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Protein

Adenylate kinase isoenzyme 1

Gene

AK1

Organism
Homo sapiens (Human)
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. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.UniRule annotation1 Publication

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation1 Publication
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei39AMPUniRule annotation2 Publications1
Binding sitei44AMPUniRule annotation2 Publications1
Binding sitei101AMPUniRule annotation2 Publications1
Binding sitei132ATPUniRule annotation2 Publications1
Binding sitei138AMPUniRule annotation2 Publications1
Binding sitei149AMPUniRule annotation2 Publications1
Binding sitei177ATP; via carbonyl oxygenUniRule annotation2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi18 – 23ATPUniRule annotation2 Publications6
Nucleotide bindingi65 – 67AMPUniRule annotation2 Publications3
Nucleotide bindingi94 – 97AMPUniRule annotation2 Publications4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS02965-MONOMER.
BRENDAi2.7.4.3. 2681.
ReactomeiR-HSA-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
SABIO-RKP00568.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate kinase isoenzyme 1UniRule annotation (EC:2.7.4.3UniRule annotation, EC:2.7.4.6UniRule annotation)
Short name:
AK 1UniRule annotation
Alternative name(s):
ATP-AMP transphosphorylase 1UniRule annotation
ATP:AMP phosphotransferaseUniRule annotation
Adenylate monophosphate kinaseUniRule annotation
MyokinaseUniRule annotation
Gene namesi
Name:AK1UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:361. AK1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • outer dense fiber Source: Ensembl
  • plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Hemolytic anemia due to adenylate kinase deficiency (HAAKD)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by hemolytic anemia and undetectable erythrocyte adenylate kinase activity.
See also OMIM:612631
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05533740G → R in HAAKD. 1 PublicationCorresponds to variant rs137853204dbSNPEnsembl.1
Natural variantiVAR_05533864G → R in HAAKD. 1 PublicationCorresponds to variant rs137853205dbSNPEnsembl.1
Natural variantiVAR_004021128R → W in HAAKD. 1 PublicationCorresponds to variant rs28930974dbSNPEnsembl.1
Natural variantiVAR_055339140Missing in HAAKD. 1 Publication1
Natural variantiVAR_055340164Y → C in HAAKD. 1 PublicationCorresponds to variant rs137853203dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Hereditary hemolytic anemia

Organism-specific databases

DisGeNETi203.
MalaCardsiAK1.
MIMi612631. phenotype.
OpenTargetsiENSG00000106992.
Orphaneti86817. Hemolytic anemia due to adenylate kinase deficiency.
PharmGKBiPA24655.

Chemistry databases

ChEMBLiCHEMBL4925.

Polymorphism and mutation databases

BioMutaiAK1.
DMDMi20178288.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001589101 – 194Adenylate kinase isoenzyme 1Add BLAST194

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineUniRule annotation1 Publication1
Modified residuei38PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP00568.
PaxDbiP00568.
PeptideAtlasiP00568.
PRIDEiP00568.
TopDownProteomicsiP00568.

2D gel databases

OGPiP00568.
REPRODUCTION-2DPAGEIPI00018342.
UCD-2DPAGEP00568.

PTM databases

iPTMnetiP00568.
PhosphoSitePlusiP00568.
SwissPalmiP00568.

Expressioni

Gene expression databases

BgeeiENSG00000106992.
CleanExiHS_AK1.
ExpressionAtlasiP00568. baseline and differential.
GenevisibleiP00568. HS.

Organism-specific databases

HPAiCAB009893.
HPA006456.

Interactioni

Subunit structurei

Monomer.UniRule annotation2 Publications

Protein-protein interaction databases

BioGridi106706. 26 interactors.
IntActiP00568. 20 interactors.
STRINGi9606.ENSP00000362249.

Structurei

Secondary structure

1194
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 5Combined sources5
Beta strandi10 – 15Combined sources6
Helixi21 – 32Combined sources12
Beta strandi35 – 38Combined sources4
Helixi39 – 48Combined sources10
Helixi52 – 62Combined sources11
Helixi69 – 83Combined sources15
Turni84 – 86Combined sources3
Beta strandi90 – 94Combined sources5
Helixi99 – 108Combined sources10
Beta strandi113 – 119Combined sources7
Helixi122 – 133Combined sources12
Beta strandi135 – 137Combined sources3
Helixi139 – 141Combined sources3
Helixi143 – 156Combined sources14
Helixi158 – 167Combined sources10
Beta strandi170 – 174Combined sources5
Helixi179 – 193Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z83X-ray1.90A/B/C1-193[»]
2C95X-ray1.71A/B1-193[»]
ProteinModelPortaliP00568.
SMRiP00568.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00568.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni38 – 67NMPbindUniRule annotation2 PublicationsAdd BLAST30
Regioni131 – 141LIDUniRule annotation2 PublicationsAdd BLAST11

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 annotation2 Publications

Sequence similaritiesi

Belongs to the adenylate kinase family. AK1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG3079. Eukaryota.
COG0563. LUCA.
GeneTreeiENSGT00390000016215.
HOGENOMiHOG000238771.
HOVERGENiHBG108060.
InParanoidiP00568.
KOiK00939.
PhylomeDBiP00568.
TreeFamiTF354283.

Family and domain databases

CDDicd01428. ADK. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk. 1 hit.
MF_03171. Adenylate_kinase_AK1. 1 hit.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
IPR033690. Adenylat_kinase_CS.
IPR028582. AK1.
IPR006267. AK1/5.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01360. aden_kin_iso1. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00568-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEKLKKTKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRSEVSSG
60 70 80 90 100
SARGKKLSEI MEKGQLVPLE TVLDMLRDAM VAKVNTSKGF LIDGYPREVQ
110 120 130 140 150
QGEEFERRIG QPTLLLYVDA GPETMTQRLL KRGETSGRVD DNEETIKKRL
160 170 180 190
ETYYKATEPV IAFYEKRGIV RKVNAEGSVD SVFSQVCTHL DALK
Length:194
Mass (Da):21,635
Last modified:April 16, 2002 - v3
Checksum:i95EC5AAA92D1F00F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9K → N in AAH01116 (PubMed:15489334).Curated1
Sequence conflicti127Q → R AA sequence (PubMed:183954).Curated1
Sequence conflicti181S → E AA sequence (PubMed:183954).Curated1

Polymorphismi

This enzyme represents the most common of at least five alleles.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05533740G → R in HAAKD. 1 PublicationCorresponds to variant rs137853204dbSNPEnsembl.1
Natural variantiVAR_05533864G → R in HAAKD. 1 PublicationCorresponds to variant rs137853205dbSNPEnsembl.1
Natural variantiVAR_034046123E → Q.Corresponds to variant rs8192462dbSNPEnsembl.1
Natural variantiVAR_004021128R → W in HAAKD. 1 PublicationCorresponds to variant rs28930974dbSNPEnsembl.1
Natural variantiVAR_055339140Missing in HAAKD. 1 Publication1
Natural variantiVAR_055340164Y → C in HAAKD. 1 PublicationCorresponds to variant rs137853203dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04809 Genomic DNA. Translation: AAA51686.1.
AB021871 mRNA. Translation: BAA78534.1.
BT019580 mRNA. Translation: AAV38387.1.
BC001116 mRNA. Translation: AAH01116.1.
CCDSiCCDS6881.1.
PIRiA33508. KIHUA.
RefSeqiNP_000467.1. NM_000476.2.
NP_001305050.1. NM_001318121.1.
XP_016869916.1. XM_017014427.1.
XP_016869917.1. XM_017014428.1.
UniGeneiHs.175473.

Genome annotation databases

EnsembliENST00000373156; ENSP00000362249; ENSG00000106992.
ENST00000373176; ENSP00000362271; ENSG00000106992.
GeneIDi203.
KEGGihsa:203.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Adenylate kinase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04809 Genomic DNA. Translation: AAA51686.1.
AB021871 mRNA. Translation: BAA78534.1.
BT019580 mRNA. Translation: AAV38387.1.
BC001116 mRNA. Translation: AAH01116.1.
CCDSiCCDS6881.1.
PIRiA33508. KIHUA.
RefSeqiNP_000467.1. NM_000476.2.
NP_001305050.1. NM_001318121.1.
XP_016869916.1. XM_017014427.1.
XP_016869917.1. XM_017014428.1.
UniGeneiHs.175473.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z83X-ray1.90A/B/C1-193[»]
2C95X-ray1.71A/B1-193[»]
ProteinModelPortaliP00568.
SMRiP00568.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106706. 26 interactors.
IntActiP00568. 20 interactors.
STRINGi9606.ENSP00000362249.

Chemistry databases

ChEMBLiCHEMBL4925.

PTM databases

iPTMnetiP00568.
PhosphoSitePlusiP00568.
SwissPalmiP00568.

Polymorphism and mutation databases

BioMutaiAK1.
DMDMi20178288.

2D gel databases

OGPiP00568.
REPRODUCTION-2DPAGEIPI00018342.
UCD-2DPAGEP00568.

Proteomic databases

EPDiP00568.
PaxDbiP00568.
PeptideAtlasiP00568.
PRIDEiP00568.
TopDownProteomicsiP00568.

Protocols and materials databases

DNASUi203.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373156; ENSP00000362249; ENSG00000106992.
ENST00000373176; ENSP00000362271; ENSG00000106992.
GeneIDi203.
KEGGihsa:203.

Organism-specific databases

CTDi203.
DisGeNETi203.
GeneCardsiAK1.
HGNCiHGNC:361. AK1.
HPAiCAB009893.
HPA006456.
MalaCardsiAK1.
MIMi103000. gene.
612631. phenotype.
neXtProtiNX_P00568.
OpenTargetsiENSG00000106992.
Orphaneti86817. Hemolytic anemia due to adenylate kinase deficiency.
PharmGKBiPA24655.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3079. Eukaryota.
COG0563. LUCA.
GeneTreeiENSGT00390000016215.
HOGENOMiHOG000238771.
HOVERGENiHBG108060.
InParanoidiP00568.
KOiK00939.
PhylomeDBiP00568.
TreeFamiTF354283.

Enzyme and pathway databases

BioCyciZFISH:HS02965-MONOMER.
BRENDAi2.7.4.3. 2681.
ReactomeiR-HSA-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
SABIO-RKP00568.

Miscellaneous databases

EvolutionaryTraceiP00568.
GenomeRNAii203.
PROiP00568.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000106992.
CleanExiHS_AK1.
ExpressionAtlasiP00568. baseline and differential.
GenevisibleiP00568. HS.

Family and domain databases

CDDicd01428. ADK. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk. 1 hit.
MF_03171. Adenylate_kinase_AK1. 1 hit.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
IPR033690. Adenylat_kinase_CS.
IPR028582. AK1.
IPR006267. AK1/5.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01360. aden_kin_iso1. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKAD1_HUMAN
AccessioniPrimary (citable) accession number: P00568
Secondary accession number(s): Q9BVK9, Q9UQC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 16, 2002
Last modified: November 30, 2016
This is version 183 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.