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Protein

Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]

Gene

NUDT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis.

Catalytic activityi

P1,P(4)-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP.

Cofactori

a divalent metal cationBy similarityNote: Divalent metal ions.By similarity

GO - Molecular functioni

  1. bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity Source: UniProtKB
  2. bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity Source: ProtInc
  3. GTP binding Source: UniProtKB-KW

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. nucleobase-containing compound metabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKP50583.

Names & Taxonomyi

Protein namesi
Recommended name:
Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] (EC:3.6.1.17)
Alternative name(s):
Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase
Short name:
Ap4A hydrolase
Short name:
Ap4Aase
Short name:
Diadenosine tetraphosphatase
Nucleoside diphosphate-linked moiety X motif 2
Short name:
Nudix motif 2
Gene namesi
Name:NUDT2
Synonyms:APAH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:8049. NUDT2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31833.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 147146Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]PRO_0000057102Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP50583.
PaxDbiP50583.
PeptideAtlasiP50583.
PRIDEiP50583.

PTM databases

PhosphoSiteiP50583.

Expressioni

Gene expression databases

BgeeiP50583.
CleanExiHS_NUDT2.
GenevestigatoriP50583.

Organism-specific databases

HPAiCAB004684.
HPA044903.

Interactioni

Protein-protein interaction databases

BioGridi106815. 2 interactions.
STRINGi9606.ENSP00000338397.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 139Combined sources
Turni17 – 193Combined sources
Beta strandi23 – 3311Combined sources
Beta strandi42 – 443Combined sources
Beta strandi47 – 493Combined sources
Helixi51 – 6313Combined sources
Helixi67 – 693Combined sources
Beta strandi70 – 8415Combined sources
Beta strandi87 – 9913Combined sources
Beta strandi111 – 1177Combined sources
Helixi119 – 1268Combined sources
Helixi129 – 14719Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XSANMR-A1-147[»]
1XSBNMR-A1-147[»]
1XSCNMR-A2-147[»]
3U53X-ray2.70A/B/C/D1-147[»]
4ICKX-ray2.10A/B1-147[»]
4IJXX-ray2.10A/B1-147[»]
ProteinModelPortaliP50583.
SMRiP50583. Positions 4-147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50583.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 139139Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi43 – 6422Nudix boxAdd
BLAST

Sequence similaritiesi

Belongs to the Nudix hydrolase family.Curated
Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0494.
GeneTreeiENSGT00390000002416.
HOGENOMiHOG000261976.
HOVERGENiHBG002853.
KOiK01518.
OMAiHYPAGHW.
OrthoDBiEOG7GBFZN.
PhylomeDBiP50583.
TreeFamiTF105958.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR003565. Tetra_PHTase.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR01405. TETRPHPHTASE.
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P50583-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALRACGLII FRRCLIPKVD NNAIEFLLLQ ASDGIHHWTP PKGHVEPGED
60 70 80 90 100
DLETALRETQ EEAGIEAGQL TIIEGFKREL NYVARNKPKT VIYWLAEVKD
110 120 130 140
YDVEIRLSHE HQAYRWLGLE EACQLAQFKE MKAALQEGHQ FLCSIEA
Length:147
Mass (Da):16,829
Last modified:January 23, 2007 - v3
Checksum:i3599B12719F94AB8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30313 mRNA. Translation: AAC50277.1.
AL356494 Genomic DNA. Translation: CAI15964.1.
CH471071 Genomic DNA. Translation: EAW58461.1.
CH471071 Genomic DNA. Translation: EAW58462.1.
CH471071 Genomic DNA. Translation: EAW58463.1.
BC004926 mRNA. Translation: AAH04926.1.
CCDSiCCDS6552.1.
PIRiS60111.
RefSeqiNP_001152.1. NM_001161.4.
NP_001231319.1. NM_001244390.1.
NP_671701.1. NM_147172.2.
NP_671702.1. NM_147173.2.
UniGeneiHs.493767.
Hs.731743.

Genome annotation databases

EnsembliENST00000346365; ENSP00000344187; ENSG00000164978.
ENST00000379155; ENSP00000368452; ENSG00000164978.
ENST00000379158; ENSP00000368455; ENSG00000164978.
ENST00000618590; ENSP00000482384; ENSG00000164978.
GeneIDi318.
KEGGihsa:318.
UCSCiuc003zub.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30313 mRNA. Translation: AAC50277.1.
AL356494 Genomic DNA. Translation: CAI15964.1.
CH471071 Genomic DNA. Translation: EAW58461.1.
CH471071 Genomic DNA. Translation: EAW58462.1.
CH471071 Genomic DNA. Translation: EAW58463.1.
BC004926 mRNA. Translation: AAH04926.1.
CCDSiCCDS6552.1.
PIRiS60111.
RefSeqiNP_001152.1. NM_001161.4.
NP_001231319.1. NM_001244390.1.
NP_671701.1. NM_147172.2.
NP_671702.1. NM_147173.2.
UniGeneiHs.493767.
Hs.731743.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XSANMR-A1-147[»]
1XSBNMR-A1-147[»]
1XSCNMR-A2-147[»]
3U53X-ray2.70A/B/C/D1-147[»]
4ICKX-ray2.10A/B1-147[»]
4IJXX-ray2.10A/B1-147[»]
ProteinModelPortaliP50583.
SMRiP50583. Positions 4-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106815. 2 interactions.
STRINGi9606.ENSP00000338397.

PTM databases

PhosphoSiteiP50583.

Proteomic databases

MaxQBiP50583.
PaxDbiP50583.
PeptideAtlasiP50583.
PRIDEiP50583.

Protocols and materials databases

DNASUi318.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000346365; ENSP00000344187; ENSG00000164978.
ENST00000379155; ENSP00000368452; ENSG00000164978.
ENST00000379158; ENSP00000368455; ENSG00000164978.
ENST00000618590; ENSP00000482384; ENSG00000164978.
GeneIDi318.
KEGGihsa:318.
UCSCiuc003zub.3. human.

Organism-specific databases

CTDi318.
GeneCardsiGC09P034329.
HGNCiHGNC:8049. NUDT2.
HPAiCAB004684.
HPA044903.
MIMi602852. gene.
neXtProtiNX_P50583.
PharmGKBiPA31833.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0494.
GeneTreeiENSGT00390000002416.
HOGENOMiHOG000261976.
HOVERGENiHBG002853.
KOiK01518.
OMAiHYPAGHW.
OrthoDBiEOG7GBFZN.
PhylomeDBiP50583.
TreeFamiTF105958.

Enzyme and pathway databases

SABIO-RKP50583.

Miscellaneous databases

ChiTaRSiNUDT2. human.
EvolutionaryTraceiP50583.
GeneWikiiNUDT2.
GenomeRNAii318.
NextBioi1299.
PROiP50583.
SOURCEiSearch...

Gene expression databases

BgeeiP50583.
CleanExiHS_NUDT2.
GenevestigatoriP50583.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR003565. Tetra_PHTase.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR01405. TETRPHPHTASE.
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human diadenosine 5',5''-P1,P4-tetraphosphate pyrophosphohydrolase is a member of the MutT family of nucleotide pyrophosphatases."
    Thorne N.M.H., Hankin S., Wilkinson M.C., Nunez C., Barraclough R., McLennan A.G.
    Biochem. J. 311:717-721(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver and Spleen.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreas.
  5. McLennan A.G.
    Submitted (JAN-1997) to UniProtKB
    Cited for: ACETYLATION AT ALA-2.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Structure and substrate-binding mechanism of human Ap4A hydrolase."
    Swarbrick J.D., Buyya S., Gunawardana D., Gayler K.R., McLennan A.G., Gooley P.R.
    J. Biol. Chem. 280:8471-8481(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiAP4A_HUMAN
AccessioniPrimary (citable) accession number: P50583
Secondary accession number(s): D3DRM0, Q5T589
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

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