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

Gene names

Name:

Ak2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › 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. 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 By similarity.
Subcellular location	Mitochondrion intermembrane space By similarity.
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
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)
Cellular component	mitochondrial inner membrane Inferred from direct assay. Source: MGI mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell
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		PRO_0000158918
Regions
	Nucleotide binding	22 – 30	9	ATP By similarity
	Nucleotide binding	45 – 74	30	AMP By similarity
Sites
	Binding site	46	1	AMP By similarity
Amino acid modifications
	Modified residue	14	1	N6-acetyllysine By similarity
	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: 16141072] [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: 19468303] [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: 15489334] [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: 16916647] [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: 19043416] [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_001033966.3. NP_058591.2. NM_016895.3.
UniGene	Mm.29460.
3D structure databases
ProteinModelPortal	Q9WTP6.
SMR	Q9WTP6. Positions 15-232.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9WTP6.
PTM databases
PhosphoSite	Q9WTP6.
2D gel databases
REPRODUCTION-2DPAGE	Q9WTP6.
Proteomic databases
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	roNOG14848.
GeneTree	ENSGT00600000084421.
HOVERGEN	HBG000458.
OMA	HEEFHPP.
PhylomeDB	Q9WTP6.
Gene expression databases
ArrayExpress	Q9WTP6.
Bgee	Q9WTP6.
CleanEx	MM_AK2.
Genevestigator	Q9WTP6.
GermOnline	ENSMUSG00000028792. Mus musculus.
Family and domain databases
InterPro	IPR006259. Adenyl_kin_sub. IPR000850. Adenylate_kin. IPR007862. Adenylate_kinase_lid-dom. [Graphical view]
KO	K00939.
PANTHER	PTHR23359. Adenylate_kin. 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
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:	November 16, 2011
This is version 104 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program