Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 174 (18 Sep 2019)
Sequence version 1 (01 May 2000)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

ADP-sugar pyrophosphatase

Gene

NUDT5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Enzyme that can either act as an ADP-sugar pyrophosphatase in absence of diphosphate or catalyze the synthesis of ATP in presence of diphosphate (PubMed:27257257). In absence of diphosphate, hydrolyzes with similar activities various modified nucleoside diphosphates such as ADP-ribose, ADP-mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP (PubMed:10567213, PubMed:10722730, PubMed:19699693, PubMed:21389046, PubMed:17052728). Can also hydrolyze other nucleotide sugars with low activity (PubMed:19699693, PubMed:21389046). In presence of diphosphate, mediates the synthesis of ATP in the nucleus by catalyzing the conversion of ADP-ribose to ATP and ribose 5-phosphate. Nuclear ATP synthesis takes place when dephosphorylated at Thr-45 (PubMed:27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257). Does not play a role in U8 snoRNA decapping activity (By similarity). Binds U8 snoRNA (By similarity).By similarity6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+3 PublicationsNote: Binds 3 Mg2+ ions per subunit.3 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 0.369 min(-1) for 8-OH-dGDP. kcat is 0.538 min(-1) for 8-OH-dADP. kcat is 0.226 min(-1) for 2-OH-dADP. kcat is 0.209 min(-1) for 5-CHO-dUDP. kcat is 0.929 min(-1) for dGDP. kcat is 0.365 min(-1) for dADP.1 Publication
  1. KM=2.1 µM for 8-oxo-dGDP1 Publication
  2. KM=2.9 µM for 8-oxo-dADP1 Publication
  3. KM=8.8 µM for 2-oxo-dADP1 Publication
  4. KM=4.0 µM for 5-CHO-dUDP1 Publication
  5. KM=7.6 µM for dGDP1 Publication
  6. KM=12.6 µM for dADP1 Publication
  7. KM=3.8 µM for 8-oxo-dGDP (at pH 8.0)1 Publication
  8. KM=3.5 µM for 8-oxo-dGDP (at pH 10.0)1 Publication
  9. KM=1.9 µM for ADP-D-ribose (at pH 8.0)1 Publication
  10. KM=36 µM for 8-oxo-dGTP (at pH 10.0)1 Publication
  11. KM=42.6 µM for ADP-D-ribose (in the presence of diphosphate)1 Publication
  1. Vmax=11 pmol/min/µg enzyme with 8-oxo-dGDP as substrate (at pH 8.0)1 Publication
  2. Vmax=2400 pmol/min/µg enzyme with ADP-D-ribose as substrate (at pH 8.0)1 Publication
  3. Vmax=46 pmol/min/µg enzyme with 8-oxo-dGDP as substrate (at pH 10.0)1 Publication
  4. Vmax=1.7 pmol/min/µg enzyme with 8-oxo-dGTP as substrate (at pH 10.0)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei28Substrate3 Publications1
Binding sitei51Substrate; shared with dimeric partner3 Publications1
Binding sitei84Substrate3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi96Magnesium 1; via carbonyl oxygen3 Publications1
Binding sitei98Substrate; via amide nitrogen1 Publication1
Metal bindingi112Magnesium 23 Publications1
Metal bindingi112Magnesium 33 Publications1
Metal bindingi116Magnesium 13 Publications1
Metal bindingi116Magnesium 33 Publications1
Binding sitei133Substrate1 Publication1
Metal bindingi166Magnesium 33 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, RNA-binding, Transferase
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS09255-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.6.1.13 2681
3.6.1.58 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-2393930 Phosphate bond hydrolysis by NUDT proteins

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q9UKK9

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
ADP-sugar pyrophosphatase (EC:3.6.1.132 Publications)
Alternative name(s):
8-oxo-dGDP phosphatase (EC:3.6.1.583 Publications)
Nuclear ATP-synthesis protein NUDIX51 Publication (EC:2.7.7.961 Publication)
Nucleoside diphosphate-linked moiety X motif 5Curated
Short name:
Nudix motif 5Curated
Short name:
hNUDT51 Publication
YSA1H1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:NUDT5
Synonyms:NUDIX51 Publication
ORF Names:HSPC1151 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 10

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:8052 NUDT5

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
609230 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9UKK9

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi28W → A: Reduces affinity for substrate about 8-fold. Strongly reduced catalytic activity and strongly reduced affinity for substrate; when associated with A-46. 1 Publication1
Mutagenesisi45T → A: Impaired phosphorylation; generates ATP in the presence of diphosphate. 1 Publication1
Mutagenesisi45T → D: Phosphomimetic mutant; unable to generate ATP in the presence of diphosphate. 1 Publication1
Mutagenesisi46W → A: Reduces affinity for substrate about 6-fold. Strongly reduced catalytic activity and strongly reduced affinity for substrate; when associated with A-28. 1 Publication1
Mutagenesisi51R → Q: Reduces affinity for substrate about 15-fold and reduces catalytic rate about 17-fold. 1 Publication1
Mutagenesisi84R → Q: Reduces affinity for substrate about 5-fold and reduces catalytic rate 67-fold. 1 Publication1
Mutagenesisi98L → A: Reduces affinity for substrate about 6-fold. 1 Publication1
Mutagenesisi112E → Q: Catalytic inactive mutant for both ADP-sugar pyrophosphatase and nuclear ATP-synthesis activities. Reduces catalytic rate 6300-fold. 2 Publications1
Mutagenesisi116E → Q: Reduces catalytic rate 2000-fold. 1 Publication1
Mutagenesisi166E → Q: Reduces catalytic rate 120-fold. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
11164

Open Targets

More...
OpenTargetsi
ENSG00000165609

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA31838

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q9UKK9

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4105713

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
NUDT5

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000570481 – 219ADP-sugar pyrophosphataseAdd BLAST219

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineCombined sources1
Modified residuei3PhosphoserineCombined sources1
Modified residuei10PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki42Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei45Phosphothreonine1 Publication1
Modified residuei74PhosphotyrosineCombined sources1
Modified residuei210N6-acetyllysineCombined sources1
Modified residuei218N6-acetyllysineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation at Thr-45 is required for homodimer stability; dephosphorylation results in destabilization of the homodimer. Dephosphorylation at Thr-45 promotes the ATP-synthesis activity.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9UKK9

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q9UKK9

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q9UKK9

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9UKK9

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9UKK9

PeptideAtlas

More...
PeptideAtlasi
Q9UKK9

PRoteomics IDEntifications database

More...
PRIDEi
Q9UKK9

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
84813

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9UKK9

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9UKK9

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q9UKK9

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed. Most abundant in liver.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Overexpressed in cancer patients with a poor outcome.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000165609 Expressed in 195 organ(s), highest expression level in liver

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9UKK9 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9UKK9 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA019827

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:27257257, PubMed:17052728, PubMed:18462755, PubMed:21768126).

Interacts with PARG (PubMed:27257257).

4 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
116335, 27 interactors

Protein interaction database and analysis system

More...
IntActi
Q9UKK9, 17 interactors

Molecular INTeraction database

More...
MINTi
Q9UKK9

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000419628

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1219
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9UKK9

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9UKK9

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini57 – 197Nudix hydrolasePROSITE-ProRule annotationAdd BLAST141

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni46 – 47Substrate binding; shared with dimeric partner3 Publications2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi97 – 118Nudix boxAdd BLAST22

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the Nudix hydrolase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3041 Eukaryota
COG0494 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154045

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000174302

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9UKK9

KEGG Orthology (KO)

More...
KOi
K13987

Database of Orthologous Groups

More...
OrthoDBi
1466354at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9UKK9

TreeFam database of animal gene trees

More...
TreeFami
TF106347

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR020476 Nudix_hydrolase
IPR015797 NUDIX_hydrolase-like_dom_sf
IPR020084 NUDIX_hydrolase_CS
IPR000086 NUDIX_hydrolase_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00293 NUDIX, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00502 NUDIXFAMILY

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55811 SSF55811, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51462 NUDIX, 1 hit
PS00893 NUDIX_BOX, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 5 potential isoforms that are computationally mapped.Show allAlign All

Q9UKK9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MESQEPTESS QNGKQYIISE ELISEGKWVK LEKTTYMDPT GKTRTWESVK
60 70 80 90 100
RTTRKEQTAD GVAVIPVLQR TLHYECIVLV KQFRPPMGGY CIEFPAGLID
110 120 130 140 150
DGETPEAAAL RELEEETGYK GDIAECSPAV CMDPGLSNCT IHIVTVTING
160 170 180 190 200
DDAENARPKP KPGDGEFVEV ISLPKNDLLQ RLDALVAEEH LTVDARVYSY
210
ALALKHANAK PFEVPFLKF
Length:219
Mass (Da):24,328
Last modified:May 1, 2000 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6574E0BF1EA2BB26
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A6NFX8A6NFX8_HUMAN
ADP-sugar pyrophosphatase
NUDT5
232Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A6NJU6A6NJU6_HUMAN
ADP-sugar pyrophosphatase
NUDT5
186Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A6NCQ0A6NCQ0_HUMAN
ADP-sugar pyrophosphatase
NUDT5
180Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YEY4H0YEY4_HUMAN
ADP-sugar pyrophosphatase
NUDT5
137Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9JYY9C9JYY9_HUMAN
ADP-sugar pyrophosphatase
NUDT5
97Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti50 – 52KRT → NVP in AAF25479 (PubMed:10722730).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_034159123I → T. Corresponds to variant dbSNP:rs34863826Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF155832 mRNA Translation: AAF06734.1
AF218818 mRNA Translation: AAF25479.1
AF161464 mRNA Translation: AAF29079.1
CR457195 mRNA Translation: CAG33476.1
AK291131 mRNA Translation: BAF83820.1
CH471072 Genomic DNA Translation: EAW86322.1
BC000025 mRNA Translation: AAH00025.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS7089.1

NCBI Reference Sequences

More...
RefSeqi
NP_054861.2, NM_014142.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000491614; ENSP00000419628; ENSG00000165609
ENST00000537776; ENSP00000445116; ENSG00000165609

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
11164

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:11164

UCSC genome browser

More...
UCSCi
uc001ilj.4 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF155832 mRNA Translation: AAF06734.1
AF218818 mRNA Translation: AAF25479.1
AF161464 mRNA Translation: AAF29079.1
CR457195 mRNA Translation: CAG33476.1
AK291131 mRNA Translation: BAF83820.1
CH471072 Genomic DNA Translation: EAW86322.1
BC000025 mRNA Translation: AAH00025.1
CCDSiCCDS7089.1
RefSeqiNP_054861.2, NM_014142.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DSBX-ray2.50A/B/C/D1-219[»]
2DSCX-ray2.00A/B1-210[»]
2DSDX-ray2.60A/B1-210[»]
3AC9X-ray2.10A/B14-208[»]
3ACAX-ray2.05A/B13-208[»]
3BM4X-ray2.00A/B1-210[»]
3L85X-ray2.30A/B14-208[»]
5NQRX-ray2.20A/B1-219[»]
5NWHX-ray2.60A/B1-219[»]
5QJ4X-ray1.89A/B/C/D1-208[»]
5QJ5X-ray1.72A/B/C/D1-208[»]
5QJ6X-ray1.65A/B/C/D1-208[»]
5QJ7X-ray1.56A/B/C/D1-208[»]
5QJ8X-ray1.76A/B/C/D1-208[»]
5QJ9X-ray1.85A/B/C/D1-208[»]
5QJAX-ray1.64A/B/C/D1-208[»]
5QJBX-ray1.66A/B/C/D1-208[»]
5QJCX-ray1.47A/B/C/D1-208[»]
5QJDX-ray1.61A/B/C/D1-208[»]
5QJEX-ray1.75A/B/C/D1-208[»]
5QJFX-ray1.63A/B/C/D1-208[»]
5QJGX-ray1.57A/B/C/D1-208[»]
5QJHX-ray2.03A/B/C/D1-208[»]
5QJIX-ray1.69A/B/C/D1-208[»]
5QJJX-ray1.71A/B/C/D1-208[»]
5QJKX-ray1.65A/B/C/D1-208[»]
5QJLX-ray1.66A/B/C/D1-208[»]
5QJMX-ray1.75A/B/C/D1-208[»]
5QJNX-ray1.77A/B/C/D1-208[»]
5QJOX-ray1.98A/B/C/D1-208[»]
5QJPX-ray1.50A/B/C/D1-208[»]
5QJQX-ray1.55A/B/C/D1-208[»]
5QJRX-ray1.62A/B/C/D1-208[»]
5QJSX-ray1.58A/B/C/D1-208[»]
5QJTX-ray1.62A/B/C/D1-208[»]
5QJUX-ray1.77A/B/C/D1-208[»]
5QJVX-ray1.61A/B/C/D1-208[»]
5QJWX-ray1.57A/B/C/D1-208[»]
5QJXX-ray1.73A/B/C/D1-208[»]
5QJYX-ray1.77A/B/C/D1-208[»]
5QJZX-ray1.52A/B/C/D1-208[»]
5QK0X-ray1.44A/B/C/D1-208[»]
5QK1X-ray1.49A/B/C/D1-208[»]
5QK2X-ray1.65A/B/C/D1-208[»]
5QK3X-ray1.71A/B/C/D1-208[»]
5QK4X-ray1.62A/B/C/D1-208[»]
5QK5X-ray1.63A/B/C/D1-208[»]
5QK6X-ray1.51A/B/C/D1-208[»]
5QK7X-ray1.66A/B/C/D1-208[»]
5QK8X-ray1.71A/B/C/D1-208[»]
5QK9X-ray1.56A/B/C/D1-208[»]
5QKAX-ray1.55A/B/C/D1-208[»]
6GRUX-ray1.93A/B/C/D1-208[»]
SMRiQ9UKK9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi116335, 27 interactors
IntActiQ9UKK9, 17 interactors
MINTiQ9UKK9
STRINGi9606.ENSP00000419628

Chemistry databases

ChEMBLiCHEMBL4105713

PTM databases

iPTMnetiQ9UKK9
PhosphoSitePlusiQ9UKK9
SwissPalmiQ9UKK9

Polymorphism and mutation databases

BioMutaiNUDT5

Proteomic databases

EPDiQ9UKK9
jPOSTiQ9UKK9
MassIVEiQ9UKK9
MaxQBiQ9UKK9
PaxDbiQ9UKK9
PeptideAtlasiQ9UKK9
PRIDEiQ9UKK9
ProteomicsDBi84813

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
11164

Genome annotation databases

EnsembliENST00000491614; ENSP00000419628; ENSG00000165609
ENST00000537776; ENSP00000445116; ENSG00000165609
GeneIDi11164
KEGGihsa:11164
UCSCiuc001ilj.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
11164
DisGeNETi11164

GeneCards: human genes, protein and diseases

More...
GeneCardsi
NUDT5
HGNCiHGNC:8052 NUDT5
HPAiHPA019827
MIMi609230 gene
neXtProtiNX_Q9UKK9
OpenTargetsiENSG00000165609
PharmGKBiPA31838

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3041 Eukaryota
COG0494 LUCA
GeneTreeiENSGT00940000154045
HOGENOMiHOG000174302
InParanoidiQ9UKK9
KOiK13987
OrthoDBi1466354at2759
PhylomeDBiQ9UKK9
TreeFamiTF106347

Enzyme and pathway databases

BioCyciMetaCyc:HS09255-MONOMER
BRENDAi3.6.1.13 2681
3.6.1.58 2681
ReactomeiR-HSA-2393930 Phosphate bond hydrolysis by NUDT proteins
SABIO-RKiQ9UKK9

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
NUDT5 human
EvolutionaryTraceiQ9UKK9

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
NUDT5

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
11164
PharosiQ9UKK9

Protein Ontology

More...
PROi
PR:Q9UKK9

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000165609 Expressed in 195 organ(s), highest expression level in liver
ExpressionAtlasiQ9UKK9 baseline and differential
GenevisibleiQ9UKK9 HS

Family and domain databases

InterProiView protein in InterPro
IPR020476 Nudix_hydrolase
IPR015797 NUDIX_hydrolase-like_dom_sf
IPR020084 NUDIX_hydrolase_CS
IPR000086 NUDIX_hydrolase_dom
PfamiView protein in Pfam
PF00293 NUDIX, 1 hit
PRINTSiPR00502 NUDIXFAMILY
SUPFAMiSSF55811 SSF55811, 1 hit
PROSITEiView protein in PROSITE
PS51462 NUDIX, 1 hit
PS00893 NUDIX_BOX, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNUDT5_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9UKK9
Secondary accession number(s): A8K516, Q6IAG0, Q9UH49
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 1, 2000
Last modified: September 18, 2019
This is version 174 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again