Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Cytoplasmic aconitate hydratase (Aconitase) (EC 4.2.1.3) (Citrate hydro-lyase) (Ferritin repressor protein) (Iron regulatory protein 1) (IRP1) (Iron-responsive element-binding protein 1) (IRE-BP 1)

 ACOC_HUMAN              Reviewed;         889 AA.
P21399; D3DRK7; Q14652; Q5VZA7;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 3.
22-NOV-2017, entry version 186.
RecName: Full=Cytoplasmic aconitate hydratase;
Short=Aconitase;
EC=4.2.1.3;
AltName: Full=Citrate hydro-lyase;
AltName: Full=Ferritin repressor protein;
AltName: Full=Iron regulatory protein 1;
Short=IRP1;
AltName: Full=Iron-responsive element-binding protein 1;
Short=IRE-BP 1;
Name=ACO1; Synonyms=IREB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1738601; DOI=10.1093/nar/20.1.33;
Hirling H., Emery-Goodman A., Thompson N., Neupert B., Seiser C.,
Kuehn L.;
"Expression of active iron regulatory factor from a full-length human
cDNA by in vitro transcription/translation.";
Nucleic Acids Res. 20:33-39(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
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.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 74-889, RNA-BINDING, AND PARTIAL PROTEIN
SEQUENCE.
PubMed=2172968; DOI=10.1073/pnas.87.20.7958;
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.;
"Cloning of the cDNA encoding an RNA regulatory protein -- the human
iron-responsive element-binding protein.";
Proc. Natl. Acad. Sci. U.S.A. 87:7958-7962(1990).
[7]
SIMILARITY TO ACONITASES AND IPM ISOMERASES.
PubMed=1903202; DOI=10.1093/nar/19.8.1739;
Hentze M.W., Argos P.;
"Homology between IRE-BP, a regulatory RNA-binding protein, aconitase,
and isopropylmalate isomerase.";
Nucleic Acids Res. 19:1739-1740(1991).
[8]
FUNCTION AS AN ACONITASE.
PubMed=1946430; DOI=10.1073/pnas.88.22.10109;
Kaptain S., Downey W.E., Tang C.K., Philpott C., Haile D.J.,
Orloff D.G., Harford J.B., Rouault T.A., Klausner R.D.;
"A regulated RNA binding protein also possesses aconitase activity.";
Proc. Natl. Acad. Sci. U.S.A. 88:10109-10113(1991).
[9]
FUNCTION, AND MUTAGENESIS OF CYS-300; CYS-437; CYS-503; CYS-506;
ARG-536; ARG-541; ARG-699; SER-778 AND ARG-780.
PubMed=8041788; DOI=10.1073/pnas.91.15.7321;
Philpott C.C., Klausner R.D., Rouault T.A.;
"The bifunctional iron-responsive element binding protein/cytosolic
aconitase: the role of active-site residues in ligand binding and
regulation.";
Proc. Natl. Acad. Sci. U.S.A. 91:7321-7325(1994).
[10]
UBIQUITINATION, AND INTERACTION WITH FBXL5.
PubMed=19762596; DOI=10.1126/science.1176333;
Vashisht A.A., Zumbrennen K.B., Huang X., Powers D.N., Durazo A.,
Sun D., Bhaskaran N., Persson A., Uhlen M., Sangfelt O., Spruck C.,
Leibold E.A., Wohlschlegel J.A.;
"Control of iron homeostasis by an iron-regulated ubiquitin ligase.";
Science 326:718-721(2009).
[11]
UBIQUITINATION, AND INTERACTION WITH FBXL5.
PubMed=19762597; DOI=10.1126/science.1176326;
Salahudeen A.A., Thompson J.W., Ruiz J.C., Ma H.-W., Kinch L.N.,
Li Q., Grishin N.V., Bruick R.K.;
"An E3 ligase possessing an iron responsive hemerythrin domain is a
regulator of iron homeostasis.";
Science 326:722-726(2009).
[12]
INTERACTION WITH FRATAXIN(81-210).
PubMed=20053667; DOI=10.1093/hmg/ddp592;
Condo I., Malisan F., Guccini I., Serio D., Rufini A., Testi R.;
"Molecular control of the cytosolic aconitase/IRP1 switch by
extramitochondrial frataxin.";
Hum. Mol. Genet. 19:1221-1229(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-628, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
CLUSTER, AND COFACTOR.
PubMed=16407072; DOI=10.1016/j.str.2005.09.009;
Dupuy J., Volbeda A., Carpentier P., Darnault C., Moulis J.-M.,
Fontecilla-Camps J.C.;
"Crystal structure of human iron regulatory protein 1 as cytosolic
aconitase.";
Structure 14:129-139(2006).
[16]
VARIANT MET-318.
PubMed=23033978; DOI=10.1056/NEJMoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
Brunner H.G., Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:1946430, ECO:0000269|PubMed:8041788}.
-!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via
cis-aconitate. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Citrate = isocitrate.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000269|PubMed:16407072};
Note=Binds 1 [4Fe-4S] cluster per subunit.
{ECO:0000269|PubMed:16407072};
-!- SUBUNIT: Interacts (when associated with the 4Fe-4S) with FBXL5.
Interacts with frataxin(81-210). {ECO:0000269|PubMed:16407072,
ECO:0000269|PubMed:19762596, ECO:0000269|PubMed:19762597,
ECO:0000269|PubMed:20053667}.
-!- INTERACTION:
P20929:NEB; NbExp=2; IntAct=EBI-2847111, EBI-1049657;
Q13326:SGCG; NbExp=2; IntAct=EBI-2847111, EBI-5357343;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Aconitase entry;
URL="https://en.wikipedia.org/wiki/Aconitase";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z11559; CAA77651.1; -; mRNA.
EMBL; DQ496106; ABF47095.1; -; Genomic_DNA.
EMBL; AL161783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471071; EAW58549.1; -; Genomic_DNA.
EMBL; CH471071; EAW58550.1; -; Genomic_DNA.
EMBL; CH471071; EAW58552.1; -; Genomic_DNA.
EMBL; BC018103; AAH18103.1; -; mRNA.
EMBL; M58510; AAA69900.1; -; mRNA.
CCDS; CCDS6525.1; -.
PIR; S26403; S26403.
RefSeq; NP_001265281.1; NM_001278352.1.
RefSeq; NP_002188.1; NM_002197.2.
RefSeq; XP_005251533.1; XM_005251476.1.
RefSeq; XP_011516190.1; XM_011517888.1.
UniGene; Hs.567229; -.
PDB; 2B3X; X-ray; 2.54 A; A=2-889.
PDB; 2B3Y; X-ray; 1.85 A; A/B=2-889.
PDBsum; 2B3X; -.
PDBsum; 2B3Y; -.
ProteinModelPortal; P21399; -.
SMR; P21399; -.
BioGrid; 106564; 18.
IntAct; P21399; 9.
STRING; 9606.ENSP00000309477; -.
DrugBank; DB06757; Manganese.
MoonProt; P21399; -.
iPTMnet; P21399; -.
PhosphoSitePlus; P21399; -.
SwissPalm; P21399; -.
BioMuta; ACO1; -.
DMDM; 3123225; -.
REPRODUCTION-2DPAGE; IPI00008485; -.
UCD-2DPAGE; P21399; -.
EPD; P21399; -.
PaxDb; P21399; -.
PeptideAtlas; P21399; -.
PRIDE; P21399; -.
Ensembl; ENST00000309951; ENSP00000309477; ENSG00000122729.
Ensembl; ENST00000379923; ENSP00000369255; ENSG00000122729.
Ensembl; ENST00000541043; ENSP00000438733; ENSG00000122729.
GeneID; 48; -.
KEGG; hsa:48; -.
CTD; 48; -.
DisGeNET; 48; -.
EuPathDB; HostDB:ENSG00000122729.18; -.
GeneCards; ACO1; -.
HGNC; HGNC:117; ACO1.
HPA; HPA019371; -.
HPA; HPA024157; -.
MIM; 100880; gene.
neXtProt; NX_P21399; -.
OpenTargets; ENSG00000122729; -.
PharmGKB; PA24442; -.
eggNOG; KOG0452; Eukaryota.
eggNOG; COG1048; LUCA.
GeneTree; ENSGT00890000139397; -.
HOGENOM; HOG000025704; -.
HOVERGEN; HBG052147; -.
InParanoid; P21399; -.
KO; K01681; -.
OMA; MRIIPPG; -.
OrthoDB; EOG091G01IX; -.
PhylomeDB; P21399; -.
TreeFam; TF313476; -.
BioCyc; MetaCyc:HS04597-MONOMER; -.
BRENDA; 4.2.1.3; 2681.
Reactome; R-HSA-917937; Iron uptake and transport.
SIGNOR; P21399; -.
ChiTaRS; ACO1; human.
EvolutionaryTrace; P21399; -.
GenomeRNAi; 48; -.
PRO; PR:P21399; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000122729; -.
CleanEx; HS_ACO1; -.
ExpressionAtlas; P21399; baseline and differential.
Genevisible; P21399; HS.
GO; GO:0005737; C:cytoplasm; IMP:CAFA.
GO; GO:0005829; C:cytosol; IDA:HGNC.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IMP:CAFA.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
GO; GO:0003994; F:aconitate hydratase activity; IDA:UniProtKB.
GO; GO:0030350; F:iron-responsive element binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
GO; GO:0006101; P:citrate metabolic process; IDA:UniProtKB.
GO; GO:0050892; P:intestinal absorption; IEA:Ensembl.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0006417; P:regulation of translation; IEA:Ensembl.
GO; GO:0010040; P:response to iron(II) ion; IDA:UniProtKB.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
Gene3D; 3.20.19.10; -; 1.
Gene3D; 3.30.499.10; -; 2.
Gene3D; 3.40.1060.10; -; 1.
InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
InterPro; IPR006249; Aconitase/IRP2.
InterPro; IPR018136; Aconitase_4Fe-4S_BS.
InterPro; IPR036008; Aconitase_4Fe-4S_dom.
InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
InterPro; IPR029784; IRE-BP1.
PANTHER; PTHR11670; PTHR11670; 1.
PANTHER; PTHR11670:SF32; PTHR11670:SF32; 1.
Pfam; PF00330; Aconitase; 1.
Pfam; PF00694; Aconitase_C; 1.
PRINTS; PR00415; ACONITASE.
SUPFAM; SSF53732; SSF53732; 1.
TIGRFAMs; TIGR01341; aconitase_1; 1.
PROSITE; PS00450; ACONITASE_1; 1.
PROSITE; PS01244; ACONITASE_2; 1.
1: Evidence at protein level;
3D-structure; 4Fe-4S; Complete proteome; Cytoplasm;
Direct protein sequencing; Iron; Iron-sulfur; Lyase; Metal-binding;
Phosphoprotein; Polymorphism; Reference proteome; RNA-binding;
Tricarboxylic acid cycle.
CHAIN 1 889 Cytoplasmic aconitate hydratase.
/FTId=PRO_0000076680.
REGION 205 207 Substrate binding. {ECO:0000250}.
REGION 779 780 Substrate binding. {ECO:0000250}.
METAL 437 437 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 503 503 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 506 506 Iron-sulfur (4Fe-4S). {ECO:0000250}.
BINDING 86 86 Substrate. {ECO:0000250}.
BINDING 536 536 Substrate. {ECO:0000250}.
BINDING 541 541 Substrate. {ECO:0000250}.
BINDING 699 699 Substrate. {ECO:0000250}.
MOD_RES 628 628 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
VARIANT 318 318 T -> M (in dbSNP:rs150373174).
{ECO:0000269|PubMed:23033978}.
/FTId=VAR_069413.
VARIANT 395 395 A -> D (in dbSNP:rs3814519).
/FTId=VAR_048180.
VARIANT 486 486 G -> R (in dbSNP:rs34630459).
/FTId=VAR_048181.
MUTAGEN 300 300 C->S: No effect on aconitase activity or
on RNA binding.
{ECO:0000269|PubMed:8041788}.
MUTAGEN 437 437 C->S: Loss of aconitase activity. Leads
to constitutive RNA binding, irrespective
of iron levels.
{ECO:0000269|PubMed:8041788}.
MUTAGEN 503 503 C->S: Loss of aconitase activity. Leads
to constitutive RNA binding, irrespective
of iron levels.
{ECO:0000269|PubMed:8041788}.
MUTAGEN 506 506 C->S: Loss of aconitase activity. Leads
of iron levels.
{ECO:0000269|PubMed:8041788}.
MUTAGEN 536 536 R->Q: Strongly reduced RNA binding.
{ECO:0000269|PubMed:8041788}.
MUTAGEN 541 541 R->Q: Strongly reduced RNA binding.
{ECO:0000269|PubMed:8041788}.
MUTAGEN 699 699 R->K: No effect on RNA binding.
{ECO:0000269|PubMed:8041788}.
MUTAGEN 778 778 S->A: No effect on iron-regulated RNA
binding. Loss of aconitase activity.
{ECO:0000269|PubMed:8041788}.
MUTAGEN 780 780 R->Q: Nearly abolishes RNA binding.
{ECO:0000269|PubMed:8041788}.
HELIX 6 8 {ECO:0000244|PDB:2B3Y}.
STRAND 9 12 {ECO:0000244|PDB:2B3Y}.
STRAND 20 22 {ECO:0000244|PDB:2B3Y}.
HELIX 24 27 {ECO:0000244|PDB:2B3Y}.
HELIX 32 34 {ECO:0000244|PDB:2B3Y}.
HELIX 37 48 {ECO:0000244|PDB:2B3Y}.
STRAND 52 55 {ECO:0000244|PDB:2B3Y}.
HELIX 57 64 {ECO:0000244|PDB:2B3Y}.
HELIX 66 69 {ECO:0000244|PDB:2B3Y}.
TURN 70 73 {ECO:0000244|PDB:2B3Y}.
STRAND 75 78 {ECO:0000244|PDB:2B3Y}.
STRAND 81 86 {ECO:0000244|PDB:2B3Y}.
HELIX 87 106 {ECO:0000244|PDB:2B3Y}.
HELIX 111 113 {ECO:0000244|PDB:2B3Y}.
STRAND 120 123 {ECO:0000244|PDB:2B3Y}.
HELIX 138 163 {ECO:0000244|PDB:2B3Y}.
STRAND 167 170 {ECO:0000244|PDB:2B3Y}.
HELIX 177 183 {ECO:0000244|PDB:2B3Y}.
STRAND 188 192 {ECO:0000244|PDB:2B3Y}.
STRAND 195 198 {ECO:0000244|PDB:2B3Y}.
STRAND 200 205 {ECO:0000244|PDB:2B3Y}.
HELIX 206 214 {ECO:0000244|PDB:2B3Y}.
STRAND 217 220 {ECO:0000244|PDB:2B3Y}.
HELIX 223 230 {ECO:0000244|PDB:2B3Y}.
STRAND 235 238 {ECO:0000244|PDB:2B3Y}.
STRAND 242 249 {ECO:0000244|PDB:2B3Y}.
HELIX 257 271 {ECO:0000244|PDB:2B3Y}.
STRAND 277 282 {ECO:0000244|PDB:2B3Y}.
HELIX 283 285 {ECO:0000244|PDB:2B3Y}.
HELIX 290 298 {ECO:0000244|PDB:2B3Y}.
HELIX 300 303 {ECO:0000244|PDB:2B3Y}.
STRAND 306 309 {ECO:0000244|PDB:2B3Y}.
HELIX 314 322 {ECO:0000244|PDB:2B3Y}.
HELIX 327 340 {ECO:0000244|PDB:2B3Y}.
HELIX 349 351 {ECO:0000244|PDB:2B3Y}.
STRAND 356 362 {ECO:0000244|PDB:2B3Y}.
HELIX 363 365 {ECO:0000244|PDB:2B3Y}.
STRAND 368 371 {ECO:0000244|PDB:2B3Y}.
STRAND 379 381 {ECO:0000244|PDB:2B3Y}.
HELIX 382 384 {ECO:0000244|PDB:2B3Y}.
HELIX 385 394 {ECO:0000244|PDB:2B3Y}.
HELIX 406 408 {ECO:0000244|PDB:2B3Y}.
STRAND 412 417 {ECO:0000244|PDB:2B3Y}.
STRAND 420 425 {ECO:0000244|PDB:2B3Y}.
STRAND 428 434 {ECO:0000244|PDB:2B3Y}.
HELIX 437 440 {ECO:0000244|PDB:2B3Y}.
HELIX 443 458 {ECO:0000244|PDB:2B3Y}.
STRAND 467 471 {ECO:0000244|PDB:2B3Y}.
HELIX 476 484 {ECO:0000244|PDB:2B3Y}.
HELIX 488 493 {ECO:0000244|PDB:2B3Y}.
STRAND 501 503 {ECO:0000244|PDB:2B3X}.
HELIX 504 507 {ECO:0000244|PDB:2B3Y}.
HELIX 515 524 {ECO:0000244|PDB:2B3Y}.
STRAND 529 535 {ECO:0000244|PDB:2B3Y}.
TURN 539 541 {ECO:0000244|PDB:2B3X}.
STRAND 547 551 {ECO:0000244|PDB:2B3Y}.
HELIX 554 563 {ECO:0000244|PDB:2B3Y}.
STRAND 564 566 {ECO:0000244|PDB:2B3X}.
TURN 570 572 {ECO:0000244|PDB:2B3Y}.
STRAND 575 578 {ECO:0000244|PDB:2B3Y}.
TURN 579 581 {ECO:0000244|PDB:2B3Y}.
STRAND 582 584 {ECO:0000244|PDB:2B3Y}.
HELIX 586 589 {ECO:0000244|PDB:2B3Y}.
HELIX 593 603 {ECO:0000244|PDB:2B3Y}.
HELIX 606 613 {ECO:0000244|PDB:2B3Y}.
TURN 614 618 {ECO:0000244|PDB:2B3Y}.
HELIX 621 625 {ECO:0000244|PDB:2B3Y}.
HELIX 647 649 {ECO:0000244|PDB:2B3Y}.
STRAND 662 671 {ECO:0000244|PDB:2B3Y}.
HELIX 677 680 {ECO:0000244|PDB:2B3Y}.
STRAND 688 690 {ECO:0000244|PDB:2B3Y}.
HELIX 691 698 {ECO:0000244|PDB:2B3Y}.
HELIX 703 705 {ECO:0000244|PDB:2B3Y}.
HELIX 710 712 {ECO:0000244|PDB:2B3Y}.
HELIX 716 721 {ECO:0000244|PDB:2B3Y}.
TURN 722 724 {ECO:0000244|PDB:2B3Y}.
TURN 732 734 {ECO:0000244|PDB:2B3Y}.
STRAND 735 737 {ECO:0000244|PDB:2B3Y}.
STRAND 739 742 {ECO:0000244|PDB:2B3Y}.
TURN 744 746 {ECO:0000244|PDB:2B3Y}.
STRAND 749 751 {ECO:0000244|PDB:2B3Y}.
HELIX 752 761 {ECO:0000244|PDB:2B3Y}.
STRAND 766 769 {ECO:0000244|PDB:2B3Y}.
STRAND 772 774 {ECO:0000244|PDB:2B3Y}.
HELIX 782 789 {ECO:0000244|PDB:2B3Y}.
STRAND 792 798 {ECO:0000244|PDB:2B3Y}.
HELIX 802 810 {ECO:0000244|PDB:2B3Y}.
STRAND 814 818 {ECO:0000244|PDB:2B3Y}.
HELIX 824 827 {ECO:0000244|PDB:2B3Y}.
STRAND 835 837 {ECO:0000244|PDB:2B3Y}.
STRAND 848 853 {ECO:0000244|PDB:2B3Y}.
STRAND 858 863 {ECO:0000244|PDB:2B3Y}.
HELIX 868 876 {ECO:0000244|PDB:2B3Y}.
HELIX 879 888 {ECO:0000244|PDB:2B3Y}.
SEQUENCE 889 AA; 98399 MW; E1A05AF701D46DCB CRC64;
MSNPFAHLAE PLDPVQPGKK FFNLNKLEDS RYGRLPFSIR VLLEAAIRNC DEFLVKKQDI
ENILHWNVTQ HKNIEVPFKP ARVILQDFTG VPAVVDFAAM RDAVKKLGGD PEKINPVCPA
DLVIDHSIQV DFNRRADSLQ KNQDLEFERN RERFEFLKWG SQAFHNMRII PPGSGIIHQV
NLEYLARVVF DQDGYYYPDS LVGTDSHTTM IDGLGILGWG VGGIEAEAVM LGQPISMVLP
QVIGYRLMGK PHPLVTSTDI VLTITKHLRQ VGVVGKFVEF FGPGVAQLSI ADRATIANMC
PEYGATAAFF PVDEVSITYL VQTGRDEEKL KYIKKYLQAV GMFRDFNDPS QDPDFTQVVE
LDLKTVVPCC SGPKRPQDKV AVSDMKKDFE SCLGAKQGFK GFQVAPEHHN DHKTFIYDNT
EFTLAHGSVV IAAITSCTNT SNPSVMLGAG LLAKKAVDAG LNVMPYIKTS LSPGSGVVTY
YLQESGVMPY LSQLGFDVVG YGCMTCIGNS GPLPEPVVEA ITQGDLVAVG VLSGNRNFEG
RVHPNTRANY LASPPLVIAY AIAGTIRIDF EKEPLGVNAK GQQVFLKDIW PTRDEIQAVE
RQYVIPGMFK EVYQKIETVN ESWNALATPS DKLFFWNSKS TYIKSPPFFE NLTLDLQPPK
SIVDAYVLLN LGDSVTTDHI SPAGNIARNS PAARYLTNRG LTPREFNSYG SRRGNDAVMA
RGTFANIRLL NRFLNKQAPQ TIHLPSGEIL DVFDAAERYQ QAGLPLIVLA GKEYGAGSSR
DWAAKGPFLL GIKAVLAESY ERIHRSNLVG MGVIPLEYLP GENADALGLT GQERYTIIIP
ENLKPQMKVQ VKLDTGKTFQ AVMRFDTDVE LTYFLNGGIL NYMIRKMAK


Related products :

Catalog number Product name Quantity
18-003-43581 Iron-responsive element-binding protein 1 - IRE-BP 1; Iron regulatory protein 1; IRP1; Ferritin repressor protein; Aconitate hydratase; EC 4.2.1.3; Citrate hydro-lyase; Aconitase Polyclonal 0.05 mg Aff Pur
29-285 ACO1, also known as iron regulatory element binding protein 1 (IREB1), is a cytosolic protein which binds to iron-responsive elements (IREs). It plays a central role in cellular iron homeostasis. It w 0.05 mg
E1263p ELISA ACO2,Aconitase,Aconitate hydratase, mitochondrial,Citrate hydro-lyase,Pig,Sus scrofa 96T
U1263p CLIA ACO2,Aconitase,Aconitate hydratase, mitochondrial,Citrate hydro-lyase,Pig,Sus scrofa 96T
E1263p ELISA kit ACO2,Aconitase,Aconitate hydratase, mitochondrial,Citrate hydro-lyase,Pig,Sus scrofa 96T
E1263m ELISA Aco2,Aconitase,Aconitate hydratase, mitochondrial,Citrate hydro-lyase,Mouse,Mus musculus 96T
U1263m CLIA Aco2,Aconitase,Aconitate hydratase, mitochondrial,Citrate hydro-lyase,Mouse,Mus musculus 96T
E1263r ELISA Aco2,Aconitase,Aconitate hydratase, mitochondrial,Citrate hydro-lyase,Rat,Rattus norvegicus 96T
E1263b ELISA kit ACO2,Aconitase,Aconitate hydratase, mitochondrial,Bos taurus,Bovine,Citrate hydro-lyase 96T
E1263b ELISA ACO2,Aconitase,Aconitate hydratase, mitochondrial,Bos taurus,Bovine,Citrate hydro-lyase 96T
E1263r ELISA kit Aco2,Aconitase,Aconitate hydratase, mitochondrial,Citrate hydro-lyase,Rat,Rattus norvegicus 96T
E1263m ELISA kit Aco2,Aconitase,Aconitate hydratase, mitochondrial,Citrate hydro-lyase,Mouse,Mus musculus 96T
U1263r CLIA Aco2,Aconitase,Aconitate hydratase, mitochondrial,Citrate hydro-lyase,Rat,Rattus norvegicus 96T
U1263b CLIA ACO2,Aconitase,Aconitate hydratase, mitochondrial,Bos taurus,Bovine,Citrate hydro-lyase 96T
E1263h ELISA ACO2,Aconitase,Aconitate hydratase, mitochondrial,Citrate hydro-lyase,Homo sapiens,Human 96T
E1263h ELISA kit ACO2,Aconitase,Aconitate hydratase, mitochondrial,Citrate hydro-lyase,Homo sapiens,Human 96T
U1263h CLIA ACO2,Aconitase,Aconitate hydratase, mitochondrial,Citrate hydro-lyase,Homo sapiens,Human 96T
E13568h Human Iron Responsive Element Binding Protein 2 EL 96T
EH1527 Iron-responsive element-binding protein 2 Elisa Kit 96T
CSB-EL011813RA Rat Iron-responsive element-binding protein 2(IREB2) ELISA kit 96T
IRF2 IREB2 Gene iron-responsive element binding protein 2
CSB-EL011813PI Pig Iron-responsive element-binding protein 2(IREB2) ELISA kit SpeciesPig 96T
CSB-EL011813MO Mouse Iron-responsive element-binding protein 2(IREB2) ELISA kit 96T
CSB-EL011813HU Human Iron-responsive element-binding protein 2(IREB2) ELISA kit 96T
CSB-EL011813CH Chicken Iron-responsive element-binding protein 2(IREB2) ELISA kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur