Full text data of NUDT16
NUDT16
[Confidence: low (only semi-automatic identification from reviews)]
U8 snoRNA-decapping enzyme; 3.6.1.62 (IDP phosphatase; IDPase; 3.6.1.-; Inosine diphosphate phosphatase; Nucleoside diphosphate-linked moiety X motif 16; Nudix motif 16; U8 snoRNA-binding protein H29K; m7GpppN-mRNA hydrolase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
U8 snoRNA-decapping enzyme; 3.6.1.62 (IDP phosphatase; IDPase; 3.6.1.-; Inosine diphosphate phosphatase; Nucleoside diphosphate-linked moiety X motif 16; Nudix motif 16; U8 snoRNA-binding protein H29K; m7GpppN-mRNA hydrolase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96DE0
ID NUD16_HUMAN Reviewed; 195 AA.
AC Q96DE0; B4E3B4; E9PED4; F5GYJ1; Q96N82;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2005, sequence version 2.
DT 22-JAN-2014, entry version 98.
DE RecName: Full=U8 snoRNA-decapping enzyme;
DE EC=3.6.1.62;
DE AltName: Full=IDP phosphatase;
DE Short=IDPase;
DE EC=3.6.1.-;
DE AltName: Full=Inosine diphosphate phosphatase;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 16;
DE Short=Nudix motif 16;
DE AltName: Full=U8 snoRNA-binding protein H29K;
DE AltName: Full=m7GpppN-mRNA hydrolase;
GN Name=NUDT16;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 21-195 (ISOFORM 1).
RC TISSUE=Kidney, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=16344560; DOI=10.1101/gr.4039406;
RA Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T.,
RA Yamashita R., Yamamoto J., Sekine M., Tsuritani K., Wakaguri H.,
RA Ishii S., Sugiyama T., Saito K., Isono Y., Irie R., Kushida N.,
RA Yoneyama T., Otsuka R., Kanda K., Yokoi T., Kondo H., Wagatsuma M.,
RA Murakawa K., Ishida S., Ishibashi T., Takahashi-Fujii A., Tanase T.,
RA Nagai K., Kikuchi H., Nakai K., Isogai T., Sugano S.;
RT "Diversification of transcriptional modulation: large-scale
RT identification and characterization of putative alternative promoters
RT of human genes.";
RL Genome Res. 16:55-65(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION AS A DECAPPING ENZYME, AND CATALYTIC ACTIVITY.
RX PubMed=15053875; DOI=10.1016/S1097-2765(04)00127-3;
RA Ghosh T., Peterson B., Tomasevic N., Peculis B.A.;
RT "Xenopus U8 snoRNA binding protein is a conserved nuclear decapping
RT enzyme.";
RL Mol. Cell 13:817-828(2004).
RN [6]
RP FUNCTION AS A DECAPPING ENZYME, SUBUNIT, CATALYTIC ACTIVITY, AND
RP COFACTOR.
RX PubMed=17567574; DOI=10.1074/jbc.M704179200;
RA Peculis B.A., Reynolds K., Cleland M.;
RT "Metal determines efficiency and substrate specificity of the nuclear
RT NUDIX decapping proteins X29 and H29K (Nudt16).";
RL J. Biol. Chem. 282:24792-24805(2007).
RN [7]
RP FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, SUBUNIT,
RP RNA-BINDING, GENE EVOLUTION, AND GENE FAMILY ORGANIZATION.
RX PubMed=18820299; DOI=10.1093/nar/gkn605;
RA Taylor M.J., Peculis B.A.;
RT "Evolutionary conservation supports ancient origin for Nudt16, a
RT nuclear-localized, RNA-binding, RNA-decapping enzyme.";
RL Nucleic Acids Res. 36:6021-6034(2008).
RN [8]
RP FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21070968; DOI=10.1016/j.molcel.2010.10.010;
RA Song M.G., Li Y., Kiledjian M.;
RT "Multiple mRNA decapping enzymes in mammalian cells.";
RL Mol. Cell 40:423-432(2010).
RN [9]
RP FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS
RP SPECTROMETRY.
