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Entry version 172 (13 Nov 2019)
Sequence version 2 (24 Jan 2006)
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Protein

Exonuclease 1

Gene

EXO1

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

5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair (MMR) to excise mismatch-containing DNA tracts directed by strand breaks located either 5' or 3' to the mismatch. Also exhibits endonuclease activity against 5'-overhanging flap structures similar to those generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Required for somatic hypermutation (SHM) and class switch recombination (CSR) of immunoglobulin genes. Essential for male and female meiosis.12 Publications

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

Mg2+By similarityNote: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi30Magnesium 1By similarity1
Metal bindingi78Magnesium 1By similarity1
Metal bindingi150Magnesium 1By similarity1
Metal bindingi152Magnesium 1By similarity1
Metal bindingi171Magnesium 2By similarity1
Metal bindingi173Magnesium 2By similarity1
Metal bindingi225Magnesium 2By 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 functionDNA-binding, Endonuclease, Excision nuclease, Exonuclease, Hydrolase, Nuclease
Biological processDNA damage, DNA excision, DNA repair, Immunity, Meiosis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.1.11.1 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-HSA-5358606 Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)
R-HSA-5685938 HDR through Single Strand Annealing (SSA)
R-HSA-5685942 HDR through Homologous Recombination (HRR)
R-HSA-5693554 Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-HSA-5693568 Resolution of D-loop Structures through Holliday Junction Intermediates
R-HSA-5693579 Homologous DNA Pairing and Strand Exchange
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-69473 G2/M DNA damage checkpoint

SIGNOR Signaling Network Open Resource

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SIGNORi
Q9UQ84

<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:
Exonuclease 1 (EC:3.1.-.-)
Short name:
hExo1
Alternative name(s):
Exonuclease I
Short name:
hExoI
<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:EXO1
Synonyms:EXOI, HEX1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:3511 EXO1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
606063 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9UQ84

<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

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi78D → A: Abrogates double-stranded DNA exonuclease activity and endonuclease activity against 5'-overhanging flap structures. Also reduces DNA-binding to 5'-overhanging flap structures. 1 Publication1
Mutagenesisi173D → A: Abrogates double-stranded DNA exonuclease activity and endonuclease activity against 5'-overhanging flap structures. No effect on DNA-binding to 5'-overhanging flap structures. 2 Publications1
Mutagenesisi225D → A: Abrogates double-stranded DNA exonuclease activity and endonuclease activity against 5'-overhanging flap structures. Also enhances DNA-binding to 5'-overhanging flap structures. 1 Publication1
Mutagenesisi418K → A or T: Complete loss of nuclear localization. 1 Publication1
Mutagenesisi419R → A: Complete loss of nuclear localization. 1 Publication1
Mutagenesisi454S → A: No rescue of HU-induced degradation. No rescue of HU-induced degradation; when associated with A-714. Loss of HU-sensitivity and resistance to HU-induced degradation; when associated with A-621 and A-714. 1 Publication1
Mutagenesisi621T → A: No rescue of HU-induced degradation. No rescue of HU-induced degradation; when associated with A-714. Loss of HU-sensitivity and resistance to HU-induced degradation; when associated with A-454 and A-714. 1 Publication1
Mutagenesisi714S → A: No rescue of HU-induced degradation and loss of HU-induced increase of phosphorylation. No rescue of HU-induced degradation; when associated with A-621. No rescue of HU-induced degradation; when associated with A-454. Loss of HU-sensitivity and resistance to HU-induced degradation; when associated with A-454 and A-621. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
9156

Open Targets

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OpenTargetsi
ENSG00000174371

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27923

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q9UQ84

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
EXO1

Domain mapping of disease mutations (DMDM)

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DMDMi
85700954

<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_00001540391 – 846Exonuclease 1Add BLAST846

