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

HLA class II histocompatibility antigen, DR beta 5 chain (DR beta-5) (DR2-beta-2) (Dw2) (MHC class II antigen DRB5)

 DRB5_HUMAN              Reviewed;         266 AA.
Q30154; B2RBV6; C7C4X3; O00157; O00283; O46700; Q29703; Q29787;
Q29788; Q30126; Q30150; Q30199; Q6SJR2; Q7M2H9; Q8HWS7; Q8WLR5;
Q9MY54; Q9XRX6;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 162.
RecName: Full=HLA class II histocompatibility antigen, DR beta 5 chain;
AltName: Full=DR beta-5;
AltName: Full=DR2-beta-2;
AltName: Full=Dw2;
AltName: Full=MHC class II antigen DRB5;
Flags: Precursor;
Name=HLA-DRB5 {ECO:0000312|EMBL:CAI18079.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|PIR:D25239}
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-28 AND ALA-154.
PubMed=3099214; DOI=10.1038/324676a0;
Wu S., Saunders T.L., Bach F.H.;
"Polymorphism of human Ia antigens generated by reciprocal intergenic
exchange between two DR beta loci.";
Nature 324:676-679(1986).
[2] {ECO:0000305, ECO:0000312|PIR:C32526}
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-28.
PubMed=3571980;
Wu S.K., Yabe T., Madden M., Saunders T.L., Bach F.H.;
"cDNA cloning and sequencing reveals that the electrophoretically
constant DR beta 2 molecules, as well as the variable DR beta 1
molecules, from HLA-DR2 subtypes have different amino acid sequences
including a hypervariable region for a functionally important
epitope.";
J. Immunol. 138:2953-2959(1987).
[3] {ECO:0000312|EMBL:AAA59822.1}
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB5*01:01).
PubMed=3259543; DOI=10.1007/BF00364432;
Lock C.B., So A.K., Welsh K.I., Parkes J.D., Trowsdale J.;
"MHC class II sequences of an HLA-DR2 narcoleptic.";
Immunogenetics 27:449-455(1988).
[4] {ECO:0000305, ECO:0000312|EMBL:AAA59791.1}
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-28.
PubMed=2001975; DOI=10.1016/0198-8859(91)90069-L;
Demopulos J.T., Hodge T.W., Wooten V., Acton R.T.;
"A novel DRB1 allele in DR2-positive American blacks.";
Hum. Immunol. 30:41-44(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DRB5*01:01).
TISSUE=Stomach;
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).
[6] {ECO:0000305, ECO:0000312|EMBL:CAI18079.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DRB5*01:01).
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7] {ECO:0000305, ECO:0000312|EMBL:AAH09234.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DRB5*01:01).
TISSUE=B-cell {ECO:0000312|EMBL:AAH09234.1};
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 28-140 (ALLELE DRB5*01:04), AND
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-119 (ALLELE DRB5*02:04).
TISSUE=Blood;
PubMed=9162096; DOI=10.1007/s002510050248;
Robbins F., Hurley C.K., Tang T., Yao H., Lin Y.S., Wade J.,
Goeken N., Hartzman R.J.;
"Diversity associated with the second expressed HLA-DRB locus in the
human population.";
Immunogenetics 46:104-110(1997).
[9] {ECO:0000312|EMBL:AAA36276.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELES DRB5*01:01 AND
DRB5*01:02).
PubMed=2885840; DOI=10.1073/pnas.84.13.4591;
Lee B.S.M., Rust N.A., McMichael A.J., McDevitt H.O.;
"HLA-DR2 subtypes form an additional supertypic family of DR beta
alleles.";
Proc. Natl. Acad. Sci. U.S.A. 84:4591-4595(1987).
[10] {ECO:0000305, ECO:0000312|EMBL:AAA59818.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 30-266, AND VARIANT ALA-154.
PubMed=3476943; DOI=10.1073/pnas.84.17.6234;
Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A.,
McDevitt H.O.;
"Allelic variation in the DR subregion of the human major
histocompatibility complex.";
Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987).
[11] {ECO:0000312|PIR:B28756}
PROTEIN SEQUENCE OF 30-148 AND 158-178.
PubMed=6576979;
Goetz H., Kratzin H., Thinnes F.P., Yang C.-Y., Kruse T., Pauly E.,
Koelbel S., Egert G., Wernet P., Hilschmann N.;
"Primary structure of human class II histocompatibility antigens 3rd
communication. Amino acid sequence comparison between DR and DC
subclass antigens derived from a lymphoblastoid B cell line homozygous
at the HLA loci (HLA-A3,3; B7,7; Dw2,2; DR2,2: MT1,1; Dc1,1: MB1,1).";
Hoppe-Seyler's Z. Physiol. Chem. 364:749-755(1983).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-122 (ALLELE DRB5*01:05).
PubMed=8773325; DOI=10.1111/j.1399-0039.1996.tb02563.x;
Poli F., Bianchi P., Crespiatico L., Terragna C.,
van den Berg-Loonen E., Sirchia G.;
"Characterization of a new HLA-DRB5 allele (DRB5*0105) by PCR-SSP and
direct sequencing.";
Tissue Antigens 47:338-340(1996).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-217 (ALLELE DRB5*01:14).
TISSUE=Blood;
Anholts J.D.H.;
"New sequences found during routine HLA typing.";
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*01:06).
PubMed=9226128; DOI=10.1111/j.1365-2370.1997.00267.x;
Kervaire B., Tiercy J.;
"Sequence of a new HLA-DR allele, DRB5*0106.";
Eur. J. Immunogenet. 24:225-228(1997).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*01:03).
TISSUE=Blood;
Hurley C.K.;
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[16]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*02:05).
Carter V., Day S., Dunn P.;
"Identification of a new DRB5*02 variant allele by PCR-SSP and SBT.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[17]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*01:11).
Greville W.D., Chapman G., Hogbin J.-P., Velickovic Z.;
"Novel HLA-DRB5 allele found by sequence based typing.";
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[18]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*01:12).
PubMed=14617041; DOI=10.1046/j.1399-0039.2003.00124.x;
Atkinson D.C., Jobson S.E., Dunn P.P., Briggs D.C.;
"Identification of a new HLA-DRB5 allele, DRB5*0112, by routine PCR-
SSP.";
Tissue Antigens 62:554-555(2003).
[19]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*01:13).
PubMed=16671952; DOI=10.1111/j.1399-0039.2006.00588.x;
Garino E., Berrino M., Bertinetto F., Caropreso P., Chidichimo R.,
Dametto E., Fasano M.E., Frisaldi E., Mazzola G., Tondat F.,
Boccadoro M., Bruno B., Amoroso A.;
"Identification of a new allele, HLA-DRB5*0113, through three
different molecular biology techniques.";
Tissue Antigens 67:427-429(2006).
[20]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DRB5*01:07).
PubMed=9458128; DOI=10.1111/j.1399-0039.1997.tb02933.x;
Buyse I.M., Couture C., Hashemi-Tavoularis S.;
"Identification of novel DRB1*11 (DRB1*11013, DRB1*1129), DRB1*08
(DRB1*0816) and DRB5* (DRB5*0107) alleles.";
Tissue Antigens 50:678-681(1997).
[21]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DRB5*01:09).
PubMed=9694360; DOI=10.1111/j.1399-0039.1998.tb03010.x;
Buyse I.M., Ouellet S., Hashemi-Tavoularis S.;
"Identification of novel DRB1*13 (DRB1*1333), DRB1*04 (DRB1*0426) and
DRB5* (DRB5*0109) alleles.";
Tissue Antigens 51:658-662(1998).
