Reviewed,
UniProtKB/Swiss-Prot P08166 (KAD2_BOVIN)
Last modified
June 16, 2009.
Version 93.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Adenylate kinase 2, mitochondrial Short name=AK 2 EC=2.7.4.3 Alternative name(s): ATP-AMP transphosphorylase 2 | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 241 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 | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth. Plays a key role in hematopoiesis By similarity. |
| Catalytic activity | ATP + AMP = 2 ADP. |
| Subunit structure | Monomer. |
| Subcellular location | |
| Sequence similarities | Belongs to the adenylate kinase family. AK2 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Coding sequence diversity | Alternative splicing |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| PTM | Acetylation Disulfide bond |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | nucleobase, nucleoside, nucleotide and nucleic acid metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | mitochondrial inner membrane Inferred from sequence or structural similarity. Source: AgBase mitochondrial intermembrane spaceInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate kinase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform AK2A (identifier: P08166-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform AK2B (identifier: P08166-2) The sequence of this isoform differs from the canonical sequence as follows: 234-241: CKDLVMFI → S |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.5 | ||||||||||||||||||||||||||||||||||||||||
| Chain | 2 – 241 | 240 | Adenylate kinase 2, mitochondrial | PRO_0000158916 | |||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||
| Nucleotide binding | 24 – 32 | 9 | ATP By similarity | ||||||||||||||||||||||||||||||||||||||||
| Nucleotide binding | 47 – 76 | 30 | AMP By similarity | ||||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||||
| Binding site | 48 | 1 | AMP By similarity | ||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 95 | 1 | N6-acetyllysine By similarity | ||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 44 ↔ 94 | Ref.6 | |||||||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 234 – 241 | 8 | CKDLVMFI → S in isoform AK2B. | VSP_002789 | |||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 19 – 23 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 30 – 41 | 12 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 44 – 47 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 48 – 58 | 11 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 61 – 71 | 11 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 78 – 89 | 12 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 92 – 94 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 98 – 102 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 107 – 120 | 14 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 126 – 131 | 6 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 134 – 142 | 9 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 148 – 150 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 153 – 155 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 156 – 158 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 168 – 170 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 182 – 205 | 24 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 209 – 213 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 218 – 232 | 15 | |||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation and characterization of two types of cDNA for mitochondrial adenylate kinase and their expression in Escherichia coli." Kishi F., Tanizawa Y., Nakazawa A. J. Biol. Chem. 262:11785-11789(1987) [PubMed: 3040716] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS AK2A AND AK2B). |
| [2] | "Isolation and characterization of the gene encoding bovine adenylate kinase isozyme 2." Tanaka H., Yamada M., Kishi F., Nakazawa A. Gene 93:221-227(1990) [PubMed: 2227435] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM AK2B). |
| [4] | NIH - Mammalian Gene Collection (MGC) project Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM AK2B). Strain: Hereford. Tissue: Testis. |
| [5] | "Mitochondrial adenylate kinase (AK2) from bovine heart. The complete primary structure." Frank R., Trosin M., Tomasselli A.G., Noda L., Krauth-Siegel R.L., Schirmer R.H. Eur. J. Biochem. 154:205-211(1986) [PubMed: 3002789] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-239. |
| [6] | "The structure of bovine mitochondrial adenylate kinase: comparison with isoenzymes in other compartments." Schlauderer G.J., Schulz G.E. Protein Sci. 5:434-441(1996) [PubMed: 8868479] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS), DISULFIDE BOND. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| M16224 mRNA. Translation: AAA30364.1. M16225 mRNA. Translation: AAA30365.1. D90069 Genomic DNA. Translation: BAA14110.1. D90069 Genomic DNA. Translation: BAA14109.1. BT025476 mRNA. Translation: ABF57432.1. BC112613 mRNA. Translation: AAI12614.1. | |||||||||||||||||||
| IPI | IPI00691138. IPI00714525. | ||||||||||||||||||
| PIR | B29792. JS0422. | ||||||||||||||||||
| RefSeq | NP_776314.1. | ||||||||||||||||||
| UniGene | Bt.946 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENSBTAG00000017605. Bos taurus. [Contig view] | ||||||||||||||||||
| GeneID | 280716. | ||||||||||||||||||
| KEGG | bta:280716. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOVERGEN | P08166. | ||||||||||||||||||
| OMA | P08166. KQTEPIV. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BRENDA | 2.7.4.3. 251. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR006259. Adenyl_kin_sub. IPR000850. Adenylate_kin. IPR007862. Adenylate_kinase_Znf_lid. [Graphical view] | ||||||||||||||||||
| PANTHER | PTHR23359. Adenylate_kin. 1 hit. | ||||||||||||||||||
| Pfam | PF00406. ADK. 1 hit. PF05191. ADK_lid. 1 hit. [Graphical view] | ||||||||||||||||||
| PRINTS | PR00094. ADENYLTKNASE. | ||||||||||||||||||
| ProDom | PD000657. Adenylate_kin. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||||||||
| TIGRFAMs | TIGR01351. adk. 1 hit. | ||||||||||||||||||
| PROSITE | PS00113. ADENYLATE_KINASE. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | KAD2_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P08166 Secondary accession number(s): P08167, Q2KIJ7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


