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Entry version 184 (17 Jun 2020)
Sequence version 2 (20 Dec 2017)
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Protein

Three-prime repair exonuclease 1

Gene

TREX1

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

Major cellular 3'-to-5' DNA exonuclease which digests single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) with mismatched 3' termini. Prevents cell-intrinsic initiation of autoimmunity. Acts by metabolizing DNA fragments from endogenous retroelements, including L1, LTR and SINE elements. Unless degraded, these DNA fragments accumulate in the cytosol and activate the IFN-stimulatory DNA (ISD) response and innate immune signaling. Prevents chronic ATM-dependent checkpoint activation, by processing ssDNA polynucleotide species arising from the processing of aberrant DNA replication intermediates. Inefficiently degrades oxidized DNA, such as that generated upon antimicrobial reactive oxygen production or upon absorption of UV light. During GZMA-mediated cell death, contributes to DNA damage in concert with NME1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair.6 Publications

Caution

The gene for this protein is either identical to or adjacent to that of ATRIP. Some of the mRNAs that encode ATRIP also encode TREX1 in another reading frame.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

  • Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates. EC:3.1.11.2

<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+By similarityNote: Binds 2 Mg2+ per subunit. The second magnesium ion interacts with only one residue. Substitution with Mn2+ results in partial activity.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi18Magnesium 1By similarity1
Metal bindingi18Magnesium 2By similarity1
Metal bindingi20Magnesium 1By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei129SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei195Proton donor/acceptorBy similarity1
Metal bindingi200Magnesium 1By similarity1
Binding sitei200SubstrateBy similarity1

<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

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
LigandMagnesium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-3248023 Regulation by TREX1
R-HSA-3270619 IRF3-mediated induction of type I IFN

<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%5Fand%5Ftaxonomy%5Fsection">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:
Three-prime repair exonuclease 1Curated (EC:3.1.11.2)
Alternative name(s):
3'-5' exonuclease TREX11 Publication
Deoxyribonuclease III1 Publication
Short name:
DNase III1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:TREX1Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000213689.10
HostDB:ENSG00000282827.1

Human Gene Nomenclature Database

More...
HGNCi
HGNC:12269 TREX1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
606609 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9NSU2

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

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

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, 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

Aicardi-Goutieres syndrome 1 (AGS1)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood.
Related information in OMIM
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_03794818D → N in CHBL1 and AGS1; loss of function. 2 PublicationsCorresponds to variant dbSNP:rs121908117EnsemblClinVar.1
Natural variantiVAR_028319114R → H in AGS1 and SLE; primary fibroblasts from an AGS1 patient carrying H-169 show defective G1/S transition and chronic G2/M DNA damage checkpoint activation; strongly reduces activity. 6 PublicationsCorresponds to variant dbSNP:rs72556554EnsemblClinVar.1
Natural variantiVAR_070899122V → A in AGS1; increases ubiquitination levels; no effect on exonuclease activity. 2 PublicationsCorresponds to variant dbSNP:rs79993407EnsemblClinVar.1
Natural variantiVAR_070900198E → K in AGS1; increases ubiquitination levels; no effect on exonuclease activity. 2 PublicationsCorresponds to variant dbSNP:rs1416519719Ensembl.1
Natural variantiVAR_028320200D → DD in AGS1; heterozygous compound with H-169; loss of activity. 2 Publications1
Natural variantiVAR_070901200D → H in AGS1 and SLE. 1 Publication1
Natural variantiVAR_032940200D → N in AGS1; autosomal dominant form; no effect on dsDNA exonuclease activity; abolishes ssDNA exonuclease activity. 3 PublicationsCorresponds to variant dbSNP:rs78846775EnsemblClinVar.1
Natural variantiVAR_028321201V → D in AGS1; reduces activity by 75%. 3 PublicationsCorresponds to variant dbSNP:rs78408272EnsemblClinVar.1
Natural variantiVAR_070902303T → P in AGS1; decreases ubiquitination levels; decreases colocalization with UBQLN1; no effect on exonuclease activity. 2 PublicationsCorresponds to variant dbSNP:rs76224909EnsemblClinVar.1
Systemic lupus erythematosus (SLE)3 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry. Enhanced immune sensing of oxidized DNA may be involved in the phototoxicity experienced by SLE patients. Exposure to UV-light produces DNA oxidative damage. Oxidized DNA being a poor TREX1 substrate, it accumulates in skin, leading to enhanced auto-immune reactivity and eventually skin lesions (PubMed:23993650).1 Publication
Disease descriptionA chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_028319114R → H in AGS1 and SLE; primary fibroblasts from an AGS1 patient carrying H-169 show defective G1/S transition and chronic G2/M DNA damage checkpoint activation; strongly reduces activity. 6 PublicationsCorresponds to variant dbSNP:rs72556554EnsemblClinVar.1
Natural variantiVAR_037949158A → V in SLE. 1 PublicationCorresponds to variant dbSNP:rs762011967Ensembl.1
Natural variantiVAR_070901200D → H in AGS1 and SLE. 1 Publication1
Natural variantiVAR_037950227G → S in SLE; associated in cis with P-302. 1 PublicationCorresponds to variant dbSNP:rs113107733EnsemblClinVar.1
Natural variantiVAR_037951240R → S in SLE. 1 PublicationCorresponds to variant dbSNP:rs72556555EnsemblClinVar.1
Natural variantiVAR_037952247A → P in SLE; associated in cis with S-282. 1 PublicationCorresponds to variant dbSNP:rs112741962EnsemblClinVar.1
Natural variantiVAR_037954290P → L in SLE; increases ubiquitination levels; no effect on exonuclease activity. 2 PublicationsCorresponds to variant dbSNP:rs148833270EnsemblClinVar.1
Natural variantiVAR_037955305Y → C in SLE; decreases ubiquitination levels; decreases colocalization with UBQLN1; no effect on exonuclease activity. 2 PublicationsCorresponds to variant dbSNP:rs370504038EnsemblClinVar.1
Natural variantiVAR_037956306G → A in SLE. 1 PublicationCorresponds to variant dbSNP:rs780022923Ensembl.1
Chilblain lupus 1 (CHBL1)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare cutaneous form of lupus erythematosus. Affected individuals present with painful bluish-red papular or nodular lesions of the skin in acral locations precipitated by cold and wet exposure.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03794818D → N in CHBL1 and AGS1; loss of function. 2 PublicationsCorresponds to variant dbSNP:rs121908117EnsemblClinVar.1
Vasculopathy, retinal, with cerebral leukodystrophy (RVCL)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA microvascular endotheliopathy resulting in central nervous system degeneration and retinopathy, with progressive loss of vision, stroke, motor impairment, and cognitive decline. The ocular manifestations are characterized by telangiectasias, microaneurysms and retinal capillary obliteration starting in the macula. Diseased cerebral white matter has prominent small infarcts that often coalesce to pseudotumors.
Related information in OMIM

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi30K → R: Reduces ubiquitination. 1 Publication1
Mutagenesisi66K → R: No effect on ubiquitination. 1 Publication1
Mutagenesisi75K → R: Reduces ubiquitination. 1 Publication1
Mutagenesisi160K → R: Reduces ubiquitination. 1 Publication1
Mutagenesisi175K → R: Reduces ubiquitination. 1 Publication1
Mutagenesisi242K → R: Reduces ubiquitination. 1 Publication1
Mutagenesisi271K → R: Reduces ubiquitination. Strongly reduces ubiquitination; when associated with R-277. 1 Publication1
Mutagenesisi277K → R: Reduces ubiquitination. Strongly reduces ubiquitination; when associated with R-271. 1 Publication1

Keywords - Diseasei

Aicardi-Goutieres syndrome, Disease mutation, Neurodegeneration, Systemic lupus erythematosus

Organism-specific databases

DisGeNET

More...
DisGeNETi
11277

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

More...
GeneReviewsi
TREX1

MalaCards human disease database

More...
MalaCardsi
TREX1
MIMi152700 phenotype
192315 phenotype
225750 phenotype
610448 phenotype

Open Targets

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OpenTargetsi
ENSG00000213689

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

More...
Orphaneti
51 Aicardi-Goutieres syndrome
481662 Familial Chilblain lupus
247691 Retinal vasculopathy with cerebral leukoencephalopathy and systemic manifestations
536 Systemic lupus erythematosus

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA36949

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q9NSU2 Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
TREX1

Domain mapping of disease mutations (DMDM)

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DMDMi
47606216

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001098681 – 314Three-prime repair exonuclease 1Add BLAST314

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 residuei78PhosphoserineCombined sources1
Modified residuei167PhosphoserineCombined sources1
Modified residuei261PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Ubiquitinated, but not targeted to proteasomal degradation. Ubiquitination may be important for interaction with UBQLN1.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9NSU2

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9NSU2

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q9NSU2

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

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PaxDbi
Q9NSU2

PeptideAtlas

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PeptideAtlasi
Q9NSU2

PRoteomics IDEntifications database

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PRIDEi
Q9NSU2

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
82580 [Q9NSU2-1]
82581 [Q9NSU2-2]
82582 [Q9NSU2-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9NSU2

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

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PhosphoSitePlusi
Q9NSU2

<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

Detected in thymus, spleen, liver, brain, heart, small intestine and colon.2 Publications

<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

Induced by cytosolic DNA. Induced by inflammatory stimuli such as IFN-alpha and IFN-gamma in B cells and also by LPS and viral and bacterial DNA (via TLR9) in dendritic cells and macrophages (By similarity).By similarity

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000213689 Expressed in adenohypophysis and 87 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9NSU2 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9NSU2 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000213689 Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

Interacts (via proline-rich region) with TCERG1/CA150 (via the second WW domain).

Component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Within this complex, directly interacts with SET; this interaction does not result in TREX1 inhibition.

Also interacts with NME1, but only following translocation to the nucleus. Directly interacts with UBQLN1 (via ubiquitin-like domain); the interaction may control TREX1 subcellular location.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
116433, 13 interactors

Protein interaction database and analysis system

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IntActi
Q9NSU2, 34 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000296443

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q9NSU2 protein

<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

3D structure databases

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

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SMRi
Q9NSU2

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

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>Regioni20 – 21Substrate bindingBy similarity2
Regioni54 – 63Proline-rich regionBy similarity10
Regioni236 – 314Necessary for endoplasmic reticulum localizationBy similarityAdd BLAST79
Regioni243 – 314Interaction with UBQLN11 PublicationAdd BLAST72
Regioni281 – 314Necessary for cytoplasmic retentionBy similarityAdd BLAST34

<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 exonuclease superfamily. TREX family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4793 Eukaryota
ENOG4111YSP LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000012715

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_067419_1_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9NSU2

KEGG Orthology (KO)

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KOi
K10790

Identification of Orthologs from Complete Genome Data

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OMAi
LAVHRCA

Database of Orthologous Groups

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OrthoDBi
1365966at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9NSU2

TreeFam database of animal gene trees

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TreeFami
TF323333

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.420.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR013520 Exonuclease_RNaseT/DNA_pol3
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00479 EXOIII, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF53098 SSF53098, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 3 (identifier: Q9NSU2-3) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGSQALPPGP MQTLIFFDME ATGLPFSQPK VTELCLLAVH RCALESPPTS
60 70 80 90 100
QGPPPTVPPP PRVVDKLSLC VAPGKACSPA ASEITGLSTA VLAAHGRQCF
110 120 130 140 150
DDNLANLLLA FLRRQPQPWC LVAHNGDRYD FPLLQAELAM LGLTSALDGA
160 170 180 190 200
FCVDSITALK ALERASSPSE HGPRKSYSLG SIYTRLYGQS PPDSHTAEGD
210 220 230 240 250
VLALLSICQW RPQALLRWVD AHARPFGTIR PMYGVTASAR TKPRPSAVTT
260 270 280 290 300
TAHLATTRNT SPSLGESRGT KDLPPVKDPG ALSREGLLAP LGLLAILTLA
310
VATLYGLSLA TPGE
Length:314
Mass (Da):33,212
Last modified:December 20, 2017 - 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:iEE8F63B6496D72F4
GO
Isoform 1 (identifier: Q9NSU2-1) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGPGARRQGRIVQGRPEMCFCPPPTPLPPLRILTLGTHTPTPCSSPGSAAGTYPTM

Show »
Length:369
Mass (Da):38,923
Checksum:i42B79047A9AD9837
GO
Isoform 2 (identifier: Q9NSU2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-10: Missing.