[22]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-119 (ALLELE DRB5*02:03).
PubMed=1471145; DOI=10.1111/j.1399-0039.1992.tb02047.x;
Grooms A., Dunckley H., Gao X., Serjeantson S.W.;
"DRB5*HK: a new HLA-DRB5 allele in Cantonese.";
Tissue Antigens 40:210-211(1992).
[23]
REVIEW.
PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9;
Cresswell P.;
"Invariant chain structure and MHC class II function.";
Cell 84:505-507(1996).
[24]
REVIEW.
PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4;
Villadangos J.A.;
"Presentation of antigens by MHC class II molecules: getting the most
out of them.";
Mol. Immunol. 38:329-346(2001).
[25]
REVIEW.
PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005;
Menendez-Benito V., Neefjes J.;
"Autophagy in MHC class II presentation: sampling from within.";
Immunity 26:1-3(2007).
[26]
REVIEW.
PubMed=18046453; DOI=10.1038/sj.emboj.7601945;
Rocha N., Neefjes J.;
"MHC class II molecules on the move for successful antigen
presentation.";
EMBO J. 27:1-5(2008).
[27]
UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION.
PubMed=18305173; DOI=10.1073/pnas.0708874105;
De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N.,
Pierre P., Gatti E.;
"MHC class II stabilization at the surface of human dendritic cells is
the result of maturation-dependent MARCH I down-regulation.";
Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008).
[28]
REVIEW.
PubMed=19092054; DOI=10.1242/jcs.035089;
Berger A.C., Roche P.A.;
"MHC class II transport at a glance.";
J. Cell Sci. 122:1-4(2009).
[29]
REVIEW.
PubMed=19533806; DOI=10.3748/wjg.15.2855;
Beswick E.J., Reyes V.E.;
"CD74 in antigen presentation, inflammation, and cancers of the
gastrointestinal tract.";
World J. Gastroenterol. 15:2855-2861(2009).
[30]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-48.
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).
[31]
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).
[32] {ECO:0000305}
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-219 OF HLA-DRA/HLA-DRB5
HETERODIMER IN COMPLEX WITH MBP PEPTIDE, SUBUNIT, AND DISULFIDE BONDS.
PubMed=11080454; DOI=10.1006/jmbi.2000.4198;
Li Y., Li H., Martin R., Mariuzza R.A.;
"Structural basis for the binding of an immunodominant peptide from
myelin basic protein in different registers by two HLA-DR2 proteins.";
J. Mol. Biol. 304:177-188(2000).
[33]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 30-219 OF HLA-DRA/HLA-DRB5
HETERODIMER IN COMPLEX WITH MPB PEPTIDE AND STREPTOCOCCUS PYOGENES
SPEC PEPTIDE, SUBUNIT, AND DISULFIDE BONDS.
PubMed=11163233; DOI=10.1016/S1074-7613(01)00092-9;
Li Y., Li H., Dimasi N., McCormick J.K., Martin R., Schuck P.,
Schlievert P.M., Mariuzza R.A.;
"Crystal structure of a superantigen bound to the high-affinity, zinc-
dependent site on MHC class II.";
Immunity 14:93-104(2001).
[34] {ECO:0000312|PDB:1H15}
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 30-219 OF HLA-DRA/HLA-DRB5
HETERODIMER IN COMPLEX EPSTEIN-BARR VIRUS BALF5 PEPTIDE, SUBUNIT, AND
DISULFIDE BONDS.
PubMed=12244309; DOI=10.1038/ni835;
Lang H.L.E., Jacobsen H., Ikemizu S., Andersson C., Harlos K.,
Madsen L., Hjorth P., Sondergaard L., Svejgaard A., Wucherpfennig K.,
Stuart D.I., Bell J.I., Jones E.Y., Fugger L.;
"A functional and structural basis for TCR cross-reactivity in
multiple sclerosis.";
Nat. Immunol. 3:940-943(2002).
[35] {ECO:0000305}
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-221 OF HLA-DRA/HLA-DRB5
