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Protein

Adenylate kinase 2, mitochondrial

Gene

Ak2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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)DescriptionActionsGraphical viewLength
Binding sitei46AMPUniRule annotation1
Binding sitei51AMPUniRule annotation1
Binding sitei107AMPUniRule annotation1
Binding sitei142ATPUniRule annotation1
Binding sitei175AMPUniRule annotation1
Binding sitei186AMPUniRule annotation1
Binding sitei214ATP; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi25 – 30ATPUniRule annotation6
Nucleotide bindingi72 – 74AMPUniRule annotation3
Nucleotide bindingi100 – 103AMPUniRule annotation4
Nucleotide bindingi151 – 152ATPUniRule annotation2

GO - Molecular functioni

  • adenylate kinase activity Source: RGD
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

  • adenine metabolic process Source: RGD
  • ADP biosynthetic process Source: RGD
  • AMP metabolic process Source: RGD
  • ATP metabolic process Source: RGD
  • brain development Source: RGD
  • dATP metabolic process Source: RGD
  • liver development Source: RGD
  • oxidative phosphorylation Source: RGD
  • response to thyroid hormone Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2077. Ak2.

Subcellular locationi

  • Mitochondrion intermembrane space UniRule annotation

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • mitochondrial intermembrane space Source: RGD
  • mitochondrion Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2376.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001589201 – 239Adenylate kinase 2, mitochondrialAdd BLAST239
Initiator methionineiRemoved; alternateBy similarity
ChainiPRO_00004232152 – 239Adenylate kinase 2, mitochondrial, N-terminally processedAdd BLAST238

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Disulfide bondi42 ↔ 92UniRule annotation
Modified residuei58PhosphoserineBy similarity1
Modified residuei62N6-succinyllysineBy similarity1
Modified residuei91PhosphoserineBy similarity1
Modified residuei93N6-succinyllysineBy similarity1
Modified residuei133PhosphoserineBy similarity1
Modified residuei181N6-acetyllysineBy similarity1
Modified residuei195PhosphothreonineBy similarity1

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP29410.
PRIDEiP29410.

PTM databases

iPTMnetiP29410.
PhosphoSitePlusiP29410.

Expressioni

Gene expression databases

BgeeiENSRNOG00000000122.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000134.

Chemistry databases

BindingDBiP29410.

Structurei

3D structure databases

ProteinModelPortaliP29410.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni45 – 74NMPbindUniRule annotationAdd BLAST30
Regioni141 – 178LIDUniRule annotationAdd BLAST38

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.
HOGENOMiHOG000238772.
HOVERGENiHBG000458.
InParanoidiP29410.
KOiK00939.
PhylomeDBiP29410.
TreeFamiTF300896.

Family and domain databases

CDDicd01428. ADK. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk. 1 hit.
MF_03168. Adenylate_kinase_AK2. 1 hit.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR033690. Adenylat_kinase_CS.
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: P29410-1) [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
MAPNALAPEP EHPEGIRAVL LGPPGAGKGT QAPKLAENFC VCHLATGDML
60 70 80 90 100
RAMVASGSEL GKKLKATMDA GKLVSDEMVV ELIEKNLETP SCKNGFLLDG
110 120 130 140 150
FPRTVKQAEM LDDLMDKRKE KLDSVIEFSI QDSLLIRRIT GRLIHPKSGR
160 170 180 190 200
SYHEEFNPPK EAMKDDITGE PLIRRSDDNE KALKTRLEAY HTQTTPLVEY
210 220 230
YRKRGIHCAI DASQTPDVVF ASILAAFSKA TCKDLVMFV
Length:239
Mass (Da):26,379
Last modified:January 23, 2007 - v2
Checksum:i075A4ACBD581DB8C
GO
Isoform 2 (identifier: P29410-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:232
Mass (Da):25,530
Checksum:i07537364EC6EEFA4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14E → K in AAH61727 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_036505232 – 239CKDLVMFV → S in isoform 2. 1 Publication8

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13061 mRNA. Translation: BAA02378.1.
BC061727 mRNA. Translation: AAH61727.1.
PIRiJQ1944.
RefSeqiNP_001029139.1. NM_001033967.2.
UniGeneiRn.3421.

Genome annotation databases

GeneIDi24184.
KEGGirno:24184.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13061 mRNA. Translation: BAA02378.1.
BC061727 mRNA. Translation: AAH61727.1.
PIRiJQ1944.
RefSeqiNP_001029139.1. NM_001033967.2.
UniGeneiRn.3421.

3D structure databases

ProteinModelPortaliP29410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000134.

Chemistry databases

BindingDBiP29410.
ChEMBLiCHEMBL2376.

PTM databases

iPTMnetiP29410.
PhosphoSitePlusiP29410.

Proteomic databases

PaxDbiP29410.
PRIDEiP29410.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24184.
KEGGirno:24184.

Organism-specific databases

CTDi204.
RGDi2077. Ak2.

Phylogenomic databases

eggNOGiKOG3078. Eukaryota.
COG0563. LUCA.
HOGENOMiHOG000238772.
HOVERGENiHBG000458.
InParanoidiP29410.
KOiK00939.
PhylomeDBiP29410.
TreeFamiTF300896.

Miscellaneous databases

PROiP29410.

Gene expression databases

BgeeiENSRNOG00000000122.

Family and domain databases

CDDicd01428. ADK. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk. 1 hit.
MF_03168. Adenylate_kinase_AK2. 1 hit.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR033690. Adenylat_kinase_CS.
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...

Entry informationi

Entry nameiKAD2_RAT
AccessioniPrimary (citable) accession number: P29410
Secondary accession number(s): Q6P7C6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 140 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

Complete proteome, Reference proteome

Documents

  1. 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.