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P50583 (AP4A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NUDT2
Synonyms:APAH1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Divalent ions By similarity.

Sequence similarities

Belongs to the Nudix hydrolase family.

Contains 1 nudix hydrolase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 147146Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
PRO_0000057102

Regions

Domain1 – 139139Nudix hydrolase
Motif43 – 6422Nudix box

Amino acid modifications

Modified residue21N-acetylalanine Ref.5

Secondary structure

....................... 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50583 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3599B12719F94AB8

FASTA14716,829
        10         20         30         40         50         60 
MALRACGLII FRRCLIPKVD NNAIEFLLLQ ASDGIHHWTP PKGHVEPGED DLETALRETQ 

        70         80         90        100        110        120 
EEAGIEAGQL TIIEGFKREL NYVARNKPKT VIYWLAEVKD YDVEIRLSHE HQAYRWLGLE 

       130        140 
EACQLAQFKE MKAALQEGHQ FLCSIEA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS6552.1.
PIRS60111.
RefSeqNP_001152.1. NM_001161.4.
NP_001231319.1. NM_001244390.1.
NP_671701.1. NM_147172.2.
NP_671702.1. NM_147173.2.
UniGeneHs.493767.
Hs.731743.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP50583.
SMRP50583. Positions 4-147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106815. 1 interaction.
STRING9606.ENSP00000338397.

PTM databases

PhosphoSiteP50583.

Proteomic databases

MaxQBP50583.
PaxDbP50583.
PeptideAtlasP50583.
PRIDEP50583.

Protocols and materials databases

DNASU318.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000346365; ENSP00000344187; ENSG00000164978.
ENST00000379155; ENSP00000368452; ENSG00000164978.
ENST00000379158; ENSP00000368455; ENSG00000164978.
GeneID318.
KEGGhsa:318.
UCSCuc003zub.3. human.

Organism-specific databases

CTD318.
GeneCardsGC09P034329.
HGNCHGNC:8049. NUDT2.
HPACAB004684.
HPA044903.
MIM602852. gene.
neXtProtNX_P50583.
PharmGKBPA31833.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0494.
HOGENOMHOG000261976.
HOVERGENHBG002853.
InParanoidP50583.
KOK01518.
OMARACGLIV.
OrthoDBEOG7GBFZN.
PhylomeDBP50583.
TreeFamTF105958.

Enzyme and pathway databases

SABIO-RKP50583.

Gene expression databases

BgeeP50583.
CleanExHS_NUDT2.
GenevestigatorP50583.

Family and domain databases

Gene3D3.90.79.10. 1 hit.
InterProIPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR003565. Tetra_PHTase.
[Graphical view]
PfamPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSPR01405. TETRPHPHTASE.
SUPFAMSSF55811. SSF55811. 1 hit.
PROSITEPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP50583.
GeneWikiNUDT2.
GenomeRNAi318.
NextBio1299.
PROP50583.
SOURCESearch...

Entry information

Entry nameAP4A_HUMAN
AccessionPrimary (citable) accession number: P50583
Secondary accession number(s): D3DRM0, Q5T589
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM