DRB1_HUMAN
ID DRB1_HUMAN Reviewed; 266 AA.
AC P01911; A0MWF2; A0N0W1; A2ICT1; A2TGX3; A4F5N0; A4ZXA5; A4ZXA6; A4ZY86;
AC A5H000; A5HKN8; A7DZP9; A7LA26; A7UHG2; A7X5B1; A7X5B7; A7X5E0; A7X5E6;
AC A7X5H8; A7X5J4; A7X5K7; A8K098; A8YQE9; A9JPG0; B0BK85; B0LUZ6; B0UYW1;
AC B1GWE7; B2CR03; B2LVF9; B2NJ29; B2ZCY1; B3VTP8; B3VTQ3; B5A8Y2; B5A8Y3;
AC B5B8U0; B5B9V5; B5B9V6; B5LZ25; B5QSK8; B6VCX2; B6VEL9; B7UDB2; B9VRA4;
AC B9X248; C0LAB5; O02876; O02930; O19585; O19717; O19718; O19739; O19788;
AC O46699; O46793; O46872; O62869; O62889; O77969; O78047; O78210; O98212;
AC P01912; P01914; P04229; P13758; P13759; P13760; P13761; P20039; P79545;
AC Q06662; Q0PGR5; Q0PQ39; Q14280; Q14QT2; Q155F7; Q19AF2; Q19K86; Q1AP33;
AC Q1G0Z9; Q1JRP3; Q1KLJ6; Q27PR6; Q27PR7; Q29673; Q29720; Q29722; Q29734;
AC Q29770; Q29771; Q29772; Q29790; Q29792; Q29800; Q29806; Q29833; Q29874;
AC Q29875; Q29886; Q29968; Q29974; Q29975; Q2A120; Q2HZE5; Q2L9H4; Q2LE76;
AC Q2MF40; Q2MJA6; Q2MZ92; Q2VQU1; Q2YHQ2; Q30006; Q30108; Q30112; Q30115;
AC Q30116; Q30117; Q30120; Q30134; Q30142; Q30145; Q30149; Q30159; Q30166;
AC Q30167; Q30200; Q307W5; Q31636; Q32MY7; Q3HUP9; Q3KTM1; Q3LA84; Q3LA87;
AC Q3LA88; Q3LA89; Q3LA90; Q3LA91; Q3LA92; Q3LA93; Q3LA94; Q3LA95; Q3LA96;
AC Q3LA97; Q3LA98; Q3LA99; Q3LAA0; Q3LAA1; Q3LAA2; Q3MQ60; Q3T919; Q4PRC3;
AC Q4PRC5; Q4VZY7; Q53IG1; Q56FN9; Q56FP1; Q56FP2; Q56FP3; Q58F52; Q5BM92;
AC Q5EER6; Q5K3W2; Q5NDB9; Q5U9W6; Q5UBA2; Q5UT58; Q5W3L4; Q5Y7A7; Q5Y7B0;
AC Q5Y7B9; Q5Y7E9; Q5Y7G0; Q683P7; Q6REE2; Q6T865; Q6U387; Q701T1; Q70GL2;
AC Q70Q85; Q768U2; Q768U4; Q7M2H4; Q7YNY9; Q7YP03; Q7YP04; Q7YQ26; Q7YQA3;
AC Q7YQA5; Q860D8; Q860D9; Q860E5; Q860H8; Q860S0; Q860Z3; Q861G6; Q861H0;
AC Q861H4; Q861H5; Q861H7; Q861H8; Q8HWQ6; Q8MH59; Q8MH60; Q8WLU3; Q8WMA0;
AC Q95348; Q95383; Q95389; Q95461; Q95HK1; Q95HL0; Q95HL1; Q95IE3; Q95IG2;
AC Q95IT6; Q96HZ9; Q9BCL7; Q9BCP0; Q9BCP1; Q9BCP2; Q9BCP5; Q9BD21; Q9BD33;
AC Q9BD40; Q9GIK5; Q9GIL5; Q9GIL6; Q9GIP3; Q9GIX8; Q9GIX9; Q9GIY0; Q9GIY1;
AC Q9GIY2; Q9GIY3; Q9GIY4; Q9GJ25; Q9GJ56; Q9GJ57; Q9GJ58; Q9GJ60; Q9GJF8;
AC Q9GJF9; Q9GJG0; Q9MXZ0; Q9MXZ5; Q9MY13; Q9MY45; Q9MY56; Q9MYF5; Q9TPB6;
AC Q9TPW1; Q9TPW3; Q9TPW9; Q9TPX4; Q9TQ37; Q9TQ91; Q9TQE0; Q9UBY1; Q9UIM9;
AC Q9UIN0; Q9XRX1; Q9XRY4; Q9XRY5; Q9Y453; Q9Y4H7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=HLA class II histocompatibility antigen, DRB1 beta chain;
DE AltName: Full=Human leukocyte antigen DRB1;
DE Short=HLA-DRB1;
DE Flags: Precursor;
GN Name=HLA-DRB1 {ECO:0000312|HGNC:HGNC:4948};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DRB1*03:01 AND DRB1*10:01).
RX PubMed=6589154; DOI=10.1002/j.1460-2075.1984.tb02026.x;
RA Peterson P.A., Gustafsson K., Wiman K.G., Emmoth E., Larhammar D.,
RA Boehme J., Hyldig-Nielsen J.J., Ronne H., Rask L.;
RT "Mutations and selection in the generation of class II histocompatibility
RT antigen polymorphism.";
RL EMBO J. 3:1655-1660(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*01:01).
RX PubMed=2998758; DOI=10.1002/j.1460-2075.1985.tb04012.x;
RA Tonnelle C., Demars R., Long E.O.;
RT "DO beta: a new beta chain gene in HLA-D with a distinct regulation of
RT expression.";
RL EMBO J. 4:2839-2847(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*04:04).
RX PubMed=3875800; DOI=10.1038/317166a0;
RA Cairns J.S., Curtsinger J.M., Dahl C.A., Freeman S., Alter B.J., Bach F.H.;
RT "Sequence polymorphism of HLA DR beta 1 alleles relating to T-cell-
RT recognized determinants.";
RL Nature 317:166-168(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*11:01).
RX PubMed=3456344; DOI=10.1016/s0021-9258(17)35847-7;
RA Tieber V.L., Abruzzini L.F., Didier D.K., Schwartz B.D., Rotwein P.;
RT "Complete characterization and sequence of an HLA class II DR beta chain
RT cDNA from the DR5 haplotype.";
RL J. Biol. Chem. 261:2738-2742(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-266 (ALLELE DRB1*15:02), AND NUCLEOTIDE
RP SEQUENCE [MRNA] (ALLELE DRB1*16:01).
RX PubMed=3571980;
RA Wu S.K., Yabe T., Madden M., Saunders T.L., Bach F.H.;
RT "cDNA cloning and sequencing reveals that the electrophoretically constant
RT DR beta 2 molecules, as well as the variable DR beta 1 molecules, from HLA-
RT DR2 subtypes have different amino acid sequences including a hypervariable
RT region for a functionally important epitope.";
RL J. Immunol. 138:2953-2959(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*15:01), AND NUCLEOTIDE
RP SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*16:01).
RC TISSUE=Lymphoblast;
RX PubMed=2885840; DOI=10.1073/pnas.84.13.4591;
RA Lee B.S.M., Rust N.A., McMichael A.J., McDevitt H.O.;
RT "HLA-DR2 subtypes form an additional supertypic family of DR beta
RT alleles.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:4591-4595(1987).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*07:01).
RX PubMed=3110774; DOI=10.1073/pnas.84.14.4929;
RA Young J.A.T., Wilkinson D., Bodmer W.F., Trowsdale J.;
RT "Sequence and evolution of HLA-DR7- and -DRw53-associated beta-chain
RT genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:4929-4933(1987).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*15:01).
RC TISSUE=B-cell;
RX PubMed=3259543; DOI=10.1007/bf00364432;
RA Lock C.B., So A.K., Welsh K.I., Parkes J.D., Trowsdale J.;
RT "MHC class II sequences of an HLA-DR2 narcoleptic.";
RL Immunogenetics 27:449-455(1988).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*16:02).
RX PubMed=3129499;
RA Liu C.P., Bach F.H., Wu S.K.;
RT "Molecular studies of a rare DR2/LD-5a/DQw3 HLA class II haplotype.
RT Multiple genetic mechanisms in the generation of polymorphic HLA class II
RT genes.";
RL J. Immunol. 140:3631-3639(1988).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*08:02).
RX PubMed=2497068; DOI=10.1007/bf00352840;
RA Jonsson A.K., Andersson L., Rask L.;
RT "A cellular and functional split in the DRw8 haplotype is due to a single
RT amino acid replacement (DR beta ser 57- asp 57).";
RL Immunogenetics 29:308-316(1989).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*09:01).
RC TISSUE=Blood;
RX PubMed=9777332; DOI=10.1046/j.1365-2370.1998.00105.x;
RA Martinez-Quiles N., Martin-Villa J.M., Ferre-Lopez S., Moreno-Pelayo M.A.,
RA Martinez-Laso J., Perez-Blas M., Alegre R., Arnaiz-Villena A.;
RT "Complete cDNA sequence of the HLA-DRB1*09012 allele.";
RL Eur. J. Immunogenet. 25:307-309(1998).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*14:05).
RX PubMed=12652907; DOI=10.1080/1042517021000041822;
RA Kohsaka H., Nasu K., Matsushita S., Miyasaka N.;
RT "Complete cDNA coding sequence of the HLA-DRB1*1405 allele.";
RL DNA Seq. 13:359-361(2002).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DRB1*04:02 AND DRB1*11:04).
RX PubMed=12358860; DOI=10.1046/j.1365-2370.2002.00354.x;
RA Ramon D., Corell A., Cox S.T., Soteriou B., Madrigal J.A., Marsh S.G.E.;
RT "Complete cDNA sequences of the HLA-DRB1*0402 and DRB1*11041 alleles.";
RL Eur. J. Immunogenet. 29:453-455(2002).
RN [14]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*14:01), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 1-264 (ALLELE DRB1*14:03).
RX PubMed=11972886; DOI=10.1034/j.1399-0039.2002.590116.x;
RA Corell A., Cox S.T., Soteriou B., Ramon D., Madrigal J.A., Marsh S.G.E.;
RT "Complete cDNA sequences of the HLA-DRB1*14011, *1402, *1403 and *1404
RT alleles.";
RL Tissue Antigens 59:66-69(2002).
RN [15]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*12:01).
RX PubMed=12028552; DOI=10.1034/j.1399-0039.2002.590221.x;
RA Zanone R., Bettens F., Tiercy J.M.;
RT "Sequence of a new DR12 allele with two silent mutations that affect PCR-
RT SSP typing.";
RL Tissue Antigens 59:165-167(2002).
RN [16]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*13:05).
RX PubMed=15896200; DOI=10.1111/j.1399-0039.2005.00407.x;
RA Vilches C., Sepulveda S., Balas A., Solis R., Aviles M.J., Estefania E.,
RA Gomez-Lozano N., Vicario J.L., DePablo R.;
RT "Complete coding sequences and haplotypic associations of HLA-B*0707,
RT -B*1524, -B*4405, -B*4802, -DRB1*0409, -DRB1*0411, -DRB1*1115, - DRB1*1305,
RT and the novel allele -DRB1*0709. Group-specific amplification of cDNA from
RT DRB1 alleles associated to DRB3 and DRB4.";
RL Tissue Antigens 65:529-538(2005).
RN [17]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DRB1*04:07; DRB1*04:08; DRB1*04:10;
RP DRB1*08:01; DRB1*11:11 AND DRB1*15:03).
RX PubMed=17174751; DOI=10.1016/j.humimm.2006.09.002;
RA Balas A., Vilches C., Rodriguez M.A., Fernandez B., Martinez M.P.,
RA de Pablo R., Garcia-Sanchez F., Vicario J.L.;
RT "Group-specific amplification of cDNA from DRB1 genes. Complete coding
RT sequences of partially defined alleles and identification of the new
RT alleles DRB1*040602, DRB1*111102, DRB1*080103, and DRB1*0113.";
RL Hum. Immunol. 67:1008-1016(2006).
RN [18]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DRB1*04:01; DRB1*04:05; DRB1*04:06;
RP DRB1*08:03; DRB1*12:02; DRB1*13:12 AND DRB1*15:02).
RX PubMed=21388356; DOI=10.1111/j.1399-0039.2010.01626.x;
RA Zhu F., He Y., Tao S., Zhang W., He J., He J., Xu X., Lv H., Yan L.;
RT "Analysis of the complete cDNA sequences of HLA-DRB1 alleles with group-
RT specific amplification primers in the Chinese Han population.";
RL Tissue Antigens 77:329-332(2011).
RN [19]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DRB1*11:06; DRB1*11:19 AND DRB1*13:03).
RX PubMed=26396036; DOI=10.1111/tan.12654;
RA Gerritsen K.E., Groeneweg M., Meertens C.M., Voorter C.E., Tilanus M.G.;
RT "Full-length HLA-DRB1 coding sequences generated by a hemizygous RNA-SBT
RT approach.";
RL Tissue Antigens 86:333-342(2015).
RN [20]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DRB1*04:04; DRB1*13:07; DRB1*14:03;
RP DRB1*14:06 AND DRB1*14:07).
RX PubMed=30337930; DOI=10.3389/fimmu.2018.02294;
RA Suzuki S., Ranade S., Osaki K., Ito S., Shigenari A., Ohnuki Y., Oka A.,
RA Masuya A., Harting J., Baybayan P., Kitazume M., Sunaga J., Morishima S.,
RA Morishima Y., Inoko H., Kulski J.K., Shiina T.;
RT "Reference Grade Characterization of Polymorphisms in Full-Length HLA Class
RT I and II Genes With Short-Read Sequencing on the ION PGM System and Long-
RT Reads Generated by Single Molecule, Real-Time Sequencing on the PacBio
RT Platform.";
RL Front. Immunol. 9:2294-2294(2018).
RN [21]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DRB1*01:02; DRB1*13:01;
RP DRB1*13:02; DRB1*14:05; DRB1*15:01 AND DRB1*15:03), NUCLEOTIDE SEQUENCE
RP [GENOMIC DNA] OF 1-262 (ALLELE DRB1*12:01), AND NUCLEOTIDE SEQUENCE
RP [GENOMIC DNA] OF 1-254 (ALLELE DRB1*15:02).
RX PubMed=16140993; DOI=10.1101/gr.3554305;
RA Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S.,
RA Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.;
RT "Ancient haplotypes of the HLA Class II region.";
RL Genome Res. 15:1250-1257(2005).
RN [22]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRB1*01:01), AND VARIANT ARG-262.
RX PubMed=17345114; DOI=10.1007/s00251-007-0196-8;
RA von Salome J., Gyllensten U., Bergstroem T.F.;
RT "Full-length sequence analysis of the HLA-DRB1 locus suggests a recent
RT origin of alleles.";
RL Immunogenetics 59:261-271(2007).
RN [23]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*04:11).
RA Zhao W., Fernandez-Vina M.A., Stastny P.;
RT "Full cDNA sequence of HLA-DRB1*0411.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [24]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*13:02).
RC TISSUE=Blood;
RA Arnaiz-Villena A., Martinez-Quiles N., De Juan-Echavarri D.,
RA Martin-Villa M., Martinez-Laso J.;
RT "New complete sequences of MHC-DR in Spanish family with systemic lupus
RT erythematosus.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [25]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*08:04).
RA Voorter C.;
RT "Tissue Typing, Transplantation Immunology, University Hospital Maastricht,
RT P Debeylaan 25, 6202 AZ Maastricht, NETHERLANDS.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [26]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRB1*03:02).
RA Turner R T.;
RT "ANTHONY NOLAN RESEARCH INSTITUTE, The Royal Free Hospital, Pond Street,
RT London, NW3 2QU, United Kingdom.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [27]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELES DRB1*01:01 AND DRB1*13:01).
RC TISSUE=Cerebellum, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [28]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELES DRB1*07:01; DRB1*13:02;
RP DRB1*15:01 AND DRB1*15:02).
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [29]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DRB1*04:01).
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [30]
RP PROTEIN SEQUENCE OF 30-228.
RC TISSUE=Lymphoblast;
RX PubMed=6947956;
RA Kratzin H., Yang C.-Y., Gotz H., Pauly E., Kolbel S., Egert G.,
RA Thinnes F.P., Wernet P., Altevogt P., Hilschmann N.;
RT "Primary structure of class II human histocompatibility antigens. 1st
RT communication. Amino acid sequence of the N-terminal 198 residues of the
RT beta chain of a HLA-Dw2,2;DR2,2-alloantigen.";
RL Hoppe-Seyler's Z. Physiol. Chem. 362:1665-1669(1981).
RN [31]
RP PROTEIN SEQUENCE OF 30-64.
RC TISSUE=B-cell;
RX PubMed=6600932; DOI=10.1021/bi00270a027;
RA Walker L.E., Hewick R., Hunkapiller M.W., Hood L.E., Dreyer W.J.,
RA Reisfeld R.A.;
RT "N-terminal amino acid sequences of the alpha and beta chains of HLA-DR1
RT and HLA-DR2 antigens.";
RL Biochemistry 22:185-188(1983).
RN [32]
RP INTERACTION WITH STAPHYLOCOCCUS AUREUS ENTEROTOXIN A/ENTA (MICROBIAL
RP INFECTION).
RX PubMed=2658055; DOI=10.1126/science.2658055;
RA Mollick J.A., Cook R.G., Rich R.R.;
RT "Class II MHC molecules are specific receptors for staphylococcus
RT enterotoxin A.";
RL Science 244:817-820(1989).
RN [33]
RP INTERACTION WITH STAPHYLOCOCCUS AUREUS ENTEROTOXIN A/ENTA; B/ENTB; C1/ENTC1
RP AND D/ENTD (MICROBIAL INFECTION).
RX PubMed=2210803;
RA Dohlsten M., Lando P.A., Hedlund G., Trowsdale J., Kalland T.;
RT "Targeting of human cytotoxic T lymphocytes to MHC class II-expressing
RT cells by staphylococcal enterotoxins.";
RL Immunology 71:96-100(1990).
RN [34]
RP INTERACTION WITH CD74 HOMOTRIMER.
RX PubMed=7479981; DOI=10.1073/pnas.92.24.11289;
RA Park S.J., Sadegh-Nasseri S., Wiley D.C.;
RT "Invariant chain made in Escherichia coli has an exposed N-terminal segment
RT that blocks antigen binding to HLA-DR1 and a trimeric C-terminal segment
RT that binds empty HLA-DR1.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11289-11293(1995).
RN [35]
RP FUNCTION (ALLELE DRB1*04:01).
RX PubMed=8642306; DOI=10.1084/jem.183.5.1965;
RA Topalian S.L., Gonzales M.I., Parkhurst M., Li Y.F., Southwood S.,
RA Sette A., Rosenberg S.A., Robbins P.F.;
RT "Melanoma-specific CD4+ T cells recognize nonmutated HLA-DR-restricted
RT tyrosinase epitopes.";
RL J. Exp. Med. 183:1965-1971(1996).
RN [36]
RP FUNCTION (ALLELE DRB1*01:01), SUBCELLULAR LOCATION, AND INTERACTION WITH
RP CLIP AND HLA-DM COMPLEX.
RX PubMed=9075930; DOI=10.1016/s1074-7613(00)80332-5;
RA Kropshofer H., Arndt S.O., Moldenhauer G., Haemmerling G.J., Vogt A.B.;
RT "HLA-DM acts as a molecular chaperone and rescues empty HLA-DR molecules at
RT lysosomal pH.";
RL Immunity 6:293-302(1997).
RN [37]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EPSTEIN-BARR VIRUS
RP GP42 PROTEIN (MICROBIAL INFECTION).
RX PubMed=9151859; DOI=10.1128/jvi.71.6.4657-4662.1997;
RA Li Q., Spriggs M.K., Kovats S., Turk S.M., Comeau M.R., Nepom B.,
RA Hutt-Fletcher L.M.;
RT "Epstein-Barr virus uses HLA class II as a cofactor for infection of B
RT lymphocytes.";
RL J. Virol. 71:4657-4662(1997).
RN [38]
RP INTERACTION WITH HLA-DM COMPLEX AND CLIP, AND MUTAGENESIS OF ASP-181;
RP LEU-213 AND GLU-216.
RX PubMed=11070170; DOI=10.1016/s1074-7613(00)00051-0;
RA Doebele R.C., Busch R., Scott H.M., Pashine A., Mellins E.D.;
RT "Determination of the HLA-DM interaction site on HLA-DR molecules.";
RL Immunity 13:517-527(2000).
RN [39]
RP FUNCTION (ALLELE DRB1*04:01).
RX PubMed=15265931; DOI=10.4049/jimmunol.173.3.1966;
RA Shams H., Klucar P., Weis S.E., Lalvani A., Moonan P.K., Safi H., Wizel B.,
RA Ewer K., Nepom G.T., Lewinsohn D.M., Andersen P., Barnes P.F.;
RT "Characterization of a Mycobacterium tuberculosis peptide that is
RT recognized by human CD4+ and CD8+ T cells in the context of multiple HLA
RT alleles.";
RL J. Immunol. 173:1966-1977(2004).
RN [40]
RP FUNCTION.
RX PubMed=16148104; DOI=10.4049/jimmunol.175.6.3603;
RA Schulze zur Wiesch J., Lauer G.M., Day C.L., Kim A.Y., Ouchi K.,
RA Duncan J.E., Wurcel A.G., Timm J., Jones A.M., Mothe B., Allen T.M.,
RA McGovern B., Lewis-Ximenez L., Sidney J., Sette A., Chung R.T.,
RA Walker B.D.;
RT "Broad repertoire of the CD4+ Th cell response in spontaneously controlled
RT hepatitis C virus infection includes dominant and highly promiscuous
RT epitopes.";
RL J. Immunol. 175:3603-3613(2005).
RN [41]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17182262; DOI=10.1016/j.immuni.2006.10.018;
RA Schmid D., Pypaert M., Muenz C.;
RT "Antigen-loading compartments for major histocompatibility complex class II
RT molecules continuously receive input from autophagosomes.";
RL Immunity 26:79-92(2007).
RN [42]
RP UBIQUITINATION BY MARCHF1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-254.
RX PubMed=18305173; DOI=10.1073/pnas.0708874105;
RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., Pierre P.,
RA Gatti E.;
RT "MHC class II stabilization at the surface of human dendritic cells is the
RT result of maturation-dependent MARCH I down-regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008).
RN [43]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [44]
RP FUNCTION (ALLELES DRB1*04:05; DRB1*15:01 AND DRB1*15:02).
RX PubMed=19120973; DOI=10.1111/j.1348-0421.2008.00080.x;
RA Fujiki F., Oka Y., Kawakatsu M., Tsuboi A., Nakajima H., Elisseeva O.A.,
RA Harada Y., Li Z., Tatsumi N., Kamino E., Shirakata T., Nishida S.,
RA Taniguchi Y., Kawase I., Oji Y., Sugiyama H.;
RT "A WT1 protein-derived, naturally processed 16-mer peptide, WT1(332), is a
RT promiscuous helper peptide for induction of WT1-specific Th1-type CD4(+) T
RT cells.";
RL Microbiol. Immunol. 52:591-600(2008).
RN [45]
RP ASSOCIATION OF ALLELES DRB1*03:01 AND DRB1*13:01 WITH GRAFT-VERSUS-LEUKEMIA
RP EFFECT, AND POLYMORPHISM.
RX PubMed=19706888; DOI=10.1182/blood-2009-03-208017;
RA Stumpf A.N., van der Meijden E.D., van Bergen C.A., Willemze R.,
RA Falkenburg J.H., Griffioen M.;
RT "Identification of 4 new HLA-DR-restricted minor histocompatibility
RT antigens as hematopoietic targets in antitumor immunity.";
RL Blood 114:3684-3692(2009).
RN [46]
RP FUNCTION (ALLELES DRB1*03:01 AND DRB1*11:01), TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19830726; DOI=10.1002/eji.200939225;
RA Faner R., James E., Huston L., Pujol-Borrel R., Kwok W.W., Juan M.;
RT "Reassessing the role of HLA-DRB3 T-cell responses: evidence for
RT significant expression and complementary antigen presentation.";
RL Eur. J. Immunol. 40:91-102(2010).
RN [47]
RP NOMENCLATURE.
RX PubMed=20356336; DOI=10.1111/j.1399-0039.2010.01466.x;
RA Marsh S.G., Albert E.D., Bodmer W.F., Bontrop R.E., Dupont B., Erlich H.A.,
RA Fernandez-Vina M., Geraghty D.E., Holdsworth R., Hurley C.K., Lau M.,
RA Lee K.W., Mach B., Maiers M., Mayr W.R., Mueller C.R., Parham P.,
RA Petersdorf E.W., Sasazuki T., Strominger J.L., Svejgaard A., Terasaki P.I.,
RA Tiercy J.M., Trowsdale J.;
RT "Nomenclature for factors of the HLA system, 2010.";
RL Tissue Antigens 75:291-455(2010).
RN [48]
RP FUNCTION (ALLELE DRB1*01:01).
RX PubMed=22327072; DOI=10.4049/jimmunol.1102190;
RA Kwok W.W., Tan V., Gillette L., Littell C.T., Soltis M.A., LaFond R.B.,
RA Yang J., James E.A., DeLong J.H.;
RT "Frequency of epitope-specific naive CD4(+) T cells correlates with
RT immunodominance in the human memory repertoire.";
RL J. Immunol. 188:2537-2544(2012).
RN [49]
RP FUNCTION (ALLELE DRB1*07:01).
RX PubMed=22929521; DOI=10.1038/leu.2012.248;
RA Anguille S., Fujiki F., Smits E.L., Oji Y., Lion E., Oka Y., Berneman Z.N.,
RA Sugiyama H.;
RT "Identification of a Wilms' tumor 1-derived immunogenic CD4(+) T-cell
RT epitope that is recognized in the context of common Caucasian HLA-DR
RT haplotypes.";
RL Leukemia 27:748-750(2013).
RN [50]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23783831; DOI=10.1038/ncomms3039;
RA Adamopoulou E., Tenzer S., Hillen N., Klug P., Rota I.A., Tietz S.,
RA Gebhardt M., Stevanovic S., Schild H., Tolosa E., Melms A., Stoeckle C.;
RT "Exploring the MHC-peptide matrix of central tolerance in the human
RT thymus.";
RL Nat. Commun. 4:2039-2039(2013).
RN [51]
RP FUNCTION (ALLELES DRB1*01:01; DRB1*03:01 AND DRB1*15:01), AND INTERACTION
RP WITH HLA-DM AND PEPTIDE.
RX PubMed=25413013; DOI=10.1038/ncomms6369;
RA Kim A., Hartman I.Z., Poore B., Boronina T., Cole R.N., Song N.,
RA Ciudad M.T., Caspi R.R., Jaraquemada D., Sadegh-Nasseri S.;
RT "Divergent paths for the selection of immunodominant epitopes from distinct
RT antigenic sources.";
RL Nat. Commun. 5:5369-5369(2014).
RN [52]
RP INTERACTION WITH CD4, DOMAIN, AND MUTAGENESIS OF GLU-166; VAL-172; ILE-177
RP AND LEU-187.
RX PubMed=27114505; DOI=10.1073/pnas.1513918113;
RA Joensson P., Southcombe J.H., Santos A.M., Huo J., Fernandes R.A.,
RA McColl J., Lever M., Evans E.J., Hudson A., Chang V.T., Hanke T.,
RA Godkin A., Dunne P.D., Horrocks M.H., Palayret M., Screaton G.R.,
RA Petersen J., Rossjohn J., Fugger L., Dushek O., Xu X.N., Davis S.J.,
RA Klenerman D.;
RT "Remarkably low affinity of CD4/peptide-major histocompatibility complex
RT class II protein interactions.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:5682-5687(2016).
RN [53]
RP FUNCTION (ALLELES DRB1*01:01; DRB1*03:01; DRB1*04:01; DRB1*04:04;
RP DRB1*07:01; DRB1*11:01 AND DRB1*15:01).
RX PubMed=27591323; DOI=10.4049/jimmunol.1600663;
RA Muehling L.M., Mai D.T., Kwok W.W., Heymann P.W., Pomes A., Woodfolk J.A.;
RT "Circulating Memory CD4+ T Cells Target Conserved Epitopes of Rhinovirus
RT Capsid Proteins and Respond Rapidly to Experimental Infection in Humans.";
RL J. Immunol. 197:3214-3224(2016).
RN [54]
RP FUNCTION (ALLELE DRB1*07:01).
RX PubMed=30282837; DOI=10.1172/jci.insight.122467;
RA Yossef R., Tran E., Deniger D.C., Gros A., Pasetto A., Parkhurst M.R.,
RA Gartner J.J., Prickett T.D., Cafri G., Robbins P.F., Rosenberg S.A.;
RT "Enhanced detection of neoantigen-reactive T cells targeting unique and
RT shared oncogenes for personalized cancer immunotherapy.";
RL JCI Insight 3:0-0(2018).
RN [55]
RP FUNCTION (ALLELES DRB1*03:01 AND DRB1*13:01).
RX PubMed=31020640; DOI=10.1002/eji.201948126;
RA Becerra-Artiles A., Cruz J., Leszyk J.D., Sidney J., Sette A.,
RA Shaffer S.A., Stern L.J.;
RT "Naturally processed HLA-DR3-restricted HHV-6B peptides are recognized
RT broadly with polyfunctional and cytotoxic CD4 T-cell responses.";
RL Eur. J. Immunol. 49:1167-1185(2019).
RN [56]
RP FUNCTION (ALLELE DRB1*11:01), AND TISSUE SPECIFICITY.
RX PubMed=31495665; DOI=10.1016/j.immuni.2019.08.012;
RA Abelin J.G., Harjanto D., Malloy M., Suri P., Colson T., Goulding S.P.,
RA Creech A.L., Serrano L.R., Nasir G., Nasrullah Y., McGann C.D., Velez D.,
RA Ting Y.S., Poran A., Rothenberg D.A., Chhangawala S., Rubinsteyn A.,
RA Hammerbacher J., Gaynor R.B., Fritsch E.F., Greshock J., Oslund R.C.,
RA Barthelme D., Addona T.A., Arieta C.M., Rooney M.S.;
RT "Defining HLA-II Ligand Processing and Binding Rules with Mass Spectrometry
RT Enhances Cancer Epitope Prediction.";
RL Immunity 0:0-0(2019).
RN [57]
RP FUNCTION (ALLELE DRB1*07:01).
RX PubMed=31308093; DOI=10.4049/jimmunol.1900377;
RA Meckiff B.J., Ladell K., McLaren J.E., Ryan G.B., Leese A.M., James E.A.,
RA Price D.A., Long H.M.;
RT "Primary EBV Infection Induces an Acute Wave of Activated Antigen-Specific
RT Cytotoxic CD4+ T Cells.";
RL J. Immunol. 203:1276-1287(2019).
RN [58]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 32-219 (ALLELE DRB1*01:01) IN
RP COMPLEX WITH HLA-DRA AND HA PEPTIDE, FUNCTION (ALLELE DRB1*01:01), AND
RP DOMAIN.
RX PubMed=8145819; DOI=10.1038/368215a0;
RA Stern L.J., Brown J.H., Jardetzky T.J., Gorga J.C., Urban R.G.,
RA Strominger J.L., Wiley D.C.;
RT "Crystal structure of the human class II MHC protein HLA-DR1 complexed with
RT an influenza virus peptide.";
RL Nature 368:215-221(1994).
RN [59]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 30-221 (ALLELE DRB1*01:01) IN
RP COMPLEX WITH STAPHYLOCOCCUS ENTEROTOXIN B/ENTB (MICROBIAL INFECTION).
RX PubMed=8152483; DOI=10.1038/368711a0;
RA Jardetzky T.S., Brown J.H., Gorga J.C., Stern L.J., Urban R.G., Chi Y.I.,
RA Stauffacher C., Strominger J.L., Wiley D.C.;
RT "Three-dimensional structure of a human class II histocompatibility
RT molecule complexed with superantigen.";
RL Nature 368:711-718(1994).
RN [60]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 34-220 (ALLELE DRB1*03:01) IN
RP COMPLEX WITH HLA-DRA AND CD74 PEPTIDE (CLIP), SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=7477400; DOI=10.1038/378457a0;
RA Ghosh P., Amaya M., Mellins E., Wiley D.C.;
RT "The structure of an intermediate in class II MHC maturation: CLIP bound to
RT HLA-DR3.";
RL Nature 378:457-462(1995).
RN [61]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF (ALLELE DRB1*04:01) IN COMPLEX
RP WITH HLA-DRA*01:01 AND A COL2A1 PEPTIDE, DOMAIN, AND FUNCTION (ALLELE
RP DRB1*04:01).
RX PubMed=9354468; DOI=10.1016/s1074-7613(00)80369-6;
RA Dessen A., Lawrence C.M., Cupo S., Zaller D.M., Wiley D.C.;
RT "X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed with a
RT peptide from human collagen II.";
RL Immunity 7:473-481(1997).
RN [62]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 32-222 (ALLELE DRB1*15:01) IN
RP COMPLEX WITH HLA-DRA AND MBP PEPTIDE, DISULFIDE BOND, DOMAIN, AND FUNCTION
RP (ALLELE DRB1*15:01).
RX PubMed=9782128; DOI=10.1084/jem.188.8.1511;
RA Smith K.J., Pyrdol J., Gauthier L., Wiley D.C., Wucherpfennig K.W.;
RT "Crystal structure of HLA-DR2 (DRA*0101, DRB1*1501) complexed with a
RT peptide from human myelin basic protein.";
RL J. Exp. Med. 188:1511-1520(1998).
RN [63]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 30-219 (ALLELE DRB1*01:01), AND
RP INTERACTION WITH STAPHYLOCOCCUS AUREUS ENTEROTOXIN H/ENTH (MICROBIAL
RP INFECTION).
RX PubMed=11432818; DOI=10.1093/emboj/20.13.3306;
RA Petersson K., Haakansson M., Nilsson H., Forsberg G., Svensson L.A.,
RA Liljas A., Walse B.;
RT "Crystal structure of a superantigen bound to MHC class II displays zinc
RT and peptide dependence.";
RL EMBO J. 20:3306-3312(2001).
RN [64]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 28-207 (ALLELE DRB1*01:01) IN
RP COMPLEX WITH EPSTEIN-BARR VIRUS BZLF2/GP42, AND FUNCTION (MICROBIAL
RP INFECTION).
RX PubMed=11864610; DOI=10.1016/s1097-2765(02)00465-3;
RA Mullen M.M., Haan K.M., Longnecker R., Jardetzky T.S.;
RT "Structure of the Epstein-Barr virus gp42 protein bound to the MHC class II
RT receptor HLA-DR1.";
RL Mol. Cell 9:375-385(2002).
RN [65]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 30-228 (ALLELE DRB1*15:01) IN
RP COMPLEX WITH HLA-DRA AND MBP PEPTIDE, INTERACTION WITH TCR, DOMAIN,
RP GLYCOSYLATION AT ASN-48, AND MOLECULAR MECHANISM RELEVANT FOR MULTIPLE
RP SCLEROSIS.
RX PubMed=19303388; DOI=10.1016/j.immuni.2009.01.009;
RA Harkiolaki M., Holmes S.L., Svendsen P., Gregersen J.W., Jensen L.T.,
RA McMahon R., Friese M.A., van Boxel G., Etzensperger R., Tzartos J.S.,
RA Kranc K., Sainsbury S., Harlos K., Mellins E.D., Palace J., Esiri M.M.,
RA van der Merwe P.A., Jones E.Y., Fugger L.;
RT "T cell-mediated autoimmune disease due to low-affinity crossreactivity to
RT common microbial peptides.";
RL Immunity 30:348-357(2009).
RN [66]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 30-221 (ALLELE DRB1*01:01),
RP INTERACTION WITH CD4, AND DOMAIN.
RX PubMed=21900604; DOI=10.1073/pnas.1109438108;
RA Wang X.X., Li Y., Yin Y., Mo M., Wang Q., Gao W., Wang L., Mariuzza R.A.;
RT "Affinity maturation of human CD4 by yeast surface display and crystal
RT structure of a CD4-HLA-DR1 complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:15960-15965(2011).
RN [67]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 30-221 (ALLELE DRB1*01:01) IN
RP COMPLEX WITH HLA-DRA AND PEPTIDE, INTERACTION WITH HLA-DMB-HLA-DMA, AND
RP MUTAGENESIS OF ASP-181; LEU-213 AND GLU-216.
RX PubMed=23260142; DOI=10.1016/j.cell.2012.11.025;
RA Pos W., Sethi D.K., Call M.J., Schulze M.S., Anders A.K., Pyrdol J.,
RA Wucherpfennig K.W.;
RT "Crystal structure of the HLA-DM-HLA-DR1 complex defines mechanisms for
RT rapid peptide selection.";
RL Cell 151:1557-1568(2012).
RN [68]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 30-219 (ALLELES DRB1*04:01;
RP DRB1*04:02 AND DRB1*04:04) IN COMPLEX WITH PEPTIDE, DISULFIDE BOND,
RP GLYCOSYLATION AT ASN-48, AND FUNCTION (ALLELES DRB1*04:01; DRB1*04:02 AND
RP DRB1*04:04).
RX PubMed=24190431; DOI=10.1084/jem.20131241;
RA Scally S.W., Petersen J., Law S.C., Dudek N.L., Nel H.J., Loh K.L.,
RA Wijeyewickrema L.C., Eckle S.B., van Heemst J., Pike R.N., McCluskey J.,
RA Toes R.E., La Gruta N.L., Purcell A.W., Reid H.H., Thomas R., Rossjohn J.;
RT "A molecular basis for the association of the HLA-DRB1 locus,
RT citrullination, and rheumatoid arthritis.";
RL J. Exp. Med. 210:2569-2582(2013).
RN [69]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 8-11 AND 29-219 (ALLELE
RP DRB1*15:01) IN COMPLEX WITH COL4A3 PEPTIDE, X-RAY CRYSTALLOGRAPHY (3.40
RP ANGSTROMS) OF 8-11 AND 30-219 (ALLELE DRB1*01:01, FUNCTION (ALLELES
RP DRB1*01:01 AND DRB1*15:01), DOMAIN, AND ASSOCIATION OF ALLELE DRB1*15:01
RP WITH GOODPASTURE SYNDROME.
RX PubMed=28467828; DOI=10.1038/nature22329;
RA Ooi J.D., Petersen J., Tan Y.H., Huynh M., Willett Z.J., Ramarathinam S.H.,
RA Eggenhuizen P.J., Loh K.L., Watson K.A., Gan P.Y., Alikhan M.A.,
RA Dudek N.L., Handel A., Hudson B.G., Fugger L., Power D.A., Holt S.G.,
RA Coates P.T., Gregersen J.W., Purcell A.W., Holdsworth S.R., La Gruta N.L.,
RA Reid H.H., Rossjohn J., Kitching A.R.;
RT "Dominant protection from HLA-linked autoimmunity by antigen-specific
RT regulatory T cells.";
RL Nature 545:243-247(2017).
RN [70]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 30-219 IN COMPLEX WITH HIV-1
RP PEPTIDE, FUNCTION (ALLELES DRB1*01:01; DRB5*01:01; DRB1*11:01 AND
RP DRB1*15:02), INTERACTION WITH TCR, AND SUBCELLULAR LOCATION.
RX PubMed=29884618; DOI=10.1126/sciimmunol.aat0687;
RA Galperin M., Farenc C., Mukhopadhyay M., Jayasinghe D., Decroos A.,
RA Benati D., Tan L.L., Ciacchi L., Reid H.H., Rossjohn J., Chakrabarti L.A.,
RA Gras S.;
RT "CD4+ T cell-mediated HLA class II cross-restriction in HIV controllers.";
RL Sci. Immunol. 3:0-0(2018).
RN [71]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 30-219 (ALLELE DRB1*01:01) IN
RP COMPLEX WITH HLA-DRA AND TPBG 5T4 PEPTIDE, FUNCTION (ALLELE DRB1*01:01),
RP SUBUNIT, AND DISULFIDE BOND.
RX PubMed=31619516; DOI=10.1074/jbc.ra119.009437;
RA MacLachlan B.J., Dolton G., Papakyriakou A., Greenshields-Watson A.,
RA Mason G.H., Schauenburg A., Besneux M., Szomolay B., Elliott T.,
RA Sewell A.K., Gallimore A., Rizkallah P., Cole D.K., Godkin A.;
RT "Human leukocyte antigen (HLA) class II peptide flanking residues tune the
RT immunogenicity of a human tumor-derived epitope.";
RL J. Biol. Chem. 294:20246-20258(2019).
RN [72]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 30-219 (ALLELE DRB1*01:01) IN
RP COMPLEX WITH HLA-DRA AND IAV PEPTIDE, FUNCTION (ALLELE DRB1*01:01), AND
RP SUBUNIT.
RX PubMed=32668259; DOI=10.1016/j.celrep.2020.107885;
RA Greenshields-Watson A., Attaf M., MacLachlan B.J., Whalley T., Rius C.,
RA Wall A., Lloyd A., Hughes H., Strange K.E., Mason G.H., Schauenburg A.J.,
RA Hulin-Curtis S.L., Geary J., Chen Y., Lauder S.N., Smart K.,
RA Vijaykrishna D., Grau M.L., Shugay M., Andrews R., Dolton G.,
RA Rizkallah P.J., Gallimore A.M., Sewell A.K., Godkin A.J., Cole D.K.;
RT "CD4+ T Cells Recognize Conserved Influenza A Epitopes through Shared
RT Patterns of V-Gene Usage and Complementary Biochemical Features.";
RL Cell Rep. 32:107885-107885(2020).
RN [73]
RP ASSOCIATION OF ALLELE DRB1*11:01 WITH SARCOIDOSIS.
RX PubMed=14508706; DOI=10.1086/378097;
RA Rossman M.D., Thompson B., Frederick M., Maliarik M., Iannuzzi M.C.,
RA Rybicki B.A., Pandey J.P., Newman L.S., Magira E., Beznik-Cizman B.,
RA Monos D.;
RT "HLA-DRB1*1101: a significant risk factor for sarcoidosis in blacks and
RT whites.";
RL Am. J. Hum. Genet. 73:720-735(2003).
RN [74]
RP ASSOCIATION OF ALLELE DRB1*15:01 WITH MULTIPLE SCLEROSIS.
RX PubMed=21833088; DOI=10.1038/nature10251;
RG International Multiple Sclerosis Genetics Consortium;
RG Wellcome Trust Case Control Consortium 2;
RA Sawcer S., Hellenthal G., Pirinen M., Spencer C.C., Patsopoulos N.A.,
RA Moutsianas L., Dilthey A., Su Z., Freeman C., Hunt S.E., Edkins S.,
RA Gray E., Booth D.R., Potter S.C., Goris A., Band G., Oturai A.B.,
RA Strange A., Saarela J., Bellenguez C., Fontaine B., Gillman M., Hemmer B.,
RA Gwilliam R., Zipp F., Jayakumar A., Martin R., Leslie S., Hawkins S.,
RA Giannoulatou E., D'alfonso S., Blackburn H., Martinelli Boneschi F.,
RA Liddle J., Harbo H.F., Perez M.L., Spurkland A., Waller M.J., Mycko M.P.,
RA Ricketts M., Comabella M., Hammond N., Kockum I., McCann O.T., Ban M.,
RA Whittaker P., Kemppinen A., Weston P., Hawkins C., Widaa S., Zajicek J.,
RA Dronov S., Robertson N., Bumpstead S.J., Barcellos L.F., Ravindrarajah R.,
RA Abraham R., Alfredsson L., Ardlie K., Aubin C., Baker A., Baker K.,
RA Baranzini S.E., Bergamaschi L., Bergamaschi R., Bernstein A., Berthele A.,
RA Boggild M., Bradfield J.P., Brassat D., Broadley S.A., Buck D.,
RA Butzkueven H., Capra R., Carroll W.M., Cavalla P., Celius E.G., Cepok S.,
RA Chiavacci R., Clerget-Darpoux F., Clysters K., Comi G., Cossburn M.,
RA Cournu-Rebeix I., Cox M.B., Cozen W., Cree B.A., Cross A.H., Cusi D.,
RA Daly M.J., Davis E., de Bakker P.I., Debouverie M., D'hooghe M.B.,
RA Dixon K., Dobosi R., Dubois B., Ellinghaus D., Elovaara I., Esposito F.,
RA Fontenille C., Foote S., Franke A., Galimberti D., Ghezzi A., Glessner J.,
RA Gomez R., Gout O., Graham C., Grant S.F., Guerini F.R., Hakonarson H.,
RA Hall P., Hamsten A., Hartung H.P., Heard R.N., Heath S., Hobart J.,
RA Hoshi M., Infante-Duarte C., Ingram G., Ingram W., Islam T., Jagodic M.,
RA Kabesch M., Kermode A.G., Kilpatrick T.J., Kim C., Klopp N., Koivisto K.,
RA Larsson M., Lathrop M., Lechner-Scott J.S., Leone M.A., Leppae V.,
RA Liljedahl U., Bomfim I.L., Lincoln R.R., Link J., Liu J., Lorentzen A.R.,
RA Lupoli S., Macciardi F., Mack T., Marriott M., Martinelli V., Mason D.,
RA McCauley J.L., Mentch F., Mero I.L., Mihalova T., Montalban X.,
RA Mottershead J., Myhr K.M., Naldi P., Ollier W., Page A., Palotie A.,
RA Pelletier J., Piccio L., Pickersgill T., Piehl F., Pobywajlo S.,
RA Quach H.L., Ramsay P.P., Reunanen M., Reynolds R., Rioux J.D., Rodegher M.,
RA Roesner S., Rubio J.P., Rueckert I.M., Salvetti M., Salvi E.,
RA Santaniello A., Schaefer C.A., Schreiber S., Schulze C., Scott R.J.,
RA Sellebjerg F., Selmaj K.W., Sexton D., Shen L., Simms-Acuna B.,
RA Skidmore S., Sleiman P.M., Smestad C., Soerensen P.S., Soendergaard H.B.,
RA Stankovich J., Strange R.C., Sulonen A.M., Sundqvist E., Syvaenen A.C.,
RA Taddeo F., Taylor B., Blackwell J.M., Tienari P., Bramon E., Tourbah A.,
RA Brown M.A., Tronczynska E., Casas J.P., Tubridy N., Corvin A., Vickery J.,
RA Jankowski J., Villoslada P., Markus H.S., Wang K., Mathew C.G., Wason J.,
RA Palmer C.N., Wichmann H.E., Plomin R., Willoughby E., Rautanen A.,
RA Winkelmann J., Wittig M., Trembath R.C., Yaouanq J., Viswanathan A.C.,
RA Zhang H., Wood N.W., Zuvich R., Deloukas P., Langford C., Duncanson A.,
RA Oksenberg J.R., Pericak-Vance M.A., Haines J.L., Olsson T., Hillert J.,
RA Ivinson A.J., De Jager P.L., Peltonen L., Stewart G.J., Hafler D.A.,
RA Hauser S.L., McVean G., Donnelly P., Compston A.;
RT "Genetic risk and a primary role for cell-mediated immune mechanisms in
RT multiple sclerosis.";
RL Nature 476:214-219(2011).
RN [75]
RP ASSOCIATION OF ALLELES DRB1*01:01; DRB1*01:02; DRB1*04:01; DRB1*04:04;
RP DRB1*04:05; DRB1*04:08 AND DRB1*10:01 WITH RHEUMATOID ARTHRITIS, AND
RP VARIANTS VAL-40; LEU-40; HIS-42 AND PHE-42.
RX PubMed=22286218; DOI=10.1038/ng.1076;
RA Raychaudhuri S., Sandor C., Stahl E.A., Freudenberg J., Lee H.S., Jia X.,
RA Alfredsson L., Padyukov L., Klareskog L., Worthington J., Siminovitch K.A.,
RA Bae S.C., Plenge R.M., Gregersen P.K., de Bakker P.I.;
RT "Five amino acids in three HLA proteins explain most of the association
RT between MHC and seropositive rheumatoid arthritis.";
RL Nat. Genet. 44:291-296(2012).
RN [76]
RP ASSOCIATION OF ALLELE DRB1*01:03 WITH CROHN DISEASE AND ULCERATIVE COLITIS.
RX PubMed=25559196; DOI=10.1038/ng.3176;
RG International Inflammatory Bowel Disease Genetics Consortium;
RG Australia and New Zealand IBDGC;
RG Belgium IBD Genetics Consortium;
RG Italian Group for IBD Genetic Consortium;
RG NIDDK Inflammatory Bowel Disease Genetics Consortium;
RG United Kingdom IBDGC;
RG Wellcome Trust Case Control Consortium;
RG Quebec IBD Genetics Consortium;
RA Goyette P., Boucher G., Mallon D., Ellinghaus E., Jostins L., Huang H.,
RA Ripke S., Gusareva E.S., Annese V., Hauser S.L., Oksenberg J.R.,
RA Thomsen I., Leslie S., Daly M.J., Van Steen K., Duerr R.H., Barrett J.C.,
RA McGovern D.P., Schumm L.P., Traherne J.A., Carrington M.N.,
RA Kosmoliaptsis V., Karlsen T.H., Franke A., Rioux J.D.;
RT "High-density mapping of the MHC identifies a shared role for HLA-
RT DRB1*01:03 in inflammatory bowel diseases and heterozygous advantage in
RT ulcerative colitis.";
RL Nat. Genet. 47:172-179(2015).
RN [77]
RP POLYMORPHISM.
RX PubMed=23510415; DOI=10.1111/tan.12093;
RA Mack S.J., Cano P., Hollenbach J.A., He J., Hurley C.K., Middleton D.,
RA Moraes M.E., Pereira S.E., Kempenich J.H., Reed E.F., Setterholm M.,
RA Smith A.G., Tilanus M.G., Torres M., Varney M.D., Voorter C.E.,
RA Fischer G.F., Fleischhauer K., Goodridge D., Klitz W., Little A.M.,
RA Maiers M., Marsh S.G., Mueller C.R., Noreen H., Rozemuller E.H.,
RA Sanchez-Mazas A., Senitzer D., Trachtenberg E., Fernandez-Vina M.;
RT "Common and well-documented HLA alleles: 2012 update to the CWD
RT catalogue.";
RL Tissue Antigens 81:194-203(2013).
CC -!- FUNCTION: A beta chain of antigen-presenting major histocompatibility
CC complex class II (MHCII) molecule. In complex with the alpha chain HLA-
CC DRA, displays antigenic peptides on professional antigen presenting
CC cells (APCs) for recognition by alpha-beta T cell receptor (TCR) on
CC HLA-DRB1-restricted CD4-positive T cells. This guides antigen-specific
CC T-helper effector functions, both antibody-mediated immune response and
CC macrophage activation, to ultimately eliminate the infectious agents
CC and transformed cells (PubMed:29884618, PubMed:22327072,
CC PubMed:27591323, PubMed:8642306, PubMed:15265931, PubMed:31495665,
CC PubMed:16148104). Typically presents extracellular peptide antigens of
CC 10 to 30 amino acids that arise from proteolysis of endocytosed
CC antigens in lysosomes (PubMed:8145819). In the tumor microenvironment,
CC presents antigenic peptides that are primarily generated in tumor-
CC resident APCs likely via phagocytosis of apoptotic tumor cells or
CC macropinocytosis of secreted tumor proteins (PubMed:31495665). Presents
CC peptides derived from intracellular proteins that are trapped in
CC autolysosomes after macroautophagy, a mechanism especially relevant for
CC T cell selection in the thymus and central immune tolerance
CC (PubMed:17182262, PubMed:23783831). The selection of the immunodominant
CC epitopes follows two processing modes: 'bind first, cut/trim later' for
CC pathogen-derived antigenic peptides and 'cut first, bind later' for
CC autoantigens/self-peptides (PubMed:25413013). The anchor residue at
CC position 1 of the peptide N-terminus, usually a large hydrophobic
CC residue, is essential for high affinity interaction with MHCII
CC molecules (PubMed:8145819). {ECO:0000269|PubMed:15265931,
CC ECO:0000269|PubMed:17182262, ECO:0000269|PubMed:22327072,
CC ECO:0000269|PubMed:23783831, ECO:0000269|PubMed:25413013,
CC ECO:0000269|PubMed:27591323, ECO:0000269|PubMed:29884618,
CC ECO:0000269|PubMed:31495665, ECO:0000269|PubMed:8145819,
CC ECO:0000269|PubMed:8642306}.
CC -!- FUNCTION: Allele DRB1*01:01: Displays an immunodominant epitope derived
CC from Bacillus anthracis pagA/protective antigen, PA
CC (KLPLYISNPNYKVNVYAVT), to both naive and PA-specific memory CD4-
CC positive T cells (PubMed:22327072). Presents immunodominant HIV-1 gag
CC peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for
CC recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls
CC viral load (PubMed:29884618). May present to T-helper 1 cells several
CC HRV-16 epitopes derived from capsid proteins VP1 (PRFSLPFLSIASAYYMFYDG)
CC and VP2 (PHQFINLRSNNSATLIVPYV), contributing to viral clearance
CC (PubMed:27591323). Displays commonly recognized peptides derived from
CC IAV external protein HA (PKYVKQNTLKLAT and SNGNFIAPEYAYKIVK) and from
CC internal proteins M, NP and PB1, with M-derived epitope
CC (GLIYNRMGAVTTEV) being the most immunogenic (PubMed:8145819,
CC PubMed:9075930, PubMed:25413013, PubMed:32668259). Presents a self-
CC peptide derived from COL4A3 (GWISLWKGFSF) to TCR (TRAV14 biased) on
CC CD4-positive, FOXP3-positive regulatory T cells and mediates immune
CC tolerance to self (PubMed:28467828). May present peptides derived from
CC oncofetal trophoblast glycoprotein TPBG 5T4, known to be recognized by
CC both T-helper 1 and regulatory T cells (PubMed:31619516). Displays with
CC low affinity a self-peptide derived from MBP (VHFFKNIVTPRTP)
CC (PubMed:9075930). {ECO:0000269|PubMed:22327072,
CC ECO:0000269|PubMed:25413013, ECO:0000269|PubMed:27591323,
CC ECO:0000269|PubMed:28467828, ECO:0000269|PubMed:29884618,
CC ECO:0000269|PubMed:31619516, ECO:0000269|PubMed:32668259,
CC ECO:0000269|PubMed:8145819, ECO:0000269|PubMed:9075930}.
CC -!- FUNCTION: Allele DRB1*03:01: May present to T-helper 1 cells an HRV-16
CC epitope derived from capsid protein VP2 (NEKQPSDDNWLNFDGTLLGN),
CC contributing to viral clearance (PubMed:27591323). Displays self-
CC peptides derived from retinal SAG (NRERRGIALDGKIKHE) and thyroid TG
CC (LSSVVVDPSIRHFDV) (PubMed:25413013). Presents viral epitopes derived
CC from HHV-6B gH/U48 and U85 antigens to polyfunctional CD4-positive T
CC cells with cytotoxic activity implicated in control of HHV-6B infection
CC (PubMed:31020640). Presents several immunogenic epitopes derived from
CC C. tetani neurotoxin tetX, playing a role in immune recognition and
CC long-term protection (PubMed:19830726). {ECO:0000269|PubMed:19830726,
CC ECO:0000269|PubMed:25413013, ECO:0000269|PubMed:27591323,
CC ECO:0000269|PubMed:31020640}.
CC -!- FUNCTION: Allele DRB1*04:01: Presents an immunodominant bacterial
CC epitope derived from M. tuberculosis esxB/culture filtrate antigen CFP-
CC 10 (EISTNIRQAGVQYSR), eliciting CD4-positive T cell effector functions
CC such as IFNG production and cytotoxic activity (PubMed:15265931). May
CC present to T-helper 1 cells an HRV-16 epitope derived from capsid
CC protein VP2 (NEKQPSDDNWLNFDGTLLGN), contributing to viral clearance
CC (PubMed:27591323). Presents tumor epitopes derived from melanoma-
CC associated TYR antigen (QNILLSNAPLGPQFP and DYSYLQDSDPDSFQD),
CC triggering CD4-positive T cell effector functions such as GMCSF
CC production (PubMed:8642306). Displays preferentially citrullinated
CC self-peptides derived from VIM (GVYATR/citSSAVR and SAVRAR/citSSVPGVR)
CC and ACAN (VVLLVATEGR/ CitVRVNSAYQDK) (PubMed:24190431). Displays self-
CC peptides derived from COL2A1 (PubMed:9354468).
CC {ECO:0000269|PubMed:15265931, ECO:0000269|PubMed:24190431,
CC ECO:0000269|PubMed:27591323, ECO:0000269|PubMed:8642306,
CC ECO:0000269|PubMed:9354468}.
CC -!- FUNCTION: Allele DRB1*04:02: Displays native or citrullinated self-
CC peptides derived from VIM. {ECO:0000269|PubMed:24190431}.
CC -!- FUNCTION: Allele DRB1*04:04: May present to T-helper 1 cells several
CC HRV-16 epitopes derived from capsid proteins VP1 (HIVMQYMYVPPGAPIPTTRN)
CC and VP2 (RGDSTITSQDVANAVVGYGV), contributing to viral clearance
CC (PubMed:27591323). Displays preferentially citrullinated self-peptides
CC derived from VIM (SAVRAR/citSSVPGVR) (PubMed:24190431).
CC {ECO:0000269|PubMed:24190431, ECO:0000269|PubMed:27591323}.
CC -!- FUNCTION: Allele DRB1*04:05: May present to T-helper 1 cells an
CC immunogenic epitope derived from tumor-associated antigen WT1
CC (KRYFKLSHLQMHSRKH), likely providing for effective antitumor immunity
CC in a wide range of solid and hematological malignancies.
CC {ECO:0000269|PubMed:19120973}.
CC -!- FUNCTION: Allele DRB1*05:01: Presents an immunodominant HIV-1 gag
CC peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for
CC recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls
CC viral load. {ECO:0000269|PubMed:29884618}.
CC -!- FUNCTION: Allele DRB1*07:01: Upon EBV infection, presents latent
CC antigen EBNA2 peptide (PRSPTVFYNIPPMPLPPSQL) to CD4-positive T cells,
CC driving oligoclonal expansion and selection of a dominant virus-
CC specific memory T cell subset with cytotoxic potential to directly
CC eliminate virus-infected B cells (PubMed:31308093). May present to T-
CC helper 1 cells several HRV-16 epitopes derived from capsid proteins VP1
CC (PRFSLPFLSIASAYYMFYDG) and VP2 (VPYVNAVPMDSMVRHNNWSL), contributing to
CC viral clearance (PubMed:27591323). In the context of tumor
CC immunesurveillance, may present to T-helper 1 cells an immunogenic
CC epitope derived from tumor-associated antigen WT1
CC (MTEYKLVVVGAVGVGKSALTIQLI), likely providing for effective antitumor
CC immunity in a wide range of solid and hematological malignancies
CC (PubMed:22929521). In metastatic epithelial tumors, presents to
CC intratumoral CD4-positive T cells a KRAS neoantigen
CC (MTEYKLVVVGAVGVGKSALTIQLI) carrying G12V hotspot driver mutation and
CC may mediate tumor regression (PubMed:30282837).
CC {ECO:0000269|PubMed:22929521, ECO:0000269|PubMed:27591323,
CC ECO:0000269|PubMed:30282837, ECO:0000269|PubMed:31308093}.
CC -!- FUNCTION: Allele DRB1*11:01: Displays an immunodominant HIV-1 gag
CC peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for
CC recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls
CC viral load (PubMed:29884618). May present to T-helper 1 cells an HRV-16
CC epitope derived from capsid protein VP2 (SDRIIQITRGDSTITSQDVA),
CC contributing to viral clearance (PubMed:27591323). Presents several
CC immunogenic epitopes derived from C. tetani neurotoxin tetX, playing a
CC role in immune recognition and longterm protection (PubMed:19830726).
CC In the context of tumor immunesurveillance, may present tumor-derived
CC neoantigens to CD4-positive T cells and trigger anti-tumor helper
CC functions (PubMed:31495665). {ECO:0000269|PubMed:19830726,
CC ECO:0000269|PubMed:27591323, ECO:0000269|PubMed:29884618,
CC ECO:0000269|PubMed:31495665}.
CC -!- FUNCTION: Allele DRB1*13:01: Presents viral epitopes derived from HHV-
CC 6B antigens to polyfunctional CD4-positive T cells implicated in
CC control of HHV-6B infection. {ECO:0000269|PubMed:31020640}.
CC -!- FUNCTION: Allele DRB1*15:01: May present to T-helper 1 cells an HRV-16
CC epitope derived from capsid protein VP2 (SNNSATLIVPYVNAVPMDSM),
CC contributing to viral clearance (PubMed:27591323). Displays a self-
CC peptide derived from MBP (ENPVVHFFKNIVTPR) (PubMed:9782128,
CC PubMed:25413013). May present to T-helper 1 cells an immunogenic
CC epitope derived from tumor-associated antigen WT1 (KRYFKLSHLQMHSRKH),
CC likely providing for effective antitumor immunity in a wide range of
CC solid and hematological malignancies. {ECO:0000269|PubMed:19120973,
CC ECO:0000269|PubMed:27591323, ECO:0000269|PubMed:9782128}.
CC -!- FUNCTION: Allele DRB1*15:02: Displays an immunodominant HIV-1 gag
CC peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for
CC recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls
CC viral load (PubMed:29884618). May present to T-helper 1 cells an
CC immunogenic epitope derived from tumor-associated antigen WT1
CC (KRYFKLSHLQMHSRKH), likely providing for effective antitumor immunity
CC in a wide range of solid and hematological malignancies
CC (PubMed:19120973). {ECO:0000269|PubMed:19120973,
CC ECO:0000269|PubMed:29884618}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Epstein-Barr
CC virus on lymphocytes. {ECO:0000269|PubMed:11864610,
CC ECO:0000269|PubMed:9151859}.
CC -!- SUBUNIT: Heterotrimer that consists of an alpha chain HLA-DRA, a beta
CC chain HLA-DRB1 and a peptide (peptide-MHCII) (PubMed:7477400,
CC PubMed:9354468, PubMed:9782128, PubMed:31619516, PubMed:32668259).
CC Newly synthesized alpha and beta chains forms a heterodimer (MHCII)
CC that associates with the CD74/invariant chain (Ii) in the endoplasmic
CC reticulum (ER). Ii is a trimer composed of three subunits and each
CC subunit interacts with one MHCII dimer, blocking the peptide-binding
CC cleft. As a result, MHCII molecules cannot bind peptides present in the
CC ER (PubMed:7479981). The complex of MHCII and CD74/Ii is transported in
CC vesicles from ER to Golgi to lysosomes, where it encounters antigenic
CC peptides generated via proteolysis of endocytosed antigens. MHCII
CC dimers are dissociated from CD74/Ii by the combined action of
CC proteolysis and HLA-DM (PubMed:25413013). Lysosomal enzymes such as
CC cathepsin, degrade CD74/Ii leaving a 24 amino acid remnant called class
CC II-associated Ii or CLIP. Interacts (via the peptide binding cleft)
CC with CLIP; this interaction inhibits antigen peptide binding before
CC entry in the endosomal compartment (PubMed:7477400, PubMed:9075930).
CC The displacement of CLIP and replacement by a high affinity peptide in
CC lysosomes is performed by HLA-DM heterodimer. HLA-DM catalyzes CLIP
CC dissociation from MHCII, stabilizes empty MHCII and mediates the
CC selection of high affinity peptides (PubMed:23260142, PubMed:11070170,
CC PubMed:9075930). Interacts with HLA-DM heterodimer; this interaction is
CC direct (PubMed:25413013). Interacts with TCR (via CDR3)
CC (PubMed:29884618). Interacts (via beta-2 domain) with CD4 coreceptor
CC (via Ig-like V-type domain); this interaction is of exceptionally low
CC affinity yet necessary for optimal recognition of antigenic peptides
CC (PubMed:21900604, PubMed:27114505). {ECO:0000269|PubMed:11070170,
CC ECO:0000269|PubMed:21900604, ECO:0000269|PubMed:23260142,
CC ECO:0000269|PubMed:25413013, ECO:0000269|PubMed:29884618,
CC ECO:0000269|PubMed:7477400, ECO:0000269|PubMed:7479981,
CC ECO:0000269|PubMed:9075930, ECO:0000269|PubMed:9354468,
CC ECO:0000269|PubMed:9782128}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
CC enterotoxin A/entA, enterotoxin B/entB, enterotoxin C1/entC1,
CC enterotoxin D/entD and enterotoxin H/entH. Enterotoxins bind outside
CC the peptide-binding cleft of MHCII: enterotoxin H/entH interacts via
CC the beta-1 domain of MHCII and in a zinc-dependent way, whereas
CC enterotoxin B/entB interacts primarily via the alpha-1 domain.
CC {ECO:0000269|PubMed:11432818, ECO:0000269|PubMed:2210803,
CC ECO:0000269|PubMed:2658055, ECO:0000269|PubMed:8152483}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus gp42
CC protein. {ECO:0000269|PubMed:11864610, ECO:0000269|PubMed:9151859}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173,
CC ECO:0000269|PubMed:19830726, ECO:0000269|PubMed:29884618}; Single-pass
CC type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:18305173,
CC ECO:0000269|PubMed:9075930}; Single-pass type I membrane protein
CC {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:18305173,
CC ECO:0000269|PubMed:9075930}; Single-pass type I membrane protein
CC {ECO:0000255}. Autolysosome membrane {ECO:0000269|PubMed:17182262}.
CC Note=The MHC class II complex transits through a number of
CC intracellular compartments in the endocytic pathway until it reaches
CC the cell membrane for antigen presentation (PubMed:18305173). Component
CC of immunological synapses at the interface between T cell and APC
CC (PubMed:29884618). {ECO:0000269|PubMed:18305173,
CC ECO:0000269|PubMed:29884618}.
CC -!- TISSUE SPECIFICITY: Expressed in professional APCs:
CC monocyte/macrophages, dendritic cells and B cells (at protein level)
CC (PubMed:31495665, PubMed:23783831, PubMed:19830726). Expressed in
CC thymic epithelial cells (at protein level) (PubMed:23783831).
CC {ECO:0000269|PubMed:23783831, ECO:0000269|PubMed:31495665}.
CC -!- DOMAIN: The beta-1 domain is a structural part of the peptide-binding
CC cleft. It contains one alpha helix and 4 beta sheets, respectively
CC forming part of the wall and the floor of the peptide-binding cleft.
CC The other 4 beta sheets of the floor and the second alpha helix wall is
CC formed by the alpha-1 domain of HLA-DRA. Forms hydrogen bonds with the
CC peptide main chain via conserved amino acid in most HLA-DRB molecules.
CC The polymorphic residues accomodate the side chains of the peptide
CC conferring peptide specificity to distinct HLA-DRB1 alleles
CC (PubMed:8145819, PubMed:28467828, PubMed:9782128, PubMed:9354468). The
CC peptide-bound beta-1 domain forms hydrogen bonds with CDR2 and CDR3
CC alpha-domains of TCR (PubMed:19303388). {ECO:0000269|PubMed:19303388,
CC ECO:0000269|PubMed:28467828, ECO:0000269|PubMed:8145819,
CC ECO:0000269|PubMed:9354468, ECO:0000269|PubMed:9782128}.
CC -!- DOMAIN: The beta-2 Ig-like domain mediates the interaction with CD4
CC coreceptor. {ECO:0000269|PubMed:27114505, ECO:0000305|PubMed:21900604}.
CC -!- PTM: Ubiquitinated by MARCHF1 and MARCHF8 at Lys-254 leading to sorting
CC into the endosome system and down-regulation of MHCII.
CC {ECO:0000305|PubMed:18305173}.
CC -!- POLYMORPHISM: Highly polymorphic. Polymorphic residues encode for the
CC beta-1 domain of the peptide-binding cleft, where they contribute to
CC variations in peptide binding and TCR recognition among different
CC alleles. The sequence shown is that of DRB1*15:01. The sequences of
CC common representative alleles of serologically distinct allele groups
CC as defined in the catalog of common and well-documented HLA alleles,
CC are described as variants of DRB1*15:01 (PubMed:23510415). In the
CC context of hematological malignancy and T cell transplantation, alleles
CC DRB1*03:01 and DRB1*13:01 present minor histocompatibility antigens
CC derived respectively from host MTHFD1 and LY75 proteins, contributing
CC to T cell-mediated graft-versus-leukemia effect and complete remission
CC (PubMed:19706888). {ECO:0000269|PubMed:19706888,
CC ECO:0000269|PubMed:23510415, ECO:0000305|PubMed:23510415}.
CC -!- DISEASE: Note=In populations of European descent, allele DRB1*01:03 is
CC associated with increased susceptibility to Crohn disease and colonic
CC ulcerative colitis. Decreased heterozygosity in individuals with
CC colonic ulcerative colitis suggests that it acts as a recessive risk
CC allele. {ECO:0000269|PubMed:25559196}.
CC -!- DISEASE: Sarcoidosis 1 (SS1) [MIM:181000]: An idiopathic, systemic,
CC inflammatory disease characterized by the formation of immune
CC granulomas in involved organs. Granulomas predominantly invade the
CC lungs and the lymphatic system, but also skin, liver, spleen, eyes and
CC other organs may be involved. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry. Alleles
CC DRB1*04:02, DRB1*11:01 and DRB1*12:01 are associated with sarcoidosis.
CC Allele DRB1*04:02 is significantly associated with specific sarcodosis
CC phenotypes such as eye, parotid and salivary gland involvement.
CC {ECO:0000269|PubMed:14508706}.
CC -!- DISEASE: Multiple sclerosis (MS) [MIM:126200]: A multifactorial,
CC inflammatory, demyelinating disease of the central nervous system.
CC Sclerotic lesions are characterized by perivascular infiltration of
CC monocytes and lymphocytes and appear as indurated areas in pathologic
CC specimens (sclerosis in plaques). The pathological mechanism is
CC regarded as an autoimmune attack of the myelin sheath, mediated by both
CC cellular and humoral immunity. Clinical manifestations include visual
CC loss, extra-ocular movement disorders, paresthesias, loss of sensation,
CC weakness, dysarthria, spasticity, ataxia and bladder dysfunction.
CC Genetic and environmental factors influence susceptibility to the
CC disease. Note=Disease susceptibility is associated with variants
CC affecting the gene represented in this entry. In populations of
CC European descent, allele DRB1*15:01 has the strongest association with
CC multiple sclerosis among all HLA class II alleles. Additional risk is
CC associated with the strongly linked alleles DRB1*03:01 and DQB1*02:01
CC as well as with allele DRB1*13:03 (PubMed:21833088). It is postulated
CC that bacterial or viral infection triggers the autoimmune MS. Microbial
CC peptides having low affinity crossreactivity to MBP autoantigen, may
CC stimulate autoreactive T cells via molecular mimicry and initiate the
CC autoimmune inflammation (PubMed:19303388).
CC {ECO:0000269|PubMed:19303388, ECO:0000269|PubMed:21833088}.
CC -!- DISEASE: Note=Allele DRB1*15:01 is associated with increased
CC susceptibility to Goodpasture syndrome. Can present a self-peptide
CC derived from COL4A3 (GWISLWKGFSF) on TCR (TRAV19 biased) in pathogenic
CC CD4-positive T-helper 1 and T-helper 17 cells, triggering autoimmune
CC inflammation. {ECO:0000269|PubMed:28467828}.
CC -!- DISEASE: Rheumatoid arthritis (RA) [MIM:180300]: An inflammatory
CC disease with autoimmune features and a complex genetic component. It
CC primarily affects the joints and is characterized by inflammatory
CC changes in the synovial membranes and articular structures, widespread
CC fibrinoid degeneration of the collagen fibers in mesenchymal tissues,
CC and by atrophy and rarefaction of bony structures.
CC {ECO:0000269|PubMed:22286218}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC Alleles DRB1*04:01; DRB1*04:04; DRB1*04:05; DRB1*04:08; DRB1*10:01;
CC DRB1*01:01 and DRB1*01:02 are associated with increased susceptibility
CC to rheumatoid arthritis, where affected individuals have antibodies to
CC cyclic citrullinated peptide (anti-CCP-positive rheumatoid arthritis).
CC Variations at position 40 in the peptide-binding cleft of these alleles
CC explain most of the association to rheumatoid arthritis risk.
CC {ECO:0000269|PubMed:22286218}.
CC ---------------------------------------------------------------------------
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DR EMBL; X00699; CAA25295.1; -; mRNA.
DR EMBL; X00700; CAA25296.1; -; mRNA.
DR EMBL; X03069; CAA26873.1; -; mRNA.
DR EMBL; X02902; CAA26660.1; -; mRNA.
DR EMBL; M11867; AAA36274.1; -; mRNA.
DR EMBL; M28584; AAA59681.1; -; mRNA.
DR EMBL; M28583; AAA59680.1; -; mRNA.
DR EMBL; M16957; AAA36279.1; -; mRNA.
DR EMBL; M16959; AAA36281.1; -; mRNA.
DR EMBL; M16941; AAA36282.1; -; mRNA.
DR EMBL; M20430; AAA59831.1; -; mRNA.
DR EMBL; M20504; AAA59827.1; -; mRNA.
DR EMBL; M26038; AAA59794.1; -; mRNA.
DR EMBL; U66826; AAD43829.1; -; mRNA.
DR EMBL; AB062112; BAB84521.2; -; mRNA.
DR EMBL; AJ297586; CAC08826.2; -; mRNA.
DR EMBL; AJ297587; CAC08827.1; -; mRNA.
DR EMBL; AJ297582; CAC08822.1; -; mRNA.
DR EMBL; AJ297584; CAC08824.1; -; mRNA.
DR EMBL; AJ302075; CAC44379.1; -; mRNA.
DR EMBL; AJ697893; CAG27026.1; -; mRNA.
DR EMBL; AY961075; AAX63463.1; -; mRNA.
DR EMBL; AY961068; AAX63456.1; -; mRNA.
DR EMBL; AY961062; AAX63450.1; -; mRNA.
DR EMBL; DQ090958; AAY96423.1; -; mRNA.
DR EMBL; AY961072; AAX63460.1; -; mRNA.
DR EMBL; AY961065; AAX63453.1; -; mRNA.
DR EMBL; HM067845; ADI59557.1; -; mRNA.
DR EMBL; HM067846; ADI59558.1; -; mRNA.
DR EMBL; HM067847; ADI59559.1; -; mRNA.
DR EMBL; HM067849; ADI59561.1; -; mRNA.
DR EMBL; HM067854; ADI59566.1; -; mRNA.
DR EMBL; HM067857; ADI59569.1; -; mRNA.
DR EMBL; HM067862; ADI59574.1; -; mRNA.
DR EMBL; HG974579; CDP32889.1; -; mRNA.
DR EMBL; HG974591; CDP32901.1; -; mRNA.
DR EMBL; HG974572; CDP32882.1; -; mRNA.
DR EMBL; LC257777; BBD34095.1; -; mRNA.
DR EMBL; LC257802; BBD34120.1; -; mRNA.
DR EMBL; LC257804; BBD34122.1; -; mRNA.
DR EMBL; LC257806; BBD34124.1; -; mRNA.
DR EMBL; LC257807; BBD34125.1; -; mRNA.
DR EMBL; AY663400; AAU87993.1; -; Genomic_DNA.
DR EMBL; AY663415; AAU88035.1; -; Genomic_DNA.
DR EMBL; AY663413; AAU88029.1; -; Genomic_DNA.
DR EMBL; AY663408; AAU88014.1; -; Genomic_DNA.
DR EMBL; AY663406; AAU88008.1; -; Genomic_DNA.
DR EMBL; AY663414; AAU88033.1; -; Genomic_DNA.
DR EMBL; AY663411; AAU88023.1; -; Genomic_DNA.
DR EMBL; AY663396; AAU87983.1; -; Genomic_DNA.
DR EMBL; AY663395; AAU87979.1; -; Genomic_DNA.
DR EMBL; AM419948; CAL99240.1; -; Genomic_DNA.
DR EMBL; L42143; AAA67104.1; -; mRNA.
DR EMBL; L76133; AAL40069.1; -; mRNA.
DR EMBL; LK391782; CDR98308.1; -; mRNA.
DR EMBL; LT963704; SOT79998.1; -; mRNA.
DR EMBL; AK289463; BAF82152.1; -; mRNA.
DR EMBL; AK293020; BAF85709.1; -; mRNA.
DR EMBL; BC001023; AAH01023.1; -; mRNA.
DR EMBL; BC007920; AAH07920.1; -; mRNA.
DR EMBL; BC033827; AAH33827.1; -; mRNA.
DR EMBL; BC108922; AAI08923.1; -; mRNA.
DR EMBL; AL137064; CAC19360.1; -; Genomic_DNA.
DR EMBL; CR753309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS47409.1; -.
DR RefSeq; NP_001230894.1; NM_001243965.1.
DR RefSeq; NP_002115.2; NM_002124.3.
DR RefSeq; XP_011546040.1; XM_011547738.2.
DR PDB; 1A6A; X-ray; 2.75 A; B=34-220.
DR PDB; 1AQD; X-ray; 2.45 A; B/E/H/K=30-227.
DR PDB; 1BX2; X-ray; 2.60 A; B/E=32-222.
DR PDB; 1D5M; X-ray; 2.00 A; B=30-221.
DR PDB; 1D5X; X-ray; 2.45 A; B=30-221.
DR PDB; 1D5Z; X-ray; 2.00 A; B=30-221.
DR PDB; 1D6E; X-ray; 2.45 A; B=30-221.
DR PDB; 1DLH; X-ray; 2.80 A; B/E=32-219.
DR PDB; 1FYT; X-ray; 2.60 A; B=30-221.
DR PDB; 1HXY; X-ray; 2.60 A; B=30-219.
DR PDB; 1J8H; X-ray; 2.40 A; B=30-221.
DR PDB; 1JWM; X-ray; 2.70 A; B=30-219.
DR PDB; 1JWS; X-ray; 2.60 A; B=30-219.
DR PDB; 1JWU; X-ray; 2.30 A; B=30-219.
DR PDB; 1KG0; X-ray; 2.65 A; B=32-219.
DR PDB; 1KLG; X-ray; 2.40 A; B=30-219.
DR PDB; 1KLU; X-ray; 1.93 A; B=30-219.
DR PDB; 1LO5; X-ray; 3.20 A; B=30-219.
DR PDB; 1PYW; X-ray; 2.10 A; B=30-219.
DR PDB; 1R5I; X-ray; 2.60 A; B/F=30-219.
DR PDB; 1SEB; X-ray; 2.70 A; B/F=30-221.
DR PDB; 1SJE; X-ray; 2.45 A; B=30-219.
DR PDB; 1SJH; X-ray; 2.25 A; B=30-219.
DR PDB; 1T5W; X-ray; 2.40 A; B/E=30-219.
DR PDB; 1T5X; X-ray; 2.50 A; B=30-219.
DR PDB; 1YMM; X-ray; 3.50 A; B=30-227.
DR PDB; 2FSE; X-ray; 3.10 A; B/D=33-219.
DR PDB; 2G9H; X-ray; 2.00 A; B=30-219.
DR PDB; 2IAM; X-ray; 2.80 A; B=30-219.
DR PDB; 2IAN; X-ray; 2.80 A; B/G/L/Q=30-219.
DR PDB; 2ICW; X-ray; 2.41 A; B/E=30-219.
DR PDB; 2IPK; X-ray; 2.30 A; B=30-219.
DR PDB; 2OJE; X-ray; 3.00 A; B/F=30-219.
DR PDB; 2SEB; X-ray; 2.50 A; B=30-221.
DR PDB; 2WBJ; X-ray; 3.00 A; B/F=30-227.
DR PDB; 2XN9; X-ray; 2.30 A; E=30-219.
DR PDB; 3L6F; X-ray; 2.10 A; B=30-221.
DR PDB; 3O6F; X-ray; 2.80 A; B/F=29-221.
DR PDB; 3PDO; X-ray; 1.95 A; B=30-227.
DR PDB; 3PGC; X-ray; 2.66 A; B/E=30-227.
DR PDB; 3PGD; X-ray; 2.72 A; B/E=30-227.
DR PDB; 3QXA; X-ray; 2.71 A; B/E=30-219.
DR PDB; 3QXD; X-ray; 2.30 A; B/E=30-219.
DR PDB; 3S4S; X-ray; 2.40 A; B/E=30-221.
DR PDB; 3S5L; X-ray; 2.10 A; B/E=30-221.
DR PDB; 3T0E; X-ray; 4.00 A; B=30-221.
DR PDB; 4AEN; X-ray; 2.20 A; B=30-227.
DR PDB; 4AH2; X-ray; 2.36 A; B=30-227.
DR PDB; 4C56; X-ray; 2.90 A; E/K=30-219.
DR PDB; 4E41; X-ray; 2.60 A; B/G=30-219.
DR PDB; 4FQX; X-ray; 2.60 A; B=30-221.
DR PDB; 4GBX; X-ray; 3.00 A; B=30-220.
DR PDB; 4I5B; X-ray; 2.12 A; B/E=31-222.
DR PDB; 4IS6; X-ray; 2.50 A; B=30-221.
DR PDB; 4MCY; X-ray; 2.30 A; B=30-219.
DR PDB; 4MCZ; X-ray; 2.41 A; B=30-219.
DR PDB; 4MD0; X-ray; 2.19 A; B=30-219.
DR PDB; 4MD4; X-ray; 1.95 A; B=30-219.
DR PDB; 4MD5; X-ray; 1.65 A; B=30-219.
DR PDB; 4MDI; X-ray; 2.00 A; B=30-219.
DR PDB; 4MDJ; X-ray; 1.70 A; B=30-219.
DR PDB; 4OV5; X-ray; 2.20 A; B/E/H/K/N/Q=30-219.
DR PDB; 4X5W; X-ray; 1.34 A; B=30-227.
DR PDB; 4X5X; X-ray; 3.20 A; B/D=30-227.
DR PDB; 4Y19; X-ray; 2.50 A; B=30-219.
DR PDB; 4Y1A; X-ray; 4.00 A; B=30-219.
DR PDB; 5JLZ; X-ray; 1.99 A; B/D=30-219.
DR PDB; 5LAX; X-ray; 2.60 A; B/D=30-219.
DR PDB; 5NI9; X-ray; 1.33 A; B=30-219.
DR PDB; 5NIG; X-ray; 1.35 A; B=30-219.
DR PDB; 6BIJ; X-ray; 2.10 A; B=31-219.
DR PDB; 6BIL; X-ray; 2.40 A; B=30-219.
DR PDB; 6BIN; X-ray; 2.50 A; B=30-219.
DR PDB; 6BIR; X-ray; 2.30 A; B=30-219.
DR PDB; 6BIV; X-ray; 2.90 A; A=30-219.
DR PDB; 6BIX; X-ray; 2.20 A; B=30-219.
DR PDB; 6BIY; X-ray; 2.05 A; B=30-219.
DR PDB; 6BIZ; X-ray; 2.10 A; B=30-219.
DR PDB; 6CPL; X-ray; 2.45 A; B=30-219.
DR PDB; 6CPN; X-ray; 2.00 A; B=30-219.
DR PDB; 6CPO; X-ray; 2.40 A; B/E=30-219.
DR PDB; 6CQJ; X-ray; 2.75 A; B/E/H=31-219.
DR PDB; 6CQL; X-ray; 2.40 A; B=30-219.
DR PDB; 6CQN; X-ray; 2.50 A; B=30-219.
DR PDB; 6CQQ; X-ray; 2.80 A; B/G=30-219.
DR PDB; 6CQR; X-ray; 3.04 A; B/G=30-219.
DR PDB; 6HBY; X-ray; 1.95 A; B/E=30-219.
DR PDB; 6NIX; X-ray; 2.10 A; B=30-219.
DR PDB; 6QZA; X-ray; 3.09 A; BBB/EEE=30-219.
DR PDB; 6QZC; X-ray; 1.64 A; BBB=30-219.
DR PDB; 6QZD; X-ray; 2.66 A; BBB/EEE=30-219.
DR PDB; 6R0E; X-ray; 1.91 A; BBB=30-219.
DR PDB; 6V0Y; X-ray; 2.70 A; B=30-219.
DR PDB; 6V13; X-ray; 2.75 A; B=30-219.
DR PDB; 6V15; X-ray; 2.80 A; B=30-219.
DR PDB; 6V18; X-ray; 2.35 A; B=30-219.
DR PDB; 6V19; X-ray; 2.60 A; B=30-219.
DR PDB; 6V1A; X-ray; 2.29 A; B=30-219.
DR PDBsum; 1A6A; -.
DR PDBsum; 1AQD; -.
DR PDBsum; 1BX2; -.
DR PDBsum; 1D5M; -.
DR PDBsum; 1D5X; -.
DR PDBsum; 1D5Z; -.
DR PDBsum; 1D6E; -.
DR PDBsum; 1DLH; -.
DR PDBsum; 1FYT; -.
DR PDBsum; 1HXY; -.
DR PDBsum; 1J8H; -.
DR PDBsum; 1JWM; -.
DR PDBsum; 1JWS; -.
DR PDBsum; 1JWU; -.
DR PDBsum; 1KG0; -.
DR PDBsum; 1KLG; -.
DR PDBsum; 1KLU; -.
DR PDBsum; 1LO5; -.
DR PDBsum; 1PYW; -.
DR PDBsum; 1R5I; -.
DR PDBsum; 1SEB; -.
DR PDBsum; 1SJE; -.
DR PDBsum; 1SJH; -.
DR PDBsum; 1T5W; -.
DR PDBsum; 1T5X; -.
DR PDBsum; 1YMM; -.
DR PDBsum; 2FSE; -.
DR PDBsum; 2G9H; -.
DR PDBsum; 2IAM; -.
DR PDBsum; 2IAN; -.
DR PDBsum; 2ICW; -.
DR PDBsum; 2IPK; -.
DR PDBsum; 2OJE; -.
DR PDBsum; 2SEB; -.
DR PDBsum; 2WBJ; -.
DR PDBsum; 2XN9; -.
DR PDBsum; 3L6F; -.
DR PDBsum; 3O6F; -.
DR PDBsum; 3PDO; -.
DR PDBsum; 3PGC; -.
DR PDBsum; 3PGD; -.
DR PDBsum; 3QXA; -.
DR PDBsum; 3QXD; -.
DR PDBsum; 3S4S; -.
DR PDBsum; 3S5L; -.
DR PDBsum; 3T0E; -.
DR PDBsum; 4AEN; -.
DR PDBsum; 4AH2; -.
DR PDBsum; 4C56; -.
DR PDBsum; 4E41; -.
DR PDBsum; 4FQX; -.
DR PDBsum; 4GBX; -.
DR PDBsum; 4I5B; -.
DR PDBsum; 4IS6; -.
DR PDBsum; 4MCY; -.
DR PDBsum; 4MCZ; -.
DR PDBsum; 4MD0; -.
DR PDBsum; 4MD4; -.
DR PDBsum; 4MD5; -.
DR PDBsum; 4MDI; -.
DR PDBsum; 4MDJ; -.
DR PDBsum; 4OV5; -.
DR PDBsum; 4X5W; -.
DR PDBsum; 4X5X; -.
DR PDBsum; 4Y19; -.
DR PDBsum; 4Y1A; -.
DR PDBsum; 5JLZ; -.
DR PDBsum; 5LAX; -.
DR PDBsum; 5NI9; -.
DR PDBsum; 5NIG; -.
DR PDBsum; 6BIJ; -.
DR PDBsum; 6BIL; -.
DR PDBsum; 6BIN; -.
DR PDBsum; 6BIR; -.
DR PDBsum; 6BIV; -.
DR PDBsum; 6BIX; -.
DR PDBsum; 6BIY; -.
DR PDBsum; 6BIZ; -.
DR PDBsum; 6CPL; -.
DR PDBsum; 6CPN; -.
DR PDBsum; 6CPO; -.
DR PDBsum; 6CQJ; -.
DR PDBsum; 6CQL; -.
DR PDBsum; 6CQN; -.
DR PDBsum; 6CQQ; -.
DR PDBsum; 6CQR; -.
DR PDBsum; 6HBY; -.
DR PDBsum; 6NIX; -.
DR PDBsum; 6QZA; -.
DR PDBsum; 6QZC; -.
DR PDBsum; 6QZD; -.
DR PDBsum; 6R0E; -.
DR PDBsum; 6V0Y; -.
DR PDBsum; 6V13; -.
DR PDBsum; 6V15; -.
DR PDBsum; 6V18; -.
DR PDBsum; 6V19; -.
DR PDBsum; 6V1A; -.
DR AlphaFoldDB; P01911; -.
DR SMR; P01911; -.
DR BioGRID; 109368; 162.
DR IntAct; P01911; 33.
DR MINT; P01911; -.
DR STRING; 9606.ENSP00000353099; -.
DR ChEMBL; CHEMBL3831291; -.
DR DrugBank; DB05121; 1D09C3.
DR DrugBank; DB11294; Coccidioides immitis spherule.
DR DrugBank; DB05259; Glatiramer.
DR GlyConnect; 1369; 11 N-Linked glycans (1 site).
DR GlyConnect; 1370; 3 N-Linked glycans (1 site).
DR GlyConnect; 1371; 3 N-Linked glycans (1 site).
DR GlyConnect; 1372; 3 N-Linked glycans (1 site).
DR GlyConnect; 1373; 11 N-Linked glycans (1 site).
DR GlyConnect; 1374; 3 N-Linked glycans (1 site).
DR GlyConnect; 1375; 4 N-Linked glycans (1 site).
DR GlyConnect; 1376; 11 N-Linked glycans (1 site).
DR GlyGen; P01911; 1 site.
DR iPTMnet; P01911; -.
DR PhosphoSitePlus; P01911; -.
DR SwissPalm; P01911; -.
DR BioMuta; HLA-DRB1; -.
DR DMDM; 122253; -.
DR jPOST; P01911; -.
DR MassIVE; P01911; -.
DR PaxDb; P01911; -.
DR PeptideAtlas; P01911; -.
DR PRIDE; P01911; -.
DR ProteomicsDB; 51511; -.
DR ProteomicsDB; 51512; -.
DR ProteomicsDB; 51688; -.
DR ProteomicsDB; 52982; -.
DR ProteomicsDB; 52983; -.
DR ProteomicsDB; 53717; -.
DR ProteomicsDB; 61281; -.
DR ProteomicsDB; 61555; -.
DR ProteomicsDB; 61557; -.
DR ProteomicsDB; 65857; -.
DR ProteomicsDB; 75737; -.
DR ProteomicsDB; 80078; -.
DR ProteomicsDB; 83918; -.
DR TopDownProteomics; P01911; -.
DR ABCD; P01911; 1 sequenced antibody.
DR Antibodypedia; 4207; 1039 antibodies from 36 providers.
DR DNASU; 3123; -.
DR Ensembl; ENST00000360004.5; ENSP00000353099.5; ENSG00000196126.11.
DR GeneID; 3123; -.
DR KEGG; hsa:3123; -.
DR MANE-Select; ENST00000360004.6; ENSP00000353099.5; NM_002124.4; NP_002115.2.
DR UCSC; uc011gjy.3; human.
DR UCSC; uc063uqx.1; human.
DR UCSC; uc063vvt.1; human.
DR CTD; 3123; -.
DR DisGeNET; 3123; -.
DR GeneCards; HLA-DRB1; -.
DR HGNC; HGNC:4948; HLA-DRB1.
DR HPA; ENSG00000196126; Tissue enhanced (lung, lymphoid tissue).
DR MalaCards; HLA-DRB1; -.
DR MIM; 126200; phenotype.
DR MIM; 180300; phenotype.
DR MIM; 181000; phenotype.
DR neXtProt; NX_P01911; -.
DR NIAGADS; ENSG00000196126; -.
DR OpenTargets; ENSG00000196126; -.
DR Orphanet; 747; Autoimmune pulmonary alveolar proteinosis.
DR Orphanet; 703; Bullous pemphigoid.
DR Orphanet; 220393; Diffuse cutaneous systemic sclerosis.
DR Orphanet; 545; Follicular lymphoma.
DR Orphanet; 397; Giant cell arteritis.
DR Orphanet; 220402; Limited cutaneous systemic sclerosis.
DR Orphanet; 220407; Limited systemic sclerosis.
DR Orphanet; 2073; Narcolepsy type 1.
DR Orphanet; 83465; Narcolepsy type 2.
DR Orphanet; 555; NON RARE IN EUROPE: Celiac disease.
DR Orphanet; 243377; NON RARE IN EUROPE: Diabetes mellitus type 1.
DR Orphanet; 802; NON RARE IN EUROPE: Multiple sclerosis.
DR Orphanet; 284130; NON RARE IN EUROPE: Rheumatoid arthritis.
DR Orphanet; 477738; Pediatric multiple sclerosis.
DR Orphanet; 797; Sarcoidosis.
DR Orphanet; 536; Systemic lupus erythematosus.
DR Orphanet; 85414; Systemic-onset juvenile idiopathic arthritis.
DR PharmGKB; PA35072; -.
DR VEuPathDB; HostDB:ENSG00000196126; -.
DR eggNOG; ENOG502RYBQ; Eukaryota.
DR GeneTree; ENSGT00940000154993; -.
DR HOGENOM; CLU_047501_13_1_1; -.
DR InParanoid; P01911; -.
DR OMA; IYNATEM; -.
DR OrthoDB; 1249505at2759; -.
DR PhylomeDB; P01911; -.
DR TreeFam; TF336626; -.
DR PathwayCommons; P01911; -.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse.
DR Reactome; R-HSA-202433; Generation of second messenger molecules.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-389948; PD-1 signaling.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; P01911; -.
DR SIGNOR; P01911; -.
DR BioGRID-ORCS; 3123; 23 hits in 993 CRISPR screens.
DR ChiTaRS; HLA-DRB1; human.
DR EvolutionaryTrace; P01911; -.
DR GeneWiki; HLA-DRB1; -.
DR GenomeRNAi; 3123; -.
DR Pharos; P01911; Tchem.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P01911; protein.
DR Bgee; ENSG00000196126; Expressed in vermiform appendix and 98 other tissues.
DR ExpressionAtlas; P01911; baseline and differential.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; TAS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0042613; C:MHC class II protein complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
DR GO; GO:0042609; F:CD4 receptor binding; IPI:CAFA.
DR GO; GO:0023026; F:MHC class II protein complex binding; HDA:UniProtKB.
DR GO; GO:0032395; F:MHC class II receptor activity; IDA:UniProtKB.
DR GO; GO:0042605; F:peptide antigen binding; IDA:UniProtKB.
DR GO; GO:0030247; F:polysaccharide binding; IDA:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:UniProtKB.
DR GO; GO:0042608; F:T cell receptor binding; IDA:UniProtKB.
DR GO; GO:0002491; P:antigen processing and presentation of endogenous peptide antigen via MHC class II; IDA:UniProtKB.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:UniProtKB.
DR GO; GO:0016045; P:detection of bacterium; IMP:UniProtKB.
DR GO; GO:0008544; P:epidermis development; TAS:UniProtKB.
DR GO; GO:0006959; P:humoral immune response; IMP:UniProtKB.
DR GO; GO:0006955; P:immune response; IDA:UniProtKB.
DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IDA:UniProtKB.
DR GO; GO:0030225; P:macrophage differentiation; IDA:ARUK-UCL.
DR GO; GO:0002469; P:myeloid dendritic cell antigen processing and presentation; IDA:UniProtKB.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IDA:UniProtKB.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IMP:UniProtKB.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:UniProtKB.
DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IDA:UniProtKB.
DR GO; GO:2000516; P:positive regulation of CD4-positive, alpha-beta T cell activation; IDA:UniProtKB.
DR GO; GO:0032831; P:positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IDA:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:CAFA.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:CAFA.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IDA:CAFA.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:CAFA.
DR GO; GO:0043382; P:positive regulation of memory T cell differentiation; IDA:UniProtKB.
DR GO; GO:0045657; P:positive regulation of monocyte differentiation; IDA:CAFA.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:CAFA.
DR GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:UniProtKB.
DR GO; GO:0002842; P:positive regulation of T cell mediated immune response to tumor cell; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:CAFA.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IDA:CAFA.
DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
DR GO; GO:0032653; P:regulation of interleukin-10 production; IDA:UniProtKB.
DR GO; GO:0032673; P:regulation of interleukin-4 production; IDA:UniProtKB.
DR GO; GO:0045622; P:regulation of T-helper cell differentiation; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0042088; P:T-helper 1 type immune response; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.320.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR InterPro; IPR014745; MHC_II_a/b_N.
DR InterPro; IPR000353; MHC_II_b_N.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00969; MHC_II_beta; 1.
DR SMART; SM00407; IGc1; 1.
DR SMART; SM00921; MHC_II_beta; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Endosome;
KW Glycoprotein; Immunity; Isopeptide bond; Lysosome; Membrane; MHC II;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:6600932,
FT ECO:0000269|PubMed:6947956"
FT CHAIN 30..266
FT /note="HLA class II histocompatibility antigen, DRB1 beta
FT chain"
FT /id="PRO_0000080744"
FT TOPO_DOM 30..227
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 126..214
FT /note="Ig-like C1-type"
FT REGION 30..124
FT /note="Beta-1"
FT REGION 125..227
FT /note="Beta-2"
FT BINDING 86
FT /ligand="a peptide antigen"
FT /ligand_id="ChEBI:CHEBI:166823"
FT /ligand_note="self- and pathogen-derived peptide antigen"
FT /evidence="ECO:0000269|PubMed:31619516,
FT ECO:0000269|PubMed:8145819"
FT BINDING 90
FT /ligand="a peptide antigen"
FT /ligand_id="ChEBI:CHEBI:166823"
FT /ligand_note="self- and pathogen-derived peptide antigen"
FT /evidence="ECO:0000269|PubMed:31619516,
FT ECO:0000269|PubMed:8145819"
FT BINDING 110
FT /ligand="a peptide antigen"
FT /ligand_id="ChEBI:CHEBI:166823"
FT /ligand_note="self- and pathogen-derived peptide antigen"
FT /evidence="ECO:0000269|PubMed:31619516,
FT ECO:0000269|PubMed:8145819"
FT BINDING 111
FT /ligand="a peptide antigen"
FT /ligand_id="ChEBI:CHEBI:166823"
FT /ligand_note="self- and pathogen-derived peptide antigen"
FT /evidence="ECO:0000269|PubMed:31619516,
FT ECO:0000269|PubMed:8145819"
FT BINDING 122
FT /ligand="a peptide antigen"
FT /ligand_id="ChEBI:CHEBI:166823"
FT /ligand_note="self- and pathogen-derived peptide antigen"
FT /evidence="ECO:0000269|PubMed:8145819"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19303388,
FT ECO:0000269|PubMed:24190431"
FT DISULFID 44..108
FT /evidence="ECO:0000269|PubMed:24190431,
FT ECO:0000269|PubMed:31619516, ECO:0000269|PubMed:7477400,
FT ECO:0000269|PubMed:9782128"
FT DISULFID 146..202
FT /evidence="ECO:0000269|PubMed:24190431,
FT ECO:0000269|PubMed:31619516, ECO:0000269|PubMed:7477400,
FT ECO:0000269|PubMed:9782128"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P20039"
FT VARIANT 5
FT /note="K -> R (in allele DRB1*03:01, allele DRB1*03:02,
FT allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03,
FT allele DRB1*08:04, allele DRB1*10:01, allele DRB1*11:01,
FT allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11,
FT allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02,
FT allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03,
FT allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12,
FT allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05,
FT allele DRB1*14:06 and allele DRB1*14:07; dbSNP:rs707953)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15896200,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:2497068,
FT ECO:0000269|PubMed:26396036, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:3456344, ECO:0000269|PubMed:6589154,
FT ECO:0000269|Ref.24, ECO:0000269|Ref.25, ECO:0000269|Ref.26"
FT /id="VAR_082703"
FT VARIANT 6
FT /note="L -> F (in allele DRB1*04:01, allele DRB1*04:02,
FT allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06,
FT allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10 and
FT allele DRB1*04:11; dbSNP:rs17879020)"
FT /evidence="ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:30337930,
FT ECO:0000269|Ref.23"
FT /id="VAR_082704"
FT VARIANT 13
FT /note="T -> A (in allele DRB1*03:01, allele DRB1*03:02,
FT allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04,
FT allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07,
FT allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11,
FT allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02,
FT allele DRB1*08:03, allele DRB1*08:04, allele DRB1*09:01,
FT allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04,
FT allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19,
FT allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01,
FT allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05,
FT allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01,
FT allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and
FT allele DRB1*14:07; dbSNP:rs9270303)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:14574404,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15896200, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:17174751, ECO:0000269|PubMed:21388356,
FT ECO:0000269|PubMed:2497068, ECO:0000269|PubMed:26396036,
FT ECO:0000269|PubMed:30337930, ECO:0000269|PubMed:3110774,
FT ECO:0000269|PubMed:3456344, ECO:0000269|PubMed:3875800,
FT ECO:0000269|PubMed:6589154, ECO:0000269|PubMed:9777332,
FT ECO:0000269|Ref.23, ECO:0000269|Ref.24, ECO:0000269|Ref.25,
FT ECO:0000269|Ref.26"
FT /id="VAR_082705"
FT VARIANT 14
FT /note="A -> V (in allele DRB1*03:01, allele DRB1*03:02,
FT allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03,
FT allele DRB1*08:04, allele DRB1*10:01, allele DRB1*11:01,
FT allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11,
FT allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02,
FT allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03,
FT allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12,
FT allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05,
FT allele DRB1*14:06 and allele DRB1*14:07; dbSNP:rs9270302)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15896200,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:2497068,
FT ECO:0000269|PubMed:26396036, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:3456344, ECO:0000269|PubMed:6589154,
FT ECO:0000269|Ref.24, ECO:0000269|Ref.25, ECO:0000269|Ref.26"
FT /id="VAR_082706"
FT VARIANT 29
FT /note="S -> A (in allele DRB1*01:01, allele DRB1*01:02,
FT allele DRB1*03:01, allele DRB1*03:02, allele DRB1*04:01,
FT allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05,
FT allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08,
FT allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01,
FT allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03,
FT allele DRB1*08:04, allele DRB1*09:01, allele DRB1*10:01,
FT allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06,
FT allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01,
FT allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02,
FT allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07,
FT allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03,
FT allele DRB1*14:05, allele DRB1*14:06, allele DRB1*14:07,
FT allele DRB1*16:01 and allele DRB1*16:02; dbSNP:rs9270299)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:14574404,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15896200, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:17174751, ECO:0000269|PubMed:17345114,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:2497068,
FT ECO:0000269|PubMed:26396036, ECO:0000269|PubMed:2885840,
FT ECO:0000269|PubMed:2998758, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:3110774, ECO:0000269|PubMed:3129499,
FT ECO:0000269|PubMed:3456344, ECO:0000269|PubMed:3571980,
FT ECO:0000269|PubMed:3875800, ECO:0000269|PubMed:6589154,
FT ECO:0000269|PubMed:9777332, ECO:0000269|Ref.23,
FT ECO:0000269|Ref.24, ECO:0000269|Ref.25, ECO:0000269|Ref.26"
FT /id="VAR_082707"
FT VARIANT 33
FT /note="R -> Q (in allele DRB1*07:01 and allele DRB1*09:01;
FT dbSNP:rs17879746)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3110774, ECO:0000269|PubMed:9777332"
FT /id="VAR_082708"
FT VARIANT 38
FT /note="W -> E (in allele DRB1*03:01, allele DRB1*03:02,
FT allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04,
FT allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07,
FT allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11,
FT allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03,
FT allele DRB1*08:04, allele DRB1*10:01, allele DRB1*11:01,
FT allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11,
FT allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02,
FT allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03,
FT allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12,
FT allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05,
FT allele DRB1*14:06 and allele DRB1*14:07; requires 2
FT nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:14574404,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15896200, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:17174751, ECO:0000269|PubMed:21388356,
FT ECO:0000269|PubMed:2497068, ECO:0000269|PubMed:26396036,
FT ECO:0000269|PubMed:30337930, ECO:0000269|PubMed:3110774,
FT ECO:0000269|PubMed:3456344, ECO:0000269|PubMed:3875800,
FT ECO:0000269|PubMed:6589154, ECO:0000269|Ref.23,
FT ECO:0000269|Ref.24, ECO:0000269|Ref.25, ECO:0000269|Ref.26"
FT /id="VAR_082709"
FT VARIANT 38
FT /note="W -> K (in allele DRB1*09:01; requires 2 nucleotide
FT substitutions)"
FT /evidence="ECO:0000269|PubMed:9777332"
FT /id="VAR_082710"
FT VARIANT 39
FT /note="Q -> E (in allele DRB1*10:01; dbSNP:rs9269957)"
FT /evidence="ECO:0000269|PubMed:6589154"
FT /id="VAR_082711"
FT VARIANT 39
FT /note="Q -> Y (in allele DRB1*03:01, allele DRB1*03:02,
FT allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03,
FT allele DRB1*08:04, allele DRB1*11:01, allele DRB1*11:04,
FT allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19,
FT allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01,
FT allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05,
FT allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01,
FT allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and
FT allele DRB1*14:07; requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15896200,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:2497068,
FT ECO:0000269|PubMed:26396036, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:3456344, ECO:0000269|PubMed:6589154,
FT ECO:0000269|Ref.24, ECO:0000269|Ref.25, ECO:0000269|Ref.26"
FT /id="VAR_082712"
FT VARIANT 40
FT /note="P -> D (in allele DRB1*09:01; requires 2 nucleotide
FT substitutions)"
FT /evidence="ECO:0000269|PubMed:9777332"
FT /id="VAR_082713"
FT VARIANT 40
FT /note="P -> G (in allele DRB1*07:01; requires 2 nucleotide
FT substitutions)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3110774, ECO:0000269|Ref.23"
FT /id="VAR_082714"
FT VARIANT 40
FT /note="P -> L (in allele DRB1*01:01 and allele DRB1*01:02;
FT associated with increased risk for rheumatoid arthritis;
FT dbSNP:rs17878703)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17345114,
FT ECO:0000269|PubMed:22286218, ECO:0000269|PubMed:2998758"
FT /id="VAR_082715"
FT VARIANT 40
FT /note="P -> S (in allele DRB1*03:01, allele DRB1*03:02,
FT allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03,
FT allele DRB1*08:04, allele DRB1*11:01, allele DRB1*11:04,
FT allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19,
FT allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01,
FT allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05,
FT allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01,
FT allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and
FT allele DRB1*14:07; dbSNP:rs9269955)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15896200,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:2497068,
FT ECO:0000269|PubMed:26396036, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:3456344, ECO:0000269|PubMed:6589154,
FT ECO:0000269|Ref.24, ECO:0000269|Ref.25, ECO:0000269|Ref.26"
FT /id="VAR_082716"
FT VARIANT 40
FT /note="P -> V (in allele DRB1*04:01, allele DRB1*04:02,
FT allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06,
FT allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10,
FT allele DRB1*04:11 and allele DRB1*10:01; associated with
FT increased risk for rheumatoid arthritis; requires 2
FT nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:22286218,
FT ECO:0000269|PubMed:30337930, ECO:0000269|PubMed:3875800,
FT ECO:0000269|PubMed:6589154, ECO:0000269|Ref.23"
FT /id="VAR_082717"
FT VARIANT 41
FT /note="K -> T (in allele DRB1*03:01, allele DRB1*03:02,
FT allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03,
FT allele DRB1*08:04, allele DRB1*11:01, allele DRB1*11:04,
FT allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19,
FT allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01,
FT allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05,
FT allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01,
FT allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and
FT allele DRB1*14:07; dbSNP:rs1136756)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15896200,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:2497068,
FT ECO:0000269|PubMed:26396036, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:3456344, ECO:0000269|PubMed:6589154,
FT ECO:0000269|Ref.24, ECO:0000269|Ref.25, ECO:0000269|Ref.26"
FT /id="VAR_082718"
FT VARIANT 42
FT /note="R -> F (in allele DRB1*01:01, allele DRB1*01:02,
FT allele DRB1*09:01 and allele DRB1*10:01; associated with
FT increased risk for rheumatoid arthritis; requires 2
FT nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17345114,
FT ECO:0000269|PubMed:22286218, ECO:0000269|PubMed:2998758,
FT ECO:0000269|PubMed:6589154"
FT /id="VAR_082719"
FT VARIANT 42
FT /note="R -> G (in allele DRB1*08:01, allele DRB1*08:02,
FT allele DRB1*08:03, allele DRB1*08:04, allele DRB1*12:01 and
FT allele DRB1*12:02; dbSNP:rs1136758)"
FT /evidence="ECO:0000269|PubMed:12028552,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:2497068,
FT ECO:0000269|PubMed:9777332, ECO:0000269|Ref.25"
FT /id="VAR_082720"
FT VARIANT 42
FT /note="R -> H (in allele DRB1*04:01, allele DRB1*04:02,
FT allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06,
FT allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10 and
FT allele DRB1*04:11; associated with increased risk for
FT rheumatoid arthritis)"
FT /evidence="ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:22286218,
FT ECO:0000269|PubMed:30337930, ECO:0000269|PubMed:3875800,
FT ECO:0000269|Ref.23"
FT /id="VAR_082721"
FT VARIANT 42
FT /note="R -> S (in allele DRB1*03:01, allele DRB1*03:02,
FT allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06,
FT allele DRB1*11:11, allele DRB1*11:19, allele DRB1*13:01,
FT allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05,
FT allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01,
FT allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and
FT allele DRB1*14:07; dbSNP:rs9269951)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12358860, ECO:0000269|PubMed:12652907,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15896200, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:17174751, ECO:0000269|PubMed:21388356,
FT ECO:0000269|PubMed:26396036, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:3456344, ECO:0000269|PubMed:6589154,
FT ECO:0000269|Ref.24, ECO:0000269|Ref.25, ECO:0000269|Ref.26"
FT /id="VAR_082722"
FT VARIANT 42
FT /note="R -> Y (in allele DRB1*07:01; requires 2 nucleotide
FT substitutions)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3110774, ECO:0000269|Ref.23"
FT /id="VAR_082723"
FT VARIANT 43
FT /note="E -> K (in allele DRB1*07:01; dbSNP:rs17882014)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3110774, ECO:0000269|Ref.23"
FT /id="VAR_082724"
FT VARIANT 45
FT /note="H -> Q (in allele DRB1*14:05; dbSNP:rs17879981)"
FT /evidence="ECO:0000269|PubMed:12652907,
FT ECO:0000269|PubMed:16140993"
FT /id="VAR_082725"
FT VARIANT 45
FT /note="H -> Y (in allele DRB1*08:01, allele DRB1*08:02,
FT allele DRB1*08:03, allele DRB1*08:04, allele DRB1*12:01 and
FT allele DRB1*12:02; dbSNP:rs17879702)"
FT /evidence="ECO:0000269|PubMed:12028552,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:2497068,
FT ECO:0000269|Ref.25"
FT /id="VAR_082726"
FT VARIANT 54
FT /note="R -> Q (in allele DRB1*07:01; dbSNP:rs17885382)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3110774"
FT /id="VAR_082727"
FT VARIANT 55
FT /note="F -> L (in allele DRB1*01:01, allele DRB1*01:02,
FT allele DRB1*10:01, allele DRB1*12:01 and allele DRB1*12:02;
FT dbSNP:rs1059572)"
FT /evidence="ECO:0000269|PubMed:12028552,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:17345114, ECO:0000269|PubMed:21388356,
FT ECO:0000269|PubMed:2998758, ECO:0000269|PubMed:6589154"
FT /id="VAR_082728"
FT VARIANT 55
FT /note="F -> Y (in allele DRB1*03:01, allele DRB1*09:01;
FT dbSNP:rs1059569)"
FT /evidence="ECO:0000269|PubMed:6589154,
FT ECO:0000269|PubMed:9777332"
FT /id="VAR_082729"
FT VARIANT 57
FT /note="D -> E (in allele DRB1*01:01, allele DRB1*01:02,
FT allele DRB1*03:02, allele DRB1*07:01, allele DRB1*10:01,
FT allele DRB1*12:01, allele DRB1*12:02, allele DRB1*14:03 and
FT allele DRB1*14:06; dbSNP:rs1059575)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:17345114, ECO:0000269|PubMed:21388356,
FT ECO:0000269|PubMed:2998758, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:3110774, ECO:0000269|PubMed:6589154,
FT ECO:0000269|Ref.23, ECO:0000269|Ref.26"
FT /id="VAR_082730"
FT VARIANT 57
FT /note="D -> H (in allele DRB1*09:01; dbSNP:rs17878947)"
FT /evidence="ECO:0000269|PubMed:9777332"
FT /id="VAR_082731"
FT VARIANT 59
FT /note="Y -> C (in allele DRB1*01:01 and allele DRB1*01:02;
FT dbSNP:rs3175105)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17345114,
FT ECO:0000269|PubMed:2998758"
FT /id="VAR_082732"
FT VARIANT 59
FT /note="Y -> G (in allele DRB1*09:01; requires 2 nucleotide
FT substitutions)"
FT /evidence="ECO:0000269|PubMed:9777332"
FT /id="VAR_082733"
FT VARIANT 59
FT /note="Y -> H (in allele DRB1*12:01, allele DRB1*12:02 and
FT allele DRB1*15:03; dbSNP:rs11554462)"
FT /evidence="ECO:0000269|PubMed:12028552,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356"
FT /id="VAR_082734"
FT VARIANT 59
FT /note="Y -> L (in allele DRB1*07:01; requires 2 nucleotide
FT substitutions)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3110774"
FT /id="VAR_082735"
FT VARIANT 59
FT /note="Y -> R (in allele DRB1*10:01; requires 2 nucleotide
FT substitutions)"
FT /evidence="ECO:0000269|PubMed:6589154"
FT /id="VAR_082736"
FT VARIANT 60
FT /note="F -> I (in allele DRB1*01:01, allele DRB1*01:02 and
FT allele DRB1*09:01; dbSNP:rs17882300)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17345114,
FT ECO:0000269|PubMed:2998758, ECO:0000269|PubMed:9777332"
FT /id="VAR_082737"
FT VARIANT 60
FT /note="F -> V (in allele DRB1*10:01; dbSNP:rs17882300)"
FT /evidence="ECO:0000269|PubMed:6589154"
FT /id="VAR_082738"
FT VARIANT 61
FT /note="Y -> H (in allele DRB1*03:01, allele DRB1*03:02,
FT allele DRB1*10:01, allele DRB1*12:01, allele DRB1*12:02,
FT allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:05,
FT allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05,
FT allele DRB1*14:06 and allele DRB1*14:07; dbSNP:rs1064664)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:12652907,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15896200, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:6589154, ECO:0000269|Ref.24,
FT ECO:0000269|Ref.26"
FT /id="VAR_082739"
FT VARIANT 62
FT /note="N -> H (in allele DRB1*04:01, allele DRB1*04:02,
FT allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06,
FT allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10 and
FT allele DRB1*04:11; dbSNP:rs17879995)"
FT /evidence="ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:3875800, ECO:0000269|Ref.23"
FT /id="VAR_082740"
FT VARIANT 66
FT /note="S -> F (in allele DRB1*07:01, allele DRB1*14:01,
FT allele DRB1*14:05 and allele DRB1*14:07; dbSNP:rs707957)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:3110774"
FT /id="VAR_082741"
FT VARIANT 66
FT /note="S -> L (in allele DRB1*12:01 and allele DRB1*12:02)"
FT /evidence="ECO:0000269|PubMed:12028552,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:21388356"
FT /id="VAR_082742"
FT VARIANT 66
FT /note="S -> N (in allele DRB1*03:01, allele DRB1*03:02,
FT allele DRB1*09:01, allele DRB1*13:01, allele DRB1*13:02,
FT allele DRB1*13:05, allele DRB1*14:03 and allele DRB1*14:06;
FT dbSNP:rs796324593)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15896200, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:30337930, ECO:0000269|PubMed:6589154,
FT ECO:0000269|PubMed:9777332, ECO:0000269|Ref.24,
FT ECO:0000269|Ref.26"
FT /id="VAR_082743"
FT VARIANT 66
FT /note="S -> Y (in allele DRB1*04:01, allele DRB1*04:02,
FT allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:07,
FT allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11,
FT allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03,
FT allele DRB1*08:04, allele DRB1*10:01, allele DRB1*11:01,
FT allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11,
FT allele DRB1*11:19, allele DRB1*13:03, allele DRB1*13:07 and
FT allele DRB1*13:12; dbSNP:rs707957)"
FT /evidence="ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:2497068,
FT ECO:0000269|PubMed:26396036, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:3456344, ECO:0000269|PubMed:3875800,
FT ECO:0000269|PubMed:6589154, ECO:0000269|Ref.23,
FT ECO:0000269|Ref.25"
FT /id="VAR_082744"
FT VARIANT 67
FT /note="V -> A (in allele DRB1*10:01; dbSNP:rs17878951)"
FT /evidence="ECO:0000269|PubMed:6589154"
FT /id="VAR_082745"
FT VARIANT 67
FT /note="V -> L (in allele DRB1*12:01 and allele DRB1*12:02;
FT dbSNP:rs17878614)"
FT /evidence="ECO:0000269|PubMed:12028552,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:21388356"
FT /id="VAR_082746"
FT VARIANT 69
FT /note="F -> Y (in allele DRB1*10:01; dbSNP:rs17882455)"
FT /evidence="ECO:0000269|PubMed:6589154"
FT /id="VAR_082747"
FT VARIANT 76
FT /note="F -> Y (in allele DRB1*01:01, allele DRB1*01:02,
FT allele DRB1*03:02, allele DRB1*04:01, allele DRB1*04:02,
FT allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06,
FT allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10,
FT allele DRB1*04:11, allele DRB1*07:01, allele DRB1*08:01,
FT allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04,
FT allele DRB1*09:01, allele DRB1*10:01, allele DRB1*13:03,
FT allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01,
FT allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06,
FT allele DRB1*14:07, allele DRB1*16:01 and allele DRB1*16:02;
FT dbSNP:rs17884945)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12358860, ECO:0000269|PubMed:12652907,
FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:17174751, ECO:0000269|PubMed:17345114,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:2497068,
FT ECO:0000269|PubMed:26396036, ECO:0000269|PubMed:2885840,
FT ECO:0000269|PubMed:2998758, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:3110774, ECO:0000269|PubMed:3129499,
FT ECO:0000269|PubMed:3571980, ECO:0000269|PubMed:3875800,
FT ECO:0000269|PubMed:6589154, ECO:0000269|PubMed:9777332,
FT ECO:0000269|Ref.23, ECO:0000269|Ref.25, ECO:0000269|Ref.26"
FT /id="VAR_082748"
FT VARIANT 86
FT /note="D -> A (in allele DRB1*14:01, allele DRB1*14:07;
FT dbSNP:rs17885129)"
FT /evidence="ECO:0000269|PubMed:11972886"
FT /id="VAR_082749"
FT VARIANT 86
FT /note="D -> S (in allele DRB1*04:05, allele DRB1*04:10;
FT allele DRB1*04:11, allele DRB1*08:01, allele DRB1*08:03,
FT allele DRB1*13:03 and allele DRB1*13:12; requires 2
FT nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:26396036,
FT ECO:0000269|Ref.23, ECO:0000269|Ref.25"
FT /id="VAR_082750"
FT VARIANT 86
FT /note="D -> V (in allele DRB1*07:01, allele DRB1*09:01,
FT allele DRB1*12:01 and allele DRB1*12:02; dbSNP:rs17885129)"
FT /evidence="ECO:0000269|PubMed:12028552,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:3110774,
FT ECO:0000269|PubMed:9777332"
FT /id="VAR_082751"
FT VARIANT 87
FT /note="A -> E (in allele DRB1*11:01, allele DRB1*11:04,
FT allele DRB1*11:06, allele DRB1*11:11 and allele
FT DRB1*11:19)"
FT /evidence="ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:17174751, ECO:0000269|PubMed:26396036,
FT ECO:0000269|PubMed:3456344"
FT /id="VAR_082752"
FT VARIANT 89
FT /note="Y -> H (in allele DRB1*14:01, allele DRB1*14:07;
FT dbSNP:rs17882583)"
FT /evidence="ECO:0000269|PubMed:11972886"
FT /id="VAR_082753"
FT VARIANT 89
FT /note="Y -> S (in allele DRB1*07:01, allele DRB1*09:01,
FT allele DRB1*12:01 and allele DRB1*12:02; dbSNP:rs1059586)"
FT /evidence="ECO:0000269|PubMed:12028552,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:3110774,
FT ECO:0000269|PubMed:9777332"
FT /id="VAR_082754"
FT VARIANT 96
FT /note="I -> F (in allele DRB1*08:01, allele DRB1*08:02,
FT allele DRB1*08:04, allele DRB1*09:01, allele DRB1*11:01,
FT allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11,
FT allele DRB1*12:02, allele DRB1*13:05, allele DRB1*13:07 and
FT allele DRB1*16:01; dbSNP:rs17886918)"
FT /evidence="ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:15896200, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:2497068,
FT ECO:0000269|PubMed:26396036, ECO:0000269|PubMed:2885840,
FT ECO:0000269|PubMed:30337930, ECO:0000269|PubMed:3456344,
FT ECO:0000269|PubMed:3571980, ECO:0000269|PubMed:9777332,
FT ECO:0000269|Ref.25"
FT /id="VAR_082755"
FT VARIANT 96
FT /note="I -> L (in allele DRB1*01:01, allele DRB1*01:02,
FT allele DRB1*03:01, allele DRB1*03:02, allele DRB1*04:01,
FT allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06,
FT allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10,
FT allele DRB1*04:11, allele DRB1*10:01, allele DRB1*14:01,
FT allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06,
FT allele DRB1*14:07 and allele DRB1*16:02; dbSNP:rs17886918)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:14574404,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:17174751, ECO:0000269|PubMed:17345114,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:2998758,
FT ECO:0000269|PubMed:30337930, ECO:0000269|PubMed:3129499,
FT ECO:0000269|PubMed:3875800, ECO:0000269|PubMed:6589154,
FT ECO:0000269|Ref.23, ECO:0000269|Ref.26"
FT /id="VAR_082756"
FT VARIANT 99
FT /note="Q -> D (in allele DRB1*04:02, allele DRB1*07:01,
FT allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03,
FT allele DRB1*08:04, allele DRB1*11:01, allele DRB1*11:04,
FT allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19,
FT allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01,
FT allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05,
FT allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:03,
FT allele DRB1*16:01 and allele DRB1*16:02; requires 2
FT nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15896200, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:17174751, ECO:0000269|PubMed:21388356,
FT ECO:0000269|PubMed:2497068, ECO:0000269|PubMed:26396036,
FT ECO:0000269|PubMed:2885840, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:3110774, ECO:0000269|PubMed:3129499,
FT ECO:0000269|PubMed:3456344, ECO:0000269|PubMed:3571980,
FT ECO:0000269|PubMed:3875800, ECO:0000269|Ref.24,
FT ECO:0000269|Ref.25"
FT /id="VAR_082757"
FT VARIANT 99
FT /note="Q -> R (in allele DRB1*09:01, allele DRB1*10:01,
FT allele DRB1*14:01, allele DRB1*14:05 and allele DRB1*14:07;
FT dbSNP:rs17884070)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:6589154, ECO:0000269|PubMed:9777332"
FT /id="VAR_082758"
FT VARIANT 100
FT /note="A -> E (in allele DRB1*04:02, allele DRB1*11:11,
FT allele DRB1*13:01 and allele DRB1*13:02; dbSNP:rs9269942)"
FT /evidence="ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17174751,
FT ECO:0000269|Ref.24"
FT /id="VAR_082759"
FT VARIANT 100
FT /note="A -> K (in allele DRB1*03:01, allele DRB1*03:02,
FT allele DRB1*04:01 and allele DRB1*13:03; requires 2
FT nucleotide substitutions; dbSNP:rs796196270)"
FT /evidence="ECO:0000269|PubMed:14574404,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:26396036,
FT ECO:0000269|PubMed:6589154, ECO:0000269|Ref.26"
FT /id="VAR_082760"
FT VARIANT 100
FT /note="A -> R (in allele DRB1*01:01, allele DRB1*01:02,
FT allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06,
FT allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10,
FT allele DRB1*04:11, allele DRB1*07:01, allele DRB1*08:01,
FT allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04,
FT allele DRB1*09:01, allele DRB1*10:01, allele DRB1*11:01,
FT allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:19,
FT allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:05,
FT allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01,
FT allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06,
FT allele DRB1*14:07, allele DRB1*16:01 and allele DRB1*16:02;
FT requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15896200,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:17345114, ECO:0000269|PubMed:21388356,
FT ECO:0000269|PubMed:2497068, ECO:0000269|PubMed:26396036,
FT ECO:0000269|PubMed:2885840, ECO:0000269|PubMed:2998758,
FT ECO:0000269|PubMed:30337930, ECO:0000269|PubMed:3110774,
FT ECO:0000269|PubMed:3129499, ECO:0000269|PubMed:3456344,
FT ECO:0000269|PubMed:3571980, ECO:0000269|PubMed:3875800,
FT ECO:0000269|PubMed:6589154, ECO:0000269|PubMed:9777332,
FT ECO:0000269|Ref.23, ECO:0000269|Ref.25"
FT /id="VAR_082761"
FT VARIANT 102
FT /note="A -> G (in allele DRB1*03:01, allele DRB1*03:02 and
FT allele DRB1*07:01; dbSNP:rs17878857)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3110774, ECO:0000269|PubMed:6589154,
FT ECO:0000269|Ref.26"
FT /id="VAR_082762"
FT VARIANT 103
FT /note="A -> E (in allele DRB1*04:06, allele DRB1*04:07,
FT allele DRB1*04:11, allele DRB1*09:01, allele DRB1*14:01,
FT allele DRB1*14:05 and allele DRB1*14:07; dbSNP:rs17886882)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:17174751, ECO:0000269|PubMed:21388356,
FT ECO:0000269|PubMed:9777332, ECO:0000269|Ref.23"
FT /id="VAR_082763"
FT VARIANT 103
FT /note="A -> L (in allele DRB1*08:01, allele DRB1*08:02,
FT allele DRB1*08:03, allele DRB1*08:04 and allele DRB1*14:03;
FT requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:17174751, ECO:0000269|PubMed:21388356,
FT ECO:0000269|PubMed:2497068, ECO:0000269|PubMed:30337930,
FT ECO:0000269|Ref.25"
FT /id="VAR_082764"
FT VARIANT 103
FT /note="A -> Q (in allele DRB1*07:01; requires 2 nucleotide
FT substitutions)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3110774"
FT /id="VAR_082765"
FT VARIANT 103
FT /note="A -> R (in allele DRB1*03:01 and allele DRB1*03:02;
FT requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:6589154, ECO:0000269|Ref.26"
FT /id="VAR_082766"
FT VARIANT 106
FT /note="T -> N (in allele DRB1*03:01, allele DRB1*03:02;
FT dbSNP:rs9269941)"
FT /evidence="ECO:0000269|PubMed:6589154, ECO:0000269|Ref.26"
FT /id="VAR_082767"
FT VARIANT 107
FT /note="Y -> V (in allele DRB1*07:01 and allele DRB1*09:01;
FT requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3110774, ECO:0000269|PubMed:9777332"
FT /id="VAR_082768"
FT VARIANT 114
FT /note="V -> A (in allele DRB1*01:02, allele DRB1*11:06,
FT allele DRB1*12:01, allele DRB1*12:02; dbSNP:rs17424145)"
FT /evidence="ECO:0000269|PubMed:12028552,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:21388356,
FT ECO:0000269|PubMed:26396036"
FT /id="VAR_082769"
FT VARIANT 115
FT /note="V -> G (in allele DRB1*01:01, allele DRB1*03:02,
FT allele DRB1*04:01, allele DRB1*04:05, allele DRB1*04:07,
FT allele DRB1*04:08, allele DRB1*07:01, allele DRB1*08:01,
FT allele DRB1*08:02, allele DRB1*08:03, allele DRB1*09:01,
FT allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:11,
FT allele DRB1*11:19, allele DRB1*13:02, allele DRB1*13:03,
FT allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12,
FT allele DRB1*14:03, allele DRB1*14:07, allele DRB1*15:02,
FT allele DRB1*16:01 and allele DRB1*16:02; dbSNP:rs17885482)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15896200,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:17345114, ECO:0000269|PubMed:21388356,
FT ECO:0000269|PubMed:2497068, ECO:0000269|PubMed:26396036,
FT ECO:0000269|PubMed:2885840, ECO:0000269|PubMed:2998758,
FT ECO:0000269|PubMed:30337930, ECO:0000269|PubMed:3110774,
FT ECO:0000269|PubMed:3129499, ECO:0000269|PubMed:3456344,
FT ECO:0000269|PubMed:3571980, ECO:0000269|PubMed:6589154,
FT ECO:0000269|PubMed:9777332, ECO:0000269|Ref.24,
FT ECO:0000269|Ref.25, ECO:0000269|Ref.26"
FT /id="VAR_082770"
FT VARIANT 125
FT /note="Q -> E (in allele DRB1*01:01 and allele DRB1*01:02;
FT dbSNP:rs17882084)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17345114,
FT ECO:0000269|PubMed:2998758"
FT /id="VAR_082771"
FT VARIANT 125
FT /note="Q -> H (in allele DRB1*03:01, allele DRB1*03:02,
FT allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02,
FT allele DRB1*08:03, allele DRB1*08:04, allele DRB1*09:01,
FT allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06,
FT allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01,
FT allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02,
FT allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07,
FT allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03,
FT allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07;
FT dbSNP:rs1071752)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15896200,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:2497068,
FT ECO:0000269|PubMed:26396036, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:3110774, ECO:0000269|PubMed:3456344,
FT ECO:0000269|PubMed:6589154, ECO:0000269|PubMed:9777332,
FT ECO:0000269|Ref.24, ECO:0000269|Ref.25, ECO:0000269|Ref.26"
FT /id="VAR_082772"
FT VARIANT 125
FT /note="Q -> Y (in allele DRB1*04:01, allele DRB1*04:02,
FT allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06,
FT allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10 and
FT allele DRB1*04:11; requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:3875800, ECO:0000269|Ref.23"
FT /id="VAR_082773"
FT VARIANT 127
FT /note="K -> E (in allele DRB1*04:01, allele DRB1*04:02,
FT allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06,
FT allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10,
FT allele DRB1*04:11, allele DRB1*07:01 and allele DRB1*09:01;
FT dbSNP:rs17405219)"
FT /evidence="ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17174751, ECO:0000269|PubMed:21388356,
FT ECO:0000269|PubMed:30337930, ECO:0000269|PubMed:3110774,
FT ECO:0000269|PubMed:3875800, ECO:0000269|PubMed:9777332,
FT ECO:0000269|Ref.23"
FT /id="VAR_082774"
FT VARIANT 133
FT /note="S -> A (in allele DRB1*04:01, allele DRB1*04:02,
FT allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06,
FT allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10,
FT allele DRB1*04:11, allele DRB1*07:01 and allele DRB1*09:01;
FT dbSNP:rs2308760)"
FT /evidence="ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17174751, ECO:0000269|PubMed:21388356,
FT ECO:0000269|PubMed:30337930, ECO:0000269|PubMed:3110774,
FT ECO:0000269|PubMed:3875800, ECO:0000269|PubMed:9777332,
FT ECO:0000269|Ref.23"
FT /id="VAR_082775"
FT VARIANT 141
FT /note="H -> Y (in allele DRB1*14:01; dbSNP:rs751099504)"
FT /evidence="ECO:0000269|PubMed:11972886"
FT /id="VAR_082776"
FT VARIANT 149
FT /note="S -> N (in allele DRB1*04:01, allele DRB1*04:02,
FT allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06,
FT allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10,
FT allele DRB1*04:11 and allele DRB1*10:01; dbSNP:rs1059351)"
FT /evidence="ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:3875800, ECO:0000269|PubMed:6589154,
FT ECO:0000269|Ref.23"
FT /id="VAR_082777"
FT VARIANT 162
FT /note="L -> R (in allele DRB1*01:01, allele DRB1*01:02,
FT allele DRB1*03:01, allele DRB1*03:02,allele DRB1*04:01,
FT allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05,
FT allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08,
FT allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01,
FT allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03,
FT allele DRB1*08:04, allele DRB1*09:01, allele DRB1*10:01,
FT allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06,
FT allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01,
FT allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02,
FT allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07,
FT allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03,
FT allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07;
FT dbSNP:rs707954)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:14574404,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15896200, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:17174751, ECO:0000269|PubMed:17345114,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:2497068,
FT ECO:0000269|PubMed:26396036, ECO:0000269|PubMed:2998758,
FT ECO:0000269|PubMed:30337930, ECO:0000269|PubMed:3110774,
FT ECO:0000269|PubMed:3456344, ECO:0000269|PubMed:3875800,
FT ECO:0000269|PubMed:6589154, ECO:0000269|PubMed:9777332,
FT ECO:0000269|Ref.23, ECO:0000269|Ref.24, ECO:0000269|Ref.25,
FT ECO:0000269|Ref.26"
FT /id="VAR_082778"
FT VARIANT 169
FT /note="A -> T (in allele DRB1*03:01, allele DRB1*03:02,
FT allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04,
FT allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07,
FT allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11,
FT allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03,
FT allele DRB1*08:04, allele DRB1*10:01, allele DRB1*11:01,
FT allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11,
FT allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02,
FT allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03,
FT allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12,
FT allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05,
FT allele DRB1*14:06 and allele DRB1*14:07; dbSNP:rs78916069)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:14574404,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15896200, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:17174751, ECO:0000269|PubMed:21388356,
FT ECO:0000269|PubMed:2497068, ECO:0000269|PubMed:26396036,
FT ECO:0000269|PubMed:30337930, ECO:0000269|PubMed:3456344,
FT ECO:0000269|PubMed:3875800, ECO:0000269|PubMed:6589154,
FT ECO:0000269|Ref.23, ECO:0000269|Ref.24, ECO:0000269|Ref.25,
FT ECO:0000269|Ref.26"
FT /id="VAR_082779"
FT VARIANT 171
FT /note="M -> V (in allele DRB1*01:01, allele DRB1*01:02,
FT allele DRB1*03:01, allele DRB1*03:02, allele DRB1*04:01,
FT allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05,
FT allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08,
FT allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01,
FT allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03,
FT allele DRB1*08:04, allele DRB1*09:01, allele DRB1*10:01,
FT allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06,
FT allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01,
FT allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02,
FT allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07,
FT allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03,
FT allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07;
FT dbSNP:rs701829)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:14574404,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15896200, ECO:0000269|PubMed:16140993,
FT ECO:0000269|PubMed:17174751, ECO:0000269|PubMed:17345114,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:2497068,
FT ECO:0000269|PubMed:26396036, ECO:0000269|PubMed:2998758,
FT ECO:0000269|PubMed:30337930, ECO:0000269|PubMed:3110774,
FT ECO:0000269|PubMed:3456344, ECO:0000269|PubMed:3875800,
FT ECO:0000269|PubMed:6589154, ECO:0000269|PubMed:9777332,
FT ECO:0000269|Ref.23, ECO:0000269|Ref.24, ECO:0000269|Ref.25,
FT ECO:0000269|Ref.26"
FT /id="VAR_082780"
FT VARIANT 178
FT /note="Q -> H (in allele DRB1*03:01, allele DRB1*03:02,
FT allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03,
FT allele DRB1*08:04, allele DRB1*11:01, allele DRB1*11:04,
FT allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19,
FT allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01,
FT allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05,
FT allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01,
FT allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and
FT allele DRB1*14:07; dbSNP:rs77637983)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15896200,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:2497068,
FT ECO:0000269|PubMed:26396036, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:3456344, ECO:0000269|PubMed:6589154,
FT ECO:0000269|Ref.24, ECO:0000269|Ref.25, ECO:0000269|Ref.26"
FT /id="VAR_082781"
FT VARIANT 195
FT /note="R -> Q (in allele DRB1*10:01; dbSNP:rs3205588)"
FT /evidence="ECO:0000269|PubMed:6589154"
FT /id="VAR_082782"
FT VARIANT 209
FT /note="V -> L (in allele DRB1*04:01, allele DRB1*04:02,
FT allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06,
FT allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10 and
FT allele DRB1*04:11; dbSNP:rs111739605)"
FT /evidence="ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:30337930,
FT ECO:0000269|PubMed:3875800, ECO:0000269|Ref.23"
FT /id="VAR_082783"
FT VARIANT 210
FT /note="T -> M (in allele DRB1*07:01, allele DRB1*09:01 and
FT allele DRB1*10:01)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3110774, ECO:0000269|PubMed:6589154,
FT ECO:0000269|PubMed:9777332"
FT /id="VAR_082784"
FT VARIANT 218
FT /note="R -> S (in allele DRB1*08:01, allele DRB1*08:02,
FT allele DRB1*08:03 and allele DRB1*08:04)"
FT /evidence="ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:2497068,
FT ECO:0000269|Ref.25"
FT /id="VAR_082785"
FT VARIANT 260
FT /note="Q -> P (in allele DRB1*10:01; dbSNP:rs17887154)"
FT /evidence="ECO:0000269|PubMed:6589154"
FT /id="VAR_082786"
FT VARIANT 262
FT /note="T -> R (in allele DRB1*03:01, allele DRB1*03:02,
FT allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06,
FT allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01,
FT allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02,
FT allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07,
FT allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03,
FT allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07;
FT dbSNP:rs9269744)"
FT /evidence="ECO:0000269|PubMed:11972886,
FT ECO:0000269|PubMed:12028552, ECO:0000269|PubMed:12358860,
FT ECO:0000269|PubMed:12652907, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15896200,
FT ECO:0000269|PubMed:16140993, ECO:0000269|PubMed:17174751,
FT ECO:0000269|PubMed:21388356, ECO:0000269|PubMed:26396036,
FT ECO:0000269|PubMed:30337930, ECO:0000269|PubMed:3456344,
FT ECO:0000269|PubMed:6589154, ECO:0000269|Ref.24,
FT ECO:0000269|Ref.25, ECO:0000269|Ref.26"
FT /id="VAR_082787"
FT MUTAGEN 166
FT /note="E->A: Decreases the interaction with CD4; when
FT assocated with A-172."
FT /evidence="ECO:0000269|PubMed:27114505"
FT MUTAGEN 172
FT /note="V->A: Decreases the interaction with CD4; when
FT assocated with A-166."
FT /evidence="ECO:0000269|PubMed:27114505"
FT MUTAGEN 177
FT /note="I->R: Decreases the interaction with CD4."
FT /evidence="ECO:0000269|PubMed:27114505"
FT MUTAGEN 181
FT /note="D->N: Reduces the interaction with HLA-DM complex
FT that results in impaired dissociation of CLIP from MHCII."
FT /evidence="ECO:0000269|PubMed:11070170,
FT ECO:0000269|PubMed:23260142"
FT MUTAGEN 187
FT /note="L->R: Decreases the interaction with CD4."
FT /evidence="ECO:0000269|PubMed:27114505"
FT MUTAGEN 213
FT /note="L->H: Reduces the interaction with HLA-DM complex
FT that results in impaired dissociation of CLIP from MHCII."
FT /evidence="ECO:0000269|PubMed:11070170,
FT ECO:0000269|PubMed:23260142"
FT MUTAGEN 216
FT /note="E->K: Reduces the interaction with HLA-DM complex
FT that results in impaired dissociation of CLIP from MHCII."
FT /evidence="ECO:0000269|PubMed:11070170,
FT ECO:0000269|PubMed:23260142"
FT MUTAGEN 254
FT /note="K->A: Impairs MARCHF1-dependent down-regulation
FT through ubiquitination."
FT /evidence="ECO:0000269|PubMed:18305173"
FT STRAND 36..47
FT /evidence="ECO:0007829|PDB:5NI9"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:5NI9"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:5NI9"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:5NI9"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:5NI9"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:5NI9"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5NI9"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:5NI9"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:5NI9"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:5NI9"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:5NI9"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:5NI9"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:5NI9"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:3PDO"
FT STRAND 142..154
FT /evidence="ECO:0007829|PDB:5NI9"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:5NI9"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:5NI9"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:5NI9"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:5NI9"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:5NI9"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:6V13"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:5NI9"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:6CPO"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:5NI9"
SQ SEQUENCE 266 AA; 29966 MW; 3B5912820A4654BE CRC64;
MVCLKLPGGS CMTALTVTLM VLSSPLALSG DTRPRFLWQP KRECHFFNGT ERVRFLDRYF
YNQEESVRFD SDVGEFRAVT ELGRPDAEYW NSQKDILEQA RAAVDTYCRH NYGVVESFTV
QRRVQPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FLNGQEEKAG MVSTGLIQNG
DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL
FLGAGLFIYF RNQKGHSGLQ PTGFLS
