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Protein

Adenylate kinase 2, mitochondrial

Gene

AK2

Organism
Bos taurus (Bovine)
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 sitei48 – 481AMPUniRule annotation
Binding sitei53 – 531AMPUniRule annotation
Binding sitei109 – 1091AMPUniRule annotation
Binding sitei144 – 1441ATPUniRule annotation
Binding sitei177 – 1771AMPUniRule annotation
Binding sitei188 – 1881AMPUniRule annotation
Binding sitei216 – 2161ATP; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi27 – 326ATPUniRule annotation
Nucleotide bindingi74 – 763AMPUniRule annotation
Nucleotide bindingi102 – 1054AMPUniRule annotation
Nucleotide bindingi153 – 1542ATPUniRule 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-BTA-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
SABIO-RKP08166.

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:
Adenylate kinase 2, mitochondrial, N-terminally processedUniRule annotation
Gene namesi
Name:AK2UniRule annotation
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 241241Adenylate kinase 2, mitochondrialPRO_0000423211Add
BLAST
Initiator methionineiRemoved; alternateUniRule annotation1 Publication
Chaini2 – 241240Adenylate kinase 2, mitochondrial, N-terminally processedPRO_0000158916Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Disulfide bondi44 ↔ 94UniRule annotation1 Publication
Modified residuei64 – 641N6-succinyllysineBy similarity
Modified residuei95 – 951N6-succinyllysineBy similarity
Modified residuei135 – 1351PhosphoserineBy similarity
Modified residuei183 – 1831N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP08166.
PRIDEiP08166.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

IntActiP08166. 1 interaction.
STRINGi9913.ENSBTAP00000023406.

Structurei

Secondary structure

1
241
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 235Combined sources
Helixi30 – 4112Combined sources
Beta strandi44 – 474Combined sources
Helixi48 – 5811Combined sources
Helixi61 – 7111Combined sources
Helixi78 – 8912Combined sources
Helixi92 – 943Combined sources
Beta strandi98 – 1025Combined sources
Helixi107 – 12014Combined sources
Beta strandi126 – 1316Combined sources
Helixi134 – 1429Combined sources
Turni148 – 1503Combined sources
Beta strandi153 – 1553Combined sources
Turni156 – 1583Combined sources
Turni168 – 1703Combined sources
Helixi182 – 20524Combined sources
Beta strandi209 – 2135Combined sources
Helixi218 – 23215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AK2X-ray1.92A2-233[»]
2AK2X-ray2.10A2-233[»]
ProteinModelPortaliP08166.
SMRiP08166. Positions 15-233.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08166.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 7630NMPbindAdd
BLAST
Regioni143 – 18038LIDAdd
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.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3078. Eukaryota.
COG0563. LUCA.
GeneTreeiENSGT00830000128340.
HOGENOMiHOG000238772.
HOVERGENiHBG000458.
InParanoidiP08166.
KOiK00939.
OMAiKEKFSCC.
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 AK2A (identifier: P08166-1) [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
MAPNVPAAEP VPESPKGVRA VLLGPPGAGK GTQAPKLAKN FCVCHLATGD
60 70 80 90 100
MLRAMVASGS ELGKKLKATM DAGKLVSDEM VLELIEKNLE TPPCKNGFLL
110 120 130 140 150
DGFPRTVRQA EMLDDLMEKR KEKLDSVIEF SIPDSLLIRR ITGRLIHPQS
160 170 180 190 200
GRSYHEEFNP PKEPMKDDIT GEPLIRRSDD NKKALKIRLE AYHTQTTPLV
210 220 230 240
EYYSKRGIHS AIDASQTPDV VFASILAAFS KATCKDLVMF I
Length:241
Mass (Da):26,497
Last modified:January 23, 2007 - v2
Checksum:iD9232C61C431F9F4
GO
Isoform AK2B (identifier: P08166-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     234-241: CKDLVMFI → S

Show »
Length:234
Mass (Da):25,634
Checksum:i1FC8BBCA024B7DD6
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei234 – 2418CKDLVMFI → S in isoform AK2B. 3 PublicationsVSP_002789

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16224 mRNA. Translation: AAA30364.1.
M16225 mRNA. Translation: AAA30365.1.
D90069 Genomic DNA. Translation: BAA14110.1.
D90069 Genomic DNA. Translation: BAA14109.1.
BT025476 mRNA. Translation: ABF57432.1.
BC112613 mRNA. Translation: AAI12614.1.
PIRiB29792.
JS0422.
RefSeqiNP_776314.1. NM_173889.1. [P08166-2]
XP_005202939.1. XM_005202882.1. [P08166-1]
UniGeneiBt.946.

Genome annotation databases

EnsembliENSBTAT00000023406; ENSBTAP00000023406; ENSBTAG00000017605. [P08166-2]
GeneIDi280716.
KEGGibta:280716.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16224 mRNA. Translation: AAA30364.1.
M16225 mRNA. Translation: AAA30365.1.
D90069 Genomic DNA. Translation: BAA14110.1.
D90069 Genomic DNA. Translation: BAA14109.1.
BT025476 mRNA. Translation: ABF57432.1.
BC112613 mRNA. Translation: AAI12614.1.
PIRiB29792.
JS0422.
RefSeqiNP_776314.1. NM_173889.1. [P08166-2]
XP_005202939.1. XM_005202882.1. [P08166-1]
UniGeneiBt.946.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AK2X-ray1.92A2-233[»]
2AK2X-ray2.10A2-233[»]
ProteinModelPortaliP08166.
SMRiP08166. Positions 15-233.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP08166. 1 interaction.
STRINGi9913.ENSBTAP00000023406.

Proteomic databases

PaxDbiP08166.
PRIDEiP08166.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000023406; ENSBTAP00000023406; ENSBTAG00000017605. [P08166-2]
GeneIDi280716.
KEGGibta:280716.

Organism-specific databases

CTDi204.

Phylogenomic databases

eggNOGiKOG3078. Eukaryota.
COG0563. LUCA.
GeneTreeiENSGT00830000128340.
HOGENOMiHOG000238772.
HOVERGENiHBG000458.
InParanoidiP08166.
KOiK00939.
OMAiKEKFSCC.
OrthoDBiEOG74TX0R.
TreeFamiTF300896.

Enzyme and pathway databases

ReactomeiR-BTA-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
SABIO-RKP08166.

Miscellaneous databases

EvolutionaryTraceiP08166.
NextBioi20804895.

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. "Isolation and characterization of two types of cDNA for mitochondrial adenylate kinase and their expression in Escherichia coli."
    Kishi F., Tanizawa Y., Nakazawa A.
    J. Biol. Chem. 262:11785-11789(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS AK2A AND AK2B).
  2. "Isolation and characterization of the gene encoding bovine adenylate kinase isozyme 2."
    Tanaka H., Yamada M., Kishi F., Nakazawa A.
    Gene 93:221-227(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM AK2B).
  4. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM AK2B).
    Strain: Hereford.
    Tissue: Testis.
  5. "Mitochondrial adenylate kinase (AK2) from bovine heart. The complete primary structure."
    Frank R., Trosin M., Tomasselli A.G., Noda L., Krauth-Siegel R.L., Schirmer R.H.
    Eur. J. Biochem. 154:205-211(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-239.
  6. "The structure of bovine mitochondrial adenylate kinase: comparison with isoenzymes in other compartments."
    Schlauderer G.J., Schulz G.E.
    Protein Sci. 5:434-441(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS), DISULFIDE BOND.

Entry informationi

Entry nameiKAD2_BOVIN
AccessioniPrimary (citable) accession number: P08166
Secondary accession number(s): P08167, Q2KIJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: February 17, 2016
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.