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Protein

[Protein ADP-ribosylarginine] hydrolase

Gene

ADPRH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reverse reaction of mono-ADP-ribosylation.

Catalytic activityi

Protein-N(omega)-(ADP-D-ribosyl)-L-arginine + H2O = ADP-D-ribose + protein-L-arginine.
N(omega)-(ADP-D-ribosyl)-L-arginine + H2O = ADP-D-ribose + L-arginine.

GO - Molecular functioni

  • ADP-ribosylarginine hydrolase activity Source: UniProtKB
  • magnesium ion binding Source: InterPro

GO - Biological processi

  • cellular protein modification process Source: UniProtKB
  • protein de-ADP-ribosylation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium

Names & Taxonomyi

Protein namesi
Recommended name:
[Protein ADP-ribosylarginine] hydrolase (EC:3.2.2.19)
Short name:
ADP-ribosylarginine hydrolase
Alternative name(s):
ADP-ribose-L-arginine cleaving enzyme
Gene namesi
Name:ADPRH
Synonyms:ARH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:269. ADPRH.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24590.

Polymorphism and mutation databases

BioMutaiADPRH.
DMDMi1703392.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 357357[Protein ADP-ribosylarginine] hydrolasePRO_0000157283Add
BLAST

Proteomic databases

MaxQBiP54922.
PaxDbiP54922.
PRIDEiP54922.

2D gel databases

OGPiP54922.

PTM databases

PhosphoSiteiP54922.

Expressioni

Gene expression databases

BgeeiP54922.
CleanExiHS_ADPRH.
ExpressionAtlasiP54922. baseline and differential.
GenevisibleiP54922. HS.

Organism-specific databases

HPAiCAB001701.
HPA036961.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TFCP2Q128003EBI-6657604,EBI-717422

Protein-protein interaction databases

BioGridi106651. 4 interactions.
IntActiP54922. 4 interactions.
MINTiMINT-7288433.
STRINGi9606.ENSP00000349496.

Structurei

Secondary structure

1
357
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1918Combined sources
Turni20 – 267Combined sources
Helixi30 – 3910Combined sources
Helixi43 – 453Combined sources
Helixi48 – 503Combined sources
Helixi55 – 7016Combined sources
Helixi76 – 9015Combined sources
Helixi91 – 933Combined sources
Helixi101 – 1099Combined sources
Turni115 – 1184Combined sources
Turni129 – 1313Combined sources
Helixi132 – 1343Combined sources
Helixi137 – 1415Combined sources
Helixi145 – 1473Combined sources
Helixi148 – 16013Combined sources
Helixi166 – 18318Combined sources
Helixi188 – 1903Combined sources
Helixi191 – 20919Combined sources
Helixi213 – 2197Combined sources
Helixi221 – 23414Combined sources
Helixi251 – 26111Combined sources
Beta strandi262 – 2654Combined sources
Helixi273 – 28513Combined sources
Helixi289 – 2968Combined sources
Beta strandi298 – 3025Combined sources
Helixi303 – 31816Combined sources
Turni319 – 3224Combined sources
Helixi325 – 3273Combined sources
Turni328 – 3303Combined sources
Helixi334 – 34815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HFWX-ray1.92A1-357[»]
ProteinModelPortaliP54922.
SMRiP54922. Positions 1-357.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54922.

Family & Domainsi

Sequence similaritiesi

Belongs to the ADP-ribosylglycohydrolase family.Curated

Phylogenomic databases

eggNOGiCOG1397.
GeneTreeiENSGT00530000063627.
HOGENOMiHOG000007974.
HOVERGENiHBG050462.
InParanoidiP54922.
KOiK01245.
OMAiSGYFVEE.
OrthoDBiEOG7SFHWT.
PhylomeDBiP54922.
TreeFamiTF329417.

Family and domain databases

InterProiIPR012108. ADP-ribosylarg_hydro.
IPR005502. Ribosyl_crysJ1.
[Graphical view]
PfamiPF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view]
PIRSFiPIRSF016939. ADP_ribslarg_hdr. 1 hit.
SUPFAMiSSF101478. SSF101478. 1 hit.

Sequencei

Sequence statusi: Complete.

P54922-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKYVAAMVL SAAGDALGYY NGKWEFLQDG EKIHRQLAQL GGLDALDVGR
60 70 80 90 100
WRVSDDTVMH LATAEALVEA GKAPKLTQLY YLLAKHYQDC MEDMDGRAPG
110 120 130 140 150
GASVHNAMQL KPGKPNGWRI PFNSHEGGCG AAMRAMCIGL RFPHHSQLDT
160 170 180 190 200
LIQVSIESGR MTHHHPTGYL GALASALFTA YAVNSRPPLQ WGKGLMELLP
210 220 230 240 250
EAKKYIVQSG YFVEENLQHW SYFQTKWENY LKLRGILDGE SAPTFPESFG
260 270 280 290 300
VKERDQFYTS LSYSGWGGSS GHDAPMIAYD AVLAAGDSWK ELAHRAFFHG
310 320 330 340 350
GDSDSTAAIA GCWWGVMYGF KGVSPSNYEK LEYRNRLEET ARALYSLGSK

EDTVISL
Length:357
Mass (Da):39,507
Last modified:October 1, 1996 - v1
Checksum:i4E23B12FAE84F12B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13291 mRNA. Translation: AAA35555.1.
AK313369 mRNA. Translation: BAG36168.1.
CH471052 Genomic DNA. Translation: EAW79562.1.
CH471052 Genomic DNA. Translation: EAW79563.1.
BC063883 mRNA. Translation: AAH63883.1.
BC074769 mRNA. Translation: AAH74769.1.
CCDSiCCDS2990.1.
PIRiB47411.
RefSeqiNP_001116.1. NM_001125.3.
NP_001278878.1. NM_001291949.1.
NP_001278879.1. NM_001291950.1.
UniGeneiHs.99884.

Genome annotation databases

EnsembliENST00000357003; ENSP00000349496; ENSG00000144843.
ENST00000465513; ENSP00000417430; ENSG00000144843.
ENST00000478399; ENSP00000420200; ENSG00000144843.
ENST00000478927; ENSP00000417528; ENSG00000144843.
GeneIDi141.
KEGGihsa:141.
UCSCiuc003ecs.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13291 mRNA. Translation: AAA35555.1.
AK313369 mRNA. Translation: BAG36168.1.
CH471052 Genomic DNA. Translation: EAW79562.1.
CH471052 Genomic DNA. Translation: EAW79563.1.
BC063883 mRNA. Translation: AAH63883.1.
BC074769 mRNA. Translation: AAH74769.1.
CCDSiCCDS2990.1.
PIRiB47411.
RefSeqiNP_001116.1. NM_001125.3.
NP_001278878.1. NM_001291949.1.
NP_001278879.1. NM_001291950.1.
UniGeneiHs.99884.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HFWX-ray1.92A1-357[»]
ProteinModelPortaliP54922.
SMRiP54922. Positions 1-357.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106651. 4 interactions.
IntActiP54922. 4 interactions.
MINTiMINT-7288433.
STRINGi9606.ENSP00000349496.

PTM databases

PhosphoSiteiP54922.

Polymorphism and mutation databases

BioMutaiADPRH.
DMDMi1703392.

2D gel databases

OGPiP54922.

Proteomic databases

MaxQBiP54922.
PaxDbiP54922.
PRIDEiP54922.

Protocols and materials databases

DNASUi141.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357003; ENSP00000349496; ENSG00000144843.
ENST00000465513; ENSP00000417430; ENSG00000144843.
ENST00000478399; ENSP00000420200; ENSG00000144843.
ENST00000478927; ENSP00000417528; ENSG00000144843.
GeneIDi141.
KEGGihsa:141.
UCSCiuc003ecs.3. human.

Organism-specific databases

CTDi141.
GeneCardsiGC03P119298.
HGNCiHGNC:269. ADPRH.
HPAiCAB001701.
HPA036961.
MIMi603081. gene.
neXtProtiNX_P54922.
PharmGKBiPA24590.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1397.
GeneTreeiENSGT00530000063627.
HOGENOMiHOG000007974.
HOVERGENiHBG050462.
InParanoidiP54922.
KOiK01245.
OMAiSGYFVEE.
OrthoDBiEOG7SFHWT.
PhylomeDBiP54922.
TreeFamiTF329417.

Miscellaneous databases

EvolutionaryTraceiP54922.
GenomeRNAii141.
NextBioi561.
PROiP54922.
SOURCEiSearch...

Gene expression databases

BgeeiP54922.
CleanExiHS_ADPRH.
ExpressionAtlasiP54922. baseline and differential.
GenevisibleiP54922. HS.

Family and domain databases

InterProiIPR012108. ADP-ribosylarg_hydro.
IPR005502. Ribosyl_crysJ1.
[Graphical view]
PfamiPF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view]
PIRSFiPIRSF016939. ADP_ribslarg_hdr. 1 hit.
SUPFAMiSSF101478. SSF101478. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase."
    Takada T., Iida K., Moss J.
    J. Biol. Chem. 268:17837-17843(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.

Entry informationi

Entry nameiADPRH_HUMAN
AccessioniPrimary (citable) accession number: P54922
Secondary accession number(s): B2R8H1, D3DN83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 121 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. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.