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UniProtKB/Swiss-Prot entry Q9NX46


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ARHL2_HUMAN
Primary accession number Q9NX46
Secondary accession numbers Q53G94 Q6IAB8 Q9BY47
Integrated into Swiss-Prot on February 6, 2007
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 59)
Name and origin of the protein
Protein name Poly(ADP-ribose) glycohydrolase ARH3
Synonyms EC 3.2.1.143
ADP-ribosylhydrolase 3
[Protein ADP-ribosylarginine] hydrolase-like protein 2
Gene name
Name: ADPRHL2
Synonyms: ARH3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
DOI=10.1110/ps.0200602; PubMed=12070318 [NCBI, ExPASy, EBI, Israel, Japan]
Glowacki G., Braren R., Firner K., Nissen M., Kuehl M., Reche P., Bazan J.F., Cetkovic-Cvrlje M., Leiter E., Haag F., Koch-Nolte F.;
"The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse.";
Protein Sci. 11:1657-1670(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver cancer;
Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.;
"A novel gene expressed in human liver cancer tissue.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-209.
TISSUE=Thyroid;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ENZYME REGULATION, COFACTOR, AND MUTAGENESIS OF 77-ASP--ASP-78; 238-GLU--GLU-239 AND 261-GLU--GLU-262.
DOI=10.1074/jbc.M510290200; PubMed=16278211 [NCBI, ExPASy, EBI, Israel, Japan]
Oka S., Kato J., Moss J.;
"Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase.";
J. Biol. Chem. 281:705-713(2006).
[9]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 19-363, AND MUTAGENESIS OF GLU-41; ASP-77; SER-148; TYR-149; ASN-151; HIS-182; ASP-314 AND THR-317.
DOI=10.1073/pnas.0606762103; PubMed=17015823 [NCBI, ExPASy, EBI, Israel, Japan]
Mueller-Dieckmann C., Kernstock S., Lisurek M., von Kries J.P., Haag F., Weiss M.S., Koch-Nolte F.;
"The structure of human ADP-ribosylhydrolase 3 (ARH3) provides insights into the reversibility of protein ADP-ribosylation.";
Proc. Natl. Acad. Sci. U.S.A. 103:15026-15031(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ313333; CAC85940.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ427295; CAD20316.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF212236; AAK14922.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK000453; BAA91174.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR457237; CAG33518.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK223037; BAD96757.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL138787; CAC21453.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014169; AAH14169.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_060295.1; -.
UniGene Hs.18021
3D structure databases
PDB
2FOZ; X-ray; 1.60 A; A=19-363.[ExPASy / RCSB / EBI]
2FP0; X-ray; 2.05 A; A/B=19-363.[ExPASy / RCSB / EBI]
2G4K; X-ray; 1.82 A; A=18-363.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2FOZ; -.
2FP0; -.
2G4K; -.
ModBase Q9NX46.
Protein-protein interaction databases
IntAct Q9NX46; -.
PTM databases
PhosphoSite Q9NX46; -.
Organism-specific databases
HGNC HGNC:21304; ADPRHL2.
GenAtlas ADPRHL2.
MIM 610624; gene. [NCBI / EBI]
PharmGKB PA134903576; -.
GeneCards Q9NX46.
Gene expression databases
CleanEx HS_ADPRHL2; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004649; Molecular function: poly(ADP-ribose) glycohydrolase activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR005502; Ribosyl_crysJ1.
Graphical view of domain structure.
Pfam PF03747; ADP_ribosyl_GH; 1.
Pfam graphical view of domain structure.
ProtoNet Q9NX46.
Proteomic databases
PeptideAtlas Q9NX46; -.
Genome annotation databases
Ensembl ENSG00000116863; Homo sapiens. [Contig view]
GeneID 54936; -.
KEGG hsa:54936; -.
Phylogenomic databases
HOVERGEN Q9NX46; -.
Other
NextBio 58054; -.
SOURCE ADPRHL2; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleus; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   363  363     Poly(ADP-ribose) glycohydrolase ARH3. PRO_0000277613
COMPBIAS   2    10  9     Poly-Ala. 
METAL   41    41        Magnesium 2. 
METAL   76    76        Magnesium 1. 
METAL   77    77        Magnesium 1. 
METAL   78    78        Magnesium 1. 
METAL   314   314        Magnesium 2. 
METAL   316   316        Magnesium 1. 
METAL   316   316        Magnesium 2. 
METAL   317   317        Magnesium 2. 
VARIANT   209   209  1     E -> K (in dbSNP:rs2236387 [NCBI]). VAR_030579 [3D]
MUTAGEN   41    41        E->A,Q: Significant loss of activity. 
MUTAGEN   77    78        DD->NN: Complete loss of activity. 
MUTAGEN   77    77        D->N: Complete loss of activity. 
MUTAGEN   148   148        S->A: Complete loss of activity. 
MUTAGEN   149   149        Y->A: Significant loss of activity. 
MUTAGEN   151   151        N->A: Partial loss of activity. 
MUTAGEN   182   182        H->Q: Complete loss of activity. 
MUTAGEN   238   239        EE->QQ: Slight reduction in activity. 
MUTAGEN   261   262        EE->QQ: Slight reduction in activity. 
MUTAGEN   314   314        D->E: Complete loss of activity. 
MUTAGEN   314   314        D->N: Significant loss of activity. 
MUTAGEN   317   317        T->A: Complete loss of activity. 
MUTAGEN   317   317        T->S: Partial loss of activity. 
CONFLICT   109   109        K -> E (in Ref. 4; CAG33518). 
HELIX   19    37  19      
HELIX   38    40  3      
HELIX   48    56  9      
HELIX   77    92  16      
HELIX   97   110  14      
HELIX   118   127  10      
HELIX   137   141  5      
TURN   142   146  5      
HELIX   152   155  4      
HELIX   158   163  6      
HELIX   167   179  13      
HELIX   185   201  17      
HELIX   208   222  15      
HELIX   226   234  9      
HELIX   241   254  14      
STRAND   255   257  3      
HELIX   260   267  8      
STRAND   270   272  3      
HELIX   273   275  3      
HELIX   277   286  10      
HELIX   300   310  11      
HELIX   315   330  16      
HELIX   332   334  3      
HELIX   337   341  5      
HELIX   346   360  15      
Sequence information
Length: 363 AA [This is the length of the unprocessed precursor] Molecular weight: 38947 Da [This is the MW of the unprocessed precursor] CRC64: 5FD99F59F27CD29F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAAAMAAAA GGGAGAARSL SRFRGCLAGA LLGDCVGSFY EAHDTVDLTS VLRHVQSLEP 

        70         80         90        100        110        120 
DPGTPGSERT EALYYTDDTA MARALVQSLL AKEAFDEVDM AHRFAQEYKK DPDRGYGAGV 

       130        140        150        160        170        180 
VTVFKKLLNP KCRDVFEPAR AQFNGKGSYG NGGAMRVAGI SLAYSSVQDV QKFARLSAQL 

       190        200        210        220        230        240 
THASSLGYNG AILQALAVHL ALQGESSSEH FLKQLLGHME DLEGDAQSVL DARELGMEER 

       250        260        270        280        290        300 
PYSSRLKKIG ELLDQASVTR EEVVSELGNG IAAFESVPTA IYCFLRCMEP DPEIPSAFNS 

       310        320        330        340        350        360 
LQRTLIYSIS LGGDTDTIAT MAGAIAGAYY GMDQVPESWQ QSCEGYEETD ILAQSLHRVF 


QKS 

Q9NX46 in FASTA format

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