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Reviewed, UniProtKB/Swiss-Prot Q99798 (ACON_HUMAN)

Last modified July 22, 2008. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Aconitate hydratase, mitochondrial
      Short name(s)=Aconitase
    EC=4.2.1.3
Alternative name(s):
    Citrate hydro-lyase
Gene names
Name: ACO2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length780 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Citrate = isocitrate.

Cofactor

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

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle.

Subunit structure

Monomer By similarity.

Subcellular location

MitochondrionBy similarity.

Sequence similarities

Belongs to the aconitase/IPM isomerase family.

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Ontologies

Keywords

   Biological processTricarboxylic acid cycle
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
   Molecular functionLyase
   PTMAcetylation
Pyrrolidone carboxylic acid
Ubl conjugation
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processcitrate metabolic process Ref.2

Inferred from direct assay. Source: MGI

tricarboxylic acid cycle Ref.2

Inferred from direct assay. Source: MGI

   Cellular componentmitochondrial matrix Ref.8

Inferred from Experiment. Source: Reactome

   Molecular functionaconitate hydratase activity Ref.8

Inferred from Experiment. Source: Reactome

iron ion binding Ref.2

Inferred from direct assay. Source: MGI

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Transit peptide1 – 2727Mitochondrion By similarity
Chain28 – 780753Aconitate hydratase, mitochondrial

Sites

Metal binding3851Iron-sulfur (4Fe-4S) By similarity
Metal binding4481Iron-sulfur (4Fe-4S) By similarity
Metal binding4511Iron-sulfur (4Fe-4S) By similarity

Amino acid modifications

Modified residue281Pyrrolidone carboxylic acid By similarity
Modified residue501N6-acetyllysine By similarity
Cross-link144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Natural variant6971T → N in a breast cancer sample; somatic mutation.
Natural variant7681A → S: dbSNP rs1804785.

Experimental info

Sequence conflict351S → T in AAB38416. Ref.1
Sequence conflict1361G → D in AAB38416. Ref.1
Sequence conflict1591A → D in AAB38416. Ref.1
Sequence conflict1671K → S in AAB38416. Ref.1
Sequence conflict1991G → D in CAG38805. Ref.4
Sequence conflict2071G → R in AAH26196. Ref.6
Sequence conflict2421S → T in AAB38416. Ref.1
Sequence conflict2701P → H in AAH26196. Ref.6
Sequence conflict2751I → M in AAB38416. Ref.1
Sequence conflict4441L → P in CAG38805. Ref.4
Sequence conflict5171T → K in AAB38416. Ref.1
Sequence conflict5531G → R in AAB38416. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q99798-1 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 58C9FFBDBDC63D5E

FASTA78085,425
        10         20         30         40         50         60 
MAPYSLLVTR LQKALGVRQY HVASVLCQRA KVAMSHFEPN EYIHYDLLEK NINIVRKRLN 

        70         80         90        100        110        120 
RPLTLSEKIV YGHLDDPASQ EIERGKSYLR LRPDRVAMQD ATAQMAMLQF ISSGLSKVAV 

       130        140        150        160        170        180 
PSTIHCDHLI EAQVGGEKDL RRAKDINQEV YNFLATAGAK YGVGFWKPGS GIIHQIILEN 

       190        200        210        220        230        240 
YAYPGVLLIG TDSHTPNGGG LGGICIGVGG ADAVDVMAGI PWELKCPKVI GVKLTGSLSG 

       250        260        270        280        290        300 
WSSPKDVILK VAGILTVKGG TGAIVEYHGP GVDSISCTGM ATICNMGAEI GATTSVFPYN 

       310        320        330        340        350        360 
HRMKKYLSKT GREDIANLAD EFKDHLVPDP GCHYDQLIEI NLSELKPHIN GPFTPDLAHP 

       370        380        390        400        410        420 
VAEVGKVAEK EGWPLDIRVG LIGSCTNSSY EDMGRSAAVA KQALAHGLKC KSQFTITPGS 

       430        440        450        460        470        480 
EQIRATIERD GYAQILRDLG GIVLANACGP CIGQWDRKDI KKGEKNTIVT SYNRNFTGRN 

       490        500        510        520        530        540 
DANPETHAFV TSPEIVTALA IAGTLKFNPE TDYLTGTDGK KFRLEAPDAD ELPKGEFDPG 

       550        560        570        580        590        600 
QDTYQHPPKD SSGQHVDVSP TSQRLQLLEP FDKWDGKDLE DLQILIKVKG KCTTDHISAA 

       610        620        630        640        650        660 
GPWLKFRGHL DNISNNLLIG AINIENGKAN SVRNAVTQEF GPVPDTARYY KKHGIRWVVI 

       670        680        690        700        710        720 
GDENYGEGSS REHAALEPRH LGGRAIITKS FARIHETNLK KQGLLPLTFA DPADYNKIHP 

       730        740        750        760        770        780 
VDKLTIQGLK DFTPGKPLKC IIKHPNGTQE TILLNHTFNE TQIEWFRAGS ALNRMKELQQ

« Hide

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References

« Hide 'large scale' references
[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: 9630632] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [Abstract]
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. expand/collapse author list , 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: 10591208] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Uterus.
[7]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 69-84; 412-424 AND 634-648, MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[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: 1946331] [Abstract]
Cited for: PROTEIN SEQUENCE OF 69-83; 96-107; 371-396 AND 524-534.
[9]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-697.

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Web resources

Wikipedia

Aconitase entry

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Cross-references

Sequence databases

U80040 mRNA. Translation: AAB38416.1.
U87939 expand/collapse EMBL AC list , 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.
PIRS17526.
T52543.
RefSeqNP_001089.1.
UniGeneHs.643610

3D structure databases

HSSPHSSP built from PDB template 7ACN based on UniProtKB P16276.
SMRQ99798. Positions 29-780.
ModBaseSearch...

PTM databases

PhosphoSiteQ99798.

2-D gel databases

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

Genome annotation databases

EnsemblENSG00000100412. Homo sapiens. [Contig view]
GeneID50.
KEGGhsa:50.
NMPDRfig|9606.3.peg.21789.

Organism-specific databases

H-InvDBHIX0016520.
HIX0056983.
HGNCHGNC:118. ACO2.
HPAHPA001097.
MIM100850. gene.
PharmGKBPA24443.
GenAtlasSearch...
GeneCardsSearch...
GeneLynxSearch...

Phylogenomic databases

HOGENOMQ99798.
HOVERGENQ99798.

Enzyme and pathway databases

ReactomeREACT_1046. Pyruvate metabolism and TCA cycle.

Gene expression databases

ArrayExpressQ99798.
CleanExHS_ACO2.
GermOnlineENSG00000100412. Homo sapiens.

Family and domain databases

InterProIPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015937. Aconitase-like_core.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR006248. Aconitase_mito-like.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
Gene3DG3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 2 hits.
G3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit.
G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
PANTHERPTHR11670. Aconitase-like_core. 1 hit.
PTHR11670:SF5. Aconitase_mito. 1 hit.
PfamPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
ProDomPD000511. Aconitase_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01340. aconitase_mito. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
BLOCKSSearch...

Other Resources

LinkHubQ99798.
SOURCESearch...
ProtoNetSearch...

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Entry information

Entry nameACON_HUMAN
AccessionPrimary (citable) accession number: Q99798
Secondary accession number(s): O75809 expand/collapse secondary AC list , Q5JZ41, Q6FHX0, Q8TAQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: July 22, 2008
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents