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Natural resistance-associated macrophage protein 2 (NRAMP 2) (Divalent cation transporter 1) (Divalent metal transporter 1) (DMT-1) (Solute carrier family 11 member 2)

 NRAM2_HUMAN             Reviewed;         568 AA.
P49281; B3KT08; B4DK84; F5H741; O43288; O60932; O94801; Q498Z5;
Q8IUD7; Q96J35;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
27-SEP-2017, entry version 166.
RecName: Full=Natural resistance-associated macrophage protein 2;
Short=NRAMP 2;
AltName: Full=Divalent cation transporter 1;
AltName: Full=Divalent metal transporter 1;
Short=DMT-1;
AltName: Full=Solute carrier family 11 member 2;
Name=SLC11A2; Synonyms=DCT1, DMT1, NRAMP2; ORFNames=OK/SW-cl.20;
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).
TISSUE=Brain;
PubMed=9464519; DOI=10.1016/S0161-5890(97)00110-7;
Kishi F., Tabuchi M.;
"Complete nucleotide sequence of human NRAMP2 cDNA.";
Mol. Immunol. 34:839-842(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=9790986; DOI=10.1006/bbrc.1998.9415;
Kishi F., Tabuchi M.;
"Human natural resistance-associated macrophage protein 2: gene
cloning and protein identification.";
Biochem. Biophys. Res. Commun. 251:775-783(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), TISSUE
SPECIFICITY, AND VARIANT ILE-435.
PubMed=9642100; DOI=10.1006/bcmd.1998.0186;
Lee P.L., Gelbart T., West C., Halloran C., Beutler E.;
"The human Nramp2 gene: characterization of the gene structure,
alternative splicing, promoter region and polymorphisms.";
Blood Cells Mol. Dis. 24:199-215(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
1-583 (ISOFORM 3), ALTERNATIVE SPLICING (ISOFORMS 2 AND 4), AND TISSUE
SPECIFICITY.
PubMed=12209011; DOI=10.1073/pnas.192423399;
Hubert N., Hentze M.W.;
"Previously uncharacterized isoforms of divalent metal transporter
(DMT)-1: implications for regulation and cellular function.";
Proc. Natl. Acad. Sci. U.S.A. 99:12345-12350(2002).
[5]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
Worthington M.T., Battle E., Luo R.Q.;
"Cloning and functional expression of the full length human NRAMP2
iron transporter.";
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
TISSUE=Brain, Thalamus, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-
reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[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] (ISOFORMS 1 AND 3).
TISSUE=Hypothalamus, and Neuroblastoma;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 58-568 (ISOFORM 1).
TISSUE=Liver;
PubMed=7613023; DOI=10.1007/BF00352405;
Vidal S., Belouchi A.-M., Cellier M., Beatty B., Gros P.;
"Cloning and characterization of a second human NRAMP gene on
chromosome 12q13.";
Mamm. Genome 6:224-230(1995).
[12]
SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, AND MUTAGENESIS OF
TYR-555.
PubMed=12475959; DOI=10.1091/mbc.E02-03-0165;
Tabuchi M., Tanaka N., Nishida-Kitayama J., Ohno H., Kishi F.;
"Alternative splicing regulates the subcellular localization of
divalent metal transporter 1 isoforms.";
Mol. Biol. Cell 13:4371-4387(2002).
[13]
FUNCTION.
PubMed=17109629; DOI=10.1042/BJ20061290;
Mackenzie B., Takanaga H., Hubert N., Rolfs A., Hediger M.A.;
"Functional properties of multiple isoforms of human divalent metal-
ion transporter 1 (DMT1).";
Biochem. J. 403:59-69(2007).
[14]
BIOPHYSICOCHEMICAL PROPERTIES, AND NIFEDIPINE TREATMENT.
PubMed=17293870; DOI=10.1038/nm1542;
Ludwiczek S., Theurl I., Muckenthaler M.U., Jakab M., Mair S.M.,
Theurl M., Kiss J., Paulmichl M., Hentze M.W., Ritter M., Weiss G.;
"Ca2+ channel blockers reverse iron overload by a new mechanism via
divalent metal transporter-1.";
Nat. Med. 13:448-454(2007).
