P50583 (AP4A_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 105.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | 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 names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 147 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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. |
Ontologies
| Keywords | |
|---|---|
| Ligand | GTP-binding Nucleotide-binding |
| Molecular function | Hydrolase |
| PTM | Acetylation |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | induction of apoptosis Inferred from sequence or structural similarity. Source: UniProtKB nucleobase-containing compound metabolic processTraceable author statement. Source: ProtInc |
| Molecular function | GTP binding Inferred from electronic annotation. Source: UniProtKB-KW bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activityInferred from sequence or structural similarity. Source: UniProtKB bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activityTraceable author statement. Source: ProtInc |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | ||||||||||||||||||||||||||||||||||
| Chain | 2 – 147 | 146 | Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] | PRO_0000057102 | |||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||
| Domain | 1 – 139 | 139 | Nudix hydrolase | ||||||||||||||||||||||||||||||||||
| Motif | 43 – 64 | 22 | Nudix box | ||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||
| Modified residue | 2 | 1 | N-acetylalanine Ref.5 | ||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||
| Beta strand | 4 – 13 | 10 | |||||||||||||||||||||||||||||||||||
| Beta strand | 19 – 21 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 23 – 31 | 9 | |||||||||||||||||||||||||||||||||||
| Turn | 32 – 35 | 4 | |||||||||||||||||||||||||||||||||||
| Beta strand | 41 – 44 | 4 | |||||||||||||||||||||||||||||||||||
| Beta strand | 47 – 49 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 51 – 62 | 12 | |||||||||||||||||||||||||||||||||||
| Helix | 67 – 69 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 70 – 72 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 79 – 81 | 3 | |||||||||||||||||||||||||||||||||||
| Turn | 84 – 86 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 90 – 99 | 10 | |||||||||||||||||||||||||||||||||||
| Beta strand | 111 – 117 | 7 | |||||||||||||||||||||||||||||||||||
| Helix | 119 – 126 | 8 | |||||||||||||||||||||||||||||||||||
| Helix | 129 – 143 | 15 | |||||||||||||||||||||||||||||||||||
Sequences
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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. 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. 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] | "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: 21269460] [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: 15596429] [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. | ||||||||||||||||||||||||
| IPI | IPI00221231. | ||||||||||||||||||||||||
| PIR | S60111. | ||||||||||||||||||||||||
| RefSeq | NP_001152.1. NM_001161.4. NP_001231319.1. NM_001244390.1. NP_671701.1. NM_147172.2. NP_671702.1. NM_147173.2. | ||||||||||||||||||||||||
| UniGene | Hs.493767. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P50583. | ||||||||||||||||||||||||
| SMR | P50583. Positions 1-147. | ||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| STRING | P50583. | ||||||||||||||||||||||||
Polymorphism databases | |||||||||||||||||||||||||
| DMDM | 1703326. | ||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||
| PeptideAtlas | P50583. | ||||||||||||||||||||||||
| PRIDE | P50583. | ||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| Ensembl | ENST00000337747; ENSP00000338397; ENSG00000164978. ENST00000346365; ENSP00000344187; ENSG00000164978. ENST00000379154; ENSP00000368451; ENSG00000164978. ENST00000379155; ENSP00000368452; ENSG00000164978. ENST00000379158; ENSP00000368455; ENSG00000164978. ENST00000407581; ENSP00000384512; ENSG00000164978. | ||||||||||||||||||||||||
| GeneID | 318. | ||||||||||||||||||||||||
| KEGG | hsa:318. | ||||||||||||||||||||||||
| UCSC | uc003zub.1. human. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| CTD | 318. | ||||||||||||||||||||||||
| GeneCards | GC09P034329. | ||||||||||||||||||||||||
| H-InvDB | HIX0007990. | ||||||||||||||||||||||||
| HGNC | HGNC:8049. NUDT2. | ||||||||||||||||||||||||
| HPA | CAB004684. | ||||||||||||||||||||||||
| MIM | 602852. gene. | ||||||||||||||||||||||||
| neXtProt | NX_P50583. | ||||||||||||||||||||||||
| PharmGKB | PA31833. | ||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| eggNOG | prNOG17445. | ||||||||||||||||||||||||
| GeneTree | ENSGT00390000002416. | ||||||||||||||||||||||||
| HOGENOM | HBG741910. | ||||||||||||||||||||||||
| HOVERGEN | HBG002853. | ||||||||||||||||||||||||
| InParanoid | P50583. | ||||||||||||||||||||||||
| OMA | RRRLIPK. | ||||||||||||||||||||||||
| OrthoDB | EOG4FTW20. | ||||||||||||||||||||||||
| PhylomeDB | P50583. | ||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||
| ArrayExpress | P50583. | ||||||||||||||||||||||||
| Bgee | P50583. | ||||||||||||||||||||||||
| CleanEx | HS_NUDT2. | ||||||||||||||||||||||||
| Genevestigator | P50583. | ||||||||||||||||||||||||
| GermOnline | ENSG00000164978. Homo sapiens. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR020084. NUDIX_hydrolase_CS. IPR000086. NUDIX_hydrolase_dom. IPR015797. NUDIX_hydrolase_dom-like. IPR003565. Tetra_PHTase. [Graphical view] | ||||||||||||||||||||||||
| Gene3D | G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit. | ||||||||||||||||||||||||
| KO | K01518. | ||||||||||||||||||||||||
| Pfam | PF00293. NUDIX. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| PRINTS | PR01405. TETRPHPHTASE. | ||||||||||||||||||||||||
| SUPFAM | SSF55811. NUDIX_hydrolase. 1 hit. | ||||||||||||||||||||||||
| PROSITE | PS51462. NUDIX. 1 hit. PS00893. NUDIX_BOX. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other | |||||||||||||||||||||||||
| NextBio | 1299. | ||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | AP4A_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P50583 Secondary accession number(s): D3DRM0, Q5T589 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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
| 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 |

Clusters with