Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

U8 snoRNA-decapping enzyme (EC 3.6.1.62) (IDP phosphatase) (IDPase) (EC 3.6.1.64) (Inosine diphosphate phosphatase) (Nucleoside diphosphate-linked moiety X motif 16) (Nudix motif 16) (Nudix hydrolase 16) (U8 snoRNA-binding protein H29K) (m7GpppN-mRNA hydrolase)

 NUD16_HUMAN             Reviewed;         195 AA.
Q96DE0; B4E3B4; E9PED4; F5GYJ1; Q96N82;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 2.
27-SEP-2017, entry version 133.
RecName: Full=U8 snoRNA-decapping enzyme;
EC=3.6.1.62 {ECO:0000269|PubMed:15053875, ECO:0000269|PubMed:17567574, ECO:0000269|PubMed:18820299, ECO:0000269|PubMed:21070968, ECO:0000269|PubMed:21337011};
AltName: Full=IDP phosphatase;
Short=IDPase;
EC=3.6.1.64 {ECO:0000269|PubMed:20385596, ECO:0000269|PubMed:26121039};
AltName: Full=Inosine diphosphate phosphatase;
AltName: Full=Nucleoside diphosphate-linked moiety X motif 16;
Short=Nudix motif 16;
AltName: Full=Nudix hydrolase 16;
AltName: Full=U8 snoRNA-binding protein H29K {ECO:0000303|PubMed:17567574};
AltName: Full=m7GpppN-mRNA hydrolase;
Name=NUDT16;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 21-195 (ISOFORM 1).
TISSUE=Kidney, and Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=16344560; DOI=10.1101/gr.4039406;
Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T.,
Yamashita R., Yamamoto J., Sekine M., Tsuritani K., Wakaguri H.,
Ishii S., Sugiyama T., Saito K., Isono Y., Irie R., Kushida N.,
Yoneyama T., Otsuka R., Kanda K., Yokoi T., Kondo H., Wagatsuma M.,
Murakawa K., Ishida S., Ishibashi T., Takahashi-Fujii A., Tanase T.,
Nagai K., Kikuchi H., Nakai K., Isogai T., Sugano S.;
"Diversification of transcriptional modulation: large-scale
identification and characterization of putative alternative promoters
of human genes.";
Genome Res. 16:55-65(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
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.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION AS A DECAPPING ENZYME, AND CATALYTIC ACTIVITY.
PubMed=15053875; DOI=10.1016/S1097-2765(04)00127-3;
Ghosh T., Peterson B., Tomasevic N., Peculis B.A.;
"Xenopus U8 snoRNA binding protein is a conserved nuclear decapping
enzyme.";
Mol. Cell 13:817-828(2004).
[6]
FUNCTION AS A DECAPPING ENZYME, SUBUNIT, CATALYTIC ACTIVITY, AND
COFACTOR.
PubMed=17567574; DOI=10.1074/jbc.M704179200;
Peculis B.A., Reynolds K., Cleland M.;
"Metal determines efficiency and substrate specificity of the nuclear
NUDIX decapping proteins X29 and H29K (Nudt16).";
J. Biol. Chem. 282:24792-24805(2007).
[7]
FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, SUBUNIT,
RNA-BINDING, GENE EVOLUTION, AND GENE FAMILY ORGANIZATION.
PubMed=18820299; DOI=10.1093/nar/gkn605;
Taylor M.J., Peculis B.A.;
"Evolutionary conservation supports ancient origin for Nudt16, a
nuclear-localized, RNA-binding, RNA-decapping enzyme.";
Nucleic Acids Res. 36:6021-6034(2008).
[8]
FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, AND SUBCELLULAR
LOCATION.
PubMed=21070968; DOI=10.1016/j.molcel.2010.10.010;
Song M.G., Li Y., Kiledjian M.;
"Multiple mRNA decapping enzymes in mammalian cells.";
Mol. Cell 40:423-432(2010).
