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P54922

- ADPRH_HUMAN

UniProt

P54922 - ADPRH_HUMAN

Protein

[Protein ADP-ribosylarginine] hydrolase

Gene

ADPRH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the reverse reaction of mono-ADP-ribosylation.

    Catalytic activityi

    Protein-N(omega)-(ADP-D-ribosyl)-L-arginine + H2O = ADP-D-ribose + protein-L-arginine.
    N(omega)-(ADP-D-ribosyl)-L-arginine + H2O = ADP-D-ribose + L-arginine.

    GO - Molecular functioni

    1. ADP-ribosylarginine hydrolase activity Source: UniProtKB
    2. magnesium ion binding Source: InterPro

    GO - Biological processi

    1. cellular protein modification process Source: UniProtKB
    2. protein de-ADP-ribosylation Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    [Protein ADP-ribosylarginine] hydrolase (EC:3.2.2.19)
    Short name:
    ADP-ribosylarginine hydrolase
    Alternative name(s):
    ADP-ribose-L-arginine cleaving enzyme
    Gene namesi
    Name:ADPRH
    Synonyms:ARH1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:269. ADPRH.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24590.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 357357[Protein ADP-ribosylarginine] hydrolasePRO_0000157283Add
    BLAST

    Proteomic databases

    MaxQBiP54922.
    PaxDbiP54922.
    PRIDEiP54922.

    2D gel databases

    OGPiP54922.

    PTM databases

    PhosphoSiteiP54922.

    Expressioni

    Gene expression databases

    ArrayExpressiP54922.
    BgeeiP54922.
    CleanExiHS_ADPRH.
    GenevestigatoriP54922.

    Organism-specific databases

    HPAiCAB001701.

    Interactioni

    Protein-protein interaction databases

    BioGridi106651. 3 interactions.
    IntActiP54922. 3 interactions.
    MINTiMINT-7288433.
    STRINGi9606.ENSP00000349496.

    Structurei

    Secondary structure

    1
    357
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 1918
    Turni20 – 267
    Helixi30 – 3910
    Helixi43 – 453
    Helixi48 – 503
    Helixi55 – 7016
    Helixi76 – 9015
    Helixi91 – 933
    Helixi101 – 1099
    Turni115 – 1184
    Turni129 – 1313
    Helixi132 – 1343
    Helixi137 – 1415
    Helixi145 – 1473
    Helixi148 – 16013
    Helixi166 – 18318
    Helixi188 – 1903
    Helixi191 – 20919
    Helixi213 – 2197
    Helixi221 – 23414
    Helixi251 – 26111
    Beta strandi262 – 2654
    Helixi273 – 28513
    Helixi289 – 2968
    Beta strandi298 – 3025
    Helixi303 – 31816
    Turni319 – 3224
    Helixi325 – 3273
    Turni328 – 3303
    Helixi334 – 34815

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HFWX-ray1.92A1-357[»]
    ProteinModelPortaliP54922.
    SMRiP54922. Positions 1-357.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54922.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ADP-ribosylglycohydrolase family.Curated

    Phylogenomic databases

    eggNOGiCOG1397.
    HOGENOMiHOG000007974.
    HOVERGENiHBG050462.
    InParanoidiP54922.
    KOiK01245.
    OMAiGKGLMEV.
    OrthoDBiEOG7SFHWT.
    PhylomeDBiP54922.
    TreeFamiTF329417.

    Family and domain databases

    InterProiIPR012108. ADP-ribosylarg_hydro.
    IPR005502. Ribosyl_crysJ1.
    [Graphical view]
    PfamiPF03747. ADP_ribosyl_GH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016939. ADP_ribslarg_hdr. 1 hit.
    SUPFAMiSSF101478. SSF101478. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P54922-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKYVAAMVL SAAGDALGYY NGKWEFLQDG EKIHRQLAQL GGLDALDVGR    50
    WRVSDDTVMH LATAEALVEA GKAPKLTQLY YLLAKHYQDC MEDMDGRAPG 100
    GASVHNAMQL KPGKPNGWRI PFNSHEGGCG AAMRAMCIGL RFPHHSQLDT 150
    LIQVSIESGR MTHHHPTGYL GALASALFTA YAVNSRPPLQ WGKGLMELLP 200
    EAKKYIVQSG YFVEENLQHW SYFQTKWENY LKLRGILDGE SAPTFPESFG 250
    VKERDQFYTS LSYSGWGGSS GHDAPMIAYD AVLAAGDSWK ELAHRAFFHG 300
    GDSDSTAAIA GCWWGVMYGF KGVSPSNYEK LEYRNRLEET ARALYSLGSK 350
    EDTVISL 357
    Length:357
    Mass (Da):39,507
    Last modified:October 1, 1996 - v1
    Checksum:i4E23B12FAE84F12B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS2990.1.
    PIRiB47411.
    RefSeqiNP_001116.1. NM_001125.3.
    UniGeneiHs.99884.

    Genome annotation databases

    EnsembliENST00000357003; ENSP00000349496; ENSG00000144843.
    ENST00000465513; ENSP00000417430; ENSG00000144843.
    ENST00000478399; ENSP00000420200; ENSG00000144843.
    ENST00000478927; ENSP00000417528; ENSG00000144843.
    GeneIDi141.
    KEGGihsa:141.
    UCSCiuc003ecs.3. human.

    Polymorphism databases

    DMDMi1703392.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS2990.1.
    PIRi B47411.
    RefSeqi NP_001116.1. NM_001125.3.
    UniGenei Hs.99884.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HFW X-ray 1.92 A 1-357 [» ]
    ProteinModelPortali P54922.
    SMRi P54922. Positions 1-357.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106651. 3 interactions.
    IntActi P54922. 3 interactions.
    MINTi MINT-7288433.
    STRINGi 9606.ENSP00000349496.

    PTM databases

    PhosphoSitei P54922.

    Polymorphism databases

    DMDMi 1703392.

    2D gel databases

    OGPi P54922.

    Proteomic databases

    MaxQBi P54922.
    PaxDbi P54922.
    PRIDEi P54922.

    Protocols and materials databases

    DNASUi 141.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357003 ; ENSP00000349496 ; ENSG00000144843 .
    ENST00000465513 ; ENSP00000417430 ; ENSG00000144843 .
    ENST00000478399 ; ENSP00000420200 ; ENSG00000144843 .
    ENST00000478927 ; ENSP00000417528 ; ENSG00000144843 .
    GeneIDi 141.
    KEGGi hsa:141.
    UCSCi uc003ecs.3. human.

    Organism-specific databases

    CTDi 141.
    GeneCardsi GC03P119298.
    HGNCi HGNC:269. ADPRH.
    HPAi CAB001701.
    MIMi 603081. gene.
    neXtProti NX_P54922.
    PharmGKBi PA24590.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1397.
    HOGENOMi HOG000007974.
    HOVERGENi HBG050462.
    InParanoidi P54922.
    KOi K01245.
    OMAi GKGLMEV.
    OrthoDBi EOG7SFHWT.
    PhylomeDBi P54922.
    TreeFami TF329417.

    Miscellaneous databases

    EvolutionaryTracei P54922.
    GenomeRNAii 141.
    NextBioi 561.
    PROi P54922.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54922.
    Bgeei P54922.
    CleanExi HS_ADPRH.
    Genevestigatori P54922.

    Family and domain databases

    InterProi IPR012108. ADP-ribosylarg_hydro.
    IPR005502. Ribosyl_crysJ1.
    [Graphical view ]
    Pfami PF03747. ADP_ribosyl_GH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016939. ADP_ribslarg_hdr. 1 hit.
    SUPFAMi SSF101478. SSF101478. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Thymus.
    3. 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.

    Entry informationi

    Entry nameiADPRH_HUMAN
    AccessioniPrimary (citable) accession number: P54922
    Secondary accession number(s): B2R8H1, D3DN83
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    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. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3