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Q9NX46

- ARHL2_HUMAN

UniProt

Q9NX46 - ARHL2_HUMAN

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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

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

Mg2+1 PublicationNote: 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
Complete GO annotation...

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. mitochondrion Source: UniProtKB-KW
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

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

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

BgeeiQ9NX46.
CleanExiHS_ADPRHL2.
ExpressionAtlasiQ9NX46. baseline and differential.
GenevestigatoriQ9NX46.

Organism-specific databases

HPAiHPA027104.
HPA027141.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi120276. 5 interactions.
IntActiQ9NX46. 3 interactions.
MINTiMINT-1420706.
STRINGi9606.ENSP00000362273.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000015369.
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

        10         20         30         40         50
MAAAAMAAAA GGGAGAARSL SRFRGCLAGA LLGDCVGSFY EAHDTVDLTS
60 70 80 90 100
VLRHVQSLEP DPGTPGSERT EALYYTDDTA MARALVQSLL AKEAFDEVDM
110 120 130 140 150
AHRFAQEYKK DPDRGYGAGV VTVFKKLLNP KCRDVFEPAR AQFNGKGSYG
160 170 180 190 200
NGGAMRVAGI SLAYSSVQDV QKFARLSAQL THASSLGYNG AILQALAVHL
210 220 230 240 250
ALQGESSSEH FLKQLLGHME DLEGDAQSVL DARELGMEER PYSSRLKKIG
260 270 280 290 300
ELLDQASVTR EEVVSELGNG IAAFESVPTA IYCFLRCMEP DPEIPSAFNS
310 320 330 340 350
LQRTLIYSIS LGGDTDTIAT MAGAIAGAYY GMDQVPESWQ QSCEGYEETD
360
ILAQSLHRVF QKS
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 5 interactions.
IntActi Q9NX46. 3 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.
GeneTreei ENSGT00390000015369.
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

Bgeei Q9NX46.
CleanExi HS_ADPRHL2.
ExpressionAtlasi Q9NX46. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 117 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