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Protein

U8 snoRNA-decapping enzyme

Gene

NUDT16

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation. Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms (PubMed:20385596, PubMed:26121039). The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP (PubMed:20385596). Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions (PubMed:20385596).7 Publications

Catalytic activityi

5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] + H2O = N(7)-methylguanosine 5'-diphosphate + 5'-phospho-[mRNA].5 Publications
IDP + H2O = IMP + phosphate.2 Publications
dIDP + H2O = dIMP + phosphate.2 Publications

Cofactori

Mg2+3 Publications, Mn2+2 Publications, Co2+2 PublicationsNote: Binds 3 or 4 divalent metal cations. Acts specifically on U8 snoRNA with magnesium as cofactor. Has broad substrate specificity with bound manganese or cobalt (in vitro).2 Publications

Enzyme regulationi

The phosphatase activity is inhibited by the product IMP.1 Publication

Kineticsi

kcat is 0.931 sec(-1) with IDP. kcat is 0.966 sec(-1) with dIDP. kcat is 0.518 sec(-1) with GDP. kcat is 0.492 sec(-1) with dGDP. kcat is 2.6 sec(-1) with XDP. kcat is 3.06 sec(-1) with ITP. kcat is 3.2 sec(-1) with dITP. The catalytic efficiency for IDP is at least 1.3-fold higher than for dIDP, 9.6-fold higher than for GDP and dGDP, 100-fold higher than for XDP, ITP and dITP.1 Publication

  1. KM=0.062 µM for IDP (at 37 degrees Celsius)1 Publication
  2. KM=0.088 µM for dIDP (at 37 degrees Celsius)1 Publication
  3. KM=0.330 µM for GDP (at 37 degrees Celsius)1 Publication
  4. KM=0.319 mM for dGDP (at 37 degrees Celsius)1 Publication
  5. KM=15.7 mM for XDP (at 37 degrees Celsius)1 Publication
  6. KM=22.1 mM for ITP (at 37 degrees Celsius)1 Publication
  7. KM=24.1 mM for dITP (at 37 degrees Celsius)1 Publication

    pH dependencei

    Gradually increased from pH 6.5 to 8.5 in its IDP hydrolyzing activity.1 Publication

    Temperature dependencei

    Exhibited a temperature-dependent increase in its IDP hydrolyzing activity up to 60 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei24 – 241Substrate1 Publication
    Binding sitei50 – 501Substrate1 Publication
    Binding sitei57 – 571Substrate; via amide nitrogen1 Publication
    Metal bindingi59 – 591Magnesium or manganese 1; via carbonyl oxygen1 Publication
    Metal bindingi76 – 761Magnesium or manganese 21 Publication
    Metal bindingi76 – 761Magnesium or manganese 3By similarity
    Metal bindingi80 – 801Magnesium or manganese 11 Publication
    Metal bindingi80 – 801Magnesium or manganese 3By similarity
    Metal bindingi136 – 1361Magnesium or manganese 3By similarity
    Metal bindingi136 – 1361Magnesium or manganese 4By similarity
    Binding sitei170 – 1701Substrate1 Publication

    GO - Molecular functioni

    • cobalt ion binding Source: UniProtKB
    • dIDP diphosphatase activity Source: Reactome
    • dITP diphosphatase activity Source: UniProtKB
    • GTP binding Source: UniProtKB
    • identical protein binding Source: IntAct
    • inosine-diphosphatase activity Source: Reactome
    • ITP binding Source: UniProtKB
    • m7G(5')pppN diphosphatase activity Source: UniProtKB
    • magnesium ion binding Source: UniProtKB
    • manganese ion binding Source: UniProtKB
    • metalloexopeptidase activity Source: UniProtKB
    • mRNA binding Source: UniProtKB
    • nucleotide phosphatase activity, acting on free nucleotides Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    • snoRNA binding Source: UniProtKB
    • XTP binding Source: UniProtKB

    GO - Biological processi

    • adenosine to inosine editing Source: UniProtKB
    • dephosphorylation Source: GOC
    • dITP catabolic process Source: UniProtKB
    • IDP catabolic process Source: UniProtKB
    • mRNA catabolic process Source: UniProtKB
    • negative regulation of rRNA processing Source: UniProtKB
    • nucleobase-containing small molecule catabolic process Source: Reactome
    • positive regulation of cell cycle process Source: UniProtKB
    • positive regulation of cell proliferation Source: UniProtKB
    • positive regulation of double-strand break repair Source: UniProtKB
    • proteolysis Source: GOC
    • snoRNA catabolic process Source: UniProtKB
    • XDP catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, Nucleotide-binding, RNA-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17869.
    BRENDAi3.6.1.62. 2681.
    3.6.1.64. 2681.
    ReactomeiR-HSA-2393930. Phosphate bond hydrolysis by NUDT proteins.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    U8 snoRNA-decapping enzyme (EC:3.6.1.625 Publications)
    Alternative name(s):
    IDP phosphatase (EC:3.6.1.642 Publications)
    Short name:
    IDPase
    Inosine diphosphate phosphatase
    Nucleoside diphosphate-linked moiety X motif 16
    Short name:
    Nudix motif 16
    U8 snoRNA-binding protein H29K1 Publication
    m7GpppN-mRNA hydrolase
    Gene namesi
    Name:NUDT16
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:26442. NUDT16.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • nucleolus Source: UniProtKB
    • nucleoplasm Source: Reactome
    • nucleus Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134955224.

    Polymorphism and mutation databases

    BioMutaiNUDT16.
    DMDMi68565926.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 195195U8 snoRNA-decapping enzymePRO_0000057117Add
    BLAST

    Proteomic databases

    EPDiQ96DE0.
    MaxQBiQ96DE0.
    PaxDbiQ96DE0.
    PRIDEiQ96DE0.
    TopDownProteomicsiQ96DE0-1. [Q96DE0-1]

    PTM databases

    iPTMnetiQ96DE0.
    PhosphoSiteiQ96DE0.

    Expressioni

    Tissue specificityi

    Expressed strongly in lung, kidney, adrenal gland, testis, heart and brain.1 Publication

    Gene expression databases

    BgeeiQ96DE0.
    CleanExiHS_NUDT16.
    GenevisibleiQ96DE0. HS.

    Organism-specific databases

    HPAiHPA060452.
    HPA062492.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-5464685,EBI-5464685

    GO - Molecular functioni

    • identical protein binding Source: IntAct
    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    BioGridi126295. 2 interactions.
    IntActiQ96DE0. 1 interaction.
    MINTiMINT-5003418.
    STRINGi9606.ENSP00000422375.

    Structurei

    Secondary structure

    1
    195
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 73Combined sources
    Helixi9 – 135Combined sources
    Beta strandi20 – 3516Combined sources
    Turni36 – 383Combined sources
    Beta strandi39 – 5012Combined sources
    Beta strandi58 – 614Combined sources
    Turni64 – 663Combined sources
    Helixi69 – 8113Combined sources
    Helixi83 – 875Combined sources
    Helixi92 – 943Combined sources
    Beta strandi95 – 1006Combined sources
    Beta strandi102 – 11413Combined sources
    Helixi117 – 12610Combined sources
    Helixi127 – 1293Combined sources
    Turni134 – 1363Combined sources
    Beta strandi137 – 1426Combined sources
    Helixi155 – 1584Combined sources
    Helixi167 – 17711Combined sources
    Turni178 – 1814Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XSQX-ray1.72A1-195[»]
    3COUX-ray1.80A1-195[»]
    3MGMX-ray1.80A/B1-195[»]
    ProteinModelPortaliQ96DE0.
    SMRiQ96DE0. Positions 18-181.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96DE0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 173156Nudix hydrolasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi61 – 8222Nudix boxAdd
    BLAST

    Sequence similaritiesi

    Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiENOG410IYGP. Eukaryota.
    ENOG4111QA1. LUCA.
    GeneTreeiENSGT00390000016224.
    HOGENOMiHOG000007083.
    HOVERGENiHBG067297.
    InParanoidiQ96DE0.
    KOiK16855.
    OMAiFYAKCLT.
    OrthoDBiEOG7J9VR4.
    PhylomeDBiQ96DE0.

    Family and domain databases

    Gene3Di3.90.79.10. 1 hit.
    InterProiIPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view]
    PfamiPF00293. NUDIX. 1 hit.
    [Graphical view]
    SUPFAMiSSF55811. SSF55811. 1 hit.
    PROSITEiPS51462. NUDIX. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q96DE0-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MAGARRLELG EALALGSGWR HACHALLYAP DPGMLFGRIP LRYAILMQMR
    60 70 80 90 100
    FDGRLGFPGG FVDTQDRSLE DGLNRELREE LGEAAAAFRV ERTDYRSSHV
    110 120 130 140 150
    GSGPRVVAHF YAKRLTLEEL LAVEAGATRA KDHGLEVLGL VRVPLYTLRD
    160 170 180 190
    GVGGLPTFLE NSFIGSAREQ LLEALQDLGL LQSGSISGLK IPAHH
    Length:195
    Mass (Da):21,273
    Last modified:July 5, 2005 - v2
    Checksum:i4AC7EA679D1D7468
    GO
    Isoform 2 (identifier: Q96DE0-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: Missing.
         138-195: LGLVRVPLYT...ISGLKIPAHH → GPAWDSVPFP...MSLCCSLLTV

    Note: No experimental confirmation available.
    Show »
    Length:194
    Mass (Da):21,816
    Checksum:iF41E209A5248D017
    GO
    Isoform 3 (identifier: Q96DE0-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-46: Missing.
         174-195: ALQDLGLLQSGSISGLKIPAHH → AALHGPMKTEMRTLVLGREGRTWECFLIGSER

    Note: No experimental confirmation available.Curated
    Show »
    Length:159
    Mass (Da):17,676
    Checksum:iA73EF509993E7BB5
    GO
    Isoform 4 (identifier: Q96DE0-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         138-195: LGLVRVPLYT...ISGLKIPAHH → GPAWDSVPFP...MSLCCSLLTV

    Show »
    Length:227
    Mass (Da):25,259
    Checksum:iFCD1CBE3CCC3F086
    GO

    Sequence cautioni

    The sequence BAB71024.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221A → V in AAH31215 (PubMed:15489334).Curated
    Isoform 3 (identifier: Q96DE0-3)
    Sequence conflicti128 – 1281Missing in BP199028 (PubMed:16344560).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4646Missing in isoform 3. 1 PublicationVSP_045449Add
    BLAST
    Alternative sequencei1 – 3333Missing in isoform 2. 1 PublicationVSP_045450Add
    BLAST
    Alternative sequencei138 – 19558LGLVR…IPAHH → GPAWDSVPFPISSSPKAFSP PRKHPWRKVFAPLTLPSPQL SWWSWDRDHLYSELVLPTWA FCKGLSHPLPGEILSRTHSS MSLCCSLLTV in isoform 2 and isoform 4. 1 PublicationVSP_045451Add
    BLAST
    Alternative sequencei174 – 19522ALQDL…IPAHH → AALHGPMKTEMRTLVLGREG RTWECFLIGSER in isoform 3. 1 PublicationVSP_045452Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK055827 mRNA. Translation: BAB71024.1. Different initiation.
    AK304650 mRNA. Translation: BAG65426.1.
    BP199028 mRNA. No translation available.
    AC010210 Genomic DNA. No translation available.
    BC009546 mRNA. Translation: AAH09546.1.
    BC031215 mRNA. Translation: AAH31215.2.
    CCDSiCCDS3070.2. [Q96DE0-1]
    CCDS54640.1. [Q96DE0-4]
    CCDS54641.1. [Q96DE0-3]
    RefSeqiNP_001165376.1. NM_001171905.1. [Q96DE0-3]
    NP_001165377.1. NM_001171906.1. [Q96DE0-4]
    NP_689608.2. NM_152395.2. [Q96DE0-1]
    UniGeneiHs.282050.

    Genome annotation databases

    EnsembliENST00000502852; ENSP00000422375; ENSG00000198585. [Q96DE0-4]
    ENST00000521288; ENSP00000429274; ENSG00000198585. [Q96DE0-1]
    ENST00000537561; ENSP00000440230; ENSG00000198585. [Q96DE0-3]
    GeneIDi131870.
    KEGGihsa:131870.
    UCSCiuc003eog.3. human. [Q96DE0-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK055827 mRNA. Translation: BAB71024.1. Different initiation.
    AK304650 mRNA. Translation: BAG65426.1.
    BP199028 mRNA. No translation available.
    AC010210 Genomic DNA. No translation available.
    BC009546 mRNA. Translation: AAH09546.1.
    BC031215 mRNA. Translation: AAH31215.2.
    CCDSiCCDS3070.2. [Q96DE0-1]
    CCDS54640.1. [Q96DE0-4]
    CCDS54641.1. [Q96DE0-3]
    RefSeqiNP_001165376.1. NM_001171905.1. [Q96DE0-3]
    NP_001165377.1. NM_001171906.1. [Q96DE0-4]
    NP_689608.2. NM_152395.2. [Q96DE0-1]
    UniGeneiHs.282050.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XSQX-ray1.72A1-195[»]
    3COUX-ray1.80A1-195[»]
    3MGMX-ray1.80A/B1-195[»]
    ProteinModelPortaliQ96DE0.
    SMRiQ96DE0. Positions 18-181.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi126295. 2 interactions.
    IntActiQ96DE0. 1 interaction.
    MINTiMINT-5003418.
    STRINGi9606.ENSP00000422375.

    PTM databases

    iPTMnetiQ96DE0.
    PhosphoSiteiQ96DE0.

    Polymorphism and mutation databases

    BioMutaiNUDT16.
    DMDMi68565926.

    Proteomic databases

    EPDiQ96DE0.
    MaxQBiQ96DE0.
    PaxDbiQ96DE0.
    PRIDEiQ96DE0.
    TopDownProteomicsiQ96DE0-1. [Q96DE0-1]

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000502852; ENSP00000422375; ENSG00000198585. [Q96DE0-4]
    ENST00000521288; ENSP00000429274; ENSG00000198585. [Q96DE0-1]
    ENST00000537561; ENSP00000440230; ENSG00000198585. [Q96DE0-3]
    GeneIDi131870.
    KEGGihsa:131870.
    UCSCiuc003eog.3. human. [Q96DE0-1]

    Organism-specific databases

    CTDi131870.
    GeneCardsiNUDT16.
    H-InvDBHIX0003684.
    HGNCiHGNC:26442. NUDT16.
    HPAiHPA060452.
    HPA062492.
    neXtProtiNX_Q96DE0.
    PharmGKBiPA134955224.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiENOG410IYGP. Eukaryota.
    ENOG4111QA1. LUCA.
    GeneTreeiENSGT00390000016224.
    HOGENOMiHOG000007083.
    HOVERGENiHBG067297.
    InParanoidiQ96DE0.
    KOiK16855.
    OMAiFYAKCLT.
    OrthoDBiEOG7J9VR4.
    PhylomeDBiQ96DE0.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17869.
    BRENDAi3.6.1.62. 2681.
    3.6.1.64. 2681.
    ReactomeiR-HSA-2393930. Phosphate bond hydrolysis by NUDT proteins.

    Miscellaneous databases

    ChiTaRSiNUDT16. human.
    EvolutionaryTraceiQ96DE0.
    GenomeRNAii131870.
    PROiQ96DE0.

    Gene expression databases

    BgeeiQ96DE0.
    CleanExiHS_NUDT16.
    GenevisibleiQ96DE0. HS.

    Family and domain databases

    Gene3Di3.90.79.10. 1 hit.
    InterProiIPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view]
    PfamiPF00293. NUDIX. 1 hit.
    [Graphical view]
    SUPFAMiSSF55811. SSF55811. 1 hit.
    PROSITEiPS51462. NUDIX. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-195 (ISOFORM 1).
      Tissue: Kidney and Uterus.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1).
      Tissue: Brain and Pancreas.
    5. "Xenopus U8 snoRNA binding protein is a conserved nuclear decapping enzyme."
      Ghosh T., Peterson B., Tomasevic N., Peculis B.A.
      Mol. Cell 13:817-828(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY.
    6. "Metal determines efficiency and substrate specificity of the nuclear NUDIX decapping proteins X29 and H29K (Nudt16)."
      Peculis B.A., Reynolds K., Cleland M.
      J. Biol. Chem. 282:24792-24805(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A DECAPPING ENZYME, SUBUNIT, CATALYTIC ACTIVITY, COFACTOR.
    7. "Evolutionary conservation supports ancient origin for Nudt16, a nuclear-localized, RNA-binding, RNA-decapping enzyme."
      Taylor M.J., Peculis B.A.
      Nucleic Acids Res. 36:6021-6034(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, SUBUNIT, RNA-BINDING, GENE EVOLUTION, GENE FAMILY ORGANIZATION.
    8. "Multiple mRNA decapping enzymes in mammalian cells."
      Song M.G., Li Y., Kiledjian M.
      Mol. Cell 40:423-432(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    9. "NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest."
      Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.
      Nucleic Acids Res. 38:4834-4843(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA."
      Lu G., Zhang J., Li Y., Li Z., Zhang N., Xu X., Wang T., Guan Z., Gao G.F., Yan J.
      Protein Cell 2:64-73(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION.
    12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    13. "Crystallization and crystallographic analysis of human NUDT16."
      Zhang J., Gao F., Zhang Q., Chen Q., Qi J., Yan J.
      Acta Crystallogr. F 64:639-640(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    14. "Structural basis for the specificity of human NUDT16 and its regulation by inosine monophosphate."
      Tresaugues L., Lundbaeck T., Welin M., Flodin S., Nyman T., Silvander C., Graeslund S., Nordlund P.
      PLoS ONE 10:E0131507-E0131507(2015) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH IMP AND MAGNESIUM IONS, SUBUNIT, CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION, COFACTOR.

    Entry informationi

    Entry nameiNUD16_HUMAN
    AccessioniPrimary (citable) accession number: Q96DE0
    Secondary accession number(s): B4E3B4
    , E9PED4, F5GYJ1, Q96N82
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: July 5, 2005
    Last modified: June 8, 2016
    This is version 121 of the entry and version 2 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.