UniProt Accession

 ACON_HUMAN; Q99798; O75809; Q5JZ41; Q6FHX0; Q8TAQ6 

Genbank Protein ID

 U80040; U87939; U87926; U87927; U87928; U87929; U87930; U87931; U87932; U87933; U87934; U87935; U87936; U87937; U87938; CR456365; CR536568; AL023553; AL008582; AL008582; AL023553; BC014092; BC026196 

Genbank Nucleotide ID

 AAB38416.1; AAC39921.1; AAC39921.1; AAC39921.1; AAC39921.1; AAC39921.1; AAC39921.1; AAC39921.1; AAC39921.1; AAC39921.1; AAC39921.1; AAC39921.1; AAC39921.1; AAC39921.1; AAC39921.1; CAG30251.1; CAG38805.1; CAI20278.1; CAI20278.1; CAI17931.1; CAI17931.1; AAH14092.1; AAH26196.1 

Protein Name

 Aconitate hydratase, mitochondrial 

Protein Synonyms/Alias

 Aconitase; Citrate hydro-lyase 

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
13	LLVTRLQKALGVRQY	ubiquitination	[1]
50	IHYDLLEKNINIVRK	acetylation	[2]
68	RPLTLSEKIVYGHLD	ubiquitination	[1]
144	EKDLRRAKDINQEVY	ubiquitination	[1]
245	LSGWSSPKDVILKVA	ubiquitination	[1]
370	EVGKVAEKEGWPLDI	ubiquitination	[1, 3]
401	GRSAAVAKQALAHGL	ubiquitination	[1]
520	YLTGTDGKKFRLEAP	ubiquitination	[1]
549	DTYQHPPKDSSGQHV	acetylation	[4]
573	QLLEPFDKWDGKDLE	acetylation	[2]
605	SAAGPWLKFRGHLDN	acetylation	[2]
701	IHETNLKKQGLLPLT	ubiquitination	[1]
723	NKIHPVDKLTIQGLK	ubiquitination	[1]
730	KLTIQGLKDFTPGKP	ubiquitination	[1]

Reference

 [1] 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]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] 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]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 

Functional Description

 Catalyzes the isomerization of citrate to isocitrate via cis-aconitate (By similarity). 

Sequence Annotation

 REGION 192 194 Substrate binding (By similarity).
 REGION 670 671 Substrate binding (By similarity).
 METAL 385 385 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 448 448 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 451 451 Iron-sulfur (4Fe-4S) (By similarity).
 BINDING 99 99 Substrate (By similarity).
 BINDING 474 474 Substrate (By similarity).
 BINDING 479 479 Substrate (By similarity).
 BINDING 607 607 Substrate (By similarity).
 MOD_RES 28 28 Pyrrolidone carboxylic acid (By
 MOD_RES 50 50 N6-acetyllysine (By similarity).
 MOD_RES 559 559 Phosphoserine.
 MOD_RES 573 573 N6-acetyllysine.
 MOD_RES 605 605 N6-acetyllysine.
 CROSSLNK 144 144 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 4Fe-4S; Acetylation; Complete proteome; Direct protein sequencing; Disease mutation; Iron; Iron-sulfur; Isopeptide bond; Lyase; Metal-binding; Mitochondrion; Neurodegeneration; Phosphoprotein; Polymorphism; Pyrrolidone carboxylic acid; Reference proteome; Transit peptide; Tricarboxylic acid cycle; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 780 AA 

Protein Sequence

Gene Ontology

 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:Compara.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0052632; F:citrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC.
 GO:0005506; F:iron ion binding; IDA:MGI.
 GO:0052633; F:isocitrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0006101; P:citrate metabolic process; IDA:MGI.
 GO:0006102; P:isocitrate metabolic process; IEA:Compara.
 GO:0006099; P:tricarboxylic acid cycle; IDA:MGI. 

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.