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Protein

2-5A-dependent ribonuclease

Gene

RNASEL

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

Endoribonuclease that functions in the interferon (IFN) antiviral response. In INF treated and virus infected cells, RNASEL probably mediates its antiviral effects through a combination of direct cleavage of single-stranded viral RNAs, inhibition of protein synthesis through the degradation of rRNA, induction of apoptosis, and induction of other antiviral genes. RNASEL mediated apoptosis is the result of a JNK-dependent stress-response pathway leading to cytochrome c release from mitochondria and caspase-dependent apoptosis. Therefore, activation of RNASEL could lead to elimination of virus infected cells under some circumstances. In the crosstalk between autophagy and apoptosis proposed to induce autophagy as an early stress response to small double-stranded RNA and at later stages of prolonged stress to activate caspase-dependent proteolytic cleavage of BECN1 to terminate autophagy and promote apoptosis (PubMed:26263979). Might play a central role in the regulation of mRNA turnover (PubMed:11585831). Cleaves 3' of UpNp dimers, with preference for UU and UA sequences, to sets of discrete products ranging from between 4 and 22 nucleotides in length.2 Publications

<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

Mn2+, Mg2+Note: Manganese or magnesium. Required for optimal RNA cleavage rates.

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

After binding to 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) the homodimerization and subsequent activation occurs. Inhibited by RNASEL inhibitor ABCE1/RLI, a cytoplasmic member of the ATP-binding cassette (ABC) transporter family.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri395 – 444C6-type; atypicalAdd BLAST50

<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

  • ATP binding Source: UniProtKB-KW
  • endoribonuclease activity Source: Reactome
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW
  • protein kinase activity Source: InterPro
  • ribonucleoprotein complex binding Source: Ensembl
  • RNA binding Source: UniProtKB
  • rRNA binding Source: Ensembl

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 processAntiviral defense
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS06069-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-8983711 OAS antiviral response
R-HSA-909733 Interferon alpha/beta signaling

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q05823

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q05823

<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:
2-5A-dependent ribonuclease (EC:3.1.26.-)
Short name:
2-5A-dependent RNase
Alternative name(s):
Ribonuclease 4
Ribonuclease L
Short name:
RNase L
<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:RNASEL
Synonyms:RNS4
<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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000135828.11

Human Gene Nomenclature Database

More...
HGNCi
HGNC:10050 RNASEL

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
180435 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q05823

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

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

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Prostate cancer, hereditary, 1 (HPC1)
Disease susceptibility is associated with variations affecting the gene represented in this entry.4 Publications
Disease descriptionA condition associated with familial predisposition to cancer of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma.
See also OMIM:601518

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>Mutagenesisi240K → N: Reduced 2-5A binding activity; almost complete loss of 2-5A binding activity; when associated with N-274. 1 Publication1
Mutagenesisi274K → N: Reduced 2-5A binding activity; almost complete loss of 2-5A binding activity; when associated with N-240. 1 Publication1
Mutagenesisi392K → R: Complete loss of enzymatic activity and enzyme dimerization. No change in binding to 2-5A and RNA. 1 Publication1
Mutagenesisi583H → A: No change in enzymatic activity. 1 Publication1
Mutagenesisi584P → A: No change in enzymatic activity. 1 Publication1
Mutagenesisi632W → A: No change in enzymatic activity. 1 Publication1
Mutagenesisi661D → A: Complete loss of enzymatic activity. 1 Publication1
Mutagenesisi667R → A: Complete loss of enzymatic activity. No change in 2-5A binding and enzyme dimerization. 1 Publication1
Mutagenesisi672H → A: Complete loss of enzymatic activity. No change in 2-5A binding activity and enzyme dimerization. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
6041

MalaCards human disease database

More...
MalaCardsi
RNASEL
MIMi176807 phenotype
601518 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000135828

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
1331 Familial prostate cancer

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34418

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3575

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
RNASEL

Domain mapping of disease mutations (DMDM)

More...
DMDMi
1350802

<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_00000670511 – 7412-5A-dependent ribonucleaseAdd BLAST741

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 residuei684N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q05823

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

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PaxDbi
Q05823

PeptideAtlas

More...
PeptideAtlasi
Q05823

PRoteomics IDEntifications database

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PRIDEi
Q05823

ProteomicsDB human proteome resource

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ProteomicsDBi
58353

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q05823

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

More...
PhosphoSitePlusi
Q05823

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
Q05823

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

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

Highly expressed in spleen and thymus followed by prostate, testis, uterus, small intestine, colon and peripheral blood leukocytes.

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By interferons. Virus replication in higher vertebrates is restrained by IFNs that cause cells to transcribe genes encoding antiviral proteins, such as 2'-5' oligoadenylate synthetases (OASs). oligoadenylate synthetase is stimulated by dsRNA to produce 5'-phosphorylated, 2'-5'-linked oligoadenylates (2-5A), whose function is to activate RNASEL.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000135828 Expressed in 190 organ(s), highest expression level in amniotic fluid

CleanEx database of gene expression profiles

More...
CleanExi
HS_RNASEL

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q05823 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB010906
HPA002633

<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

Monomer (inactive form) or homodimer. Interacts with ABCE1; this interaction inhibits the RNASEL.2 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

WithEntry#Exp.IntActNotes
IQGAP1P469402EBI-8390477,EBI-297509

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111969, 13 interactors

Database of interacting proteins

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DIPi
DIP-61367N

Protein interaction database and analysis system

More...
IntActi
Q05823, 4 interactors

Molecular INTeraction database

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MINTi
Q05823

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000356530

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q05823

<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

1741
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q05823

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

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SMRi
Q05823

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q05823

<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 ‘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>Repeati24 – 53ANK 1Add BLAST30
Repeati58 – 87ANK 2Add BLAST30
Repeati91 – 120ANK 3Add BLAST30
Repeati124 – 153ANK 4Add BLAST30
Repeati167 – 197ANK 5Add BLAST31
Repeati201 – 234ANK 6Add BLAST34
Repeati238 – 268ANK 7Add BLAST31
Repeati272 – 301ANK 8Add BLAST30
Repeati303 – 329ANK 9Add BLAST27
<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>Domaini365 – 586Protein kinasePROSITE-ProRule annotationAdd BLAST222
Domaini589 – 723KENPROSITE-ProRule annotationAdd BLAST135

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>Regioni229 – 2422-5A binding (P-loop) 1Add BLAST14
Regioni253 – 2752-5A binding (P-loop) 2Add BLAST23

<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 nine ankyrin repeats also called 2-5A sensor constitute the N-terminus 2-5A binding domain.
The protein kinase domain is predicted to be catalytically inactive. It allows the homodimerization.
The ribonuclease domain is located in the C-terminus. A single active nuclease domain in a dimer is sufficient for ribonuclease activity (By similarity).By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri395 – 444C6-type; atypicalAdd BLAST50

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1027 Eukaryota
KOG4177 Eukaryota
COG0666 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000161114

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000276879

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG012673

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q05823

KEGG Orthology (KO)

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KOi
K01165

Identification of Orthologs from Complete Genome Data

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OMAi
WSPLHNA

Database of Orthologous Groups

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OrthoDBi
EOG091G03H3

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q05823

TreeFam database of animal gene trees

More...
TreeFami
TF344032

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00204 ANK, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.1440.180, 1 hit
1.25.40.20, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
IPR010513 KEN_dom
IPR038357 KEN_sf
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR018997 PUB_domain

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12796 Ank_2, 3 hits
PF00069 Pkinase, 1 hit
PF06479 Ribonuc_2-5A, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01415 ANKYRIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00248 ANK, 8 hits
SM00580 PUG, 1 hit
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48403 SSF48403, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 6 hits
PS51392 KEN, 1 hit
PS50011 PROTEIN_KINASE_DOM, 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 basket
Isoform 1 (identifier: Q05823-1) [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
MESRDHNNPQ EGPTSSSGRR AAVEDNHLLI KAVQNEDVDL VQQLLEGGAN
60 70 80 90 100
VNFQEEEGGW TPLHNAVQMS REDIVELLLR HGADPVLRKK NGATPFILAA
110 120 130 140 150
IAGSVKLLKL FLSKGADVNE CDFYGFTAFM EAAVYGKVKA LKFLYKRGAN
160 170 180 190 200
VNLRRKTKED QERLRKGGAT ALMDAAEKGH VEVLKILLDE MGADVNACDN
210 220 230 240 250
MGRNALIHAL LSSDDSDVEA ITHLLLDHGA DVNVRGERGK TPLILAVEKK
260 270 280 290 300
HLGLVQRLLE QEHIEINDTD SDGKTALLLA VELKLKKIAE LLCKRGASTD
310 320 330 340 350
CGDLVMTARR NYDHSLVKVL LSHGAKEDFH PPAEDWKPQS SHWGAALKDL
360 370 380 390 400
HRIYRPMIGK LKFFIDEKYK IADTSEGGIY LGFYEKQEVA VKTFCEGSPR
410 420 430 440 450
AQREVSCLQS SRENSHLVTF YGSESHRGHL FVCVTLCEQT LEACLDVHRG
460 470 480 490 500
EDVENEEDEF ARNVLSSIFK AVQELHLSCG YTHQDLQPQN ILIDSKKAAH
510 520 530 540 550
LADFDKSIKW AGDPQEVKRD LEDLGRLVLY VVKKGSISFE DLKAQSNEEV
560 570 580 590 600
VQLSPDEETK DLIHRLFHPG EHVRDCLSDL LGHPFFWTWE SRYRTLRNVG
610 620 630 640 650
NESDIKTRKS ESEILRLLQP GPSEHSKSFD KWTTKINECV MKKMNKFYEK
660 670 680 690 700
RGNFYQNTVG DLLKFIRNLG EHIDEEKHKK MKLKIGDPSL YFQKTFPDLV
710 720 730 740
IYVYTKLQNT EYRKHFPQTH SPNKPQCDGA GGASGLASPG C
Length:741
Mass (Da):83,533
Last modified:February 1, 1996 - 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:i91385EA307E3CE1D
GO
Isoform 2 (identifier: Q05823-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     636-652: INECVMKKMNKFYEKRG → MSKLRHRQIIFPTTQNQ
     653-741: Missing.

Show »
Length:652
Mass (Da):73,416
Checksum:i4F39B25B82F07216
GO

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_01350959G → S2 PublicationsCorresponds to variant dbSNP:rs151296858Ensembl.1
Natural variantiVAR_04235897I → L1 PublicationCorresponds to variant dbSNP:rs56250729Ensembl.1
Natural variantiVAR_042359289A → T1 PublicationCorresponds to variant dbSNP:rs35553278Ensembl.1
Natural variantiVAR_013510406S → F1 PublicationCorresponds to variant dbSNP:rs145787003Ensembl.1
Natural variantiVAR_012056462R → Q Risk factor for prostate cancer; reduced enzymatic activity. 4 PublicationsCorresponds to variant dbSNP:rs486907EnsemblClinVar.1
Natural variantiVAR_012057541D → E No change in enzymatic activity. 4 PublicationsCorresponds to variant dbSNP:rs627928Ensembl.1
Natural variantiVAR_042360592R → H1 PublicationCorresponds to variant dbSNP:rs35896902Ensembl.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_056272636 – 652INECV…YEKRG → MSKLRHRQIIFPTTQNQ in isoform 2. 2 PublicationsAdd BLAST17
Alternative sequenceiVSP_056273653 – 741Missing in isoform 2. 2 PublicationsAdd BLAST89

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
L10381 Genomic DNA Translation: AAA18032.1
CR627369 mRNA Translation: CAH10468.1
AL138776 Genomic DNA No translation available.
CH471067 Genomic DNA Translation: EAW91128.1
BC090934 mRNA Translation: AAH90934.1
BC114433 mRNA Translation: AAI14434.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS1347.1 [Q05823-1]

Protein sequence database of the Protein Information Resource

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PIRi
A45771

NCBI Reference Sequences

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RefSeqi
NP_066956.1, NM_021133.3 [Q05823-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.518545

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000367559; ENSP00000356530; ENSG00000135828 [Q05823-1]
ENST00000539397; ENSP00000440844; ENSG00000135828 [Q05823-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
6041

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:6041

UCSC genome browser

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UCSCi
uc001gpk.4 human [Q05823-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10381 Genomic DNA Translation: AAA18032.1
CR627369 mRNA Translation: CAH10468.1
AL138776 Genomic DNA No translation available.
CH471067 Genomic DNA Translation: EAW91128.1
BC090934 mRNA Translation: AAH90934.1
BC114433 mRNA Translation: AAI14434.1
CCDSiCCDS1347.1 [Q05823-1]
PIRiA45771
RefSeqiNP_066956.1, NM_021133.3 [Q05823-1]
UniGeneiHs.518545

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
1WDYX-ray1.80A21-305[»]
4G8KX-ray2.40A/B1-337[»]
4G8LX-ray2.80A/B/C/D1-337[»]
4OAUX-ray2.60C21-719[»]
4OAVX-ray2.10B/D21-719[»]
ProteinModelPortaliQ05823
SMRiQ05823
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111969, 13 interactors
DIPiDIP-61367N
IntActiQ05823, 4 interactors
MINTiQ05823
STRINGi9606.ENSP00000356530

Chemistry databases

BindingDBiQ05823
ChEMBLiCHEMBL3575

PTM databases

iPTMnetiQ05823
PhosphoSitePlusiQ05823

Polymorphism and mutation databases

BioMutaiRNASEL
DMDMi1350802

Proteomic databases

EPDiQ05823
PaxDbiQ05823
PeptideAtlasiQ05823
PRIDEiQ05823
ProteomicsDBi58353

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
6041
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367559; ENSP00000356530; ENSG00000135828 [Q05823-1]
ENST00000539397; ENSP00000440844; ENSG00000135828 [Q05823-2]
GeneIDi6041
KEGGihsa:6041
UCSCiuc001gpk.4 human [Q05823-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
6041
DisGeNETi6041
EuPathDBiHostDB:ENSG00000135828.11

GeneCards: human genes, protein and diseases

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GeneCardsi
RNASEL
HGNCiHGNC:10050 RNASEL
HPAiCAB010906
HPA002633
MalaCardsiRNASEL
MIMi176807 phenotype
180435 gene
601518 phenotype
neXtProtiNX_Q05823
OpenTargetsiENSG00000135828
Orphaneti1331 Familial prostate cancer
PharmGKBiPA34418

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1027 Eukaryota
KOG4177 Eukaryota
COG0666 LUCA
GeneTreeiENSGT00940000161114
HOGENOMiHOG000276879
HOVERGENiHBG012673
InParanoidiQ05823
KOiK01165
OMAiWSPLHNA
OrthoDBiEOG091G03H3
PhylomeDBiQ05823
TreeFamiTF344032

Enzyme and pathway databases

BioCyciMetaCyc:HS06069-MONOMER
ReactomeiR-HSA-8983711 OAS antiviral response
R-HSA-909733 Interferon alpha/beta signaling
SignaLinkiQ05823
SIGNORiQ05823

Miscellaneous databases

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

More...
ChiTaRSi
RNASEL human
EvolutionaryTraceiQ05823

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Ribonuclease_L
RNASEL

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

More...
GenomeRNAii
6041
PMAP-CutDBiQ05823

Protein Ontology

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PROi
PR:Q05823

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000135828 Expressed in 190 organ(s), highest expression level in amniotic fluid
CleanExiHS_RNASEL
GenevisibleiQ05823 HS

Family and domain databases

CDDicd00204 ANK, 2 hits
Gene3Di1.20.1440.180, 1 hit
1.25.40.20, 1 hit
InterProiView protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
IPR010513 KEN_dom
IPR038357 KEN_sf
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR018997 PUB_domain
PfamiView protein in Pfam
PF12796 Ank_2, 3 hits
PF00069 Pkinase, 1 hit
PF06479 Ribonuc_2-5A, 1 hit
PRINTSiPR01415 ANKYRIN
SMARTiView protein in SMART
SM00248 ANK, 8 hits
SM00580 PUG, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF48403 SSF48403, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 6 hits
PS51392 KEN, 1 hit
PS50011 PROTEIN_KINASE_DOM, 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 nameiRN5A_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: Q05823
Secondary accession number(s): Q5W0L2, Q6AI46
<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: November 1, 1995
Last sequence update: February 1, 1996
Last modified: December 5, 2018
This is version 182 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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