RX PubMed=20385596; DOI=10.1093/nar/gkq249;
RA Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.;
RT "NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces
RT accumulation of single-strand breaks in nuclear DNA and growth
RT arrest.";
RL Nucleic Acids Res. 38:4834-4843(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, COFACTOR, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21337011; DOI=10.1007/s13238-011-1009-2;
RA Lu G., Zhang J., Li Y., Li Z., Zhang N., Xu X., Wang T., Guan Z.,
RA Gao G.F., Yan J.;
RT "hNUDT16: a universal decapping enzyme for small nucleolar RNA and
RT cytoplasmic mRNA.";
RL Protein Cell 2:64-73(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=18607096; DOI=10.1107/S1744309108016928;
RA Zhang J., Gao F., Zhang Q., Chen Q., Qi J., Yan J.;
RT "Crystallization and crystallographic analysis of human NUDT16.";
RL Acta Crystallogr. F 64:639-640(2008).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RG Structural genomics consortium (SGC);
RT "Crystal structure of human nudix motif 16 (NUDT16).";
RL Submitted (FEB-2009) to the PDB data bank.
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH IMP AND
RP MAGNESIUM IONS.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human NUDT16 in complex with IMP and
RT magnesium.";
RL Submitted (NOV-2010) to the PDB data bank.
CC -!- FUNCTION: RNA-binding and decapping enzyme that catalyzes the
CC cleavage of the cap structure of snoRNAs and mRNAs in a metal-
CC dependent manner. Part of the U8 snoRNP complex that is required
CC for the accumulation of mature 5.8S and 28S rRNA. Has
CC diphosphatase activity and removes m7G and/or m227G caps from U8
CC snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the
CC cleavage of the cap structure on mRNAs. Does not hydrolyze cap
CC analog structures like 7-methylguanosine nucleoside triphosphate
CC (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with
CC less efficiencies. Has broad substrate specificity with manganese
CC or cobalt as cofactor and can act on various RNA species. Binds to
CC the U8 snoRNA; metal is not required for RNA-binding. May play a
CC role in the regulation of snoRNAs and mRNAs degradation. Acts also
CC as a phosphatase; hydrolyzes the non-canonical purine nucleotides
CC inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as
CC well as guanosine diphosphate (GDP), deoxyguanosine diphosphate
CC (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and
CC deoxyinosine triphosphate (ITP) to their respective monophosphate
CC derivatives and does not distinguish between the deoxy- and ribose
CC forms. The order of activity with different substrates is IDP >
CC dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP
CC and XTP. Participates in the hydrolysis of dIDP/IDP and probably
CC excludes non-canonical purines from RNA and DNA precursor pools,
CC thus preventing their incorporation into RNA and DNA and avoiding
CC chromosomal lesions.
CC -!- CATALYTIC ACTIVITY: 5'-(N(7)-methylguanosine 5'-triphospho)-(mRNA)
CC + H(2)O = N(7)-methylguanosine 5'-diphosphate + 5'-phospho-(mRNA).
CC -!- CATALYTIC ACTIVITY: IDP + H(2)O = IMP + phosphate.
CC -!- COFACTOR: Magnesium, manganese or cobalt. Binds 3 or 4 divalent
CC metal cations. Acts specifically on U8 snoRNA with magnesium as
CC cofactor. Has broad substrate specificity with bound manganese or
CC cobalt (in vitro).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.062 uM for IDP (at 37 degrees Celsius);
CC KM=0.088 uM for dIDP (at 37 degrees Celsius);
CC KM=0.330 uM for GDP (at 37 degrees Celsius);
CC KM=0.319 mM for dGDP (at 37 degrees Celsius);
CC KM=15.7 mM for XDP (at 37 degrees Celsius);
CC KM=22.1 mM for ITP (at 37 degrees Celsius);
CC KM=24.1 mM for dITP (at 37 degrees Celsius);
CC Note=kcat is 0.931 sec(-1) with IDP. kcat is 0.966 sec(-1) with
CC dIDP. kcat is 0.518 sec(-1) with GDP. kcat is 0.492 sec(-1) with
CC dGDP. kcat is 2.6 sec(-1) with XDP. kcat is 3.06 sec(-1) with
CC ITP. kcat is 3.2 sec(-1) with dITP. The catalytic efficiency for
CC IDP is at least 1.3-fold higher than for dIDP, 9.6-fold higher
CC than for GDP and dGDP, 100-fold higher than for XDP, ITP and
CC dITP;
CC pH dependence:
CC Gradually increased from pH 6.5 to 8.5 in its IDP hydrolyzing
CC activity;
CC Temperature dependence:
CC Exhibited a temperature-dependent increase in its IDP
CC hydrolyzing activity up to 60 degrees Celsius;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleoplasm (By
CC similarity). Nucleus, nucleolus. Cytoplasm. Note=Localized
CC predominantly in the cytoplasm. Localized in nucleolus, and in a
CC minor proportion in distinct foci in the nucleoplasm (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96DE0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96DE0-2; Sequence=VSP_045450, VSP_045451;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q96DE0-3; Sequence=VSP_045449, VSP_045452;
CC Note=No experimental confirmation available. Ref.2 (BP199028)
CC sequence is in conflict in position: 128:A->Missing;
CC Name=4;
CC IsoId=Q96DE0-4; Sequence=VSP_045451;
CC -!- TISSUE SPECIFICITY: Expressed strongly in lung, kidney, adrenal
CC gland, testis, heart and brain.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NUDT16
CC subfamily.
CC -!- SIMILARITY: Contains 1 nudix hydrolase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71024.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AK055827; BAB71024.1; ALT_INIT; mRNA.
DR EMBL; AK304650; BAG65426.1; -; mRNA.
DR EMBL; BP199028; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC010210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009546; AAH09546.1; -; mRNA.
DR EMBL; BC031215; AAH31215.2; -; mRNA.
DR RefSeq; NP_001165376.1; NM_001171905.1.
DR RefSeq; NP_001165377.1; NM_001171906.1.
DR RefSeq; NP_689608.2; NM_152395.2.
DR UniGene; Hs.282050; -.
DR PDB; 2XSQ; X-ray; 1.72 A; A=1-195.
DR PDB; 3COU; X-ray; 1.80 A; A=1-195.
DR PDB; 3MGM; X-ray; 1.80 A; A/B=1-195.
DR PDBsum; 2XSQ; -.
DR PDBsum; 3COU; -.
DR PDBsum; 3MGM; -.
DR ProteinModelPortal; Q96DE0; -.
DR SMR; Q96DE0; 18-181.
DR MINT; MINT-5003418; -.
DR STRING; 9606.ENSP00000352911; -.
DR PhosphoSite; Q96DE0; -.
DR DMDM; 68565926; -.
DR PaxDb; Q96DE0; -.
DR PRIDE; Q96DE0; -.
DR Ensembl; ENST00000359850; ENSP00000352911; ENSG00000198585.
DR Ensembl; ENST00000502852; ENSP00000422375; ENSG00000198585.
DR Ensembl; ENST00000521288; ENSP00000429274; ENSG00000198585.
DR Ensembl; ENST00000537561; ENSP00000440230; ENSG00000198585.
DR GeneID; 131870; -.
DR KEGG; hsa:131870; -.
DR UCSC; uc021xeb.1; human.
DR CTD; 131870; -.
DR GeneCards; GC03P131100; -.
DR H-InvDB; HIX0003684; -.
DR HGNC; HGNC:26442; NUDT16.
DR neXtProt; NX_Q96DE0; -.
DR PharmGKB; PA134955224; -.
DR eggNOG; NOG38933; -.
DR HOGENOM; HOG000007083; -.
DR HOVERGEN; HBG067297; -.
DR InParanoid; Q96DE0; -.
DR KO; K16855; -.
DR OMA; FYAKCLT; -.
DR OrthoDB; EOG7J9VR4; -.
DR BioCyc; MetaCyc:MONOMER-17869; -.
DR Reactome; REACT_111217; Metabolism.
DR EvolutionaryTrace; Q96DE0; -.
DR GenomeRNAi; 131870; -.
DR NextBio; 82972; -.
DR PRO; PR:Q96DE0; -.
DR ArrayExpress; Q96DE0; -.
