CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002445
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Adenylate kinase 
Protein Synonyms/Alias
 ATP-AMP transphosphorylase; ATP:AMP phosphotransferase; Adenylate kinase cytosolic and mitochondrial; Adenylate monophosphate kinase 
Gene Name
 ADK1 
Gene Synonyms/Alias
 AKY; AKY1; AKY2; YDR226W; YD9934.11 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
19IGPPGAGKGTQAPNLacetylation[1]
47MLRSQIAKGTQLGLEacetylation[1]
47MLRSQIAKGTQLGLEubiquitination[2]
102RTIPQAEKLDQMLKEacetylation[1]
108EKLDQMLKEQGTPLEacetylation[1]
116EQGTPLEKAIELKVDacetylation[1]
116EQGTPLEKAIELKVDubiquitination[2]
146ASGRSYHKIFNPPKEacetylation[1]
156NPPKEDMKDDVTGEAacetylation[1]
176DDNADALKKRLAAYHacetylation[1]
194EPIVDFYKKTGIWAGacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 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. 
Sequence Annotation
 NP_BIND 16 21 ATP.
 NP_BIND 63 65 AMP.
 NP_BIND 92 95 AMP.
 NP_BIND 143 144 ATP.
 REGION 36 65 NMPbind.
 REGION 133 170 LID.
 BINDING 37 37 AMP.
 BINDING 42 42 AMP.
 BINDING 99 99 AMP.
 BINDING 134 134 ATP.
 BINDING 167 167 AMP.
 BINDING 178 178 AMP.
 BINDING 206 206 ATP; via carbonyl oxygen.
 MOD_RES 3 3 N-acetylserine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; Mitochondrion; Nucleotide-binding; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 222 AA 
Protein Sequence
MSSSESIRMV LIGPPGAGKG TQAPNLQERF HAAHLATGDM LRSQIAKGTQ LGLEAKKIMD 60
QGGLVSDDIM VNMIKDELTN NPACKNGFIL DGFPRTIPQA EKLDQMLKEQ GTPLEKAIEL 120
KVDDELLVAR ITGRLIHPAS GRSYHKIFNP PKEDMKDDVT GEALVQRSDD NADALKKRLA 180
AYHAQTEPIV DFYKKTGIWA GVDASQPPAT VWADILNKLG KD 222 
Gene Ontology
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
 GO:0004017; F:adenylate kinase activity; IMP:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0006172; P:ADP biosynthetic process; IDA:SGD.
 GO:0006270; P:DNA replication initiation; IMP:SGD. 
Interpro
 IPR006259; Adenyl_kin_sub.
 IPR000850; Adenylate_kin.
 IPR007862; Adenylate_kinase_lid-dom.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00406; ADK
 PF05191; ADK_lid 
SMART
  
PROSITE
 PS00113; ADENYLATE_KINASE 
PRINTS
 PR00094; ADENYLTKNASE.