ID HLAA_HUMAN Reviewed; 365 AA. AC P04439; B1PKZ3; O02939; O02954; O02955; O02963; O19509; O19546; O19598; AC O19605; O19606; O19619; O19647; O19673; O19687; O19695; O19756; O19794; AC O19795; O43906; O43907; O46874; O62921; O62924; O77937; O77938; O77964; AC O78073; O78171; O98009; O98010; O98011; O98137; P01891; P01892; P05534; AC P06338; P10313; P10314; P10315; P10316; P13746; P16188; P16189; P16190; AC P18462; P30443; P30444; P30445; P30446; P30447; P30448; P30449; P30450; AC P30451; P30452; P30453; P30454; P30455; P30456; P30457; P30458; P30459; AC P30512; P30514; P79505; P79562; P79563; Q09160; Q29680; Q29747; Q29835; AC Q29837; Q29838; Q29899; Q29908; Q29909; Q29910; Q30208; Q31623; Q5S3G1; AC Q65A82; Q8MHM1; Q8MHN9; Q95352; Q95355; Q95362; Q95377; Q95380; Q95IZ5; AC Q9BCN0; Q9BD15; Q9BD19; Q9GJE6; Q9GJE7; Q9GJE8; Q9MW42; Q9MY89; Q9MYA3; AC Q9MYA5; Q9MYC4; Q9MYE6; Q9MYE9; Q9MYG4; Q9MYG5; Q9MYI5; Q9TP25; Q9TPQ3; AC Q9TPR8; Q9TPX8; Q9TPX9; Q9TPY0; Q9TQ24; Q9TQE8; Q9TQE9; Q9TQF1; Q9TQF5; AC Q9TQF8; Q9TQF9; Q9TQG0; Q9TQG5; Q9TQG7; Q9TQH5; Q9TQI3; Q9TQK5; Q9TQM6; AC Q9TQN5; Q9TQP5; Q9TQP6; Q9TQP7; Q9UIN1; Q9UIN2; Q9UIP7; Q9UQU3; Q9UQU6; AC Q9UQU7; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2003, sequence version 2. DT 27-MAR-2024, entry version 216. DE RecName: Full=HLA class I histocompatibility antigen, A alpha chain; DE AltName: Full=Human leukocyte antigen A; DE Short=HLA-A; DE Flags: Precursor; GN Name=HLA-A {ECO:0000312|HGNC:HGNC:4931}; Synonyms=HLAA; 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 OF 25-298 (ALLELE A*32:01). RX PubMed=2431040; RA Wan A.M., Ennis P., Parham P., Holmes N.; RT "The primary structure of HLA-A32 suggests a region involved in formation RT of the Bw4/Bw6 epitopes."; RL J. Immunol. 137:3671-3674(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:05). RX PubMed=3496393; RA Holmes N., Ennis P., Wan A.M., Denney D.W., Parham P.; RT "Multiple genetic mechanisms have contributed to the generation of the HLA- RT A2/A28 family of class I MHC molecules."; RL J. Immunol. 139:936-941(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*11:01). RX PubMed=2460344; DOI=10.1002/j.1460-2075.1988.tb03131.x; RA Mayer W.E., Jonker M., Klein D., Ivanyi P., van Seventer G., Klein J.; RT "Nucleotide sequences of chimpanzee MHC class I alleles: evidence for RT trans-species mode of evolution."; RL EMBO J. 7:2765-2774(1988). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*29:01). RX PubMed=2461903; DOI=10.1007/bf02341610; RA Trapani J.A., Mizuno S., Kang S.H., Yang S.Y., Dupont B.; RT "Molecular mapping of a new public HLA class I epitope shared by all HLA-B RT and HLA-C antigens and defined by a monoclonal antibody."; RL Immunogenetics 29:25-32(1989). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ALLELES A*30:01; A*31:01 AND RP A*33:01). RX PubMed=2478623; RA Kato K., Trapani J.A., Allopenna J., Dupont B., Yang S.Y.; RT "Molecular analysis of the serologically defined HLA-Aw19 antigens. A RT genetically distinct family of HLA-A antigens comprising A29, A31, A32, and RT Aw33, but probably not A30."; RL J. Immunol. 143:3371-3378(1989). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ALLELE A*01:01). RX PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A*02:01 AND A*25:01). RX PubMed=2320591; DOI=10.1073/pnas.87.7.2833; RA Ennis P.D., Zemmour J., Salter R.D., Parham P.; RT "Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction: RT frequency and nature of errors produced in amplification."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*29:02). RX PubMed=1782566; RA Tabary T., Prochnicka-Chalufour A., Cornillet P., Lehoang P., Betuel H., RA Cohen H.M.; RT "HLA-A29 sub-types and 'Birdshot' choroido-retinopathy susceptibility: a RT possible 'resistance motif' in the HLA-A29.1 molecule."; RL C. R. Acad. Sci. III, Sci. Vie 313:599-605(1991). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A*23:01 AND A*24:02). RX PubMed=1729171; DOI=10.1007/bf00216625; RA Little A.-M., Madrigal J.A., Parham P.; RT "Molecular definition of an elusive third HLA-A9 molecule: HLA-A9.3."; RL Immunogenetics 35:41-45(1992). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A*34:01; A*36:01; A*43:01; A*66:01 AND RP A*74:01). RX PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., Little A.-M., RA Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., Martell R.W., RA du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by interallelic RT conversion."; RL J. Immunol. 149:3411-3415(1992). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*31:01). RX PubMed=1317015; DOI=10.1038/357326a0; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., Williams R.C., RA Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*26:01). RX PubMed=8475492; DOI=10.1111/j.1399-0039.1993.tb01982.x; RA Madrigal J.A., Hildebrand W.H., Belich M.P., Benjamin R.J., Little A.-M., RA Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., du Toit E.D., RA Parham P.; RT "Structural diversity in the HLA-A10 family of alleles: correlations with RT serology."; RL Tissue Antigens 41:72-80(1993). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*80:01). RX PubMed=8284791; DOI=10.1111/j.1399-0039.1993.tb02186.x; RA Domena J.D., Hildebrand W.H., Bias W.B., Parham P.; RT "A sixth family of HLA-A alleles defined by HLA-A*8001."; RL Tissue Antigens 42:156-159(1993). RN [14] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A*26:01). RC TISSUE=Blood; RX PubMed=8026990; DOI=10.1016/0198-8859(94)90263-1; RA Ishikawa Y., Tokunaga K., Lin L., Imanishi T., Saitou S., Kashiwase K., RA Akaza T., Tadokoro K., Juji T.; RT "Sequences of four splits of HLA-A10 group. Implications for serologic RT cross-reactivities and their evolution."; RL Hum. Immunol. 39:220-224(1994). RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*80:01). RX PubMed=8188325; DOI=10.1007/bf00176169; RA Balas A., Garcia-Sanchez F., Gomez-Reino F., Vicario J.L.; RT "Characterization of a new and highly distinguishable HLA-A allele in a RT Spanish family."; RL Immunogenetics 39:452-452(1994). RN [16] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*11:01). RX PubMed=8016845; DOI=10.1111/j.1399-0039.1994.tb02304.x; RA Lin L., Tokunaga K., Ishikawa Y., Bannai M., Kashiwase K., Kuwata S., RA Akaza T., Tadokoro K., Shibata Y., Juji T.; RT "Sequence analysis of serological HLA-A11 split antigens, A11.1 and RT A11.2."; RL Tissue Antigens 43:78-82(1994). RN [17] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*30:01). RX PubMed=7871528; DOI=10.1111/j.1399-0039.1994.tb02393.x; RA Olerup O., Daniels T.J., Baxter-Lowe L.; RT "Correct sequence of the A*3001 allele obtained by PCR-SSP typing and RT automated nucleotide sequencing."; RL Tissue Antigens 44:265-267(1994). RN [18] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*11:01) (ISOFORM 2). RX PubMed=17092262; DOI=10.1111/j.1399-0039.2006.00687.x; RA Sun Y., Liu S., Luo Y., Liang F., Xi Y.; RT "Identification and frequency of a novel HLA-A allele, A*110104."; RL Tissue Antigens 68:453-454(2006). RN [19] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*03:01). RX PubMed=6609814; DOI=10.1002/j.1460-2075.1984.tb01901.x; RA Strachan T., Sodoyer R., Damotte M., Jordan B.R.; RT "Complete nucleotide sequence of a functional class I HLA gene, HLA-A3: RT implications for the evolution of HLA genes."; RL EMBO J. 3:887-894(1984). RN [20] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-297 (ALLELES A*68:01 AND A*69:01). RX PubMed=3877632; DOI=10.1002/j.1460-2075.1985.tb04013.x; RA Holmes N., Parham P.; RT "Exon shuffling in vivo can generate novel HLA class I molecules."; RL EMBO J. 4:2849-2854(1985). RN [21] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*02:01). RX PubMed=2982951; RA Koller B.H., Orr H.T.; RT "Cloning and complete sequence of an HLA-A2 gene: analysis of two HLA-A RT alleles at the nucleotide level."; RL J. Immunol. 