[9]
FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20385596; DOI=10.1093/nar/gkq249;
Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.;
"NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces
accumulation of single-strand breaks in nuclear DNA and growth
arrest.";
Nucleic Acids Res. 38:4834-4843(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, COFACTOR, AND
SUBCELLULAR LOCATION.
PubMed=21337011; DOI=10.1007/s13238-011-1009-2;
Lu G., Zhang J., Li Y., Li Z., Zhang N., Xu X., Wang T., Guan Z.,
Gao G.F., Yan J.;
"hNUDT16: a universal decapping enzyme for small nucleolar RNA and
cytoplasmic mRNA.";
Protein Cell 2:64-73(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=18607096; DOI=10.1107/S1744309108016928;
Zhang J., Gao F., Zhang Q., Chen Q., Qi J., Yan J.;
"Crystallization and crystallographic analysis of human NUDT16.";
Acta Crystallogr. F 64:639-640(2008).
[14]
X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH IMP AND
MAGNESIUM IONS, SUBUNIT, CATALYTIC ACTIVITY, ENZYME REGULATION,
FUNCTION, AND COFACTOR.
PubMed=26121039; DOI=10.1371/journal.pone.0131507;
Tresaugues L., Lundbaeck T., Welin M., Flodin S., Nyman T.,
Silvander C., Graeslund S., Nordlund P.;
"Structural basis for the specificity of human NUDT16 and its
regulation by inosine monophosphate.";
PLoS ONE 10:E0131507-E0131507(2015).
-!- FUNCTION: 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).
{ECO:0000269|PubMed:15053875, ECO:0000269|PubMed:17567574,
ECO:0000269|PubMed:18820299, ECO:0000269|PubMed:20385596,
ECO:0000269|PubMed:21070968, ECO:0000269|PubMed:21337011,
ECO:0000269|PubMed:26121039}.
-!- CATALYTIC ACTIVITY: 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA]
+ H(2)O = N(7)-methylguanosine 5'-diphosphate + 5'-phospho-[mRNA].
{ECO:0000269|PubMed:15053875, ECO:0000269|PubMed:17567574,
ECO:0000269|PubMed:18820299, ECO:0000269|PubMed:21070968,
ECO:0000269|PubMed:21337011}.
-!- CATALYTIC ACTIVITY: IDP + H(2)O = IMP + phosphate.
{ECO:0000269|PubMed:20385596, ECO:0000269|PubMed:26121039}.
-!- CATALYTIC ACTIVITY: dIDP + H(2)O = dIMP + phosphate.
{ECO:0000269|PubMed:20385596, ECO:0000269|PubMed:26121039}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:17567574,
ECO:0000269|PubMed:21337011, ECO:0000269|PubMed:26121039};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:17567574,
ECO:0000269|PubMed:21337011};
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000269|PubMed:17567574,
ECO:0000269|PubMed:21337011};
Note=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).
{ECO:0000269|PubMed:17567574, ECO:0000269|PubMed:21337011};
-!- ENZYME REGULATION: The phosphatase activity is inhibited by the
product IMP. {ECO:0000269|PubMed:26121039}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.062 uM for IDP (at 37 degrees Celsius)
{ECO:0000269|PubMed:20385596};
KM=0.088 uM for dIDP (at 37 degrees Celsius)
{ECO:0000269|PubMed:20385596};
KM=0.330 uM for GDP (at 37 degrees Celsius)
{ECO:0000269|PubMed:20385596};
KM=0.319 mM for dGDP (at 37 degrees Celsius)
{ECO:0000269|PubMed:20385596};
KM=15.7 mM for XDP (at 37 degrees Celsius)
{ECO:0000269|PubMed:20385596};
KM=22.1 mM for ITP (at 37 degrees Celsius)
{ECO:0000269|PubMed:20385596};
KM=24.1 mM for dITP (at 37 degrees Celsius)
{ECO:0000269|PubMed:20385596};
Note=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. {ECO:0000269|PubMed:20385596};
pH dependence:
Gradually increased from pH 6.5 to 8.5 in its IDP hydrolyzing
activity. {ECO:0000269|PubMed:20385596};
Temperature dependence:
Exhibited a temperature-dependent increase in its IDP
hydrolyzing activity up to 60 degrees Celsius.
