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P21399

- ACOC_HUMAN

UniProt

P21399 - ACOC_HUMAN

Protein

Cytoplasmic aconitate hydratase

Gene

ACO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 3 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    Iron sensor. Binds a 4Fe-4S cluster and functions as aconitase when cellular iron levels are high. Functions as mRNA binding protein that regulates uptake, sequestration and utilization of iron when cellular iron levels are low. Binds to iron-responsive elements (IRES) in target mRNA species when iron levels are low. Binding of a 4Fe-4S cluster precludes RNA binding.2 Publications
    Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.By similarity

    Catalytic activityi

    Citrate = isocitrate.

    Cofactori

    Binds 1 4Fe-4S cluster per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei86 – 861SubstrateBy similarity
    Metal bindingi437 – 4371Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi503 – 5031Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi506 – 5061Iron-sulfur (4Fe-4S)By similarity
    Binding sitei536 – 5361SubstrateBy similarity
    Binding sitei541 – 5411SubstrateBy similarity
    Binding sitei699 – 6991SubstrateBy similarity

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB
    2. aconitate hydratase activity Source: UniProtKB
    3. iron-responsive element binding Source: UniProtKB
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: UniProtKB
    6. RNA binding Source: UniProtKB

    GO - Biological processi

    1. cellular iron ion homeostasis Source: Ensembl
    2. citrate metabolic process Source: UniProtKB
    3. intestinal absorption Source: Ensembl
    4. post-embryonic development Source: Ensembl
    5. regulation of translation Source: Ensembl
    6. response to iron(II) ion Source: UniProtKB
    7. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04597-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytoplasmic aconitate hydratase (EC:4.2.1.3)
    Short name:
    Aconitase
    Alternative name(s):
    Citrate hydro-lyase
    Ferritin repressor protein
    Iron regulatory protein 1
    Short name:
    IRP1
    Iron-responsive element-binding protein 1
    Short name:
    IRE-BP 1
    Gene namesi
    Name:ACO1
    Synonyms:IREB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:117. ACO1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: HGNC
    3. endoplasmic reticulum Source: MGI
    4. extracellular vesicular exosome Source: UniProt
    5. Golgi apparatus Source: MGI
    6. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi300 – 3001C → S: No effect on aconitase activity or on RNA binding. 1 Publication
    Mutagenesisi437 – 4371C → S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels. 1 Publication
    Mutagenesisi503 – 5031C → S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels. 1 Publication
    Mutagenesisi506 – 5061C → S: Loss of aconitase activity. Leads of iron levels. 1 Publication
    Mutagenesisi536 – 5361R → Q: Strongly reduced RNA binding. 1 Publication
    Mutagenesisi541 – 5411R → Q: Strongly reduced RNA binding. 1 Publication
    Mutagenesisi699 – 6991R → K: No effect on RNA binding. 1 Publication
    Mutagenesisi778 – 7781S → A: No effect on iron-regulated RNA binding. Loss of aconitase activity. 1 Publication
    Mutagenesisi780 – 7801R → Q: Nearly abolishes RNA binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA24442.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 889889Cytoplasmic aconitate hydratasePRO_0000076680Add
    BLAST

    Proteomic databases

    MaxQBiP21399.
    PaxDbiP21399.
    PeptideAtlasiP21399.
    PRIDEiP21399.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00008485.
    UCD-2DPAGEP21399.

    PTM databases

    PhosphoSiteiP21399.

    Expressioni

    Gene expression databases

    ArrayExpressiP21399.
    BgeeiP21399.
    CleanExiHS_ACO1.
    GenevestigatoriP21399.

    Organism-specific databases

    HPAiHPA019371.
    HPA024157.

    Interactioni

    Subunit structurei

    Interacts (when associated with the 4Fe-4S) with FBXL5. Interacts with frataxin(81-210).4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NEBP209292EBI-2847111,EBI-1049657
    SGCGQ133262EBI-2847111,EBI-5357343

    Protein-protein interaction databases

    BioGridi106564. 13 interactions.
    IntActiP21399. 8 interactions.
    STRINGi9606.ENSP00000309477.

