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Protein

Adenylate kinase isoenzyme 1

Gene

Ak1

Organism
Rattus norvegicus (Rat)
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 annotation

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391AMPUniRule annotation
Binding sitei44 – 441AMPUniRule annotation
Binding sitei101 – 1011AMPUniRule annotation
Binding sitei132 – 1321ATPUniRule annotation
Binding sitei138 – 1381AMPUniRule annotation
Binding sitei149 – 1491AMPUniRule annotation
Binding sitei177 – 1771ATP; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 236ATPUniRule annotation
Nucleotide bindingi65 – 673AMPUniRule annotation
Nucleotide bindingi94 – 974AMPUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  • adenine metabolic process Source: RGD
  • ADP biosynthetic process Source: RGD
  • AMP metabolic process Source: RGD
  • ATP metabolic process Source: UniProtKB-HAMAP
  • cerebellum development Source: RGD
  • inosine biosynthetic process Source: RGD
  • muscle organ development Source: RGD
  • neuron differentiation Source: RGD
  • nucleoside diphosphate phosphorylation Source: UniProtKB
  • nucleoside triphosphate biosynthetic process Source: UniProtKB
  • olfactory bulb development Source: RGD
  • positive regulation of glucose transport Source: RGD
  • positive regulation of neuron maturation Source: RGD
  • response to activity Source: RGD
  • response to drug Source: RGD
  • response to estradiol Source: RGD
  • response to testosterone Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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:Ak1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2076. Ak1.

Subcellular locationi

GO - Cellular componenti

  • neuron projection Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • sarcomere Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3773.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 194194Adenylate kinase isoenzyme 1PRO_0000158914Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineUniRule annotationBy similarity
Modified residuei38 – 381PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP39069.

PTM databases

iPTMnetiP39069.
PhosphoSiteiP39069.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

IntActiP39069. 1 interaction.

Chemistry

BindingDBiP39069.

Structurei

3D structure databases

ProteinModelPortaliP39069.
SMRiP39069. Positions 1-194.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 6730NMPbindUniRule annotationAdd
BLAST
Regioni131 – 14111LIDUniRule 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. AK1 subfamily.UniRule annotation

Phylogenomic databases

HOVERGENiHBG108060.
InParanoidiP39069.
KOiK00939.
PhylomeDBiP39069.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P39069-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDKLKKAKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRAEVSSG
60 70 80 90 100
SSRGKMLSSI MEKGELVPLE TVLDMLRDAM LAKVDSSNGF LIDGYPREVK
110 120 130 140 150
QGEEFERKIA QPTLLLYVDA GPETMTQRLL KRGETSGRVD DNEETIKKRL
160 170 180 190
ETYYKATEPV ISFYDKRGIV RKVNAEGSVD TVFSQVCTYL DSLK
Length:194
Mass (Da):21,584
Last modified:January 9, 2007 - v3
Checksum:i4D53BCB3EF8B7629
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811L → F in BAA97655 (Ref. 1) Curated
Sequence conflicti104 – 1041E → S in BAA02643 (PubMed:8468325).Curated
Sequence conflicti175 – 1751A → L in BAA02643 (PubMed:8468325).Curated
Sequence conflicti179 – 1791V → W in BAA02643 (PubMed:8468325).Curated
Sequence conflicti187 – 1871C → S in BAA97655 (Ref. 1) Curated
Sequence conflicti187 – 1871C → S in BAA02643 (PubMed:8468325).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022701 mRNA. Translation: BAA97655.1.
BC089797 mRNA. Translation: AAH89797.1.
D13376 mRNA. Translation: BAA02643.1.
PIRiPQ0534.
RefSeqiNP_077325.2. NM_024349.3.
UniGeneiRn.219384.
Rn.79537.

Genome annotation databases

GeneIDi24183.
KEGGirno:24183.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022701 mRNA. Translation: BAA97655.1.
BC089797 mRNA. Translation: AAH89797.1.
D13376 mRNA. Translation: BAA02643.1.
PIRiPQ0534.
RefSeqiNP_077325.2. NM_024349.3.
UniGeneiRn.219384.
Rn.79537.

3D structure databases

ProteinModelPortaliP39069.
SMRiP39069. Positions 1-194.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP39069. 1 interaction.

Chemistry

BindingDBiP39069.
ChEMBLiCHEMBL3773.

PTM databases

iPTMnetiP39069.
PhosphoSiteiP39069.

Proteomic databases

PRIDEiP39069.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24183.
KEGGirno:24183.

Organism-specific databases

CTDi203.
RGDi2076. Ak1.

Phylogenomic databases

HOVERGENiHBG108060.
InParanoidiP39069.
KOiK00939.
PhylomeDBiP39069.

Miscellaneous databases

PROiP39069.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Rat adenylate kinase isozyme 1."
    Noma T.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "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].
    Tissue: Kidney.
  3. Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 10-21; 32-44; 64-77; 84-97; 101-128; 156-167 AND 172-194, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  4. "Tissue-specific and developmentally regulated expression of the genes encoding adenylate kinase isozymes."
    Tanabe T., Yamada M., Noma T., Kajii T., Nakazawa A.
    J. Biochem. 113:200-207(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 72-194.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKAD1_RAT
AccessioniPrimary (citable) accession number: P39069
Secondary accession number(s): Q5EBC5, Q9JJN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 9, 2007
Last modified: June 8, 2016
This is version 107 of the entry and version 3 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. 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.