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HLA class II histocompatibility antigen, DRB1-1 beta chain (MHC class II antigen DRB1*1) (DR-1) (DR1)

 2B11_HUMAN              Reviewed;         266 AA.
P04229; A4F5N0; A8K098; O62869; P13758; Q06662; Q30116; Q30117;
Q5Y7E9; Q7M2H4; Q95461; Q9BCL7; Q9GIK5; Q9MXZ0; Q9MXZ5; Q9TQ91;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
29-AUG-2003, sequence version 2.
27-SEP-2017, entry version 171.
RecName: Full=HLA class II histocompatibility antigen, DRB1-1 beta chain;
AltName: Full=MHC class II antigen DRB1*1;
Short=DR-1;
Short=DR1;
Flags: Precursor;
Name=HLA-DRB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*01:01).
PubMed=2998758;
Tonnelle C., Demars R., Long E.O.;
"DO beta: a new beta chain gene in HLA-D with a distinct regulation of
expression.";
EMBO J. 4:2839-2847(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*01:01).
PubMed=3858829; DOI=10.1073/pnas.82.10.3405;
Bell J.I., Estess P., St John T., Saiki R., Watling D.L., Erlich H.A.,
McDevitt H.O.;
"DNA sequence and characterization of human class II major
histocompatibility complex beta chains from the DR1 haplotype.";
Proc. Natl. Acad. Sci. U.S.A. 82:3405-3409(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*01:03).
PubMed=1688595;
Coppin H.L., Avoustin P., Fabron J., Huchenq A., Garnier J.-M.,
Thomsen M., De Preval C.;
"Evolution of the HLA-DR1 gene family. Structural and functional
analysis of the new allele 'DR-BON'.";
J. Immunol. 144:984-989(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=16140993; DOI=10.1101/gr.3554305;
Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S.,
Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.;
"Ancient haplotypes of the HLA Class II region.";
Genome Res. 15:1250-1257(2005).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRB1*01:01), AND VARIANT
ARG-262.
PubMed=17345114; DOI=10.1007/s00251-007-0196-8;
von Salome J., Gyllensten U., Bergstroem T.F.;
"Full-length sequence analysis of the HLA-DRB1 locus suggests a recent
origin of alleles.";
Immunogenetics 59:261-271(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
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 [GENOMIC DNA] OF 1-29.
TISSUE=B-cell;
PubMed=8462990; DOI=10.1007/BF00216386;
Louis P., Eliaou J.F., Kerlan-Candon S., Pinet V., Vincent R.,
Clot J.;
"Polymorphism in the regulatory region of HLA-DRB genes correlating
with haplotype evolution.";
Immunogenetics 38:21-26(1993).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*01:04).
Middleton D., Versluis L.F., Tilanus M.G.J.;
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
[9]
PROTEIN SEQUENCE OF 30-64.
TISSUE=B-cell;
PubMed=6600932; DOI=10.1021/bi00270a027;
Walker L.E., Hewick R., Hunkapiller M.W., Hood L.E., Dreyer W.J.,
Reisfeld R.A.;
"N-terminal amino acid sequences of the alpha and beta chains of HLA-
DR1 and HLA-DR2 antigens.";
Biochemistry 22:185-188(1983).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:06).
PubMed=10203026; DOI=10.1034/j.1399-0039.1999.530313.x;
Palou E., Mongay L., Arias M.T., Isart F., Suarez B., Masso M.,
Fabregat V., Martorell J., Gaya A.;
"Identification of a novel DRB1-allele (DRB1*0106) by sequence-based
typing.";
Tissue Antigens 53:308-310(1999).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:07).
PubMed=12753659; DOI=10.1034/j.1399-0039.2003.00034.x;
Voorter C.E.M., Hepkema B.G., Lems S.P.M., van den Berg-Loonen E.M.;
"Identification of three new DRB1 alleles, DRB1*0107, *0425 and *13012
and confirmation of DRB4*01033.";
Tissue Antigens 61:398-402(2003).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:05).
Kashiwase K., Akaza T., Juji T.;
"HLA-DRB1 new alleles.";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:07).
Dormoy A., Froelich N., Leisenbach R., Tongio M.M.;
"A new HLA-DRB1*01 allele.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELE DRB1*01:02).