    Structurei

    Secondary structure

    1
    889
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 83
    Beta strandi9 – 124
    Beta strandi20 – 223
    Helixi24 – 274
    Helixi32 – 343
    Helixi37 – 4812
    Beta strandi52 – 554
    Helixi57 – 648
    Helixi66 – 694
    Turni70 – 734
    Beta strandi75 – 784
    Beta strandi81 – 866
    Helixi87 – 10620
    Helixi111 – 1133
    Beta strandi120 – 1234
    Helixi138 – 16326
    Beta strandi167 – 1704
    Helixi177 – 1837
    Beta strandi188 – 1925
    Beta strandi195 – 1984
    Beta strandi200 – 2056
    Helixi206 – 2149
    Beta strandi217 – 2204
    Helixi223 – 2308
    Beta strandi235 – 2384
    Beta strandi242 – 2498
    Helixi257 – 27115
    Beta strandi277 – 2826
    Helixi283 – 2853
    Helixi290 – 2989
    Helixi300 – 3034
    Beta strandi306 – 3094
    Helixi314 – 3229
    Helixi327 – 34014
    Helixi349 – 3513
    Beta strandi356 – 3627
    Helixi363 – 3653
    Beta strandi368 – 3714
    Beta strandi379 – 3813
    Helixi382 – 3843
    Helixi385 – 39410
    Helixi406 – 4083
    Beta strandi412 – 4176
    Beta strandi420 – 4256
    Beta strandi428 – 4347
    Helixi437 – 4404
    Helixi443 – 45816
    Beta strandi467 – 4715
    Helixi476 – 4849
    Helixi488 – 4936
    Beta strandi501 – 5033
    Helixi504 – 5074
    Helixi515 – 52410
    Beta strandi529 – 5357
    Turni539 – 5413
    Beta strandi547 – 5515
    Helixi554 – 56310
    Beta strandi564 – 5663
    Turni570 – 5723
    Beta strandi575 – 5784
    Turni579 – 5813
    Beta strandi582 – 5843
    Helixi586 – 5894
    Helixi593 – 60311
    Helixi606 – 6138
    Turni614 – 6185
    Helixi621 – 6255
    Helixi647 – 6493
    Beta strandi662 – 67110
    Helixi677 – 6804
    Beta strandi688 – 6903
    Helixi691 – 6988
    Helixi703 – 7053
    Helixi710 – 7123
    Helixi716 – 7216
    Turni722 – 7243
    Turni732 – 7343
    Beta strandi735 – 7373
    Beta strandi739 – 7424
    Turni744 – 7463
    Beta strandi749 – 7513
    Helixi752 – 76110
    Beta strandi766 – 7694
    Beta strandi772 – 7743
    Helixi782 – 7898
    Beta strandi792 – 7987
    Helixi802 – 8109
    Beta strandi814 – 8185
    Helixi824 – 8274
    Beta strandi835 – 8373
    Beta strandi848 – 8536
    Beta strandi858 – 8636
    Helixi868 – 8769
    Helixi879 – 88810

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B3XX-ray2.54A2-889[»]
    2B3YX-ray1.85A/B2-889[»]
    ProteinModelPortaliP21399.
    SMRiP21399. Positions 2-889.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21399.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni205 – 2073Substrate bindingBy similarity
    Regioni779 – 7802Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the aconitase/IPM isomerase family.Curated

    Phylogenomic databases

    eggNOGiCOG1048.
    HOGENOMiHOG000025704.
    HOVERGENiHBG052147.
    InParanoidiP21399.
    KOiK01681.
    OMAiSEFSLAH.
    OrthoDBiEOG7CG6Z7.
    PhylomeDBiP21399.
    TreeFamiTF313476.

    Family and domain databases

    Gene3Di3.20.19.10. 1 hit.
    3.30.499.10. 3 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.
    IPR006249. Aconitase/Fe_reg_2.
    IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
    IPR018136. Aconitase_4Fe-4S_BS.
    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.
    TIGRFAMsiTIGR01341. aconitase_1. 1 hit.
    PROSITEiPS00450. ACONITASE_1. 1 hit.
    PS01244. ACONITASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P21399-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNPFAHLAE PLDPVQPGKK FFNLNKLEDS RYGRLPFSIR VLLEAAIRNC    50
    DEFLVKKQDI ENILHWNVTQ HKNIEVPFKP ARVILQDFTG VPAVVDFAAM 100
    RDAVKKLGGD PEKINPVCPA DLVIDHSIQV DFNRRADSLQ KNQDLEFERN 150
    RERFEFLKWG SQAFHNMRII PPGSGIIHQV NLEYLARVVF DQDGYYYPDS 200
    LVGTDSHTTM IDGLGILGWG VGGIEAEAVM LGQPISMVLP QVIGYRLMGK 250
    PHPLVTSTDI VLTITKHLRQ VGVVGKFVEF FGPGVAQLSI ADRATIANMC 300
    PEYGATAAFF PVDEVSITYL VQTGRDEEKL KYIKKYLQAV GMFRDFNDPS 350
    QDPDFTQVVE LDLKTVVPCC SGPKRPQDKV AVSDMKKDFE SCLGAKQGFK 400
    GFQVAPEHHN DHKTFIYDNT EFTLAHGSVV IAAITSCTNT SNPSVMLGAG 450
    LLAKKAVDAG LNVMPYIKTS LSPGSGVVTY YLQESGVMPY LSQLGFDVVG 500
    YGCMTCIGNS GPLPEPVVEA ITQGDLVAVG VLSGNRNFEG RVHPNTRANY 550
    LASPPLVIAY AIAGTIRIDF EKEPLGVNAK GQQVFLKDIW PTRDEIQAVE 600
    RQYVIPGMFK EVYQKIETVN ESWNALATPS DKLFFWNSKS TYIKSPPFFE 650
    NLTLDLQPPK SIVDAYVLLN LGDSVTTDHI SPAGNIARNS PAARYLTNRG 700
    LTPREFNSYG SRRGNDAVMA RGTFANIRLL NRFLNKQAPQ TIHLPSGEIL 750
    DVFDAAERYQ QAGLPLIVLA GKEYGAGSSR DWAAKGPFLL GIKAVLAESY 800
    ERIHRSNLVG MGVIPLEYLP GENADALGLT GQERYTIIIP ENLKPQMKVQ 850
    VKLDTGKTFQ AVMRFDTDVE LTYFLNGGIL NYMIRKMAK 889
    Length:889
    Mass (Da):98,399
    Last modified:July 15, 1998 - v3
    Checksum:iE1A05AF701D46DCB
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti318 – 3181T → M.1 Publication
    VAR_069413
    Natural varianti395 – 3951A → D.
    Corresponds to variant rs3814519 [ dbSNP | Ensembl ].
    VAR_048180
    Natural varianti486 – 4861G → R.
    Corresponds to variant rs34630459 [ dbSNP | Ensembl ].
    VAR_048181

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11559 mRNA. Translation: CAA77651.1.
    DQ496106 Genomic DNA. Translation: ABF47095.1.
    AL161783 Genomic DNA. Translation: CAH72598.1.
    CH471071 Genomic DNA. Translation: EAW58549.1.
    CH471071 Genomic DNA. Translation: EAW58550.1.
    CH471071 Genomic DNA. Translation: EAW58552.1.
    BC018103 mRNA. Translation: AAH18103.1.
    M58510 mRNA. Translation: AAA69900.1.
    CCDSiCCDS6525.1.
    PIRiS26403.
    RefSeqiNP_001265281.1. NM_001278352.1.
    NP_002188.1. NM_002197.2.
    XP_005251533.1. XM_005251476.1.
    UniGeneiHs.567229.

    Genome annotation databases

    EnsembliENST00000309951; ENSP00000309477; ENSG00000122729.
    ENST00000379923; ENSP00000369255; ENSG00000122729.
    GeneIDi48.
    KEGGihsa:48.
    UCSCiuc003zqw.4. human.

    Polymorphism databases

    DMDMi3123225.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Aconitase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11559 mRNA. Translation: CAA77651.1 .
    DQ496106 Genomic DNA. Translation: ABF47095.1 .
    AL161783 Genomic DNA. Translation: CAH72598.1 .
    CH471071 Genomic DNA. Translation: EAW58549.1 .
    CH471071 Genomic DNA. Translation: EAW58550.1 .
    CH471071 Genomic DNA. Translation: EAW58552.1 .
    BC018103 mRNA. Translation: AAH18103.1 .
    M58510 mRNA. Translation: AAA69900.1 .
    CCDSi CCDS6525.1.
    PIRi S26403.
    RefSeqi NP_001265281.1. NM_001278352.1.
    NP_002188.1. NM_002197.2.
    XP_005251533.1. XM_005251476.1.
    UniGenei Hs.567229.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2B3X X-ray 2.54 A 2-889 [» ]
    2B3Y X-ray 1.85 A/B 2-889 [» ]
    ProteinModelPortali P21399.
    SMRi P21399. Positions 2-889.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106564. 13 interactions.
    IntActi P21399. 8 interactions.
    STRINGi 9606.ENSP00000309477.

