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Hereditary hemochromatosis protein (HLA-H)

 HFE_HUMAN               Reviewed;         348 AA.
Q30201; B2CKL0; O75929; O75930; O75931; Q17RT0; Q96KU5; Q96KU6;
Q96KU7; Q96KU8; Q9HC64; Q9HC68; Q9HC70; Q9HC83;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
25-OCT-2017, entry version 189.
RecName: Full=Hereditary hemochromatosis protein;
AltName: Full=HLA-H;
Flags: Precursor;
Name=HFE; Synonyms=HLAH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT HFE1 TYR-282, AND
VARIANT ASP-63.
PubMed=8696333; DOI=10.1038/ng0896-399;
Feder J.N., Gnirke A., Thomas W., Tsuchihashi Z., Ruddy D.A.,
Basava A., Dormishian F., Domingo R. Jr., Ellis M.C. Jr., Fullan A.,
Hinton L.M., Jones N.L., Kimmel B.E., Kronmal G.S., Lauer P.,
Lee V.K., Loeb D.B., Mapa F.A., McClelland E., Meyer N.C.,
Mintier G.A., Moeller N., Moore T., Morikang E., Prass C.E.,
Quintana L., Starnes S.M., Schatzman R.C., Brunke K.J., Drayna D.T.,
Risch N.J., Bacon B.R., Wolff R.K.;
"A novel MHC class I-like gene is mutated in patients with hereditary
haemochromatosis.";
Nat. Genet. 13:399-409(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
PubMed=9149941;
Ruddy D.A., Kronmal G.S., Lee V.K., Mintier G.A., Quintana L.,
Domingo R. Jr., Meyer N.C., Irrinki A., McClelland E.E., Fullan A.,
Mapa F.A., Moore T., Thomas W., Loeb D.B., Harmon C., Tsuchihashi Z.,
Wolff R.K., Schatzman R.C., Feder J.N.;
"A 1.1-Mb transcript map of the hereditary hemochromatosis locus.";
Genome Res. 7:441-456(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=9548560;
DOI=10.1002/(SICI)1097-4644(19980501)69:2<117::AID-JCB3>3.0.CO;2-V;
Albig W., Drabent B., Burmester N., Bode C., Doenecke D.;
"The haemochromatosis candidate gene HFE (HLA-H) of man and mouse is
located in syntenic regions within the histone gene.";
J. Cell. Biochem. 69:117-126(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Gasparini P.;
"Hereditary hemochromatosis genomic structure and organization of HLA-
H gene.";
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4).
PubMed=10079302; DOI=10.1007/s002510050505;
Rhodes D.A., Trowsdale J.;
"Alternate splice variants of the hemochromatosis gene Hfe.";
Immunogenetics 49:357-359(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 7; 8; 9 AND 10).
PubMed=11001625; DOI=10.1006/bcmd.2000.0291;
Thenie A., Orhant M., Gicquel I., Fergelot P., Le Gall J.-Y.,
David V., Mosser J.;
"The HFE gene undergoes alternate splicing processes.";
Blood Cells Mol. Dis. 26:155-162(2000).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 5; 6; 7 AND 11).
PubMed=11358357; DOI=10.1006/bcmd.2000.0346;
Sanchez M., Bruguera M., Rodos J., Oliva R.;
"Complete characterization of the 3' region of the human and mouse
hereditary hemochromatosis HFE gene and detection of novel splicing
forms.";
Blood Cells Mol. Dis. 27:35-43(2001).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-53; ASP-63;
GLN-224 AND TYR-282.
NIEHS SNPs program;
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
[9]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
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).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9465039; DOI=10.1073/pnas.95.4.1472;
Feder J.N., Penny D.M., Irrinki A., Lee V.K., Lebron J.A., Watson N.,
Tsuchihashi Z., Sigal E., Bjorkman P.J., Schatzman R.C.;
"The hemochromatosis gene product complexes with the transferrin
receptor and lowers its affinity for ligand binding.";
Proc. Natl. Acad. Sci. U.S.A. 95:1472-1477(1998).
[12]
INVOLVEMENT IN TFQTL2.
PubMed=19084217; DOI=10.1016/j.ajhg.2008.11.011;
Benyamin B., McRae A.F., Zhu G., Gordon S., Henders A.K., Palotie A.,
Peltonen L., Martin N.G., Montgomery G.W., Whitfield J.B.,
Visscher P.M.;
"Variants in TF and HFE explain approximately 40% of genetic variation
in serum-transferrin levels.";
Am. J. Hum. Genet. 84:60-65(2009).
[13]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 23-297 IN COMPLEX WITH TFR.
PubMed=9546397; DOI=10.1016/S0092-8674(00)81151-4;
Lebron J.A., Bennett M.J., Vaughn D.E., Chirino A.J., Snow P.M.,
Mintier G.A., Feder J.N., Bjorkman P.J.;
"Crystal structure of the hemochromatosis protein HFE and
characterization of its interaction with transferrin receptor.";
Cell 93:111-123(1998).
[14]
3D-STRUCTURE MODELING OF 26-293 IN COMPLEX WITH B2MG.
PubMed=11018711; DOI=10.1016/S0167-4838(00)00126-6;
Dupradeau F., Altenberg-Greulich B., Warin R., Fuentes V., Monti J.,
Rochette J.;
"A 3-dimensional model building by homology of the HFE protein:
molecular consequences and application to antibody development.";
Biochim. Biophys. Acta 1481:213-221(2000).
[15]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 26-297 IN COMPLEX WITH TFR.
PubMed=10638746; DOI=10.1038/47417;
Bennett M.J., Lebron J.A., Bjorkman P.J.;
"Crystal structure of the hereditary haemochromatosis protein HFE
complexed with transferrin receptor.";
Nature 403:46-53(2000).
[16]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[17]
VARIANT HFE1 TYR-282, AND VARIANT ASP-63.
PubMed=9106528;
Carella M., D'Ambrosio L., Totaro A., Grifa A., Valentino M.A.,
Piperno A., Girelli D., Roetto A., Franco B., Gasparini P.,
Camaschella C.;
"Mutation analysis of the HLA-H gene in Italian hemochromatosis
patients.";
Am. J. Hum. Genet. 60:828-832(1997).
[18]
VARIANT HFE1 TYR-282, AND ASSOCIATION WITH PORPHYRIA CUTANEA TARDA.
PubMed=9024376; DOI=10.1016/S0140-6736(96)09436-6;
Roberts A.G., Whatley S.D., Morgan R.R., Worwood M., Elder G.H.;
"Increased frequency of the haemochromatosis Cys282Tyr mutation in
sporadic porphyria cutanea tarda.";
Lancet 349:321-323(1997).
[19]
VARIANT ASP-63.
PubMed=9425935; DOI=10.1002/hep.510270128;
Sampietro M., Piperno A., Lupica L., Arosio C., Vergani A.,
Corbetta N., Malosio I., Mattioli M., Fracanzani A.L.,
Cappellini M.D., Fiorelli G., Fargion S.;
"High prevalence of the His63Asp HFE mutation in Italian patients with
porphyria cutanea tarda.";
Hepatology 27:181-184(1998).
[20]
VARIANT HFE1 TYR-282, AND VARIANT ASP-63.
PubMed=9620340; DOI=10.1002/hep.510270627;
Bonkovsky H.L., Poh-Fitzpatrick M., Pimstone N., Obando J.,
Di Bisceglie A., Tattrie C., Tortorelli K., LeClair P., Mercurio M.G.,
Lambrecht R.W.;
"Porphyria cutanea tarda, hepatitis C, and HFE gene mutations in North
America.";
Hepatology 27:1661-1669(1998).
[21]
VARIANTS HFE1 CYS-65 AND TYR-282, AND VARIANT ASP-63.
PubMed=10194428;
Mura C., Raguenes O., Ferec C.;
"HFE mutations analysis in 711 hemochromatosis probands: evidence for
S65C implication in mild form of hemochromatosis.";
Blood 93:2502-2505(1999).
[22]
VARIANTS HFE1 CYS-65; ARG-93 AND THR-105.
PubMed=10575540; DOI=10.1006/bcmd.1999.0240;
Barton J.C., Sawada-Hirai R., Rothenberg B.E., Acton R.T.;
"Two novel missense mutations of the HFE gene (I105T and G93R) and
identification of the S65C mutation in Alabama hemochromatosis
probands.";
Blood Cells Mol. Dis. 25:147-155(1999).
[23]
VARIANTS HFE1 HIS-127 AND MET-330, AND VARIANTS MET-53; MET-59 AND
ASP-63.
PubMed=10401000; DOI=10.1093/hmg/8.8.1517;
de Villiers J.N.P., Hillermann R., Loubser L., Kotze M.J.;
"Spectrum of mutations in the HFE gene implicated in haemochromatosis
and porphyria.";
Hum. Mol. Genet. 8:1517-1522(1999).
[24]
VARIANT HFE1 TYR-282, AND VARIANT ASP-63.
PubMed=10094552;
DOI=10.1002/(SICI)1098-1004(1999)13:2<154::AID-HUMU8>3.0.CO;2-E;
Merryweather-Clarke A.T., Simonsen H., Shearman J.D., Pointon J.J.,
Norgaard-Pedersen B., Robson K.J.H.;
"A retrospective anonymous pilot study in screening newborns for HFE
mutations in Scandinavian populations.";
Hum. Mutat. 13:154-159(1999).
[25]
VARIANT HFE1 CYS-65.
Fagan E., Payne S.J.;
"A novel missense mutation S65C in the HFE gene with a possible role
in hereditary haemochromatosis.";
Hum. Mutat. 13:507-508(1999).
[26]
VARIANT LYS-277.
PubMed=10612845;
DOI=10.1002/(SICI)1098-1004(200001)15:1<120::AID-HUMU32>3.0.CO;2-B;
Bradbury R., Fagan E., Payne S.J.;
"Two novel polymorphisms (E277K and V212V) in the haemochromatosis
gene HFE.";
Hum. Mutat. 15:120-120(2000).
[27]
VARIANTS ASP-63 AND TYR-282.
