AK2

Mammalian protein found in Homo sapiens

AK2

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
2C9Y

Identifiers

Aliases

AK2, ADK2, AK 2, adenylate kinase 2

External IDs

OMIM: 103020; MGI: 87978; HomoloGene: 1227; GeneCards: AK2; OMA:AK2 - orthologs

EC number

2.7.4.3

Gene location (Human)

Chr.	Chromosome 1 (human)^[1]

Band	1p35.1	Start	33,007,986 bp^[1]
Band	1p35.1	End	33,080,996 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 4 (mouse)^[2]

Band	4 D2.2\|4 62.62 cM	Start	128,885,751 bp^[2]
Band	4 D2.2\|4 62.62 cM	End	128,905,322 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

rectum

mucosa of transverse colon

epithelium of colon

gastrocnemius muscle

right auricle

left lobe of thyroid gland

right lobe of thyroid gland

right lobe of liver

apex of heart

left adrenal cortex

Top expressed in

right kidney

jejunum

brown adipose tissue

duodenum

crypt of lieberkuhn of small intestine

proximal tubule

left lobe of liver

granulocyte

primary oocyte

white adipose tissue

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	transferase activity nucleotide binding phosphotransferase activity, phosphate group as acceptor kinase activity nucleobase-containing compound kinase activity ATP binding adenylate kinase activity
Cellular component	sperm mitochondrial sheath mitochondrial intermembrane space sperm flagellum mitochondrion mitochondrial inner membrane extracellular exosome
Biological process	nucleobase-containing small molecule interconversion phosphorylation nucleobase-containing compound metabolic process ADP biosynthetic process nucleotide phosphorylation AMP metabolic process ATP metabolic process nucleoside monophosphate phosphorylation
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


204


11637

Ensembl


ENSG00000004455


ENSMUSG00000028792

UniProt


P54819


Q9WTP6

RefSeq (mRNA)

NM_001199199 NM_001625 NM_013411 NM_001319139 NM_001319140
NM_001319141 NM_001319142 NM_001319143 NM_172199


NM_001033966 NM_016895

RefSeq (protein)

NP_001186128 NP_001306068 NP_001306069 NP_001306070 NP_001306071
NP_001306072 NP_001616 NP_037543


NP_001029138 NP_058591

Location (UCSC)

Chr 1: 33.01 – 33.08 Mb

Chr 4: 128.89 – 128.91 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Adenylate kinase 2 is an enzyme that is encoded in humans by the AK2 gene.^[5]^[6]^[7] The AK2 protein is found in the intermembrane space of the mitochondrion.^[8]^[9]

Function

Adenylate kinases are involved in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate groups among adenine nucleotides. Three isozymes of adenylate kinase, namely 1, 2, and 3, have been identified in vertebrates; this gene encodes isozyme 2. Expression of these isozymes is tissue-specific and developmentally regulated. Isozyme 2 is localized in the mitochondrial intermembrane space and may play a role in apoptosis. Two transcript variants encoding distinct isoforms have been identified for this gene.^[7]

AK2 deficiency

Adenylate Kinase 2 (AK2) deficiency in humans causes hematopoietic defects associated with sensorineural deafness.^[10]^[11] Reticular dysgenesis is an autosomal recessive form of human combined immunodeficiency. It is also characterized by an impaired lymphoid maturation and early differentiation arrest in the myeloid lineage. AK2 deficiency results in absent or a large decrease in the expression of proteins. AK2 is specifically expressed in the stria vascularis of the inner ear which indicates why individuals with an AK2 deficiency will have sensorineural deafness.^[11]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000004455 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028792 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Lee Y, Kim JW, Lee IA, Kang HB, Choe YK, Lee HG, Lim JS, Kim HJ, Park C, Choe IS (Feb 1997). "Cloning and characterization of cDNA for human adenylate kinase 2A". Biochem Mol Biol Int. 39 (4): 833–42. doi:10.1080/15216549600201931. PMID 8843353. S2CID 20344485.
^ Carritt B, King J, Welch HM (Mar 1983). "Gene order and localization of enzyme loci on the short arm of chromosome 1". Ann Hum Genet. 46 (Pt 4): 329–35. doi:10.1111/j.1469-1809.1982.tb01583.x. PMID 6961883. S2CID 30856048.
^ ^a ^b "Entrez Gene: AK2 adenylate kinase 2".
^ Bruns GA, Regina VM (1977). "Adenylate kinase 2, a mitochondrial enzyme". Biochem. Genet. 15 (5–6): 477–86. doi:10.1007/BF00520192. PMID 195572. S2CID 21214450.
^ Köhler C, Gahm A, Noma T, et al. (1999). "Release of adenylate kinase 2 from the mitochondrial intermembrane space during apoptosis". FEBS Lett. 447 (1): 10–2. doi:10.1016/S0014-5793(99)00251-3. PMID 10218571. S2CID 21280401.
^ Pannicke U, Hönig M, Hess I, et al. (January 2009). "Reticular dysgenesis (aleukocytosis) is caused by mutations in the gene encoding mitochondrial adenylate kinase 2". Nat. Genet. 41 (1): 101–105. doi:10.1038/ng.265. PMID 19043417. S2CID 205347130.
^ ^a ^b Lagresle-Peyrou C, Six EM, Picard C, et al. (January 2009). "Human adenylate kinase 2 deficiency causes a profound haematopoietic defect associated with sensorineural deafness". Nat. Genet. 41 (1): 106–11. doi:10.1038/ng.278. PMC 2612090. PMID 19043416.

External links

Human AK2 genome location and AK2 gene details page in the UCSC Genome Browser.

Lee Y, Kim JW, Lee SM, et al. (1998). "Cloning and expression of human adenylate kinase 2 isozymes: differential expression of adenylate kinase 1 and 2 in human muscle tissues". J. Biochem. 123 (1): 47–54. doi:10.1093/oxfordjournals.jbchem.a021915. PMID 9504408.
Noma T, Song S, Yoon YS, et al. (1998). "cDNA cloning and tissue-specific expression of the gene encoding human adenylate kinase isozyme 2". Biochim. Biophys. Acta. 1395 (1): 34–9. doi:10.1016/s0167-4781(97)00193-0. PMID 9434148.
Hamada M, Sumida M, Okuda H, et al. (1982). "Adenosine triphosphate-adenosine-5'-monophosphate phosphotransferase from normal human liver mitochondria. Isolation, chemical properties, and immunochemical comparison with Duchenne dystrophic serum aberrant adenylate kinase". J. Biol. Chem. 257 (21): 13120–8. doi:10.1016/S0021-9258(18)33631-7. PMID 6182143.

PDB gallery

1ak2: ADENYLATE KINASE ISOENZYME-2
2ak2: ADENYLATE KINASE ISOENZYME-2
2c9y: STRUCTURE OF HUMAN ADENYLATE KINASE 2

Transferases: phosphorus-containing groups (EC 2.7)

2.7.1-2.7.4:
phosphotransferase/kinase
(PO₄)

2.7.1: OH acceptor	Hexo- Gluco- Fructo- Hepatic Galacto- Phosphofructo- 1 Liver Muscle Platelet 2 Riboflavin Shikimate Thymidine ADP-thymidine NAD⁺ Glycerol Pantothenate Mevalonate Pyruvate Deoxycytidine PFP Diacylglycerol Phosphoinositide 3 Class I PI 3 Class II PI 3 Sphingosine Glucose-1,6-bisphosphate synthase
2.7.2: COOH acceptor	Phosphoglycerate Aspartate kinase
2.7.3: N acceptor	Creatine
2.7.4: PO₄ acceptor	Phosphomevalonate Adenylate Nucleoside-diphosphate Uridylate Guanylate Thiamine-diphosphate

2.7.6: diphosphotransferase
(P₂O₇)

2.7.7: nucleotidyltransferase
(PO₄-nucleoside)

Polymerase

DNA polymerase	DNA-directed DNA polymerase I/A γ θ ν T7 Taq II/B α δ ε ζ Pfu III/C IV/X β λ μ TDT V/Y η ι κ RNA-directed DNA polymerase Reverse transcriptase Telomerase
RNA polymerase	Template-directed RNA polymerase I II III IV V ssRNAP POLRMT Primase 1 2 PrimPol RNA-dependent RNA polymerase Polyadenylation PAP PNPase

Phosphorolytic
3' to 5' exoribonuclease

Nucleotidyltransferase

Guanylyltransferase

mRNA capping enzyme

Other

2.7.8: miscellaneous

Phosphatidyltransferases	CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase CDP-diacylglycerol—serine O-phosphatidyltransferase CDP-diacylglycerol—inositol 3-phosphatidyltransferase CDP-diacylglycerol—choline O-phosphatidyltransferase
Glycosyl-1-phosphotransferase	N-acetylglucosamine-1-phosphate transferase

2.7.10-2.7.13: protein kinase
(PO₄; protein acceptor)

2.7.10: protein-tyrosine	see tyrosine kinases
2.7.11: protein-serine/threonine	see serine/threonine-specific protein kinases
2.7.12: protein-dual-specificity	see serine/threonine-specific protein kinases
2.7.13: protein-histidine	Protein-histidine pros-kinase Protein-histidine tele-kinase Histidine kinase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)