Q9WTP6 · KAD2_MOUSE
- ProteinAdenylate kinase 2, mitochondrial
- GeneAk2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids239 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis.
Catalytic activity
- AMP + ATP = 2 ADP
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 25-30 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GAGKGT | ||||||
Binding site | 46 | AMP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 51 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 72-74 | AMP (UniProtKB | ChEBI) | ||||
Sequence: KLV | ||||||
Binding site | 100-103 | AMP (UniProtKB | ChEBI) | ||||
Sequence: GFPR | ||||||
Binding site | 107 | AMP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 142 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 151-152 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SY | ||||||
Binding site | 175 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 186 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 214 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrial intermembrane space | |
Cellular Component | mitochondrion | |
Cellular Component | sperm flagellum | |
Cellular Component | sperm mitochondrial sheath | |
Molecular Function | adenylate kinase activity | |
Molecular Function | ATP binding | |
Biological Process | ADP biosynthetic process | |
Biological Process | AMP metabolic process | |
Biological Process | ATP metabolic process | |
Biological Process | dATP metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenylate kinase 2, mitochondrial
- EC number
- Short namesAK 2
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9WTP6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for modified residue, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000158918 | 1-239 | Adenylate kinase 2, mitochondrial | |||
Sequence: MAPNVLASEPEIPKGIRAVLLGPPGAGKGTQAPKLAENFCVCHLATGDMLRAMVASGSELGKKLKATMDAGKLVSDEMVVELIEKNLETPSCKNGFLLDGFPRTVRQAEMLDDLMEKRKEKLDSVIEFSIQDSLLIRRITGRLIHPKSGRSYHEEFNPPKEPMKDDITGEPLIRRSDDNEKALKTRLEAYHTQTTPLVEYYRKRGIHCAIDASQTPDIVFASILAAFSKATCKDLVMFI | ||||||
Disulfide bond | 42↔92 | |||||
Sequence: CHLATGDMLRAMVASGSELGKKLKATMDAGKLVSDEMVVELIEKNLETPSC | ||||||
Modified residue | 58 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 62 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 91 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 93 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 133 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 181 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 195 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Present in the inner ear. Not detected in the vestibule at any developmental stage. Present at high level in the cochlea uniquely in the stria vascularis at postnatal day 7 but not at birth. Present within the lumen of the stria vascularis capillaries. Not detected in the capillaries or vessels of the adjacent connective tissue (at protein level).
Gene expression databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 45-74 | NMP | ||||
Sequence: ATGDMLRAMVASGSELGKKLKATMDAGKLV | ||||||
Region | 141-178 | LID | ||||
Sequence: GRLIHPKSGRSYHEEFNPPKEPMKDDITGEPLIRRSDD |
Domain
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Sequence similarities
Belongs to the adenylate kinase family. AK2 subfamily.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9WTP6-1
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.
- Name1
- Length239
- Mass (Da)26,469
- Last updated2009-03-03 v5
- ChecksumCAFF06F053CECE36
Q9WTP6-2
- Name2
- Differences from canonical
- 232-239: CKDLVMFI → S
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F7BP55 | F7BP55_MOUSE | Ak2 | 72 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 61 | in Ref. 1; BAA77359 | ||||
Sequence: G → R | ||||||
Sequence conflict | 110 | in Ref. 2; BAE40113 | ||||
Sequence: M → V | ||||||
Sequence conflict | 113 | in Ref. 1; BAA77359 | ||||
Sequence: D → E | ||||||
Sequence conflict | 121 | in Ref. 1; BAA77359 | ||||
Sequence: K → E | ||||||
Sequence conflict | 145 | in Ref. 1; BAA77359 | ||||
Sequence: H → R | ||||||
Sequence conflict | 146 | in Ref. 2; BAE40113 | ||||
Sequence: P → R | ||||||
Sequence conflict | 151 | in Ref. 1; BAA77359 | ||||
Sequence: S → F | ||||||
Sequence conflict | 191 | in Ref. 1; BAA77359 | ||||
Sequence: H → Y | ||||||
Sequence conflict | 204 | in Ref. 2; BAE40035 | ||||
Sequence: R → H | ||||||
Alternative sequence | VSP_036504 | 232-239 | in isoform 2 | |||
Sequence: CKDLVMFI → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB020202 EMBL· GenBank· DDBJ | BAA77359.1 EMBL· GenBank· DDBJ | mRNA | ||
AK010951 EMBL· GenBank· DDBJ | BAB27286.1 EMBL· GenBank· DDBJ | mRNA | ||
AK050133 EMBL· GenBank· DDBJ | BAC34085.1 EMBL· GenBank· DDBJ | mRNA | ||
AK166976 EMBL· GenBank· DDBJ | BAE39159.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168056 EMBL· GenBank· DDBJ | BAE40035.1 EMBL· GenBank· DDBJ | mRNA | ||
AK168148 EMBL· GenBank· DDBJ | BAE40113.1 EMBL· GenBank· DDBJ | mRNA | ||
AL607086 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CU210866 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC008610 EMBL· GenBank· DDBJ | AAH08610.1 EMBL· GenBank· DDBJ | mRNA |