P54922 (ADPRH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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)

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.
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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein de-ADP-ribosylation Inferred from electronic annotation. Source: InterPro
Molecular function	ADP-ribosylarginine hydrolase activity Inferred from mutant phenotype Ref.1. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: InterPro
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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

357

Helix Strand Turn

Details...

Helix

2 – 12

11

Helix

32 – 39

8

Helix

55 – 69

15

Helix

76 – 90

15

Helix

91 – 93

3

Helix

103 – 109

7

Helix

132 – 134

3

Helix

145 – 147

3

Helix

148 – 157

10

Helix

173 – 183

11

Helix

188 – 190

3

Turn

196 – 198

3

Helix

199 – 208

10

Helix

213 – 219

7

Helix

221 – 233

13

Helix

252 – 261

10

Helix

273 – 284

12

Helix

289 – 296

8

Helix

303 – 309

7

Helix

325 – 327

3

Turn

328 – 330

3

Helix

334 – 346

13

Sequences

	Sequence		Length	Mass (Da)
	P54922 [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

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.

IPI

IPI00009258.

PIR

B47411.

RefSeq

NP_001116.1. NM_001125.2.

UniGene

Hs.99884.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3HFW	X-ray	1.92	A	1-357	[»]

ProteinModelPortal

P54922.

SMR

P54922. Positions 1-357.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-7288433.

STRING

P54922.

PTM databases

PhosphoSite

P54922.

Polymorphism databases

DMDM

1703392.

2D gel databases

OGP

P54922.

Proteomic databases

PRIDE

P54922.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000357003; ENSP00000349496; ENSG00000144843.
ENST00000465513; ENSP00000417430; ENSG00000144843.
ENST00000478399; ENSP00000420200; ENSG00000144843.
ENST00000478927; ENSP00000417528; ENSG00000144843.

GeneID

141.

KEGG

hsa:141.

UCSC

uc003ecs.1. human.

Organism-specific databases

CTD

141.

GeneCards

GC03P119298.

H-InvDB

HIX0030805.

HGNC

HGNC:269. ADPRH.

HPA

CAB001701.

MIM

603081. gene.

neXtProt

NX_P54922.

PharmGKB

PA24590.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14273.

GeneTree

ENSGT00530000063627.

HOGENOM

HBG715225.

HOVERGEN

HBG050462.

InParanoid

P54922.

OMA

HWSYFQD.

OrthoDB

EOG4QJRNH.

PhylomeDB

P54922.

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]

KO

K01245.

Pfam

PF03747. ADP_ribosyl_GH. 1 hit.
[Graphical view]

PIRSF

PIRSF016939. ADP_ribslarg_hdr. 1 hit.

SUPFAM

SSF101478. Ribosyl_crysJ1. 1 hit.

ProtoNet

Search...

Other

NextBio

561.

SOURCE

Search...

Entry information

Entry name

ADPRH_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

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.