DR Bgee; Q96DE0; -.
DR CleanEx; HS_NUDT16; -.
DR Genevestigator; Q96DE0; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
DR GO; GO:0097383; F:dIDP diphosphatase activity; EXP:Reactome.
DR GO; GO:0035870; F:dITP diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0090450; F:inosine-diphosphatase activity; EXP:Reactome.
DR GO; GO:1901641; F:ITP binding; IDA:UniProtKB.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0008235; F:metalloexopeptidase activity; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030515; F:snoRNA binding; IDA:UniProtKB.
DR GO; GO:1901640; F:XTP binding; IDA:UniProtKB.
DR GO; GO:0006382; P:adenosine to inosine editing; IMP:UniProtKB.
DR GO; GO:0035863; P:dITP catabolic process; ISS:UniProtKB.
DR GO; GO:0046709; P:IDP catabolic process; IDA:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
DR GO; GO:2000233; P:negative regulation of rRNA processing; ISS:UniProtKB.
DR GO; GO:0034656; P:nucleobase-containing small molecule catabolic process; TAS:Reactome.
DR GO; GO:0090068; P:positive regulation of cell cycle process; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IMP:UniProtKB.
DR GO; GO:0016077; P:snoRNA catabolic process; IDA:UniProtKB.
DR GO; GO:1901639; P:XDP catabolic process; IDA:UniProtKB.
DR Gene3D; 3.90.79.10; -; 1.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR015797; NUDIX_hydrolase_dom-like.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide metabolism;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1 195 U8 snoRNA-decapping enzyme.
FT /FTId=PRO_0000057117.
FT DOMAIN 18 173 Nudix hydrolase.
FT MOTIF 61 82 Nudix box.
FT METAL 59 59 Magnesium or manganese 1; via carbonyl
FT oxygen (By similarity).
FT METAL 76 76 Magnesium or manganese 2 (By similarity).
FT METAL 76 76 Magnesium or manganese 3 (By similarity).
FT METAL 80 80 Magnesium or manganese 1 (By similarity).
FT METAL 80 80 Magnesium or manganese 3 (By similarity).
FT METAL 136 136 Magnesium or manganese 3 (By similarity).
FT METAL 136 136 Magnesium or manganese 4 (By similarity).
FT BINDING 24 24 Substrate (By similarity).
FT BINDING 50 50 Substrate (By similarity).
FT BINDING 170 170 Substrate (By similarity).
FT VAR_SEQ 1 46 Missing (in isoform 3).
FT /FTId=VSP_045449.
FT VAR_SEQ 1 33 Missing (in isoform 2).
FT /FTId=VSP_045450.
FT VAR_SEQ 138 195 LGLVRVPLYTLRDGVGGLPTFLENSFIGSAREQLLEALQDL
FT GLLQSGSISGLKIPAHH -> GPAWDSVPFPISSSPKAFSP
FT PRKHPWRKVFAPLTLPSPQLSWWSWDRDHLYSELVLPTWAF
FT CKGLSHPLPGEILSRTHSSMSLCCSLLTV (in isoform
FT 2 and isoform 4).
FT /FTId=VSP_045451.
FT VAR_SEQ 174 195 ALQDLGLLQSGSISGLKIPAHH -> AALHGPMKTEMRTLV
FT LGREGRTWECFLIGSER (in isoform 3).
FT /FTId=VSP_045452.
FT CONFLICT 22 22 A -> V (in Ref. 4; AAH31215).
FT STRAND 5 7
FT HELIX 9 13
FT STRAND 20 35
FT TURN 36 38
FT STRAND 39 50
FT STRAND 58 61
FT TURN 64 66
FT HELIX 69 81
FT HELIX 83 87
FT HELIX 92 94
FT STRAND 95 100
FT STRAND 102 114
FT HELIX 117 126
FT HELIX 127 129
FT TURN 134 136
FT STRAND 137 142
FT HELIX 155 158
FT HELIX 167 177
FT TURN 178 181
SQ SEQUENCE 195 AA; 21273 MW; 4AC7EA679D1D7468 CRC64;
MAGARRLELG EALALGSGWR HACHALLYAP DPGMLFGRIP LRYAILMQMR FDGRLGFPGG
FVDTQDRSLE DGLNRELREE LGEAAAAFRV ERTDYRSSHV GSGPRVVAHF YAKRLTLEEL
LAVEAGATRA KDHGLEVLGL VRVPLYTLRD GVGGLPTFLE NSFIGSAREQ LLEALQDLGL
LQSGSISGLK IPAHH
//
ID NUD16_HUMAN Reviewed; 195 AA.
AC Q96DE0; B4E3B4; E9PED4; F5GYJ1; Q96N82;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2005, sequence version 2.
DT 22-JAN-2014, entry version 98.
DE RecName: Full=U8 snoRNA-decapping enzyme;
DE EC=3.6.1.62;
DE AltName: Full=IDP phosphatase;
DE Short=IDPase;
DE EC=3.6.1.-;
DE AltName: Full=Inosine diphosphate phosphatase;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 16;
DE Short=Nudix motif 16;
DE AltName: Full=U8 snoRNA-binding protein H29K;
DE AltName: Full=m7GpppN-mRNA hydrolase;
GN Name=NUDT16;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 21-195 (ISOFORM 1).
RC TISSUE=Kidney, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=16344560; DOI=10.1101/gr.4039406;
RA Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T.,
RA Yamashita R., Yamamoto J., Sekine M., Tsuritani K., Wakaguri H.,
RA Ishii S., Sugiyama T., Saito K., Isono Y., Irie R., Kushida N.,
RA Yoneyama T., Otsuka R., Kanda K., Yokoi T., Kondo H., Wagatsuma M.,
RA Murakawa K., Ishida S., Ishibashi T., Takahashi-Fujii A., Tanase T.,
RA Nagai K., Kikuchi H., Nakai K., Isogai T., Sugano S.;
RT "Diversification of transcriptional modulation: large-scale
RT identification and characterization of putative alternative promoters
RT of human genes.";
RL Genome Res. 16:55-65(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION AS A DECAPPING ENZYME, AND CATALYTIC ACTIVITY.
RX PubMed=15053875; DOI=10.1016/S1097-2765(04)00127-3;
RA Ghosh T., Peterson B., Tomasevic N., Peculis B.A.;
RT "Xenopus U8 snoRNA binding protein is a conserved nuclear decapping
RT enzyme.";
RL Mol. Cell 13:817-828(2004).
RN [6]
RP FUNCTION AS A DECAPPING ENZYME, SUBUNIT, CATALYTIC ACTIVITY, AND
RP COFACTOR.
RX PubMed=17567574; DOI=10.1074/jbc.M704179200;
RA Peculis B.A., Reynolds K., Cleland M.;
RT "Metal determines efficiency and substrate specificity of the nuclear
RT NUDIX decapping proteins X29 and H29K (Nudt16).";
RL J. Biol. Chem. 282:24792-24805(2007).
RN [7]
RP FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, SUBUNIT,
RP RNA-BINDING, GENE EVOLUTION, AND GENE FAMILY ORGANIZATION.
RX PubMed=18820299; DOI=10.1093/nar/gkn605;
RA Taylor M.J., Peculis B.A.;
RT "Evolutionary conservation supports ancient origin for Nudt16, a
RT nuclear-localized, RNA-binding, RNA-decapping enzyme.";
RL Nucleic Acids Res. 36:6021-6034(2008).
RN [8]
RP FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21070968; DOI=10.1016/j.molcel.2010.10.010;
RA Song M.G., Li Y., Kiledjian M.;
RT "Multiple mRNA decapping enzymes in mammalian cells.";
RL Mol. Cell 40:423-432(2010).
RN [9]
RP FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS
RP SPECTROMETRY.
RX PubMed=20385596; DOI=10.1093/nar/gkq249;
RA Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.;
RT "NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces
RT accumulation of single-strand breaks in nuclear DNA and growth
RT arrest.";
RL Nucleic Acids Res. 38:4834-4843(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, COFACTOR, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21337011; DOI=10.1007/s13238-011-1009-2;
RA Lu G., Zhang J., Li Y., Li Z., Zhang N., Xu X., Wang T., Guan Z.,
RA Gao G.F., Yan J.;
RT "hNUDT16: a universal decapping enzyme for small nucleolar RNA and
RT cytoplasmic mRNA.";
RL Protein Cell 2:64-73(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=18607096; DOI=10.1107/S1744309108016928;
RA Zhang J., Gao F., Zhang Q., Chen Q., Qi J., Yan J.;
RT "Crystallization and crystallographic analysis of human NUDT16.";
RL Acta Crystallogr. F 64:639-640(2008).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RG Structural genomics consortium (SGC);
RT "Crystal structure of human nudix motif 16 (NUDT16).";
RL Submitted (FEB-2009) to the PDB data bank.
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH IMP AND
RP MAGNESIUM IONS.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human NUDT16 in complex with IMP and
RT magnesium.";
RL Submitted (NOV-2010) to the PDB data bank.
CC -!- FUNCTION: RNA-binding and decapping enzyme that catalyzes the
CC cleavage of the cap structure of snoRNAs and mRNAs in a metal-
CC dependent manner. Part of the U8 snoRNP complex that is required
CC for the accumulation of mature 5.8S and 28S rRNA. Has
CC diphosphatase activity and removes m7G and/or m227G caps from U8
CC snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the
CC cleavage of the cap structure on mRNAs. Does not hydrolyze cap
CC analog structures like 7-methylguanosine nucleoside triphosphate
CC (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with
CC less efficiencies. Has broad substrate specificity with manganese
CC or cobalt as cofactor and can act on various RNA species. Binds to
CC the U8 snoRNA; metal is not required for RNA-binding. May play a
CC role in the regulation of snoRNAs and mRNAs degradation. Acts also
CC as a phosphatase; hydrolyzes the non-canonical purine nucleotides
CC inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as
CC well as guanosine diphosphate (GDP), deoxyguanosine diphosphate
CC (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and
CC deoxyinosine triphosphate (ITP) to their respective monophosphate
CC derivatives and does not distinguish between the deoxy- and ribose
CC forms. The order of activity with different substrates is IDP >
CC dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP
CC and XTP. Participates in the hydrolysis of dIDP/IDP and probably
CC excludes non-canonical purines from RNA and DNA precursor pools,
CC thus preventing their incorporation into RNA and DNA and avoiding
CC chromosomal lesions.
CC -!- CATALYTIC ACTIVITY: 5'-(N(7)-methylguanosine 5'-triphospho)-(mRNA)
CC + H(2)O = N(7)-methylguanosine 5'-diphosphate + 5'-phospho-(mRNA).
CC -!- CATALYTIC ACTIVITY: IDP + H(2)O = IMP + phosphate.
CC -!- COFACTOR: Magnesium, manganese or cobalt. Binds 3 or 4 divalent
CC metal cations. Acts specifically on U8 snoRNA with magnesium as
CC cofactor. Has broad substrate specificity with bound manganese or
CC cobalt (in vitro).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.062 uM for IDP (at 37 degrees Celsius);
CC KM=0.088 uM for dIDP (at 37 degrees Celsius);
CC KM=0.330 uM for GDP (at 37 degrees Celsius);
CC KM=0.319 mM for dGDP (at 37 degrees Celsius);
CC KM=15.7 mM for XDP (at 37 degrees Celsius);
CC KM=22.1 mM for ITP (at 37 degrees Celsius);
CC KM=24.1 mM for dITP (at 37 degrees Celsius);
CC Note=kcat is 0.931 sec(-1) with IDP. kcat is 0.966 sec(-1) with
CC dIDP. kcat is 0.518 sec(-1) with GDP. kcat is 0.492 sec(-1) with
CC dGDP. kcat is 2.6 sec(-1) with XDP. kcat is 3.06 sec(-1) with
CC ITP. kcat is 3.2 sec(-1) with dITP. The catalytic efficiency for
CC IDP is at least 1.3-fold higher than for dIDP, 9.6-fold higher
CC than for GDP and dGDP, 100-fold higher than for XDP, ITP and
CC dITP;
CC pH dependence:
CC Gradually increased from pH 6.5 to 8.5 in its IDP hydrolyzing
CC activity;
CC Temperature dependence:
CC Exhibited a temperature-dependent increase in its IDP
CC hydrolyzing activity up to 60 degrees Celsius;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleoplasm (By
CC similarity). Nucleus, nucleolus. Cytoplasm. Note=Localized
CC predominantly in the cytoplasm. Localized in nucleolus, and in a
CC minor proportion in distinct foci in the nucleoplasm (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96DE0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96DE0-2; Sequence=VSP_045450, VSP_045451;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q96DE0-3; Sequence=VSP_045449, VSP_045452;
CC Note=No experimental confirmation available. Ref.2 (BP199028)
CC sequence is in conflict in position: 128:A->Missing;
CC Name=4;
CC IsoId=Q96DE0-4; Sequence=VSP_045451;
CC -!- TISSUE SPECIFICITY: Expressed strongly in lung, kidney, adrenal
CC gland, testis, heart and brain.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NUDT16
CC subfamily.
CC -!- SIMILARITY: Contains 1 nudix hydrolase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71024.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AK055827; BAB71024.1; ALT_INIT; mRNA.
DR EMBL; AK304650; BAG65426.1; -; mRNA.
DR EMBL; BP199028; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC010210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009546; AAH09546.1; -; mRNA.
DR EMBL; BC031215; AAH31215.2; -; mRNA.
DR RefSeq; NP_001165376.1; NM_001171905.1.
DR RefSeq; NP_001165377.1; NM_001171906.1.
DR RefSeq; NP_689608.2; NM_152395.2.
DR UniGene; Hs.282050; -.
DR PDB; 2XSQ; X-ray; 1.72 A; A=1-195.
DR PDB; 3COU; X-ray; 1.80 A; A=1-195.
DR PDB; 3MGM; X-ray; 1.80 A; A/B=1-195.
DR PDBsum; 2XSQ; -.
DR PDBsum; 3COU; -.
DR PDBsum; 3MGM; -.
DR ProteinModelPortal; Q96DE0; -.
DR SMR; Q96DE0; 18-181.
DR MINT; MINT-5003418; -.
DR STRING; 9606.ENSP00000352911; -.
DR PhosphoSite; Q96DE0; -.
DR DMDM; 68565926; -.
DR PaxDb; Q96DE0; -.
DR PRIDE; Q96DE0; -.
DR Ensembl; ENST00000359850; ENSP00000352911; ENSG00000198585.
DR Ensembl; ENST00000502852; ENSP00000422375; ENSG00000198585.
DR Ensembl; ENST00000521288; ENSP00000429274; ENSG00000198585.
DR Ensembl; ENST00000537561; ENSP00000440230; ENSG00000198585.
DR GeneID; 131870; -.
DR KEGG; hsa:131870; -.
DR UCSC; uc021xeb.1; human.
DR CTD; 131870; -.
DR GeneCards; GC03P131100; -.
DR H-InvDB; HIX0003684; -.
DR HGNC; HGNC:26442; NUDT16.
DR neXtProt; NX_Q96DE0; -.
DR PharmGKB; PA134955224; -.
DR eggNOG; NOG38933; -.
DR HOGENOM; HOG000007083; -.
DR HOVERGEN; HBG067297; -.
DR InParanoid; Q96DE0; -.
DR KO; K16855; -.
DR OMA; FYAKCLT; -.
DR OrthoDB; EOG7J9VR4; -.
DR BioCyc; MetaCyc:MONOMER-17869; -.
DR Reactome; REACT_111217; Metabolism.
DR EvolutionaryTrace; Q96DE0; -.
DR GenomeRNAi; 131870; -.
DR NextBio; 82972; -.
DR PRO; PR:Q96DE0; -.
DR ArrayExpress; Q96DE0; -.
DR Bgee; Q96DE0; -.
DR CleanEx; HS_NUDT16; -.
DR Genevestigator; Q96DE0; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
DR GO; GO:0097383; F:dIDP diphosphatase activity; EXP:Reactome.
DR GO; GO:0035870; F:dITP diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0090450; F:inosine-diphosphatase activity; EXP:Reactome.
DR GO; GO:1901641; F:ITP binding; IDA:UniProtKB.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0008235; F:metalloexopeptidase activity; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030515; F:snoRNA binding; IDA:UniProtKB.
DR GO; GO:1901640; F:XTP binding; IDA:UniProtKB.
DR GO; GO:0006382; P:adenosine to inosine editing; IMP:UniProtKB.
DR GO; GO:0035863; P:dITP catabolic process; ISS:UniProtKB.
DR GO; GO:0046709; P:IDP catabolic process; IDA:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
DR GO; GO:2000233; P:negative regulation of rRNA processing; ISS:UniProtKB.
DR GO; GO:0034656; P:nucleobase-containing small molecule catabolic process; TAS:Reactome.
DR GO; GO:0090068; P:positive regulation of cell cycle process; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IMP:UniProtKB.
DR GO; GO:0016077; P:snoRNA catabolic process; IDA:UniProtKB.
DR GO; GO:1901639; P:XDP catabolic process; IDA:UniProtKB.
DR Gene3D; 3.90.79.10; -; 1.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR015797; NUDIX_hydrolase_dom-like.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide metabolism;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1 195 U8 snoRNA-decapping enzyme.
FT /FTId=PRO_0000057117.
FT DOMAIN 18 173 Nudix hydrolase.
FT MOTIF 61 82 Nudix box.
FT METAL 59 59 Magnesium or manganese 1; via carbonyl
FT oxygen (By similarity).
FT METAL 76 76 Magnesium or manganese 2 (By similarity).
FT METAL 76 76 Magnesium or manganese 3 (By similarity).
FT METAL 80 80 Magnesium or manganese 1 (By similarity).
FT METAL 80 80 Magnesium or manganese 3 (By similarity).
FT METAL 136 136 Magnesium or manganese 3 (By similarity).
FT METAL 136 136 Magnesium or manganese 4 (By similarity).
FT BINDING 24 24 Substrate (By similarity).
FT BINDING 50 50 Substrate (By similarity).
FT BINDING 170 170 Substrate (By similarity).
FT VAR_SEQ 1 46 Missing (in isoform 3).
FT /FTId=VSP_045449.
FT VAR_SEQ 1 33 Missing (in isoform 2).
FT /FTId=VSP_045450.
FT VAR_SEQ 138 195 LGLVRVPLYTLRDGVGGLPTFLENSFIGSAREQLLEALQDL
FT GLLQSGSISGLKIPAHH -> GPAWDSVPFPISSSPKAFSP
FT PRKHPWRKVFAPLTLPSPQLSWWSWDRDHLYSELVLPTWAF
FT CKGLSHPLPGEILSRTHSSMSLCCSLLTV (in isoform
FT 2 and isoform 4).
FT /FTId=VSP_045451.
FT VAR_SEQ 174 195 ALQDLGLLQSGSISGLKIPAHH -> AALHGPMKTEMRTLV
FT LGREGRTWECFLIGSER (in isoform 3).
FT /FTId=VSP_045452.
FT CONFLICT 22 22 A -> V (in Ref. 4; AAH31215).
FT STRAND 5 7
FT HELIX 9 13
FT STRAND 20 35
FT TURN 36 38
FT STRAND 39 50
FT STRAND 58 61
FT TURN 64 66
FT HELIX 69 81
FT HELIX 83 87
FT HELIX 92 94
FT STRAND 95 100
FT STRAND 102 114
FT HELIX 117 126
FT HELIX 127 129
FT TURN 134 136
FT STRAND 137 142
FT HELIX 155 158
FT HELIX 167 177
FT TURN 178 181
SQ SEQUENCE 195 AA; 21273 MW; 4AC7EA679D1D7468 CRC64;
MAGARRLELG EALALGSGWR HACHALLYAP DPGMLFGRIP LRYAILMQMR FDGRLGFPGG
FVDTQDRSLE DGLNRELREE LGEAAAAFRV ERTDYRSSHV GSGPRVVAHF YAKRLTLEEL
LAVEAGATRA KDHGLEVLGL VRVPLYTLRD GVGGLPTFLE NSFIGSAREQ LLEALQDLGL
LQSGSISGLK IPAHH
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