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Q9NX46

- ARHL2_HUMAN

UniProt

Q9NX46 - ARHL2_HUMAN

Protein

Poly(ADP-ribose) glycohydrolase ARH3

Gene

ADPRHL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. Poly(ADP-ribose) metabolism may be required for maintenance of the normal function of neuronal cells. Generates ADP-ribose from poly-(ADP-ribose), but does not hydrolyze ADP-ribose-arginine, -cysteine, -diphthamide, or -asparagine bonds. Due to catalytic inactivity of PARG mitochondrial isoforms, ARH3 is the only PAR hydrolyzing enzyme in mitochondria.1 Publication

    Catalytic activityi

    Hydrolyzes poly(ADP-D-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-D-ribose.1 Publication

    Cofactori

    Binds 2 magnesium ions per subunit.1 Publication

    Enzyme regulationi

    Activity is enhanced by magnesium.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi41 – 411Magnesium 2
    Metal bindingi76 – 761Magnesium 1
    Metal bindingi77 – 771Magnesium 1
    Metal bindingi78 – 781Magnesium 1
    Binding sitei254 – 2541SubstrateBy similarity
    Metal bindingi314 – 3141Magnesium 2
    Metal bindingi316 – 3161Magnesium 1
    Metal bindingi316 – 3161Magnesium 2
    Metal bindingi317 – 3171Magnesium 2

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. poly(ADP-ribose) glycohydrolase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.2.1.143. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Poly(ADP-ribose) glycohydrolase ARH3 (EC:3.2.1.143)
    Alternative name(s):
    ADP-ribosylhydrolase 3
    [Protein ADP-ribosylarginine] hydrolase-like protein 2
    Gene namesi
    Name:ADPRHL2
    Synonyms:ARH3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:21304. ADPRHL2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi41 – 411E → A or Q: Significant loss of activity. 2 Publications
    Mutagenesisi77 – 782DD → NN: Complete loss of activity. 2 Publications
    Mutagenesisi77 – 771D → N: Complete loss of activity. 2 Publications
    Mutagenesisi148 – 1481S → A: Complete loss of activity. 2 Publications
    Mutagenesisi149 – 1491Y → A: Significant loss of activity. 2 Publications
    Mutagenesisi151 – 1511N → A: Partial loss of activity. 2 Publications
    Mutagenesisi182 – 1821H → Q: Complete loss of activity. 2 Publications
    Mutagenesisi238 – 2392EE → QQ: Slight reduction in activity. 1 Publication
    Mutagenesisi261 – 2622EE → QQ: Slight reduction in activity. 1 Publication
    Mutagenesisi314 – 3141D → E: Complete loss of activity. 2 Publications
    Mutagenesisi314 – 3141D → N: Significant loss of activity. 2 Publications
    Mutagenesisi317 – 3171T → A: Complete loss of activity. 2 Publications
    Mutagenesisi317 – 3171T → S: Partial loss of activity. 2 Publications

    Organism-specific databases

    PharmGKBiPA134903576.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2727MitochondrionSequence AnalysisAdd
    BLAST
    Chaini28 – 363336Poly(ADP-ribose) glycohydrolase ARH3PRO_0000277613Add
    BLAST

    Proteomic databases

    MaxQBiQ9NX46.
    PaxDbiQ9NX46.
    PeptideAtlasiQ9NX46.
    PRIDEiQ9NX46.

    PTM databases

    PhosphoSiteiQ9NX46.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ9NX46.
    BgeeiQ9NX46.
    CleanExiHS_ADPRHL2.
    GenevestigatoriQ9NX46.

    Organism-specific databases

    HPAiHPA027104.
    HPA027141.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi120276. 3 interactions.
    IntActiQ9NX46. 2 interactions.
    MINTiMINT-1420706.
    STRINGi9606.ENSP00000362273.

    Structurei

    Secondary structure

    1
    363
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 3719
    Helixi38 – 403
    Helixi48 – 569
    Helixi77 – 9216
    Helixi97 – 11014
    Turni112 – 1154
    Helixi118 – 12710
    Helixi137 – 1415
    Turni142 – 1465
    Helixi152 – 1554
    Helixi158 – 1636
    Helixi167 – 17913
    Helixi185 – 20117
    Helixi208 – 22215
    Helixi226 – 2349
    Helixi241 – 25414
    Beta strandi255 – 2573
    Helixi260 – 2678
    Beta strandi270 – 2723
    Helixi273 – 2753
    Helixi277 – 28610
    Helixi300 – 31011
    Helixi315 – 33016
    Helixi332 – 3343
    Helixi337 – 3415
    Helixi346 – 36015

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FOZX-ray1.60A19-363[»]
    2FP0X-ray2.05A/B19-363[»]
    2G4KX-ray1.82A18-363[»]
    ProteinModelPortaliQ9NX46.
    SMRiQ9NX46. Positions 19-363.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NX46.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 109Poly-Ala

    Sequence similaritiesi

    Belongs to the ADP-ribosylglycohydrolase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1397.
    HOGENOMiHOG000225333.
    HOVERGENiHBG080863.
    InParanoidiQ9NX46.
    KOiK11687.
    OMAiYKKDPDR.
    OrthoDBiEOG7D2FFB.
    PhylomeDBiQ9NX46.
    TreeFamiTF324754.

    Family and domain databases

    InterProiIPR005502. Ribosyl_crysJ1.
    [Graphical view]
    PfamiPF03747. ADP_ribosyl_GH. 1 hit.
    [Graphical view]
    SUPFAMiSSF101478. SSF101478. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9NX46-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAAMAAAA GGGAGAARSL SRFRGCLAGA LLGDCVGSFY EAHDTVDLTS    50
    VLRHVQSLEP DPGTPGSERT EALYYTDDTA MARALVQSLL AKEAFDEVDM 100
    AHRFAQEYKK DPDRGYGAGV VTVFKKLLNP KCRDVFEPAR AQFNGKGSYG 150
    NGGAMRVAGI SLAYSSVQDV QKFARLSAQL THASSLGYNG AILQALAVHL 200
    ALQGESSSEH FLKQLLGHME DLEGDAQSVL DARELGMEER PYSSRLKKIG 250
    ELLDQASVTR EEVVSELGNG IAAFESVPTA IYCFLRCMEP DPEIPSAFNS 300
    LQRTLIYSIS LGGDTDTIAT MAGAIAGAYY GMDQVPESWQ QSCEGYEETD 350
    ILAQSLHRVF QKS 363
    Length:363
    Mass (Da):38,947
    Last modified:October 1, 2000 - v1
    Checksum:i5FD99F59F27CD29F
    GO

    Sequence cautioni

    The sequence AAK14922.1 differs from that shown. Reason: Frameshift at several positions.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti109 – 1091K → E in CAG33518. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti209 – 2091E → K.1 Publication
    Corresponds to variant rs2236387 [ dbSNP | Ensembl ].
    VAR_030579

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ313333 Genomic DNA. Translation: CAC85940.1.
    AJ427295 mRNA. Translation: CAD20316.1.
    AF212236 mRNA. Translation: AAK14922.1. Frameshift.
    AK000453 mRNA. Translation: BAA91174.1.
    CR457237 mRNA. Translation: CAG33518.1.
    AK223037 mRNA. Translation: BAD96757.1.
    AL138787 Genomic DNA. Translation: CAC21453.1.
    BC014169 mRNA. Translation: AAH14169.1.
    CCDSiCCDS402.1.
    RefSeqiNP_060295.1. NM_017825.2.
    UniGeneiHs.18021.

    Genome annotation databases

    EnsembliENST00000373178; ENSP00000362273; ENSG00000116863.
    GeneIDi54936.
    KEGGihsa:54936.
    UCSCiuc001bzt.3. human.

    Polymorphism databases

    DMDMi74753038.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ313333 Genomic DNA. Translation: CAC85940.1 .
    AJ427295 mRNA. Translation: CAD20316.1 .
    AF212236 mRNA. Translation: AAK14922.1 . Frameshift.
    AK000453 mRNA. Translation: BAA91174.1 .
    CR457237 mRNA. Translation: CAG33518.1 .
    AK223037 mRNA. Translation: BAD96757.1 .
    AL138787 Genomic DNA. Translation: CAC21453.1 .
    BC014169 mRNA. Translation: AAH14169.1 .
    CCDSi CCDS402.1.
    RefSeqi NP_060295.1. NM_017825.2.
    UniGenei Hs.18021.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FOZ X-ray 1.60 A 19-363 [» ]
    2FP0 X-ray 2.05 A/B 19-363 [» ]
    2G4K X-ray 1.82 A 18-363 [» ]
    ProteinModelPortali Q9NX46.
    SMRi Q9NX46. Positions 19-363.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120276. 3 interactions.
    IntActi Q9NX46. 2 interactions.
    MINTi MINT-1420706.
    STRINGi 9606.ENSP00000362273.

    PTM databases

    PhosphoSitei Q9NX46.

    Polymorphism databases

    DMDMi 74753038.

    Proteomic databases

    MaxQBi Q9NX46.
    PaxDbi Q9NX46.
    PeptideAtlasi Q9NX46.
    PRIDEi Q9NX46.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373178 ; ENSP00000362273 ; ENSG00000116863 .
    GeneIDi 54936.
    KEGGi hsa:54936.
    UCSCi uc001bzt.3. human.

    Organism-specific databases

    CTDi 54936.
    GeneCardsi GC01P036554.
    HGNCi HGNC:21304. ADPRHL2.
    HPAi HPA027104.
    HPA027141.
    MIMi 610624. gene.
    neXtProti NX_Q9NX46.
    PharmGKBi PA134903576.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1397.
    HOGENOMi HOG000225333.
    HOVERGENi HBG080863.
    InParanoidi Q9NX46.
    KOi K11687.
    OMAi YKKDPDR.
    OrthoDBi EOG7D2FFB.
    PhylomeDBi Q9NX46.
    TreeFami TF324754.

    Enzyme and pathway databases

    BRENDAi 3.2.1.143. 2681.

    Miscellaneous databases

    EvolutionaryTracei Q9NX46.
    GeneWikii ADPRHL2.
    GenomeRNAii 54936.
    NextBioi 58054.
    PROi Q9NX46.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NX46.
    Bgeei Q9NX46.
    CleanExi HS_ADPRHL2.
    Genevestigatori Q9NX46.

    Family and domain databases

    InterProi IPR005502. Ribosyl_crysJ1.
    [Graphical view ]
    Pfami PF03747. ADP_ribosyl_GH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101478. SSF101478. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse."
      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.
      Protein Sci. 11:1657-1670(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "A novel gene expressed in human liver cancer tissue."
      Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Liver cancer.
    3. "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].
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. 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
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LYS-209.
      Tissue: Thyroid.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      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.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Skin.
    8. "Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase."
      Oka S., Kato J., Moss J.
      J. Biol. Chem. 281:705-713(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ENZYME REGULATION, COFACTOR, MUTAGENESIS OF 77-ASP--ASP-78; 238-GLU--GLU-239 AND 261-GLU--GLU-262.
    9. "Functional localization of two poly(ADP-ribose)-degrading enzymes to the mitochondrial matrix."
      Niere M., Kernstock S., Koch-Nolte F., Ziegler M.
      Mol. Cell. Biol. 28:814-824(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose)."
      Niere M., Mashimo M., Agledal L., Dolle C., Kasamatsu A., Kato J., Moss J., Ziegler M.
      J. Biol. Chem. 287:16088-16102(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "The structure of human ADP-ribosylhydrolase 3 (ARH3) provides insights into the reversibility of protein ADP-ribosylation."
      Mueller-Dieckmann C., Kernstock S., Lisurek M., von Kries J.P., Haag F., Weiss M.S., Koch-Nolte F.
      Proc. Natl. Acad. Sci. U.S.A. 103:15026-15031(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 19-363, MUTAGENESIS OF GLU-41; ASP-77; SER-148; TYR-149; ASN-151; HIS-182; ASP-314 AND THR-317.
    15. "The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase."
      Slade D., Dunstan M.S., Barkauskaite E., Weston R., Lafite P., Dixon N., Ahel M., Leys D., Ahel I.
      Nature 477:616-620(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 19-363, SUBSTRATE-BINDING SITE, METAL-BINDING SITES.

    Entry informationi

    Entry nameiARHL2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NX46
    Secondary accession number(s): Q53G94, Q6IAB8, Q9BY47
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 6, 2007
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 115 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. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3