Reviewed,
UniProtKB/Swiss-Prot Q9Y6K8 (KAD5_HUMAN)
Last modified
June 16, 2009.
Version 80.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Adenylate kinase isoenzyme 5 Short name=AK 5 EC=2.7.4.3 Alternative name(s): ATP-AMP transphosphorylase 5 | ||
| Gene names |
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| 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 | 198 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. |
| Catalytic activity | ATP + AMP = 2 ADP. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | |
| Tissue specificity | Brain specific. |
| Sequence similarities | Belongs to the adenylate kinase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | ADP biosynthetic process Ref.1 Traceable author statement. Source: ProtInc ATP metabolic processInferred from electronic annotation. Source: InterPro dADP biosynthetic process Ref.1Traceable author statement. Source: ProtInc pyrimidine ribonucleotide biosynthetic process Ref.1Traceable author statement. Source: ProtInc |
| Cellular component | cytosol Ref.1 Inferred from Experiment. Source: Reactome |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate kinase activity Ref.1Traceable author statement. Source: ProtInc nucleoside kinase activity Ref.1Inferred from Experiment. Source: Reactome |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 198 | 198 | Adenylate kinase isoenzyme 5 | PRO_0000158930 | |||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||
| Nucleotide binding | 18 – 26 | 9 | ATP By similarity | ||||||||||||||||||||||||||||||
| Nucleotide binding | 97 – 104 | 8 | AMP By similarity | ||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||
| Binding site | 42 | 1 | AMP By similarity | ||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||
| Sequence conflict | 197 | 1 | Missing in AAH12467. Ref.3 | ||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||
| Helix | 4 – 10 | 7 | |||||||||||||||||||||||||||||||
| Beta strand | 13 – 18 | 6 | |||||||||||||||||||||||||||||||
| Helix | 24 – 35 | 12 | |||||||||||||||||||||||||||||||
| Beta strand | 38 – 41 | 4 | |||||||||||||||||||||||||||||||
| Helix | 42 – 52 | 11 | |||||||||||||||||||||||||||||||
| Helix | 55 – 65 | 11 | |||||||||||||||||||||||||||||||
| Helix | 72 – 86 | 15 | |||||||||||||||||||||||||||||||
| Beta strand | 93 – 96 | 4 | |||||||||||||||||||||||||||||||
| Helix | 102 – 111 | 10 | |||||||||||||||||||||||||||||||
| Beta strand | 116 – 122 | 7 | |||||||||||||||||||||||||||||||
| Helix | 125 – 134 | 10 | |||||||||||||||||||||||||||||||
| Helix | 142 – 170 | 29 | |||||||||||||||||||||||||||||||
| Beta strand | 171 – 177 | 7 | |||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification of a novel human adenylate kinase. cDNA cloning, expression analysis, chromosome localization and characterization of the recombinant protein." Van Rompay A.R., Johansson M., Karlsson A. Eur. J. Biochem. 261:509-517(1999) [PubMed: 10215863] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [3] | "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: Liver. |
| [4] | "Crystal structure of adenylate kinase 5." Structural genomics consortium (SGC) Submitted (JUL-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH AMP. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AF062595 mRNA. Translation: AAD27956.1. CR541890 mRNA. Translation: CAG46688.1. BC012467 mRNA. Translation: AAH12467.2. Different initiation. | |||||||||||||
| IPI | IPI00844054. | ||||||||||||
| RefSeq | NP_036225.2. | ||||||||||||
| UniGene | Hs.559718 | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q9Y6K8. 7 interactions. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSG00000154027. Homo sapiens. [Contig view] | ||||||||||||
| GeneID | 26289. | ||||||||||||
| KEGG | hsa:26289. | ||||||||||||
Organism-specific databases | |||||||||||||
| GeneCards | GC01P077459. | ||||||||||||
| H-InvDB | HIX0020812. | ||||||||||||
| HGNC | HGNC:365. AK5. | ||||||||||||
| MIM | 608009. gene. | ||||||||||||
| PharmGKB | PA24659. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOVERGEN | Q9Y6K8. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 2.7.4.3. 247. | ||||||||||||
| Reactome | REACT_1698. Nucleotide metabolism. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q9Y6K8. | ||||||||||||
| Bgee | Q9Y6K8. | ||||||||||||
| CleanEx | HS_AK5. | ||||||||||||
| GermOnline | ENSG00000154027. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR000850. Adenylate_kin. IPR006267. Adenylate_kin1. [Graphical view] | ||||||||||||
| PANTHER | PTHR23359. Adenylate_kin. 1 hit. | ||||||||||||
| Pfam | PF00406. ADK. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00094. ADENYLTKNASE. | ||||||||||||
| ProDom | PD000657. Adenylate_kin. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| TIGRFAMs | TIGR01360. aden_kin_iso1. 1 hit. | ||||||||||||
| PROSITE | PS00113. ADENYLATE_KINASE. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| NextBio | 48625. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | KAD5_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9Y6K8 Secondary accession number(s): Q6FH66, Q96EC9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 1 Human chromosome 1: 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