    PTM databases

    PhosphoSitei P21399.

    Polymorphism databases

    DMDMi 3123225.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00008485.
    UCD-2DPAGE P21399.

    Proteomic databases

    MaxQBi P21399.
    PaxDbi P21399.
    PeptideAtlasi P21399.
    PRIDEi P21399.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309951 ; ENSP00000309477 ; ENSG00000122729 .
    ENST00000379923 ; ENSP00000369255 ; ENSG00000122729 .
    GeneIDi 48.
    KEGGi hsa:48.
    UCSCi uc003zqw.4. human.

    Organism-specific databases

    CTDi 48.
    GeneCardsi GC09P032374.
    HGNCi HGNC:117. ACO1.
    HPAi HPA019371.
    HPA024157.
    MIMi 100880. gene.
    neXtProti NX_P21399.
    PharmGKBi PA24442.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1048.
    HOGENOMi HOG000025704.
    HOVERGENi HBG052147.
    InParanoidi P21399.
    KOi K01681.
    OMAi SEFSLAH.
    OrthoDBi EOG7CG6Z7.
    PhylomeDBi P21399.
    TreeFami TF313476.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS04597-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P21399.
    GenomeRNAii 48.
    NextBioi 187.
    PROi P21399.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21399.
    Bgeei P21399.
    CleanExi HS_ACO1.
    Genevestigatori P21399.

    Family and domain databases

    Gene3Di 3.20.19.10. 1 hit.
    3.30.499.10. 3 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.
    IPR006249. Aconitase/Fe_reg_2.
    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. 1 hit.
    PF00694. Aconitase_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00415. ACONITASE.
    SUPFAMi SSF52016. SSF52016. 1 hit.
    SSF53732. SSF53732. 1 hit.
    TIGRFAMsi TIGR01341. aconitase_1. 1 hit.
    PROSITEi PS00450. ACONITASE_1. 1 hit.
    PS01244. ACONITASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression of active iron regulatory factor from a full-length human cDNA by in vitro transcription/translation."
      Hirling H., Emery-Goodman A., Thompson N., Neupert B., Seiser C., Kuehn L.
      Nucleic Acids Res. 20:33-39(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. NHLBI resequencing and genotyping service (RS&G)
      Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Uterus.
    6. "Cloning of the cDNA encoding an RNA regulatory protein -- the human iron-responsive element-binding protein."
      Rouault T.A., Tang C.K., Kaptain S., Burgess W.H., Haile D.J., Samaniego F., McBride O.W., Harford J.B., Klausner R.D.
      Proc. Natl. Acad. Sci. U.S.A. 87:7958-7962(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-889, RNA-BINDING, PARTIAL PROTEIN SEQUENCE.
    7. "Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase."
      Hentze M.W., Argos P.
      Nucleic Acids Res. 19:1739-1740(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIMILARITY TO ACONITASES AND IPM ISOMERASES.
    8. Cited for: FUNCTION AS AN ACONITASE.
    9. "The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active-site residues in ligand binding and regulation."
      Philpott C.C., Klausner R.D., Rouault T.A.
      Proc. Natl. Acad. Sci. U.S.A. 91:7321-7325(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-300; CYS-437; CYS-503; CYS-506; ARG-536; ARG-541; ARG-699; SER-778 AND ARG-780.
    10. Cited for: UBIQUITINATION, INTERACTION WITH FBXL5.
    11. "An E3 ligase possessing an iron responsive hemerythrin domain is a regulator of iron homeostasis."
      Salahudeen A.A., Thompson J.W., Ruiz J.C., Ma H.-W., Kinch L.N., Li Q., Grishin N.V., Bruick R.K.
      Science 326:722-726(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH FBXL5.
    12. "Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin."
      Condo I., Malisan F., Guccini I., Serio D., Rufini A., Testi R.
      Hum. Mol. Genet. 19:1221-1229(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FRATAXIN(81-210).
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Crystal structure of human iron regulatory protein 1 as cytosolic aconitase."
      Dupuy J., Volbeda A., Carpentier P., Darnault C., Moulis J.-M., Fontecilla-Camps J.C.
      Structure 14:129-139(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER, COFACTOR.
    15. Cited for: VARIANT MET-318.

    Entry informationi

    Entry nameiACOC_HUMAN
    AccessioniPrimary (citable) accession number: P21399
    Secondary accession number(s): D3DRK7, Q14652, Q5VZA7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 155 of the entry and version 3 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3