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P50583

- AP4A_HUMAN

UniProt

P50583 - AP4A_HUMAN

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Protein

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

Gene
NUDT2, APAH1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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

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
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 – 11Removed
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.

Miscellaneous databases

EvolutionaryTraceiP50583.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 139139Nudix hydrolaseAdd
BLAST

Motif

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

Sequence similaritiesi

Belongs to the Nudix hydrolase family.

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

« 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: July 9, 2014
This is version 131 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

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