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P50583

- AP4A_HUMAN

UniProt

P50583 - AP4A_HUMAN

Protein

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

Gene

NUDT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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

    Divalent 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

    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

    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. 1 interaction.
    STRINGi9606.ENSP00000338397.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000261976.
    HOVERGENiHBG002853.
    InParanoidiP50583.
    KOiK01518.
    OMAiRACGLIV.
    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

    MALRACGLII FRRCLIPKVD NNAIEFLLLQ ASDGIHHWTP PKGHVEPGED    50
    DLETALRETQ EEAGIEAGQL TIIEGFKREL NYVARNKPKT VIYWLAEVKD 100
    YDVEIRLSHE HQAYRWLGLE EACQLAQFKE MKAALQEGHQ FLCSIEA 147
    Length:147
    Mass (Da):16,829
    Last modified:January 23, 2007 - v3
    Checksum:i3599B12719F94AB8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    GeneIDi318.
    KEGGihsa:318.
    UCSCiuc003zub.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6552.1.
    PIRi S60111.
    RefSeqi NP_001152.1. NM_001161.4.
    NP_001231319.1. NM_001244390.1.
    NP_671701.1. NM_147172.2.
    NP_671702.1. NM_147173.2.
    UniGenei Hs.493767.
    Hs.731743.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XSA NMR - A 1-147 [» ]
    1XSB NMR - A 1-147 [» ]
    1XSC NMR - A 2-147 [» ]
    3U53 X-ray 2.70 A/B/C/D 1-147 [» ]
    4ICK X-ray 2.10 A/B 1-147 [» ]
    4IJX X-ray 2.10 A/B 1-147 [» ]
    ProteinModelPortali P50583.
    SMRi P50583. Positions 4-147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106815. 1 interaction.
    STRINGi 9606.ENSP00000338397.

    PTM databases

    PhosphoSitei P50583.

    Proteomic databases

    MaxQBi P50583.
    PaxDbi P50583.
    PeptideAtlasi P50583.
    PRIDEi P50583.

    Protocols and materials databases

    DNASUi 318.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000346365 ; ENSP00000344187 ; ENSG00000164978 .
    ENST00000379155 ; ENSP00000368452 ; ENSG00000164978 .
    ENST00000379158 ; ENSP00000368455 ; ENSG00000164978 .
    GeneIDi 318.
    KEGGi hsa:318.
    UCSCi uc003zub.3. human.

    Organism-specific databases

    CTDi 318.
    GeneCardsi GC09P034329.
    HGNCi HGNC:8049. NUDT2.
    HPAi CAB004684.
    HPA044903.
    MIMi 602852. gene.
    neXtProti NX_P50583.
    PharmGKBi PA31833.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0494.
    HOGENOMi HOG000261976.
    HOVERGENi HBG002853.
    InParanoidi P50583.
    KOi K01518.
    OMAi RACGLIV.
    OrthoDBi EOG7GBFZN.
    PhylomeDBi P50583.
    TreeFami TF105958.

    Enzyme and pathway databases

    SABIO-RK P50583.

    Miscellaneous databases

    EvolutionaryTracei P50583.
    GeneWikii NUDT2.
    GenomeRNAii 318.
    NextBioi 1299.
    PROi P50583.
    SOURCEi Search...

    Gene expression databases

    Bgeei P50583.
    CleanExi HS_NUDT2.
    Genevestigatori P50583.

    Family and domain databases

    Gene3Di 3.90.79.10. 1 hit.
    InterProi IPR020084. NUDIX_hydrolase_CS.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    IPR003565. Tetra_PHTase.
    [Graphical view ]
    Pfami PF00293. NUDIX. 1 hit.
    [Graphical view ]
    PRINTSi PR01405. TETRPHPHTASE.
    SUPFAMi SSF55811. SSF55811. 1 hit.
    PROSITEi PS51462. NUDIX. 1 hit.
    PS00893. NUDIX_BOX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 132 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