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Reviewed, UniProtKB/Swiss-Prot P50583 (AP4A_HUMAN)

Last modified November 4, 2008. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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=Diadenosine tetraphosphatase
      Short name=Ap4A hydrolase
      Short name=Ap4Aase
    Nucleoside diphosphate-linked moiety X motif 2
      Short name=Nudix motif 2
Gene names
Name: NUDT2
Synonyms: APAH1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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General annotation (Comments)

Function

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

Catalytic activity

P(1),P(4)-bis(5'-guanosyl) tetraphosphate + H(2)O = GTP + GMP.

Cofactor

Divalent ions By similarity.

Sequence similarities

Belongs to the Nudix hydrolase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Motif43 – 6422Nudix box

Amino acid modifications

Modified residue21N-acetylalanine

Secondary structure

1 ............................. 147
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P50583-1 [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

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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: 7487923] [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: 15164053] [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: 15489334] [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]"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: 15596429] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

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Cross-references

Sequence databases

U30313 mRNA. Translation: AAC50277.1.
AL356494 Genomic DNA. Translation: CAI15964.1.
CH471071 Genomic DNA. Translation: EAW58461.1.
BC004926 mRNA. Translation: AAH04926.1.
PIRS60111.
RefSeqNP_001152.1.
NP_671701.1.
NP_671702.1.
UniGeneHs.493767

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1XSANMR-A1-147[»]
1XSBNMR-A1-147[»]
1XSCNMR-A1-147[»]
ModBaseSearch...

Proteomic databases

PeptideAtlasP50583.

Genome annotation databases

EnsemblENSG00000164978. Homo sapiens. [Contig view]
GeneID318.
KEGGhsa:318.

Organism-specific databases

H-InvDBHIX0007990.
HGNCHGNC:8049. NUDT2.
HPACAB004684.
MIM602852. gene.
PharmGKBPA31833.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMP50583.
HOVERGENP50583.

Gene expression databases

ArrayExpressP50583.
CleanExHS_NUDT2.
GermOnlineENSG00000164978. Homo sapiens.

Family and domain databases

InterProIPR000086. NUDIX_hydrolase_core.
IPR003565. Tetra_PHTase.
[Graphical view]
Gene3DG3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
PfamPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSPR00502. NUDIXFAMILY.
PR01405. TETRPHPHTASE.
PROSITEPS00893. NUDIX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio1299.
SOURCESearch...

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Entry information

Entry nameAP4A_HUMAN
AccessionPrimary (citable) accession number: P50583
Secondary accession number(s): Q5T589
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 4, 2008
This is version 73 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 9

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents