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Entry version 151 (16 Oct 2019)
Sequence version 2 (31 Oct 2012)
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Protein

Exonuclease 3'-5' domain-containing protein 2

Gene

EXD2

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

Exonuclease that has both 3'-5' exoribonuclease and exodeoxyribonuclease activities, depending on the divalent metal cation used as cofactor (PubMed:29335528, PubMed:31127291). In presence of Mg2+, only shows 3'-5' exoribonuclease activity, while it shows both exoribonuclease and exodeoxyribonuclease activities in presence of Mn2+ (PubMed:29335528, PubMed:31127291). Acts as an exoribonuclease in mitochondrion, possibly by regulating ATP production and mitochondrial translation (PubMed:29335528). Also involved in the response to DNA damage (PubMed:26807646, PubMed:31255466). Acts as 3'-5' exodeoxyribonuclease for double-strand breaks resection and efficient homologous recombination (PubMed:20603073, PubMed:26807646). Plays a key role in controlling the initial steps of chromosomal break repair, it is recruited to chromatin in a damage-dependent manner and functionally interacts with the MRN complex to accelerate resection through its 3'-5' exonuclease activity, which efficiently processes double-stranded DNA substrates containing nicks (PubMed:26807646). Also involved in response to replicative stress: recruited to stalled forks and is required to stabilize and restart stalled replication forks by restraining excessive fork regression, thereby suppressing their degradation (PubMed:31255466).5 Publications

Caution

Subcellular location is subject to discussion. Different publications report a mitochondrial localization (PubMed:29335528, PubMed:29599527, PubMed:31127291). According to some reports, tranlocates to the nucleus in response of DNA damage (PubMed:26807646, PubMed:31255466). However, according to another publication, DNA damage does not result in nuclear translocation (PubMed:31127291). Its precise localization in mitochondrion is also controversial (PubMed:29335528, PubMed:29599527, PubMed:31127291). Two different groups report a localization to the mitochondrial outer membrane, which is consistent with the presence of a N-terminal transmembrane region (PubMed:29599527, PubMed:31127291). In contrast, a publication reports localization to the mitochondrial matrix; protease accessibility used in this assay can however lead to misinterpretation if the target protein is unexpectedly resistant to proteases (PubMed:29335528). Mechanisms that explain its dual role in mitochondrion and nuclear DNA repair are unknown and additional evidences are needed to reconciliate these two apparently incompatible functions.Curated5 Publications

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

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

Mg2+2 Publications, Mn2+2 PublicationsNote: Divalent metal cations; Mg2+ or Mn2+ (PubMed:31127291). Acts as a 3'-5' exoribonuclease in presence of Mg2+, while it has no 3'-5' exodeoxyribonuclease activity (PubMed:29335528, PubMed:31127291). Has both as a 3'-5' exoribonuclease and exodeoxyribonuclease activities in presence of Mn2+ (PubMed:31127291).2 Publications

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 bindingi108Divalent metal cation 1; catalyticCombined sources1 Publication1
Metal bindingi108Divalent metal cation 2; catalyticCombined sources1 Publication1
Metal bindingi110Divalent metal cation 1; catalyticCombined sources1 Publication1
Metal bindingi246Divalent metal cation 1; catalyticCombined sources1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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
Biological processDNA damage, DNA repair
LigandMagnesium, Manganese, Metal-binding

<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 3'-5' domain-containing protein 21 Publication (EC:3.1.11.12 Publications)
Alternative name(s):
3'-5' exoribonuclease EXD2Curated (EC:3.1.13.-2 Publications)
Exonuclease 3'-5' domain-like-containing protein 21 Publication
<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:EXD21 PublicationImported
Synonyms:C14orf114Imported, EXDL21 Publication
<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 14

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:20217 EXD2

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
616940 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9NVH0

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 4Mitochondrial intermembrane1 Publication4
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei5 – 25HelicalSequence analysisAdd BLAST21
Topological domaini26 – 621Cytoplasmic1 PublicationAdd BLAST596

