Q9WTP6 (KAD2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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
ATP:AMP phosphotransferase
Adenylate monophosphate kinase

Gene names

Name:

Ak2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	239 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. 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 By similarity. HAMAP-Rule MF_03168
Catalytic activity	ATP + AMP = 2 ADP. HAMAP-Rule MF_03168
Subunit structure	Monomer By similarity.
Subcellular location	Mitochondrion intermembrane space By similarity HAMAP-Rule MF_03168.
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). Ref.7
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 By similarity. HAMAP-Rule MF_03168
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	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ADP biosynthetic process Inferred from electronic annotation. Source: Compara AMP metabolic process Inferred from electronic annotation. Source: Compara ATP metabolic process Inferred from electronic annotation. Source: Compara brain development Inferred from electronic annotation. Source: Compara dATP metabolic process Inferred from electronic annotation. Source: Compara liver development Inferred from electronic annotation. Source: Compara oxidative phosphorylation Inferred from electronic annotation. Source: Compara response to thyroid hormone stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from electronic annotation. Source: Compara mitochondrial inner membrane Inferred from direct assay PubMed 12865426. Source: MGI mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell sperm mitochondrial sheath Inferred from direct assay PubMed 16790685. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: 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.

Isoform 2 (identifier: Q9WTP6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     232-239: CKDLVMFI → S

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 239	238	Adenylate kinase 2, mitochondrial HAMAP-Rule MF_03168		PRO_0000158918
Regions
	Nucleotide binding	25 – 30	6	ATP By similarity
	Nucleotide binding	72 – 74	3	AMP By similarity
	Nucleotide binding	100 – 103	4	AMP By similarity
	Nucleotide binding	151 – 152	2	ATP By similarity
	Region	45 – 74	30	NMPbind By similarity
	Region	141 – 178	38	LID By similarity
Sites
	Binding site	46	1	AMP By similarity
	Binding site	51	1	AMP By similarity
	Binding site	107	1	AMP By similarity
	Binding site	142	1	ATP By similarity
	Binding site	175	1	AMP By similarity
	Binding site	186	1	AMP By similarity
	Binding site	214	1	ATP; via carbonyl oxygen By similarity
Amino acid modifications
	Modified residue	93	1	N6-acetyllysine Ref.6
	Disulfide bond	42 ↔ 92		By similarity
Natural variations
	Alternative sequence	232 – 239	8	CKDLVMFI → S in isoform 2.		VSP_036504
Experimental info
	Sequence conflict	61	1	G → R in BAA77359. Ref.1
	Sequence conflict	110	1	M → V in BAE40113. Ref.2
	Sequence conflict	113	1	D → E in BAA77359. Ref.1
	Sequence conflict	121	1	K → E in BAA77359. Ref.1
	Sequence conflict	145	1	H → R in BAA77359. Ref.1
	Sequence conflict	146	1	P → R in BAE40113. Ref.2
	Sequence conflict	151	1	S → F in BAA77359. Ref.1
	Sequence conflict	191	1	H → Y in BAA77359. Ref.1
	Sequence conflict	204	1	R → H in BAE40035. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 3, 2009. Version 5. Checksum: CAFF06F053CECE36	FASTA	239	26,469
	10 20 30 40 50 60 MAPNVLASEP EIPKGIRAVL LGPPGAGKGT QAPKLAENFC VCHLATGDML RAMVASGSEL 70 80 90 100 110 120 GKKLKATMDA GKLVSDEMVV ELIEKNLETP SCKNGFLLDG FPRTVRQAEM LDDLMEKRKE 130 140 150 160 170 180 KLDSVIEFSI QDSLLIRRIT GRLIHPKSGR SYHEEFNPPK EPMKDDITGE PLIRRSDDNE 190 200 210 220 230 KALKTRLEAY HTQTTPLVEY YRKRGIHCAI DASQTPDIVF ASILAAFSKA TCKDLVMFI
	Isoform 2 [UniParc]. Checksum: EDD60400562323CF	FASTA	232	25,606
	10 20 30 40 50 60 MAPNVLASEP EIPKGIRAVL LGPPGAGKGT QAPKLAENFC VCHLATGDML RAMVASGSEL 70 80 90 100 110 120 GKKLKATMDA GKLVSDEMVV ELIEKNLETP SCKNGFLLDG FPRTVRQAEM LDDLMEKRKE 130 140 150 160 170 180 KLDSVIEFSI QDSLLIRRIT GRLIHPKSGR SYHEEFNPPK EPMKDDITGE PLIRRSDDNE 190 200 210 220 230 KALKTRLEAY HTQTTPLVEY YRKRGIHCAI DASQTPDIVF ASILAAFSKA TS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Noma T. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: BALB/c and C57BL/6J. Tissue: Embryonic liver and Liver.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]	Lubec G., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 94-103. Tissue: Brain.
[6]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-93, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Human adenylate kinase 2 deficiency causes a profound hematopoietic defect associated with sensorineural deafness." Lagresle-Peyrou C., Six E.M., Picard C., Rieux-Laucat F., Michel V., Ditadi A., Chappedelaine C.D., Morillon E., Valensi F., Simon-Stoos K.L., Mullikin J.C., Noroski L.M., Besse C., Wulffraat N.M., Ferster A., Abecasis M.M., Calvo F., Petit C. , Candotti F., Abel L., Fischer A., Cavazzana-Calvo M. Nat. Genet. 41:106-111(2009) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB020202 mRNA. Translation: BAA77359.1. AK010951 mRNA. Translation: BAB27286.1. AK050133 mRNA. Translation: BAC34085.1. AK166976 mRNA. Translation: BAE39159.1. AK168056 mRNA. Translation: BAE40035.1. AK168148 mRNA. Translation: BAE40113.1. AL607086 Genomic DNA. Translation: CAM19113.1. AL607086 Genomic DNA. Translation: CAM19114.1. CU210866 Genomic DNA. Translation: CAQ51906.1. CU210866 Genomic DNA. Translation: CAQ51907.1. BC008610 mRNA. Translation: AAH08610.1.
IPI	IPI00269076. IPI00648318.
RefSeq	NP_001029138.1. NM_001033966.4. NP_058591.2. NM_016895.4.
UniGene	Mm.29460.
3D structure databases
ProteinModelPortal	Q9WTP6.
SMR	Q9WTP6. Positions 15-232.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000030583.
PTM databases
PhosphoSite	Q9WTP6.
2D gel databases
REPRODUCTION-2DPAGE	Q9WTP6.
Proteomic databases
PaxDb	Q9WTP6.
PRIDE	Q9WTP6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030583; ENSMUSP00000030583; ENSMUSG00000028792. ENSMUST00000102604; ENSMUSP00000099664; ENSMUSG00000028792.
GeneID	11637.
KEGG	mmu:11637.
UCSC	uc008uvt.1. mouse. uc008uvu.1. mouse.
Organism-specific databases
CTD	204.
MGI	MGI:87978. Ak2.
Phylogenomic databases
eggNOG	COG0563.
GeneTree	ENSGT00700000104498.
HOVERGEN	HBG000458.
InParanoid	Q8C7I9.
KO	K00939.
OMA	QADAMKD.
Gene expression databases
ArrayExpress	Q9WTP6.
Bgee	Q9WTP6.
CleanEx	MM_AK2.
Genevestigator	Q9WTP6.
GermOnline	ENSMUSG00000028792. Mus musculus.
Family and domain databases
HAMAP	MF_00235. Adenylate_kinase_Adk. MF_03168. Adenylate_kinase_AK2.
InterPro	IPR006259. Adenyl_kin_sub. IPR000850. Adenylate_kin. IPR007862. Adenylate_kinase_lid-dom. [Graphical view]
PANTHER	PTHR23359. PTHR23359. 1 hit.
Pfam	PF00406. ADK. 1 hit. PF05191. ADK_lid. 1 hit. [Graphical view]
PRINTS	PR00094. ADENYLTKNASE.
TIGRFAMs	TIGR01351. adk. 1 hit.
PROSITE	PS00113. ADENYLATE_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	AK2. mouse.
NextBio	279209.
SOURCE	Search...

Entry information

Entry name

KAD2_MOUSE

Accession

Primary (citable) accession number: Q9WTP6
Secondary accession number(s): A2A820 , Q3THT3, Q3TI11, Q3TKI6, Q8C7I9, Q9CY37

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	March 3, 2009
Last modified:	May 1, 2013
This is version 115 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program