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Q99798

- ACON_HUMAN

UniProt

Q99798 - ACON_HUMAN

Protein

Aconitate hydratase, mitochondrial

Gene

ACO2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    Citrate = isocitrate.

    Cofactori

    Binds 1 4Fe-4S cluster per subunit. Binding of a 3Fe-4S cluster leads to an inactive enzyme By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei99 – 991SubstrateBy similarity
    Metal bindingi385 – 3851Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi448 – 4481Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi451 – 4511Iron-sulfur (4Fe-4S)By similarity
    Binding sitei474 – 4741SubstrateBy similarity
    Binding sitei479 – 4791SubstrateBy similarity
    Binding sitei607 – 6071SubstrateBy similarity

    GO - Molecular functioni

    1. 3 iron, 4 sulfur cluster binding Source: Ensembl
    2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    3. aconitate hydratase activity Source: UniProtKB-EC
    4. iron ion binding Source: MGI

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. cellular metabolic process Source: Reactome
    3. citrate metabolic process Source: MGI
    4. generation of precursor metabolites and energy Source: ProtInc
    5. isocitrate metabolic process Source: Ensembl
    6. small molecule metabolic process Source: Reactome
    7. tricarboxylic acid cycle Source: MGI

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    4Fe-4S, Iron, Iron-sulfur, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02077-MONOMER.
    ReactomeiREACT_118595. Mitochondrial protein import.
    REACT_1785. Citric acid cycle (TCA cycle).
    UniPathwayiUPA00223; UER00718.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aconitate hydratase, mitochondrial (EC:4.2.1.3)
    Short name:
    Aconitase
    Alternative name(s):
    Citrate hydro-lyase
    Gene namesi
    Name:ACO2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:118. ACO2.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrion Source: UniProt
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Infantile cerebellar-retinal degeneration (ICRD) [MIM:614559]: A severe autosomal recessive neurodegenerative disorder characterized by onset between ages 2 and 6 months of truncal hypotonia, athetosis, seizures, and ophthalmologic abnormalities, particularly optic atrophy and retinal degeneration. Affected individuals show profound psychomotor retardation, with only some achieving rolling, sitting, or recognition of family. Brain MRI shows progressive cerebral and cerebellar degeneration.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti112 – 1121S → R in ICRD; functional expression studies in yeast show that the mutant has decreased function under growth conditions requiring the TCA cycle and the glyoxylate shunt. 1 Publication
    VAR_067543

    Keywords - Diseasei

    Disease mutation, Neurodegeneration

    Organism-specific databases

    MIMi614559. phenotype.
    Orphaneti313850. Infantile cerebellar-retinal degeneration.
    PharmGKBiPA24443.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2727MitochondrionBy similarityAdd
    BLAST
    Chaini28 – 780753Aconitate hydratase, mitochondrialPRO_0000000541Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei28 – 281Pyrrolidone carboxylic acidBy similarity
    Modified residuei31 – 311N6-succinyllysineBy similarity
    Modified residuei50 – 501N6-acetyllysine; alternateBy similarity
    Modified residuei50 – 501N6-succinyllysine; alternateBy similarity
    Modified residuei138 – 1381N6-acetyllysine; alternateBy similarity
    Modified residuei138 – 1381N6-succinyllysine; alternateBy similarity
    Modified residuei144 – 1441N6-acetyllysine; alternateBy similarity
    Modified residuei144 – 1441N6-succinyllysine; alternateBy similarity
    Cross-linki144 – 144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
    Modified residuei233 – 2331N6-acetyllysine; alternateBy similarity
    Modified residuei233 – 2331N6-succinyllysine; alternateBy similarity
    Modified residuei411 – 4111N6-succinyllysineBy similarity
    Modified residuei549 – 5491N6-succinyllysineBy similarity
    Modified residuei559 – 5591Phosphoserine1 Publication
    Modified residuei573 – 5731N6-acetyllysine; alternate1 Publication
    Modified residuei573 – 5731N6-succinyllysine; alternateBy similarity
    Modified residuei577 – 5771N6-succinyllysineBy similarity
    Modified residuei591 – 5911N6-succinyllysineBy similarity
    Modified residuei605 – 6051N6-acetyllysine; alternate1 Publication
    Modified residuei605 – 6051N6-succinyllysine; alternateBy similarity
    Modified residuei628 – 6281N6-succinyllysineBy similarity
    Modified residuei689 – 6891N6-succinyllysineBy similarity
    Modified residuei723 – 7231N6-acetyllysine; alternateBy similarity
    Modified residuei723 – 7231N6-succinyllysine; alternateBy similarity
    Modified residuei730 – 7301N6-acetyllysine; alternateBy similarity
    Modified residuei730 – 7301N6-succinyllysine; alternateBy similarity
    Modified residuei736 – 7361N6-acetyllysineBy similarity
    Modified residuei739 – 7391N6-acetyllysineBy similarity
    Modified residuei743 – 7431N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Pyrrolidone carboxylic acid, Ubl conjugation