[15]
INTERACTION WITH NDFIP1; NDFIP2 AND WWP2, AND SUBCELLULAR LOCATION.
PubMed=18776082; DOI=10.1182/blood-2008-04-150953;
Foot N.J., Dalton H.E., Shearwin-Whyatt L.M., Dorstyn L., Tan S.S.,
Yang B., Kumar S.;
"Regulation of the divalent metal ion transporter DMT1 and iron
homeostasis by a ubiquitin-dependent mechanism involving Ndfips and
WWP2.";
Blood 112:4268-4275(2008).
[16]
INTERACTION WITH NDFIP1 AND NEDD4L.
PubMed=19706893; DOI=10.1073/pnas.0904880106;
Howitt J., Putz U., Lackovic J., Doan A., Dorstyn L., Cheng H.,
Yang B., Chan-Ling T., Silke J., Kumar S., Tan S.S.;
"Divalent metal transporter 1 (DMT1) regulation by Ndfip1 prevents
metal toxicity in human neurons.";
Proc. Natl. Acad. Sci. U.S.A. 106:15489-15494(2009).
[17]
ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, FUNCTION, AND
GLYCOSYLATION.
PubMed=25491917; DOI=10.1002/cbin.10403;
Yanatori I., Yasui Y., Noguchi Y., Kishi F.;
"Inhibition of iron uptake by ferristatin II is exerted through
internalization of DMT1 at the plasma membrane.";
Cell Biol. Int. 39:427-434(2015).
[18]
SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH COX2 AND TOM6.
PubMed=24448823; DOI=10.1096/fj.13-240564;
Wolff N.A., Ghio A.J., Garrick L.M., Garrick M.D., Zhao L.,
Fenton R.A., Thevenod F.;
"Evidence for mitochondrial localization of divalent metal transporter
1 (DMT1).";
FASEB J. 28:2134-2145(2014).
[19]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-86; ASN-89 AND
MET-265.
PubMed=25326704; DOI=10.1038/nsmb.2904;
Ehrnstorfer I.A., Geertsma E.R., Pardon E., Steyaert J., Dutzler R.;
"Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
for transition-metal ion transport.";
Nat. Struct. Mol. Biol. 21:990-996(2014).
[20]
VARIANT AHMIO1 ASP-399.
PubMed=15459009; DOI=10.1182/blood-2004-07-2966;
Mims M.P., Guan Y., Pospisilova D., Priwitzerova M., Indrak K.,
Ponka P., Divoky V., Prchal J.T.;
"Identification of a human mutation of DMT1 in a patient with
microcytic anemia and iron overload.";
Blood 105:1337-1342(2005).
[21]
VARIANT AHMIO1 CYS-416.
PubMed=16160008; DOI=10.1182/blood-2005-06-2477;
Iolascon A., d'Apolito M., Servedio V., Cimmino F., Piga A.,
Camaschella C.;
"Microcytic anemia and hepatic iron overload in a child with compound
heterozygous mutations in DMT1 (SCL11A2).";
Blood 107:349-354(2006).
[22]
VARIANTS AHMIO1 VAL-114 DEL AND VAL-212.
PubMed=16439678; DOI=10.1182/blood-2005-10-4269;
Beaumont C., Delaunay J., Hetet G., Grandchamp B., de Montalembert M.,
Tchernia G.;
"Two new human DMT1 gene mutations in a patient with microcytic
anemia, low ferritinemia, and liver iron overload.";
Blood 107:4168-4170(2006).
[23]
VARIANT [LARGE SCALE ANALYSIS] THR-48.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Important in metal transport, in particular iron. Can
also transport manganese, cobalt, cadmium, nickel, vanadium and
lead. Involved in apical iron uptake into duodenal enterocytes.
Involved in iron transport from acidified endosomes into the
cytoplasm of erythroid precursor cells. May play an important role
in hepatic iron accumulation and tissue iron distribution. May
serve to import iron into the mitochondria.
{ECO:0000269|PubMed:17109629, ECO:0000269|PubMed:24448823,
ECO:0000269|PubMed:25326704, ECO:0000269|PubMed:25491917}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 5.5-6.5 for Fe(2+) uptake.
{ECO:0000269|PubMed:17293870};
-!- SUBUNIT: Forms a complex with NDFIP1 and NEDD4L, in cortical
neurons, in response to iron and colbalt exposure; this
interaction leads to ubiquitination by NEDD4L and proteasome-
dependent degradation. Interacts with NDFIP2. Interacts with COX2
and TOM6 at the outer mitochondrion membrane.
{ECO:0000269|PubMed:18776082, ECO:0000269|PubMed:19706893,
ECO:0000269|PubMed:24448823}.
-!- INTERACTION:
P00403:MT-CO2; NbExp=2; IntAct=EBI-10828817, EBI-2105756;
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane
{ECO:0000269|PubMed:12475959, ECO:0000269|PubMed:25491917}; Multi-
pass membrane protein {ECO:0000305}. Early endosome
{ECO:0000269|PubMed:12475959}.
-!- SUBCELLULAR LOCATION: Endosome membrane
{ECO:0000269|PubMed:12475959, ECO:0000269|PubMed:18776082,
ECO:0000269|PubMed:25491917}; Multi-pass membrane protein
{ECO:0000269|PubMed:18776082}. Mitochondrion outer membrane
{ECO:0000269|PubMed:24448823}; Multi-pass membrane protein. Cell
membrane {ECO:0000269|PubMed:12475959,
ECO:0000269|PubMed:25326704, ECO:0000269|PubMed:25491917}; Multi-
pass membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=2; Synonyms=Non-IRE, DMT1B;
IsoId=P49281-1; Sequence=Displayed;
Name=1; Synonyms=IRE;
IsoId=P49281-2; Sequence=VSP_003595;
Name=3; Synonyms=1A-IRE;
IsoId=P49281-3; Sequence=VSP_038144, VSP_003595;
Name=4; Synonyms=1A-Non-IRE;
IsoId=P49281-4; Sequence=VSP_038144;
Note=No experimental confirmation available.;
Name=5;
IsoId=P49281-5; Sequence=VSP_046058, VSP_003595;
Note=No experimental confirmation available. Ref.6
(BAG59096/BAH14878) sequences are in conflict in position:
6:Y->S. {ECO:0000305};
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 1 is highly
expressed in brain. Isoform 2 is highly expressed in spleen,
thymus and pancreas. Isoform 3 and isoform 4 are abundantly
expressed in duodenum and kidney. {ECO:0000269|PubMed:12209011,
ECO:0000269|PubMed:9642100}.
-!- PTM: Ubiquitinated by WWP2. {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:25491917}.
-!- DISEASE: Anemia, hypochromic microcytic, with iron overload 1
(AHMIO1) [MIM:206100]: A hematologic disease characterized by
abnormal hemoglobin content in the erythrocytes which are reduced
in size. The disorder is due to an error of iron metabolism that
results in high serum iron, massive hepatic iron deposition, and
absence of sideroblasts and stainable bone marrow iron store.
Despite adequate transferrin-iron complex, delivery of iron to the
erythroid bone marrow is apparently insufficient for the demands
of hemoglobin synthesis. {ECO:0000269|PubMed:15459009,
ECO:0000269|PubMed:16160008, ECO:0000269|PubMed:16439678}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: NRAMP2-mediated iron uptake is markedly stimulated
by nifedipine in a concentration-dependent manner.
-!- SIMILARITY: Belongs to the NRAMP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH02592.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA34374.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AB004857; BAA24933.1; -; mRNA.
EMBL; AB015355; BAA34374.1; ALT_SEQ; Genomic_DNA.
EMBL; AF064482; AAC21460.1; -; Genomic_DNA.
EMBL; AF064476; AAC21460.1; JOINED; Genomic_DNA.
EMBL; AF064477; AAC21460.1; JOINED; Genomic_DNA.
EMBL; AF064478; AAC21460.1; JOINED; Genomic_DNA.
EMBL; AF064479; AAC21460.1; JOINED; Genomic_DNA.
EMBL; AF064480; AAC21460.1; JOINED; Genomic_DNA.
EMBL; AF064481; AAC21460.1; JOINED; Genomic_DNA.
EMBL; AF064483; AAC21461.1; -; Genomic_DNA.
EMBL; AF064476; AAC21461.1; JOINED; Genomic_DNA.
EMBL; AF064477; AAC21461.1; JOINED; Genomic_DNA.
EMBL; AF064478; AAC21461.1; JOINED; Genomic_DNA.
EMBL; AF064479; AAC21461.1; JOINED; Genomic_DNA.
EMBL; AF064480; AAC21461.1; JOINED; Genomic_DNA.
EMBL; AF064481; AAC21461.1; JOINED; Genomic_DNA.
EMBL; AF064482; AAC21461.1; JOINED; Genomic_DNA.
EMBL; AF064484; AAC21459.1; -; mRNA.
EMBL; AJ493662; CAD38517.1; -; mRNA.
EMBL; AF046997; AAC18078.1; -; mRNA.
EMBL; AK094735; BAG52920.1; -; mRNA.
EMBL; AK296445; BAG59096.1; -; mRNA.
EMBL; AK316507; BAH14878.1; -; mRNA.
EMBL; AB062284; BAB93467.1; -; mRNA.
EMBL; AC087884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471111; EAW58159.1; -; Genomic_DNA.
EMBL; BC002592; AAH02592.1; ALT_INIT; mRNA.
EMBL; BC100014; AAI00015.1; -; mRNA.
EMBL; L37347; AAA79219.1; -; mRNA.
CCDS; CCDS53791.1; -. [P49281-5]
CCDS; CCDS53792.1; -. [P49281-1]
CCDS; CCDS53793.1; -. [P49281-3]
CCDS; CCDS8805.1; -. [P49281-2]
PIR; I57022; I57022.
RefSeq; NP_000608.1; NM_000617.2. [P49281-2]
RefSeq; NP_001167596.1; NM_001174125.1. [P49281-3]
RefSeq; NP_001167597.1; NM_001174126.1. [P49281-1]
RefSeq; NP_001167598.1; NM_001174127.1. [P49281-1]
RefSeq; NP_001167599.1; NM_001174128.1. [P49281-2]
RefSeq; NP_001167600.1; NM_001174129.1. [P49281-2]
RefSeq; NP_001167601.1; NM_001174130.1. [P49281-5]
RefSeq; XP_005268968.1; XM_005268911.3. [P49281-4]
RefSeq; XP_011536706.1; XM_011538404.2. [P49281-1]
RefSeq; XP_011536707.1; XM_011538405.2. [P49281-1]
RefSeq; XP_016874844.1; XM_017019355.1. [P49281-1]
UniGene; Hs.505545; -.
PDB; 5F0L; X-ray; 3.20 A; D=545-568.
PDB; 5F0M; X-ray; 3.10 A; D=549-560.
PDB; 5F0P; X-ray; 2.78 A; D=549-560.
PDBsum; 5F0L; -.
PDBsum; 5F0M; -.
PDBsum; 5F0P; -.
ProteinModelPortal; P49281; -.
SMR; P49281; -.
BioGrid; 110950; 7.
DIP; DIP-48957N; -.
IntAct; P49281; 4.
STRING; 9606.ENSP00000378364; -.
BindingDB; P49281; -.
ChEMBL; CHEMBL1932895; -.
GuidetoPHARMACOLOGY; 967; -.
TCDB; 2.A.55.2.1; the metal ion (mn(2+)-iron) transporter (nramp) family.
iPTMnet; P49281; -.
PhosphoSitePlus; P49281; -.
SwissPalm; P49281; -.
BioMuta; SLC11A2; -.
DMDM; 8247934; -.
MaxQB; P49281; -.
PaxDb; P49281; -.