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 residuei376Phosphoserine1 Publication1
Modified residuei422PhosphoserineCombined sources1 Publication1
Modified residuei454Phosphoserine1 Publication1
Modified residuei482N6-acetyllysine1 Publication1
Modified residuei581Phosphothreonine1 Publication1
Modified residuei598PhosphoserineCombined sources1 Publication1
Modified residuei610PhosphoserineCombined sources1
Modified residuei621Phosphothreonine1 Publication1
Modified residuei623PhosphoserineCombined sources1 Publication1
Modified residuei639Phosphoserine1 Publication1
Modified residuei660Phosphoserine1 Publication1
Modified residuei674Phosphoserine1 Publication1
Modified residuei714Phosphoserine; by ATR1 Publication1
Modified residuei746Phosphoserine1 Publication1

<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

Phosphorylated upon DNA damage and in response to agents stalling DNA replication, probably by ATM or ATR. Phosphorylation at Ser-454, Thr-621 and Ser-714 is induced upon DNA-damage caused by treatment with hydroxyurea (HU) but not upon IR treatment. The HU-induced EXO1 triple phosphorylation facilitates destabilisation/degradation of the protein.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9UQ84

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9UQ84

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q9UQ84

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

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PaxDbi
Q9UQ84

PeptideAtlas

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PeptideAtlasi
Q9UQ84

PRoteomics IDEntifications database

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PRIDEi
Q9UQ84

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
85518 [Q9UQ84-1]
85519 [Q9UQ84-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9UQ84

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

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PhosphoSitePlusi
Q9UQ84

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

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

Highly expressed in bone marrow, testis and thymus. Expressed at lower levels in colon, lymph nodes, ovary, placenta, prostate, small intestine, spleen and stomach.4 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Highly expressed in fetal liver and at lower levels in fetal brain, heart, kidney, spleen and thymus.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000174371 Expressed in 105 organ(s), highest expression level in lung

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9UQ84 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9UQ84 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA053079
HPA069738

<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

Interacts with the MLH1-PMS2 heterodimer via MLH1.

Interacts with MSH3.

Interacts with the MSH2-MSH6 heterodimer via MSH2, and this interaction may increase the processivity of the 5'->3' exonuclease activity.

Interacts with PCNA, and this interaction may both stimulate the cryptic 3'->5' exonuclease activity and suppress the 5'->3' exonuclease activity.

Interacts with WRN, and this interaction stimulates both the 5'->3' exonuclease activity and cleavage of 5'-overhanging flap structures.

Interacts with RECQL/RECQ1, and this interaction stimulates cleavage of 5'-overhanging flap structures.

9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
114602, 34 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9UQ84

Database of interacting proteins

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DIPi
DIP-36701N

Protein interaction database and analysis system

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IntActi
Q9UQ84, 19 interactors

Molecular INTeraction database

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MINTi
Q9UQ84

STRING: functional protein association networks

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STRINGi
9606.ENSP00000355506

<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

1846
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
Q9UQ84

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q9UQ84

<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>Regioni1 – 99N-domainAdd BLAST99
Regioni129 – 387Interaction with MSH31 PublicationAdd BLAST259
Regioni138 – 229I-domainAdd BLAST92
Regioni388 – 490Interaction with MLH1Add BLAST103
Regioni600 – 846Interaction with MSH2Add BLAST247
Regioni787 – 846Interaction with MLH1Add BLAST60

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi418 – 421Nuclear localization signal4

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2518 Eukaryota
COG0258 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00510000047676

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9UQ84

KEGG Orthology (KO)

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KOi
K10746

Identification of Orthologs from Complete Genome Data

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OMAi
HESEYGD

Database of Orthologous Groups

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OrthoDBi
796591at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9UQ84

TreeFam database of animal gene trees

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TreeFami
TF314997

Family and domain databases

Conserved Domains Database

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CDDi
cd09908 H3TH_EXO1, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR036279 5-3_exonuclease_C_sf
IPR032641 Exo1
IPR037315 EXO1_H3TH
IPR008918 HhH2
IPR029060 PIN-like_dom_sf
IPR006086 XPG-I_dom
IPR006084 XPG/Rad2
IPR019974 XPG_CS
IPR006085 XPG_DNA_repair_N

The PANTHER Classification System

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PANTHERi
PTHR11081 PTHR11081, 1 hit
PTHR11081:SF53 PTHR11081:SF53, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00867 XPG_I, 1 hit
PF00752 XPG_N, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00853 XPGRADSUPER

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00279 HhH2, 1 hit
SM00484 XPGI, 1 hit
SM00485 XPGN, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47807 SSF47807, 1 hit
SSF88723 SSF88723, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00841 XPG_1, 1 hit
PS00842 XPG_2, 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>. 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 (2+)i

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

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9UQ84-1) [UniParc]FASTAAdd to basket
Also known as: B

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
MGIQGLLQFI KEASEPIHVR KYKGQVVAVD TYCWLHKGAI ACAEKLAKGE
60 70 80 90 100
PTDRYVGFCM KFVNMLLSHG IKPILVFDGC TLPSKKEVER SRRERRQANL
110 120 130 140 150
LKGKQLLREG KVSEARECFT RSINITHAMA HKVIKAARSQ GVDCLVAPYE
160 170 180 190 200
ADAQLAYLNK AGIVQAIITE DSDLLAFGCK KVILKMDQFG NGLEIDQARL
210 220 230 240 250
GMCRQLGDVF TEEKFRYMCI LSGCDYLSSL RGIGLAKACK VLRLANNPDI
260 270 280 290 300
VKVIKKIGHY LKMNITVPED YINGFIRANN TFLYQLVFDP IKRKLIPLNA
310 320 330 340 350
YEDDVDPETL SYAGQYVDDS IALQIALGNK DINTFEQIDD YNPDTAMPAH
360 370 380 390 400
SRSHSWDDKT CQKSANVSSI WHRNYSPRPE SGTVSDAPQL KENPSTVGVE
410 420 430 440 450
RVISTKGLNL PRKSSIVKRP RSAELSEDDL LSQYSLSFTK KTKKNSSEGN
460 470 480 490 500
KSLSFSEVFV PDLVNGPTNK KSVSTPPRTR NKFATFLQRK NEESGAVVVP
510 520 530 540 550
GTRSRFFCSS DSTDCVSNKV SIQPLDETAV TDKENNLHES EYGDQEGKRL
560 570 580 590 600
VDTDVARNSS DDIPNNHIPG DHIPDKATVF TDEESYSFES SKFTRTISPP
610 620 630 640 650
TLGTLRSCFS WSGGLGDFSR TPSPSPSTAL QQFRRKSDSP TSLPENNMSD
660 670 680 690 700
VSQLKSEESS DDESHPLREE ACSSQSQESG EFSLQSSNAS KLSQCSSKDS
710 720 730 740 750
DSEESDCNIK LLDSQSDQTS KLRLSHFSKK DTPLRNKVPG LYKSSSADSL
760 770 780 790 800
STTKIKPLGP ARASGLSKKP ASIQKRKHHN AENKPGLQIK LNELWKNFGF
810 820 830 840
KKDSEKLPPC KKPLSPVRDN IQLTPEAEED IFNKPECGRV QRAIFQ
Length:846
Mass (Da):94,103
Last modified:January 24, 2006 - 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:i850BC21CA9790D08
GO
Isoform 2 (identifier: Q9UQ84-4) [UniParc]FASTAAdd to basket
Also known as: A

The sequence of this isoform differs from the canonical sequence as follows:
     803-803: D → F
     804-846: Missing.

Show »
Length:803
Mass (Da):89,231
Checksum:i1EDC61DB5D70A0B6
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 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5T398Q5T398_HUMAN
Exonuclease 1
EXO1
166Annotation 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>
Q5T397Q5T397_HUMAN
Exonuclease 1
EXO1
169Annotation 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>
H0YAZ2H0YAZ2_HUMAN
Exonuclease 1
EXO1
208Annotation 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>
Q5T399Q5T399_HUMAN
Exonuclease 1
EXO1
135Annotation 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>
E5RGY3E5RGY3_HUMAN
Exonuclease 1
EXO1
95Annotation 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>
E5RHK1E5RHK1_HUMAN
Exonuclease 1
EXO1
11Annotation score:

Annotation score:1 out of 5

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

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

The sequence AAC33874 differs from that shown. Reason: Frameshift.Curated

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

Most naturally occurring variants in this protein are not associated with familial disposition to hereditary non-polyposis colorectal cancer (HNPCC) (PubMed:12517792). Furthermore, germline deletions involving this locus are not associated with clinically manifested colorectal tumors (PubMed:14623461).2 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_02496627V → A1 PublicationCorresponds to variant dbSNP:rs1472620416Ensembl.1
Natural variantiVAR_02496776V → I1 PublicationCorresponds to variant dbSNP:rs4149864Ensembl.1
Natural variantiVAR_02496893R → G1 PublicationCorresponds to variant dbSNP:rs4149865Ensembl.1
Natural variantiVAR_024969109E → K Abrogates exonuclease activity. 2 PublicationsCorresponds to variant dbSNP:rs143546023Ensembl.1
Natural variantiVAR_024970137A → S1 PublicationCorresponds to variant dbSNP:rs147663824Ensembl.1
Natural variantiVAR_077352153A → V1 Publication1
Natural variantiVAR_024971279N → S1 PublicationCorresponds to variant dbSNP:rs4149909Ensembl.1
Natural variantiVAR_024972299N → S1 PublicationCorresponds to variant dbSNP:rs4149910Ensembl.1
Natural variantiVAR_024973354H → R5 PublicationsCorresponds to variant dbSNP:rs735943Ensembl.1
Natural variantiVAR_024974410L → R Abrogates exonuclease activity. 3 PublicationsCorresponds to variant dbSNP:rs571928768Ensembl.1
Natural variantiVAR_024975428D → N1 PublicationCorresponds to variant dbSNP:rs4149962Ensembl.1
Natural variantiVAR_024976438F → C1 Publication1
Natural variantiVAR_024977439T → M May be associated with an increased risk of colorectal cancer. 3 PublicationsCorresponds to variant dbSNP:rs4149963Ensembl.1
Natural variantiVAR_024978456S → Y1 PublicationCorresponds to variant dbSNP:rs4149964Ensembl.1
Natural variantiVAR_024979458V → M1 PublicationCorresponds to variant dbSNP:rs4149965Ensembl.1
Natural variantiVAR_024980460V → L1 PublicationCorresponds to variant dbSNP:rs4149966Ensembl.1
Natural variantiVAR_024981503R → T1 PublicationCorresponds to variant dbSNP:rs4149967Ensembl.1
Natural variantiVAR_024982589E → K6 PublicationsCorresponds to variant dbSNP:rs1047840Ensembl.1
Natural variantiVAR_024983610S → G2 PublicationsCorresponds to variant dbSNP:rs12122770Ensembl.1
Natural variantiVAR_024984634R → Q1 PublicationCorresponds to variant dbSNP:rs4149978Ensembl.1
Natural variantiVAR_024985640P → A2 PublicationsCorresponds to variant dbSNP:rs61736331Ensembl.1
Natural variantiVAR_024986640P → S Reduces interaction with MSH2; abrogates interaction with MSH2; when associated with L-770. 3 PublicationsCorresponds to variant dbSNP:rs61736331Ensembl.1
Natural variantiVAR_024987670E → G8 PublicationsCorresponds to variant dbSNP:rs1776148Ensembl.1
Natural variantiVAR_024988723R → C7 PublicationsCorresponds to variant dbSNP:rs1635498Ensembl.1
Natural variantiVAR_024989726H → P1 Publication1
Natural variantiVAR_024990757P → L May be associated with a reduced risk of colorectal cancer. 4 PublicationsCorresponds to variant dbSNP:rs9350Ensembl.1
Natural variantiVAR_024991759G → E Reduces interaction with MSH2; abrogates interaction with MSH2; when associated with L-770. 4 PublicationsCorresponds to variant dbSNP:rs4150001EnsemblClinVar.1
Natural variantiVAR_024992770P → L Reduces interaction with MSH2; abrogates interaction with MSH2; when associated with S-640 or E-759. 2 PublicationsCorresponds to variant dbSNP:rs200622305Ensembl.1
Natural variantiVAR_024993827A → V1 PublicationCorresponds to variant dbSNP:rs145975455Ensembl.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_017029803D → F in isoform 2. 1 Publication1
Alternative sequenceiVSP_017030804 – 846Missing in isoform 2. 1 PublicationAdd BLAST43

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
AF084974 mRNA Translation: AAD13754.1
AF091740 mRNA Translation: AAC63043.1
AF091754
, AF091742, AF091743, AF091744, AF091745, AF091746, AF091747, AF091748, AF091749, AF091750, AF091751, AF091752, AF091753 Genomic DNA Translation: AAC69879.1
AF091754
, AF091742, AF091743, AF091744, AF091745, AF091746, AF091747, AF091748, AF091749, AF091750, AF091751, AF091752, AF091753 Genomic DNA Translation: AAC69880.1
AF042282 mRNA Translation: AAC32259.1
AC004783 Genomic DNA Translation: AAC32424.1
AF060479 mRNA Translation: AAC33874.1 Frameshift.
AF549168 Genomic DNA Translation: AAN39382.1
AL365366 Genomic DNA No translation available.
BC007491 mRNA Translation: AAH07491.1
AL080139 mRNA Translation: CAB45733.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS1620.1 [Q9UQ84-1]
CCDS44336.1 [Q9UQ84-4]

Protein sequence database of the Protein Information Resource

More...
PIRi
T12524

NCBI Reference Sequences

More...
RefSeqi
NP_003677.4, NM_003686.4 [Q9UQ84-4]
NP_006018.4, NM_006027.4 [Q9UQ84-1]
NP_569082.2, NM_130398.3 [Q9UQ84-1]
XP_006711903.1, XM_006711840.2 [Q9UQ84-1]
XP_011542623.1, XM_011544321.1 [Q9UQ84-1]
XP_011542624.1, XM_011544322.1 [Q9UQ84-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000348581; ENSP00000311873; ENSG00000174371 [Q9UQ84-1]
ENST00000366548; ENSP00000355506; ENSG00000174371 [Q9UQ84-1]
ENST00000518483; ENSP00000430251; ENSG00000174371 [Q9UQ84-4]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
9156

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:9156

UCSC genome browser

More...
UCSCi
uc001hzh.4 human [Q9UQ84-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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

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

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

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF084974 mRNA Translation: AAD13754.1
AF091740 mRNA Translation: AAC63043.1
AF091754
, AF091742, AF091743, AF091744, AF091745, AF091746, AF091747, AF091748, AF091749, AF091750, AF091751, AF091752, AF091753 Genomic DNA Translation: AAC69879.1
AF091754
, AF091742, AF091743, AF091744, AF091745, AF091746, AF091747, AF091748, AF091749, AF091750, AF091751, AF091752, AF091753 Genomic DNA Translation: AAC69880.1
AF042282 mRNA Translation: AAC32259.1
AC004783 Genomic DNA Translation: AAC32424.1
AF060479 mRNA Translation: AAC33874.1 Frameshift.
AF549168 Genomic DNA Translation: AAN39382.1
AL365366 Genomic DNA No translation available.
BC007491 mRNA Translation: AAH07491.1
AL080139 mRNA Translation: CAB45733.1
CCDSiCCDS1620.1 [Q9UQ84-1]
CCDS44336.1 [Q9UQ84-4]
PIRiT12524
RefSeqiNP_003677.4, NM_003686.4 [Q9UQ84-4]
NP_006018.4, NM_006027.4 [Q9UQ84-1]
NP_569082.2, NM_130398.3 [Q9UQ84-1]
XP_006711903.1, XM_006711840.2 [Q9UQ84-1]
XP_011542623.1, XM_011544321.1 [Q9UQ84-1]
XP_011542624.1, XM_011544322.1 [Q9UQ84-1]

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
3QE9X-ray2.51Y/Z1-352[»]
3QEAX-ray3.10Z1-352[»]
3QEBX-ray3.00Z1-352[»]
5UZVX-ray2.45Z1-352[»]
5V04X-ray2.65Z1-352[»]
5V05X-ray2.90Z1-352[»]
5V06X-ray2.75Z1-352[»]
5V07X-ray2.15Z1-352[»]
5V08X-ray2.81Z1-352[»]
5V09X-ray2.75Z1-352[»]
5V0AX-ray2.38Z1-352[»]
5V0BX-ray2.63Z1-352[»]
5V0CX-ray2.58Z1-352[»]
5V0DX-ray2.63Z1-352[»]
5V0EX-ray2.74Z1-352[»]
SMRiQ9UQ84
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi114602, 34 interactors
CORUMiQ9UQ84
DIPiDIP-36701N
IntActiQ9UQ84, 19 interactors
MINTiQ9UQ84
STRINGi9606.ENSP00000355506

PTM databases

iPTMnetiQ9UQ84
PhosphoSitePlusiQ9UQ84

Polymorphism and mutation databases

BioMutaiEXO1
DMDMi85700954

Proteomic databases

EPDiQ9UQ84
jPOSTiQ9UQ84
MassIVEiQ9UQ84
PaxDbiQ9UQ84
PeptideAtlasiQ9UQ84
PRIDEiQ9UQ84
ProteomicsDBi85518 [Q9UQ84-1]
85519 [Q9UQ84-4]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
9156

Genome annotation databases

EnsembliENST00000348581; ENSP00000311873; ENSG00000174371 [Q9UQ84-1]
ENST00000366548; ENSP00000355506; ENSG00000174371 [Q9UQ84-1]
ENST00000518483; ENSP00000430251; ENSG00000174371 [Q9UQ84-4]
GeneIDi9156
KEGGihsa:9156
UCSCiuc001hzh.4 human [Q9UQ84-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
9156
DisGeNETi9156

GeneCards: human genes, protein and diseases

More...
GeneCardsi
EXO1
HGNCiHGNC:3511 EXO1
HPAiHPA053079
HPA069738
MIMi606063 gene
neXtProtiNX_Q9UQ84
OpenTargetsiENSG00000174371
PharmGKBiPA27923

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2518 Eukaryota
COG0258 LUCA
GeneTreeiENSGT00510000047676
InParanoidiQ9UQ84
KOiK10746
OMAiHESEYGD
OrthoDBi796591at2759
PhylomeDBiQ9UQ84
TreeFamiTF314997

Enzyme and pathway databases

BRENDAi3.1.11.1 2681
ReactomeiR-HSA-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-HSA-5358606 Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)
R-HSA-5685938 HDR through Single Strand Annealing (SSA)
R-HSA-5685942 HDR through Homologous Recombination (HRR)
R-HSA-5693554 Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-HSA-5693568 Resolution of D-loop Structures through Holliday Junction Intermediates
R-HSA-5693579 Homologous DNA Pairing and Strand Exchange
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-69473 G2/M DNA damage checkpoint
SIGNORiQ9UQ84

Miscellaneous databases

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

More...
ChiTaRSi
EXO1 human
EvolutionaryTraceiQ9UQ84

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Exonuclease_1

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

More...
GenomeRNAii
9156
PharosiQ9UQ84

Protein Ontology

More...
PROi
PR:Q9UQ84

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000174371 Expressed in 105 organ(s), highest expression level in lung
ExpressionAtlasiQ9UQ84 baseline and differential
GenevisibleiQ9UQ84 HS

Family and domain databases

CDDicd09908 H3TH_EXO1, 1 hit
InterProiView protein in InterPro
IPR036279 5-3_exonuclease_C_sf
IPR032641 Exo1
IPR037315 EXO1_H3TH
IPR008918 HhH2
IPR029060 PIN-like_dom_sf
IPR006086 XPG-I_dom
IPR006084 XPG/Rad2
IPR019974 XPG_CS
IPR006085 XPG_DNA_repair_N
PANTHERiPTHR11081 PTHR11081, 1 hit
PTHR11081:SF53 PTHR11081:SF53, 1 hit
PfamiView protein in Pfam
PF00867 XPG_I, 1 hit
PF00752 XPG_N, 1 hit
PRINTSiPR00853 XPGRADSUPER
SMARTiView protein in SMART
SM00279 HhH2, 1 hit
SM00484 XPGI, 1 hit
SM00485 XPGN, 1 hit
SUPFAMiSSF47807 SSF47807, 1 hit
SSF88723 SSF88723, 1 hit
PROSITEiView protein in PROSITE
PS00841 XPG_1, 1 hit
PS00842 XPG_2, 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 nameiEXO1_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: Q9UQ84
Secondary accession number(s): O60545
, O75214, O75466, Q5T396, Q96IJ1, Q9UG38, Q9UNW0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: November 13, 2019
This is version 172 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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