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P54922

- ADPRH_HUMAN

UniProt

P54922 - ADPRH_HUMAN

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Protein
[Protein ADP-ribosylarginine] hydrolase
Gene
ADPRH, ARH1
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. ADP-ribosylarginine hydrolase activity Source: UniProtKB
  2. magnesium ion binding Source: InterPro

GO - Biological processi

  1. cellular protein modification process Source: UniProtKB
  2. 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: Chromosome 3

Organism-specific databases

HGNCiHGNC:269. ADPRH.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24590.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 357357[Protein ADP-ribosylarginine] hydrolase
PRO_0000157283Add
BLAST

Proteomic databases

MaxQBiP54922.
PaxDbiP54922.
PRIDEiP54922.

2D gel databases

OGPiP54922.

PTM databases

PhosphoSiteiP54922.

Expressioni

Gene expression databases

ArrayExpressiP54922.
BgeeiP54922.
CleanExiHS_ADPRH.
GenevestigatoriP54922.

Organism-specific databases

HPAiCAB001701.

Interactioni

Protein-protein interaction databases

BioGridi106651. 3 interactions.
IntActiP54922. 3 interactions.
MINTiMINT-7288433.
STRINGi9606.ENSP00000349496.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HFWX-ray1.92A1-357[»]
ProteinModelPortaliP54922.
SMRiP54922. Positions 1-357.

Miscellaneous databases

EvolutionaryTraceiP54922.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1397.
HOGENOMiHOG000007974.
HOVERGENiHBG050462.
InParanoidiP54922.
KOiK01245.
OMAiGKGLMEV.
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

MEKYVAAMVL SAAGDALGYY NGKWEFLQDG EKIHRQLAQL GGLDALDVGR    50
WRVSDDTVMH LATAEALVEA GKAPKLTQLY YLLAKHYQDC MEDMDGRAPG 100
GASVHNAMQL KPGKPNGWRI PFNSHEGGCG AAMRAMCIGL RFPHHSQLDT 150
LIQVSIESGR MTHHHPTGYL GALASALFTA YAVNSRPPLQ WGKGLMELLP 200
EAKKYIVQSG YFVEENLQHW SYFQTKWENY LKLRGILDGE SAPTFPESFG 250
VKERDQFYTS LSYSGWGGSS GHDAPMIAYD AVLAAGDSWK ELAHRAFFHG 300
GDSDSTAAIA GCWWGVMYGF KGVSPSNYEK LEYRNRLEET ARALYSLGSK 350
EDTVISL 357
Length:357
Mass (Da):39,507
Last modified:October 1, 1996 - v1
Checksum:i4E23B12FAE84F12B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UniGeneiHs.99884.

Genome annotation databases

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

Polymorphism databases

DMDMi1703392.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2990.1.
PIRi B47411.
RefSeqi NP_001116.1. NM_001125.3.
UniGenei Hs.99884.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3HFW X-ray 1.92 A 1-357 [» ]
ProteinModelPortali P54922.
SMRi P54922. Positions 1-357.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106651. 3 interactions.
IntActi P54922. 3 interactions.
MINTi MINT-7288433.
STRINGi 9606.ENSP00000349496.

PTM databases

PhosphoSitei P54922.

Polymorphism databases

DMDMi 1703392.

2D gel databases

OGPi P54922.

Proteomic databases

MaxQBi P54922.
PaxDbi P54922.
PRIDEi P54922.

Protocols and materials databases

DNASUi 141.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000357003 ; ENSP00000349496 ; ENSG00000144843 .
ENST00000465513 ; ENSP00000417430 ; ENSG00000144843 .
ENST00000478399 ; ENSP00000420200 ; ENSG00000144843 .
ENST00000478927 ; ENSP00000417528 ; ENSG00000144843 .
GeneIDi 141.
KEGGi hsa:141.
UCSCi uc003ecs.3. human.

Organism-specific databases

CTDi 141.
GeneCardsi GC03P119298.
HGNCi HGNC:269. ADPRH.
HPAi CAB001701.
MIMi 603081. gene.
neXtProti NX_P54922.
PharmGKBi PA24590.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1397.
HOGENOMi HOG000007974.
HOVERGENi HBG050462.
InParanoidi P54922.
KOi K01245.
OMAi GKGLMEV.
OrthoDBi EOG7SFHWT.
PhylomeDBi P54922.
TreeFami TF329417.

Miscellaneous databases

EvolutionaryTracei P54922.
GenomeRNAii 141.
NextBioi 561.
PROi P54922.
SOURCEi Search...

Gene expression databases

ArrayExpressi P54922.
Bgeei P54922.
CleanExi HS_ADPRH.
Genevestigatori P54922.

Family and domain databases

InterProi IPR012108. ADP-ribosylarg_hydro.
IPR005502. Ribosyl_crysJ1.
[Graphical view ]
Pfami PF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view ]
PIRSFi PIRSF016939. ADP_ribslarg_hdr. 1 hit.
SUPFAMi SSF101478. SSF101478. 1 hit.
ProtoNeti Search...

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: July 9, 2014
This is version 114 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

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