PeptideAtlas; P49281; -.
PRIDE; P49281; -.
DNASU; 4891; -.
Ensembl; ENST00000262051; ENSP00000262051; ENSG00000110911. [P49281-1]
Ensembl; ENST00000262052; ENSP00000262052; ENSG00000110911. [P49281-2]
Ensembl; ENST00000394904; ENSP00000378364; ENSG00000110911. [P49281-3]
Ensembl; ENST00000541174; ENSP00000444542; ENSG00000110911. [P49281-2]
Ensembl; ENST00000545993; ENSP00000442810; ENSG00000110911. [P49281-5]
Ensembl; ENST00000546636; ENSP00000449008; ENSG00000110911. [P49281-1]
Ensembl; ENST00000547198; ENSP00000446769; ENSG00000110911. [P49281-1]
Ensembl; ENST00000547688; ENSP00000449200; ENSG00000110911. [P49281-3]
GeneID; 4891; -.
KEGG; hsa:4891; -.
UCSC; uc001rxc.5; human. [P49281-1]
CTD; 4891; -.
DisGeNET; 4891; -.
EuPathDB; HostDB:ENSG00000110911.14; -.
GeneCards; SLC11A2; -.
HGNC; HGNC:10908; SLC11A2.
HPA; HPA032139; -.
HPA; HPA032140; -.
MalaCards; SLC11A2; -.
MIM; 206100; phenotype.
MIM; 600523; gene.
neXtProt; NX_P49281; -.
OpenTargets; ENSG00000110911; -.
Orphanet; 83642; Microcytic anemia with liver iron overload.
PharmGKB; PA259; -.
eggNOG; KOG1291; Eukaryota.
eggNOG; COG1914; LUCA.
GeneTree; ENSGT00390000006526; -.
HOVERGEN; HBG052665; -.
InParanoid; P49281; -.
KO; K21398; -.
OMA; TFCLAMF; -.
OrthoDB; EOG091G05M9; -.
PhylomeDB; P49281; -.
TreeFam; TF315185; -.
Reactome; R-HSA-425410; Metal ion SLC transporters.
Reactome; R-HSA-917937; Iron uptake and transport.
ChiTaRS; SLC11A2; human.
GeneWiki; DMT1; -.
GenomeRNAi; 4891; -.
PRO; PR:P49281; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000110911; -.
CleanEx; HS_SLC11A2; -.
ExpressionAtlas; P49281; baseline and differential.
Genevisible; P49281; HS.
GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0045178; C:basal part of cell; IDA:UniProtKB.
GO; GO:0031526; C:brush border membrane; ISS:BHF-UCL.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IDA:BHF-UCL.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0070826; C:paraferritin complex; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0005773; C:vacuole; IMP:BHF-UCL.
GO; GO:0046870; F:cadmium ion binding; IDA:UniProtKB.
GO; GO:0015086; F:cadmium ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0005375; F:copper ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0015639; F:ferrous iron uptake transmembrane transporter activity; IMP:UniProtKB.
GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:Ensembl.
GO; GO:0022890; F:inorganic cation transmembrane transporter activity; IGI:UniProtKB.
GO; GO:0005381; F:iron ion transmembrane transporter activity; TAS:Reactome.
GO; GO:0015094; F:lead ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0005384; F:manganese ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0015099; F:nickel cation transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0015295; F:solute:proton symporter activity; IDA:UniProtKB.
GO; GO:0046915; F:transition metal ion transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0015100; F:vanadium ion transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0005385; F:zinc ion transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0070574; P:cadmium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
GO; GO:0006824; P:cobalt ion transport; IDA:UniProtKB.
GO; GO:0006825; P:copper ion transport; IDA:BHF-UCL.
GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
GO; GO:0003032; P:detection of oxygen; IEP:UniProtKB.
GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
GO; GO:0070627; P:ferrous iron import; IDA:UniProtKB.
GO; GO:0015684; P:ferrous iron transport; IDA:BHF-UCL.
GO; GO:0006783; P:heme biosynthetic process; IEA:Ensembl.
GO; GO:0015692; P:lead ion transport; IDA:BHF-UCL.
GO; GO:0007611; P:learning or memory; IEA:Ensembl.
GO; GO:0006828; P:manganese ion transport; IDA:BHF-UCL.
GO; GO:0060586; P:multicellular organismal iron ion homeostasis; IMP:BHF-UCL.
GO; GO:0015675; P:nickel cation transport; IDA:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IEP:UniProtKB.
GO; GO:0010039; P:response to iron ion; IEP:UniProtKB.
GO; GO:0015676; P:vanadium ion transport; IDA:UniProtKB.
HAMAP; MF_00221; NRAMP; 1.
InterPro; IPR001046; NRAMP_fam.
PANTHER; PTHR11706; PTHR11706; 1.
Pfam; PF01566; Nramp; 1.
PRINTS; PR00447; NATRESASSCMP.
TIGRFAMs; TIGR01197; nramp; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disease mutation; Endosome; Glycoprotein; Ion transport; Iron;
Iron transport; Membrane; Mitochondrion; Mitochondrion outer membrane;
Phosphoprotein; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix; Transport; Ubl conjugation.
CHAIN 1 568 Natural resistance-associated macrophage
protein 2.
/FTId=PRO_0000212594.
TOPO_DOM 1 69 Cytoplasmic. {ECO:0000255}.
TRANSMEM 70 90 Helical. {ECO:0000255}.
TOPO_DOM 91 96 Extracellular. {ECO:0000255}.
TRANSMEM 97 117 Helical. {ECO:0000255}.
TOPO_DOM 118 154 Cytoplasmic. {ECO:0000255}.
TRANSMEM 155 175 Helical. {ECO:0000255}.
TOPO_DOM 176 179 Extracellular. {ECO:0000255}.
TRANSMEM 180 200 Helical. {ECO:0000255}.
TOPO_DOM 201 208 Cytoplasmic. {ECO:0000255}.
TRANSMEM 209 229 Helical. {ECO:0000255}.
TOPO_DOM 230 255 Extracellular. {ECO:0000255}.
TRANSMEM 256 276 Helical. {ECO:0000255}.
TOPO_DOM 277 301 Cytoplasmic. {ECO:0000255}.
TRANSMEM 302 322 Helical. {ECO:0000255}.
TOPO_DOM 323 360 Extracellular. {ECO:0000255}.
TRANSMEM 361 381 Helical. {ECO:0000255}.
TOPO_DOM 382 408 Cytoplasmic. {ECO:0000255}.
TRANSMEM 409 429 Helical. {ECO:0000255}.
TOPO_DOM 430 440 Extracellular. {ECO:0000255}.
TRANSMEM 441 461 Helical. {ECO:0000255}.
TOPO_DOM 462 482 Cytoplasmic. {ECO:0000255}.
TRANSMEM 483 503 Helical. {ECO:0000255}.
TOPO_DOM 504 506 Extracellular. {ECO:0000255}.
TRANSMEM 507 527 Helical. {ECO:0000255}.
TOPO_DOM 528 568 Cytoplasmic. {ECO:0000255}.
MOD_RES 564 564 Phosphoserine.
{ECO:0000250|UniProtKB:P49282}.
MOD_RES 567 567 Phosphoserine.
{ECO:0000250|UniProtKB:P49282}.
CARBOHYD 336 336 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 349 349 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 12 MVLGPEQKMSDD -> MSTVDYLN (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046058.
VAR_SEQ 1 1 M -> MRKKQLKTEAAPHCELKSYSKNSATQVSTM (in
isoform 3 and isoform 4).
{ECO:0000303|PubMed:12209011,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_038144.
VAR_SEQ 544 568 CHLGLTAQPELYLLNTMDADSLVSR -> VSISKGLLTEEA
TRGYVK (in isoform 1, isoform 3 and
isoform 5). {ECO:0000303|PubMed:12209011,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7613023,
ECO:0000303|PubMed:9464519,
ECO:0000303|PubMed:9642100}.
