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A2A274

- A2A274_HUMAN

UniProt

A2A274 - A2A274_HUMAN

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Protein
Submitted name: Aconitate hydratase, mitochondrial
Gene
ACO2
Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 1 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Biological processi

  1. metabolic process Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Aconitate hydratase, mitochondrialImported
Gene namesi
Name:ACO2Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:118. ACO2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: HPA
  2. nucleus Source: HPA
Complete GO annotation...

PTM / Processingi

Proteomic databases

PRIDEiA2A274.

Expressioni

Gene expression databases

ArrayExpressiA2A274.

Structurei

3D structure databases

ProteinModelPortaliA2A274.
SMRiA2A274. Positions 29-805.

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000224293.
HOVERGENiHBG000248.
OMAiPLKCIIK.
PhylomeDBiA2A274.

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.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiPF00330. Aconitase. 2 hits.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2A274-1 [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 GVDSISCTGE EGGQATWPLP CAGPDGSPVG 300
SRSGMATICN MGAEIGATTS VFPYNHRMKK YLSKTGREDI ANLADEFKDH 350
LVPDPGCHYD QLIEINLSEL KPHINGPFTP DLAHPVAEVG KVAEKEGWPL 400
DIRVGLIGSC TNSSYEDMGR SAAVAKQALA HGLKCKSQFT ITPGSEQIRA 450
TIERDGYAQI LRDLGGIVLA NACGPCIGQW DRKDIKKGEK NTIVTSYNRN 500
FTGRNDANPE THAFVTSPEI VTALAIAGTL KFNPETDYLT GTDGKKFRLE 550
APDADELPKG EFDPGQDTYQ HPPKDSSGQH VDVSPTSQRL QLLEPFDKWD 600
GKDLEDLQIL IKVKGKCTTD HISAAGPWLK FRGHLDNISN NLLIGAINIE 650
NGKANSVRNA VTQEFGPVPD TARYYKKHGI RWVVIGDENY GEGSSREHAA 700
LEPRHLGGRA IITKSFARIH ETNLKKQGLL PLTFADPADY NKIHPVDKLT 750
IQGLKDFTPG KPLKCIIKHP NGTQETILLN HTFNETQIEW FRAGSALNRM 800
KELQQ 805
Length:805
Mass (Da):87,820
Last modified:February 20, 2007 - v1
Checksum:i8584824DB3C3EAD0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL008582 Genomic DNA. No translation available.
AL023553 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000396512; ENSP00000379769; ENSG00000100412.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL008582 Genomic DNA. No translation available.
AL023553 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortali A2A274.
SMRi A2A274. Positions 29-805.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi A2A274.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000396512 ; ENSP00000379769 ; ENSG00000100412 .

Organism-specific databases

HGNCi HGNC:118. ACO2.
GenAtlasi Search...

Phylogenomic databases

HOGENOMi HOG000224293.
HOVERGENi HBG000248.
OMAi PLKCIIK.
PhylomeDBi A2A274.

Miscellaneous databases

ChiTaRSi ACO2. human.
NextBioi 35460679.

Gene expression databases

ArrayExpressi A2A274.

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.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view ]
PANTHERi PTHR11670. PTHR11670. 1 hit.
Pfami PF00330. Aconitase. 2 hits.
PF00694. Aconitase_C. 1 hit.
[Graphical view ]
PRINTSi PR00415. ACONITASE.
SUPFAMi SSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
PROSITEi PS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiA2A274_HUMAN
AccessioniPrimary (citable) accession number: A2A274
Entry historyi
Integrated into UniProtKB/TrEMBL: February 20, 2007
Last sequence update: February 20, 2007
Last modified: July 9, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Reference proteome

External Data

Dasty 3

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