PubMed=11069625; DOI=10.1046/j.1523-1747.2000.00148.x;
Brady J.J., Jackson H.A., Roberts A.G., Morgan R.R., Whatley S.D.,
Rowlands G.L., Darby C., Shudell E., Watson R., Paiker J.,
Worwood M.W., Elder G.H.;
"Co-inheritance of mutations in the uroporphyrinogen decarboxylase and
hemochromatosis genes accelerates the onset of porphyria cutanea
tarda.";
J. Invest. Dermatol. 115:868-874(2000).
[28]
VARIANT HFE1 TYR-282, VARIANT ASP-63, AND ASSOCIATION WITH DIABETIC
NEPHROPATHY SUSCEPTIBILITY.
PubMed=11423500; DOI=10.2337/diacare.24.7.1187;
Moczulski D.K., Grzeszczak W., Gawlik B.;
"Role of hemochromatosis C282Y and H63D mutations in HFE gene in
development of type 2 diabetes and diabetic nephropathy.";
Diabetes Care 24:1187-1191(2001).
[29]
VARIANT HFE1 VAL-176.
PubMed=11446670;
Imanishi H., Liu W., Cheng J., Ikeda N., Amuro Y., Hada T.;
"Idiopathic hemochromatosis with the mutation of Ala176Val
heterozygous for HFE gene.";
Intern. Med. 40:479-483(2001).
[30]
VARIANTS HFE1 CYS-65; TYR-282 AND ALA-295.
PubMed=12542741; DOI=10.1034/j.1399-0039.2002.600603.x;
Jones D.C., Young N.T., Pigott C., Fuggle S.V., Barnardo M.C.N.M.,
Marshall S.E., Bunce M.;
"Comprehensive hereditary hemochromatosis genotyping.";
Tissue Antigens 60:481-488(2002).
[31]
VARIANT HFE1 PRO-283, AND CHARACTERIZATION OF VARIANT HFE1 PRO-283.
PubMed=12737937; DOI=10.1016/S1079-9796(03)00036-6;
Le Gac G., Dupradeau F.-Y., Mura C., Jacolot S., Scotet V.,
Esnault G., Mercier A.-Y., Rochette J., Ferec C.;
"Phenotypic expression of the C282Y/Q283P compound heterozygosity in
HFE and molecular modeling of the Q283P mutation effect.";
Blood Cells Mol. Dis. 30:231-237(2003).
[32]
VARIANTS HFE1 CYS-65; CYS-66; GLY-224 AND TYR-282.
PubMed=14633868; DOI=10.1373/clinchem.2003.023440;
Biasiotto G., Belloli S., Ruggeri G., Zanella I., Gerardi G.,
Corrado M., Gobbi E., Albertini A., Arosio P.;
"Identification of new mutations of the HFE, hepcidin, and transferrin
receptor 2 genes by denaturing HPLC analysis of individuals with
biochemical indications of iron overload.";
Clin. Chem. 49:1981-1988(2003).
[33]
VARIANT HFE1 SER-6.
PubMed=12584229; DOI=10.1136/gut.52.3.433;
Wigg A.J., Harley H., Casey G.;
"Heterozygous recipient and donor HFE mutations associated with a
hereditary haemochromatosis phenotype after liver transplantation.";
Gut 52:433-435(2003).
[34]
VARIANT HFE1 ALA-295.
PubMed=15046077;
Bento M.C., Ribeiro M.L., Relvas L.;
"Gene symbol: HFE. Disease: haemochromatosis.";
Hum. Genet. 114:405-405(2004).
[35]
CHARACTERIZATION OF VARIANT HFE1 PRO-283.
PubMed=15965644; DOI=10.1007/s00439-005-1307-y;
Ka C., Le Gac G., Dupradeau F.-Y., Rochette J., Ferec C.;
"The Q283P amino-acid change in HFE leads to structural and functional
consequences similar to those described for the mutated 282Y HFE
protein.";
Hum. Genet. 117:467-475(2005).
[36]
VARIANTS HFE1 ASP-43 AND TYR-282, AND VARIANT ASP-63.
PubMed=18157833; DOI=10.1002/humu.9517;
Dupradeau F.-Y., Pissard S., Coulhon M.-P., Cadet E., Foulon K.,
Fourcade C., Goossens M., Case D.A., Rochette J.;
"An unusual case of hemochromatosis due to a new compound
heterozygosity in HFE (p.[Gly43Asp;His63Asp]+[Cys282Tyr]): structural
implications with respect to binding with transferrin receptor 1.";
Hum. Mutat. 29:206-206(2008).
-!- FUNCTION: Binds to transferrin receptor (TFR) and reduces its
affinity for iron-loaded transferrin.
{ECO:0000269|PubMed:9465039}.
-!- SUBUNIT: Binds TFR through the extracellular domain in a pH-
dependent manner. {ECO:0000269|PubMed:10638746,
ECO:0000269|PubMed:9546397}.
-!- INTERACTION:
P61769:B2M; NbExp=4; IntAct=EBI-1028850, EBI-714718;
P02786:TFRC; NbExp=3; IntAct=EBI-1028850, EBI-355727;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9465039};
Single-pass type I membrane protein {ECO:0000305|PubMed:8696333}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=11;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q30201-1; Sequence=Displayed;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=2; Synonyms=delE2;
IsoId=Q30201-2; Sequence=VSP_003218;
Name=3; Synonyms=del14E4;
IsoId=Q30201-3; Sequence=VSP_003225;
Name=4; Synonyms=delE214E4;
IsoId=Q30201-4; Sequence=VSP_003218, VSP_003225;
Name=5;
IsoId=Q30201-5; Sequence=VSP_003219;
Name=6;
IsoId=Q30201-6; Sequence=VSP_047336, VSP_003220;
Name=7; Synonyms=delE3;
IsoId=Q30201-7; Sequence=VSP_003221;
Name=8; Synonyms=1043-2283del,intron6ins;
IsoId=Q30201-8; Sequence=VSP_003226, VSP_003227;
Name=9; Synonyms=delE3-7;
IsoId=Q30201-9; Sequence=VSP_003223, VSP_003224;
Name=10; Synonyms=562-878del;
IsoId=Q30201-10; Sequence=VSP_003222;
Name=11;
IsoId=Q30201-11; Sequence=VSP_043477, VSP_043478;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in all tissues tested except brain.
-!- POLYMORPHISM: Genetic variations in HFE define the transferrin
serum level quantitative trait locus 2 (TFQTL2) [MIM:614193]. Iron
is essential for biochemical functions such as oxygen transport
and oxidative phosphorylation. Excessive iron can cause iron-
overload-related liver diseases, whereas iron deficiency can lead
to anemia. Iron status can be assessed by measuring the levels of
serum iron, serum transferrin, transferrin saturation with iron,
and serum ferritin.
-!- DISEASE: Hemochromatosis 1 (HFE1) [MIM:235200]: A disorder of iron
metabolism characterized by iron overload. Excess iron is
deposited in a variety of organs leading to their failure, and
resulting in serious illnesses including cirrhosis, hepatomas,
diabetes, cardiomyopathy, arthritis, and hypogonadotropic
hypogonadism. Severe effects of the disease usually do not appear
until after decades of progressive iron loading.
{ECO:0000269|PubMed:10094552, ECO:0000269|PubMed:10194428,
ECO:0000269|PubMed:10401000, ECO:0000269|PubMed:10575540,
ECO:0000269|PubMed:11423500, ECO:0000269|PubMed:11446670,
ECO:0000269|PubMed:12542741, ECO:0000269|PubMed:12584229,
ECO:0000269|PubMed:12737937, ECO:0000269|PubMed:14633868,
ECO:0000269|PubMed:15046077, ECO:0000269|PubMed:15965644,
ECO:0000269|PubMed:18157833, ECO:0000269|PubMed:8696333,
ECO:0000269|PubMed:9024376, ECO:0000269|PubMed:9106528,
ECO:0000269|PubMed:9620340, ECO:0000269|Ref.25}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Variegate porphyria (VP) [MIM:176200]: A form of
porphyria. Porphyrias are inherited defects in the biosynthesis of
heme, resulting in the accumulation and increased excretion of
porphyrins or porphyrin precursors. They are classified as
erythropoietic or hepatic, depending on whether the enzyme
deficiency occurs in red blood cells or in the liver. Variegate
porphyria is the most common form of porphyria in South Africa. It
is characterized by skin hyperpigmentation and hypertrichosis,
abdominal pain, tachycardia, hypertension and neuromuscular
disturbances. High fecal levels of protoporphyrin and
coproporphyrin, increased urine uroporphyrins and iron overload
are typical markers of the disease. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry. Iron overload due to HFE variants is a precipitating or
exacerbating factor in variegate porphyria.
-!- DISEASE: Microvascular complications of diabetes 7 (MVCD7)
[MIM:612635]: Pathological conditions that develop in numerous
tissues and organs as a consequence of diabetes mellitus. They
include diabetic retinopathy, diabetic nephropathy leading to end-
stage renal disease, and diabetic neuropathy. Diabetic retinopathy
remains the major cause of new-onset blindness among diabetic
adults. It is characterized by vascular permeability and increased
tissue ischemia and angiogenesis. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/HFEID44099ch6p22.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/hfe/";
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EMBL; U60319; AAC51823.1; -; mRNA.
EMBL; U91328; AAB82083.1; -; Genomic_DNA.
EMBL; Z92910; CAB07442.1; -; Genomic_DNA.
EMBL; Y09801; CAA70934.1; -; Genomic_DNA.
EMBL; Y09800; CAA70934.1; JOINED; Genomic_DNA.
EMBL; Y09803; CAA70934.1; JOINED; Genomic_DNA.
EMBL; Y09799; CAA70934.1; JOINED; Genomic_DNA.
EMBL; AF079407; AAC62646.1; -; mRNA.
EMBL; AF079408; AAC62647.1; -; mRNA.
EMBL; AF079409; AAC62648.1; -; mRNA.
EMBL; AF115264; AAG29571.1; -; mRNA.
EMBL; AF115265; AAG29572.1; -; mRNA.
EMBL; AF144240; AAG29575.1; -; mRNA.
EMBL; AF144242; AAG29577.1; -; mRNA.
EMBL; AF149804; AAG29342.1; -; mRNA.
EMBL; AJ249335; CAC67792.1; -; mRNA.
EMBL; AJ249336; CAC67793.1; -; mRNA.
EMBL; AJ249337; CAC67794.1; -; mRNA.
EMBL; AJ249338; CAC67795.1; -; mRNA.
EMBL; AJ250635; CAC80805.1; -; mRNA.
EMBL; EU523119; ACB21042.1; -; Genomic_DNA.
EMBL; CH471087; EAW55524.1; -; Genomic_DNA.
EMBL; CH471087; EAW55526.1; -; Genomic_DNA.
EMBL; BC117201; AAI17202.1; -; mRNA.
EMBL; BC117203; AAI17204.1; -; mRNA.
CCDS; CCDS4578.1; -. [Q30201-1]
CCDS; CCDS4579.1; -. [Q30201-7]
CCDS; CCDS4580.1; -. [Q30201-2]
CCDS; CCDS4581.1; -. [Q30201-6]
CCDS; CCDS4582.1; -. [Q30201-11]
CCDS; CCDS47386.1; -. [Q30201-10]
CCDS; CCDS47387.1; -. [Q30201-5]
CCDS; CCDS54974.1; -. [Q30201-3]
CCDS; CCDS54975.1; -. [Q30201-4]
RefSeq; NP_000401.1; NM_000410.3. [Q30201-1]
RefSeq; NP_001287678.1; NM_001300749.1.
RefSeq; NP_620572.1; NM_139003.2. [Q30201-10]
RefSeq; NP_620573.1; NM_139004.2. [Q30201-7]
RefSeq; NP_620575.1; NM_139006.2. [Q30201-3]
RefSeq; NP_620576.1; NM_139007.2. [Q30201-2]
RefSeq; NP_620577.1; NM_139008.2. [Q30201-4]
RefSeq; NP_620578.1; NM_139009.2. [Q30201-5]
RefSeq; NP_620579.1; NM_139010.2. [Q30201-6]
RefSeq; NP_620580.1; NM_139011.2. [Q30201-11]
UniGene; Hs.233325; -.
PDB; 1A6Z; X-ray; 2.60 A; A/C=23-297.
PDB; 1C42; Model; -; A=26-293.
PDB; 1DE4; X-ray; 2.80 A; A/D/G=23-297.
PDBsum; 1A6Z; -.
PDBsum; 1C42; -.
PDBsum; 1DE4; -.
ProteinModelPortal; Q30201; -.
SMR; Q30201; -.
BioGrid; 109325; 95.
DIP; DIP-2737N; -.
IntAct; Q30201; 8.
MINT; MINT-7896047; -.
STRING; 9606.ENSP00000417404; -.
iPTMnet; Q30201; -.
PhosphoSitePlus; Q30201; -.
BioMuta; HFE; -.
DMDM; 2497915; -.
MaxQB; Q30201; -.
PaxDb; Q30201; -.
PeptideAtlas; Q30201; -.
PRIDE; Q30201; -.
TopDownProteomics; Q30201-1; -. [Q30201-1]
DNASU; 3077; -.
Ensembl; ENST00000317896; ENSP00000313776; ENSG00000010704. [Q30201-7]
Ensembl; ENST00000336625; ENSP00000337819; ENSG00000010704. [Q30201-10]
Ensembl; ENST00000349999; ENSP00000259699; ENSG00000010704. [Q30201-2]
Ensembl; ENST00000352392; ENSP00000315936; ENSG00000010704. [Q30201-11]
Ensembl; ENST00000353147; ENSP00000312342; ENSG00000010704. [Q30201-6]
Ensembl; ENST00000357618; ENSP00000417404; ENSG00000010704. [Q30201-1]
Ensembl; ENST00000397022; ENSP00000380217; ENSG00000010704. [Q30201-5]
Ensembl; ENST00000461397; ENSP00000420802; ENSG00000010704. [Q30201-3]
Ensembl; ENST00000488199; ENSP00000420559; ENSG00000010704. [Q30201-4]
GeneID; 3077; -.
KEGG; hsa:3077; -.
UCSC; uc003nfx.2; human. [Q30201-1]
CTD; 3077; -.
DisGeNET; 3077; -.
EuPathDB; HostDB:ENSG00000010704.18; -.
GeneCards; HFE; -.
GeneReviews; HFE; -.
H-InvDB; HIX0025100; -.
HGNC; HGNC:4886; HFE.
HPA; HPA017276; -.
HPA; HPA053470; -.
MalaCards; HFE; -.
MIM; 176200; phenotype.
MIM; 235200; phenotype.
MIM; 612635; phenotype.
MIM; 613609; gene.
MIM; 614193; phenotype.
neXtProt; NX_Q30201; -.
OpenTargets; ENSG00000010704; -.
Orphanet; 139498; Hemochromatosis type 1.
Orphanet; 101330; Porphyria cutanea tarda.
Orphanet; 79473; Porphyria variegata.
PharmGKB; PA29263; -.
eggNOG; ENOG410IFNV; Eukaryota.
eggNOG; ENOG4111CQR; LUCA.
GeneTree; ENSGT00740000114936; -.
HOGENOM; HOG000151270; -.
HOVERGEN; HBG016709; -.
InParanoid; Q30201; -.
OMA; ITMKWLK; -.
OrthoDB; EOG091G0K1X; -.
PhylomeDB; Q30201; -.
TreeFam; TF336617; -.
Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
EvolutionaryTrace; Q30201; -.
GeneWiki; HFE_(gene); -.
GenomeRNAi; 3077; -.
PRO; PR:Q30201; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000010704; -.
ExpressionAtlas; Q30201; baseline and differential.
Genevisible; Q30201; HS.
GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
GO; GO:0045178; C:basal part of cell; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:1990712; C:HFE-transferrin receptor complex; IDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:1990357; C:terminal web; IEA:Ensembl.
GO; GO:0030881; F:beta-2-microglobulin binding; IPI:BHF-UCL.
GO; GO:0039706; F:co-receptor binding; IPI:BHF-UCL.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:1990459; F:transferrin receptor binding; IPI:BHF-UCL.
GO; GO:0006953; P:acute-phase response; IEA:Ensembl.
GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:ProtInc.
GO; GO:0071281; P:cellular response to iron ion; IGI:BHF-UCL.
GO; GO:0010106; P:cellular response to iron ion starvation; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0042446; P:hormone biosynthetic process; IEA:Ensembl.
GO; GO:0055072; P:iron ion homeostasis; IMP:BHF-UCL.
GO; GO:0098711; P:iron ion import across plasma membrane; IDA:UniProtKB.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0060586; P:multicellular organismal iron ion homeostasis; IEA:Ensembl.
GO; GO:1904283; P:negative regulation of antigen processing and presentation of endogenous peptide antigen via MHC class I; IGI:BHF-UCL.
GO; GO:2001186; P:negative regulation of CD8-positive, alpha-beta T cell activation; IGI:BHF-UCL.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IC:BHF-UCL.
GO; GO:2000059; P:negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
GO; GO:2000272; P:negative regulation of receptor activity; IDA:BHF-UCL.
GO; GO:1900121; P:negative regulation of receptor binding; IDA:BHF-UCL.
GO; GO:0002626; P:negative regulation of T cell antigen processing and presentation; IEA:InterPro.
GO; GO:0002725; P:negative regulation of T cell cytokine production; IGI:BHF-UCL.
GO; GO:1904434; P:positive regulation of ferrous iron binding; IGI:BHF-UCL.
GO; GO:1904440; P:positive regulation of ferrous iron import across plasma membrane; IGI:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; ISS:BHF-UCL.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0090277; P:positive regulation of peptide hormone secretion; IMP:BHF-UCL.
GO; GO:0032092; P:positive regulation of protein binding; IGI:BHF-UCL.
GO; GO:2000273; P:positive regulation of receptor activity; IGI:BHF-UCL.
GO; GO:1900122; P:positive regulation of receptor binding; IGI:BHF-UCL.
GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IGI:BHF-UCL.
GO; GO:1904437; P:positive regulation of transferrin receptor binding; IGI:BHF-UCL.
GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
GO; GO:2000008; P:regulation of protein localization to cell surface; IMP:BHF-UCL.
GO; GO:0010039; P:response to iron ion; IMP:BHF-UCL.
GO; GO:1990641; P:response to iron ion starvation; IEA:Ensembl.
GO; GO:0033572; P:transferrin transport; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.30.500.10; -; 1.
InterPro; IPR031092; HFE.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
InterPro; IPR011161; MHC_I-like_Ag-recog.
InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
InterPro; IPR011162; MHC_I/II-like_Ag-recog.
InterPro; IPR001039; MHC_I_a_a1/a2.
PANTHER; PTHR16675:SF172; PTHR16675:SF172; 1.
Pfam; PF07654; C1-set; 1.
Pfam; PF00129; MHC_I; 1.
PRINTS; PR01638; MHCCLASSI.
SMART; SM00407; IGc1; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF54452; SSF54452; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disease mutation; Disulfide bond; Glycoprotein; Ion transport; Iron;
Iron transport; Membrane; Polymorphism; Reference proteome; Signal;
Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 22
CHAIN 23 348 Hereditary hemochromatosis protein.
/FTId=PRO_0000018892.
TOPO_DOM 23 306 Extracellular.
{ECO:0000305|PubMed:9465039}.
TRANSMEM 307 330 Helical. {ECO:0000255}.
TOPO_DOM 331 348 Cytoplasmic.
{ECO:0000305|PubMed:9465039}.
DOMAIN 207 298 Ig-like C1-type.
REGION 23 114 Alpha-1.
REGION 115 205 Alpha-2.
REGION 206 297 Alpha-3.
REGION 298 306 Connecting peptide.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 124 187
DISULFID 225 282
VAR_SEQ 26 114 RSHSLHYLFMGASEQDLGLSLFEALGYVDDQLFVFYDHESR
RVEPRTPWVSSRISSQMWLQLSQSLKGWDHMFTVDFWTIME
NHNHSKE -> Q (in isoform 2 and isoform
4). {ECO:0000303|PubMed:10079302,
ECO:0000303|PubMed:11358357}.
/FTId=VSP_003218.
VAR_SEQ 26 49 RSHSLHYLFMGASEQDLGLSLFEA -> P (in isoform
5). {ECO:0000303|PubMed:11358357}.
/FTId=VSP_003219.
VAR_SEQ 26 26 R -> Q (in isoform 11).
{ECO:0000303|PubMed:11358357}.
/FTId=VSP_043477.
VAR_SEQ 26 26 R -> L (in isoform 6).
{ECO:0000303|PubMed:11358357}.
/FTId=VSP_047336.
VAR_SEQ 27 298 Missing (in isoform 11).
{ECO:0000303|PubMed:11358357}.
/FTId=VSP_043478.
VAR_SEQ 27 206 Missing (in isoform 6).
{ECO:0000303|PubMed:11358357}.
/FTId=VSP_003220.
VAR_SEQ 114 219 Missing (in isoform 10).
{ECO:0000303|PubMed:11001625}.
/FTId=VSP_003222.
VAR_SEQ 114 205 Missing (in isoform 7).
{ECO:0000303|PubMed:11001625,
ECO:0000303|PubMed:11358357}.
/FTId=VSP_003221.
VAR_SEQ 144 161 DHLEFCPDTLDWRAAEPR -> VLQDTIYSSEVSSLGIKF
(in isoform 9).
{ECO:0000303|PubMed:11001625}.
/FTId=VSP_003223.
VAR_SEQ 162 348 Missing (in isoform 9).
{ECO:0000303|PubMed:11001625}.
/FTId=VSP_003224.
VAR_SEQ 207 220 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:10079302}.
/FTId=VSP_003225.
VAR_SEQ 275 276 GE -> KY (in isoform 8).
{ECO:0000303|PubMed:11001625}.
/FTId=VSP_003226.
VAR_SEQ 277 348 Missing (in isoform 8).
{ECO:0000303|PubMed:11001625}.
/FTId=VSP_003227.
VARIANT 6 6 R -> S (in HFE1; dbSNP:rs149342416).
{ECO:0000269|PubMed:12584229}.
/FTId=VAR_042506.
VARIANT 43 43 G -> D (in HFE1; associated with D-63 in
one patient).
{ECO:0000269|PubMed:18157833}.
/FTId=VAR_042507.
VARIANT 53 53 V -> M (in dbSNP:rs28934889).
{ECO:0000269|PubMed:10401000,
ECO:0000269|Ref.8}.
/FTId=VAR_008111.
VARIANT 59 59 V -> M (in dbSNP:rs28934890).
{ECO:0000269|PubMed:10401000}.
/FTId=VAR_008112.
VARIANT 63 63 H -> D (polymorphism associated with
hemochromatosis and variegate porphyria;
increased frequency among patients with
diabetic nephropathy; dbSNP:rs1799945).
{ECO:0000269|PubMed:10094552,
ECO:0000269|PubMed:10194428,
ECO:0000269|PubMed:10401000,
ECO:0000269|PubMed:11069625,
ECO:0000269|PubMed:11423500,
ECO:0000269|PubMed:18157833,
ECO:0000269|PubMed:8696333,
ECO:0000269|PubMed:9106528,
ECO:0000269|PubMed:9425935,
ECO:0000269|PubMed:9620340,
ECO:0000269|Ref.8}.
/FTId=VAR_004396.
VARIANT 65 65 S -> C (in HFE1; mild form;
dbSNP:rs1800730).
{ECO:0000269|PubMed:10194428,
ECO:0000269|PubMed:10575540,
ECO:0000269|PubMed:12542741,
ECO:0000269|PubMed:14633868,
ECO:0000269|Ref.25}.
/FTId=VAR_004397.
VARIANT 66 66 R -> C (in HFE1; dbSNP:rs747739169).
{ECO:0000269|PubMed:14633868}.
/FTId=VAR_042508.
VARIANT 93 93 G -> R (in HFE1; dbSNP:rs28934597).
{ECO:0000269|PubMed:10575540}.
/FTId=VAR_008729.
VARIANT 105 105 I -> T (in HFE1; dbSNP:rs28934596).
{ECO:0000269|PubMed:10575540}.
/FTId=VAR_008730.
VARIANT 127 127 Q -> H (in HFE1; dbSNP:rs28934595).
{ECO:0000269|PubMed:10401000}.
/FTId=VAR_008113.
VARIANT 176 176 A -> V (in HFE1; uncertain pathological
significance).
{ECO:0000269|PubMed:11446670}.
/FTId=VAR_042509.
VARIANT 217 217 T -> I (in dbSNP:rs4986950).
/FTId=VAR_020270.
VARIANT 224 224 R -> G (in HFE1).
{ECO:0000269|PubMed:14633868}.
/FTId=VAR_042510.
VARIANT 224 224 R -> Q (in dbSNP:rs62625346).
{ECO:0000269|Ref.8}.
/FTId=VAR_062279.
VARIANT 277 277 E -> K (rare polymorphism;
dbSNP:rs140080192).
{ECO:0000269|PubMed:10612845}.
/FTId=VAR_008731.
VARIANT 282 282 C -> Y (in HFE1; associated with
susceptibility to porphyria cutanea
tarda; associated with increased serum
transferrin levels; higher frequency in
patients with type 2 diabetes than in
controls; dbSNP:rs1800562).
{ECO:0000269|PubMed:10094552,
ECO:0000269|PubMed:10194428,
ECO:0000269|PubMed:11069625,
ECO:0000269|PubMed:11423500,
ECO:0000269|PubMed:12542741,
ECO:0000269|PubMed:14633868,
ECO:0000269|PubMed:18157833,
ECO:0000269|PubMed:8696333,
ECO:0000269|PubMed:9024376,
ECO:0000269|PubMed:9106528,
ECO:0000269|PubMed:9620340,
ECO:0000269|Ref.8}.
/FTId=VAR_004398.
VARIANT 283 283 Q -> P (in HFE1; destabilizing effect on
the tertiary structure of the protein;
prevents the normal interaction between
HFE and B2M and between HFE and TFRC;
decreases the capacity of HFE to reduce
transferrin-mediated iron uptake;
dbSNP:rs111033563).
{ECO:0000269|PubMed:12737937,
ECO:0000269|PubMed:15965644}.
/FTId=VAR_037304.
VARIANT 295 295 V -> A (in HFE1; dbSNP:rs143175221).
{ECO:0000269|PubMed:12542741,
ECO:0000269|PubMed:15046077}.
/FTId=VAR_042511.
VARIANT 330 330 R -> M (in HFE1; dbSNP:rs111033558).
{ECO:0000269|PubMed:10401000}.
/FTId=VAR_008114.
CONFLICT 230 230 Y -> H (in Ref. 7; AAG29342).
{ECO:0000305}.
CONFLICT 248 248 A -> T (in Ref. 7; AAG29575).
{ECO:0000305}.
CONFLICT 256 256 V -> A (in Ref. 7; AAG29577).
{ECO:0000305}.
CONFLICT 275 275 G -> E (in Ref. 7; AAG29342).
{ECO:0000305}.
CONFLICT 311 311 S -> R (in Ref. 7; AAG29342).
{ECO:0000305}.
CONFLICT 339 339 M -> V (in Ref. 7; AAG29577).
{ECO:0000305}.
STRAND 28 38 {ECO:0000244|PDB:1A6Z}.
STRAND 43 45 {ECO:0000244|PDB:1A6Z}.
STRAND 48 53 {ECO:0000244|PDB:1A6Z}.
STRAND 56 65 {ECO:0000244|PDB:1A6Z}.
STRAND 68 70 {ECO:0000244|PDB:1A6Z}.
HELIX 75 78 {ECO:0000244|PDB:1DE4}.
TURN 79 82 {ECO:0000244|PDB:1A6Z}.
HELIX 83 107 {ECO:0000244|PDB:1A6Z}.
TURN 108 110 {ECO:0000244|PDB:1A6Z}.
STRAND 112 114 {ECO:0000244|PDB:1A6Z}.
STRAND 117 126 {ECO:0000244|PDB:1A6Z}.
STRAND 132 140 {ECO:0000244|PDB:1A6Z}.
STRAND 143 149 {ECO:0000244|PDB:1A6Z}.
HELIX 150 152 {ECO:0000244|PDB:1A6Z}.
STRAND 154 159 {ECO:0000244|PDB:1A6Z}.
HELIX 160 162 {ECO:0000244|PDB:1A6Z}.
HELIX 163 170 {ECO:0000244|PDB:1A6Z}.
HELIX 174 184 {ECO:0000244|PDB:1A6Z}.
HELIX 186 198 {ECO:0000244|PDB:1A6Z}.
TURN 199 201 {ECO:0000244|PDB:1A6Z}.
STRAND 209 216 {ECO:0000244|PDB:1A6Z}.
STRAND 221 233 {ECO:0000244|PDB:1A6Z}.
STRAND 236 241 {ECO:0000244|PDB:1A6Z}.
HELIX 248 250 {ECO:0000244|PDB:1A6Z}.
STRAND 255 258 {ECO:0000244|PDB:1A6Z}.
STRAND 264 272 {ECO:0000244|PDB:1A6Z}.
HELIX 276 279 {ECO:0000244|PDB:1A6Z}.
STRAND 280 285 {ECO:0000244|PDB:1A6Z}.
STRAND 289 291 {ECO:0000244|PDB:1A6Z}.
STRAND 293 296 {ECO:0000244|PDB:1A6Z}.
SEQUENCE 348 AA; 40108 MW; 432EB9A314A55BEA CRC64;
MGPRARPALL LLMLLQTAVL QGRLLRSHSL HYLFMGASEQ DLGLSLFEAL GYVDDQLFVF
YDHESRRVEP RTPWVSSRIS SQMWLQLSQS LKGWDHMFTV DFWTIMENHN HSKESHTLQV
ILGCEMQEDN STEGYWKYGY DGQDHLEFCP DTLDWRAAEP RAWPTKLEWE RHKIRARQNR
AYLERDCPAQ LQQLLELGRG VLDQQVPPLV KVTHHVTSSV TTLRCRALNY YPQNITMKWL
KDKQPMDAKE FEPKDVLPNG DGTYQGWITL AVPPGEEQRY TCQVEHPGLD QPLIVIWEPS
PSGTLVIGVI SGIAVFVVIL FIGILFIILR KRQGSRGAMG HYVLAERE


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