{ECO:0000269|PubMed:20385596};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17567574,
ECO:0000269|PubMed:18820299, ECO:0000269|PubMed:26121039}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-5464685, EBI-5464685;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20385596,
ECO:0000269|PubMed:21337011}. Nucleus, nucleoplasm
{ECO:0000250|UniProtKB:Q6TEC1}. Nucleus, nucleolus
{ECO:0000250|UniProtKB:Q6TEC1}. Cytoplasm
{ECO:0000269|PubMed:21070968, ECO:0000269|PubMed:21337011}.
Note=Localized predominantly in the cytoplasm (PubMed:21070968).
Localized in nucleolus, and in a minor proportion in distinct foci
in the nucleoplasm (By similarity). {ECO:0000250|UniProtKB:Q6TEC1,
ECO:0000269|PubMed:21070968}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q96DE0-1; Sequence=Displayed;
Name=2;
IsoId=Q96DE0-2; Sequence=VSP_045450, VSP_045451;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q96DE0-3; Sequence=VSP_045449, VSP_045452;
Note=No experimental confirmation available. Ref.2 (BP199028)
sequence is in conflict in position: 128:A->Missing.
{ECO:0000305};
Name=4;
IsoId=Q96DE0-4; Sequence=VSP_045451;
-!- TISSUE SPECIFICITY: Expressed strongly in lung, kidney, adrenal
gland, testis, heart and brain. {ECO:0000269|PubMed:20385596}.
-!- SIMILARITY: Belongs to the Nudix hydrolase family. NUDT16
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB71024.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK055827; BAB71024.1; ALT_INIT; mRNA.
EMBL; AK304650; BAG65426.1; -; mRNA.
EMBL; BP199028; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC010210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC009546; AAH09546.1; -; mRNA.
EMBL; BC031215; AAH31215.2; -; mRNA.
CCDS; CCDS3070.2; -. [Q96DE0-1]
CCDS; CCDS54640.1; -. [Q96DE0-4]
CCDS; CCDS54641.1; -. [Q96DE0-3]
RefSeq; NP_001165376.1; NM_001171905.1. [Q96DE0-3]
RefSeq; NP_001165377.1; NM_001171906.1. [Q96DE0-4]
RefSeq; NP_689608.2; NM_152395.2. [Q96DE0-1]
UniGene; Hs.282050; -.
PDB; 2XSQ; X-ray; 1.72 A; A=1-195.
PDB; 3COU; X-ray; 1.80 A; A=1-195.
PDB; 3MGM; X-ray; 1.80 A; A/B=1-195.
PDBsum; 2XSQ; -.
PDBsum; 3COU; -.
PDBsum; 3MGM; -.
ProteinModelPortal; Q96DE0; -.
SMR; Q96DE0; -.
BioGrid; 126295; 13.
IntAct; Q96DE0; 1.
MINT; MINT-5003418; -.
STRING; 9606.ENSP00000422375; -.
iPTMnet; Q96DE0; -.
PhosphoSitePlus; Q96DE0; -.
BioMuta; NUDT16; -.
DMDM; 68565926; -.
EPD; Q96DE0; -.
MaxQB; Q96DE0; -.
PaxDb; Q96DE0; -.
PeptideAtlas; Q96DE0; -.
PRIDE; Q96DE0; -.
TopDownProteomics; Q96DE0-1; -. [Q96DE0-1]
Ensembl; ENST00000502852; ENSP00000422375; ENSG00000198585. [Q96DE0-4]
Ensembl; ENST00000521288; ENSP00000429274; ENSG00000198585. [Q96DE0-1]
Ensembl; ENST00000537561; ENSP00000440230; ENSG00000198585. [Q96DE0-3]
GeneID; 131870; -.
KEGG; hsa:131870; -.
UCSC; uc003eog.3; human. [Q96DE0-1]
CTD; 131870; -.
DisGeNET; 131870; -.
EuPathDB; HostDB:ENSG00000198585.11; -.
GeneCards; NUDT16; -.
H-InvDB; HIX0003684; -.
HGNC; HGNC:26442; NUDT16.
HPA; HPA060452; -.
HPA; HPA062492; -.
MIM; 617381; gene.
neXtProt; NX_Q96DE0; -.
OpenTargets; ENSG00000198585; -.
PharmGKB; PA134955224; -.
eggNOG; ENOG410IYGP; Eukaryota.
eggNOG; ENOG4111QA1; LUCA.
GeneTree; ENSGT00390000016224; -.
HOGENOM; HOG000007083; -.
HOVERGEN; HBG067297; -.
InParanoid; Q96DE0; -.
KO; K16855; -.
OMA; FYAKCLT; -.
OrthoDB; EOG091G0XY4; -.
PhylomeDB; Q96DE0; -.
BioCyc; MetaCyc:MONOMER-17869; -.
BRENDA; 3.6.1.62; 2681.
BRENDA; 3.6.1.64; 2681.
Reactome; R-HSA-2393930; Phosphate bond hydrolysis by NUDT proteins.
ChiTaRS; NUDT16; human.
EvolutionaryTrace; Q96DE0; -.
GenomeRNAi; 131870; -.
PRO; PR:Q96DE0; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000198585; -.
CleanEx; HS_NUDT16; -.
Genevisible; Q96DE0; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
GO; GO:0097383; F:dIDP diphosphatase activity; EXP:Reactome.
GO; GO:0035870; F:dITP diphosphatase activity; ISS:UniProtKB.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:1990003; F:IDP phosphatase activity; EXP:Reactome.
GO; GO:1901641; F:ITP binding; IDA:UniProtKB.
GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
GO; GO:0008235; F:metalloexopeptidase activity; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0030515; F:snoRNA binding; IDA:UniProtKB.
GO; GO:1901640; F:XTP binding; IDA:UniProtKB.
GO; GO:0006382; P:adenosine to inosine editing; IMP:UniProtKB.
GO; GO:0035863; P:dITP catabolic process; ISS:UniProtKB.
GO; GO:0046709; P:IDP catabolic process; IDA:UniProtKB.
GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
GO; GO:2000233; P:negative regulation of rRNA processing; ISS:UniProtKB.
GO; GO:0034656; P:nucleobase-containing small molecule catabolic process; TAS:Reactome.
GO; GO:0090068; P:positive regulation of cell cycle process; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:2000781; P:positive regulation of double-strand break repair; IMP:UniProtKB.
GO; GO:0016077; P:snoRNA catabolic process; IDA:UniProtKB.
GO; GO:1901639; P:XDP catabolic process; IDA:UniProtKB.
InterPro; IPR000086; NUDIX_hydrolase_dom.
InterPro; IPR015797; NUDIX_hydrolase_dom-like.
Pfam; PF00293; NUDIX; 1.
SUPFAM; SSF55811; SSF55811; 1.
PROSITE; PS51462; NUDIX; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide metabolism;
Nucleotide-binding; Nucleus; Reference proteome; RNA-binding.
CHAIN 1 195 U8 snoRNA-decapping enzyme.
/FTId=PRO_0000057117.
DOMAIN 18 173 Nudix hydrolase. {ECO:0000255|PROSITE-
ProRule:PRU00794}.
MOTIF 61 82 Nudix box.
METAL 59 59 Magnesium or manganese 1; via carbonyl
oxygen. {ECO:0000269|PubMed:26121039}.
METAL 76 76 Magnesium or manganese 2.
{ECO:0000269|PubMed:26121039}.
METAL 76 76 Magnesium or manganese 3.
{ECO:0000250|UniProtKB:Q6TEC1}.
METAL 80 80 Magnesium or manganese 1.
{ECO:0000269|PubMed:26121039}.
METAL 80 80 Magnesium or manganese 3.
{ECO:0000250|UniProtKB:Q6TEC1}.
METAL 136 136 Magnesium or manganese 3.
{ECO:0000250|UniProtKB:Q6TEC1}.
METAL 136 136 Magnesium or manganese 4.
{ECO:0000250|UniProtKB:Q6TEC1}.
BINDING 24 24 Substrate. {ECO:0000305|PubMed:26121039}.
BINDING 50 50 Substrate. {ECO:0000305|PubMed:26121039}.
BINDING 57 57 Substrate; via amide nitrogen.
{ECO:0000305|PubMed:26121039}.
BINDING 170 170 Substrate. {ECO:0000305|PubMed:26121039}.
VAR_SEQ 1 46 Missing (in isoform 3).
{ECO:0000303|PubMed:16344560}.
/FTId=VSP_045449.
VAR_SEQ 1 33 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045450.
VAR_SEQ 138 195 LGLVRVPLYTLRDGVGGLPTFLENSFIGSAREQLLEALQDL
GLLQSGSISGLKIPAHH -> GPAWDSVPFPISSSPKAFSP
PRKHPWRKVFAPLTLPSPQLSWWSWDRDHLYSELVLPTWAF
CKGLSHPLPGEILSRTHSSMSLCCSLLTV (in isoform
2 and isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045451.
VAR_SEQ 174 195 ALQDLGLLQSGSISGLKIPAHH -> AALHGPMKTEMRTLV
LGREGRTWECFLIGSER (in isoform 3).
{ECO:0000303|PubMed:16344560}.
/FTId=VSP_045452.
CONFLICT 22 22 A -> V (in Ref. 4; AAH31215).
{ECO:0000305}.
STRAND 5 7 {ECO:0000244|PDB:2XSQ}.
HELIX 9 13 {ECO:0000244|PDB:2XSQ}.
STRAND 20 35 {ECO:0000244|PDB:2XSQ}.
TURN 36 38 {ECO:0000244|PDB:2XSQ}.
STRAND 39 50 {ECO:0000244|PDB:2XSQ}.
STRAND 58 61 {ECO:0000244|PDB:2XSQ}.
TURN 64 66 {ECO:0000244|PDB:3MGM}.
HELIX 69 81 {ECO:0000244|PDB:2XSQ}.
HELIX 83 87 {ECO:0000244|PDB:2XSQ}.
HELIX 92 94 {ECO:0000244|PDB:2XSQ}.
STRAND 95 100 {ECO:0000244|PDB:2XSQ}.
STRAND 102 114 {ECO:0000244|PDB:2XSQ}.
HELIX 117 126 {ECO:0000244|PDB:2XSQ}.
HELIX 127 129 {ECO:0000244|PDB:2XSQ}.
TURN 134 136 {ECO:0000244|PDB:2XSQ}.
STRAND 137 142 {ECO:0000244|PDB:2XSQ}.
HELIX 155 158 {ECO:0000244|PDB:2XSQ}.
HELIX 167 177 {ECO:0000244|PDB:2XSQ}.
TURN 178 181 {ECO:0000244|PDB:2XSQ}.
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


Related products :

Catalog number Product name Quantity
EIAAB28212 Homo sapiens,Human,Nucleoside diphosphate-linked moiety X motif 16,Nudix motif 16,NUDT16,U8 snoRNA-binding protein H29K,U8 snoRNA-decapping enzyme
EIAAB28211 Mouse,Mus musculus,Nucleoside diphosphate-linked moiety X motif 16,Nudix motif 16,Nudt16,U8 snoRNA-decapping enzyme
EIAAB28213 Bos taurus,Bovine,Nucleoside diphosphate-linked moiety X motif 16,Nudix motif 16,NUDT16,U8 snoRNA-decapping enzyme
EIAAB10637 DCP2,hDpc,Homo sapiens,Human,mRNA-decapping enzyme 2,Nucleoside diphosphate-linked moiety X motif 20,Nudix motif 20,NUDT20
EIAAB28246 Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 2,Diphosphoinositol polyphosphate phosphohydrolase 2,Dipp2,DIPP-2,Mouse,Mus musculus,Nucleoside diphosphate-linked moiety X motif 4,Nudix motif 4,Nudt
EIAAB28245 Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 2,Diphosphoinositol polyphosphate phosphohydrolase 2,Dipp2,DIPP-2,Nucleoside diphosphate-linked moiety X motif 4,Nudix motif 4,Nudt4,Rat,Rattus norveg
EIAAB28243 Bos taurus,Bovine,Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 1,Diphosphoinositol polyphosphate phosphohydrolase 1,DIPP1,DIPP-1,Nucleoside diphosphate-linked moiety X motif 3,Nudix motif 3,NUDT3
EIAAB28241 Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 1,Diphosphoinositol polyphosphate phosphohydrolase 1,Dipp,Dipp1,DIPP-1,Nucleoside diphosphate-linked moiety X motif 3,Nudix motif 3,Nudt3,Rat,Rattus n
EIAAB28240 Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 1,Diphosphoinositol polyphosphate phosphohydrolase 1,DIPP,DIPP1,DIPP-1,Homo sapiens,Human,Nucleoside diphosphate-linked moiety X motif 3,Nudix motif 3
60265 IgG,nudix (nucleoside diphosphate linked moiety X)_type motif 21 (NUDT21), mRNA 0.1 mg
GWB-16C9CD nudix (nucleoside diphosphate linked moiety X)-type motif 21 (NUDT21) mRNA, Antibody
EIAAB28252 Nucleoside diphosphate-linked moiety X motif 6,Nudix motif 6,Nudt6,Protein GFG,Rat,Rattus norvegicus
EIAAB28242 Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 1,Diphosphoinositol polyphosphate phosphohydrolase 1,Dipp,Dipp1,DIPP-1,Mouse,muDIPP1,Mus musculus,Nucleoside diphosphate-linked moiety X motif 3,Nudix
EIAAB28207 Mouse,Mus musculus,Nucleoside diphosphate-linked moiety X motif 14,Nudix motif 14,Nudt14,UDPG pyrophosphatase,UGPPase,Uridine diphosphate glucose pyrophosphatase
EIAAB28205 Homo sapiens,Human,Nucleoside diphosphate-linked moiety X motif 13,Nudix motif 13,NUDT13,Protein KiSS-16
EIAAB28208 Bos taurus,Bovine,Nucleoside diphosphate-linked moiety X motif 14,Nudix motif 14,NUDT14,UDPG pyrophosphatase,UGPP,UGPPase,Uridine diphosphate glucose pyrophosphatase
EIAAB28206 Homo sapiens,Human,Nucleoside diphosphate-linked moiety X motif 14,Nudix motif 14,NUDT14,UDPG pyrophosphatase,UGPP,UGPPase,Uridine diphosphate glucose pyrophosphatase
EIAAB28217 Nucleoside diphosphate-linked moiety X motif 18,Nudix motif 18,Nudt18,Rat,Rattus norvegicus
EIAAB28227 Nucleoside diphosphate-linked moiety X motif 22,Nudix motif 22,Nudt22,Rat,Rattus norvegicus
EIAAB28214 Mouse,Mus musculus,Nucleoside diphosphate-linked moiety X motif 17,Nudix motif 17,Nudt17
EIAAB28216 Bos taurus,Bovine,Nucleoside diphosphate-linked moiety X motif 17,Nudix motif 17,NUDT17
EIAAB28226 Bos taurus,Bovine,Nucleoside diphosphate-linked moiety X motif 22,Nudix motif 22,NUDT22
EIAAB28218 Mouse,Mus musculus,Nucleoside diphosphate-linked moiety X motif 18,Nudix motif 18,Nudt18
EIAAB28225 Mouse,Mus musculus,Nucleoside diphosphate-linked moiety X motif 22,Nudix motif 22,Nudt22
EIAAB28204 Mouse,Mus musculus,Nucleoside diphosphate-linked moiety X motif 13,Nudix motif 13,Nudt13


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur