UniProtKB - Q9NR30 (DDX21_HUMAN)
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- BLAST>sp|Q9NR30|DDX21_HUMAN Nucleolar RNA helicase 2 OS=Homo sapiens OX=9606 GN=DDX21 PE=1 SV=5 MPGKLRSDAGLESDTAMKKGETLRKQTEEKEKKEKPKSDKTEEIAEEEETVFPKAKQVKK KAEPSEVDMNSPKSKKAKKKEEPSQNDISPKTKSLRKKKEPIEKKVVSSKTKKVTKNEEP SEEEIDAPKPKKMKKEKEMNGETREKSPKLKNGFPHPEPDCNPSEAASEESNSEIEQEIP VEQKEGAFSNFPISEETIKLLKGRGVTFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSF AIPLIEKLHGELQDRKRGRAPQVLVLAPTRELANQVSKDFSDITKKLSVACFYGGTPYGG QFERMRNGIDILVGTPGRIKDHIQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEILSVA YKKDSEDNPQTLLFSATCPHWVFNVAKKYMKSTYEQVDLIGKKTQKTAITVEHLAIKCHW TQRAAVIGDVIRVYSGHQGRTIIFCETKKEAQELSQNSAIKQDAQSLHGDIPQKQREITL KGFRNGSFGVLVATNVAARGLDIPEVDLVIQSSPPKDVESYIHRSGRTGRAGRTGVCICF YQHKEEYQLVQVEQKAGIKFKRIGVPSATEIIKASSKDAIRLLDSVPPTAISHFKQSAEK LIEEKGAVEALAAALAHISGATSVDQRSLINSNVGFVTMILQCSIEMPNISYAWKELKEQ LGEEIDSKVKGMVFLKGKLGVCFDVPTASVTEIQEKWHDSRRWQLSVATEQPELEGPREG YGGFRGQREGSRGFRGQRDGNRRFRGQREGSRGPRGQRSGGGNKSNRSQNKGQKRSFSKA FGQ
- Align
Nucleolar RNA helicase 2
DDX21
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>Select a section on the left to see content.
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"The DEXD/H-box RNA helicase RHII/Gu is a co-factor for c-Jun-activated transcription."
Westermarck J., Weiss C., Saffrich R., Kast J., Musti A.M., Wessely M., Ansorge W., Seraphin B., Wilm M., Valdez B.C., Bohmann D.
EMBO J. 21:451-460(2002) [PubMed] [Europe PMC] [Abstract] - Ref.10"RNA-unwinding and RNA-folding activities of RNA helicase II/Gu--two activities in separate domains of the same protein."
Valdez B.C., Henning D., Perumal K., Busch H.
Eur. J. Biochem. 250:800-807(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF 339-ASP-GLU-340 AND 375-SER-ALA-376. - Ref.11"Silencing of RNA helicase II/Gualpha inhibits mammalian ribosomal RNA production."
Henning D., So R.B., Jin R., Lau L.F., Valdez B.C.
J. Biol. Chem. 278:52307-52314(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.15"c-Jun supports ribosomal RNA processing and nucleolar localization of RNA helicase DDX21."
Holmstrom T.H., Mialon A., Kallio M., Nymalm Y., Mannermaa L., Holm T., Johansson H., Black E., Gillespie D., Salminen T.A., Langel U., Valdez B.C., Westermarck J.
J. Biol. Chem. 283:7046-7053(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.28"Elevated DDX21 regulates c-Jun activity and rRNA processing in human breast cancers."
Zhang Y., Baysac K.C., Yee L.F., Saporita A.J., Weber J.D.
Breast Cancer Res. 16:449-449(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.31"RNA helicase DDX21 coordinates transcription and ribosomal RNA processing."
Calo E., Flynn R.A., Martin L., Spitale R.C., Chang H.Y., Wysocka J.
Nature 518:249-253(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF 339-ASP-GLU-340 AND 375-SER-ALA-376. - Ref.32"The association of late-acting snoRNPs with human pre-ribosomal complexes requires the RNA helicase DDX21."
