Reviewed, UniProtKB/Swiss-Prot P54922 (ADPRH_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	357 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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-ribose + protein-L-arginine. N(omega)-(ADP-D-ribosyl)-L-arginine + H2O = ADP-ribose + L-arginine.
Sequence similarities	Belongs to the ADP-ribosylglycohydrolase family.

Ontologies

Keywords
Ligand	Magnesium
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid de-ADP-ribosylation Inferred from electronic annotation. Source: InterPro
Molecular function	ADP-ribosylarginine hydrolase activity Ref.1 Inferred from mutant phenotype. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 357	357	[Protein ADP-ribosylarginine] hydrolase		PRO_0000157283

Sequences

	Sequence		Length	Mass (Da)
	P54922-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 4E23B12FAE84F12B	FASTA	357	39,507
	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

References

	« Hide 'large scale' referencesShow '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: 8349667] [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: 14702039] [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. , 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L13291 mRNA. Translation: AAA35555.1. AK313369 mRNA. Translation: BAG36168.1. CH471052 Genomic DNA. Translation: EAW79562.1. BC063883 mRNA. Translation: AAH63883.1. BC074769 mRNA. Translation: AAH74769.1.
IPI	IPI00009258.
PIR	B47411.
RefSeq	NP_001116.1.
UniGene	Hs.99884
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P54922.
PTM databases
PhosphoSite	P54922.
2-D gel databases
OGP	P54922.
Proteomic databases
PRIDE	P54922.
Genome annotation databases
Ensembl	ENST00000357003; ENSP00000349496; ENSG00000144843; Homo sapiens. [Genome view] ENST00000451955; ENSP00000413806; ENSG00000144843; Homo sapiens. [Genome view]
GeneID	141.
KEGG	hsa:141.
UCSC	uc003ecs.1. human.
Organism-specific databases
CTD	141.
GeneCards	GC03P120781.
H-InvDB	HIX0030805.
HGNC	HGNC:269. ADPRH.
HPA	CAB001701.
MIM	603081. gene.
PharmGKB	PA24590.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P54922.
HOVERGEN	P54922.
OMA	IPFNSHE.
Enzyme and pathway databases
BRENDA	3.2.2.19. 247.
Gene expression databases
ArrayExpress	P54922.
Bgee	P54922.
CleanEx	HS_ADPRH.
Genevestigator	P54922.
GermOnline	ENSG00000144843. Homo sapiens.
Family and domain databases
InterPro	IPR012108. ADP-ribosylarg_hydro. IPR005502. Ribosyl_crysJ1. [Graphical view]
PANTHER	PTHR22957:SF7. ADP-ribosylarg_hydro. 1 hit.
Pfam	PF03747. ADP_ribosyl_GH. 1 hit. [Graphical view]
PIRSF	PIRSF016939. ADP_ribslarg_hdr. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	561.
SOURCE	Search...

Entry information

Entry name

ADPRH_HUMAN

Accession

Primary (citable) accession number: P54922
Secondary accession number(s): B2R8H1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 3, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.