HETERODIMER IN COMPLEX WITH MBP PEPTIDE AND TRAC, SUBUNIT, AND
DISULFIDE BONDS.
PubMed=16079912; DOI=10.1038/sj.emboj.7600771;
Li Y., Huang Y., Lue J., Quandt J.A., Martin R., Mariuzza R.A.;
"Structure of a human autoimmune TCR bound to a myelin basic protein
self-peptide and a multiple sclerosis-associated MHC class II
molecule.";
EMBO J. 24:2968-2979(2005).
-!- FUNCTION: Binds peptides derived from antigens that access the
endocytic route of antigen presenting cells (APC) and presents
them on the cell surface for recognition by the CD4 T-cells. The
peptide binding cleft accommodates peptides of 10-30 residues. The
peptides presented by MHC class II molecules are generated mostly
by degradation of proteins that access the endocytic route, where
they are processed by lysosomal proteases and other hydrolases.
Exogenous antigens that have been endocytosed by the APC are thus
readily available for presentation via MHC II molecules, and for
this reason this antigen presentation pathway is usually referred
to as exogenous. As membrane proteins on their way to degradation
in lysosomes as part of their normal turn-over are also contained
in the endosomal/lysosomal compartments, exogenous antigens must
compete with those derived from endogenous components. Autophagy
is also a source of endogenous peptides, autophagosomes
constitutively fuse with MHC class II loading compartments. In
addition to APCs, other cells of the gastrointestinal tract, such
as epithelial cells, express MHC class II molecules and CD74 and
act as APCs, which is an unusual trait of the GI tract. To produce
a MHC class II molecule that presents an antigen, three MHC class
II molecules (heterodimers of an alpha and a beta chain) associate
with a CD74 trimer in the ER to form a heterononamer. Soon after
the entry of this complex into the endosomal/lysosomal system
where antigen processing occurs, CD74 undergoes a sequential
degradation by various proteases, including CTSS and CTSL, leaving
a small fragment termed CLIP (class-II-associated invariant chain
peptide). The removal of CLIP is facilitated by HLA-DM via direct
binding to the alpha-beta-CLIP complex so that CLIP is released.
HLA-DM stabilizes MHC class II molecules until primary high
affinity antigenic peptides are bound. The MHC II molecule bound
to a peptide is then transported to the cell membrane surface. In
B-cells, the interaction between HLA-DM and MHC class II molecules
is regulated by HLA-DO. Primary dendritic cells (DCs) also to
express HLA-DO. Lysosomal microenvironment has been implicated in
the regulation of antigen loading into MHC II molecules, increased
acidification produces increased proteolysis and efficient peptide
loading.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred
as MHC class II molecule. In the endoplasmic reticulum (ER) it
forms a heterononamer; 3 MHC class II molecules bind to a CD74
homotrimer (also known as invariant chain or HLA class II
histocompatibility antigen gamma chain). In the
endosomal/lysosomal system; CD74 undergoes sequential degradation
by various proteases; leaving a small fragment termed CLIP on each
MHC class II molecule. MHC class II molecule interacts with
HLA_DM, and HLA_DO in B-cells, in order to release CLIP and
facilitate the binding of antigenic peptides.
{ECO:0000269|PubMed:11080454, ECO:0000269|PubMed:11163233,
ECO:0000269|PubMed:12244309, ECO:0000269|PubMed:16079912}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173};
Single-pass type I membrane protein {ECO:0000269|PubMed:18305173,
ECO:0000305}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18305173, ECO:0000305}. Golgi apparatus,
trans-Golgi network membrane {ECO:0000269|PubMed:18305173};
Single-pass type I membrane protein {ECO:0000269|PubMed:18305173,
ECO:0000305}. Endosome membrane {ECO:0000269|PubMed:18305173};
Single-pass type I membrane protein {ECO:0000269|PubMed:18305173,
ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:18305173};
Single-pass type I membrane protein {ECO:0000269|PubMed:18305173,
ECO:0000305}. Late endosome membrane
{ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18305173, ECO:0000305}. Note=The MHC class II
complex transits through a number of intracellular compartments in
the endocytic pathway until it reaches the cell membrane for
antigen presentation.
-!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to
down-regulation of MHC class II. {ECO:0000305|PubMed:18305173}.
-!- POLYMORPHISM: The following alleles of DRB5 are known: DRB5*01:01,
DRB5*01:02, DRB5*01:03, DRB5*01:04, DRB5*01:05, DRB5*01:06,
DRB5*01:07, DRB5*01:09, DRB5*01:11, DRB5*01:12 DRB5*01:13,
DRB5*01:14, DRB5*02:02, DRB5*02:03, DRB5*02:04, DRB5*02:05. The
sequence shown is that of DRB5*01:01.
-!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000255}.
-!- CAUTION: HLA-DRB3, HLA-DRB4 and HLA-DRB5 may represent a unique
gene. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M20429; AAA59822.1; -; mRNA.
EMBL; M35159; AAA59791.1; -; Genomic_DNA.
EMBL; AL713966; CAI18079.1; -; Genomic_DNA.
EMBL; AK314834; BAG37353.1; -; mRNA.
EMBL; BC009234; AAH09234.1; -; mRNA.
EMBL; U31770; AAB63983.1; -; mRNA.
EMBL; U59685; AAB52229.1; -; Genomic_DNA.
EMBL; M16954; AAA36276.1; -; mRNA.
EMBL; M16955; AAA36277.1; -; mRNA.
EMBL; M17377; AAA59818.1; -; mRNA.
EMBL; X87210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; FN430425; CAZ86696.1; -; Genomic_DNA.
EMBL; Z83201; CAB05668.1; -; Genomic_DNA.
EMBL; AF122887; AAD31766.1; -; Genomic_DNA.
EMBL; AJ271159; CAB71144.1; -; Genomic_DNA.
EMBL; AY141137; AAN28924.1; -; Genomic_DNA.
EMBL; AJ427352; CAD20460.1; -; Genomic_DNA.
EMBL; AY457037; AAR20446.2; -; Genomic_DNA.
EMBL; Y09342; CAA70524.1; -; Genomic_DNA.
EMBL; Y13727; CAA74055.1; -; Genomic_DNA.
EMBL; M91001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS4751.1; -.
PIR; B27060; B27060.
PIR; B28043; B28043.
PIR; B28756; B28756.
PIR; C32526; C32526.
PIR; D25239; D25239.
PIR; I68733; I68733.
PIR; PT0169; PT0169.
PIR; PT0170; PT0170.
PIR; PT0171; PT0171.
RefSeq; NP_002116.2; NM_002125.3.
UniGene; Hs.485130; -.
UniGene; Hs.534322; -.
UniGene; Hs.696211; -.
UniGene; Hs.736560; -.
PDB; 1FV1; X-ray; 1.90 A; B/E=30-219.
PDB; 1H15; X-ray; 3.10 A; B/E=30-219.
PDB; 1HQR; X-ray; 3.20 A; B=30-219.
PDB; 1ZGL; X-ray; 2.80 A; B/E/H/K=30-221.
PDBsum; 1FV1; -.
PDBsum; 1H15; -.
PDBsum; 1HQR; -.
PDBsum; 1ZGL; -.
ProteinModelPortal; Q30154; -.
SMR; Q30154; -.
BioGrid; 109372; 16.
IntAct; Q30154; 6.
STRING; 9606.ENSP00000364114; -.
ChEMBL; CHEMBL3988561; -.
iPTMnet; Q30154; -.
SwissPalm; Q30154; -.
BioMuta; HLA-DRB5; -.
DMDM; 74754558; -.
PaxDb; Q30154; -.
PeptideAtlas; Q30154; -.
PRIDE; Q30154; -.
ProteomicsDB; 61556; -.
DNASU; 3127; -.
Ensembl; ENST00000374975; ENSP00000364114; ENSG00000198502.
GeneID; 3127; -.
KEGG; hsa:3127; -.
UCSC; uc003obj.4; human.
CTD; 3127; -.
DisGeNET; 3127; -.
EuPathDB; HostDB:ENSG00000198502.5; -.
