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Protein

Poly(A)-specific ribonuclease PARN

Gene

PARN

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

3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization (PubMed:10882133, PubMed:11359775, PubMed:12748283, PubMed:15175153, PubMed:9736620). Also able to recognize and trim poly(A) tails of microRNAs such as MIR21 and H/ACA box snoRNAs (small nucleolar RNAs) leading to microRNAs degradation or snoRNA increased stability (PubMed:25049417, PubMed:22442037).7 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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

Mg2+2 PublicationsNote: Divalent metal cations. Mg2+ is the most probable.2 Publications

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 bindingi28Divalent metal cation; catalyticCurated1
Metal bindingi30Divalent metal cation; catalyticCurated1
Metal bindingi292Divalent metal cation; catalyticCurated1
Metal bindingi382Divalent metal cation; catalyticCurated1

<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

  • 3'-5'-exoribonuclease activity Source: GO_Central
  • cation binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • mRNA 3'-UTR binding Source: ProtInc
  • nuclease activity Source: ProtInc
  • poly(A)-specific ribonuclease activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • telomerase RNA 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 functionExonuclease, Hydrolase, Nuclease, RNA-binding
Biological processNonsense-mediated mRNA decay
LigandMagnesium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-380994 ATF4 activates genes
R-HSA-429947 Deadenylation of mRNA
R-HSA-450604 KSRP (KHSRP) binds and destabilizes mRNA

SIGNOR Signaling Network Open Resource

More...
SIGNORi
O95453

<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:
Poly(A)-specific ribonuclease PARN (EC:3.1.13.4)
Alternative name(s):
Deadenylating nuclease
Deadenylation nuclease
Polyadenylate-specific ribonuclease
<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:PARN
Synonyms:DAN
<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 16

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000140694.16

Human Gene Nomenclature Database

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HGNCi
HGNC:8609 PARN

Online Mendelian Inheritance in Man (OMIM)

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MIMi
604212 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_O95453

<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, 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

<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

Dyskeratosis congenita, autosomal recessive, 6 (DKCB6)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of dyskeratosis congenita, a rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy.
See also OMIM:616353
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_073782383A → V in DKCB6. 1 PublicationCorresponds to variant dbSNP:rs786200999EnsemblClinVar.1
Pulmonary fibrosis, and/or bone marrow failure, telomere-related, 4 (PFBMFT4)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease associated with shortened telomeres. Pulmonary fibrosis is the most common manifestation. Other manifestations include aplastic anemia due to bone marrow failure, hepatic fibrosis, and increased cancer risk, particularly myelodysplastic syndrome and acute myeloid leukemia. Phenotype, age at onset, and severity are determined by telomere length.
See also OMIM:616371
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073783421K → R in PFBMFT4. 1 PublicationCorresponds to variant dbSNP:rs777090017EnsemblClinVar.1

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>Mutagenesisi28D → A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs. 3 Publications1
Mutagenesisi28D → C: Loss of function in the presence of Mg(2+) but not in the presence of Mn(2+), Zn(2+), Co(2+) or Cd(2+). 3 Publications1
Mutagenesisi30E → A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs. 3 Publications1
Mutagenesisi30E → C: Loss of function in the presence of Mg(2+), Mn(2+), Zn(2+), Co(2+) or Cd(2+). 3 Publications1
Mutagenesisi31F → A: Reduced affinity for poly(A). Loss of activity. 1 Publication1
Mutagenesisi34I → A: Reduced affinity for poly(A). Strongly reduced activity. 1 Publication1
Mutagenesisi113I → A: Loss of dimerization. Loss of activity. 1 Publication1
Mutagenesisi115F → A: Reduced affinity for poly(A). Little effect on activity. 1
Mutagenesisi123F → A: Loss of dimerization. Loss of activity. 1 Publication1
Mutagenesisi292D → A: Loss of function but does not abolish ability to bind RNA. 2 Publications1
Mutagenesisi292D → C: Loss of function in the presence of Mg(2+) but not in the presence of Mn(2+), Zn(2+), Co(2+) or Cd(2+). 2 Publications1
Mutagenesisi326K → A: Reduced affinity for poly(A). Little effect on activity. 1
Mutagenesisi377H → A: Loss of activity. 1 Publication1
Mutagenesisi382D → A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs. 3 Publications1
Mutagenesisi382D → C: Loss of function in the presence of Mg(2+) but not in the presence of Mn(2+), Zn(2+), Co(2+) or Cd(2+). 3 Publications1
Mutagenesisi557S → A: Strong reduction of phosphorylation by MAPKAPK2. 1

Keywords - Diseasei

Disease mutation, Dyskeratosis congenita

Organism-specific databases

DisGeNET

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DisGeNETi
5073

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
PARN

MalaCards human disease database

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MalaCardsi
PARN
MIMi616353 phenotype
616371 phenotype

Open Targets

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OpenTargetsi
ENSG00000140694

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

More...
Orphaneti
1775 Dyskeratosis congenita
3322 Hoyeraal-Hreidarsson syndrome
2032 Idiopathic pulmonary fibrosis

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29072
PA32949

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3616362

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PARN

<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_00002128511 – 639Poly(A)-specific ribonuclease PARNAdd BLAST639

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 residuei163PhosphoserineCombined sources1
Modified residuei167PhosphoserineCombined sources1
Modified residuei220N6-acetyllysineCombined sources1
Modified residuei499N6-acetyllysineCombined sources1
Modified residuei530PhosphoserineCombined sources1
Modified residuei557Phosphoserine; by MAPKAPK2Combined sources1 Publication1
Modified residuei583PhosphoserineBy similarity1
Modified residuei587PhosphoserineBy similarity1
Modified residuei619PhosphoserineCombined sources1
Modified residuei623PhosphoserineCombined sources1
Modified residuei628PhosphoserineCombined sources1
Modified residuei631PhosphothreonineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation by MAPKAPK2, preventing GADD45A mRNA degradation after genotoxic stress.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O95453

MaxQB - The MaxQuant DataBase

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MaxQBi
O95453

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

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PaxDbi
O95453

PeptideAtlas

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PeptideAtlasi
O95453

PRoteomics IDEntifications database

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PRIDEi
O95453

ProteomicsDB human proteome resource

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ProteomicsDBi
50886
50887 [O95453-2]
50888 [O95453-3]

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
O95453

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O95453

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

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PhosphoSitePlusi
O95453

SwissPalm database of S-palmitoylation events

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SwissPalmi
O95453

<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.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000140694 Expressed in 220 organ(s), highest expression level in testis

CleanEx database of gene expression profiles

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CleanExi
HS_PARN

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O95453 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O95453 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB011673
HPA006314
HPA012010

<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

Homodimer (PubMed:10801819, PubMed:16281054). Found in a mRNA decay complex with RENT1, RENT2 and RENT3B (PubMed:14527413). Interacts with KHSRP (PubMed:15175153). Interacts with CELF1/CUGBP1 (PubMed:16601207). Interacts with ZC3HAV1 in an RNA-independent manner (PubMed:21876179). Interacts with DHX36 (PubMed:14731398).7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei326Interaction with poly(A)1 Publication1

<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)

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BioGridi
111107, 29 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O95453

Database of interacting proteins

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DIPi
DIP-31124N

Protein interaction database and analysis system

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IntActi
O95453, 11 interactors

Molecular INTeraction database

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MINTi
O95453

STRING: functional protein association networks

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STRINGi
9606.ENSP00000387911

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O95453

<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

1639
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
O95453

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

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SMRi
O95453

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

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EvolutionaryTracei
O95453

<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>Domaini178 – 245R3HPROSITE-ProRule annotationAdd BLAST68

<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 CAF1 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1990 Eukaryota
ENOG410XS9D LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153167

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000007285

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG053512

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O95453

KEGG Orthology (KO)

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KOi
K01148

Identification of Orthologs from Complete Genome Data

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OMAi
KETPFSP

Database of Orthologous Groups

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OrthoDBi
EOG091G04CM

Database for complete collections of gene phylogenies

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PhylomeDBi
O95453

TreeFam database of animal gene trees

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TreeFami
TF314502

Family and domain databases

Conserved Domains Database

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CDDi
cd02637 R3H_PARN, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.1370.50, 1 hit
3.30.420.10, 2 hits
3.30.70.330, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR034042 PARN_R3H
IPR014789 PolyA-riboNase_RNA_binding
IPR001374 R3H_dom
IPR036867 R3H_dom_sf
IPR035979 RBD_domain_sf
IPR006941 RNase_CAF1
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF04857 CAF1, 1 hit
PF01424 R3H, 1 hit
PF08675 RNA_bind, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF53098 SSF53098, 1 hit
SSF54928 SSF54928, 1 hit
SSF82708 SSF82708, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51061 R3H, 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 (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 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O95453-1) [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
MEIIRSNFKS NLHKVYQAIE EADFFAIDGE FSGISDGPSV SALTNGFDTP
60 70 80 90 100
EERYQKLKKH SMDFLLFQFG LCTFKYDYTD SKYITKSFNF YVFPKPFNRS
110 120 130 140 150
SPDVKFVCQS SSIDFLASQG FDFNKVFRNG IPYLNQEEER QLREQYDEKR
160 170 180 190 200
SQANGAGALS YVSPNTSKCP VTIPEDQKKF IDQVVEKIED LLQSEENKNL
210 220 230 240 250
DLEPCTGFQR KLIYQTLSWK YPKGIHVETL ETEKKERYIV ISKVDEEERK
260 270 280 290 300
RREQQKHAKE QEELNDAVGF SRVIHAIANS GKLVIGHNML LDVMHTVHQF
310 320 330 340 350
YCPLPADLSE FKEMTTCVFP RLLDTKLMAS TQPFKDIINN TSLAELEKRL
360 370 380 390 400
KETPFNPPKV ESAEGFPSYD TASEQLHEAG YDAYITGLCF ISMANYLGSF
410 420 430 440 450
LSPPKIHVSA RSKLIEPFFN KLFLMRVMDI PYLNLEGPDL QPKRDHVLHV
460 470 480 490 500
TFPKEWKTSD LYQLFSAFGN IQISWIDDTS AFVSLSQPEQ VKIAVNTSKY
510 520 530 540 550
AESYRIQTYA EYMGRKQEEK QIKRKWTEDS WKEADSKRLN PQCIPYTLQN
560 570 580 590 600
HYYRNNSFTA PSTVGKRNLS PSQEEAGLED GVSGEISDTE LEQTDSCAEP
610 620 630
LSEGRKKAKK LKRMKKELSP AGSISKNSPA TLFEVPDTW
Length:639
Mass (Da):73,451
Last modified:May 1, 1999 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6994BE39384DF7AC
GO
Isoform 2 (identifier: O95453-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.

Note: No experimental confirmation available. Non canonical splice junctions.
Show »
Length:578
Mass (Da):66,574
Checksum:i5E62F237DB650802
GO
Isoform 3 (identifier: O95453-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     53-98: Missing.

Show »
Length:593
Mass (Da):67,722
Checksum:i2908EEB765F91D80
GO
Isoform 4 (identifier: O95453-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     59-233: Missing.

Note: No experimental confirmation available.
Show »
Length:464
Mass (Da):52,989
Checksum:i6C4163C9604DFC5C
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F5H1Z4F5H1Z4_HUMAN
Poly(A)-specific ribonuclease PARN
PARN
207Annotation 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>
H3BRK1H3BRK1_HUMAN
Poly(A)-specific ribonuclease PARN
PARN
261Annotation 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>
H3BT23H3BT23_HUMAN
Poly(A)-specific ribonuclease PARN
PARN
109Annotation 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>
H3BVG1H3BVG1_HUMAN
Poly(A)-specific ribonuclease PARN
PARN
65Annotation score:

Annotation score:1 out of 5

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073782383A → V in DKCB6. 1 PublicationCorresponds to variant dbSNP:rs786200999EnsemblClinVar.1
Natural variantiVAR_073783421K → R in PFBMFT4. 1 PublicationCorresponds to variant dbSNP:rs777090017EnsemblClinVar.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_0428461 – 61Missing in isoform 2. 1 PublicationAdd BLAST61
Alternative sequenceiVSP_04284753 – 98Missing in isoform 3. 1 PublicationAdd BLAST46
Alternative sequenceiVSP_05726959 – 233Missing in isoform 4. 1 PublicationAdd BLAST175

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
AJ005698 mRNA Translation: CAA06683.1
AK293189 mRNA Translation: BAG56729.1
AK299653 mRNA Translation: BAG61572.1
AK301648 mRNA Translation: BAG63126.1
AK315020 mRNA Translation: BAG37510.1
AC009167 Genomic DNA No translation available.
AC092291 Genomic DNA No translation available.
KF456163 Genomic DNA No translation available.
CH471112 Genomic DNA Translation: EAW85110.1
BC050029 mRNA Translation: AAH50029.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS45419.1 [O95453-1]
CCDS45420.1 [O95453-2]
CCDS58425.1 [O95453-3]

NCBI Reference Sequences

More...
RefSeqi
NP_001127949.1, NM_001134477.2 [O95453-2]
NP_001229921.1, NM_001242992.1 [O95453-3]
NP_002573.1, NM_002582.3 [O95453-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.253197

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000341484; ENSP00000345456; ENSG00000140694 [O95453-2]
ENST00000420015; ENSP00000410525; ENSG00000140694 [O95453-3]
ENST00000437198; ENSP00000387911; ENSG00000140694 [O95453-1]
ENST00000539279; ENSP00000444381; ENSG00000140694 [O95453-4]
ENST00000615183; ENSP00000478668; ENSG00000274829 [O95453-1]
ENST00000618929; ENSP00000484279; ENSG00000274829 [O95453-3]
ENST00000631868; ENSP00000488554; ENSG00000274829 [O95453-4]
ENST00000634004; ENSP00000487634; ENSG00000274829 [O95453-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5073

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5073

UCSC genome browser

More...
UCSCi
uc010uzc.3 human [O95453-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AJ005698 mRNA Translation: CAA06683.1
AK293189 mRNA Translation: BAG56729.1
AK299653 mRNA Translation: BAG61572.1
AK301648 mRNA Translation: BAG63126.1
AK315020 mRNA Translation: BAG37510.1
AC009167 Genomic DNA No translation available.
AC092291 Genomic DNA No translation available.
KF456163 Genomic DNA No translation available.
CH471112 Genomic DNA Translation: EAW85110.1
BC050029 mRNA Translation: AAH50029.1
CCDSiCCDS45419.1 [O95453-1]
CCDS45420.1 [O95453-2]
CCDS58425.1 [O95453-3]
RefSeqiNP_001127949.1, NM_001134477.2 [O95453-2]
NP_001229921.1, NM_001242992.1 [O95453-3]
NP_002573.1, NM_002582.3 [O95453-1]
UniGeneiHs.253197

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2A1RX-ray2.60A/B1-430[»]
2A1SX-ray2.60A/B/C/D1-430[»]
3CTRX-ray2.10A445-540[»]
ProteinModelPortaliO95453
SMRiO95453
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111107, 29 interactors
CORUMiO95453
DIPiDIP-31124N
IntActiO95453, 11 interactors
MINTiO95453
STRINGi9606.ENSP00000387911

Chemistry databases

BindingDBiO95453
ChEMBLiCHEMBL3616362

PTM databases

iPTMnetiO95453
PhosphoSitePlusiO95453
SwissPalmiO95453

Polymorphism and mutation databases

BioMutaiPARN

2D gel databases

SWISS-2DPAGEiO95453

Proteomic databases

EPDiO95453
MaxQBiO95453
PaxDbiO95453
PeptideAtlasiO95453
PRIDEiO95453
ProteomicsDBi50886
50887 [O95453-2]
50888 [O95453-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
2987
5073
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341484; ENSP00000345456; ENSG00000140694 [O95453-2]
ENST00000420015; ENSP00000410525; ENSG00000140694 [O95453-3]
ENST00000437198; ENSP00000387911; ENSG00000140694 [O95453-1]
ENST00000539279; ENSP00000444381; ENSG00000140694 [O95453-4]
ENST00000615183; ENSP00000478668; ENSG00000274829 [O95453-1]
ENST00000618929; ENSP00000484279; ENSG00000274829 [O95453-3]
ENST00000631868; ENSP00000488554; ENSG00000274829 [O95453-4]
ENST00000634004; ENSP00000487634; ENSG00000274829 [O95453-2]
GeneIDi5073
KEGGihsa:5073
UCSCiuc010uzc.3 human [O95453-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5073
DisGeNETi5073
EuPathDBiHostDB:ENSG00000140694.16

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PARN
GeneReviewsiPARN
HGNCiHGNC:8609 PARN
HPAiCAB011673
HPA006314
HPA012010
MalaCardsiPARN
MIMi604212 gene
616353 phenotype
616371 phenotype
neXtProtiNX_O95453
OpenTargetsiENSG00000140694
Orphaneti1775 Dyskeratosis congenita
3322 Hoyeraal-Hreidarsson syndrome
2032 Idiopathic pulmonary fibrosis
PharmGKBiPA29072
PA32949

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1990 Eukaryota
ENOG410XS9D LUCA
GeneTreeiENSGT00940000153167
HOGENOMiHOG000007285
HOVERGENiHBG053512
InParanoidiO95453
KOiK01148
OMAiKETPFSP
OrthoDBiEOG091G04CM
PhylomeDBiO95453
TreeFamiTF314502

Enzyme and pathway databases

ReactomeiR-HSA-380994 ATF4 activates genes
R-HSA-429947 Deadenylation of mRNA
R-HSA-450604 KSRP (KHSRP) binds and destabilizes mRNA
SIGNORiO95453

Miscellaneous databases

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

More...
ChiTaRSi
PARN human
EvolutionaryTraceiO95453

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PARN
Poly(A)-specific_ribonuclease

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

More...
GenomeRNAii
5073

Protein Ontology

More...
PROi
PR:O95453

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000140694 Expressed in 220 organ(s), highest expression level in testis
CleanExiHS_PARN
ExpressionAtlasiO95453 baseline and differential
GenevisibleiO95453 HS

Family and domain databases

CDDicd02637 R3H_PARN, 1 hit
Gene3Di3.30.1370.50, 1 hit
3.30.420.10, 2 hits
3.30.70.330, 1 hit
InterProiView protein in InterPro
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR034042 PARN_R3H
IPR014789 PolyA-riboNase_RNA_binding
IPR001374 R3H_dom
IPR036867 R3H_dom_sf
IPR035979 RBD_domain_sf
IPR006941 RNase_CAF1
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
PfamiView protein in Pfam
PF04857 CAF1, 1 hit
PF01424 R3H, 1 hit
PF08675 RNA_bind, 1 hit
SUPFAMiSSF53098 SSF53098, 1 hit
SSF54928 SSF54928, 1 hit
SSF82708 SSF82708, 1 hit
PROSITEiView protein in PROSITE
PS51061 R3H, 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 nameiPARN_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: O95453
Secondary accession number(s): B2RCB3
, B4DDG8, B4DSB0, B4DWR4, B4E1H6
<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: March 1, 2005
Last sequence update: May 1, 1999
Last modified: December 5, 2018
This is version 167 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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