CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-028395
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Aconitate hydratase, mitochondrial 
Protein Synonyms/Alias
  
Gene Name
 ACO2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
13LLVTRLQKALGVRQYubiquitination[1, 2, 3]
68RPLTLSEKIVYGHLDubiquitination[2]
144EKDLRRAKDINQEVYacetylation[3]
144EKDLRRAKDINQEVYubiquitination[1, 2]
245LSGWSSPKDVILKVAubiquitination[1, 2]
395EVGKVAEKEGWPLDIacetylation[4]
395EVGKVAEKEGWPLDIubiquitination[2, 5, 6]
426GRSAAVAKQALAHGLubiquitination[1, 2]
436LAHGLKCKSQFTITPubiquitination[1]
545YLTGTDGKKFRLEAPacetylation[4]
545YLTGTDGKKFRLEAPubiquitination[2]
559PDADELPKGEFDPGQacetylation[4]
598QLLEPFDKWDGKDLEacetylation[4]
630SAAGPWLKFRGHLDNacetylation[3, 7]
630SAAGPWLKFRGHLDNubiquitination[3]
714GGRAIITKSFARIHEubiquitination[1]
726IHETNLKKQGLLPLTubiquitination[2]
748NKIHPVDKLTIQGLKubiquitination[2]
755KLTIQGLKDFTPGKPubiquitination[2, 8]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] 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]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 805 AA 
Protein Sequence
MAPYSLLVTR LQKALGVRQY HVASVLCQRA KVAMSHFEPN EYIHYDLLEK NINIVRKRLN 60
RPLTLSEKIV YGHLDDPASQ EIERGKSYLR LRPDRVAMQD ATAQMAMLQF ISSGLSKVAV 120
PSTIHCDHLI EAQVGGEKDL RRAKDINQEV YNFLATAGAK YGVGFWKPGS GIIHQIILEN 180
YAYPGVLLIG TDSHTPNGGG LGGICIGVGG ADAVDVMAGI PWELKCPKVI GVKLTGSLSG 240
WSSPKDVILK VAGILTVKGG TGAIVEYHGP GVDSISCTGE EGGQATWPLP CAGPDGSPVG 300
SRSGMATICN MGAEIGATTS VFPYNHRMKK YLSKTGREDI ANLADEFKDH LVPDPGCHYD 360
QLIEINLSEL KPHINGPFTP DLAHPVAEVG KVAEKEGWPL DIRVGLIGSC TNSSYEDMGR 420
SAAVAKQALA HGLKCKSQFT ITPGSEQIRA TIERDGYAQI LRDLGGIVLA NACGPCIGQW 480
DRKDIKKGEK NTIVTSYNRN FTGRNDANPE THAFVTSPEI VTALAIAGTL KFNPETDYLT 540
GTDGKKFRLE APDADELPKG EFDPGQDTYQ HPPKDSSGQH VDVSPTSQRL QLLEPFDKWD 600
GKDLEDLQIL IKVKGKCTTD HISAAGPWLK FRGHLDNISN NLLIGAINIE NGKANSVRNA 660
VTQEFGPVPD TARYYKKHGI RWVVIGDENY GEGSSREHAA LEPRHLGGRA IITKSFARIH 720
ETNLKKQGLL PLTFADPADY NKIHPVDKLT IQGLKDFTPG KPLKCIIKHP NGTQETILLN 780
HTFNETQIEW FRAGSALNRM KELQQ 805 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
 GO:0003994; F:aconitate hydratase activity; IEA:InterPro.
 GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. 
Interpro
 IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
 IPR015937; Acoase/IPM_deHydtase.
 IPR001030; Acoase/IPM_deHydtase_lsu_aba.
 IPR015928; Aconitase/3IPM_dehydase_swvl.
 IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
 IPR018136; Aconitase_4Fe-4S_BS.
 IPR006248; Aconitase_mito-like.
 IPR000573; AconitaseA/IPMdHydase_ssu_swvl. 
Pfam
 PF00330; Aconitase
 PF00694; Aconitase_C 
SMART
  
PROSITE
 PS00450; ACONITASE_1
 PS01244; ACONITASE_2 
PRINTS
 PR00415; ACONITASE.