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Protein

Cytoplasmic aconitate hydratase

Gene

ACO1

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

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

[4Fe-4S] cluster1 PublicationNote: 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. 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
Complete GO annotation...

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.
BRENDAi4.2.1.3. 2681.

Protein family/group databases

MoonProtiP21399.

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 Componenti: 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: UniProtKB
  5. Golgi apparatus Source: MGI
  6. mitochondrion Source: HPA
Complete GO annotation...

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei628 – 6281Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP21399.
PaxDbiP21399.
PeptideAtlasiP21399.
PRIDEiP21399.

2D gel databases

REPRODUCTION-2DPAGEIPI00008485.
UCD-2DPAGEP21399.

PTM databases

PhosphoSiteiP21399.

Expressioni

Gene expression databases

BgeeiP21399.
CleanExiHS_ACO1.
ExpressionAtlasiP21399. baseline and differential.
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. 17 interactions.
IntActiP21399. 9 interactions.
STRINGi9606.ENSP00000309477.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiEHVENLA.
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.
IPR029784. IRE-BP1.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF32. PTHR11670:SF32. 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

        10         20         30         40         50
MSNPFAHLAE PLDPVQPGKK FFNLNKLEDS RYGRLPFSIR VLLEAAIRNC
60 70 80 90 100
DEFLVKKQDI ENILHWNVTQ HKNIEVPFKP ARVILQDFTG VPAVVDFAAM
110 120 130 140 150
RDAVKKLGGD PEKINPVCPA DLVIDHSIQV DFNRRADSLQ KNQDLEFERN
160 170 180 190 200
RERFEFLKWG SQAFHNMRII PPGSGIIHQV NLEYLARVVF DQDGYYYPDS
210 220 230 240 250
LVGTDSHTTM IDGLGILGWG VGGIEAEAVM LGQPISMVLP QVIGYRLMGK
260 270 280 290 300
PHPLVTSTDI VLTITKHLRQ VGVVGKFVEF FGPGVAQLSI ADRATIANMC
310 320 330 340 350
PEYGATAAFF PVDEVSITYL VQTGRDEEKL KYIKKYLQAV GMFRDFNDPS
360 370 380 390 400
QDPDFTQVVE LDLKTVVPCC SGPKRPQDKV AVSDMKKDFE SCLGAKQGFK
410 420 430 440 450
GFQVAPEHHN DHKTFIYDNT EFTLAHGSVV IAAITSCTNT SNPSVMLGAG
460 470 480 490 500
LLAKKAVDAG LNVMPYIKTS LSPGSGVVTY YLQESGVMPY LSQLGFDVVG
510 520 530 540 550
YGCMTCIGNS GPLPEPVVEA ITQGDLVAVG VLSGNRNFEG RVHPNTRANY
560 570 580 590 600
LASPPLVIAY AIAGTIRIDF EKEPLGVNAK GQQVFLKDIW PTRDEIQAVE
610 620 630 640 650
RQYVIPGMFK EVYQKIETVN ESWNALATPS DKLFFWNSKS TYIKSPPFFE
660 670 680 690 700
NLTLDLQPPK SIVDAYVLLN LGDSVTTDHI SPAGNIARNS PAARYLTNRG
710 720 730 740 750
LTPREFNSYG SRRGNDAVMA RGTFANIRLL NRFLNKQAPQ TIHLPSGEIL
760 770 780 790 800
DVFDAAERYQ QAGLPLIVLA GKEYGAGSSR DWAAKGPFLL GIKAVLAESY
810 820 830 840 850
ERIHRSNLVG MGVIPLEYLP GENADALGLT GQERYTIIIP ENLKPQMKVQ
860 870 880
VKLDTGKTFQ AVMRFDTDVE LTYFLNGGIL NYMIRKMAK
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:
EMBLi
GenBanki
DDBJi
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.
ENST00000541043; ENSP00000438733; 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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi106564. 17 interactions.
IntActiP21399. 9 interactions.
STRINGi9606.ENSP00000309477.

Protein family/group databases

MoonProtiP21399.

PTM databases

PhosphoSiteiP21399.

Polymorphism databases

DMDMi3123225.

2D gel databases

REPRODUCTION-2DPAGEIPI00008485.
UCD-2DPAGEP21399.

Proteomic databases

MaxQBiP21399.
PaxDbiP21399.
PeptideAtlasiP21399.
PRIDEiP21399.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309951; ENSP00000309477; ENSG00000122729.
ENST00000379923; ENSP00000369255; ENSG00000122729.
ENST00000541043; ENSP00000438733; ENSG00000122729.
GeneIDi48.
KEGGihsa:48.
UCSCiuc003zqw.4. human.

Organism-specific databases

CTDi48.
GeneCardsiGC09P032374.
HGNCiHGNC:117. ACO1.
HPAiHPA019371.
HPA024157.
MIMi100880. gene.
neXtProtiNX_P21399.
PharmGKBiPA24442.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciMetaCyc:HS04597-MONOMER.
BRENDAi4.2.1.3. 2681.

Miscellaneous databases

ChiTaRSiACO1. human.
EvolutionaryTraceiP21399.
GenomeRNAii48.
NextBioi187.
PROiP21399.
SOURCEiSearch...

Gene expression databases

BgeeiP21399.
CleanExiHS_ACO1.
ExpressionAtlasiP21399. baseline and differential.
GenevestigatoriP21399.

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.
IPR029784. IRE-BP1.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF32. PTHR11670:SF32. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. NHLBI resequencing and genotyping service (RS&G)
    Submitted (MAR-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(2003) [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(2003) [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(1989) [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(1990) [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(1993) [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(2008) [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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FRATAXIN(81-210).
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-628, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER, COFACTOR.
  16. 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: April 1, 2015
This is version 160 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

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.