A0A140VK93 · A0A140VK93_HUMAN

  • Protein
    Adenylate kinase 2, mitochondrial
  • Gene
    AK2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

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

Features

Showing features for binding site.

123920406080100120140160180200220
TypeIDPosition(s)Description
Binding site25-30ATP (UniProtKB | ChEBI)
Binding site46AMP (UniProtKB | ChEBI)
Binding site51AMP (UniProtKB | ChEBI)
Binding site72-74AMP (UniProtKB | ChEBI)
Binding site100-103AMP (UniProtKB | ChEBI)
Binding site107AMP (UniProtKB | ChEBI)
Binding site142ATP (UniProtKB | ChEBI)
Binding site151-152ATP (UniProtKB | ChEBI)
Binding site175AMP (UniProtKB | ChEBI)
Binding site186AMP (UniProtKB | ChEBI)
Binding site214ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrial intermembrane space
Cellular Componentsperm mitochondrial sheath
Molecular Functionadenylate kinase activity
Molecular FunctionATP binding
Biological ProcessADP biosynthetic process
Biological ProcessAMP metabolic process
Biological ProcessATP metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adenylate kinase 2, mitochondrial
  • EC number
  • Short names
    AK 2
  • Alternative names
    • ATP-AMP transphosphorylase 2
    • ATP:AMP phosphotransferase
    • Adenylate monophosphate kinase

Gene names

    • Name
      AK2

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    A0A140VK93

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Organism-specific databases

PTM/Processing

Features

Showing features for initiator methionine, disulfide bond.

TypeIDPosition(s)Description
Initiator methionine1Removed
Disulfide bond42↔92

Keywords

Expression

Gene expression databases

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region45-74NMPbind
Region141-178LID
Domain142-177Adenylate kinase active site lid
Region150-169Disordered

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

  • Sequence status
    Complete
  • Length
    239
  • Mass (Da)
    26,478
  • Last updated
    2016-06-08 v1
  • Checksum
    86FA94F9EE33629F
MAPSVPAAEPEYPKGIRAVLLGPPGAGKGTQAPRLAENFCVCHLATGDMLRAMVASGSELGKKLKATMDAGKLVSDEMVVELIEKNLETPLCKNGFLLDGFPRTVRQAEMLDDLMEKRKEKLDSVIEFSIPDSLLIRRITGRLIHPKSGRSYHEEFNPPKEPMKDDITGEPLIRRSDDNEKALKIRLQAYHTQTTPLIEYYRKRGIHSAIDASQTPDVVFASILAAFSKATCKDLVMFI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HM005633
EMBL· GenBank· DDBJ
AEE61230.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp