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Lysosome-associated membrane glycoprotein 2 (LAMP-2) (Lysosome-associated membrane protein 2) (CD107 antigen-like family member B) (LGP-96) (CD antigen CD107b)

 LAMP2_HUMAN             Reviewed;         410 AA.
P13473; A8K4X5; D3DTF0; Q16641; Q6Q3G8; Q96J30; Q99534; Q9UD93;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
27-SEP-2017, entry version 192.
RecName: Full=Lysosome-associated membrane glycoprotein 2;
Short=LAMP-2;
Short=Lysosome-associated membrane protein 2;
AltName: Full=CD107 antigen-like family member B;
AltName: Full=LGP-96 {ECO:0000303|PubMed:8662539};
AltName: CD_antigen=CD107b;
Flags: Precursor;
Name=LAMP2;
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 LAMP-2A), AND PROTEIN SEQUENCE OF
29-64; 216-223 AND 238-256.
PubMed=3198605;
Fukuda M., Viitala J., Matteson J., Carlsson S.R.;
"Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-
lamp-1 and h-lamp-2. Comparison of their deduced amino acid
sequences.";
J. Biol. Chem. 263:18920-18928(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LAMP-2A).
TISSUE=Placenta;
PubMed=8517882;
Sawada R., Jardine K.A., Fukuda M.;
"The genes of major lysosomal membrane glycoproteins, lamp-1 and lamp-
2. 5'-flanking sequence of lamp-2 gene and comparison of exon
organization in two genes.";
J. Biol. Chem. 268:9014-9022(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LAMP-2B).
TISSUE=Fibroblast;
PubMed=8407947;
Fritz G., Dosch J., Thielmann H.W., Kaina B.;
"Molecular and cellular characterization of Mex-/methylation-resistant
phenotype. Gene and cDNA cloning, serum dependence, and tumor
suppression of transfectant strains.";
J. Biol. Chem. 268:21102-21112(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LAMP-2A).
TISSUE=Liver;
PubMed=7999007; DOI=10.1006/bbrc.1994.2620;
Konecki D.S., Foetisch K., Schlotter M., Lichter-Konecki U.;
"Complete cDNA sequence of human lysosome-associated membrane protein-
2.";
Biochem. Biophys. Res. Commun. 205:1-5(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LAMP-2B), AND TISSUE SPECIFICITY.
PubMed=7488019; DOI=10.1006/bbrc.1995.2528;
Konecki D.S., Foetisch K., Zimmer K.P., Schlotter M.,
Lichter-Konecki U.;
"An alternatively spliced form of the human lysosome-associated
membrane protein-2 gene is expressed in a tissue-specific manner.";
Biochem. Biophys. Res. Commun. 215:757-767(1995).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LAMP-2C).
Zhou D., Blum J.S.;
"Lamp-2 isoforms play different roles in lysosomal biogenesis.";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LAMP-2A).
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LAMP-2B).
TISSUE=Lymph;
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]
PROTEIN SEQUENCE OF 29-66, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
PubMed=2912382; DOI=10.1016/0003-9861(89)90597-3;
Mane S.M., Marzella L., Bainton D.F., Holt V.K., Cha Y.,
Hildreth J.E.K., August J.T.;
"Purification and characterization of human lysosomal membrane
glycoproteins.";
Arch. Biochem. Biophys. 268:360-378(1989).
[12]
PROTEIN SEQUENCE OF 29-43.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[13]
POLYLACTOSAMINOGLYCANS, AND GLYCOSYLATION.
PubMed=2243102;
Carlsson S.R., Fukuda M.;
"The polylactosaminoglycans of human lysosomal membrane glycoproteins
lamp-1 and lamp-2. Localization on the peptide backbones.";
J. Biol. Chem. 265:20488-20495(1990).
[14]
GLYCOSYLATION OF HINGE REGION, AND PROTEIN SEQUENCE OF 187-215.
PubMed=8323299; DOI=10.1006/abbi.1993.1322;
Carlsson S.R., Lycksell P.-O., Fukuda M.;
"Assignment of O-glycan attachment sites to the hinge-like regions of
human lysosomal membrane glycoproteins lamp-1 and lamp-2.";
Arch. Biochem. Biophys. 304:65-73(1993).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8662539; DOI=10.1126/science.273.5274.501;
Cuervo A.M., Dice J.F.;
"A receptor for the selective uptake and degradation of proteins by
lysosomes.";
Science 273:501-503(1996).
[16]
FUNCTION (ISOFORM LAMP-2A), SUBCELLULAR LOCATION, TOPOLOGY, AND
MUTAGENESIS OF 401-LYS--HIS-404.
PubMed=11082038;
Cuervo A.M., Dice J.F.;
"Unique properties of lamp2a compared to other lamp2 isoforms.";
J. Cell Sci. 113:4441-4450(2000).
[17]
GLYCOSYLATION AT ASN-49 AND ASN-101.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-32; ASN-38; ASN-49;
ASN-101; ASN-123 AND ASN-257.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[19]
NOMENCLATURE.
PubMed=16190986; DOI=10.1111/j.1600-0854.2005.00337.x;
Eskelinen E.L., Cuervo A.M., Taylor M.R., Nishino I., Blum J.S.,
Dice J.F., Sandoval I.V., Lippincott-Schwartz J., August J.T.,
Saftig P.;
"Unifying nomenclature for the isoforms of the lysosomal membrane
protein LAMP-2.";
Traffic 6:1058-1061(2005).
[20]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Placenta;
PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B.,
Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.;
"Integral and associated lysosomal membrane proteins.";
Traffic 8:1676-1686(2007).
[21]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=18644871; DOI=10.1128/MCB.02070-07;
Bandyopadhyay U., Kaushik S., Varticovski L., Cuervo A.M.;
"The chaperone-mediated autophagy receptor organizes in dynamic
protein complexes at the lysosomal membrane.";
Mol. Cell. Biol. 28:5747-5763(2008).
[22]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101; ASN-123; ASN-257 AND
ASN-356.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[23]
FUNCTION.
PubMed=20518820; DOI=10.1111/j.1365-2567.2010.03309.x;
Crotzer V.L., Glosson N., Zhou D., Nishino I., Blum J.S.;
"LAMP-2-deficient human B cells exhibit altered MHC class II
presentation of exogenous antigens.";
Immunology 131:318-330(2010).
[24]
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).
[25]
INTERACTION WITH MLLT11, AND FUNCTION.
PubMed=24880125; DOI=10.1016/j.yexcr.2014.05.013;
Li P., Ji M., Lu F., Zhang J., Li H., Cui T., Li Wang X., Tang D.,
Ji C.;
"Degradation of AF1Q by chaperone-mediated autophagy.";
Exp. Cell Res. 327:48-56(2014).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[27]
FUNCTION.
PubMed=27628032; DOI=10.1242/bio.018648;
Hubert V., Peschel A., Langer B., Groeger M., Rees A., Kain R.;
"LAMP-2 is required for incorporating syntaxin-17 into autophagosomes
and for their fusion with lysosomes.";
Biol. Open 5:1516-1529(2016).
[28]
FUNCTION (ISOFORM LAMP-2C), TISSUE SPECIFICITY, AND INDUCTION BY B
CELL STIMULATION.
PubMed=26856698; DOI=10.4049/jimmunol.1501476;
Perez L., McLetchie S., Gardiner G.J., Deffit S.N., Zhou D.,
Blum J.S.;
"LAMP-2C inhibits MHC class II presentation of cytoplasmic antigens by
disrupting chaperone-mediated autophagy.";
J. Immunol. 196:2457-2465(2016).
[29]
STRUCTURE BY NMR OF 369-410, INTERACTION WITH HSPA8, AND SUBUNIT.
PubMed=25342746; DOI=10.1074/jbc.M114.609446;
Rout A.K., Strub M.P., Piszczek G., Tjandra N.;
"Structure of transmembrane domain of lysosome-associated membrane
protein type 2a (LAMP-2A) reveals key features for substrate
specificity in chaperone-mediated autophagy.";
J. Biol. Chem. 289:35111-35123(2014).
[30]
VARIANT DAND ARG-321.
PubMed=15673802; DOI=10.1056/NEJMoa033349;
Arad M., Maron B.J., Gorham J.M., Johnson W.H. Jr., Saul J.P.,
Perez-Atayde A.R., Spirito P., Wright G.B., Kanter R.J., Seidman C.E.,
Seidman J.G.;
"Glycogen storage diseases presenting as hypertrophic
cardiomyopathy.";
N. Engl. J. Med. 352:362-372(2005).
[31]
VARIANT DAND ARG-321.