TISSUE=Blood;
Hashemi S., Couture C., Cole R., Buyse I.;
"Identification and sequencing of a novel DRB1*01 allele.";
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 37-266 (ALLELE DRB1*01:02).
PubMed=2453563;
Hurley C.K., Ziff B.L., Silver J., Gregersen P.K., Hartzman R.,
Johnson A.H.;
"Polymorphism of the HLA-DR1 haplotype in American blacks.
Identification of a DR1 beta-chain determinant recognized in the mixed
lymphocyte reaction.";
J. Immunol. 140:4019-4023(1988).
[16]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-115 (ALLELES DRB1*01:01 AND
DRB1*01:02).
TISSUE=Blood;
Arnaiz-Villena A.;
"HLA class II polymorphism.";
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[17]
DISEASE.
PubMed=14508706; DOI=10.1086/378097;
Rossman M.D., Thompson B., Frederick M., Maliarik M., Iannuzzi M.C.,
Rybicki B.A., Pandey J.P., Newman L.S., Magira E., Beznik-Cizman B.,
Monos D.;
"HLA-DRB1*1101: a significant risk factor for sarcoidosis in blacks
and whites.";
Am. J. Hum. Genet. 73:720-735(2003).
[18]
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).
[19]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EPSTEIN-BARR
VIRUS GP42 PROTEIN.
PubMed=9151859;
Li Q., Spriggs M.K., Kovats S., Turk S.M., Comeau M.R., Nepom B.,
Hutt-Fletcher L.M.;
"Epstein-Barr virus uses HLA class II as a cofactor for infection of B
lymphocytes.";
J. Virol. 71:4657-4662(1997).
[20]
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).
[21]
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).
[22]
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).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
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).
[25]
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).
[26]
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).
[27]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 32-219.
PubMed=8316295; DOI=10.1038/364033a0;
Brown J.H., Jardetzky T.S., Gorga J.C., Stern L.J., Urban R.G.,
Strominger J.L., Wiley D.C.;
"Three-dimensional structure of the human class II histocompatibility
antigen HLA-DR1.";
Nature 364:33-39(1993).
[28]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 32-219.
PubMed=8145819; DOI=10.1038/368215a0;
Stern L.J., Brown J.H., Jardetzky T.J., Gorga J.C., Urban R.G.,
Strominger J.L., Wiley D.C.;
"Crystal structure of the human class II MHC protein HLA-DR1 complexed
with an influenza virus peptide.";
Nature 368:215-221(1994).
[29]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH SEB.
PubMed=8152483; DOI=10.1038/368711a0;
Jardetzky T.S., Brown J.H., Gorga J.C., Stern L.J., Urban R.G.,
Chi Y.I., Stauffacher C., Strominger J.L., Wiley D.C.;
"Three-dimensional structure of a human class II histocompatibility
molecule complexed with superantigen.";
Nature 368:711-718(1994).
[30]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 28-207 IN COMPLEX WITH
EPSTEIN-BARR VIRUS BZLF2/GP42, AND FUNCTION (MICROBIAL INFECTION).
PubMed=11864610; DOI=10.1016/S1097-2765(02)00465-3;
Mullen M.M., Haan K.M., Longnecker R., Jardetzky T.S.;
"Structure of the Epstein-Barr virus gp42 protein bound to the MHC
class II receptor HLA-DR1.";
Mol. Cell 9:375-385(2002).
-!- 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.
-!- FUNCTION: (Microbial infection) Acts as a receptor for Epstein-
Barr virus on lymphocytes. {ECO:0000269|PubMed:11864610,
ECO:0000269|PubMed:9151859}.
-!- 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.
-!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
gp42 protein (PubMed:11864610, PubMed:9151859).
{ECO:0000269|PubMed:11864610, ECO:0000269|PubMed:9151859}.
-!- INTERACTION:
P01903:HLA-DRA; NbExp=4; IntAct=EBI-3865697, EBI-1030473;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173};
Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}.
Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173};
Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}.
Golgi apparatus, trans-Golgi network membrane
{ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18305173}. Endosome membrane
{ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18305173}. Lysosome membrane
{ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18305173}. Late endosome membrane
{ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18305173}. 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
sorting into the endosome system and down-regulation of MHC class
II. {ECO:0000305|PubMed:18305173}.
-!- POLYMORPHISM: The following alleles of DRB1-1 are known:
DRB1*01:01; DRB1*01:02; DRB1*01:03; DRB1*01:04; DRB1*01:05;
DRB1*01:06; DRB1*01:07; DRB1*01:08; DRB1*01:09; DRB1*01:10;
DRB1*01:11; DRB1*01:12; DRB1*01:13; DRB1*01:14; DRB1*01:15;
DRB1*01:16; DRB1*01:17; DRB1*01:18; DRB1*01:19; DRB1*01:20 and
DRB1*01:21. The sequence shown is that of DRB1*01:01.
-!- DISEASE: Sarcoidosis 1 (SS1) [MIM:181000]: An idiopathic,
systemic, inflammatory disease characterized by the formation of
immune granulomas in involved organs. Granulomas predominantly
invade the lungs and the lymphatic system, but also skin, liver,
spleen, eyes and other organs may be involved. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
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EMBL; X03069; CAA26873.1; -; mRNA.
EMBL; M11161; AAA59781.1; -; mRNA.
EMBL; M33600; AAA59782.1; -; mRNA.
EMBL; AY663400; AAU87993.1; -; Genomic_DNA.
EMBL; AM419948; CAL99240.1; -; Genomic_DNA.
EMBL; AK289463; BAF82152.1; -; mRNA.
EMBL; X64547; CAA45845.1; -; Genomic_DNA.
EMBL; X99896; CAA68171.1; -; mRNA.
EMBL; AF089723; AAD51131.1; -; Genomic_DNA.
EMBL; AJ276206; CAC27123.1; -; Genomic_DNA.
EMBL; AB015184; BAA28761.1; -; Genomic_DNA.
EMBL; AJ303118; CAC19693.1; -; Genomic_DNA.
EMBL; Z50871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M21008; AAA59780.1; -; mRNA.
EMBL; AF029288; AAF65497.1; -; Genomic_DNA.
EMBL; AF029293; AAF65502.1; -; Genomic_DNA.
PIR; A19197; A19197.
PIR; D24669; HLHU1B.
PIR; I56072; I56072.
PIR; PH0147; PH0147.
UniGene; Hs.534322; -.
UniGene; Hs.696211; -.
UniGene; Hs.736560; -.
PDB; 1AQD; X-ray; 2.45 A; B/E/H/K=30-227.
PDB; 1DLH; X-ray; 2.80 A; B/E=32-219.
PDB; 1FYT; X-ray; 2.60 A; B=30-221.
PDB; 1HXY; X-ray; 2.60 A; B=30-219.
PDB; 1JWM; X-ray; 2.70 A; B=30-219.
PDB; 1JWS; X-ray; 2.60 A; B=30-219.
PDB; 1JWU; X-ray; 2.30 A; B=30-219.
PDB; 1KG0; X-ray; 2.65 A; B=32-219.
PDB; 1KLG; X-ray; 2.40 A; B=30-219.
PDB; 1KLU; X-ray; 1.93 A; B=30-219.
PDB; 1LO5; X-ray; 3.20 A; B=30-219.
PDB; 1PYW; X-ray; 2.10 A; B=30-219.
PDB; 1R5I; X-ray; 2.60 A; B/F=30-219.
PDB; 1SEB; X-ray; 2.70 A; B/F=30-221.
PDB; 1SJE; X-ray; 2.45 A; B=30-219.
PDB; 1SJH; X-ray; 2.25 A; B=30-219.
PDB; 1T5W; X-ray; 2.40 A; B/E=30-219.
PDB; 1T5X; X-ray; 2.50 A; B=30-219.
PDB; 2FSE; X-ray; 3.10 A; B/D=33-219.
PDB; 2G9H; X-ray; 2.00 A; B=30-219.
PDB; 2IAM; X-ray; 2.80 A; B=30-219.
PDB; 2IAN; X-ray; 2.80 A; B/G/L/Q=30-219.
PDB; 2ICW; X-ray; 2.41 A; B/E=30-219.
PDB; 2IPK; X-ray; 2.30 A; B=30-219.
PDB; 2OJE; X-ray; 3.00 A; B/F=30-219.
PDB; 2XN9; X-ray; 2.30 A; E=30-219.
PDB; 3L6F; X-ray; 2.10 A; B=30-221.
PDB; 3PDO; X-ray; 1.95 A; B=30-227.
PDB; 3PGC; X-ray; 2.66 A; B/E=30-227.
PDB; 3PGD; X-ray; 2.72 A; B/E=30-227.
PDB; 3QXA; X-ray; 2.71 A; B/E=30-219.
PDB; 3QXD; X-ray; 2.30 A; B/E=30-219.
PDB; 3S4S; X-ray; 2.40 A; B/E=30-221.
PDB; 3S5L; X-ray; 2.10 A; B/E=30-221.
PDB; 4AEN; X-ray; 2.20 A; B=30-227.
PDB; 4AH2; X-ray; 2.36 A; B=30-227.
PDB; 4C56; X-ray; 2.90 A; E/K=30-219.
PDB; 4E41; X-ray; 2.60 A; B/G=30-219.
PDB; 4FQX; X-ray; 2.60 A; B=30-221.
PDB; 4GBX; X-ray; 3.00 A; B=30-220.
PDB; 4I5B; X-ray; 2.12 A; B/E=31-222.
PDB; 4OV5; X-ray; 2.20 A; B/E/H/K/N/Q=30-219.
PDB; 4X5W; X-ray; 1.34 A; B=30-227.
PDB; 4X5X; X-ray; 3.20 A; B/D=30-227.
PDBsum; 1AQD; -.
PDBsum; 1DLH; -.
PDBsum; 1FYT; -.
PDBsum; 1HXY; -.
PDBsum; 1JWM; -.
PDBsum; 1JWS; -.
PDBsum; 1JWU; -.
PDBsum; 1KG0; -.
PDBsum; 1KLG; -.
PDBsum; 1KLU; -.
PDBsum; 1LO5; -.
PDBsum; 1PYW; -.
PDBsum; 1R5I; -.
PDBsum; 1SEB; -.
PDBsum; 1SJE; -.
PDBsum; 1SJH; -.
PDBsum; 1T5W; -.
PDBsum; 1T5X; -.
PDBsum; 2FSE; -.
PDBsum; 2G9H; -.
PDBsum; 2IAM; -.
PDBsum; 2IAN; -.
PDBsum; 2ICW; -.
PDBsum; 2IPK; -.
PDBsum; 2OJE; -.
PDBsum; 2XN9; -.
PDBsum; 3L6F; -.
PDBsum; 3PDO; -.
PDBsum; 3PGC; -.
PDBsum; 3PGD; -.
PDBsum; 3QXA; -.
PDBsum; 3QXD; -.
PDBsum; 3S4S; -.
PDBsum; 3S5L; -.
PDBsum; 4AEN; -.
PDBsum; 4AH2; -.
PDBsum; 4C56; -.
PDBsum; 4E41; -.
PDBsum; 4FQX; -.
PDBsum; 4GBX; -.
PDBsum; 4I5B; -.
PDBsum; 4OV5; -.
PDBsum; 4X5W; -.
PDBsum; 4X5X; -.
ProteinModelPortal; P04229; -.
SMR; P04229; -.
DIP; DIP-6143N; -.
IntAct; P04229; 7.
MINT; MINT-203282; -.
BindingDB; P04229; -.
ChEMBL; CHEMBL1943; -.
DrugBank; DB05259; Glatiramer Acetate.
iPTMnet; P04229; -.
PhosphoSitePlus; P04229; -.
SwissPalm; P04229; -.
DMDM; 34395916; -.
PeptideAtlas; P04229; -.
PRIDE; P04229; -.
Ensembl; ENST00000360004; ENSP00000353099; ENSG00000196126.
DisGeNET; 3123; -.
EuPathDB; HostDB:ENSG00000196126.10; -.
GeneCards; HLA-DRB1; -.
HGNC; HGNC:4948; HLA-DRB1.
HPA; CAB015400; -.
HPA; CAB034021; -.
HPA; HPA043151; -.
MalaCards; HLA-DRB1; -.
MIM; 142857; gene.
MIM; 181000; phenotype.
neXtProt; NX_P04229; -.
Orphanet; 703; Bullous pemphigoid.
Orphanet; 555; Celiac disease.
Orphanet; 243377; Diabetes mellitus type 1.
Orphanet; 220393; Diffuse cutaneous systemic sclerosis.
Orphanet; 545; Follicular lymphoma.
Orphanet; 220402; Limited cutaneous systemic sclerosis.
Orphanet; 220407; Limited systemic sclerosis.
Orphanet; 802; Multiple sclerosis.
Orphanet; 83465; Narcolepsy without cataplexy.
Orphanet; 2073; Narcolepsy-cataplexy.
Orphanet; 284130; Rheumatoid arthritis.
Orphanet; 797; Sarcoidosis.
Orphanet; 536; Systemic lupus erythematosus.
HOVERGEN; HBG012730; -.
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.
ChiTaRS; HLA-DRB1; human.
EvolutionaryTrace; P04229; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000196126; -.
CleanEx; HS_HLA-DRB1; -.
ExpressionAtlas; P04229; baseline and differential.
Genevisible; P04229; 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:0009897; C:external side of plasma membrane; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA: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:0023026; F:MHC class II protein complex binding; IDA:UniProtKB.
GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0016045; P:detection of bacterium; ISS:UniProtKB.
GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISS:UniProtKB.
GO; GO:0006955; P:immune response; ISS:UniProtKB.
GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; ISS:UniProtKB.
GO; GO:0002437; P:inflammatory response to antigenic stimulus; ISS:UniProtKB.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0032689; P:negative regulation of interferon-gamma production; ISS:UniProtKB.
GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB.
GO; GO:2001179; P:regulation of interleukin-10 secretion; ISS:UniProtKB.
GO; GO:0032673; P:regulation of interleukin-4 production; ISS:UniProtKB.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0042088; P:T-helper 1 type immune response; ISS:UniProtKB.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.10.320.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
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;
Host cell receptor for virus entry; Host-virus interaction; Immunity;
Isopeptide bond; Lysosome; Membrane; MHC II; Polymorphism; Receptor;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Ubl conjugation.
SIGNAL 1 29 {ECO:0000269|PubMed:6600932}.
CHAIN 30 266 HLA class II histocompatibility antigen,
DRB1-1 beta chain.
/FTId=PRO_0000018949.
TOPO_DOM 30 227 Extracellular. {ECO:0000255}.
TRANSMEM 228 250 Helical. {ECO:0000255}.
TOPO_DOM 251 266 Cytoplasmic. {ECO:0000255}.
DOMAIN 126 214 Ig-like C1-type.
REGION 30 124 Beta-1.
REGION 125 227 Beta-2.
CARBOHYD 48 48 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 44 108 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 146 202 {ECO:0000255|PROSITE-ProRule:PRU00114}.
CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P20039}.
VARIANT 5 5 K -> R (in dbSNP:rs9270305).
/FTId=VAR_056527.
VARIANT 29 29 A -> S (in dbSNP:rs9270299).
/FTId=VAR_033378.
VARIANT 33 33 R -> K (in dbSNP:rs34716432).
/FTId=VAR_033379.
VARIANT 33 33 R -> Q (in dbSNP:rs34716432).
/FTId=VAR_033380.
VARIANT 39 39 Q -> E (in allele DRB1*01:07).
/FTId=VAR_016740.
VARIANT 66 66 S -> Y (in dbSNP:rs16822820).
/FTId=VAR_033381.
VARIANT 74 74 G -> R (in allele DRB1*01:05).
/FTId=VAR_016741.
VARIANT 89 89 Y -> S (in dbSNP:rs36074728).
/FTId=VAR_033383.
VARIANT 96 96 L -> I (in allele DRB1*01:03).
/FTId=VAR_016710.
VARIANT 99 99 Q -> D (in allele DRB1*01:03; requires 2
nucleotide substitutions).
/FTId=VAR_016711.
VARIANT 99 99 Q -> E (in dbSNP:rs17881965).
/FTId=VAR_033384.
VARIANT 99 99 Q -> H (in dbSNP:rs17879599).
/FTId=VAR_033385.
VARIANT 100 100 R -> A (in allele DRB1*01:06; requires 2
nucleotide substitutions).
/FTId=VAR_016742.
VARIANT 100 100 R -> E (in allele DRB1*01:03; requires 2
nucleotide substitutions).
/FTId=VAR_016712.
VARIANT 102 102 A -> G (in dbSNP:rs17878857).
/FTId=VAR_033386.
VARIANT 103 103 A -> E (in dbSNP:rs16822805).
/FTId=VAR_033387.
VARIANT 106 106 T -> N (in allele DRB1*01:04).
/FTId=VAR_016713.
VARIANT 107 107 Y -> H (in dbSNP:rs16822512).
/FTId=VAR_033388.
VARIANT 114 114 V -> A (in allele DRB1*01:02;
dbSNP:rs17424145).
/FTId=VAR_016714.
VARIANT 115 115 G -> V (in allele DRB1*01:02, allele
DRB1*01:04 and allele DRB1*01:06).
/FTId=VAR_016715.
VARIANT 164 164 G -> D (in dbSNP:rs1059633).
/FTId=VAR_033389.
VARIANT 169 169 A -> T (in dbSNP:rs2308768).
/FTId=VAR_033390.
VARIANT 171 171 V -> M (in dbSNP:rs701829).
/FTId=VAR_033391.
VARIANT 195 195 R -> Q (in dbSNP:rs3205588).
/FTId=VAR_033393.
VARIANT 253 253 Q -> E (in allele DRB1*01:02).
/FTId=VAR_016716.
VARIANT 262 262 T -> R (in dbSNP:rs9269744).
{ECO:0000269|PubMed:17345114}.
/FTId=VAR_056528.
CONFLICT 25 25 P -> R (in Ref. 2; AAA59781).
{ECO:0000305}.
CONFLICT 36 36 F -> S (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 58 59 RC -> LF (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 80 80 T -> E (in Ref. 2; AAA59781).
{ECO:0000305}.
CONFLICT 100 103 RRAA -> KRGQ (in Ref. 2; AAA59781).
{ECO:0000305}.
CONFLICT 192 192 T -> I (in Ref. 2; AAA59781).
{ECO:0000305}.
STRAND 36 47 {ECO:0000244|PDB:4X5W}.
TURN 48 51 {ECO:0000244|PDB:4X5W}.
STRAND 52 61 {ECO:0000244|PDB:4X5W}.
STRAND 64 70 {ECO:0000244|PDB:4X5W}.
TURN 71 73 {ECO:0000244|PDB:4X5W}.
STRAND 75 80 {ECO:0000244|PDB:4X5W}.
HELIX 81 83 {ECO:0000244|PDB:4X5W}.
HELIX 84 91 {ECO:0000244|PDB:4X5W}.
HELIX 94 106 {ECO:0000244|PDB:4X5W}.
HELIX 108 115 {ECO:0000244|PDB:4X5W}.
HELIX 116 118 {ECO:0000244|PDB:4X5W}.
TURN 119 121 {ECO:0000244|PDB:4X5W}.
STRAND 127 132 {ECO:0000244|PDB:4X5W}.
STRAND 135 139 {ECO:0000244|PDB:3PDO}.
STRAND 144 154 {ECO:0000244|PDB:4X5W}.
STRAND 157 162 {ECO:0000244|PDB:4X5W}.
STRAND 165 167 {ECO:0000244|PDB:4X5W}.
STRAND 171 173 {ECO:0000244|PDB:4X5W}.
STRAND 180 182 {ECO:0000244|PDB:4X5W}.
STRAND 184 190 {ECO:0000244|PDB:4X5W}.
STRAND 199 205 {ECO:0000244|PDB:4X5W}.
STRAND 213 218 {ECO:0000244|PDB:4X5W}.
SEQUENCE 266 AA; 29914 MW; CC9CC7E2D0DD036C CRC64;
MVCLKLPGGS CMTALTVTLM VLSSPLALAG DTRPRFLWQL KFECHFFNGT ERVRLLERCI
YNQEESVRFD SDVGEYRAVT ELGRPDAEYW NSQKDLLEQR RAAVDTYCRH NYGVGESFTV
QRRVEPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG
DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL
FLGAGLFIYF RNQKGHSGLQ PTGFLS


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