Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 155 (08 May 2019)
Sequence version 1 (01 Oct 2000)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

ADP-ribose glycohydrolase ARH3

Gene

ADPRHL2

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

ADP-ribose glycohydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose (PubMed:21498885, PubMed:30045870, PubMed:29907568, PubMed:30401461). Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response (PubMed:28650317, PubMed:29234005, PubMed:30045870). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:29480802). Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds (PubMed:16278211). Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos (PubMed:16278211). Also hydrolyzes free poly(ADP-ribose) in mitochondria (PubMed:22433848). Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins (PubMed:17075046, PubMed:21498885). Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers (PubMed:21498885).10 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+4 PublicationsNote: Binds 2 magnesium ions per subunit.3 Publications

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

The protein undergoes a dramatic conformational switch from closed to open states upon substrate-binding, which enables specific substrate recognition for the 1''-O-linkage (PubMed:29907568). The glutamate flap (Glu-41) blocks substrate entrance to Mg2+ in the unliganded closed state (PubMed:30045870, PubMed:29907568). In presence of substrate, Glu-41 is ejected from the active site: this closed-to-open transition significantly widens the substrate-binding channel and precisely positions the scissile 1''-O-linkage for cleavage while securing tightly 2'- and 3'-hydroxyls of ADP-ribose (PubMed:30045870, PubMed:29907568).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 bindingi41Magnesium 2Combined sources3 Publications1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei41Glutamate flap2 Publications1
Metal bindingi76Magnesium 1Combined sources3 Publications1
Metal bindingi77Magnesium 1Combined sources3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei77SubstrateCombined sources2 Publications1
Metal bindingi78Magnesium 1Combined sources3 Publications1
Binding sitei182SubstrateCombined sources2 Publications1
Binding sitei235SubstrateCombined sources1 Publication1
Binding sitei271SubstrateCombined sources1 Publication1
Metal bindingi314Magnesium 2Combined sources3 Publications1
Metal bindingi316Magnesium 1Combined sources3 Publications1
Metal bindingi316Magnesium 2Combined sources3 Publications1
Metal bindingi317Magnesium 2Combined sources3 Publications1

<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 functionHydrolase
Biological processDNA damage, DNA repair
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.143 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-110362 POLB-Dependent Long Patch Base Excision Repair

<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:
ADP-ribose glycohydrolase ARH3Curated
Alternative name(s):
ADP-ribosylhydrolase 31 Publication
O-acetyl-ADP-ribose deacetylase ARH3Curated (EC:3.5.1.-2 Publications)
Poly(ADP-ribose) glycohydrolase ARH3Curated (EC:3.2.1.1433 Publications)
[Protein ADP-ribosylarginine] hydrolase-like protein 2Curated
[Protein ADP-ribosylserine] hydrolaseCurated (EC:3.2.2.-2 Publications)
<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:ADPRHL2Imported
Synonyms:ARH31 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 1

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:21304 ADPRHL2

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
610624 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9NX46

<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

Chromosome, Cytoplasm, Mitochondrion, 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

Neurodegeneration, childhood-onset, stress-induced, with variable ataxia and seizures (CONDSIAS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive neurodegenerative disorder characterized by pediatric onset of progressive brain atrophy, developmental regression, and seizures in association with periods of stress, such as infections.
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_08126434D → N in CONDSIAS; unknown pathological significance. 1 Publication1
Natural variantiVAR_08126579T → P in CONDSIAS; severely reduced protein levels in patient fibroblasts; decreased stability and reduced Tm; reduced alpha-helix content and altered secondary structure detected by circular dichroism spectroscopy. 1 Publication1
Natural variantiVAR_081266106 – 363Missing in CONDSIAS; no detectable protein in patient fibroblasts. 1 PublicationAdd BLAST258
Natural variantiVAR_081267177S → L in CONDSIAS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs200626873Ensembl.1
Natural variantiVAR_081268248 – 249KI → N in CONDSIAS; no detectable protein levels in patient fibroblasts. 1 Publication2
Natural variantiVAR_081269334 – 363Missing in CONDSIAS; no detectable protein in patient fibroblasts. 1 PublicationAdd BLAST30
Natural variantiVAR_081270335V → G in CONDSIAS; results in accumulation of poly(ADP-ribose) in patient cells after exposure to H(2)O(2); no detectable protein levels in patient fibroblasts. 1 PublicationCorresponds to variant dbSNP:rs201735454Ensembl.1
Natural variantiVAR_081271346 – 363Missing in CONDSIAS; unknown pathological significance. 1 PublicationAdd BLAST18

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>Mutagenesisi41E → A or Q: Significant loss of activity. Does not affect recruitment to DNA lesion regions following DNA damage. Strongly reduced ability to hydrolyze proteins ADP-ribosylated on serine. 3 Publications1
Mutagenesisi77 – 78DD → AA: Retains ability to bind proteins ADP-ribosylated on serine but is unable to hydrolyze them. 1 Publication2
Mutagenesisi77 – 78DD → NN: Complete loss of activity. 3 Publications2
Mutagenesisi77D → N or A: Complete loss of activity. Does not affect recruitment to DNA lesion regions following DNA damage. Strongly reduced ability to hydrolyze proteins ADP-ribosylated on serine. 4 Publications1
Mutagenesisi78D → N: Complete loss of activity. 1 Publication1
Mutagenesisi115G → D: Abolished ability to bind and hydrolyze proteins ADP-ribosylated on serine. 1 Publication1
Mutagenesisi148S → A: Complete loss of activity. Abolished recruitment to DNA lesion regions following DNA damage. Abolished ability to hydrolyze proteins ADP-ribosylated on serine. 3 Publications1
Mutagenesisi149Y → A: Significant loss of activity. Abolished recruitment to DNA lesion regions following DNA damage. Abolished ability to hydrolyze proteins ADP-ribosylated on serine. 3 Publications1
Mutagenesisi151N → A: Partial loss of activity. 1 Publication1
Mutagenesisi182H → Q or A: Complete loss of activity. Abolished recruitment to DNA lesion regions following DNA damage. Abolished ability to hydrolyze proteins ADP-ribosylated on serine. 3 Publications1
Mutagenesisi238 – 239EE → QQ: Slight reduction in activity toward poly(ADP-ribose). Does not affect ability to degrade O-acetyl-ADP-D-ribose. 2 Publications2
Mutagenesisi261 – 262EE → QQ: Slight reduction in activity toward poly(ADP-ribose). Does not affect ability to degrade O-acetyl-ADP-D-ribose. 2 Publications2
Mutagenesisi314D → A or E: Complete loss of activity. Does not affect recruitment to DNA lesion regions following DNA damage. Retains ability to bind proteins ADP-ribosylated on serine but is unable to hydrolyze them. 4 Publications1
Mutagenesisi314D → N: Significant loss of activity. 1 Publication1
Mutagenesisi317T → A: Complete loss of activity. Does not affect recruitment to DNA lesion regions following DNA damage. Retains ability to bind proteins ADP-ribosylated on serine but is unable to hydrolyze them. 3 Publications1
Mutagenesisi317T → S: Partial loss of activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNET

More...
DisGeNETi
54936
MIMi618170 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000116863

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA134903576

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ADPRHL2

Domain mapping of disease mutations (DMDM)

More...
DMDMi
74753038

<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_00002776131 – 363ADP-ribose glycohydrolase ARH3Add BLAST363

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 residuei64PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9NX46

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q9NX46

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9NX46

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

More...
PaxDbi
Q9NX46

PeptideAtlas

More...
PeptideAtlasi
Q9NX46

PRoteomics IDEntifications database

More...
PRIDEi
Q9NX46

ProteomicsDB human proteome resource

More...
ProteomicsDBi
83037

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
Q9NX46

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9NX46

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

More...
PhosphoSitePlusi
Q9NX46

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

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

Ubiquitous.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000116863 Expressed in 199 organ(s), highest expression level in vagina

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9NX46 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA027104
HPA027141

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

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

Monomer.1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
120276, 12 interactors

Protein interaction database and analysis system

More...
IntActi
Q9NX46, 5 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000362273

<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

1363
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

More...
SMRi
Q9NX46

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9NX46

<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>Regioni146 – 152Substrate bindingCombined sources2 Publications7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi2 – 10Poly-Ala9

<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 ADP-ribosylglycohydrolase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IGSE Eukaryota
COG1397 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000015369

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000225333

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9NX46

KEGG Orthology (KO)

More...
KOi
K11687

Identification of Orthologs from Complete Genome Data

More...
OMAi
LQRTIIY

Database of Orthologous Groups

More...
OrthoDBi
988788at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9NX46

TreeFam database of animal gene trees

More...
TreeFami
TF324754

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.4080.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005502 Ribosyl_crysJ1
IPR036705 Ribosyl_crysJ1_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03747 ADP_ribosyl_GH, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF101478 SSF101478, 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>Sequencei

<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.

Q9NX46-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAAAAMAAAA GGGAGAARSL SRFRGCLAGA LLGDCVGSFY EAHDTVDLTS
60 70 80 90 100
VLRHVQSLEP DPGTPGSERT EALYYTDDTA MARALVQSLL AKEAFDEVDM
110 120 130 140 150
AHRFAQEYKK DPDRGYGAGV VTVFKKLLNP KCRDVFEPAR AQFNGKGSYG
160 170 180 190 200
NGGAMRVAGI SLAYSSVQDV QKFARLSAQL THASSLGYNG AILQALAVHL
210 220 230 240 250
ALQGESSSEH FLKQLLGHME DLEGDAQSVL DARELGMEER PYSSRLKKIG
260 270 280 290 300
ELLDQASVTR EEVVSELGNG IAAFESVPTA IYCFLRCMEP DPEIPSAFNS
310 320 330 340 350
LQRTLIYSIS LGGDTDTIAT MAGAIAGAYY GMDQVPESWQ QSCEGYEETD
360
ILAQSLHRVF QKS
Length:363
Mass (Da):38,947
Last modified:October 1, 2000 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5FD99F59F27CD29F
GO

<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 AAK14922 differs from that shown. Reason: Frameshift at several positions.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 conflicti109K → E in CAG33518 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_08126434D → N in CONDSIAS; unknown pathological significance. 1 Publication1
Natural variantiVAR_08126579T → P in CONDSIAS; severely reduced protein levels in patient fibroblasts; decreased stability and reduced Tm; reduced alpha-helix content and altered secondary structure detected by circular dichroism spectroscopy. 1 Publication1
Natural variantiVAR_081266106 – 363Missing in CONDSIAS; no detectable protein in patient fibroblasts. 1 PublicationAdd BLAST258
Natural variantiVAR_081267177S → L in CONDSIAS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs200626873Ensembl.1
Natural variantiVAR_030579209E → K1 PublicationCorresponds to variant dbSNP:rs2236387Ensembl.1
Natural variantiVAR_081268248 – 249KI → N in CONDSIAS; no detectable protein levels in patient fibroblasts. 1 Publication2
Natural variantiVAR_081269334 – 363Missing in CONDSIAS; no detectable protein in patient fibroblasts. 1 PublicationAdd BLAST30
Natural variantiVAR_081270335V → G in CONDSIAS; results in accumulation of poly(ADP-ribose) in patient cells after exposure to H(2)O(2); no detectable protein levels in patient fibroblasts. 1 PublicationCorresponds to variant dbSNP:rs201735454Ensembl.1
Natural variantiVAR_081271346 – 363Missing in CONDSIAS; unknown pathological significance. 1 PublicationAdd BLAST18

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
AJ313333 Genomic DNA Translation: CAC85940.1
AJ427295 mRNA Translation: CAD20316.1
AF212236 mRNA Translation: AAK14922.1 Frameshift.
AK000453 mRNA Translation: BAA91174.1
CR457237 mRNA Translation: CAG33518.1
AK223037 mRNA Translation: BAD96757.1
AL138787 Genomic DNA No translation available.
BC014169 mRNA Translation: AAH14169.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS402.1

NCBI Reference Sequences

More...
RefSeqi
NP_060295.1, NM_017825.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000373178; ENSP00000362273; ENSG00000116863

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
54936

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:54936

UCSC genome browser

More...
UCSCi
uc001bzt.4 human

Keywords - Coding sequence diversityi

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
AJ313333 Genomic DNA Translation: CAC85940.1
AJ427295 mRNA Translation: CAD20316.1
AF212236 mRNA Translation: AAK14922.1 Frameshift.
AK000453 mRNA Translation: BAA91174.1
CR457237 mRNA Translation: CAG33518.1
AK223037 mRNA Translation: BAD96757.1
AL138787 Genomic DNA No translation available.
BC014169 mRNA Translation: AAH14169.1
CCDSiCCDS402.1
RefSeqiNP_060295.1, NM_017825.2

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
2FOZX-ray1.60A19-363[»]
2FP0X-ray2.05A/B19-363[»]
2G4KX-ray1.82A18-363[»]
5ZQYX-ray1.58A19-363[»]
6D36X-ray1.70A/B/C/D1-363[»]
6D3AX-ray1.60A/B/C/D1-363[»]
SMRiQ9NX46
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120276, 12 interactors
IntActiQ9NX46, 5 interactors
STRINGi9606.ENSP00000362273

PTM databases

iPTMnetiQ9NX46
PhosphoSitePlusiQ9NX46

Polymorphism and mutation databases

BioMutaiADPRHL2
DMDMi74753038

Proteomic databases

EPDiQ9NX46
jPOSTiQ9NX46
MaxQBiQ9NX46
PaxDbiQ9NX46
PeptideAtlasiQ9NX46
PRIDEiQ9NX46
ProteomicsDBi83037
TopDownProteomicsiQ9NX46

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373178; ENSP00000362273; ENSG00000116863
GeneIDi54936
KEGGihsa:54936
UCSCiuc001bzt.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
54936
DisGeNETi54936

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ADPRHL2
HGNCiHGNC:21304 ADPRHL2
HPAiHPA027104
HPA027141
MIMi610624 gene
618170 phenotype
neXtProtiNX_Q9NX46
OpenTargetsiENSG00000116863
PharmGKBiPA134903576

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IGSE Eukaryota
COG1397 LUCA
GeneTreeiENSGT00390000015369
HOGENOMiHOG000225333
InParanoidiQ9NX46
KOiK11687
OMAiLQRTIIY
OrthoDBi988788at2759
PhylomeDBiQ9NX46
TreeFamiTF324754

Enzyme and pathway databases

BRENDAi3.2.1.143 2681
ReactomeiR-HSA-110362 POLB-Dependent Long Patch Base Excision Repair

Miscellaneous databases

EvolutionaryTraceiQ9NX46

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
ADPRHL2

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

More...
GenomeRNAii
54936

Protein Ontology

More...
PROi
PR:Q9NX46

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000116863 Expressed in 199 organ(s), highest expression level in vagina
GenevisibleiQ9NX46 HS

Family and domain databases

Gene3Di1.10.4080.10, 1 hit
InterProiView protein in InterPro
IPR005502 Ribosyl_crysJ1
IPR036705 Ribosyl_crysJ1_sf
PfamiView protein in Pfam
PF03747 ADP_ribosyl_GH, 1 hit
SUPFAMiSSF101478 SSF101478, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiARHL2_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: Q9NX46
Secondary accession number(s): Q53G94, Q6IAB8, Q9BY47
<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: February 6, 2007
Last sequence update: October 1, 2000
Last modified: May 8, 2019
This is version 155 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again