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Protein

Poly(ADP-ribose) glycohydrolase ARH3

Gene

ADPRHL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. Poly(ADP-ribose) metabolism may be required for maintenance of the normal function of neuronal cells. Generates ADP-ribose from poly-(ADP-ribose), but does not hydrolyze ADP-ribose-arginine, -cysteine, -diphthamide, or -asparagine bonds. Due to catalytic inactivity of PARG mitochondrial isoforms, ARH3 is the only PAR hydrolyzing enzyme in mitochondria.1 Publication

Catalytic activityi

Hydrolyzes poly(ADP-D-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-D-ribose.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 2 magnesium ions per subunit.1 Publication

Enzyme regulationi

Activity is enhanced by magnesium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi41Magnesium 21
Metal bindingi76Magnesium 11
Metal bindingi77Magnesium 11
Metal bindingi78Magnesium 11
Binding sitei254SubstrateBy similarity1
Metal bindingi314Magnesium 21
Metal bindingi316Magnesium 11
Metal bindingi316Magnesium 21
Metal bindingi317Magnesium 21

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS04064-MONOMER.
BRENDAi3.2.1.143. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(ADP-ribose) glycohydrolase ARH3 (EC:3.2.1.143)
Alternative name(s):
ADP-ribosylhydrolase 3
[Protein ADP-ribosylarginine] hydrolase-like protein 2
Gene namesi
Name:ADPRHL2
Synonyms:ARH3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:21304. ADPRHL2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi41E → A or Q: Significant loss of activity. 1 Publication1
Mutagenesisi77 – 78DD → NN: Complete loss of activity. 1 Publication2
Mutagenesisi77D → N: Complete loss of activity. 1 Publication1
Mutagenesisi148S → A: Complete loss of activity. 1 Publication1
Mutagenesisi149Y → A: Significant loss of activity. 1 Publication1
Mutagenesisi151N → A: Partial loss of activity. 1 Publication1
Mutagenesisi182H → Q: Complete loss of activity. 1 Publication1
Mutagenesisi238 – 239EE → QQ: Slight reduction in activity. 1 Publication2
Mutagenesisi261 – 262EE → QQ: Slight reduction in activity. 1 Publication2
Mutagenesisi314D → E: Complete loss of activity. 1 Publication1
Mutagenesisi314D → N: Significant loss of activity. 1 Publication1
Mutagenesisi317T → A: Complete loss of activity. 1 Publication1
Mutagenesisi317T → S: Partial loss of activity. 1 Publication1

Organism-specific databases

DisGeNETi54936.
OpenTargetsiENSG00000116863.
PharmGKBiPA134903576.

Polymorphism and mutation databases

BioMutaiADPRHL2.
DMDMi74753038.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 27MitochondrionSequence analysisAdd BLAST27
ChainiPRO_000027761328 – 363Poly(ADP-ribose) glycohydrolase ARH3Add BLAST336

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei64PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NX46.
MaxQBiQ9NX46.
PaxDbiQ9NX46.
PeptideAtlasiQ9NX46.
PRIDEiQ9NX46.
TopDownProteomicsiQ9NX46.

PTM databases

iPTMnetiQ9NX46.
PhosphoSitePlusiQ9NX46.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSG00000116863.
CleanExiHS_ADPRHL2.
GenevisibleiQ9NX46. HS.

Organism-specific databases

HPAiHPA027104.
HPA027141.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi120276. 10 interactors.
IntActiQ9NX46. 3 interactors.
MINTiMINT-1420706.
STRINGi9606.ENSP00000362273.

Structurei

Secondary structure

1363
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi19 – 37Combined sources19
Helixi38 – 40Combined sources3
Helixi48 – 56Combined sources9
Helixi77 – 92Combined sources16
Helixi97 – 110Combined sources14
Turni112 – 115Combined sources4
Helixi118 – 127Combined sources10
Helixi137 – 141Combined sources5
Turni142 – 146Combined sources5
Helixi152 – 155Combined sources4
Helixi158 – 163Combined sources6
Helixi167 – 179Combined sources13
Helixi185 – 201Combined sources17
Helixi208 – 222Combined sources15
Helixi226 – 234Combined sources9
Helixi241 – 254Combined sources14
Beta strandi255 – 257Combined sources3
Helixi260 – 267Combined sources8
Beta strandi270 – 272Combined sources3
Helixi273 – 275Combined sources3
Helixi277 – 286Combined sources10
Helixi300 – 310Combined sources11
Helixi315 – 330Combined sources16
Helixi332 – 334Combined sources3
Helixi337 – 341Combined sources5
Helixi346 – 360Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FOZX-ray1.60A19-363[»]
2FP0X-ray2.05A/B19-363[»]
2G4KX-ray1.82A18-363[»]
ProteinModelPortaliQ9NX46.
SMRiQ9NX46.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NX46.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 10Poly-Ala9

Sequence similaritiesi

Belongs to the ADP-ribosylglycohydrolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IGSE. Eukaryota.
COG1397. LUCA.
GeneTreeiENSGT00390000015369.
HOGENOMiHOG000225333.
HOVERGENiHBG080863.
InParanoidiQ9NX46.
KOiK11687.
OMAiKCRDVYE.
OrthoDBiEOG091G0DA4.
PhylomeDBiQ9NX46.
TreeFamiTF324754.

Family and domain databases

InterProiIPR005502. Ribosyl_crysJ1.
[Graphical view]
PfamiPF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view]
SUPFAMiSSF101478. SSF101478. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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
Checksum:i5FD99F59F27CD29F
GO

Sequence cautioni

The sequence AAK14922 differs from that shown. Reason: Frameshift at several positions.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti109K → E in CAG33518 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_030579209E → K.1 PublicationCorresponds to variant rs2236387dbSNPEnsembl.1

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. Translation: CAC21453.1.
BC014169 mRNA. Translation: AAH14169.1.
CCDSiCCDS402.1.
RefSeqiNP_060295.1. NM_017825.2.
UniGeneiHs.18021.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

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. Translation: CAC21453.1.
BC014169 mRNA. Translation: AAH14169.1.
CCDSiCCDS402.1.
RefSeqiNP_060295.1. NM_017825.2.
UniGeneiHs.18021.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FOZX-ray1.60A19-363[»]
2FP0X-ray2.05A/B19-363[»]
2G4KX-ray1.82A18-363[»]
ProteinModelPortaliQ9NX46.
SMRiQ9NX46.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120276. 10 interactors.
IntActiQ9NX46. 3 interactors.
MINTiMINT-1420706.
STRINGi9606.ENSP00000362273.

PTM databases

iPTMnetiQ9NX46.
PhosphoSitePlusiQ9NX46.

Polymorphism and mutation databases

BioMutaiADPRHL2.
DMDMi74753038.

Proteomic databases

EPDiQ9NX46.
MaxQBiQ9NX46.
PaxDbiQ9NX46.
PeptideAtlasiQ9NX46.
PRIDEiQ9NX46.
TopDownProteomicsiQ9NX46.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi54936.
DisGeNETi54936.
GeneCardsiADPRHL2.
HGNCiHGNC:21304. ADPRHL2.
HPAiHPA027104.
HPA027141.
MIMi610624. gene.
neXtProtiNX_Q9NX46.
OpenTargetsiENSG00000116863.
PharmGKBiPA134903576.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGSE. Eukaryota.
COG1397. LUCA.
GeneTreeiENSGT00390000015369.
HOGENOMiHOG000225333.
HOVERGENiHBG080863.
InParanoidiQ9NX46.
KOiK11687.
OMAiKCRDVYE.
OrthoDBiEOG091G0DA4.
PhylomeDBiQ9NX46.
TreeFamiTF324754.

Enzyme and pathway databases

BioCyciZFISH:HS04064-MONOMER.
BRENDAi3.2.1.143. 2681.

Miscellaneous databases

EvolutionaryTraceiQ9NX46.
GeneWikiiADPRHL2.
GenomeRNAii54936.
PROiQ9NX46.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000116863.
CleanExiHS_ADPRHL2.
GenevisibleiQ9NX46. HS.

Family and domain databases

InterProiIPR005502. Ribosyl_crysJ1.
[Graphical view]
PfamiPF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view]
SUPFAMiSSF101478. SSF101478. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiARHL2_HUMAN
AccessioniPrimary (citable) accession number: Q9NX46
Secondary accession number(s): Q53G94, Q6IAB8, Q9BY47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  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
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.