GeneCards; HLA-DRB5; -.
HGNC; HGNC:4953; HLA-DRB5.
HPA; HPA043151; -.
MIM; 604776; gene.
neXtProt; NX_Q30154; -.
OpenTargets; ENSG00000198502; -.
PharmGKB; PA35076; -.
eggNOG; ENOG410IWG3; Eukaryota.
eggNOG; ENOG410YI0S; LUCA.
GeneTree; ENSGT00900000140849; -.
HOVERGEN; HBG012730; -.
InParanoid; Q30154; -.
KO; K06752; -.
OMA; RWFRNSQ; -.
OrthoDB; EOG091G15IU; -.
PhylomeDB; Q30154; -.
TreeFam; TF336626; -.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-389948; PD-1 signaling.
Reactome; R-HSA-877300; Interferon gamma signaling.
SIGNOR; Q30154; -.
ChiTaRS; HLA-DRB5; human.
EvolutionaryTrace; Q30154; -.
GeneWiki; HLA-DRB5; -.
GenomeRNAi; 3127; -.
PRO; PR:Q30154; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000198502; -.
Genevisible; Q30154; HS.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0042613; C:MHC class II protein complex; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.10.320.10; -; 1.
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; IPR011162; MHC_I/II-like_Ag-recog.
InterPro; IPR014745; MHC_II_a/b_N.
InterPro; IPR000353; MHC_II_b_N.
Pfam; PF07654; C1-set; 1.
Pfam; PF00969; MHC_II_beta; 1.
ProDom; PD000328; MHC_II_b_N; 1.
SMART; SM00407; IGc1; 1.
SMART; SM00921; MHC_II_beta; 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; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Endosome; Glycoprotein; Golgi apparatus; Immunity; Lysosome; Membrane;
MHC II; Polymorphism; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1 29 {ECO:0000269|PubMed:6576979}.
CHAIN 30 266 HLA class II histocompatibility antigen,
DR beta 5 chain.
/FTId=PRO_5000143106.
TOPO_DOM 30 227 Extracellular. {ECO:0000255}.
TRANSMEM 228 248 Helical. {ECO:0000255}.
TOPO_DOM 249 266 Cytoplasmic. {ECO:0000255}.
DOMAIN 126 214 Ig-like C1-type. {ECO:0000255}.
REGION 30 124 Beta-1. {ECO:0000255}.
REGION 125 227 Beta-2. {ECO:0000255}.
CARBOHYD 48 48 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 44 108
DISULFID 146 202
VARIANT 14 14 K -> M (in dbSNP:rs1064587).
/FTId=VAR_060951.
VARIANT 14 14 K -> Q (in dbSNP:rs701884).
/FTId=VAR_060952.
VARIANT 14 14 K -> V (in allele DRB5*02:02; requires 2
nucleotide substitutions).
/FTId=VAR_060953.
VARIANT 20 20 M -> T (in dbSNP:rs17211043).
/FTId=VAR_050355.
VARIANT 28 28 L -> S. {ECO:0000269|PubMed:2001975,
ECO:0000269|PubMed:3099214,
ECO:0000269|PubMed:3571980}.
/FTId=VAR_039871.
VARIANT 33 33 R -> Q (in dbSNP:rs1141741).
/FTId=VAR_050356.
VARIANT 35 35 R -> C (in allele DRB5*02:02, allele
DRB5*02:04 and allele DRB5*02:05;
dbSNP:rs1136744).
/FTId=VAR_060954.
VARIANT 41 41 K -> T (in dbSNP:rs200581589).
/FTId=VAR_050357.
VARIANT 57 57 H -> Q (in dbSNP:rs202185589).
/FTId=VAR_060955.
VARIANT 59 59 D -> G (in allele DRB5*01:02, allele
DRB5*01:03, allele DRB5*02:02, allele
DRB5*02:03, allele DRB5*02:04 and allele
DRB5*02:05; dbSNP:rs41546317).
/FTId=VAR_060956.
VARIANT 62 62 N -> H (in dbSNP:rs1059576).
/FTId=VAR_050358.
VARIANT 66 66 D -> N (in allele DRB5*01:02, allele
DRB5*01:03, allele DRB5*02:02, allele
DRB5*02:03, allele DRB5*02:04 and allele
DRB5*02:05; dbSNP:rs707956).
/FTId=VAR_060958.
VARIANT 66 66 D -> Y (in allele DRB5*01:14;
dbSNP:rs707956).
/FTId=VAR_060959.
VARIANT 67 67 L -> V (in allele DRB5*01:02, allele
DRB5*01:03, allele DRB5*01:05, allele
DRB5*01:14, allele DRB5*02:02, allele
DRB5*02:03, allele DRB5*02:04 and allele
DRB5*02:05; dbSNP:rs1059580).
/FTId=VAR_060960.
VARIANT 87 87 A -> E (in allele DRB5*01:13).
/FTId=VAR_060961.
VARIANT 89 89 Y -> S (in allele DRB5*01:12;
dbSNP:rs41541218).
/FTId=VAR_060962.
VARIANT 96 96 F -> I (in allele DRB5*01:06, allele
DRB5*01:07, allele DRB5*01:11, allele
DRB5*02:02 and allele DRB5*02:03;
dbSNP:rs696318).
/FTId=VAR_060964.
VARIANT 96 96 F -> L (in allele DRB5*02:05;
dbSNP:rs696318).
/FTId=VAR_060963.
VARIANT 99 99 D -> E (in dbSNP:rs41559913).
/FTId=VAR_060965.
VARIANT 99 99 D -> G (in dbSNP:rs41545413).
/FTId=VAR_060966.
VARIANT 99 99 D -> H (in dbSNP:rs41547217).
/FTId=VAR_060967.
VARIANT 99 99 D -> N (in allele DRB5*01:09;
dbSNP:rs41547217).
/FTId=VAR_060968.
VARIANT 99 99 D -> Q (in allele DRB5*01:06, allele
DRB5*01:11, allele DRB5*02:02, allele
DRB5*02:03, allele DRB5*02:04 and allele
DRB5*02:05; requires 2 nucleotide
substitutions).
/FTId=VAR_060969.
VARIANT 99 99 D -> R (in allele DRB5*01:12; requires 2
nucleotide substitutions).
/FTId=VAR_060970.
VARIANT 100 100 R -> A (in allele DRB5*01:06, allele
DRB5*01:11, allele DRB5*02:02, allele
DRB5*02:03 and allele DRB5*02:04;
requires 2 nucleotide substitutions).
/FTId=VAR_060971.
VARIANT 100 100 R -> G (in dbSNP:rs41551116).
/FTId=VAR_060972.
VARIANT 100 100 R -> T (in allele DRB5*01:03;
dbSNP:rs41544215).
/FTId=VAR_060973.
VARIANT 103 103 A -> E (in allele DRB5*01:12;
dbSNP:rs1059598).
/FTId=VAR_060974.
VARIANT 103 103 A -> L (in allele DRB5*01:04; requires 2
nucleotide substitutions).
/FTId=VAR_060975.
VARIANT 106 106 T -> N (in dbSNP:rs115817940).
/FTId=VAR_050359.
VARIANT 107 107 Y -> V (in allele DRB5*01:12; requires 2
nucleotide substitutions).
/FTId=VAR_060976.
VARIANT 114 114 V -> A (in allele DRB5*01:06, allele
DRB5*02:02, allele DRB5*02:04 and allele
DRB5*02:05; dbSNP:rs1136778).
/FTId=VAR_060977.
VARIANT 115 115 G -> V (in allele DRB5*01:06, allele
DRB5*02:02, allele DRB5*02:04 and allele
DRB5*02:05; dbSNP:rs41556512).
/FTId=VAR_060978.
VARIANT 154 154 G -> A (in dbSNP:rs113395425).
{ECO:0000269|PubMed:3099214,
ECO:0000269|PubMed:3476943}.
/FTId=VAR_039872.
VARIANT 164 164 S -> G (in allele DRB5*02:02;
dbSNP:rs1059633).
/FTId=VAR_060979.
VARIANT 186 186 T -> I (in allele DRB5*02:02;
dbSNP:rs41559420).
/FTId=VAR_060980.
VARIANT 232 232 V -> I (in allele DRB5*02:02;
dbSNP:rs41553512).
/FTId=VAR_060981.
CONFLICT 139 139 Q -> E (in Ref. 11; AA sequence).
{ECO:0000305}.
STRAND 36 47 {ECO:0000244|PDB:1FV1}.
TURN 48 51 {ECO:0000244|PDB:1FV1}.
STRAND 52 61 {ECO:0000244|PDB:1FV1}.
STRAND 64 70 {ECO:0000244|PDB:1FV1}.
TURN 71 73 {ECO:0000244|PDB:1FV1}.
STRAND 75 80 {ECO:0000244|PDB:1FV1}.
HELIX 81 83 {ECO:0000244|PDB:1FV1}.
HELIX 84 91 {ECO:0000244|PDB:1FV1}.
HELIX 94 101 {ECO:0000244|PDB:1FV1}.
HELIX 103 106 {ECO:0000244|PDB:1FV1}.
HELIX 108 115 {ECO:0000244|PDB:1FV1}.
HELIX 116 118 {ECO:0000244|PDB:1FV1}.
TURN 119 121 {ECO:0000244|PDB:1FV1}.
STRAND 127 132 {ECO:0000244|PDB:1FV1}.
STRAND 137 154 {ECO:0000244|PDB:1FV1}.
STRAND 157 166 {ECO:0000244|PDB:1FV1}.
STRAND 169 173 {ECO:0000244|PDB:1FV1}.
STRAND 180 182 {ECO:0000244|PDB:1FV1}.
STRAND 184 192 {ECO:0000244|PDB:1FV1}.
STRAND 199 205 {ECO:0000244|PDB:1FV1}.
STRAND 213 218 {ECO:0000244|PDB:1FV1}.
SEQUENCE 266 AA; 30056 MW; 0D4335BAEEA6AF22 CRC64;
MVCLKLPGGS YMAKLTVTLM VLSSPLALAG DTRPRFLQQD KYECHFFNGT ERVRFLHRDI
YNQEEDLRFD SDVGEYRAVT ELGRPDAEYW NSQKDFLEDR RAAVDTYCRH NYGVGESFTV
QRRVEPKVTV YPARTQTLQH HNLLVCSVNG FYPGSIEVRW FRNSQEEKAG VVSTGLIQNG
DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAQ SESAQSKMLS GVGGFVLGLL
FLGAGLFIYF KNQKGHSGLH PTGLVS


Related products :

Catalog number Product name Quantity
EIAAB11905 DR beta-5,DR2-beta-2,Dw2,HLA class II histocompatibility antigen, DR beta 5 chain,HLA-DRB5,Homo sapiens,Human,MHC class II antigen DRB5
EIAAB11729 HLA class II histocompatibility antigen, DP beta 1 chain,HLA class II histocompatibility antigen, DP(W4) beta chain,HLA-DP1B,HLA-DPB1,Homo sapiens,Human,MHC class II antigen DPB1
EIAAB11886 HLA class II histocompatibility antigen, DQ beta 2 chain,HLA class II histocompatibility antigen, DX beta chain,HLA-DQB2,HLA-DXB,Homo sapiens,Human,MHC class II antigen DQB2
EIAAB11453 DMB,HLA class II histocompatibility antigen, DM beta chain,HLA-DMB,Homo sapiens,Human,MHC class II antigen DMB,Really interesting new gene 7 protein,RING7
EIAAB11640 HLA class II histocompatibility antigen, DO beta chain,HLA-DOB,Homo sapiens,Human,MHC class II antigen DOB
EIAAB11452 Class II histocompatibility antigen, M beta 1 chain,H2-DMb1,H2-M beta 1 chain,H-2Mb1,Mb,Mouse,Mus musculus
EIAAB11904 HLA class II histocompatibility antigen, DR beta 4 chain,HLA-DRB4,Homo sapiens,Human,MHC class II antigen DRB4
EIAAB11903 HLA class II histocompatibility antigen, DR beta 3 chain,HLA-DRB3,Homo sapiens,Human,MHC class II antigen DRB3
EIAAB11885 HLA class II histocompatibility antigen, DQ beta 1 chain,HLA-DQB,HLA-DQB1,Homo sapiens,Human,MHC class II antigen DQB1
EH1734 HLA class II histocompatibility antigen, DR beta 5 chain Elisa Kit 96T
HB2A_MOUSE Mouse ELISA Kit FOR H-2 class II histocompatibility antigen, A beta chain 96T
DPB1_HUMAN Human ELISA Kit FOR HLA class II histocompatibility antigen, DP beta 1 chain 96T
DRB3_HUMAN Human ELISA Kit FOR HLA class II histocompatibility antigen, DR beta 3 chain 96T
EH2447 HLA class II histocompatibility antigen, DRB1-15 beta chain Elisa Kit 96T
HB2F_MOUSE Mouse ELISA Kit FOR H-2 class II histocompatibility antigen, A-F beta chain 96T
HB2B_RAT Rat ELISA Kit FOR Rano class II histocompatibility antigen, B-1 beta chain 96T
CSB-RP148494h Recombinant human HLA class II histocompatibility antigen, DQ beta 1 chain protein 500ug
CSB-RP148094h Recombinant human HLA class II histocompatibility antigen, DP beta 1 chain protein 500ug
HB2D_MOUSE ELISA Kit FOR H-2 class II histocompatibility antigen, A-D beta chain; organism: Mouse; gene name: H2-Ab1 96T
HB2J_MOUSE ELISA Kit FOR H-2 class II histocompatibility antigen, I-E beta chain; organism: Mouse; gene name: H2-Eb1 96T
HB2I_MOUSE ELISA Kit FOR H-2 class II histocompatibility antigen, I-A beta chain; organism: Mouse; gene name: H2-Eb1 96T
HB21_MOUSE ELISA Kit FOR H-2 class II histocompatibility antigen, E-B beta chain; organism: Mouse; gene name: H2-Eb1 96T
HB2A_MOUSE ELISA Kit FOR H-2 class II histocompatibility antigen, A beta chain; organism: Mouse; gene name: H2-Ab1 96T
HB2K_MOUSE ELISA Kit FOR H-2 class II histocompatibility antigen, A-K beta chain; organism: Mouse; gene name: H2-Ab1 96T
HB23_MOUSE ELISA Kit FOR H-2 class II histocompatibility antigen, E-S beta chain; organism: Mouse; gene name: H2-Eb1 96T


 

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

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





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

 

 




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

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

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

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

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

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

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




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






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






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

GENTAUR Poland Sp. z o.o.


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

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

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