    Proteomic databases

    MaxQBiQ99798.
    PaxDbiQ99798.
    PRIDEiQ99798.

    2D gel databases

    DOSAC-COBS-2DPAGEQ99798.
    REPRODUCTION-2DPAGEIPI00017855.
    Q99798.
    SWISS-2DPAGEQ99798.
    UCD-2DPAGEQ99798.

    PTM databases

    PhosphoSiteiQ99798.

    Expressioni

    Gene expression databases

    ArrayExpressiQ99798.
    BgeeiQ99798.
    CleanExiHS_ACO2.
    GenevestigatoriQ99798.

    Organism-specific databases

    HPAiHPA001097.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi106566. 16 interactions.
    IntActiQ99798. 2 interactions.
    MINTiMINT-2856402.
    STRINGi9606.ENSP00000216254.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99798.
    SMRiQ99798. Positions 29-780.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni192 – 1943Substrate bindingBy similarity
    Regioni670 – 6712Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the aconitase/IPM isomerase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1048.
    HOGENOMiHOG000224293.
    HOVERGENiHBG000248.
    KOiK01681.
    OrthoDBiEOG74FF06.
    PhylomeDBiQ99798.
    TreeFamiTF300627.

    Family and domain databases

    Gene3Di3.20.19.10. 1 hit.
    3.30.499.10. 2 hits.
    3.40.1060.10. 1 hit.
    InterProiIPR015931. 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.
    [Graphical view]
    PANTHERiPTHR11670. PTHR11670. 1 hit.
    PfamiPF00330. Aconitase. 1 hit.
    PF00694. Aconitase_C. 1 hit.
    [Graphical view]
    PRINTSiPR00415. ACONITASE.
    SUPFAMiSSF52016. SSF52016. 1 hit.
    SSF53732. SSF53732. 1 hit.
    TIGRFAMsiTIGR01340. aconitase_mito. 1 hit.
    PROSITEiPS00450. ACONITASE_1. 1 hit.
    PS01244. ACONITASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q99798-1 [UniParc]FASTAAdd to Basket

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    MAPYSLLVTR LQKALGVRQY HVASVLCQRA KVAMSHFEPN EYIHYDLLEK    50
    NINIVRKRLN RPLTLSEKIV YGHLDDPASQ EIERGKSYLR LRPDRVAMQD 100
    ATAQMAMLQF ISSGLSKVAV PSTIHCDHLI EAQVGGEKDL RRAKDINQEV 150
    YNFLATAGAK YGVGFWKPGS GIIHQIILEN YAYPGVLLIG TDSHTPNGGG 200
    LGGICIGVGG ADAVDVMAGI PWELKCPKVI GVKLTGSLSG WSSPKDVILK 250
    VAGILTVKGG TGAIVEYHGP GVDSISCTGM ATICNMGAEI GATTSVFPYN 300
    HRMKKYLSKT GREDIANLAD EFKDHLVPDP GCHYDQLIEI NLSELKPHIN 350
    GPFTPDLAHP VAEVGKVAEK EGWPLDIRVG LIGSCTNSSY EDMGRSAAVA 400
    KQALAHGLKC KSQFTITPGS EQIRATIERD GYAQILRDLG GIVLANACGP 450
    CIGQWDRKDI KKGEKNTIVT SYNRNFTGRN DANPETHAFV TSPEIVTALA 500
    IAGTLKFNPE TDYLTGTDGK KFRLEAPDAD ELPKGEFDPG QDTYQHPPKD 550
    SSGQHVDVSP TSQRLQLLEP FDKWDGKDLE DLQILIKVKG KCTTDHISAA 600
    GPWLKFRGHL DNISNNLLIG AINIENGKAN SVRNAVTQEF GPVPDTARYY 650
    KKHGIRWVVI GDENYGEGSS REHAALEPRH LGGRAIITKS FARIHETNLK 700
    KQGLLPLTFA DPADYNKIHP VDKLTIQGLK DFTPGKPLKC IIKHPNGTQE 750
    TILLNHTFNE TQIEWFRAGS ALNRMKELQQ 780
    Length:780
    Mass (Da):85,425
    Last modified:May 30, 2000 - v2
    Checksum:i58C9FFBDBDC63D5E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 351S → T in AAB38416. 1 PublicationCurated
    Sequence conflicti136 – 1361G → D in AAB38416. 1 PublicationCurated
    Sequence conflicti159 – 1591A → D in AAB38416. 1 PublicationCurated
    Sequence conflicti167 – 1671K → S in AAB38416. 1 PublicationCurated
    Sequence conflicti199 – 1991G → D in CAG38805. 1 PublicationCurated
    Sequence conflicti207 – 2071G → R in AAH26196. (PubMed:15489334)Curated
    Sequence conflicti242 – 2421S → T in AAB38416. 1 PublicationCurated
    Sequence conflicti270 – 2701P → H in AAH26196. (PubMed:15489334)Curated
    Sequence conflicti275 – 2751I → M in AAB38416. 1 PublicationCurated
    Sequence conflicti444 – 4441L → P in CAG38805. 1 PublicationCurated
    Sequence conflicti517 – 5171T → K in AAB38416. 1 PublicationCurated
    Sequence conflicti553 – 5531G → R in AAB38416. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti112 – 1121S → R in ICRD; functional expression studies in yeast show that the mutant has decreased function under growth conditions requiring the TCA cycle and the glyoxylate shunt. 1 Publication
    VAR_067543
    Natural varianti697 – 6971T → N in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036572
    Natural varianti768 – 7681A → S.
    Corresponds to variant rs1804785 [ dbSNP | Ensembl ].
    VAR_033297

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U80040 mRNA. Translation: AAB38416.1.
    U87939
    , U87926, U87927, U87928, U87929, U87930, U87931, U87932, U87933, U87934, U87935, U87936, U87937, U87938 Genomic DNA. Translation: AAC39921.1.
    CR456365 mRNA. Translation: CAG30251.1.
    CR536568 mRNA. Translation: CAG38805.1.
    AL023553, AL008582 Genomic DNA. Translation: CAI20278.1.
    AL008582, AL023553 Genomic DNA. Translation: CAI17931.1.
    BC014092 mRNA. Translation: AAH14092.1.
    BC026196 mRNA. Translation: AAH26196.1.
    CCDSiCCDS14017.1.
    PIRiS17526.
    T52543.
    RefSeqiNP_001089.1. NM_001098.2.
    UniGeneiHs.643610.

    Genome annotation databases

    EnsembliENST00000216254; ENSP00000216254; ENSG00000100412.
    GeneIDi50.
    KEGGihsa:50.
    UCSCiuc003bac.3. human.

    Polymorphism databases

    DMDMi6686275.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Aconitase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U80040 mRNA. Translation: AAB38416.1 .
    U87939
    , U87926 , U87927 , U87928 , U87929 , U87930 , U87931 , U87932 , U87933 , U87934 , U87935 , U87936 , U87937 , U87938 Genomic DNA. Translation: AAC39921.1 .
    CR456365 mRNA. Translation: CAG30251.1 .
    CR536568 mRNA. Translation: CAG38805.1 .
    AL023553 , AL008582 Genomic DNA. Translation: CAI20278.1 .
    AL008582 , AL023553 Genomic DNA. Translation: CAI17931.1 .
    BC014092 mRNA. Translation: AAH14092.1 .
    BC026196 mRNA. Translation: AAH26196.1 .
    CCDSi CCDS14017.1.
    PIRi S17526.
    T52543.
    RefSeqi NP_001089.1. NM_001098.2.
    UniGenei Hs.643610.

    3D structure databases

    ProteinModelPortali Q99798.
    SMRi Q99798. Positions 29-780.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106566. 16 interactions.
    IntActi Q99798. 2 interactions.
    MINTi MINT-2856402.
    STRINGi 9606.ENSP00000216254.

    PTM databases

    PhosphoSitei Q99798.

    Polymorphism databases

    DMDMi 6686275.

    2D gel databases

    DOSAC-COBS-2DPAGE Q99798.
    REPRODUCTION-2DPAGE IPI00017855.
    Q99798.
    SWISS-2DPAGE Q99798.
    UCD-2DPAGE Q99798.

    Proteomic databases

    MaxQBi Q99798.
    PaxDbi Q99798.
    PRIDEi Q99798.

    Protocols and materials databases

    DNASUi 50.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216254 ; ENSP00000216254 ; ENSG00000100412 .
    GeneIDi 50.
    KEGGi hsa:50.
    UCSCi uc003bac.3. human.

    Organism-specific databases

    CTDi 50.
    GeneCardsi GC22P041865.
    HGNCi HGNC:118. ACO2.
    HPAi HPA001097.
    MIMi 100850. gene.
    614559. phenotype.
    neXtProti NX_Q99798.
    Orphaneti 313850. Infantile cerebellar-retinal degeneration.
    PharmGKBi PA24443.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1048.
    HOGENOMi HOG000224293.
    HOVERGENi HBG000248.
    KOi K01681.
    OrthoDBi EOG74FF06.
    PhylomeDBi Q99798.
    TreeFami TF300627.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00718 .
    BioCyci MetaCyc:HS02077-MONOMER.
    Reactomei REACT_118595. Mitochondrial protein import.
    REACT_1785. Citric acid cycle (TCA cycle).

    Miscellaneous databases

    ChiTaRSi ACO2. human.
    GenomeRNAii 50.
    NextBioi 195.
    PROi Q99798.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99798.
    Bgeei Q99798.
    CleanExi HS_ACO2.
    Genevestigatori Q99798.

    Family and domain databases

    Gene3Di 3.20.19.10. 1 hit.
    3.30.499.10. 2 hits.
    3.40.1060.10. 1 hit.
    InterProi 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.
    [Graphical view ]
    PANTHERi PTHR11670. PTHR11670. 1 hit.
    Pfami PF00330. Aconitase. 1 hit.
    PF00694. Aconitase_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00415. ACONITASE.
    SUPFAMi SSF52016. SSF52016. 1 hit.
    SSF53732. SSF53732. 1 hit.
    TIGRFAMsi TIGR01340. aconitase_mito. 1 hit.
    PROSITEi PS00450. ACONITASE_1. 1 hit.
    PS01244. ACONITASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and structural characterization of human mitochondrial aconitase."
      Juang H.H., Chiou B.
      Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Skeletal muscle.
    2. "Characterization of the human mitochondrial aconitase gene (ACO2)."
      Mirel D.B., Marder K., Graziano J., Freyer G., Zhao Q., Mayeux R., Wilhelmsen K.C.
      Gene 213:205-218(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain and Uterus.
    7. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 69-84; 234-245; 313-323; 379-395; 412-424; 430-437; 507-520; 565-573; 608-628; 634-648 AND 657-671, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    8. "Purification and partial amino acid sequence of human aconitase."
      Baldwin G.S., Seet K.L., Callaghan J., Toncich G., Toh B.H., Moritz R.L., Rubira M.R., Simpson R.
      Protein Seq. Data Anal. 4:63-67(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 69-83; 96-107; 371-396 AND 524-534.
    9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-573 AND LYS-605, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-697.
    13. "Infantile cerebellar-retinal degeneration associated with a mutation in mitochondrial aconitase, ACO2."
      Spiegel R., Pines O., Ta-Shma A., Burak E., Shaag A., Halvardson J., Edvardson S., Mahajna M., Zenvirt S., Saada A., Shalev S., Feuk L., Elpeleg O.
      Am. J. Hum. Genet. 90:518-523(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ICRD ARG-112, CHARACTERIZATION OF VARIANT ICRD ARG-112.

    Entry informationi

    Entry nameiACON_HUMAN
    AccessioniPrimary (citable) accession number: Q99798
    Secondary accession number(s): O75809
    , Q5JZ41, Q6FHX0, Q8TAQ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3