CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023486
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 GTP:AMP phosphotransferase AK3, mitochondrial 
Protein Synonyms/Alias
 Adenylate kinase 3; AK 3; Adenylate kinase 3 alpha-like 1 
Gene Name
 Ak3 
Gene Synonyms/Alias
 Ak3l; Ak3l1; Akl3l 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
20MGAPGSGKGTVSSRIacetylation[1]
20MGAPGSGKGTVSSRIsuccinylation[1]
29TVSSRITKHFELKHLacetylation[1, 2, 3, 4, 5, 6]
29TVSSRITKHFELKHLsuccinylation[1]
34ITKHFELKHLSSGDLacetylation[1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11]
34ITKHFELKHLSSGDLsuccinylation[1]
57TEIGVLAKTFIDQGKacetylation[1, 5]
57TEIGVLAKTFIDQGKsuccinylation[1]
64KTFIDQGKLIPDDVMacetylation[1, 2, 3, 4, 5, 6, 9]
64KTFIDQGKLIPDDVMsuccinylation[1]
80RLALHELKTLTQCSWacetylation[1, 2, 5, 9]
80RLALHELKTLTQCSWsuccinylation[1]
122NVPFEVIKQRLTARWacetylation[5]
165LIQREDDKPETVIKRacetylation[4]
171DKPETVIKRLKAYEAacetylation[4]
174ETVIKRLKAYEAQTEacetylation[1, 2, 5]
174ETVIKRLKAYEAQTEsuccinylation[1]
174ETVIKRLKAYEAQTEubiquitination[12]
189PVLQYYQKKGVLETFacetylation[1, 2, 3, 4, 5, 6, 9, 10]
189PVLQYYQKKGVLETFsuccinylation[1]
189PVLQYYQKKGVLETFubiquitination[12]
203FSGTETNKIWPHVYSacetylation[4, 5, 6]
Reference
 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [3] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [5] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [6] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [7] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [8] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [9] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [10] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [11] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [12] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities (By similarity). 
Sequence Annotation
 NP_BIND 17 22 GTP (By similarity).
 NP_BIND 64 66 AMP (By similarity).
 NP_BIND 91 94 AMP (By similarity).
 NP_BIND 137 138 GTP (By similarity).
 REGION 37 66 NMPbind (By similarity).
 REGION 127 164 LID (By similarity).
 BINDING 38 38 AMP (By similarity).
 BINDING 43 43 AMP (By similarity).
 BINDING 98 98 AMP (By similarity).
 BINDING 128 128 GTP (By similarity).
 BINDING 161 161 AMP (By similarity).
 BINDING 172 172 AMP (By similarity).
 BINDING 201 201 GTP; via carbonyl oxygen (By similarity).
 MOD_RES 34 34 N6-acetyllysine.  
Keyword
 Acetylation; Complete proteome; GTP-binding; Kinase; Mitochondrion; Nucleotide-binding; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 227 AA 
Protein Sequence
MGASGRLLRA VIMGAPGSGK GTVSSRITKH FELKHLSSGD LLRQNMLQGT EIGVLAKTFI 60
DQGKLIPDDV MTRLALHELK TLTQCSWLLD GFPRTLPQAE ALDKVYQIDT VINLNVPFEV 120
IKQRLTARWI HPASGRVYNI EFNPPKTVGI DDLTGEPLIQ REDDKPETVI KRLKAYEAQT 180
EPVLQYYQKK GVLETFSGTE TNKIWPHVYS FLQTKVPETT QKASVTP 227 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IDA:BHF-UCL.
 GO:0004017; F:adenylate kinase activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0046899; F:nucleoside triphosphate adenylate kinase activity; IEA:EC. 
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.