CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005662
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cytoplasmic aconitate hydratase 
Protein Synonyms/Alias
 Aconitase; Citrate hydro-lyase; Iron regulatory protein 1; IRP1; Iron-responsive element-binding protein 1; IRE-BP 1 
Gene Name
 Aco1 
Gene Synonyms/Alias
 Ireb1; Irebp 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
2******MKNPFAHLAubiquitination[1]
19LDAAQPGKRFFNLNKubiquitination[1]
26KRFFNLNKLEDSRYGacetylation[2]
26KRFFNLNKLEDSRYGubiquitination[1]
56NCDEFLVKKNDIENIubiquitination[1]
79KNIEVPFKPARVILQubiquitination[1]
141RRADSLQKNQDLEFEubiquitination[1]
379GPKRPQDKVAVSEMKubiquitination[1]
396FESCLGAKQGFKGFQacetylation[3]
396FESCLGAKQGFKGFQubiquitination[1]
455GAGLLAKKAVEAGLSubiquitination[1]
464VEAGLSVKPYIKTSLubiquitination[1]
572TVRIDFEKEPLGVNAubiquitination[1]
610HVIPGMFKEVYQKIEubiquitination[1]
615MFKEVYQKIETVNKSacetylation[2, 3, 4, 5]
615MFKEVYQKIETVNKSubiquitination[1]
621QKIETVNKSWNALAAubiquitination[1]
632ALAAPSEKLYAWNPKubiquitination[1]
639KLYAWNPKSTYIKSPacetylation[6]
639KLYAWNPKSTYIKSPsuccinylation[6]
639KLYAWNPKSTYIKSPubiquitination[1]
644NPKSTYIKSPPFFESubiquitination[1]
732ANIRLLNKFLNKQAPubiquitination[1]
736LLNKFLNKQAPQTVHubiquitination[1]
772PLIVLAGKEYGSGSSubiquitination[1]
785SSRDWAAKGPFLLGIubiquitination[1]
844INIPEDLKPRMTVQIubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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]
 [6] 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
Functional Description
 Iron sensor. Binds a 4Fe-4S cluster and functions as aconitase when cellular iron levels are high. Functions as mRNA binding protein that regulates uptake, sequestration and utilization of iron when cellular iron levels are low. Binds to iron-responsive elements (IRES) in target mRNA species when iron levels are low. Binding of a 4Fe-4S cluster precludes RNA binding (By similarity). 
Sequence Annotation
 REGION 205 207 Substrate binding (By similarity).
 REGION 779 780 Substrate binding (By similarity).
 METAL 437 437 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 503 503 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 506 506 Iron-sulfur (4Fe-4S) (By similarity).
 BINDING 86 86 Substrate (By similarity).
 BINDING 536 536 Substrate (By similarity).
 BINDING 541 541 Substrate (By similarity).
 BINDING 699 699 Substrate (By similarity).  
Keyword
 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome; RNA-binding; Tricarboxylic acid cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 889 AA 
Protein Sequence
MKNPFAHLAE PLDAAQPGKR FFNLNKLEDS RYGRLPFSIR VLLEAAVRNC DEFLVKKNDI 60
ENILNWNVMQ HKNIEVPFKP ARVILQDFTG VPAVVDFAAM RDAVKKLGGN PEKINPVCPA 120
DLVIDHSIQV DFNRRADSLQ KNQDLEFERN KERFEFLKWG SQAFCNMRII PPGSGIIHQV 180
NLEYLARVVF DQDGCYYPDS LVGTDSHTTM IDGLGVLGWG VGGIEAEAVM LGQPISMVLP 240
QVIGYKLMGK PHPLVTSTDI VLTITKHLRQ VGVVGKFVEF FGPGVAQLSI ADRATIANMC 300
PEYGATAAFF PVDEVSIAYL LQTGREEDKV KHIQKYLQAV GMFRDFNDTS QDPDFTQVVE 360
LDLKTVVPCC SGPKRPQDKV AVSEMKKDFE SCLGAKQGFK GFQVAPDRHN DRKTFLYSNS 420
EFTLAHGSVV IAAITSCTNT SNPSVMLGAG LLAKKAVEAG LSVKPYIKTS LSPGSGVVTY 480
YLRESGVMPY LSQLGFDVVG YGCMTCIGNS GPLPEPVVEA ITQGDLVAVG VLSGNRNFEG 540
RVHPNTRANY LASPPLVIAY AIAGTVRIDF EKEPLGVNAQ GRQVFLKDIW PTRDEIQAVE 600
RQHVIPGMFK EVYQKIETVN KSWNALAAPS EKLYAWNPKS TYIKSPPFFE SLTLDLQPPK 660
SIVDAYVLLN LGDSVTTDHI SPAGNIARNS PAARYLTNRG LTPREFNSYG SRRGNDAIMA 720
RGTFANIRLL NKFLNKQAPQ TVHLPSGETL DVFDAAERYQ QAGLPLIVLA GKEYGSGSSR 780
DWAAKGPFLL GIKAVLAESY ERIHRSNLVG MGVIPLEYLP GETADSLGLT GRERYTINIP 840
EDLKPRMTVQ IKLDTGKTFQ AVMRFDTDVE LTYFHNGGIL NYMIRKMAQ 889 
Gene Ontology
 GO:0005829; C:cytosol; IDA:MGI.
 GO:0005783; C:endoplasmic reticulum; IEA:Compara.
 GO:0005794; C:Golgi apparatus; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
 GO:0003994; F:aconitate hydratase activity; ISS:UniProtKB.
 GO:0052632; F:citrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC.
 GO:0030350; F:iron-responsive element binding; ISS:UniProtKB.
 GO:0052633; F:isocitrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006879; P:cellular iron ion homeostasis; IMP:MGI.
 GO:0006101; P:citrate metabolic process; ISS:UniProtKB.
 GO:0050892; P:intestinal absorption; IGI:MGI.
 GO:0009791; P:post-embryonic development; IGI:MGI.
 GO:0006417; P:regulation of translation; IMP:MGI.
 GO:0010040; P:response to iron(II) ion; ISS:UniProtKB.
 GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. 
Interpro
 IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
 IPR015937; Acoase/IPM_deHydtase.
 IPR001030; Acoase/IPM_deHydtase_lsu_aba.
 IPR015928; Aconitase/3IPM_dehydase_swvl.
 IPR006249; Aconitase/Fe_reg_prot_2.
 IPR015934; Aconitase/Fe_reg_prot_2/AcnD.
 IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
 IPR018136; Aconitase_4Fe-4S_BS.
 IPR000573; AconitaseA/IPMdHydase_ssu_swvl. 
Pfam
 PF00330; Aconitase
 PF00694; Aconitase_C 
SMART
  
PROSITE
 PS00450; ACONITASE_1
 PS01244; ACONITASE_2 
PRINTS
 PR00415; ACONITASE.