1 Publication

<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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

ATPase activity is enhanced in the presence of homopolymeric poly(U) RNAs, but not by double-stranded DNA (dsDNA), double-stranded RNA (dsRNA) and tRNA.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi337MagnesiumCombined sources1 Publication1
Metal bindingi339MagnesiumCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei559ATP; via amide nitrogenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi235 – 240ATPCombined sources1 Publication6
Nucleotide bindingi604 – 607ATPCombined sources1 Publication4

<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, Developmental protein, DNA-binding, Helicase, Hydrolase, Repressor, RNA-binding
Biological processAntiviral defense, Differentiation, Immunity, Innate immunity, Transcription, Transcription regulation, Translation regulation, Transport
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-BTA-3134963 DEx/H-box helicases activate type I IFN and inflammatory cytokines production

<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 DNA/RNA helicase DHX36Curated (EC:3.6.4.12By similarity, EC:3.6.4.13By similarity)
Alternative name(s):
DEAD/H box polypeptide 36By similarity
DEAH-box protein 36Curated
G4-resolvase-1By similarity
Short name:
G4R1By similarity
MLE-like protein 1By similarity
RNA helicase associated with AU-rich element proteinBy similarity
<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:DHX36By 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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
<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
  • UP000009136 <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

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:28054 DHX36

<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

Cell projection, Chromosome, Cytoplasm, Mitochondrion, Nucleus, Telomere

<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>Mutagenesisi63R → A: Decreases G4-DNA-binding; when associated with A-65. 1 Publication1
Mutagenesisi65I → A: Decreases G4-DNA-binding; when associated with A-63. 1 Publication1
Mutagenesisi69Y → A: Decreases strongly G4-DNA-binding. 1 Publication1
Mutagenesisi76K → G: Decreases G4-DNA-binding; when associated with G-77 and G-78. 1 Publication1
Mutagenesisi77N → G: Decreases G4-DNA-binding; when associated with G-76 and G-78. 1 Publication1
Mutagenesisi78K → G: Decreases G4-DNA-binding; when associated with G-76 and G-77. 1 Publication1

<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_00004454441 – 1010ATP-dependent DNA/RNA helicase DHX36Add BLAST1010

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 residuei949N6-acetyllysineBy similarity1
Modified residuei965PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
Q05B79

<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

More...
Bgeei
ENSBTAG00000006142 Expressed in 10 organ(s), highest expression level in testis

<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

Found in a multi-helicase-TICAM1 complex at least composed of DHX36, DDX1, DDX21 and TICAM1; this complex exists in resting cells with or without dsRNA poly(I:C) ligand stimulation.

Interacts (via C-terminus) with TICAM1 (via TIR domain).

Interacts (via C-terminus) with DDX21; this interaction serves as bridges to TICAM1 (By similarity).

Interacts with TERT; this interaction is dependent on the ability of DHX36 to bind to the G-quadruplex RNA (G4-RNA) structure present in the telomerase RNA template component (TERC).

Interacts with DKC1; this interaction is dependent on the ability of DHX36 to bind to the G4-RNA structure present in TERC.

Interacts with PARN; this interaction stimulates PARN to enhance uPA mRNA decay.

Interacts with EXOSC3; this interaction occurs in a RNase-insensitive manner.

Interacts with EXOSC10; this interaction occurs in a RNase-insensitive manner.

Interacts with ILF3; this interaction occurs in a RNA-dependent manner.

Interacts with ELAVL1; this interaction occurs in an RNA-dependent manner.

Interacts with DDX5; this interaction occurs in a RNA-dependent manner.

Interacts with DDX17; this interaction occurs in a RNA-dependent manner.

Interacts with HDAC1; this interaction occurs in a RNA-dependent manner (By similarity).

Interacts with HDAC3; this interaction occurs in a RNA-dependent manner (By similarity).

Interacts with HDAC4 (By similarity).

Interacts with AGO1.

Interacts with AGO2 (By similarity).

Interacts with ERCC6 (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000008082

<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

11010
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
Q05B79

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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>Domaini219 – 389Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST171
Domaini479 – 649Helicase C-terminalPROSITE-ProRule annotationAdd BLAST171

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 – 202Necessary for nuclear and nucleolar caps localizationsBy similarityAdd BLAST202
Regioni1 – 107Required for the pre-miR-134 transportBy similarityAdd BLAST107
Regioni1 – 54Required for recruitment to cytoplasmic stress granulesBy similarityAdd BLAST54
Regioni56 – 108Required for G4-DNA- and G4-RNA-bindingBy similarityAdd BLAST53
Regioni56 – 78DSM (DHX36-specific motif)1 PublicationAdd BLAST23
Regioni109 – 388RecA-like domain 11 PublicationAdd BLAST280
Regioni267 – 319Necessary for interaction with single-stranded DNA at the 3'-end of the G4-DNA structure1 PublicationAdd BLAST53
Regioni389 – 630RecA-like domain 21 PublicationAdd BLAST242
Regioni500 – 559Necessary for interaction with single-stranded DNA at the 3'-end of the G4-DNA structure1 PublicationAdd BLAST60
Regioni631 – 700WH domain1 PublicationAdd BLAST70
Regioni640 – 699Necessary for interaction with single-stranded DNA at the 3'-end of the G4-DNA structure1 PublicationAdd BLAST60
Regioni843 – 907OB-fold-like subdomains1 PublicationAdd BLAST65
Regioni851 – 862Necessary for interaction with single-stranded DNA at the 3'-end of the G4-DNA structure1 PublicationAdd BLAST12
Regioni872 – 902Necessary for interaction with single-stranded DNA at the 3'-end of the G4-DNA structure1 PublicationAdd BLAST31

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi336 – 339DEAH boxPROSITE-ProRule annotation4
Motifi519 – 530Nuclear localization signalBy similarityAdd BLAST12

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

The DHX36-specific motif (DSM) form folds into a DNA-binding-induced alpha-helix that together with the oligonucleotide and oligosaccharide-binding-fold-like (OB-fold-like) subdomain bind to Myc-promoter G4-DNA-containing structure in an ATP-dependent manner. Upon G4-DNA-binding, DHX36 pulls on DSM in the 3'-direction, inducing rearrangement of the RecA-like 1 and 2 and the degenerate-winged-helix (WH) regions; these rearrangements are probably responsible for the ATP-independent repetitive G4-DNA unfolding activity, one residue at a time. Upon resolving of G4-DNA into separate nucleotide strands, and ATP hydrolysis, the apoprotein of DHX36 seems incompatible with G4-DNA-binding (PubMed:29899445). The N-terminus is necessary for its recruitment to cytoplasmic stress granules (SGs) upon arsenite-induced treatment (By similarity).By similarity1 Publication

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0920 Eukaryota
COG1643 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156903

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000247063

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q05B79

KEGG Orthology (KO)

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KOi
K14442

Identification of Orthologs from Complete Genome Data

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OMAi
TMVFPMA

Database of Orthologous Groups

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OrthoDBi
278674at2759

TreeFam database of animal gene trees

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TreeFami
TF324744

Family and domain databases

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
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
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
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
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit

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

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

Q05B79-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSYDYHQNWG RDGGPRSSGG GYGGSYGGSH GGGHGGNRGS GGGGGGGGGR
60 70 80 90 100
GGRGRHPGHL KGREIGLWYA KKQGQKNKEA ERQERAVVHM DERREEQIVQ
110 120 130 140 150
LLHSVQTKND KDEEAQISWF APEDHGYGTE APAENKPNSV KNVEHQEKKM
160 170 180 190 200
INQEKRPFRI RDKYIDRDSE YLLQENEPDA TLDQQLLEDL QKKKTDLRYI
210 220 230 240 250
EMQRFREKLP SYGMQKELVN MIDNHQVTVI SGETGCGKTT QVTQFILDNY
260 270 280 290 300
IERGKGSACR IVCTQPRRIS AISVAERVAA ERAESCGNGN STGYQIRLQS
310 320 330 340 350
RLPRKQGSIL YCTTGIILQW LQSDPHLSSV SHIVLDEIHE RNLQSDVLMT
360 370 380 390 400
VVKDLLSYRP DLKVVLMSAT LNAEKFSEYF GNCPMIHIPG FTFPVVEYLL
410 420 430 440 450
EDIIEKIRYV PEQKEHRSQF KKGFMQGHVN RQEKEEKEAI YKERWPGYLR
460 470 480 490 500
ELRQRYSAST VDVVEMMDDE KVDLNLIAAL IRYIVLEEED GAILVFLPGW
510 520 530 540 550
DNISTLHDLL MSQVMFKSDK FIIIPLHSLM PTVNQTQVFK RTPPGVRKIV
560 570 580 590 600
IATNIAETSI TIDDVVYVID GGKIKETHFD TQNNISTMSA EWVSKANAKQ
610 620 630 640 650
RKGRAGRVQP GHCYHLYNSL RASLLDDYQL PEILRTPLEE LCLQIKILRL
660 670 680 690 700
GGIAHFLSRL MDPPSNEAVL LSIKHLMELN ALDKQEELTP LGVHLARLPV
710 720 730 740 750
EPHIGKMILF GALFCCLDPV LTIAASLSFK DPFVIPLGKE KVADARRKEL
760 770 780 790 800
AKDTKSDHLT VVNAFKGWEK AKQRGFRYEK DYCWEYFLSS NTLQMLHNMK
810 820 830 840 850
GQFAEHLLGA GFVSSRNPQD PESNINSDNE KIIKAVICAG LYPKVAKIRL
860 870 880 890 900
NLGKKRKMVK VYTKTDGVVA IHPKSVNVEQ TEFNYNWLIY HLKMRTSSIY
910 920 930 940 950
LYDCTEVSPY CLLFFGGDIS IQKDNDQETI AVDEWIIFQS PARIAHLVKE
960 970 980 990 1000
LRKELDILLQ EKIESPHPVD WKDTKSRDCA VLSAIIDLIK TQEKATPRNL
1010
PPRFQDGYYS
Length:1,010
Mass (Da):114,826
Last modified:November 14, 2006 - 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:i8205792C016B1018
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
DAAA02002573 Genomic DNA No translation available.
DAAA02002574 Genomic DNA No translation available.
BC122652 mRNA Translation: AAI22653.1

NCBI Reference Sequences

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RefSeqi
NP_001073720.1, NM_001080251.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSBTAT00000008082; ENSBTAP00000008082; ENSBTAG00000006142

Database of genes from NCBI RefSeq genomes

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GeneIDi
509583

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
bta:509583

<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

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EMBLi
GenBanki
DDBJi
Links Updated
DAAA02002573 Genomic DNA No translation available.
DAAA02002574 Genomic DNA No translation available.
BC122652 mRNA Translation: AAI22653.1
RefSeqiNP_001073720.1, NM_001080251.1

3D structure databases

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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
5VHAX-ray2.23A150-1010[»]
5VHCX-ray2.49D150-1010[»]
5VHDX-ray2.55D150-1010[»]
5VHEX-ray3.79A56-1010[»]
SMRiQ05B79
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008082

Proteomic databases

PaxDbiQ05B79

Genome annotation databases

EnsembliENSBTAT00000008082; ENSBTAP00000008082; ENSBTAG00000006142
GeneIDi509583
KEGGibta:509583

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
170506
VGNCiVGNC:28054 DHX36

Phylogenomic databases

eggNOGiKOG0920 Eukaryota
COG1643 LUCA
GeneTreeiENSGT00940000156903
HOGENOMiHOG000247063
InParanoidiQ05B79
KOiK14442
OMAiTMVFPMA
OrthoDBi278674at2759
TreeFamiTF324744

Enzyme and pathway databases

ReactomeiR-BTA-3134963 DEx/H-box helicases activate type I IFN and inflammatory cytokines production

Gene expression databases

BgeeiENSBTAG00000006142 Expressed in 10 organ(s), highest expression level in testis

Family and domain databases

InterProiView protein in InterPro
IPR011545 DEAD/DEAH_box_helicase_dom
IPR002464 DNA/RNA_helicase_DEAH_CS
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
PF04408 HA2, 1 hit
PF00271 Helicase_C, 1 hit
PF07717 OB_NTP_bind, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00847 HA2, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00690 DEAH_ATP_HELICASE, 1 hit
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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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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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 nameiDHX36_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: Q05B79
<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: October 10, 2018
Last sequence update: November 14, 2006
Last modified: October 16, 2019
This is version 101 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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