Sloan K.E., Leisegang M.S., Doebele C., Ramirez A.S., Simm S., Safferthal C., Kretschmer J., Schorge T., Markoutsa S., Haag S., Karas M., Ebersberger I., Schleiff E., Watkins N.J., Bohnsack M.T.
Nucleic Acids Res. 43:553-564(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING. - Ref.33"A Compendium of RNA-Binding Proteins that Regulate MicroRNA Biogenesis."
Treiber T., Treiber N., Plessmann U., Harlander S., Daiss J.L., Eichner N., Lehmann G., Schall K., Urlaub H., Meister G.
Mol. Cell 66:270-284(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MIRNA-BINDING.
Miscellaneous
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A nucleolar RNA helicase recognized by autoimmune antibodies from a patient with watermelon stomach disease."
Valdez B.C., Henning D., Busch R.K., Woods K., Flores-Rozas H., Hurwitz J., Perlaky L., Busch H.
Nucleic Acids Res. 24:1220-1224(1996) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, VARIANT ILE-27.
<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. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"RNA-unwinding and RNA-folding activities of RNA helicase II/Gu--two activities in separate domains of the same protein."
Valdez B.C., Henning D., Perumal K., Busch H.
Eur. J. Biochem. 250:800-807(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF 339-ASP-GLU-340 AND 375-SER-ALA-376.
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 bindingi | 230 – 237 | ATPPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 8 |
<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
- 7SK snRNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ATP binding Source: UniProtKB-KW
- ATP-dependent RNA helicase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- double-stranded RNA binding Source: Ensembl
- miRNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- RNA binding Source: UniProtKBInferred from high throughput direct assayi
- rRNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- snoRNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<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 - Biological processi
- osteoblast differentiation Source: UniProtKBInferred from high throughput direct assayi
- positive regulation of gene expression, epigenetic Source: Reactome
- response to exogenous dsRNA Source: Ensembl
- response to virus Source: Ensembl
- RNA secondary structure unwinding Source: GO_Central
- rRNA processing Source: UniProtKB-KW
- transcription by RNA polymerase II Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
<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 function | Helicase, Hydrolase, RNA-binding |
| Biological process | rRNA processing, Transcription |
| Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-5250924 B-WICH complex positively regulates rRNA expression R-HSA-6791226 Major pathway of rRNA processing in the nucleolus and cytosol |
<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: Nucleolar RNA helicase 2Curated (EC:3.6.4.131 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Alternative name(s): DEAD box protein 21 Gu-alpha Nucleolar RNA helicase Gu Nucleolar RNA helicase II RH II/Gu |
| <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:DDX21 |
| <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>Organismi | Homo 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 identifieri | 9606 [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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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 |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000165732.12 |
Human Gene Nomenclature Database More...HGNCi | HGNC:2744 DDX21 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 606357 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9NR30 |
<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
Nucleus
- nucleolus 6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A nucleolar RNA helicase recognized by autoimmune antibodies from a patient with watermelon stomach disease."
Valdez B.C., Henning D., Busch R.K., Woods K., Flores-Rozas H., Hurwitz J., Perlaky L., Busch H.
Nucleic Acids Res. 24:1220-1224(1996) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, VARIANT ILE-27. - Ref.9"The DEXD/H-box RNA helicase RHII/Gu is a co-factor for c-Jun-activated transcription."
Westermarck J., Weiss C., Saffrich R., Kast J., Musti A.M., Wessely M., Ansorge W., Seraphin B., Wilm M., Valdez B.C., Bohmann D.
EMBO J. 21:451-460(2002) [PubMed] [Europe PMC] [Abstract] - Ref.15"c-Jun supports ribosomal RNA processing and nucleolar localization of RNA helicase DDX21."
Holmstrom T.H., Mialon A., Kallio M., Nymalm Y., Mannermaa L., Holm T., Johansson H., Black E., Gillespie D., Salminen T.A., Langel U., Valdez B.C., Westermarck J.
J. Biol. Chem. 283:7046-7053(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.26"Nucleolar scaffold protein, WDR46, determines the granular compartmental localization of nucleolin and DDX21."
Hirai Y., Louvet E., Oda T., Kumeta M., Watanabe Y., Horigome T., Takeyasu K.
Genes Cells 18:780-797(2013) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH WDR46. - Ref.28"Elevated DDX21 regulates c-Jun activity and rRNA processing in human breast cancers."
Zhang Y., Baysac K.C., Yee L.F., Saporita A.J., Weber J.D.
Breast Cancer Res. 16:449-449(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.31"RNA helicase DDX21 coordinates transcription and ribosomal RNA processing."
Calo E., Flynn R.A., Martin L., Spitale R.C., Chang H.Y., Wysocka J.
Nature 518:249-253(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF 339-ASP-GLU-340 AND 375-SER-ALA-376.
- nucleoplasm 4 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"The DEXD/H-box RNA helicase RHII/Gu is a co-factor for c-Jun-activated transcription."
Westermarck J., Weiss C., Saffrich R., Kast J., Musti A.M., Wessely M., Ansorge W., Seraphin B., Wilm M., Valdez B.C., Bohmann D.
EMBO J. 21:451-460(2002) [PubMed] [Europe PMC] [Abstract] - Ref.15"c-Jun supports ribosomal RNA processing and nucleolar localization of RNA helicase DDX21."
Holmstrom T.H., Mialon A., Kallio M., Nymalm Y., Mannermaa L., Holm T., Johansson H., Black E., Gillespie D., Salminen T.A., Langel U., Valdez B.C., Westermarck J.
J. Biol. Chem. 283:7046-7053(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.28"Elevated DDX21 regulates c-Jun activity and rRNA processing in human breast cancers."
Zhang Y., Baysac K.C., Yee L.F., Saporita A.J., Weber J.D.
Breast Cancer Res. 16:449-449(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.31"RNA helicase DDX21 coordinates transcription and ribosomal RNA processing."
Calo E., Flynn R.A., Martin L., Spitale R.C., Chang H.Y., Wysocka J.
Nature 518:249-253(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF 339-ASP-GLU-340 AND 375-SER-ALA-376.
Note: Present both in nucleolus and nucleoplasm. Interaction with JUN promotes translocation from the nucleolus to the nucleoplasm (PubMed:11823437, PubMed:18180292). Interaction with WDR46 is required for localization to the nucleolus (PubMed:23848194).3 Publications- nucleolus 6 Publications
- Ref.9"The DEXD/H-box RNA helicase RHII/Gu is a co-factor for c-Jun-activated transcription."
Westermarck J., Weiss C., Saffrich R., Kast J., Musti A.M., Wessely M., Ansorge W., Seraphin B., Wilm M., Valdez B.C., Bohmann D.
EMBO J. 21:451-460(2002) [PubMed] [Europe PMC] [Abstract] - Ref.15"c-Jun supports ribosomal RNA processing and nucleolar localization of RNA helicase DDX21."
Holmstrom T.H., Mialon A., Kallio M., Nymalm Y., Mannermaa L., Holm T., Johansson H., Black E., Gillespie D., Salminen T.A., Langel U., Valdez B.C., Westermarck J.
J. Biol. Chem. 283:7046-7053(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.26"Nucleolar scaffold protein, WDR46, determines the granular compartmental localization of nucleolin and DDX21."
Hirai Y., Louvet E., Oda T., Kumeta M., Watanabe Y., Horigome T., Takeyasu K.
Genes Cells 18:780-797(2013) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH WDR46.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
<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>Keywords - Cellular componenti
Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Mutagenesisi | 339 – 340 | DE → HG in mutant DEV; loss of helicase activity. Defects in release of P-TEFb from inhibitory 7SK snRNP. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 2 | |
| <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>Mutagenesisi | 375 – 376 | SA → LE in mutant SAT; ATPase defective. Defects in release of P-TEFb from inhibitory 7SK snRNP. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 2 |
Organism-specific databases
DisGeNET More...DisGeNETi | 9188 |
Open Targets More...OpenTargetsi | ENSG00000165732 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA27210 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | DDX21 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 76803555 |
<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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_0000055027 | 1 – 783 | Nucleolar RNA helicase 2Add BLAST | 783 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
|---|---|---|---|---|---|
| <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 residuei | 7 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <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 residuei | 13 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <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 residuei | 71 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <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 residuei | 89 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), 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-linki | 116 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| |||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), 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-linki | 116 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| |||
| <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 residuei | 121 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | ||
| <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 residuei | 147 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <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 residuei | 164 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <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 residuei | 171 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <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 residuei | 173 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| <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 residuei | 296 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <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 residuei | 567 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <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 residuei | 779 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Isoform 2 (identifier: Q9NR30-2) | |||||
| <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 residuei | 1 | N-acetylmethionineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
<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>Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9NR30 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9NR30 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9NR30 |
PeptideAtlas More...PeptideAtlasi | Q9NR30 |
PRoteomics IDEntifications database More...PRIDEi | Q9NR30 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 82265 82266 [Q9NR30-2] |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q9NR30-1 [Q9NR30-1] |
2D gel databases
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | Q9NR30 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9NR30 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9NR30 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q9NR30 |
<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 | ENSG00000165732 |
CleanEx database of gene expression profiles More...CleanExi | HS_DDX21 |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9NR30 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA036592 HPA036593 |
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"The DEXD/H-box RNA helicase RHII/Gu is a co-factor for c-Jun-activated transcription."
Westermarck J., Weiss C., Saffrich R., Kast J., Musti A.M., Wessely M., Ansorge W., Seraphin B., Wilm M., Valdez B.C., Bohmann D.
EMBO J. 21:451-460(2002) [PubMed] [Europe PMC] [Abstract] - Ref.13"The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription."
Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.
J. Biol. Chem. 281:16264-16271(2006) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN THE B-WICH COMPLEX. - Ref.15"c-Jun supports ribosomal RNA processing and nucleolar localization of RNA helicase DDX21."
Holmstrom T.H., Mialon A., Kallio M., Nymalm Y., Mannermaa L., Holm T., Johansson H., Black E., Gillespie D., Salminen T.A., Langel U., Valdez B.C., Westermarck J.
J. Biol. Chem. 283:7046-7053(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.23"Splicing factor 2-associated protein p32 participates in ribosome biogenesis by regulating the binding of Nop52 and fibrillarin to preribosome particles."
Yoshikawa H., Komatsu W., Hayano T., Miura Y., Homma K., Izumikawa K., Ishikawa H., Miyazawa N., Tachikawa H., Yamauchi Y., Isobe T., Takahashi N.
Mol. Cell. Proteomics 10:0-0(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH C1QBP. - Ref.26"Nucleolar scaffold protein, WDR46, determines the granular compartmental localization of nucleolin and DDX21."
Hirai Y., Louvet E., Oda T., Kumeta M., Watanabe Y., Horigome T., Takeyasu K.
Genes Cells 18:780-797(2013) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH WDR46.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| KPNA3 | O00505 | 3 | EBI-357942,EBI-358297 | |
| TERF2 | Q15554 | 2 | EBI-357942,EBI-706637 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 114625, 160 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-1099 B-WICH chromatin remodelling complex |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q9NR30 |
Database of interacting proteins More...DIPi | DIP-32941N |
Protein interaction database and analysis system More...IntActi | Q9NR30, 64 interactors |
Molecular INTeraction database More...MINTi | Q9NR30 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000346120 |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 631 – 642 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 651 – 660 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 664 – 667 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 676 – 678 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 679 – 686 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 687 – 693 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 704 – 707 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2M3D | NMR | - | A | 617-710 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9NR30 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9NR30 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Domaini | 217 – 396 | Helicase ATP-bindingPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 180 | |
| <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>Domaini | 429 – 573 | Helicase C-terminalPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 145 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 724 – 728 | 1 | 5 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 734 – 738 | 2 | 5 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 744 – 748 | 3 | 5 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Regioni | 724 – 748 | 3 X 5 AA repeatsAdd BLAST | 25 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Motifi | 186 – 214 | Q motifPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 29 | |
| <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>Motifi | 339 – 342 | DEAD boxPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 4 |
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"RNA-unwinding and RNA-folding activities of RNA helicase II/Gu--two activities in separate domains of the same protein."
Valdez B.C., Henning D., Perumal K., Busch H.
Eur. J. Biochem. 250:800-807(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF 339-ASP-GLU-340 AND 375-SER-ALA-376.
<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
<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>Keywords - Domaini
RepeatPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0331 Eukaryota COG0513 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000149066 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000268805 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG051331 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9NR30 |
KEGG Orthology (KO) More...KOi | K16911 |
Identification of Orthologs from Complete Genome Data More...OMAi | RFRGQRE |
Database of Orthologous Groups More...OrthoDBi | EOG091G04F8 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9NR30 |
TreeFam database of animal gene trees More...TreeFami | TF328622 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00079 HELICc, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR011545 DEAD/DEAH_box_helicase_dom IPR012562 GUCT IPR014001 Helicase_ATP-bd IPR001650 Helicase_C IPR027417 P-loop_NTPase IPR035979 RBD_domain_sf IPR014014 RNA_helicase_DEAD_Q_motif |
Pfam protein domain database More...Pfami | View protein in Pfam PF00270 DEAD, 1 hit PF08152 GUCT, 1 hit PF00271 Helicase_C, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00487 DEXDc, 1 hit SM00490 HELICc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF52540 SSF52540, 3 hits SSF54928 SSF54928, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51192 HELICASE_ATP_BIND_1, 1 hit PS51194 HELICASE_CTER, 1 hit PS51195 Q_MOTIF, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded 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.
10 20 30 40 50
MPGKLRSDAG LESDTAMKKG ETLRKQTEEK EKKEKPKSDK TEEIAEEEET
60 70 80 90 100
VFPKAKQVKK KAEPSEVDMN SPKSKKAKKK EEPSQNDISP KTKSLRKKKE
110 120 130 140 150
PIEKKVVSSK TKKVTKNEEP SEEEIDAPKP KKMKKEKEMN GETREKSPKL
160 170 180 190 200
KNGFPHPEPD CNPSEAASEE SNSEIEQEIP VEQKEGAFSN FPISEETIKL
210 220 230 240 250
LKGRGVTFLF PIQAKTFHHV YSGKDLIAQA RTGTGKTFSF AIPLIEKLHG
260 270 280 290 300
ELQDRKRGRA PQVLVLAPTR ELANQVSKDF SDITKKLSVA CFYGGTPYGG
310 320 330 340 350
QFERMRNGID ILVGTPGRIK DHIQNGKLDL TKLKHVVLDE VDQMLDMGFA
360 370 380 390 400
DQVEEILSVA YKKDSEDNPQ TLLFSATCPH WVFNVAKKYM KSTYEQVDLI
410 420 430 440 450
GKKTQKTAIT VEHLAIKCHW TQRAAVIGDV IRVYSGHQGR TIIFCETKKE
460 470 480 490 500
AQELSQNSAI KQDAQSLHGD IPQKQREITL KGFRNGSFGV LVATNVAARG
510 520 530 540 550
LDIPEVDLVI QSSPPKDVES YIHRSGRTGR AGRTGVCICF YQHKEEYQLV
560 570 580 590 600
QVEQKAGIKF KRIGVPSATE IIKASSKDAI RLLDSVPPTA ISHFKQSAEK
610 620 630 640 650
LIEEKGAVEA LAAALAHISG ATSVDQRSLI NSNVGFVTMI LQCSIEMPNI
660 670 680 690 700
SYAWKELKEQ LGEEIDSKVK GMVFLKGKLG VCFDVPTASV TEIQEKWHDS
710 720 730 740 750
RRWQLSVATE QPELEGPREG YGGFRGQREG SRGFRGQRDG NRRFRGQREG
760 770 780
SRGPRGQRSG GGNKSNRSQN KGQKRSFSKA FGQ
The sequence of this isoform differs from the canonical sequence as follows:
1-68: Missing.
10 20 30 40 50
MNSPKSKKAK KKEEPSQNDI SPKTKSLRKK KEPIEKKVVS SKTKKVTKNE
60 70 80 90 100
EPSEEEIDAP KPKKMKKEKE MNGETREKSP KLKNGFPHPE PDCNPSEAAS
110 120 130 140 150
EESNSEIEQE IPVEQKEGAF SNFPISEETI KLLKGRGVTF LFPIQAKTFH
160 170 180 190 200
HVYSGKDLIA QARTGTGKTF SFAIPLIEKL HGELQDRKRG RAPQVLVLAP
210 220 230 240 250
TRELANQVSK DFSDITKKLS VACFYGGTPY GGQFERMRNG IDILVGTPGR
260 270 280 290 300
IKDHIQNGKL DLTKLKHVVL DEVDQMLDMG FADQVEEILS VAYKKDSEDN
310 320 330 340 350
PQTLLFSATC PHWVFNVAKK YMKSTYEQVD LIGKKTQKTA ITVEHLAIKC
360 370 380 390 400
HWTQRAAVIG DVIRVYSGHQ GRTIIFCETK KEAQELSQNS AIKQDAQSLH
410 420 430 440 450
GDIPQKQREI TLKGFRNGSF GVLVATNVAA RGLDIPEVDL VIQSSPPKDV
460 470 480 490 500
ESYIHRSGRT GRAGRTGVCI CFYQHKEEYQ LVQVEQKAGI KFKRIGVPSA
510 520 530 540 550
TEIIKASSKD AIRLLDSVPP TAISHFKQSA EKLIEEKGAV EALAAALAHI
560 570 580 590 600
SGATSVDQRS LINSNVGFVT MILQCSIEMP NISYAWKELK EQLGEEIDSK
610 620 630 640 650
VKGMVFLKGK LGVCFDVPTA SVTEIQEKWH DSRRWQLSVA TEQPELEGPR
660 670 680 690 700
EGYGGFRGQR EGSRGFRGQR DGNRRFRGQR EGSRGPRGQR SGGGNKSNRS
710
QNKGQKRSFS KAFGQ
<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
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 conflicti | 273 | A → C in AAF78930 (PubMed:11237763).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_052161 | 27 | T → I2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | U41387 mRNA Translation: AAB02546.1 Different initiation. AF261903 Genomic DNA No translation available. AF261917 , AF261904, AF261905, AF261906, AF261907, AF261908, AF261909, AF261910, AF261911, AF261912, AF261913, AF261914, AF261915, AF261916 Genomic DNA Translation: AAF78930.2 AK315585 mRNA Translation: BAG37957.1 CR749598 mRNA Translation: CAH18395.1 AL359844 Genomic DNA No translation available. CH471083 Genomic DNA Translation: EAW54307.1 BC008071 mRNA Translation: AAH08071.2 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS31211.1 [Q9NR30-1] CCDS73144.1 [Q9NR30-2] |
Protein sequence database of the Protein Information Resource More...PIRi | PC6010 |
NCBI Reference Sequences More...RefSeqi | NP_001243839.1, NM_001256910.1 [Q9NR30-2] NP_004719.2, NM_004728.3 [Q9NR30-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.223141 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000354185; ENSP00000346120; ENSG00000165732 [Q9NR30-1] ENST00000620315; ENSP00000480334; ENSG00000165732 [Q9NR30-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 9188 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:9188 |
UCSC genome browser More...UCSCi | uc001jov.3 human [Q9NR30-1] |
<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>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
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9NR30 | nucleolar RNA helicase 2 | 784 | |||
| DDX21 isoform 1 | 783 | ||||
| DDX21 isoform 1 | 783 | ||||
| DExD-box helicase 21 | 783 | ||||
| DExD-box helicase 21 | 783 | ||||
| +9 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9NR30 | nucleolar RNA helicase 2 | 784 | |||
| Uncharacterized protein | 783 | ||||
| DDX21 isoform 1 | 783 | ||||
| DDX21 isoform 1 | 783 | ||||
| DExD-box helicase 21 | 783 | ||||
| +518 | |||||
<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: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | U41387 mRNA Translation: AAB02546.1 Different initiation. AF261903 Genomic DNA No translation available. AF261917 , AF261904, AF261905, AF261906, AF261907, AF261908, AF261909, AF261910, AF261911, AF261912, AF261913, AF261914, AF261915, AF261916 Genomic DNA Translation: AAF78930.2 AK315585 mRNA Translation: BAG37957.1 CR749598 mRNA Translation: CAH18395.1 AL359844 Genomic DNA No translation available. CH471083 Genomic DNA Translation: EAW54307.1 BC008071 mRNA Translation: AAH08071.2 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS31211.1 [Q9NR30-1] CCDS73144.1 [Q9NR30-2] |
Protein sequence database of the Protein Information Resource More...PIRi | PC6010 |
NCBI Reference Sequences More...RefSeqi | NP_001243839.1, NM_001256910.1 [Q9NR30-2] NP_004719.2, NM_004728.3 [Q9NR30-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.223141 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2M3D | NMR | - | A | 617-710 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9NR30 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9NR30 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 114625, 160 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-1099 B-WICH chromatin remodelling complex |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q9NR30 |
Database of interacting proteins More...DIPi | DIP-32941N |
Protein interaction database and analysis system More...IntActi | Q9NR30, 64 interactors |
Molecular INTeraction database More...MINTi | Q9NR30 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000346120 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9NR30 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9NR30 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q9NR30 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | DDX21 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 76803555 |
2D gel databases
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | Q9NR30 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9NR30 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9NR30 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9NR30 |
PeptideAtlas More...PeptideAtlasi | Q9NR30 |
PRoteomics IDEntifications database More...PRIDEi | Q9NR30 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 82265 82266 [Q9NR30-2] |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q9NR30-1 [Q9NR30-1] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 9188 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000354185; ENSP00000346120; ENSG00000165732 [Q9NR30-1] ENST00000620315; ENSP00000480334; ENSG00000165732 [Q9NR30-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 9188 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:9188 |
UCSC genome browser More...UCSCi | uc001jov.3 human [Q9NR30-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 9188 |
DisGeNET More...DisGeNETi | 9188 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000165732.12 |
GeneCards: human genes, protein and diseases More...GeneCardsi | DDX21 |
H-Invitational Database, human transcriptome db More...H-InvDBi | HIX0008880 |
Human Gene Nomenclature Database More...HGNCi | HGNC:2744 DDX21 |
Human Protein Atlas More...HPAi | HPA036592 HPA036593 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 606357 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9NR30 |
Open Targets More...OpenTargetsi | ENSG00000165732 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA27210 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0331 Eukaryota COG0513 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000149066 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000268805 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG051331 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9NR30 |
KEGG Orthology (KO) More...KOi | K16911 |
Identification of Orthologs from Complete Genome Data More...OMAi | RFRGQRE |
Database of Orthologous Groups More...OrthoDBi | EOG091G04F8 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9NR30 |
TreeFam database of animal gene trees More...TreeFami | TF328622 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-5250924 B-WICH complex positively regulates rRNA expression R-HSA-6791226 Major pathway of rRNA processing in the nucleolus and cytosol |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | DDX21 human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | DDX21 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 9188 |
Protein Ontology More...PROi | PR:Q9NR30 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000165732 |
CleanEx database of gene expression profiles More...CleanExi | HS_DDX21 |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9NR30 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd00079 HELICc, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR011545 DEAD/DEAH_box_helicase_dom IPR012562 GUCT IPR014001 Helicase_ATP-bd IPR001650 Helicase_C IPR027417 P-loop_NTPase IPR035979 RBD_domain_sf IPR014014 RNA_helicase_DEAD_Q_motif |
Pfam protein domain database More...Pfami | View protein in Pfam PF00270 DEAD, 1 hit PF08152 GUCT, 1 hit PF00271 Helicase_C, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00487 DEXDc, 1 hit SM00490 HELICc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF52540 SSF52540, 3 hits SSF54928 SSF54928, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51192 HELICASE_ATP_BIND_1, 1 hit PS51194 HELICASE_CTER, 1 hit PS51195 Q_MOTIF, 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 namei | DDX21_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>Accessioni | Q9NR30Primary (citable) accession number: Q9NR30 Secondary accession number(s): B2RDL0 , Q13436, Q5VX41, Q68D35 | |
| <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 historyi | Integrated into UniProtKB/Swiss-Prot: | April 27, 2001 |
| Last sequence update: | September 27, 2005 | |
| Last modified: | June 20, 2018 | |
| This is version 196 of the entry and version 5 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 statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any 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. | |
