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P21399

- ACOC_HUMAN

UniProt

P21399 - ACOC_HUMAN

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Protein

Cytoplasmic aconitate hydratase

Gene
ACO1, IREB1
Organism
Homo sapiens (Human)
Status
Reviewed - 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.2 Publications

Catalytic activityi

Citrate = isocitrate.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei86 – 861Substrate By 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 – 5361Substrate By similarity
Binding sitei541 – 5411Substrate By similarity
Binding sitei699 – 6991Substrate By 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
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.

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
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

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).3 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.

Miscellaneous databases

EvolutionaryTraceiP21399.

Family & Domainsi

Region

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

Sequence similaritiesi

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

« 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(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: September 3, 2014
This is version 154 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

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