PubMed=15907287; DOI=10.1016/j.nmd.2005.02.008;
Musumeci O., Rodolico C., Nishino I., Di Guardo G., Migliorato A.,
Aguennouz M., Mazzeo A., Messina C., Vita G., Toscano A.;
"Asymptomatic hyperCKemia in a case of Danon disease due to a missense
mutation in Lamp-2 gene.";
Neuromuscul. Disord. 15:409-411(2005).
-!- FUNCTION: Plays an important role in chaperone-mediated autophagy,
a process that mediates lysosomal degradation of proteins in
response to various stresses and as part of the normal turnover of
proteins with a long biological half-live (PubMed:8662539,
PubMed:11082038, PubMed:18644871, PubMed:24880125,
PubMed:27628032). Functions by binding target proteins, such as
GAPDH and MLLT11, and targeting them for lysosomal degradation
(PubMed:8662539, PubMed:11082038, PubMed:18644871,
PubMed:24880125). Plays a role in lysosomal protein degradation in
response to starvation (By similarity). Required for the fusion of
autophagosomes with lysosomes during autophagy (PubMed:27628032).
Cells that lack LAMP2 express normal levels of VAMP8, but fail to
accumulate STX17 on autophagosomes, which is the most likely
explanation for the lack of fusion between autophagosomes and
lysosomes (PubMed:27628032). Required for normal degradation of
the contents of autophagosomes (PubMed:27628032). Required for
efficient MHCII-mediated presentation of exogenous antigens via
its function in lysosomal protein degradation; antigenic peptides
generated by proteases in the endosomal/lysosomal compartment are
captured by nascent MHCII subunits (PubMed:20518820). Is not
required for efficient MHCII-mediated presentation of endogenous
antigens (PubMed:20518820). {ECO:0000250|UniProtKB:P17046,
ECO:0000269|PubMed:11082038, ECO:0000269|PubMed:18644871,
ECO:0000269|PubMed:20518820, ECO:0000269|PubMed:24880125,
ECO:0000269|PubMed:27628032, ECO:0000269|PubMed:8662539}.
-!- FUNCTION: Isoform LAMP-2C: Modulates chaperone-mediated autophagy.
Decreases presentation of endogenous antigens by MHCII. Does not
play a role in the presentation of exogenous and membrane-derived
antigens by MHCII. {ECO:0000269|PubMed:26856698}.
-!- SUBUNIT: Monomer (PubMed:18644871, PubMed:25342746). Homodimer
(PubMed:25342746). Homotrimer (PubMed:25342746). Forms large
homooligomers (PubMed:18644871). Interacts (via its cytoplasmic
region) with HSPA8 (PubMed:25342746). Interacts with HSP90 in the
lysosome lumen; this enhances LAMP2 stability (By similarity).
Interacts with MLLT11 (PubMed:24880125).
{ECO:0000250|UniProtKB:P17046, ECO:0000269|PubMed:18644871,
ECO:0000269|PubMed:24880125, ECO:0000269|PubMed:25342746}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17897319,
ECO:0000269|PubMed:2912382}; Single-pass type I membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00740,
ECO:0000269|PubMed:17897319}. Endosome membrane
{ECO:0000269|PubMed:17897319}; Single-pass type I membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00740,
ECO:0000269|PubMed:17897319}. Lysosome membrane
{ECO:0000255|PROSITE-ProRule:PRU00740,
ECO:0000269|PubMed:11082038, ECO:0000269|PubMed:17897319,
ECO:0000269|PubMed:18644871, ECO:0000269|PubMed:2912382}; Single-
pass type I membrane protein {ECO:0000255|PROSITE-
ProRule:PRU00740, ECO:0000269|PubMed:17897319}. Cytoplasmic
vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P17047}.
Note=This protein shuttles between lysosomes, endosomes, and the
plasma membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=LAMP-2A;
IsoId=P13473-1; Sequence=Displayed;
Name=LAMP-2B;
IsoId=P13473-2; Sequence=VSP_003044;
Name=LAMP-2C;
IsoId=P13473-3; Sequence=VSP_042519;
-!- TISSUE SPECIFICITY: Isoform LAMP-2A is highly expressed in
placenta, lung and liver, less in kidney and pancreas, low in
brain and skeletal muscle (PubMed:7488019, PubMed:26856698).
Isoform LAMP-2B is detected in spleen, thymus, prostate, testis,
small intestine, colon, skeletal muscle, brain, placenta, lung,
kidney, ovary and pancreas and liver (PubMed:7488019,
PubMed:26856698). Isoform LAMP-2C is detected in small intestine,
colon, heart, brain, skeletal muscle, and at lower levels in
kidney and placenta (PubMed:26856698).
{ECO:0000269|PubMed:26856698, ECO:0000269|PubMed:7488019}.
-!- INDUCTION: In peripheral blood B cells isoform LAMP-2A, LAMP-2B
and LAMP-2C are up-regulated in response to treatments that
stimulate immune responses via the Toll-like receptors TLR7 or
TLR9. {ECO:0000269|PubMed:26856698}.
-!- PTM: O- and N-glycosylated; some of the 16 N-linked glycans are
polylactosaminoglycans. {ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:2243102, ECO:0000269|PubMed:2912382,
ECO:0000269|PubMed:8323299}.
-!- DISEASE: Danon disease (DAND) [MIM:300257]: DAND is a lysosomal
glycogen storage disease characterized by the clinical triad of
cardiomyopathy, vacuolar myopathy and mental retardation. It is
often associated with an accumulation of glycogen in muscle and
lysosomes. {ECO:0000269|PubMed:15673802,
ECO:0000269|PubMed:15907287}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the LAMP family. {ECO:0000255|PROSITE-
ProRule:PRU00740}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; J04183; AAA60383.1; -; mRNA.
EMBL; L09717; AAB41647.1; -; Genomic_DNA.
EMBL; L09709; AAB41647.1; JOINED; Genomic_DNA.
EMBL; L09710; AAB41647.1; JOINED; Genomic_DNA.
EMBL; L09711; AAB41647.1; JOINED; Genomic_DNA.
EMBL; L09712; AAB41647.1; JOINED; Genomic_DNA.
EMBL; L09713; AAB41647.1; JOINED; Genomic_DNA.
EMBL; L09714; AAB41647.1; JOINED; Genomic_DNA.
EMBL; L09715; AAB41647.1; JOINED; Genomic_DNA.
EMBL; L09716; AAB41647.1; JOINED; Genomic_DNA.
EMBL; X77196; CAA54416.1; -; mRNA.
EMBL; S79873; AAB35426.1; -; mRNA.
EMBL; U36336; AAA91149.1; -; mRNA.
EMBL; AY561849; AAS67876.1; -; mRNA.
EMBL; AK291090; BAF83779.1; -; mRNA.
EMBL; AC002476; AAB67313.1; -; Genomic_DNA.
EMBL; AC002476; AAB67314.1; -; Genomic_DNA.
EMBL; CH471107; EAX11881.1; -; Genomic_DNA.
EMBL; CH471107; EAX11882.1; -; Genomic_DNA.
EMBL; CH471107; EAX11883.1; -; Genomic_DNA.
EMBL; CH471107; EAX11884.1; -; Genomic_DNA.
EMBL; BC002965; AAH02965.1; -; mRNA.
CCDS; CCDS14599.1; -. [P13473-1]
CCDS; CCDS14600.1; -. [P13473-2]
CCDS; CCDS48159.1; -. [P13473-3]
PIR; JC2414; B31959.
PIR; JC4317; JC4317.
RefSeq; NP_001116078.1; NM_001122606.1. [P13473-3]
RefSeq; NP_002285.1; NM_002294.2. [P13473-1]
RefSeq; NP_054701.1; NM_013995.2. [P13473-2]
UniGene; Hs.496684; -.
PDB; 2MOF; NMR; -; A=369-410.
PDB; 2MOM; NMR; -; A/B/C=369-410.
PDBsum; 2MOF; -.
PDBsum; 2MOM; -.
ProteinModelPortal; P13473; -.
SMR; P13473; -.
BioGrid; 110114; 93.
IntAct; P13473; 15.
MINT; MINT-5003281; -.
TCDB; 9.A.16.1.2; the lysosomal protein import (lpi) family.
iPTMnet; P13473; -.
PhosphoSitePlus; P13473; -.
SwissPalm; P13473; -.
UniCarbKB; P13473; -.
BioMuta; LAMP2; -.
DMDM; 1708854; -.
EPD; P13473; -.
MaxQB; P13473; -.
PeptideAtlas; P13473; -.
PRIDE; P13473; -.
DNASU; 3920; -.
Ensembl; ENST00000200639; ENSP00000200639; ENSG00000005893. [P13473-1]
Ensembl; ENST00000371335; ENSP00000360386; ENSG00000005893. [P13473-2]
Ensembl; ENST00000434600; ENSP00000408411; ENSG00000005893. [P13473-3]
GeneID; 3920; -.
KEGG; hsa:3920; -.
UCSC; uc004ess.5; human. [P13473-1]
CTD; 3920; -.
DisGeNET; 3920; -.
EuPathDB; HostDB:ENSG00000005893.15; -.
GeneCards; LAMP2; -.
HGNC; HGNC:6501; LAMP2.
HPA; CAB005272; -.
HPA; HPA029100; -.
MalaCards; LAMP2; -.
MIM; 300257; phenotype.
MIM; 309060; gene.
neXtProt; NX_P13473; -.
OpenTargets; ENSG00000005893; -.
Orphanet; 34587; Glycogen storage disease due to LAMP-2 deficiency.
PharmGKB; PA30285; -.
GeneTree; ENSGT00530000063068; -.
HOGENOM; HOG000230942; -.
HOVERGEN; HBG052303; -.
InParanoid; P13473; -.
KO; K06528; -.
OMA; PIIHTTV; -.
OrthoDB; EOG091G09EV; -.
PhylomeDB; P13473; -.
TreeFam; TF316339; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; LAMP2; human.
GeneWiki; LAMP2; -.
GenomeRNAi; 3920; -.
PMAP-CutDB; P13473; -.
PRO; PR:P13473; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000005893; -.
CleanEx; HS_LAMP2; -.
ExpressionAtlas; P13473; baseline and differential.
Genevisible; P13473; HS.
GO; GO:0044754; C:autolysosome; IDA:MGI.
GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
GO; GO:0061742; C:chaperone-mediated autophagy translocation complex; IMP:ParkinsonsUK-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0097637; C:integral component of autophagosome membrane; IEA:Ensembl.
GO; GO:0005770; C:late endosome; IDA:MGI.
GO; GO:0031902; C:late endosome membrane; IDA:MGI.
GO; GO:0043202; C:lysosomal lumen; TAS:ParkinsonsUK-UCL.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:ParkinsonsUK-UCL.
GO; GO:0030670; C:phagocytic vesicle membrane; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031088; C:platelet dense granule membrane; IDA:MGI.
GO; GO:0005802; C:trans-Golgi network; IMP:ParkinsonsUK-UCL.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
GO; GO:0061684; P:chaperone-mediated autophagy; IMP:ParkinsonsUK-UCL.
GO; GO:1905146; P:lysosomal protein catabolic process; IMP:UniProtKB.
GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
GO; GO:0032463; P:negative regulation of protein homooligomerization; IDA:ParkinsonsUK-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0017038; P:protein import; TAS:ParkinsonsUK-UCL.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0006605; P:protein targeting; ISS:UniProtKB.
GO; GO:0061740; P:protein targeting to lysosome involved in chaperone-mediated autophagy; IMP:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; IMP:ParkinsonsUK-UCL.
InterPro; IPR018134; LAMP_CS.
InterPro; IPR002000; Lysosome-assoc_membr_glycop.
PANTHER; PTHR11506; PTHR11506; 1.
Pfam; PF01299; Lamp; 1.
PRINTS; PR00336; LYSASSOCTDMP.
PROSITE; PS00310; LAMP_1; 1.
PROSITE; PS00311; LAMP_2; 1.
PROSITE; PS51407; LAMP_3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Autophagy; Cell membrane;
Complete proteome; Cytoplasmic vesicle; Direct protein sequencing;
Disease mutation; Disulfide bond; Endosome; Glycogen storage disease;
Glycoprotein; Lysosome; Membrane; Polymorphism; Reference proteome;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 28 {ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:2912382,
ECO:0000269|PubMed:3198605}.
CHAIN 29 410 Lysosome-associated membrane glycoprotein
2.
/FTId=PRO_0000017110.
TOPO_DOM 29 375 Lumenal. {ECO:0000255}.
TRANSMEM 376 399 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00740}.
TOPO_DOM 400 410 Cytoplasmic. {ECO:0000255|PROSITE-
ProRule:PRU00740}.
REGION 29 192 First lumenal domain.
REGION 193 228 Hinge.
REGION 229 375 Second lumenal domain.
REGION 401 404 Important for binding and subsequent
lysosomal degradation of target proteins.
{ECO:0000269|PubMed:11082038}.
CARBOHYD 32 32 N-linked (GlcNAc...)
(polylactosaminoglycan) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 38 38 N-linked (GlcNAc...)
(polylactosaminoglycan) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 49 49 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16335952}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 75 75 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 195 195 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 196 196 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 200 200 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 203 203 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 204 204 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 207 207 O-linked (GalNAc...) serine; partial.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 209 209 O-linked (GalNAc...) threonine; partial.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 210 210 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 211 211 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 213 213 O-linked (GalNAc...) threonine; partial.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 242 242 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 257 257 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 300 300 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 307 307 N-linked (GlcNAc...)
(polylactosaminoglycan) asparagine.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 317 317 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8323299}.
CARBOHYD 356 356 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 41 79 {ECO:0000255|PROSITE-ProRule:PRU00740}.
DISULFID 153 189 {ECO:0000255|PROSITE-ProRule:PRU00740}.
DISULFID 232 265 {ECO:0000255|PROSITE-ProRule:PRU00740}.
DISULFID 331 368 {ECO:0000255|PROSITE-ProRule:PRU00740}.
VAR_SEQ 366 410 QDCSADDDNFLVPIAVGAALAGVLILVLLAYFIGLKHHHAG
YEQF -> EECSADSDLNFLIPVAVGVALGFLIIVVFISYM
IGRRKSRTGYQSV (in isoform LAMP-2C).
{ECO:0000303|Ref.6}.
/FTId=VSP_042519.
VAR_SEQ 367 410 DCSADDDNFLVPIAVGAALAGVLILVLLAYFIGLKHHHAGY
EQF -> ECSLDDDTILIPIIVGAGLSGLIIVIVIAYVIGR
RKSYAGYQTL (in isoform LAMP-2B).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7488019,
ECO:0000303|PubMed:8407947}.
/FTId=VSP_003044.
VARIANT 256 256 P -> H (in dbSNP:rs1043878).
/FTId=VAR_011992.
VARIANT 321 321 W -> R (in DAND; dbSNP:rs104894859).
{ECO:0000269|PubMed:15673802,
ECO:0000269|PubMed:15907287}.
/FTId=VAR_026230.
MUTAGEN 401 404 KHHH->AAAA: Impairs binding and
subsequent lysosomal degradation of
target proteins, such as GAPDH.
{ECO:0000269|PubMed:11082038}.
CONFLICT 8 13 PVPGSG -> RFRSGLR (in Ref. 3; no
nucleotide entry). {ECO:0000305}.
CONFLICT 53 53 R -> G (in Ref. 3; no nucleotide entry).
{ECO:0000305}.
CONFLICT 68 68 D -> V (in Ref. 2; AAB41647).
{ECO:0000305}.
CONFLICT 111 111 I -> N (in Ref. 2; AAB41647).
{ECO:0000305}.
CONFLICT 143 143 I -> Y (in Ref. 2; AAB41647).
{ECO:0000305}.
CONFLICT 220 220 A -> P (in Ref. 2; AAB41647).
{ECO:0000305}.
CONFLICT 234 234 L -> R (in Ref. 2; AAB41647).
{ECO:0000305}.
CONFLICT 263 269 GSCRSHT -> AAAVSH (in Ref. 3; no
nucleotide entry). {ECO:0000305}.
CONFLICT 322 326 DAPLG -> MPP (in Ref. 1; AAA60383).
{ECO:0000305}.
STRAND 374 377 {ECO:0000244|PDB:2MOF}.
HELIX 380 400 {ECO:0000244|PDB:2MOF}.
SEQUENCE 410 AA; 44961 MW; 9E08E3B62D58F454 CRC64;
MVCFRLFPVP GSGLVLVCLV LGAVRSYALE LNLTDSENAT CLYAKWQMNF TVRYETTNKT
YKTVTISDHG TVTYNGSICG DDQNGPKIAV QFGPGFSWIA NFTKAASTYS IDSVSFSYNT
GDNTTFPDAE DKGILTVDEL LAIRIPLNDL FRCNSLSTLE KNDVVQHYWD VLVQAFVQNG
TVSTNEFLCD KDKTSTVAPT IHTTVPSPTT TPTPKEKPEA GTYSVNNGND TCLLATMGLQ
LNITQDKVAS VININPNTTH STGSCRSHTA LLRLNSSTIK YLDFVFAVKN ENRFYLKEVN
ISMYLVNGSV FSIANNNLSY WDAPLGSSYM CNKEQTVSVS GAFQINTFDL RVQPFNVTQG
KYSTAQDCSA DDDNFLVPIA VGAALAGVLI LVLLAYFIGL KHHHAGYEQF


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