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Q99798

- ACON_HUMAN

UniProt

Q99798 - ACON_HUMAN

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Protein

Aconitate hydratase, mitochondrial

Gene
ACO2
Organism
Homo sapiens (Human)
Status
Reviewed - 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

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 – 991Substrate By 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 – 4741Substrate By similarity
Binding sitei479 – 4791Substrate By similarity
Binding sitei607 – 6071Substrate By 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
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: UniProt
  3. nucleus Source: HPA
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 – 2727Mitochondrion By similarityAdd
BLAST
Chaini28 – 780753Aconitate hydratase, mitochondrialPRO_0000000541Add
BLAST

Amino acid modifications

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

Family & Domainsi

Region

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

Sequence similaritiesi

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

« Hide

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

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 conflict

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

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

« 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. 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: September 3, 2014
This is version 151 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

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