ID A0A0U5Q247_HUMAN Unreviewed; 261 AA. AC A0A0U5Q247; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 13-FEB-2019, entry version 32. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000388763}; DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:CUX91142.1}; GN Name=HLA-DQB1 {ECO:0000313|EMBL:CUX91142.1, GN ECO:0000313|Ensembl:ENSP00000388763}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:CUX91142.1}; RN [1] {ECO:0000313|Ensembl:ENSP00000388763, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA 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., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000213|PDB:5KS9, ECO:0000213|PDB:5KSA, ECO:0000213|PDB:5KSB} RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 33-224, AND DISULFIDE BONDS. RX PubMed=27568928; DOI=10.1016/j.str.2016.07.010; RA Petersen J., Kooy-Winkelaar Y., Loh K.L., Tran M., van Bergen J., RA Koning F., Rossjohn J., Reid H.H.; RT "Diverse T cell receptor gene usage in HLA-DQ8-associated celiac RT disease converges into a consensus binding solution."; RL Structure 24:1643-1657(2016). RN [4] {ECO:0000313|Ensembl:ENSP00000388763} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. RN [5] {ECO:0000313|EMBL:CUX91142.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28547825; DOI=.1111/tan.13057; RA Albrecht V., Zweiniger C., Surendranath V., Lang K., Schofl G., RA Dahl A., Winkler S., Lange V., Bohme I., Schmidt A.H.; RT "Dual redundant sequencing strategy: Full-length gene characterisation RT of 1056 novel and confirmatory HLA alleles."; RL HLA 90:79-87(2017). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX248406; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; LN999749; CUX91142.1; -; Genomic_DNA. DR UniGene; Hs.409934; -. DR UniGene; Hs.534322; -. DR PDB; 5KS9; X-ray; 2.55 A; B/D=33-224. DR PDB; 5KSA; X-ray; 2.00 A; B=12-12, B=33-224. DR PDB; 5KSB; X-ray; 2.90 A; B/D=12-12, B/D=33-224. DR PDBsum; 5KS9; -. DR PDBsum; 5KSA; -. DR PDBsum; 5KSB; -. DR SMR; A0A0U5Q247; -. DR EPD; A0A0U5Q247; -. DR jPOST; A0A0U5Q247; -. DR Ensembl; ENST00000414518; ENSP00000388763; ENSG00000231939. DR HGNC; HGNC:4944; HLA-DQB1. DR ChiTaRS; HLA-DQB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. 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 ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:5KS9, ECO:0000213|PDB:5KSA, KW ECO:0000213|PDB:5KSB}; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A0U5Q247, KW ECO:0000213|PeptideAtlas:A0A0U5Q247}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 261 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015049031. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 233 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT CARBOHYD 51 51 N-linked (GlcNAc...) asparagine. FT {ECO:0000213|PDB:5KS9, FT ECO:0000213|PDB:5KSB}. FT DISULFID 47 111 {ECO:0000213|PDB:5KS9, FT ECO:0000213|PDB:5KSA, FT ECO:0000213|PDB:5KSB}. FT DISULFID 149 205 {ECO:0000213|PDB:5KS9, FT ECO:0000213|PDB:5KSA, FT ECO:0000213|PDB:5KSB}. SQ SEQUENCE 261 AA; 29814 MW; ED31E2DF40FF1752 CRC64; MSWKKALRIP GGLRVATVTL MLAMLSTPVA EGRDSPEDFV YQFKGMCYFT NGTERVRGVT RYIYNREEYA RFDSDVGVYR AVTPLGPPAA EYWNSQKEVL ERTRAELDTV CRHNYQLELR TTLQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPAQIK VRWFRNDQEE TTGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQNPIIVEW RAQSESAQSK MLSGIGGFVL GLIFLGLGLI IHHRSQKGLL H //