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Protein

Aconitate hydratase, mitochondrial

Gene

ACO2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Citrate = isocitrate.

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster per subunit. Binding of a [3Fe-4S] cluster leads to an inactive enzyme.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. cellular metabolic process Source: Reactome
  2. citrate metabolic process Source: MGI
  3. generation of precursor metabolites and energy Source: ProtInc
  4. isocitrate metabolic process Source: Ensembl
  5. small molecule metabolic process Source: Reactome
  6. tricarboxylic acid cycle Source: MGI
Complete GO annotation...

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: UniProtKB
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Infantile cerebellar-retinal degeneration1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:614559
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

BgeeiQ99798.
CleanExiHS_ACO2.
ExpressionAtlasiQ99798. baseline and differential.
GenevestigatoriQ99798.

Organism-specific databases

HPAiHPA001097.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi106566. 17 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.
GeneTreeiENSGT00760000119287.
HOGENOMiHOG000224293.
HOVERGENiHBG000248.
InParanoidiQ99798.
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

« Hide

        10         20         30         40         50
MAPYSLLVTR LQKALGVRQY HVASVLCQRA KVAMSHFEPN EYIHYDLLEK
60 70 80 90 100
NINIVRKRLN RPLTLSEKIV YGHLDDPASQ EIERGKSYLR LRPDRVAMQD
110 120 130 140 150
ATAQMAMLQF ISSGLSKVAV PSTIHCDHLI EAQVGGEKDL RRAKDINQEV
160 170 180 190 200
YNFLATAGAK YGVGFWKPGS GIIHQIILEN YAYPGVLLIG TDSHTPNGGG
210 220 230 240 250
LGGICIGVGG ADAVDVMAGI PWELKCPKVI GVKLTGSLSG WSSPKDVILK
260 270 280 290 300
VAGILTVKGG TGAIVEYHGP GVDSISCTGM ATICNMGAEI GATTSVFPYN
310 320 330 340 350
HRMKKYLSKT GREDIANLAD EFKDHLVPDP GCHYDQLIEI NLSELKPHIN
360 370 380 390 400
GPFTPDLAHP VAEVGKVAEK EGWPLDIRVG LIGSCTNSSY EDMGRSAAVA
410 420 430 440 450
KQALAHGLKC KSQFTITPGS EQIRATIERD GYAQILRDLG GIVLANACGP
460 470 480 490 500
CIGQWDRKDI KKGEKNTIVT SYNRNFTGRN DANPETHAFV TSPEIVTALA
510 520 530 540 550
IAGTLKFNPE TDYLTGTDGK KFRLEAPDAD ELPKGEFDPG QDTYQHPPKD
560 570 580 590 600
SSGQHVDVSP TSQRLQLLEP FDKWDGKDLE DLQILIKVKG KCTTDHISAA
610 620 630 640 650
GPWLKFRGHL DNISNNLLIG AINIENGKAN SVRNAVTQEF GPVPDTARYY
660 670 680 690 700
KKHGIRWVVI GDENYGEGSS REHAALEPRH LGGRAIITKS FARIHETNLK
710 720 730 740 750
KQGLLPLTFA DPADYNKIHP VDKLTIQGLK DFTPGKPLKC IIKHPNGTQE
760 770 780
TILLNHTFNE TQIEWFRAGS ALNRMKELQQ
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 (Ref. 1) Curated
Sequence conflicti136 – 1361G → D in AAB38416 (Ref. 1) Curated
Sequence conflicti159 – 1591A → D in AAB38416 (Ref. 1) Curated
Sequence conflicti167 – 1671K → S in AAB38416 (Ref. 1) Curated
Sequence conflicti199 – 1991G → D in CAG38805 (Ref. 4) Curated
Sequence conflicti207 – 2071G → R in AAH26196 (PubMed:15489334).Curated
Sequence conflicti242 – 2421S → T in AAB38416 (Ref. 1) Curated
Sequence conflicti270 – 2701P → H in AAH26196 (PubMed:15489334).Curated
Sequence conflicti275 – 2751I → M in AAB38416 (Ref. 1) Curated
Sequence conflicti444 – 4441L → P in CAG38805 (Ref. 4) Curated
Sequence conflicti517 – 5171T → K in AAB38416 (Ref. 1) Curated
Sequence conflicti553 – 5531G → R in AAB38416 (Ref. 1) Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi106566. 17 interactions.
IntActiQ99798. 2 interactions.
MINTiMINT-2856402.
STRINGi9606.ENSP00000216254.

PTM databases

PhosphoSiteiQ99798.

Polymorphism databases

DMDMi6686275.

2D gel databases

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

Proteomic databases

MaxQBiQ99798.
PaxDbiQ99798.
PRIDEiQ99798.

Protocols and materials databases

DNASUi50.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi50.
GeneCardsiGC22P041865.
HGNCiHGNC:118. ACO2.
HPAiHPA001097.
MIMi100850. gene.
614559. phenotype.
neXtProtiNX_Q99798.
Orphaneti313850. Infantile cerebellar-retinal degeneration.
PharmGKBiPA24443.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1048.
GeneTreeiENSGT00760000119287.
HOGENOMiHOG000224293.
HOVERGENiHBG000248.
InParanoidiQ99798.
KOiK01681.
OrthoDBiEOG74FF06.
PhylomeDBiQ99798.
TreeFamiTF300627.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiACO2. human.
GenomeRNAii50.
NextBioi195.
PROiQ99798.
SOURCEiSearch...

Gene expression databases

BgeeiQ99798.
CleanExiHS_ACO2.
ExpressionAtlasiQ99798. baseline and differential.
GenevestigatoriQ99798.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-697.
  14. "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: March 4, 2015
This is version 156 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.