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Protein

Adenylate kinase 2, mitochondrial

Gene

Ak2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei46 – 461AMPUniRule annotation
Binding sitei51 – 511AMPUniRule annotation
Binding sitei107 – 1071AMPUniRule annotation
Binding sitei142 – 1421ATPUniRule annotation
Binding sitei175 – 1751AMPUniRule annotation
Binding sitei186 – 1861AMPUniRule annotation
Binding sitei214 – 2141ATP; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi25 – 306ATPUniRule annotation
Nucleotide bindingi72 – 743AMPUniRule annotation
Nucleotide bindingi100 – 1034AMPUniRule annotation
Nucleotide bindingi151 – 1522ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate kinase 2, mitochondrialUniRule annotation (EC:2.7.4.3UniRule annotation)
Short name:
AK 2UniRule annotation
Alternative name(s):
ATP-AMP transphosphorylase 2UniRule annotation
ATP:AMP phosphotransferaseUniRule annotation
Adenylate monophosphate kinaseUniRule annotation
Cleaved into the following chain:
Gene namesi
Name:Ak2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:87978. Ak2.

Subcellular locationi

  • Mitochondrion intermembrane space UniRule annotation

GO - Cellular componenti

  • cytosol Source: Ensembl
  • extracellular exosome Source: MGI
  • mitochondrial inner membrane Source: MGI
  • mitochondrial intermembrane space Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
  • sperm flagellum Source: MGI
  • sperm mitochondrial sheath Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 239239Adenylate kinase 2, mitochondrialPRO_0000158918Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 239238Adenylate kinase 2, mitochondrial, N-terminally processedPRO_0000434353Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Disulfide bondi42 ↔ 92UniRule annotation
Modified residuei62 – 621N6-succinyllysineCombined sources
Modified residuei91 – 911PhosphoserineCombined sources
Modified residuei93 – 931N6-succinyllysineCombined sources
Modified residuei133 – 1331PhosphoserineBy similarity
Modified residuei181 – 1811N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiQ9WTP6.
MaxQBiQ9WTP6.
PaxDbiQ9WTP6.
PRIDEiQ9WTP6.

2D gel databases

REPRODUCTION-2DPAGEQ9WTP6.

PTM databases

iPTMnetiQ9WTP6.
PhosphoSiteiQ9WTP6.
SwissPalmiQ9WTP6.

Expressioni

Tissue specificityi

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).1 Publication

Gene expression databases

BgeeiQ9WTP6.
CleanExiMM_AK2.
ExpressionAtlasiQ9WTP6. baseline and differential.
GenevisibleiQ9WTP6. MM.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi198046. 1 interaction.
IntActiQ9WTP6. 4 interactions.
MINTiMINT-1859211.
STRINGi10090.ENSMUSP00000030583.

Structurei

3D structure databases

ProteinModelPortaliQ9WTP6.
SMRiQ9WTP6. Positions 15-232.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 7430NMPbindUniRule annotationAdd
BLAST
Regioni141 – 17838LIDUniRule annotationAdd
BLAST

Domaini

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.UniRule annotation

Sequence similaritiesi

Belongs to the adenylate kinase family. AK2 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG3078. Eukaryota.
COG0563. LUCA.
GeneTreeiENSGT00830000128340.
HOVERGENiHBG000458.
InParanoidiQ9WTP6.
KOiK00939.
OMAiKRPAQIQ.
OrthoDBiEOG74TX0R.
TreeFamiTF300896.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03168. Adenylate_kinase_AK2.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR028587. AK2.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PfamiPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01351. adk. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9WTP6-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAPNVLASEP EIPKGIRAVL LGPPGAGKGT QAPKLAENFC VCHLATGDML
60 70 80 90 100
RAMVASGSEL GKKLKATMDA GKLVSDEMVV ELIEKNLETP SCKNGFLLDG
110 120 130 140 150
FPRTVRQAEM LDDLMEKRKE KLDSVIEFSI QDSLLIRRIT GRLIHPKSGR
160 170 180 190 200
SYHEEFNPPK EPMKDDITGE PLIRRSDDNE KALKTRLEAY HTQTTPLVEY
210 220 230
YRKRGIHCAI DASQTPDIVF ASILAAFSKA TCKDLVMFI
Length:239
Mass (Da):26,469
Last modified:March 3, 2009 - v5
Checksum:iCAFF06F053CECE36
GO
Isoform 2 (identifier: Q9WTP6-2) [UniParc]FASTAAdd to basket

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

Show »
Length:232
Mass (Da):25,606
Checksum:iEDD60400562323CF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611G → R in BAA77359 (Ref. 1) Curated
Sequence conflicti110 – 1101M → V in BAE40113 (PubMed:16141072).Curated
Sequence conflicti113 – 1131D → E in BAA77359 (Ref. 1) Curated
Sequence conflicti121 – 1211K → E in BAA77359 (Ref. 1) Curated
Sequence conflicti145 – 1451H → R in BAA77359 (Ref. 1) Curated
Sequence conflicti146 – 1461P → R in BAE40113 (PubMed:16141072).Curated
Sequence conflicti151 – 1511S → F in BAA77359 (Ref. 1) Curated
Sequence conflicti191 – 1911H → Y in BAA77359 (Ref. 1) Curated
Sequence conflicti204 – 2041R → H in BAE40035 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei232 – 2398CKDLVMFI → S in isoform 2. 3 PublicationsVSP_036504

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18679.1. [Q9WTP6-2]
CCDS18680.1. [Q9WTP6-1]
RefSeqiNP_001029138.1. NM_001033966.4. [Q9WTP6-1]
NP_058591.2. NM_016895.4. [Q9WTP6-2]
UniGeneiMm.29460.

Genome annotation databases

EnsembliENSMUST00000030583; ENSMUSP00000030583; ENSMUSG00000028792. [Q9WTP6-1]
ENSMUST00000102604; ENSMUSP00000099664; ENSMUSG00000028792. [Q9WTP6-2]
GeneIDi11637.
KEGGimmu:11637.
UCSCiuc008uvt.2. mouse. [Q9WTP6-1]
uc008uvu.2. mouse. [Q9WTP6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18679.1. [Q9WTP6-2]
CCDS18680.1. [Q9WTP6-1]
RefSeqiNP_001029138.1. NM_001033966.4. [Q9WTP6-1]
NP_058591.2. NM_016895.4. [Q9WTP6-2]
UniGeneiMm.29460.

3D structure databases

ProteinModelPortaliQ9WTP6.
SMRiQ9WTP6. Positions 15-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198046. 1 interaction.
IntActiQ9WTP6. 4 interactions.
MINTiMINT-1859211.
STRINGi10090.ENSMUSP00000030583.

PTM databases

iPTMnetiQ9WTP6.
PhosphoSiteiQ9WTP6.
SwissPalmiQ9WTP6.

2D gel databases

REPRODUCTION-2DPAGEQ9WTP6.

Proteomic databases

EPDiQ9WTP6.
MaxQBiQ9WTP6.
PaxDbiQ9WTP6.
PRIDEiQ9WTP6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030583; ENSMUSP00000030583; ENSMUSG00000028792. [Q9WTP6-1]
ENSMUST00000102604; ENSMUSP00000099664; ENSMUSG00000028792. [Q9WTP6-2]
GeneIDi11637.
KEGGimmu:11637.
UCSCiuc008uvt.2. mouse. [Q9WTP6-1]
uc008uvu.2. mouse. [Q9WTP6-2]

Organism-specific databases

CTDi204.
MGIiMGI:87978. Ak2.

Phylogenomic databases

eggNOGiKOG3078. Eukaryota.
COG0563. LUCA.
GeneTreeiENSGT00830000128340.
HOVERGENiHBG000458.
InParanoidiQ9WTP6.
KOiK00939.
OMAiKRPAQIQ.
OrthoDBiEOG74TX0R.
TreeFamiTF300896.

Enzyme and pathway databases

ReactomeiR-MMU-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

ChiTaRSiAk2. mouse.
PROiQ9WTP6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WTP6.
CleanExiMM_AK2.
ExpressionAtlasiQ9WTP6. baseline and differential.
GenevisibleiQ9WTP6. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03168. Adenylate_kinase_AK2.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR028587. AK2.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PfamiPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01351. adk. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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/cJ and C57BL/6J.
    Tissue: Embryonic liver and Liver.
  3. 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. Cited for: TISSUE SPECIFICITY.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-62 AND LYS-93, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiKAD2_MOUSE
AccessioniPrimary (citable) accession number: Q9WTP6
Secondary accession number(s): A2A820
, Q3THT3, Q3TI11, Q3TKI6, Q8C7I9, Q9CY37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: March 3, 2009
Last modified: June 8, 2016
This is version 144 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.