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Protein

Ribonuclease 3

Gene

DROSHA

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

Ribonuclease III double-stranded (ds) RNA-specific endoribonuclease that is involved in the initial step of microRNA (miRNA) biogenesis. Component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, DROSHA cleaves the 3' and 5' strands of a stem-loop in pri-miRNAs (processing center 11 bp from the dsRNA-ssRNA junction) to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. Involved also in pre-rRNA processing. Cleaves double-strand RNA and does not cleave single-strand RNA. Involved in the formation of GW bodies.11 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+1 Publication, Mn2+1 PublicationNote: Each RNase III domain binds at least one Mg2+ or Mn2+ ion.Curated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi536Zinc 11 Publication1
Metal bindingi538Zinc 11 Publication1
Metal bindingi549Zinc 11 Publication1
Metal bindingi561Zinc 21 Publication1
Metal bindingi609Zinc 21 Publication1
Metal bindingi676Zinc 21 Publication1
Metal bindingi680Zinc 21 Publication1
Metal bindingi969Magnesium or manganese 1By similarity1
Metal bindingi1026Zinc 11 Publication1
Metal bindingi1042Magnesium or manganese 1By similarity1
Metal bindingi1045Magnesium or manganese 1By similarity1 Publication1
Metal bindingi1147Magnesium or manganese 2By similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1215Important for activityBy similarity1
Metal bindingi1219Magnesium or manganese 2By similarity1
Metal bindingi1222Magnesium or manganese 2By similarity1 Publication1

<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

  • DEAD/H-box RNA helicase binding Source: BHF-UCL
  • double-stranded RNA binding Source: GO_Central
  • lipopolysaccharide binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • primary miRNA binding Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • ribonuclease III activity Source: WormBase
  • RNA binding Source: UniProtKB
  • R-SMAD binding Source: BHF-UCL
  • SMAD binding Source: BHF-UCL

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionEndonuclease, Hydrolase, Nuclease, RNA-binding
Biological processRibosome biogenesis, RNA-mediated gene silencing
LigandMagnesium, Manganese, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.26.3 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-203927 MicroRNA (miRNA) biogenesis

<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:
Ribonuclease 3 (EC:3.1.26.34 Publications)
Alternative name(s):
Protein Drosha1 Publication
Ribonuclease III
Short name:
RNase III
p241
<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:DROSHA
Synonyms:RN3, RNASE3L, RNASEN
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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 5

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000113360.16

Human Gene Nomenclature Database

More...
HGNCi
HGNC:17904 DROSHA

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
608828 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9NRR4

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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 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>Mutagenesisi536C → A: Impairs protein folding and stability; when associated with A-538. 1 Publication1
Mutagenesisi538C → A: Impairs protein folding and stability; when associated with A-536. 1 Publication1
Mutagenesisi561C → A: Impairs protein folding and stability. 1 Publication1
Mutagenesisi622 – 623RF → AA: Abolishes RNase activity. 1 Publication2
Mutagenesisi676C → A: Impairs protein folding and stability. 1 Publication1
Mutagenesisi835 – 836RR → AA: Abolishes RNase activity. 1 Publication2
Mutagenesisi914R → M: Impairs RNase activity. 1 Publication1
Mutagenesisi923R → A: Abolishes RNase activity; when associated with A-927. 1 Publication1
Mutagenesisi927Y → A: Abolishes RNase activity; when associated with A-923. 1 Publication1
Mutagenesisi938 – 940RKK → QQQ: Abolishes RNase activity. 1 Publication3
Mutagenesisi993E → A or Q: No effect on pri-miRNA processing activity. 1 Publication1
Mutagenesisi1045E → Q: Impairs pri-miRNA processing activity. Abolishes cleavage of the 3' strand. Abolishes enzyme activity; when associated with Q-1222. 2 Publications1
Mutagenesisi1077V → E: Loss of one DGCR8 interaction site; no effect on the second DGCR8 interaction site. 1 Publication1
Mutagenesisi1171E → A or Q: No effect on pri-miRNA processing activity. 1 Publication1
Mutagenesisi1194L → R: Abolishes interaction with DGCR8. 1 Publication1
Mutagenesisi1222E → Q: Impairs pri-miRNA processing activity. Abolishes cleavage of the 5' strand. Abolishes enzyme activity; when associated with Q-1045. 2 Publications1
Mutagenesisi1243V → D: Abolishes interaction with DGCR8. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
29102

Open Targets

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OpenTargetsi
ENSG00000113360

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA142671060

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
DROSHA

Domain mapping of disease mutations (DMDM)

More...
DMDMi
20139357

<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_00001804681 – 1374Ribonuclease 3Add BLAST1374

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 residuei355PhosphoserineCombined sources1
Modified residuei373PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9NRR4

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q9NRR4

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9NRR4

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

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PaxDbi
Q9NRR4

PeptideAtlas

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PeptideAtlasi
Q9NRR4

PRoteomics IDEntifications database

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PRIDEi
Q9NRR4

ProteomicsDB human proteome resource

More...
ProteomicsDBi
82409
82410 [Q9NRR4-2]
82411 [Q9NRR4-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9NRR4

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

More...
PhosphoSitePlusi
Q9NRR4

<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

Ubiquitous.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000113360 Expressed in 221 organ(s), highest expression level in endothelial cell

CleanEx database of gene expression profiles

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CleanExi
HS_RNASEN

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9NRR4 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9NRR4 HS

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the microprocessor complex, or pri-miRNA processing protein complex, which is composed of DROSHA and DGCR8 (PubMed:15589161, PubMed:15574589, PubMed:15531877, PubMed:16751099, PubMed:26027739, PubMed:26748718). The microprocessor complex is a heterotrimer; each of the two DROSHA RNase III domains binds one DGCR8 (via C-terminal region) (PubMed:26027739, PubMed:26748718). Interacts with SP1 and SNIP1 (PubMed:10976766, PubMed:18632581). Interacts with SRRT/ARS2 (By similarity).By similarity8 Publications

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
118870, 44 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-3080 Microprocessor complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9NRR4

Database of interacting proteins

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DIPi
DIP-33300N

Protein interaction database and analysis system

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IntActi
Q9NRR4, 31 interactors

Molecular INTeraction database

More...
MINTi
Q9NRR4

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000339845

<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

11374
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KHXNMR-A1259-1337[»]
2NA2NMR-A1259-1337[»]
5B16X-ray3.20A411-458[»]
A522-711[»]
A850-1365[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q9NRR4

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

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SMRi
Q9NRR4

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9NRR4

<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>Domaini876 – 1056RNase III 1Add BLAST181
Domaini1107 – 1233RNase III 2Add BLAST127
Domaini1260 – 1334DRBMAdd BLAST75

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>Regioni390 – 1365Necessary for interaction with DGCR8 and pri-miRNA processing activity2 PublicationsAdd BLAST976

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 biasi1 – 212Pro-richAdd BLAST212
Compositional biasi219 – 316Arg-richAdd BLAST98

<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 2 RNase III domains form an intramolecular dimer where the domain 1 cuts the 3'strand while the domain 2 cleaves the 5'strand of pri-miRNAs, independently of each other.1 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 ribonuclease III family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1817 Eukaryota
COG0571 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00730000111052

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000122291

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG023130

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9NRR4

KEGG Orthology (KO)

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KOi
K03685

Identification of Orthologs from Complete Genome Data

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OMAi
EYLYRHF

Database of Orthologous Groups

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OrthoDBi
935825at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9NRR4

TreeFam database of animal gene trees

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TreeFami
TF314734

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00048 DSRM, 1 hit
cd00593 RIBOc, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.1520.10, 1 hit

HAMAP database of protein families

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HAMAPi
MF_00104 RNase_III, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR014720 dsRBD_dom
IPR011907 RNase_III
IPR000999 RNase_III_dom
IPR036389 RNase_III_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00035 dsrm, 1 hit
PF14622 Ribonucleas_3_3, 1 hit
PF00636 Ribonuclease_3, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00358 DSRM, 1 hit
SM00535 RIBOc, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF69065 SSF69065, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50137 DS_RBD, 1 hit
PS00517 RNASE_3_1, 2 hits
PS50142 RNASE_3_2, 2 hits

<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 (4+)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 4 <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 4 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9NRR4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MMQGNTCHRM SFHPGRGCPR GRGGHGARPS APSFRPQNLR LLHPQQPPVQ
60 70 80 90 100
YQYEPPSAPS TTFSNSPAPN FLPPRPDFVP FPPPMPPSAQ GPLPPCPIRP
110 120 130 140 150
PFPNHQMRHP FPVPPCFPPM PPPMPCPNNP PVPGAPPGQG TFPFMMPPPS
160 170 180 190 200
MPHPPPPPVM PQQVNYQYPP GYSHHNFPPP SFNSFQNNPS SFLPSANNSS
210 220 230 240 250
SPHFRHLPPY PLPKAPSERR SPERLKHYDD HRHRDHSHGR GERHRSLDRR
260 270 280 290 300
ERGRSPDRRR QDSRYRSDYD RGRTPSRHRS YERSRERERE RHRHRDNRRS
310 320 330 340 350
PSLERSYKKE YKRSGRSYGL SVVPEPAGCT PELPGEIIKN TDSWAPPLEI
360 370 380 390 400
VNHRSPSREK KRARWEEEKD RWSDNQSSGK DKNYTSIKEK EPEETMPDKN
410 420 430 440 450
EEEEEELLKP VWIRCTHSEN YYSSDPMDQV GDSTVVGTSR LRDLYDKFEE
460 470 480 490 500
ELGSRQEKAK AARPPWEPPK TKLDEDLESS SESECESDED STCSSSSDSE
510 520 530 540 550
VFDVIAEIKR KKAHPDRLHD ELWYNDPGQM NDGPLCKCSA KARRTGIRHS
560 570 580 590 600
IYPGEEAIKP CRPMTNNAGR LFHYRITVSP PTNFLTDRPT VIEYDDHEYI
610 620 630 640 650
FEGFSMFAHA PLTNIPLCKV IRFNIDYTIH FIEEMMPENF CVKGLELFSL
660 670 680 690 700
FLFRDILELY DWNLKGPLFE DSPPCCPRFH FMPRFVRFLP DGGKEVLSMH
710 720 730 740 750
QILLYLLRCS KALVPEEEIA NMLQWEELEW QKYAEECKGM IVTNPGTKPS
760 770 780 790 800
SVRIDQLDRE QFNPDVITFP IIVHFGIRPA QLSYAGDPQY QKLWKSYVKL
810 820 830 840 850
RHLLANSPKV KQTDKQKLAQ REEALQKIRQ KNTMRREVTV ELSSQGFWKT
860 870 880 890 900
GIRSDVCQHA MMLPVLTHHI RYHQCLMHLD KLIGYTFQDR CLLQLAMTHP
910 920 930 940 950
SHHLNFGMNP DHARNSLSNC GIRQPKYGDR KVHHMHMRKK GINTLINIMS
960 970 980 990 1000
RLGQDDPTPS RINHNERLEF LGDAVVEFLT SVHLYYLFPS LEEGGLATYR
1010 1020 1030 1040 1050
TAIVQNQHLA MLAKKLELDR FMLYAHGPDL CRESDLRHAM ANCFEALIGA
1060 1070 1080 1090 1100
VYLEGSLEEA KQLFGRLLFN DPDLREVWLN YPLHPLQLQE PNTDRQLIET
1110 1120 1130 1140 1150
SPVLQKLTEF EEAIGVIFTH VRLLARAFTL RTVGFNHLTL GHNQRMEFLG
1160 1170 1180 1190 1200
DSIMQLVATE YLFIHFPDHH EGHLTLLRSS LVNNRTQAKV AEELGMQEYA
1210 1220 1230 1240 1250
ITNDKTKRPV ALRTKTLADL LESFIAALYI DKDLEYVHTF MNVCFFPRLK
1260 1270 1280 1290 1300
EFILNQDWND PKSQLQQCCL TLRTEGKEPD IPLYKTLQTV GPSHARTYTV
1310 1320 1330 1340 1350
AVYFKGERIG CGKGPSIQQA EMGAAMDALE KYNFPQMAHQ KRFIERKYRQ
1360 1370
ELKEMRWERE HQEREPDETE DIKK
Length:1,374
Mass (Da):159,316
Last modified:January 23, 2002 - 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:iED6FDEA09F3B8092
GO
Isoform 2 (identifier: Q9NRR4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     285-353: RERERERHRHRDNRRSPSLERSYKKEYKRSGRSYGLSVVPEPAGCTPELPGEIIKNTDSWAPPLEIVNH → S

Note: No experimental confirmation available.
Show »
Length:1,306
Mass (Da):151,296
Checksum:iE2A0A46BE0E0A692
GO
Isoform 3 (identifier: Q9NRR4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     316-352: Missing.
     353-353: H → S
     1198-1229: EYAITNDKTKRPVALRTKTLADLLESFIAALY → VWSIYLLSNCDCCLLRPSLVFLQTMNEVCSLK
     1230-1374: Missing.

Note: No experimental confirmation available.
Show »
Length:1,192
Mass (Da):138,157
Checksum:i18479E41CFD76BAC
GO
Isoform 4 (identifier: Q9NRR4-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     316-352: Missing.
     353-353: H → S

Note: No experimental confirmation available.
Show »
Length:1,337
Mass (Da):155,333
Checksum:i834B12891D1DB08D
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0YB67H0YB67_HUMAN
Ribonuclease 3
DROSHA
195Annotation 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>
H7C5U6H7C5U6_HUMAN
Ribonuclease 3
DROSHA
375Annotation 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>
E5RHD1E5RHD1_HUMAN
Ribonuclease 3
DROSHA
201Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

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

The sequence AAD29637 differs from that shown. Reason: Frameshift at position 775.Curated
The sequence BAA91511 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti166 – 174YQYPPGYSH → RERERTSLE in CAB45133 (PubMed:10976766).Curated9
Sequence conflicti612L → P in CAB45133 (PubMed:10976766).Curated1
Sequence conflicti1020R → P in AAF80558 (PubMed:10948199).Curated1
Sequence conflicti1230I → T in AAF80558 (PubMed:10948199).Curated1
Sequence conflicti1272L → R in BX647724 (PubMed:17974005).Curated1

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_05186667P → T. Corresponds to variant dbSNP:rs35342496Ensembl.1
Natural variantiVAR_061778321S → L. Corresponds to variant dbSNP:rs55656741Ensembl.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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_005777285 – 353RERER…EIVNH → S in isoform 2. 1 PublicationAdd BLAST69
Alternative sequenceiVSP_012450316 – 352Missing in isoform 3 and isoform 4. 2 PublicationsAdd BLAST37
Alternative sequenceiVSP_012451353H → S in isoform 3 and isoform 4. 2 Publications1
Alternative sequenceiVSP_0124521198 – 1229EYAIT…IAALY → VWSIYLLSNCDCCLLRPSLV FLQTMNEVCSLK in isoform 3. 1 PublicationAdd BLAST32
Alternative sequenceiVSP_0124531230 – 1374Missing in isoform 3. 1 PublicationAdd BLAST145

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
AF189011 mRNA Translation: AAF80558.1
BX647724 mRNA No translation available.
AC008768 Genomic DNA No translation available.
AC022417 Genomic DNA No translation available.
AC106802 Genomic DNA No translation available.
AJ242976 mRNA Translation: CAB45133.1
AK001121 mRNA Translation: BAA91511.1 Different initiation.
BC041162 mRNA Translation: AAH41162.1
BC054003 mRNA Translation: AAH54003.1
AF116910 mRNA Translation: AAD29637.1 Frameshift.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS47194.1 [Q9NRR4-4]
CCDS47195.1 [Q9NRR4-1]

NCBI Reference Sequences

More...
RefSeqi
NP_001093882.1, NM_001100412.1 [Q9NRR4-4]
NP_037367.3, NM_013235.4 [Q9NRR4-1]
XP_005248348.1, XM_005248291.3 [Q9NRR4-1]
XP_005248351.1, XM_005248294.3 [Q9NRR4-2]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.97997

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000344624; ENSP00000339845; ENSG00000113360 [Q9NRR4-1]
ENST00000442743; ENSP00000409335; ENSG00000113360 [Q9NRR4-4]
ENST00000511367; ENSP00000425979; ENSG00000113360 [Q9NRR4-1]
ENST00000513349; ENSP00000424161; ENSG00000113360 [Q9NRR4-4]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
29102

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:29102

UCSC genome browser

More...
UCSCi
uc003jhg.3 human [Q9NRR4-1]

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Protein Spotlight

The dark side of RNA - Issue 87 of October 2007

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF189011 mRNA Translation: AAF80558.1
BX647724 mRNA No translation available.
AC008768 Genomic DNA No translation available.
AC022417 Genomic DNA No translation available.
AC106802 Genomic DNA No translation available.
AJ242976 mRNA Translation: CAB45133.1
AK001121 mRNA Translation: BAA91511.1 Different initiation.
BC041162 mRNA Translation: AAH41162.1
BC054003 mRNA Translation: AAH54003.1
AF116910 mRNA Translation: AAD29637.1 Frameshift.
CCDSiCCDS47194.1 [Q9NRR4-4]
CCDS47195.1 [Q9NRR4-1]
RefSeqiNP_001093882.1, NM_001100412.1 [Q9NRR4-4]
NP_037367.3, NM_013235.4 [Q9NRR4-1]
XP_005248348.1, XM_005248291.3 [Q9NRR4-1]
XP_005248351.1, XM_005248294.3 [Q9NRR4-2]
UniGeneiHs.97997

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KHXNMR-A1259-1337[»]
2NA2NMR-A1259-1337[»]
5B16X-ray3.20A411-458[»]
A522-711[»]
A850-1365[»]
ProteinModelPortaliQ9NRR4
SMRiQ9NRR4
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118870, 44 interactors
ComplexPortaliCPX-3080 Microprocessor complex
CORUMiQ9NRR4
DIPiDIP-33300N
IntActiQ9NRR4, 31 interactors
MINTiQ9NRR4
STRINGi9606.ENSP00000339845

PTM databases

iPTMnetiQ9NRR4
PhosphoSitePlusiQ9NRR4

Polymorphism and mutation databases

BioMutaiDROSHA
DMDMi20139357

Proteomic databases

EPDiQ9NRR4
jPOSTiQ9NRR4
MaxQBiQ9NRR4
PaxDbiQ9NRR4
PeptideAtlasiQ9NRR4
PRIDEiQ9NRR4
ProteomicsDBi82409
82410 [Q9NRR4-2]
82411 [Q9NRR4-3]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000344624; ENSP00000339845; ENSG00000113360 [Q9NRR4-1]
ENST00000442743; ENSP00000409335; ENSG00000113360 [Q9NRR4-4]
ENST00000511367; ENSP00000425979; ENSG00000113360 [Q9NRR4-1]
ENST00000513349; ENSP00000424161; ENSG00000113360 [Q9NRR4-4]
GeneIDi29102
KEGGihsa:29102
UCSCiuc003jhg.3 human [Q9NRR4-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
29102
DisGeNETi29102
EuPathDBiHostDB:ENSG00000113360.16

GeneCards: human genes, protein and diseases

More...
GeneCardsi
DROSHA

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0004780
HGNCiHGNC:17904 DROSHA
MIMi608828 gene
neXtProtiNX_Q9NRR4
OpenTargetsiENSG00000113360
PharmGKBiPA142671060

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1817 Eukaryota
COG0571 LUCA
GeneTreeiENSGT00730000111052
HOGENOMiHOG000122291
HOVERGENiHBG023130
InParanoidiQ9NRR4
KOiK03685
OMAiEYLYRHF
OrthoDBi935825at2759
PhylomeDBiQ9NRR4
TreeFamiTF314734

Enzyme and pathway databases

BRENDAi3.1.26.3 2681
ReactomeiR-HSA-203927 MicroRNA (miRNA) biogenesis

Miscellaneous databases

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

More...
ChiTaRSi
DROSHA human
EvolutionaryTraceiQ9NRR4

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
RNASEN

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

More...
GenomeRNAii
29102

Protein Ontology

More...
PROi
PR:Q9NRR4

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000113360 Expressed in 221 organ(s), highest expression level in endothelial cell
CleanExiHS_RNASEN
ExpressionAtlasiQ9NRR4 baseline and differential
GenevisibleiQ9NRR4 HS

Family and domain databases

CDDicd00048 DSRM, 1 hit
cd00593 RIBOc, 2 hits
Gene3Di1.10.1520.10, 1 hit
HAMAPiMF_00104 RNase_III, 1 hit
InterProiView protein in InterPro
IPR014720 dsRBD_dom
IPR011907 RNase_III
IPR000999 RNase_III_dom
IPR036389 RNase_III_sf
PfamiView protein in Pfam
PF00035 dsrm, 1 hit
PF14622 Ribonucleas_3_3, 1 hit
PF00636 Ribonuclease_3, 1 hit
SMARTiView protein in SMART
SM00358 DSRM, 1 hit
SM00535 RIBOc, 2 hits
SUPFAMiSSF69065 SSF69065, 2 hits
PROSITEiView protein in PROSITE
PS50137 DS_RBD, 1 hit
PS00517 RNASE_3_1, 2 hits
PS50142 RNASE_3_2, 2 hits

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 nameiRNC_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: Q9NRR4
Secondary accession number(s): E7EMP9
, Q7Z5V2, Q86YH0, Q9NW73, Q9Y2V9, Q9Y4Y0
<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: January 23, 2002
Last sequence update: January 23, 2002
Last modified: January 16, 2019
This is version 173 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. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  7. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
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