UniProtKB - Q9NX46 (ADPRS_HUMAN)
Protein
ADP-ribose glycohydrolase ARH3
Gene
ADPRS
Organism
Homo sapiens (Human)
Status
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
Catalytic activityi
- EC:3.2.1.1433 PublicationsThis reaction proceeds in the forward3 Publications direction.
- This reaction proceeds in the forward2 Publications direction.
- This reaction proceeds in the forward2 Publications direction.
Cofactori
Mg2+4 PublicationsNote: Binds 2 magnesium ions per subunit.3 Publications
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 41 | Magnesium 2Combined sources3 Publications | 1 | |
Sitei | 41 | Glutamate flap2 Publications | 1 | |
Metal bindingi | 76 | Magnesium 1Combined sources3 Publications | 1 | |
Metal bindingi | 77 | Magnesium 1Combined sources3 Publications | 1 | |
Binding sitei | 77 | SubstrateCombined sources2 Publications | 1 | |
Metal bindingi | 78 | Magnesium 1Combined sources3 Publications | 1 | |
Binding sitei | 182 | SubstrateCombined sources2 Publications | 1 | |
Binding sitei | 235 | SubstrateCombined sources1 Publication | 1 | |
Binding sitei | 271 | SubstrateCombined sources1 Publication | 1 | |
Metal bindingi | 314 | Magnesium 2Combined sources3 Publications | 1 | |
Metal bindingi | 316 | Magnesium 1Combined sources3 Publications | 1 | |
Metal bindingi | 316 | Magnesium 2Combined sources3 Publications | 1 | |
Metal bindingi | 317 | Magnesium 2Combined sources3 Publications | 1 |
GO - Molecular functioni
- ADP-ribosylserine hydrolase activity Source: UniProtKB
- hydrolase activity, hydrolyzing O-glycosyl compounds Source: UniProtKB
- magnesium ion binding Source: UniProtKB
- O-acetyl-ADP-ribose deacetylase activity Source: UniProtKB
- poly(ADP-ribose) glycohydrolase activity Source: UniProtKB
GO - Biological processi
- cellular response to superoxide Source: UniProtKB
- DNA repair Source: UniProtKB
- peptidyl-serine ADP-deribosylation Source: UniProtKB
Keywordsi
Molecular function | Hydrolase |
Biological process | DNA damage, DNA repair |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BRENDAi | 3.2.1.143, 2681 |
PathwayCommonsi | Q9NX46 |
Reactomei | R-HSA-110362, POLB-Dependent Long Patch Base Excision Repair |
Names & Taxonomyi
Protein namesi | Recommended name: ADP-ribose glycohydrolase ARH3CuratedAlternative 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) |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000116863.10 |
HGNCi | HGNC:21304, ADPRS |
MIMi | 610624, gene |
neXtProti | NX_Q9NX46 |
Subcellular locationi
Mitochondrion
- Mitochondrion matrix 1 Publication1 Publication
Nucleus
- Nucleus 1 Publication
Other locations
- Cytoplasm 1 Publication
- Chromosome 1 Publication
Note: Recruited to DNA lesion regions following DNA damage; ADP-D-ribose-recognition is required for recruitment to DNA damage sites.1 Publication
Mitochondrion
- mitochondrial matrix Source: Reactome
- mitochondrion Source: GO_Central
Nucleus
- nuclear body Source: HPA
- nucleoplasm Source: HPA
- nucleus Source: UniProtKB
Other locations
- site of DNA damage Source: UniProtKB
Keywords - Cellular componenti
Chromosome, Cytoplasm, Mitochondrion, NucleusPathology & Biotechi
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 OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_081264 | 34 | D → N in CONDSIAS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1557732234EnsemblClinVar. | 1 | |
Natural variantiVAR_081265 | 79 | T → 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 PublicationCorresponds to variant dbSNP:rs1557733311EnsemblClinVar. | 1 | |
Natural variantiVAR_081266 | 106 – 363 | Missing in CONDSIAS; no detectable protein in patient fibroblasts. 1 PublicationAdd BLAST | 258 | |
Natural variantiVAR_081267 | 177 | S → L in CONDSIAS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs200626873EnsemblClinVar. | 1 | |
Natural variantiVAR_081268 | 248 – 249 | KI → N in CONDSIAS; no detectable protein levels in patient fibroblasts. 1 Publication | 2 | |
Natural variantiVAR_081269 | 334 – 363 | Missing in CONDSIAS; no detectable protein in patient fibroblasts. 1 PublicationAdd BLAST | 30 | |
Natural variantiVAR_081270 | 335 | V → 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:rs201735454EnsemblClinVar. | 1 | |
Natural variantiVAR_081271 | 346 – 363 | Missing in CONDSIAS; unknown pathological significance. 1 PublicationAdd BLAST | 18 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 41 | E → 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 Publications | 1 | |
Mutagenesisi | 77 – 78 | DD → AA: Retains ability to bind proteins ADP-ribosylated on serine but is unable to hydrolyze them. 1 Publication | 2 | |
Mutagenesisi | 77 – 78 | DD → NN: Complete loss of activity. 3 Publications | 2 | |
Mutagenesisi | 77 | D → 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 Publications | 1 | |
Mutagenesisi | 78 | D → N: Complete loss of activity. 1 Publication | 1 | |
Mutagenesisi | 115 | G → D: Abolished ability to bind and hydrolyze proteins ADP-ribosylated on serine. 1 Publication | 1 | |
Mutagenesisi | 148 | S → A: Complete loss of activity. Abolished recruitment to DNA lesion regions following DNA damage. Abolished ability to hydrolyze proteins ADP-ribosylated on serine. 3 Publications | 1 | |
Mutagenesisi | 149 | Y → A: Significant loss of activity. Abolished recruitment to DNA lesion regions following DNA damage. Abolished ability to hydrolyze proteins ADP-ribosylated on serine. 3 Publications | 1 | |
Mutagenesisi | 151 | N → A: Partial loss of activity. 1 Publication | 1 | |
Mutagenesisi | 182 | H → 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 Publications | 1 | |
Mutagenesisi | 238 – 239 | EE → QQ: Slight reduction in activity toward poly(ADP-ribose). Does not affect ability to degrade O-acetyl-ADP-D-ribose. 2 Publications | 2 | |
Mutagenesisi | 261 – 262 | EE → QQ: Slight reduction in activity toward poly(ADP-ribose). Does not affect ability to degrade O-acetyl-ADP-D-ribose. 2 Publications | 2 | |
Mutagenesisi | 314 | D → 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 Publications | 1 | |
Mutagenesisi | 314 | D → N: Significant loss of activity. 1 Publication | 1 | |
Mutagenesisi | 317 | T → 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 Publications | 1 | |
Mutagenesisi | 317 | T → S: Partial loss of activity. 1 Publication | 1 |
Keywords - Diseasei
Disease mutation, NeurodegenerationOrganism-specific databases
DisGeNETi | 54936 |
MalaCardsi | ADPRS |
MIMi | 618170, phenotype |
OpenTargetsi | ENSG00000116863 |
PharmGKBi | PA134903576 |
Miscellaneous databases
Pharosi | Q9NX46, Tbio |
Chemistry databases
ChEMBLi | CHEMBL4295963 |
Polymorphism and mutation databases
BioMutai | ADPRHL2 |
DMDMi | 74753038 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000277613 | 1 – 363 | ADP-ribose glycohydrolase ARH3Add BLAST | 363 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 64 | PhosphothreonineCombined sources | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
EPDi | Q9NX46 |
jPOSTi | Q9NX46 |
MassIVEi | Q9NX46 |
MaxQBi | Q9NX46 |
PaxDbi | Q9NX46 |
PeptideAtlasi | Q9NX46 |
PRIDEi | Q9NX46 |
ProteomicsDBi | 83037 |
TopDownProteomicsi | Q9NX46 |
PTM databases
iPTMneti | Q9NX46 |
MetOSitei | Q9NX46 |
PhosphoSitePlusi | Q9NX46 |
Expressioni
Tissue specificityi
Ubiquitous.1 Publication
Gene expression databases
Bgeei | ENSG00000116863, Expressed in vagina and 212 other tissues |
Genevisiblei | Q9NX46, HS |
Organism-specific databases
HPAi | ENSG00000116863, Low tissue specificity |
Interactioni
Subunit structurei
Monomer.
1 PublicationBinary interactionsi
Hide detailsQ9NX46
With | #Exp. | IntAct |
---|---|---|
PRDM5 - isoform 2 [Q9NQX1-2] | 3 | EBI-718580,EBI-12859340 |
TNKS [O95271] | 3 | EBI-718580,EBI-1105254 |
Protein-protein interaction databases
BioGRIDi | 120276, 26 interactors |
IntActi | Q9NX46, 7 interactors |
STRINGi | 9606.ENSP00000362273 |
Miscellaneous databases
RNActi | Q9NX46, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q9NX46 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q9NX46 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 146 – 152 | Substrate bindingCombined sources2 Publications | 7 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 2 – 10 | Poly-Ala | 9 |
Sequence similaritiesi
Belongs to the ADP-ribosylglycohydrolase family.Curated
Phylogenomic databases
eggNOGi | ENOG502QUER, Eukaryota |
GeneTreei | ENSGT00390000015369 |
HOGENOMi | CLU_024566_6_0_1 |
InParanoidi | Q9NX46 |
OMAi | RCCEGAE |
OrthoDBi | 988788at2759 |
PhylomeDBi | Q9NX46 |
TreeFami | TF324754 |
Family and domain databases
Gene3Di | 1.10.4080.10, 1 hit |
InterProi | View protein in InterPro IPR005502, Ribosyl_crysJ1 IPR036705, Ribosyl_crysJ1_sf |
Pfami | View protein in Pfam PF03747, ADP_ribosyl_GH, 1 hit |
SUPFAMi | SSF101478, SSF101478, 1 hit |
i Sequence
Sequence statusi: Complete.
Q9NX46-1 [UniParc]FASTAAdd to basket
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
Sequence cautioni
The sequence AAK14922 differs from that shown. Reason: Frameshift.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 109 | K → E in CAG33518 (Ref. 4) Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_081264 | 34 | D → N in CONDSIAS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1557732234EnsemblClinVar. | 1 | |
Natural variantiVAR_081265 | 79 | T → 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 PublicationCorresponds to variant dbSNP:rs1557733311EnsemblClinVar. | 1 | |
Natural variantiVAR_081266 | 106 – 363 | Missing in CONDSIAS; no detectable protein in patient fibroblasts. 1 PublicationAdd BLAST | 258 | |
Natural variantiVAR_081267 | 177 | S → L in CONDSIAS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs200626873EnsemblClinVar. | 1 | |
Natural variantiVAR_030579 | 209 | E → K1 PublicationCorresponds to variant dbSNP:rs2236387Ensembl. | 1 | |
Natural variantiVAR_081268 | 248 – 249 | KI → N in CONDSIAS; no detectable protein levels in patient fibroblasts. 1 Publication | 2 | |
Natural variantiVAR_081269 | 334 – 363 | Missing in CONDSIAS; no detectable protein in patient fibroblasts. 1 PublicationAdd BLAST | 30 | |
Natural variantiVAR_081270 | 335 | V → 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:rs201735454EnsemblClinVar. | 1 | |
Natural variantiVAR_081271 | 346 – 363 | Missing in CONDSIAS; unknown pathological significance. 1 PublicationAdd BLAST | 18 |
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 |
CCDSi | CCDS402.1 |
RefSeqi | NP_060295.1, NM_017825.2 |
Genome annotation databases
Ensembli | ENST00000373178; ENSP00000362273; ENSG00000116863 |
GeneIDi | 54936 |
KEGGi | hsa:54936 |
UCSCi | uc001bzt.4, human |
Keywords - Coding sequence diversityi
PolymorphismSimilar proteinsi
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 |
CCDSi | CCDS402.1 |
RefSeqi | NP_060295.1, NM_017825.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2FOZ | X-ray | 1.60 | A | 19-363 | [»] | |
2FP0 | X-ray | 2.05 | A/B | 19-363 | [»] | |
2G4K | X-ray | 1.82 | A | 18-363 | [»] | |
5ZQY | X-ray | 1.58 | A | 19-363 | [»] | |
6D36 | X-ray | 1.70 | A/B/C/D | 1-363 | [»] | |
6D3A | X-ray | 1.60 | A/B/C/D | 1-363 | [»] | |
SMRi | Q9NX46 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 120276, 26 interactors |
IntActi | Q9NX46, 7 interactors |
STRINGi | 9606.ENSP00000362273 |
Chemistry databases
ChEMBLi | CHEMBL4295963 |
PTM databases
iPTMneti | Q9NX46 |
MetOSitei | Q9NX46 |
PhosphoSitePlusi | Q9NX46 |
Polymorphism and mutation databases
BioMutai | ADPRHL2 |
DMDMi | 74753038 |
Proteomic databases
EPDi | Q9NX46 |
jPOSTi | Q9NX46 |
MassIVEi | Q9NX46 |
MaxQBi | Q9NX46 |
PaxDbi | Q9NX46 |
PeptideAtlasi | Q9NX46 |
PRIDEi | Q9NX46 |
ProteomicsDBi | 83037 |
TopDownProteomicsi | Q9NX46 |
Protocols and materials databases
Antibodypediai | 17409, 106 antibodies |
Genome annotation databases
Ensembli | ENST00000373178; ENSP00000362273; ENSG00000116863 |
GeneIDi | 54936 |
KEGGi | hsa:54936 |
UCSCi | uc001bzt.4, human |
Organism-specific databases
CTDi | 54936 |
DisGeNETi | 54936 |
EuPathDBi | HostDB:ENSG00000116863.10 |
GeneCardsi | ADPRS |
HGNCi | HGNC:21304, ADPRS |
HPAi | ENSG00000116863, Low tissue specificity |
MalaCardsi | ADPRS |
MIMi | 610624, gene 618170, phenotype |
neXtProti | NX_Q9NX46 |
OpenTargetsi | ENSG00000116863 |
PharmGKBi | PA134903576 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | ENOG502QUER, Eukaryota |
GeneTreei | ENSGT00390000015369 |
HOGENOMi | CLU_024566_6_0_1 |
InParanoidi | Q9NX46 |
OMAi | RCCEGAE |
OrthoDBi | 988788at2759 |
PhylomeDBi | Q9NX46 |
TreeFami | TF324754 |
Enzyme and pathway databases
BRENDAi | 3.2.1.143, 2681 |
PathwayCommonsi | Q9NX46 |
Reactomei | R-HSA-110362, POLB-Dependent Long Patch Base Excision Repair |
Miscellaneous databases
BioGRID-ORCSi | 54936, 53 hits in 845 CRISPR screens |
EvolutionaryTracei | Q9NX46 |
GeneWikii | ADPRHL2 |
GenomeRNAii | 54936 |
Pharosi | Q9NX46, Tbio |
PROi | PR:Q9NX46 |
RNActi | Q9NX46, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000116863, Expressed in vagina and 212 other tissues |
Genevisiblei | Q9NX46, HS |
Family and domain databases
Gene3Di | 1.10.4080.10, 1 hit |
InterProi | View protein in InterPro IPR005502, Ribosyl_crysJ1 IPR036705, Ribosyl_crysJ1_sf |
Pfami | View protein in Pfam PF03747, ADP_ribosyl_GH, 1 hit |
SUPFAMi | SSF101478, SSF101478, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ADPRS_HUMAN | |
Accessioni | Q9NX46Primary (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: | December 2, 2020 | |
This is version 165 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Reference proteomeDocuments
- Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries