NUD14_HUMAN
ID NUD14_HUMAN Reviewed; 222 AA.
AC O95848; Q86SJ8;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Uridine diphosphate glucose pyrophosphatase NUDT14;
DE Short=UDPG pyrophosphatase;
DE Short=UGPPase;
DE EC=3.6.1.45;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 14;
DE Short=Nudix motif 14;
GN Name=NUDT14; Synonyms=UGPP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10662552; DOI=10.1006/geno.1999.6045;
RA Deng Y., Madan A., Banta A.B., Friedman C., Trask B.J., Hood L., Li L.;
RT "Characterization, chromosomal localization, and the complete 30-kb DNA
RT sequence of the human Jagged2 (JAG2) gene.";
RL Genomics 63:133-138(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RC TISSUE=Thyroid;
RX PubMed=12429023; DOI=10.1042/bj20021140;
RA Yagi T., Baroja-Fernandez E., Yamamoto R., Munoz F.J., Akazawa T.,
RA Hong K.S., Pozueta-Romero J.;
RT "Cloning, expression and characterization of a mammalian Nudix hydrolase-
RT like enzyme that cleaves the pyrophosphate bond of UDP-glucose.";
RL Biochem. J. 370:409-415(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 28-222.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human uridine diphosphate glucose pyrophosphatase
RT (NUDT14).";
RL Submitted (FEB-2011) to the PDB data bank.
CC -!- FUNCTION: Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and
CC ADP-ribose to ribose 5-phosphate and AMP. The physiological substrate
CC is probably UDP-glucose. Poor activity on other substrates such as ADP-
CC glucose, CDP-glucose, GDP-glucose and GDP-mannose.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.;
CC EC=3.6.1.45;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0-9.5.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12429023}.
CC -!- INTERACTION:
CC O95848; P10398: ARAF; NbExp=3; IntAct=EBI-536866, EBI-365961;
CC O95848; Q8TBB1: LNX1; NbExp=8; IntAct=EBI-536866, EBI-739832;
CC O95848; Q9GZT8: NIF3L1; NbExp=6; IntAct=EBI-536866, EBI-740897;
CC O95848; Q96HA8: NTAQ1; NbExp=4; IntAct=EBI-536866, EBI-741158;
CC O95848; O95848: NUDT14; NbExp=5; IntAct=EBI-536866, EBI-536866;
CC O95848; Q04864: REL; NbExp=3; IntAct=EBI-536866, EBI-307352;
CC O95848; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-536866, EBI-11139477;
CC O95848; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-536866, EBI-750109;
CC O95848; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-536866, EBI-597063;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12429023}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD15563.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF111170; AAD15563.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB087802; BAC65455.1; -; mRNA.
DR EMBL; AL512355; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041584; AAH41584.1; -; mRNA.
DR CCDS; CCDS10000.1; -.
DR RefSeq; NP_803877.2; NM_177533.4.
DR PDB; 3Q91; X-ray; 2.70 A; A/B/C/D=28-222.
DR PDBsum; 3Q91; -.
DR AlphaFoldDB; O95848; -.
DR SMR; O95848; -.
DR BioGRID; 129152; 19.
DR IntAct; O95848; 12.
DR STRING; 9606.ENSP00000376349; -.
DR BindingDB; O95848; -.
DR ChEMBL; CHEMBL4105943; -.
DR iPTMnet; O95848; -.
DR PhosphoSitePlus; O95848; -.
DR BioMuta; NUDT14; -.
DR EPD; O95848; -.
DR jPOST; O95848; -.
DR MassIVE; O95848; -.
DR MaxQB; O95848; -.
DR PaxDb; O95848; -.
DR PeptideAtlas; O95848; -.
DR PRIDE; O95848; -.
DR ProteomicsDB; 51089; -.
DR Antibodypedia; 49103; 73 antibodies from 17 providers.
DR DNASU; 256281; -.
DR Ensembl; ENST00000392568.7; ENSP00000376349.2; ENSG00000183828.15.
DR GeneID; 256281; -.
DR KEGG; hsa:256281; -.
DR MANE-Select; ENST00000392568.7; ENSP00000376349.2; NM_177533.5; NP_803877.2.
DR UCSC; uc010tyn.4; human.
DR CTD; 256281; -.
DR GeneCards; NUDT14; -.
DR HGNC; HGNC:20141; NUDT14.
DR HPA; ENSG00000183828; Low tissue specificity.
DR MIM; 609219; gene.
DR neXtProt; NX_O95848; -.
DR OpenTargets; ENSG00000183828; -.
DR PharmGKB; PA134971372; -.
DR VEuPathDB; HostDB:ENSG00000183828; -.
DR eggNOG; KOG4432; Eukaryota.
DR GeneTree; ENSGT00940000154045; -.
DR HOGENOM; CLU_062658_1_0_1; -.
DR InParanoid; O95848; -.
DR OMA; YTYELCA; -.
DR OrthoDB; 1164318at2759; -.
DR PhylomeDB; O95848; -.
DR TreeFam; TF313661; -.
DR BRENDA; 3.6.1.45; 2681.
DR PathwayCommons; O95848; -.
DR Reactome; R-HSA-480985; Synthesis of dolichyl-phosphate-glucose.
DR SignaLink; O95848; -.
DR BioGRID-ORCS; 256281; 10 hits in 1072 CRISPR screens.
DR EvolutionaryTrace; O95848; -.
DR GenomeRNAi; 256281; -.
DR Pharos; O95848; Tbio.
DR PRO; PR:O95848; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O95848; protein.
DR Bgee; ENSG00000183828; Expressed in adenohypophysis and 145 other tissues.
DR ExpressionAtlas; O95848; baseline and differential.
DR Genevisible; O95848; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008768; F:UDP-sugar diphosphatase activity; IBA:GO_Central.
DR GO; GO:0006753; P:nucleoside phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR GO; GO:0019693; P:ribose phosphate metabolic process; IBA:GO_Central.
DR InterPro; IPR004385; NDP_pyrophosphatase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR TIGRFAMs; TIGR00052; TIGR00052; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Magnesium; Reference proteome.
FT CHAIN 1..222
FT /note="Uridine diphosphate glucose pyrophosphatase NUDT14"
FT /id="PRO_0000057113"
FT DOMAIN 38..206
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 111..129
FT /note="Nudix box"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:3Q91"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:3Q91"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:3Q91"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:3Q91"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:3Q91"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3Q91"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:3Q91"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:3Q91"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:3Q91"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:3Q91"
FT STRAND 151..160
FT /evidence="ECO:0007829|PDB:3Q91"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:3Q91"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:3Q91"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:3Q91"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:3Q91"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:3Q91"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:3Q91"
SQ SEQUENCE 222 AA; 24118 MW; FB1DFA40A67E72B6 CRC64;
MERIEGASVG RCAASPYLRP LTLHYRQNGA QKSWDFMKTH DSVTVLLFNS SRRSLVLVKQ
FRPAVYAGEV ERRFPGSLAA VDQDGPRELQ PALPGSAGVT VELCAGLVDQ PGLSLEEVAC
KEAWEECGYH LAPSDLRRVA TYWSGVGLTG SRQTMFYTEV TDAQRSGPGG GLVEEGELIE
VVHLPLEGAQ AFADDPDIPK TLGVIFGVSW FLSQVAPNLD LQ