/FTId=VSP_003595.
VARIANT 48 48 A -> T (in a colorectal cancer sample;
somatic mutation; dbSNP:rs760028045).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036434.
VARIANT 114 114 Missing (in AHMIO1).
{ECO:0000269|PubMed:16439678}.
/FTId=VAR_033011.
VARIANT 212 212 G -> V (in AHMIO1; dbSNP:rs121918367).
{ECO:0000269|PubMed:16439678}.
/FTId=VAR_033012.
VARIANT 399 399 E -> D (in AHMIO1; increased skipping of
exon 12; dbSNP:rs121918365).
{ECO:0000269|PubMed:15459009}.
/FTId=VAR_033013.
VARIANT 416 416 R -> C (in AHMIO1; dbSNP:rs121918366).
{ECO:0000269|PubMed:16160008}.
/FTId=VAR_033014.
VARIANT 435 435 L -> I (in dbSNP:rs144863268).
{ECO:0000269|PubMed:9642100}.
/FTId=VAR_008882.
MUTAGEN 86 86 D->A: Abolishes ion transport across the
cell membrane.
{ECO:0000269|PubMed:25326704}.
MUTAGEN 89 89 N->A: Decreases affinity for divalent
metal cations. Impairs ion transport
across the cell membrane.
{ECO:0000269|PubMed:25326704}.
MUTAGEN 265 265 M->A: Abolishes ion transport across the
cell membrane.
{ECO:0000269|PubMed:25326704}.
MUTAGEN 555 555 Y->A: Abolishes localization at early
endosomes and leads to localization at
late endosomes and lysosomes.
{ECO:0000269|PubMed:12475959}.
MUTAGEN 557 557 L->A: Abolishes localization at early
endosomes and leads to localization at
late endosomes and lysosomes.
{ECO:0000269|PubMed:12475959}.
CONFLICT 58 59 PE -> GM (in Ref. 11; AAA79219).
{ECO:0000305}.
CONFLICT 81 81 S -> T (in Ref. 11; AAA79219).
{ECO:0000305}.
CONFLICT 119 119 Q -> K (in Ref. 10; AAI00015).
{ECO:0000305}.
CONFLICT 124 124 R -> K (in Ref. 11; AAA79219).
{ECO:0000305}.
CONFLICT 462 463 SL -> YV (in Ref. 11; AAA79219).
{ECO:0000305}.
CONFLICT 476 476 W -> C (in Ref. 11; AAA79219).
{ECO:0000305}.
STRAND 554 556 {ECO:0000244|PDB:5F0P}.
SEQUENCE 568 AA; 62266 MW; 4E45D6A448A23263 CRC64;
MVLGPEQKMS DDSVSGDHGE SASLGNINPA YSNPSLSQSP GDSEEYFATY FNEKISIPEE
EYSCFSFRKL WAFTGPGFLM SIAYLDPGNI ESDLQSGAVA GFKLLWILLL ATLVGLLLQR
LAARLGVVTG LHLAEVCHRQ YPKVPRVILW LMVELAIIGS DMQEVIGSAI AINLLSVGRI
PLWGGVLITI ADTFVFLFLD KYGLRKLEAF FGFLITIMAL TFGYEYVTVK PSQSQVLKGM
FVPSCSGCRT PQIEQAVGIV GAVIMPHNMY LHSALVKSRQ VNRNNKQEVR EANKYFFIES
CIALFVSFII NVFVVSVFAE AFFGKTNEQV VEVCTNTSSP HAGLFPKDNS TLAVDIYKGG
VVLGCYFGPA ALYIWAVGIL AAGQSSTMTG TYSGQFVMEG FLNLKWSRFA RVVLTRSIAI
IPTLLVAVFQ DVEHLTGMND FLNVLQSLQL PFALIPILTF TSLRPVMSDF ANGLGWRIAG
GILVLIICSI NMYFVVVYVR DLGHVALYVV AAVVSVAYLG FVFYLGWQCL IALGMSFLDC
GHTCHLGLTA QPELYLLNTM DADSLVSR


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