Keywords - Cellular componenti

Chromosome, Membrane, Mitochondrion, Mitochondrion outer 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

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>Mutagenesisi108 – 110DCE → ACA: Loss of 3'-5' exonuclease activity. Impaired ability to stabilize and restart stalled replication forks in response to replication stress. 2 Publications3
Mutagenesisi190R → A: Abolished exodeoxyribonuclease activity. 1 Publication1
Mutagenesisi195R → A: Impaired exonuclease activity. 1 Publication1
Mutagenesisi197R → A: Impaired exonuclease activity. 1 Publication1
Mutagenesisi221K → A: Impaired exonuclease activity. 1 Publication1
Mutagenesisi226R → A: Abolished exonuclease activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
55218

Open Targets

More...
OpenTargetsi
ENSG00000081177

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA164719421

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q9NVH0

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
EXD2

Domain mapping of disease mutations (DMDM)

More...
DMDMi
410516875

<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_00000899241 – 621Exonuclease 3'-5' domain-containing protein 2Add BLAST621

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9NVH0

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q9NVH0

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q9NVH0

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9NVH0

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

More...
PaxDbi
Q9NVH0

PeptideAtlas

More...
PeptideAtlasi
Q9NVH0

PRoteomics IDEntifications database

More...
PRIDEi
Q9NVH0

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
33827
82795 [Q9NVH0-1]

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
Q9NVH0-2 [Q9NVH0-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9NVH0

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

More...
PhosphoSitePlusi
Q9NVH0

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000081177 Expressed in 217 organ(s), highest expression level in C1 segment of cervical spinal cord

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9NVH0 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9NVH0 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA002906
HPA005848

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

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

Homodimer (PubMed:31127291).

Interacts with RBBP8, MRE11 and BRCA1 (PubMed:26807646).

2 Publications

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

WithEntry#Exp.IntActNotes
Q997083EBI-11324738,EBI-745715

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
120514, 23 interactors

Database of interacting proteins

More...
DIPi
DIP-61996N

Protein interaction database and analysis system

More...
IntActi
Q9NVH0, 18 interactors

Molecular INTeraction database

More...
MINTi
Q9NVH0

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000313140

<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

1621
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
Q9NVH0

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini155 – 2473'-5' exonucleaseSequence analysisAdd BLAST93

<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 EXD2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4373 Eukaryota
ENOG410XS63 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000014318

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000046597

KEGG Orthology (KO)

More...
KOi
K20777

Identification of Orthologs from Complete Genome Data

More...
OMAi
DCEWITV

Database of Orthologous Groups

More...
OrthoDBi
692844at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9NVH0

TreeFam database of animal gene trees

More...
TreeFami
TF324246

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.420.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002562 3'-5'_exonuclease_dom
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01612 DNA_pol_A_exo1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00474 35EXOc, 1 hit

Superfamily database of structural and functional annotation

More...
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_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 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9NVH0-1) [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
MSRQNLVALT VTTLLGVAVG GFVLWKGIQR RRRSKTSPVT QQPQQKVLGS
60 70 80 90 100
RELPPPEDDQ LHSSAPRSSW KERILKAKVV TVSQEAEWDQ IEPLLRSELE
110 120 130 140 150
DFPVLGIDCE WVNLEGKASP LSLLQMASPS GLCVLVRLPK LICGGKTLPR
160 170 180 190 200
TLLDILADGT ILKVGVGCSE DASKLLQDYG LVVRGCLDLR YLAMRQRNNL
210 220 230 240 250
LCNGLSLKSL AETVLNFPLD KSLLLRCSNW DAETLTEDQV IYAARDAQIS
260 270 280 290 300
VALFLHLLGY PFSRNSPGEK NDDHSSWRKV LEKCQGVVDI PFRSKGMSRL
310 320 330 340 350
GEEVNGEATE SQQKPRNKKS KMDGMVPGNH QGRDPRKHKR KPLGVGYSAR
360 370 380 390 400
KSPLYDNCFL HAPDGQPLCT CDRRKAQWYL DKGIGELVSE EPFVVKLRFE
410 420 430 440 450
PAGRPESPGD YYLMVKENLC VVCGKRDSYI RKNVIPHEYR KHFPIEMKDH
460 470 480 490 500
NSHDVLLLCT SCHAISNYYD NHLKQQLAKE FQAPIGSEEG LRLLEDPERR
510 520 530 540 550
QVRSGARALL NAESLPTQRK EELLQALREF YNTDVVTEEM LQEAASLETR
560 570 580 590 600
ISNENYVPHG LKVVQCHSQG GLRSLMQLES RWRQHFLDSM QPKHLPQQWS
610 620
VDHNHQKLLR KFGEDLPIQL S
Length:621
Mass (Da):70,353
Last modified:October 31, 2012 - 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:iCD66A3E68A40C7FF
GO
Isoform 2 (identifier: Q9NVH0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-125: Missing.

Show »
Length:496
Mass (Da):56,346
Checksum:iD07693402FB5BFB6
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
C9JLF4C9JLF4_HUMAN
Exonuclease 3'-5' domain-containing...
EXD2
114Annotation 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 CAH10568 differs from that shown. Reason: Frameshift.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 conflicti287V → G in CAD39094 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_050980231D → N. Corresponds to variant dbSNP:rs35010854Ensembl.1
Natural variantiVAR_050981518Q → H2 PublicationsCorresponds to variant dbSNP:rs8007859Ensembl.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_0443671 – 125Missing in isoform 2. 3 PublicationsAdd BLAST125

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AK001600 mRNA Translation: BAA91781.1
AK295601 mRNA Translation: BAG58488.1
AL834434 mRNA Translation: CAD39094.2
BX647767 mRNA Translation: CAH10568.1 Frameshift.
AL359317 Genomic DNA No translation available.
CH471061 Genomic DNA Translation: EAW80985.1
BC001962 mRNA Translation: AAH01962.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS53902.1 [Q9NVH0-1]
CCDS9793.1 [Q9NVH0-2]

NCBI Reference Sequences

More...
RefSeqi
NP_001180289.1, NM_001193360.1 [Q9NVH0-1]
NP_001180290.1, NM_001193361.1 [Q9NVH0-1]
NP_001180291.1, NM_001193362.1 [Q9NVH0-1]
NP_001180292.1, NM_001193363.1 [Q9NVH0-1]
NP_060669.1, NM_018199.3 [Q9NVH0-2]
XP_005267874.1, XM_005267817.3 [Q9NVH0-2]
XP_011535210.1, XM_011536908.2 [Q9NVH0-2]
XP_016876910.1, XM_017021421.1 [Q9NVH0-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000312994; ENSP00000313140; ENSG00000081177 [Q9NVH0-1]
ENST00000409014; ENSP00000386915; ENSG00000081177 [Q9NVH0-2]
ENST00000409018; ENSP00000387331; ENSG00000081177 [Q9NVH0-1]
ENST00000409242; ENSP00000386839; ENSG00000081177 [Q9NVH0-2]
ENST00000409675; ENSP00000386762; ENSG00000081177 [Q9NVH0-2]
ENST00000409949; ENSP00000386632; ENSG00000081177 [Q9NVH0-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
55218

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:55218

UCSC genome browser

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UCSCi
uc001xkt.4 human [Q9NVH0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001600 mRNA Translation: BAA91781.1
AK295601 mRNA Translation: BAG58488.1
AL834434 mRNA Translation: CAD39094.2
BX647767 mRNA Translation: CAH10568.1 Frameshift.
AL359317 Genomic DNA No translation available.
CH471061 Genomic DNA Translation: EAW80985.1
BC001962 mRNA Translation: AAH01962.1
CCDSiCCDS53902.1 [Q9NVH0-1]
CCDS9793.1 [Q9NVH0-2]
RefSeqiNP_001180289.1, NM_001193360.1 [Q9NVH0-1]
NP_001180290.1, NM_001193361.1 [Q9NVH0-1]
NP_001180291.1, NM_001193362.1 [Q9NVH0-1]
NP_001180292.1, NM_001193363.1 [Q9NVH0-1]
NP_060669.1, NM_018199.3 [Q9NVH0-2]
XP_005267874.1, XM_005267817.3 [Q9NVH0-2]
XP_011535210.1, XM_011536908.2 [Q9NVH0-2]
XP_016876910.1, XM_017021421.1 [Q9NVH0-2]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6K17X-ray1.60A/B76-295[»]
6K18X-ray2.30A/B76-295[»]
6K19X-ray2.20A/B76-295[»]
6K1AX-ray2.60A/B76-295[»]
6K1BX-ray2.60A/B76-295[»]
6K1CX-ray2.45A/B76-295[»]
6K1DX-ray3.00A/B76-295[»]
6K1EX-ray2.90A/B76-295[»]
SMRiQ9NVH0
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi120514, 23 interactors
DIPiDIP-61996N
IntActiQ9NVH0, 18 interactors
MINTiQ9NVH0
STRINGi9606.ENSP00000313140

PTM databases

iPTMnetiQ9NVH0
PhosphoSitePlusiQ9NVH0

Polymorphism and mutation databases

BioMutaiEXD2
DMDMi410516875

Proteomic databases

EPDiQ9NVH0
jPOSTiQ9NVH0
MassIVEiQ9NVH0
MaxQBiQ9NVH0
PaxDbiQ9NVH0
PeptideAtlasiQ9NVH0
PRIDEiQ9NVH0
ProteomicsDBi33827
82795 [Q9NVH0-1]
TopDownProteomicsiQ9NVH0-2 [Q9NVH0-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
55218

Genome annotation databases

EnsembliENST00000312994; ENSP00000313140; ENSG00000081177 [Q9NVH0-1]
ENST00000409014; ENSP00000386915; ENSG00000081177 [Q9NVH0-2]
ENST00000409018; ENSP00000387331; ENSG00000081177 [Q9NVH0-1]
ENST00000409242; ENSP00000386839; ENSG00000081177 [Q9NVH0-2]
ENST00000409675; ENSP00000386762; ENSG00000081177 [Q9NVH0-2]
ENST00000409949; ENSP00000386632; ENSG00000081177 [Q9NVH0-2]
GeneIDi55218
KEGGihsa:55218
UCSCiuc001xkt.4 human [Q9NVH0-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
55218
DisGeNETi55218

GeneCards: human genes, protein and diseases

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GeneCardsi
EXD2
HGNCiHGNC:20217 EXD2
HPAiHPA002906
HPA005848
MIMi616940 gene
neXtProtiNX_Q9NVH0
OpenTargetsiENSG00000081177
PharmGKBiPA164719421

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4373 Eukaryota
ENOG410XS63 LUCA
GeneTreeiENSGT00390000014318
HOGENOMiHOG000046597
KOiK20777
OMAiDCEWITV
OrthoDBi692844at2759
PhylomeDBiQ9NVH0
TreeFamiTF324246

Miscellaneous databases

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

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ChiTaRSi
EXD2 human

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

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GenomeRNAii
55218
PharosiQ9NVH0

Protein Ontology

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PROi
PR:Q9NVH0

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000081177 Expressed in 217 organ(s), highest expression level in C1 segment of cervical spinal cord
ExpressionAtlasiQ9NVH0 baseline and differential
GenevisibleiQ9NVH0 HS

Family and domain databases

Gene3Di3.30.420.10, 1 hit
InterProiView protein in InterPro
IPR002562 3'-5'_exonuclease_dom
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
PfamiView protein in Pfam
PF01612 DNA_pol_A_exo1, 1 hit
SMARTiView protein in SMART
SM00474 35EXOc, 1 hit
SUPFAMiSSF53098 SSF53098, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiEXD2_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: Q9NVH0
Secondary accession number(s): B4DIH6
, G5E947, Q6AWB6, Q8N3D3
<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: October 24, 2003
Last sequence update: October 31, 2012
Last modified: October 16, 2019
This is version 151 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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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