Show »
Length:304
Mass (Da):32,276
Checksum:i922048DCC4122124
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9J052C9J052_HUMAN
Three-prime repair exonuclease 1
TREX1
175Annotation score:

Annotation score:2 out of 5

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

<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 AAD48774 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAL82504 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.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 conflicti265G → R in CAB50866 (PubMed:10393201).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03794818D → N in CHBL1 and AGS1; loss of function. 2 PublicationsCorresponds to variant dbSNP:rs121908117EnsemblClinVar.1
Natural variantiVAR_028319114R → H in AGS1 and SLE; primary fibroblasts from an AGS1 patient carrying H-169 show defective G1/S transition and chronic G2/M DNA damage checkpoint activation; strongly reduces activity. 6 PublicationsCorresponds to variant dbSNP:rs72556554EnsemblClinVar.1
Natural variantiVAR_070899122V → A in AGS1; increases ubiquitination levels; no effect on exonuclease activity. 2 PublicationsCorresponds to variant dbSNP:rs79993407EnsemblClinVar.1
Natural variantiVAR_037949158A → V in SLE. 1 PublicationCorresponds to variant dbSNP:rs762011967Ensembl.1
Natural variantiVAR_070900198E → K in AGS1; increases ubiquitination levels; no effect on exonuclease activity. 2 PublicationsCorresponds to variant dbSNP:rs1416519719Ensembl.1
Natural variantiVAR_028320200D → DD in AGS1; heterozygous compound with H-169; loss of activity. 2 Publications1
Natural variantiVAR_070901200D → H in AGS1 and SLE. 1 Publication1
Natural variantiVAR_032940200D → N in AGS1; autosomal dominant form; no effect on dsDNA exonuclease activity; abolishes ssDNA exonuclease activity. 3 PublicationsCorresponds to variant dbSNP:rs78846775EnsemblClinVar.1
Natural variantiVAR_028321201V → D in AGS1; reduces activity by 75%. 3 PublicationsCorresponds to variant dbSNP:rs78408272EnsemblClinVar.1
Natural variantiVAR_037950227G → S in SLE; associated in cis with P-302. 1 PublicationCorresponds to variant dbSNP:rs113107733EnsemblClinVar.1
Natural variantiVAR_037951240R → S in SLE. 1 PublicationCorresponds to variant dbSNP:rs72556555EnsemblClinVar.1
Natural variantiVAR_037952247A → P in SLE; associated in cis with S-282. 1 PublicationCorresponds to variant dbSNP:rs112741962EnsemblClinVar.1
Natural variantiVAR_037953266E → G1 PublicationCorresponds to variant dbSNP:rs55999987EnsemblClinVar.1
Natural variantiVAR_037954290P → L in SLE; increases ubiquitination levels; no effect on exonuclease activity. 2 PublicationsCorresponds to variant dbSNP:rs148833270EnsemblClinVar.1
Natural variantiVAR_070902303T → P in AGS1; decreases ubiquitination levels; decreases colocalization with UBQLN1; no effect on exonuclease activity. 2 PublicationsCorresponds to variant dbSNP:rs76224909EnsemblClinVar.1
Natural variantiVAR_037955305Y → C in SLE; decreases ubiquitination levels; decreases colocalization with UBQLN1; no effect on exonuclease activity. 2 PublicationsCorresponds to variant dbSNP:rs370504038EnsemblClinVar.1
Natural variantiVAR_037956306G → A in SLE. 1 PublicationCorresponds to variant dbSNP:rs780022923Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0104451 – 10Missing in isoform 2. 1 Publication10
Alternative sequenceiVSP_0592791M → MGPGARRQGRIVQGRPEMCF CPPPTPLPPLRILTLGTHTP TPCSSPGSAAGTYPTM in isoform 1. 1 Publication1

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

More...
DDBJi
Links Updated
AJ243797 mRNA Translation: CAB50866.1
AF151105 mRNA Translation: AAD48774.2 Different initiation.
AF319566 mRNA Translation: AAK07613.1
AF319567 mRNA Translation: AAK07614.1
AF319568 mRNA Translation: AAK07615.1
AF319569 mRNA Translation: AAK07616.1
AK315196 mRNA Translation: BAG37636.1
AL137745 mRNA No translation available.
AF483777 Genomic DNA Translation: AAL82504.1 Different initiation.
BC023630 mRNA Translation: AAH23630.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS2769.1 [Q9NSU2-3]
CCDS59451.1 [Q9NSU2-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
T46299

NCBI Reference Sequences

More...
RefSeqi
NP_009179.2, NM_007248.3 [Q9NSU2-2]
NP_057465.1, NM_016381.5
NP_338599.1, NM_033629.4 [Q9NSU2-3]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000444177; ENSP00000415972; ENSG00000213689 [Q9NSU2-2]
ENST00000625293; ENSP00000486676; ENSG00000213689 [Q9NSU2-3]

Database of genes from NCBI RefSeq genomes

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GeneIDi
11277

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:11277

UCSC genome browser

More...
UCSCi
uc031rzp.2 human [Q9NSU2-3]

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">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

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243797 mRNA Translation: CAB50866.1
AF151105 mRNA Translation: AAD48774.2 Different initiation.
AF319566 mRNA Translation: AAK07613.1
AF319567 mRNA Translation: AAK07614.1
AF319568 mRNA Translation: AAK07615.1
AF319569 mRNA Translation: AAK07616.1
AK315196 mRNA Translation: BAG37636.1
AL137745 mRNA No translation available.
AF483777 Genomic DNA Translation: AAL82504.1 Different initiation.
BC023630 mRNA Translation: AAH23630.1
CCDSiCCDS2769.1 [Q9NSU2-3]
CCDS59451.1 [Q9NSU2-2]
PIRiT46299
RefSeqiNP_009179.2, NM_007248.3 [Q9NSU2-2]
NP_057465.1, NM_016381.5
NP_338599.1, NM_033629.4 [Q9NSU2-3]

3D structure databases

SMRiQ9NSU2
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi116433, 13 interactors
IntActiQ9NSU2, 34 interactors
STRINGi9606.ENSP00000296443

PTM databases

iPTMnetiQ9NSU2
PhosphoSitePlusiQ9NSU2

Polymorphism and mutation databases

BioMutaiTREX1
DMDMi47606216

Proteomic databases

EPDiQ9NSU2
jPOSTiQ9NSU2
MassIVEiQ9NSU2
PaxDbiQ9NSU2
PeptideAtlasiQ9NSU2
PRIDEiQ9NSU2
ProteomicsDBi82580 [Q9NSU2-1]
82581 [Q9NSU2-2]
82582 [Q9NSU2-3]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
30103 273 antibodies

The DNASU plasmid repository

More...
DNASUi
11277

Genome annotation databases

EnsembliENST00000444177; ENSP00000415972; ENSG00000213689 [Q9NSU2-2]
ENST00000625293; ENSP00000486676; ENSG00000213689 [Q9NSU2-3]
GeneIDi11277
KEGGihsa:11277
UCSCiuc031rzp.2 human [Q9NSU2-3]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
11277
DisGeNETi11277
EuPathDBiHostDB:ENSG00000213689.10
HostDB:ENSG00000282827.1

GeneCards: human genes, protein and diseases

More...
GeneCardsi
TREX1
GeneReviewsiTREX1
HGNCiHGNC:12269 TREX1
HPAiENSG00000213689 Low tissue specificity
MalaCardsiTREX1
MIMi152700 phenotype
192315 phenotype
225750 phenotype
606609 gene
610448 phenotype
neXtProtiNX_Q9NSU2
OpenTargetsiENSG00000213689
Orphaneti51 Aicardi-Goutieres syndrome
481662 Familial Chilblain lupus
247691 Retinal vasculopathy with cerebral leukoencephalopathy and systemic manifestations
536 Systemic lupus erythematosus
PharmGKBiPA36949

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4793 Eukaryota
ENOG4111YSP LUCA
GeneTreeiENSGT00390000012715
HOGENOMiCLU_067419_1_0_1
InParanoidiQ9NSU2
KOiK10790
OMAiLAVHRCA
OrthoDBi1365966at2759
PhylomeDBiQ9NSU2
TreeFamiTF323333

Enzyme and pathway databases

ReactomeiR-HSA-3248023 Regulation by TREX1
R-HSA-3270619 IRF3-mediated induction of type I IFN

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
11277 1 hit in 790 CRISPR screens

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
TREX1

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

More...
GenomeRNAii
11277
PharosiQ9NSU2 Tbio

Protein Ontology

More...
PROi
PR:Q9NSU2
RNActiQ9NSU2 protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000213689 Expressed in adenohypophysis and 87 other tissues
ExpressionAtlasiQ9NSU2 baseline and differential
GenevisibleiQ9NSU2 HS

Family and domain databases

Gene3Di3.30.420.10, 1 hit
InterProiView protein in InterPro
IPR013520 Exonuclease_RNaseT/DNA_pol3
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
SMARTiView protein in SMART
SM00479 EXOIII, 1 hit
SUPFAMiSSF53098 SSF53098, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTREX1_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: Q9NSU2
Secondary accession number(s): B2RCN9
, Q8TEU2, Q9BPW1, Q9Y4X2
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: December 20, 2017
Last modified: June 17, 2020
This is version 184 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

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. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
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