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Protein

Adenylate kinase 4, mitochondrial

Gene

Ak4

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

Functioni

Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Efficiently phosphorylates AMP and dAMP using ATP as phosphate donor, but phosphorylates only AMP when using GTP as phosphate donor. Also displays broad nucleoside diphosphate kinase activity.UniRule annotation

Catalytic activityi

NTP + AMP = NDP + ADP.UniRule annotation
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361AMPUniRule annotation
Binding sitei41 – 411AMPUniRule annotation
Binding sitei96 – 961AMPUniRule annotation
Binding sitei126 – 1261NTPUniRule annotation
Binding sitei170 – 1701AMPUniRule annotation
Binding sitei199 – 1991NTP; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 206NTPUniRule annotation
Nucleotide bindingi62 – 643AMPUniRule annotation
Nucleotide bindingi89 – 924AMPUniRule annotation
Nucleotide bindingi135 – 1362NTPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, GTP-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 4, mitochondrialUniRule annotation (EC:2.7.4.10UniRule annotation, EC:2.7.4.6UniRule annotation)
Short name:
AK 4UniRule annotation
Alternative name(s):
Adenylate kinase 3-likeUniRule annotation
Adenylate kinase isoenzyme 4
GTP:AMP phosphotransferase AK4UniRule annotation
Gene namesi
Name:Ak4
Synonyms:Ak-4, Ak3b, Ak3l1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:87979. Ak4.

Subcellular locationi

  • Mitochondrion matrix UniRule annotation

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrial matrix Source: BHF-UCL
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 223223Adenylate kinase 4, mitochondrialPRO_0000158927Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601N6-succinyllysineCombined sources
Modified residuei175 – 1751N6-acetyllysineCombined sources
Modified residuei179 – 1791N6-acetyllysine; alternateCombined sources
Modified residuei179 – 1791N6-succinyllysine; alternateCombined sources
Modified residuei186 – 1861N6-acetyllysine; alternateCombined sources
Modified residuei186 – 1861N6-succinyllysine; alternateCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9WUR9.
MaxQBiQ9WUR9.
PaxDbiQ9WUR9.
PRIDEiQ9WUR9.

2D gel databases

REPRODUCTION-2DPAGEQ9WUR9.

PTM databases

iPTMnetiQ9WUR9.
PhosphoSiteiQ9WUR9.
SwissPalmiQ9WUR9.

Expressioni

Tissue specificityi

Expressed in the pyramidal cells in the hippocampus.

Developmental stagei

Expressed in the central nervous system in a region-specific manner from the middle stage of embryogenesis to the adulthood in the rodent.

Gene expression databases

BgeeiQ9WUR9.
CleanExiMM_AK3L1.
ExpressionAtlasiQ9WUR9. baseline and differential.
GenevisibleiQ9WUR9. MM.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

IntActiQ9WUR9. 2 interactions.
MINTiMINT-1866526.
STRINGi10090.ENSMUSP00000099841.

Structurei

3D structure databases

ProteinModelPortaliQ9WUR9.
SMRiQ9WUR9. Positions 4-223.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 6430NMPbindUniRule annotationAdd
BLAST
Regioni125 – 16238LIDUniRule 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 GTP/ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent GTP/ATP hydrolysis.UniRule annotation

Sequence similaritiesi

Belongs to the adenylate kinase family. AK3 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG3078. Eukaryota.
COG0563. LUCA.
GeneTreeiENSGT00550000074679.
HOGENOMiHOG000238772.
HOVERGENiHBG000458.
InParanoidiQ9WUR9.
KOiK00939.
OMAiYPRNISQ.
OrthoDBiEOG74TX0R.
PhylomeDBiQ9WUR9.
TreeFamiTF312916.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03169. Adenylate_kinase_AK3.
MF_03170. Adenylate_kinase_AK4.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR028586. AK3/Ak4_mitochondrial.
IPR028585. AK4_mitochondrial.
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]

Sequencei

Sequence statusi: Complete.

Q9WUR9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASKLLRAVI LGPPGSGKGT VCERIAQNFG LQHLSSGHLL RENLKTGTEV
60 70 80 90 100
GDVAKQYLEK GLLVPDHVIT RLMMSELETR SAQHWLLDGF PRTLVQAEAL
110 120 130 140 150
DGICDVDLVI SLNIPFETLK DRLSRRWIHP SSGRVYNLDF NPPQVQGIDD
160 170 180 190 200
ITGEPLVQQE DDKPEAVAAR LRRYKDAAKP VIELYKSRGV LHQFSGTETN
210 220
RIWPYVYTLF SNKITPIQSK EAY
Length:223
Mass (Da):25,062
Last modified:November 1, 1999 - v1
Checksum:i50552294971515EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681V → A in BAA77363 (Ref. 2) Curated
Sequence conflicti187 – 1871S → N in BAA77363 (Ref. 2) Curated
Sequence conflicti190 – 1901V → M in BAA77363 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D85036 mRNA. Translation: BAA77760.1.
AB020239 mRNA. Translation: BAA77363.1.
BC086663 mRNA. Translation: AAH86663.1.
CCDSiCCDS18394.1.
RefSeqiNP_001171073.1. NM_001177602.1.
NP_001171075.1. NM_001177604.1.
NP_001171076.1. NM_001177605.1.
NP_033777.1. NM_009647.5.
UniGeneiMm.42040.

Genome annotation databases

EnsembliENSMUST00000102780; ENSMUSP00000099841; ENSMUSG00000028527.
ENSMUST00000106945; ENSMUSP00000102558; ENSMUSG00000028527.
ENSMUST00000106946; ENSMUSP00000102559; ENSMUSG00000028527.
GeneIDi11639.
KEGGimmu:11639.
UCSCiuc008tvn.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D85036 mRNA. Translation: BAA77760.1.
AB020239 mRNA. Translation: BAA77363.1.
BC086663 mRNA. Translation: AAH86663.1.
CCDSiCCDS18394.1.
RefSeqiNP_001171073.1. NM_001177602.1.
NP_001171075.1. NM_001177604.1.
NP_001171076.1. NM_001177605.1.
NP_033777.1. NM_009647.5.
UniGeneiMm.42040.

3D structure databases

ProteinModelPortaliQ9WUR9.
SMRiQ9WUR9. Positions 4-223.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9WUR9. 2 interactions.
MINTiMINT-1866526.
STRINGi10090.ENSMUSP00000099841.

PTM databases

iPTMnetiQ9WUR9.
PhosphoSiteiQ9WUR9.
SwissPalmiQ9WUR9.

2D gel databases

REPRODUCTION-2DPAGEQ9WUR9.

Proteomic databases

EPDiQ9WUR9.
MaxQBiQ9WUR9.
PaxDbiQ9WUR9.
PRIDEiQ9WUR9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102780; ENSMUSP00000099841; ENSMUSG00000028527.
ENSMUST00000106945; ENSMUSP00000102558; ENSMUSG00000028527.
ENSMUST00000106946; ENSMUSP00000102559; ENSMUSG00000028527.
GeneIDi11639.
KEGGimmu:11639.
UCSCiuc008tvn.2. mouse.

Organism-specific databases

CTDi205.
MGIiMGI:87979. Ak4.

Phylogenomic databases

eggNOGiKOG3078. Eukaryota.
COG0563. LUCA.
GeneTreeiENSGT00550000074679.
HOGENOMiHOG000238772.
HOVERGENiHBG000458.
InParanoidiQ9WUR9.
KOiK00939.
OMAiYPRNISQ.
OrthoDBiEOG74TX0R.
PhylomeDBiQ9WUR9.
TreeFamiTF312916.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiAk4. mouse.
PROiQ9WUR9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WUR9.
CleanExiMM_AK3L1.
ExpressionAtlasiQ9WUR9. baseline and differential.
GenevisibleiQ9WUR9. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03169. Adenylate_kinase_AK3.
MF_03170. Adenylate_kinase_AK4.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR028586. AK3/Ak4_mitochondrial.
IPR028585. AK4_mitochondrial.
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. "Identification of a novel adenylate kinase system in the brain: cloning of the fourth adenylate kinase."
    Yoneda T., Sato M., Maeda M., Takagi H.
    Brain Res. Mol. Brain Res. 62:187-195(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. Noma T.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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].
    Strain: C57BL/6J.
    Tissue: Eye.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver and Testis.
  5. "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-60; LYS-179 AND LYS-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  6. "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-175; LYS-179 AND LYS-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiKAD4_MOUSE
AccessioniPrimary (citable) accession number: Q9WUR9
Secondary accession number(s): Q9R1X7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 132 of the entry and version 1 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. 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.