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P54922 (ADPRH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
[Protein ADP-ribosylarginine] hydrolase

Short name=ADP-ribosylarginine hydrolase
EC=3.2.2.19
Alternative name(s):
ADP-ribose-L-arginine cleaving enzyme
Gene names
Name:ADPRH
Synonyms:ARH1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length357 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reverse reaction of mono-ADP-ribosylation.

Catalytic activity

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.

Sequence similarities

Belongs to the ADP-ribosylglycohydrolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 357357[Protein ADP-ribosylarginine] hydrolase
PRO_0000157283

Secondary structure

.................................................... 357
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54922 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 4E23B12FAE84F12B

FASTA35739,507
        10         20         30         40         50         60 
MEKYVAAMVL SAAGDALGYY NGKWEFLQDG EKIHRQLAQL GGLDALDVGR WRVSDDTVMH 

        70         80         90        100        110        120 
LATAEALVEA GKAPKLTQLY YLLAKHYQDC MEDMDGRAPG GASVHNAMQL KPGKPNGWRI 

       130        140        150        160        170        180 
PFNSHEGGCG AAMRAMCIGL RFPHHSQLDT LIQVSIESGR MTHHHPTGYL GALASALFTA 

       190        200        210        220        230        240 
YAVNSRPPLQ WGKGLMELLP EAKKYIVQSG YFVEENLQHW SYFQTKWENY LKLRGILDGE 

       250        260        270        280        290        300 
SAPTFPESFG VKERDQFYTS LSYSGWGGSS GHDAPMIAYD AVLAAGDSWK ELAHRAFFHG 

       310        320        330        340        350 
GDSDSTAAIA GCWWGVMYGF KGVSPSNYEK LEYRNRLEET ARALYSLGSK EDTVISL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2990.1.
PIRB47411.
RefSeqNP_001116.1. NM_001125.3.
UniGeneHs.99884.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HFWX-ray1.92A1-357[»]
ProteinModelPortalP54922.
SMRP54922. Positions 1-357.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106651. 3 interactions.
IntActP54922. 3 interactions.
MINTMINT-7288433.
STRING9606.ENSP00000349496.

PTM databases

PhosphoSiteP54922.

Polymorphism databases

DMDM1703392.

2D gel databases

OGPP54922.

Proteomic databases

MaxQBP54922.
PaxDbP54922.
PRIDEP54922.

Protocols and materials databases

DNASU141.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357003; ENSP00000349496; ENSG00000144843.
ENST00000465513; ENSP00000417430; ENSG00000144843.
ENST00000478399; ENSP00000420200; ENSG00000144843.
ENST00000478927; ENSP00000417528; ENSG00000144843.
GeneID141.
KEGGhsa:141.
UCSCuc003ecs.3. human.

Organism-specific databases

CTD141.
GeneCardsGC03P119298.
HGNCHGNC:269. ADPRH.
HPACAB001701.
MIM603081. gene.
neXtProtNX_P54922.
PharmGKBPA24590.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1397.
HOGENOMHOG000007974.
HOVERGENHBG050462.
InParanoidP54922.
KOK01245.
OMAGKGLMEV.
OrthoDBEOG7SFHWT.
PhylomeDBP54922.
TreeFamTF329417.

Gene expression databases

ArrayExpressP54922.
BgeeP54922.
CleanExHS_ADPRH.
GenevestigatorP54922.

Family and domain databases

InterProIPR012108. ADP-ribosylarg_hydro.
IPR005502. Ribosyl_crysJ1.
[Graphical view]
PfamPF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view]
PIRSFPIRSF016939. ADP_ribslarg_hdr. 1 hit.
SUPFAMSSF101478. SSF101478. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP54922.
GenomeRNAi141.
NextBio561.
PROP54922.
SOURCESearch...

Entry information

Entry nameADPRH_HUMAN
AccessionPrimary (citable) accession number: P54922
Secondary accession number(s): B2R8H1, D3DN83
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM