Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q9H2U1 (DHX36_HUMAN)

Entry version 171 (16 Oct 2019)
Sequence version 2 (30 Nov 2010)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

ATP-dependent DNA/RNA helicase DHX36

Gene

DHX36

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Multifunctional ATP-dependent helicase that unwinds G-quadruplex (G4) structures (PubMed:16150737, PubMed:18854321, PubMed:20472641, PubMed:21586581). Plays a role in many biological processes such as genomic integrity, gene expression regulations and as a sensor to initiate antiviral responses (PubMed:14731398, PubMed:18279852, PubMed:21993297, PubMed:22238380, PubMed:25579584). G4 structures correspond to helical structures containing guanine tetrads (By similarity). Binds with high affinity to and unwinds G4 structures that are formed in nucleic acids (G4-ADN and G4-RNA) (PubMed:16150737, PubMed:18842585, PubMed:20472641, PubMed:21586581, PubMed:24369427, PubMed:26195789). Plays a role in genomic integrity (PubMed:22238380). 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 (PubMed:20472641, PubMed:21149580, PubMed:21846770, PubMed:22238380, PubMed:24151078, PubMed:25579584). Plays a role in transcriptional regulation (PubMed:21586581, PubMed:21993297). Resolves G4-DNA structures in promoters of genes, such as YY1, KIT/c-kit and ALPL and positively regulates their expression (PubMed:21993297). Plays a role in post-transcriptional regulation (PubMed:27940037). 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 (PubMed:27940037). 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 (PubMed:24369427, PubMed:26489465). 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 (PubMed:24369427). 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 (PubMed:26489465). Binds also to ARE sequences present in several mRNAs mediating exosome-mediated 3'-5' mRNA degradation (PubMed:14731398, PubMed:18279852). Involved in cytoplasmic urokinase-type plasminogen activator (uPA) mRNA decay (PubMed:14731398). 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 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 similarity17 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

<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+2 Publications

<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.1 Publication

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 bindingi335MagnesiumBy similarity1
Metal bindingi337MagnesiumBy similarity1
<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 sitei557ATP; via amide nitrogenBy similarity1

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 bindingi233 – 238ATPBy similarity6
Nucleotide bindingi602 – 605ATPBy similarity4

<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, 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-HSA-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:3.6.4.123 Publications, EC:3.6.4.133 Publications)
Alternative name(s):
DEAD/H box polypeptide 361 Publication
DEAH-box protein 36Curated
G4-resolvase-11 Publication
Short name:
G4R11 Publication
MLE-like protein 11 Publication
RNA helicase associated with AU-rich element protein1 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:DHX36Imported
Synonyms:DDX361 Publication, KIAA1488, MLEL11 Publication, RHAU1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:14410 DHX36

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		612767 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9H2U1

<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>Mutagenesisi54P → G: Reduces G4-RNA binding; when associated with A-57, A-59, A-62 and A-63. 1 Publication1
Mutagenesisi55G → L: Inhibits G4-DNA-binding; when associated with L-59 and L-63. 1 Publication1
Mutagenesisi57L → A: Reduces G4-RNA-binding; when associated with G-54, A-59, A-62 and A-63. 1 Publication1
Mutagenesisi59G → A: Reduces G4-RNA-binding; when associated with G-54, A-57, A-62 and A-63. 1 Publication1
Mutagenesisi59G → L: Inhibits G4-DNA-binding; when associated with L-55 and L-63. 1 Publication1
Mutagenesisi59G → P: Greatly reduces G4-RNA-binding; when associated with P-63. 1 Publication1
Mutagenesisi62I → A: Reduces G4-RNA-binding; when associated with G-54, A-57, A-59 and A-63. 1 Publication1
Mutagenesisi63G → A: Reduces G4-RNA-binding; when associated with G-54, A-57, A-59 and A-62. 1 Publication1
Mutagenesisi63G → L: Inhibits G4-DNA-binding; when associated with L-55 and L-59. 1 Publication1
Mutagenesisi63G → P: Greatly reduces G4-RNA-binding; when associated with P-59. 1 Publication1
Mutagenesisi65W → A: Does not inhibit G4-DNA-binding; when associated with A-66. 1 Publication1
Mutagenesisi66Y → A: Does not inhibit G4-DNA-binding; when associated with A-65. 1 Publication1
Mutagenesisi335E → A: Loss of ATPase activity; results in an increased in G4-DNA- and G4-RNA-binding stabilities, increases localization in cytoplasmic stress granules and loss of mRNA deadenylation and mRNA decay. 4 Publications1

Organism-specific databases

DisGeNET

More...DisGeNETi		170506

Open Targets

More...OpenTargetsi		ENSG00000174953

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27223

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q9H2U1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2040704

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		DHX36

Domain mapping of disease mutations (DMDM)

More...DMDMi		313104099

<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_00002475301 – 1008ATP-dependent DNA/RNA helicase DHX36Add BLAST1008

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 residuei161PhosphoserineCombined sources1
Modified residuei947N6-acetyllysineCombined sources1
Modified residuei963PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9H2U1

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9H2U1

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q9H2U1

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9H2U1

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

More...PaxDbi		Q9H2U1

PeptideAtlas

More...PeptideAtlasi		Q9H2U1

PRoteomics IDEntifications database

More...PRIDEi		Q9H2U1

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		80591 [Q9H2U1-1]
80592 [Q9H2U1-2]
80593 [Q9H2U1-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9H2U1

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

More...PhosphoSitePlusi		Q9H2U1

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highly expressed in testis.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000174953 Expressed in 205 organ(s), highest expression level in testis

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9H2U1 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9H2U1 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA035399

<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 (By similarity).

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

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) (PubMed:21846770).

Interacts with DKC1; this interaction is dependent on the ability of DHX36 to bind to the G4-RNA structure present in TERC (PubMed:21846770).

Interacts with PARN; this interaction stimulates PARN to enhance uPA mRNA decay (PubMed:14731398).

Interacts with EXOSC3; this interaction occurs in a RNase-insensitive manner (PubMed:14731398).

Interacts with EXOSC10; this interaction occurs in a RNase-insensitive manner (PubMed:14731398).

Interacts with ILF3; this interaction occurs in a RNA-dependent manner (PubMed:14731398).

Interacts with ELAVL1; this interaction occurs in an RNA-dependent manner (PubMed:14731398, PubMed:26489465).

Interacts with DDX5; this interaction occurs in a RNA-dependent manner (PubMed:18279852).

Interacts with DDX17; this interaction occurs in a RNA-dependent manner (PubMed:18279852).

Interacts with HDAC1; this interaction occurs in a RNA-dependent manner (PubMed:18279852).

Interacts with HDAC3; this interaction occurs in a RNA-dependent manner (PubMed:18279852).

Interacts with HDAC4 (By similarity).

Interacts with AGO1 (PubMed:17932509).

Interacts with AGO2 (PubMed:17932509).

Interacts with ERCC6 (PubMed:26030138).

By similarity6 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		128022, 149 interactors

Protein interaction database and analysis system

More...IntActi		Q9H2U1, 26 interactors

Molecular INTeraction database

More...MINTi		Q9H2U1

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000417078

<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

11008
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

More...SMRi		Q9H2U1

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>Domaini217 – 387Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST171
Domaini477 – 647Helicase 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 – 200Necessary for nuclear and nucleolar caps localizations1 PublicationAdd BLAST200
Regioni1 – 104Required for the pre-miR-134 transportBy similarityAdd BLAST104
Regioni1 – 51Required for recruitment to cytoplasmic stress granules1 PublicationAdd BLAST51
Regioni53 – 105Required for G4-DNA- and G4-RNA-binding3 PublicationsAdd BLAST53
Regioni53 – 75DSM (DHX36-specific motif)5 PublicationsAdd BLAST23
Regioni106 – 386RecA-like domain 1By similarityAdd BLAST281
Regioni265 – 317Necessary for interaction with single-stranded DNA at the 3'-end of the G4-DNA structureBy similarityAdd BLAST53
Regioni387 – 628RecA-like domain 2By similarityAdd BLAST242
Regioni498 – 557Necessary for interaction with single-stranded DNA at the 3'-end of the G4-DNA structureBy similarityAdd BLAST60
Regioni629 – 698WH domainBy similarityAdd BLAST70
Regioni638 – 697Necessary for interaction with single-stranded DNA at the 3'-end of the G4-DNA structureBy similarityAdd BLAST60
Regioni841 – 905OB-fold-like subdomainsBy similarityAdd BLAST65
Regioni849 – 860Necessary for interaction with single-stranded DNA at the 3'-end of the G4-DNA structureBy similarityAdd BLAST12
Regioni870 – 900Necessary for interaction with single-stranded DNA at the 3'-end of the G4-DNA structureBy similarityAdd BLAST31

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili72 – 157Sequence analysisAdd BLAST86

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>Motifi334 – 337DEAH boxPROSITE-ProRule annotation4
Motifi517 – 528Nuclear localization signal1 PublicationAdd BLAST12

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 biasi10 – 63Gly-richAdd BLAST54

<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, selectively 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 propbably 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 (By similarity). The N-terminus is necessary for its recruitment to cytoplasmic stress granules (SGs) upon arsenite-induced treatment (PubMed:18854321).By similarity1 Publication

<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

Coiled coil, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0920 Eukaryota
COG1643 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156903

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000247063

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9H2U1

KEGG Orthology (KO)

More...KOi		K14442

Identification of Orthologs from Complete Genome Data

More...OMAi		TMVFPMA

Database of Orthologous Groups

More...OrthoDBi		278674at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9H2U1

TreeFam database of animal gene trees

More...TreeFami		TF324744

Family and domain databases

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
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
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
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
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>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: Q9H2U1-1) [UniParc]FASTAAdd to basket
Also known as: Nuclear isoform1 Publication

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MSYDYHQNWG RDGGPRSSGG GYGGGPAGGH GGNRGSGGGG GGGGGGRGGR 
        60         70         80         90        100
GRHPGHLKGR EIGMWYAKKQ GQKNKEAERQ ERAVVHMDER REEQIVQLLN 
       110        120        130        140        150
SVQAKNDKES EAQISWFAPE DHGYGTEVST KNTPCSENKL DIQEKKLINQ 
       160        170        180        190        200
EKKMFRIRNR SYIDRDSEYL LQENEPDGTL DQKLLEDLQK KKNDLRYIEM 
       210        220        230        240        250
QHFREKLPSY GMQKELVNLI DNHQVTVISG ETGCGKTTQV TQFILDNYIE 
       260        270        280        290        300
RGKGSACRIV CTQPRRISAI SVAERVAAER AESCGSGNST GYQIRLQSRL 
       310        320        330        340        350
PRKQGSILYC TTGIILQWLQ SDPYLSSVSH IVLDEIHERN LQSDVLMTVV 
       360        370        380        390        400
KDLLNFRSDL KVILMSATLN AEKFSEYFGN CPMIHIPGFT FPVVEYLLED 
       410        420        430        440        450
VIEKIRYVPE QKEHRSQFKR GFMQGHVNRQ EKEEKEAIYK ERWPDYVREL 
       460        470        480        490        500
RRRYSASTVD VIEMMEDDKV DLNLIVALIR YIVLEEEDGA ILVFLPGWDN 
       510        520        530        540        550
ISTLHDLLMS QVMFKSDKFL IIPLHSLMPT VNQTQVFKRT PPGVRKIVIA 
       560        570        580        590        600
TNIAETSITI DDVVYVIDGG KIKETHFDTQ NNISTMSAEW VSKANAKQRK 
       610        620        630        640        650
GRAGRVQPGH CYHLYNGLRA SLLDDYQLPE ILRTPLEELC LQIKILRLGG 
       660        670        680        690        700
IAYFLSRLMD PPSNEAVLLS IRHLMELNAL DKQEELTPLG VHLARLPVEP 
       710        720        730        740        750
HIGKMILFGA LFCCLDPVLT IAASLSFKDP FVIPLGKEKI ADARRKELAK 
       760        770        780        790        800
DTRSDHLTVV NAFEGWEEAR RRGFRYEKDY CWEYFLSSNT LQMLHNMKGQ 
       810        820        830        840        850
FAEHLLGAGF VSSRNPKDPE SNINSDNEKI IKAVICAGLY PKVAKIRLNL 
       860        870        880        890        900
GKKRKMVKVY TKTDGLVAVH PKSVNVEQTD FHYNWLIYHL KMRTSSIYLY 
       910        920        930        940        950
DCTEVSPYCL LFFGGDISIQ KDNDQETIAV DEWIVFQSPA RIAHLVKELR 
       960        970        980        990       1000
KELDILLQEK IESPHPVDWN DTKSRDCAVL SAIIDLIKTQ EKATPRNFPP 

RFQDGYYS
Length:1,008
Mass (Da):114,760
Last modified:November 30, 2010 - 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:i66A28A1FE93C62AE
GO
Isoform 2 (identifier: Q9H2U1-2) [UniParc]FASTAAdd to basket
Also known as: Cytoplasmic isoform, RHAU-delta 141 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     517-530: Missing.

Note: More unstable than isoform 1.1 Publication
Show »
Length:994
Mass (Da):113,153
Checksum:i47809C3BDA49B709
GO
Isoform 3 (identifier: Q9H2U1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     737-765: Missing.

Note: No experimental confirmation available.
Show »
Length:979
Mass (Da):111,479
Checksum:iE8F39FA84E4DA91D
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
E7EWK3E7EWK3_HUMAN
ATP-dependent DNA/RNA helicase DHX3...
DHX36
797Annotation score:

Annotation score:2 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>
H7C514H7C514_HUMAN
ATP-dependent DNA/RNA helicase DHX3...
DHX36
119Annotation 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>
H7C5F5H7C5F5_HUMAN
ATP-dependent DNA/RNA helicase DHX3...
DHX36
187Annotation 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>
A0A0G2JQU7A0A0G2JQU7_HUMAN
ATP-dependent DNA/RNA helicase DHX3...
DHX36
216Annotation 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>
A0A0G2JRP3A0A0G2JRP3_HUMAN
ATP-dependent DNA/RNA helicase DHX3...
DHX36
91Annotation 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>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_027140151E → K. Corresponds to variant dbSNP:rs1058299Ensembl.1
Natural variantiVAR_027141416S → C3 PublicationsCorresponds to variant dbSNP:rs9438Ensembl.1
Natural variantiVAR_027142583I → N1 PublicationCorresponds to variant dbSNP:rs17853513Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_020006517 – 530Missing in isoform 2. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_020007737 – 765Missing in isoform 3. 1 PublicationAdd BLAST29

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
AF217190 mRNA Translation: AAG36783.1
AJ577133 mRNA Translation: CAE11802.1
AJ577134 mRNA Translation: CAE11803.1
AK314435 mRNA Translation: BAG37047.1
AC018452 Genomic DNA No translation available.
AC134026 Genomic DNA No translation available.
CH471052 Genomic DNA Translation: EAW78761.1
BC036035 mRNA Translation: AAH36035.1
AB040921 mRNA Translation: BAA96012.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS3171.1 [Q9H2U1-1]
CCDS54657.1 [Q9H2U1-2]

Protein sequence database of the Protein Information Resource

More...PIRi		D56236

NCBI Reference Sequences

More...RefSeqi		NP_001107869.1, NM_001114397.1 [Q9H2U1-2]
NP_065916.2, NM_020865.2 [Q9H2U1-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000308361; ENSP00000309296; ENSG00000174953 [Q9H2U1-3]
ENST00000329463; ENSP00000330113; ENSG00000174953 [Q9H2U1-2]
ENST00000496811; ENSP00000417078; ENSG00000174953 [Q9H2U1-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		170506

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:170506

UCSC genome browser

More...UCSCi		uc003ezy.5 human [Q9H2U1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF217190 mRNA Translation: AAG36783.1
AJ577133 mRNA Translation: CAE11802.1
AJ577134 mRNA Translation: CAE11803.1
AK314435 mRNA Translation: BAG37047.1
AC018452 Genomic DNA No translation available.
AC134026 Genomic DNA No translation available.
CH471052 Genomic DNA Translation: EAW78761.1
BC036035 mRNA Translation: AAH36035.1
AB040921 mRNA Translation: BAA96012.1
CCDSiCCDS3171.1 [Q9H2U1-1]
CCDS54657.1 [Q9H2U1-2]
PIRiD56236
RefSeqiNP_001107869.1, NM_001114397.1 [Q9H2U1-2]
NP_065916.2, NM_020865.2 [Q9H2U1-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2N16NMR-A53-70[»]
2N21NMR-A53-70[»]
SMRiQ9H2U1
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi128022, 149 interactors
IntActiQ9H2U1, 26 interactors
MINTiQ9H2U1
STRINGi9606.ENSP00000417078

Chemistry databases

ChEMBLiCHEMBL2040704

PTM databases

iPTMnetiQ9H2U1
PhosphoSitePlusiQ9H2U1

Polymorphism and mutation databases

BioMutaiDHX36
DMDMi313104099

Proteomic databases

EPDiQ9H2U1
jPOSTiQ9H2U1
MassIVEiQ9H2U1
MaxQBiQ9H2U1
PaxDbiQ9H2U1
PeptideAtlasiQ9H2U1
PRIDEiQ9H2U1
ProteomicsDBi80591 [Q9H2U1-1]
80592 [Q9H2U1-2]
80593 [Q9H2U1-3]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		170506

Genome annotation databases

EnsembliENST00000308361; ENSP00000309296; ENSG00000174953 [Q9H2U1-3]
ENST00000329463; ENSP00000330113; ENSG00000174953 [Q9H2U1-2]
ENST00000496811; ENSP00000417078; ENSG00000174953 [Q9H2U1-1]
GeneIDi170506
KEGGihsa:170506
UCSCiuc003ezy.5 human [Q9H2U1-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		170506
DisGeNETi170506

GeneCards: human genes, protein and diseases

More...GeneCardsi		DHX36
HGNCiHGNC:14410 DHX36
HPAiHPA035399
MIMi612767 gene
neXtProtiNX_Q9H2U1
OpenTargetsiENSG00000174953
PharmGKBiPA27223

Human Unidentified Gene-Encoded large proteins database

More...HUGEi		Search...

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0920 Eukaryota
COG1643 LUCA
GeneTreeiENSGT00940000156903
HOGENOMiHOG000247063
InParanoidiQ9H2U1
KOiK14442
OMAiTMVFPMA
OrthoDBi278674at2759
PhylomeDBiQ9H2U1
TreeFamiTF324744

Enzyme and pathway databases

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

Miscellaneous databases

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

More...ChiTaRSi		DHX36 human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		DHX36

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

More...GenomeRNAii		170506
PharosiQ9H2U1

Protein Ontology

More...PROi		PR:Q9H2U1

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000174953 Expressed in 205 organ(s), highest expression level in testis
ExpressionAtlasiQ9H2U1 baseline and differential
GenevisibleiQ9H2U1 HS

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

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 nameiDHX36_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9H2U1
Secondary accession number(s): B2RB00
, Q70JU3, Q8IYE5, Q9P240
<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: July 25, 2006
Last sequence update: November 30, 2010
Last modified: October 16, 2019
This is version 171 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again