134:2727-2733(1985). RN [22] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-365 (ALLELE A*11:01). RX PubMed=2437024; DOI=10.1007/bf00404694; RA Cowan E.P., Jelachich M.L., Biddison W.E., Coligan J.E.; RT "DNA sequence of HLA-A11: remarkable homology with HLA-A3 allows RT identification of residues involved in epitopes recognized by antibodies RT and T cells."; RL Immunogenetics 25:241-250(1987). RN [23] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*01:01). RX PubMed=2251137; DOI=10.1093/nar/18.22.6701; RA Girdlestone J.; RT "Nucleotide sequence of an HLA-A1 gene."; RL Nucleic Acids Res. 18:6701-6701(1990). RN [24] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*02:01). RC TISSUE=Blood; RX PubMed=7836067; DOI=10.1016/0198-8859(94)90087-6; RA Balas A., Garcia-Sanchez F., Gomez-Reino F., Vicario J.L.; RT "HLA class I allele (HLA-A2) expression defect associated with a mutation RT in its enhancer B inverted CAT box in two families."; RL Hum. Immunol. 41:69-73(1994). RN [25] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*31:01). RX PubMed=8795145; DOI=10.1111/j.1399-0039.1996.tb02580.x; RA Arnett K.L., Adams E.J., Parham P.; RT "On the sequence of A*3101."; RL Tissue Antigens 47:428-430(1996). RN [26] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*24:02). RX PubMed=9349616; DOI=10.1111/j.1399-0039.1997.tb02884.x; RA Laforet M., Froelich N., Parissiadis A., Bausinger H., Pfeiffer B., RA Tongio M.M.; RT "An intronic mutation responsible for a low level of expression of an HLA- RT A*24 allele."; RL Tissue Antigens 50:340-346(1997). RN [27] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*01:01). RX PubMed=9349617; DOI=10.1111/j.1399-0039.1997.tb02885.x; RA Laforet M., Froelich N., Parissiadis A., Pfeiffer B., Schell A., Faller B., RA Woehl-Jaegle M.L., Cazenave J.-P., Tongio M.M.; RT "A nucleotide insertion in exon 4 is responsible for the absence of RT expression of an HLA-A*01 allele."; RL Tissue Antigens 50:347-350(1997). RN [28] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*69:01). RX PubMed=19735485; DOI=10.1111/j.1744-313x.2009.00874.x; RA Zhu F., He Y., Zhang W., He J., He J., Xu X., Yan L.; RT "Analysis of the complete genomic sequence of HLA-A alleles in the Chinese RT Han population."; RL Int. J. Immunogenet. 36:351-360(2009). RN [29] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*32:01). RA Domena J.D.; RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases. RN [30] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*74:01). RA Hurley C.K.; RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases. RN [31] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*03:01). RA Ellexson M.E., Hildebrand W.H.; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. RN [32] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*03:01). RA Mayor N.P.; RT "Full length sequence of an HLA-A*0301 intron 2 variant."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [33] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [34] 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., 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 [35] RP PROTEIN SEQUENCE OF 25-295 (ALLELE A*02:01). RX PubMed=92029; DOI=10.1073/pnas.76.9.4395; RA Orr H.T., Lopez de Castro J.A., Parham P., Ploegh H.L., Strominger J.L.; RT "Comparison of amino acid sequences of two human histocompatibility RT antigens, HLA-A2 and HLA-B7: location of putative alloantigenic sites."; RL Proc. Natl. Acad. Sci. U.S.A. 76:4395-4399(1979). RN [36] RP PROTEIN SEQUENCE OF 25-294 (ALLELE A*68:01). RX PubMed=6179086; DOI=10.1073/pnas.79.12.3813; RA Lopez de Castro J.A., Strominger J.L., Strong D.M., Orr H.T.; RT "Structure of crossreactive human histocompatibility antigens HLA-A28 and RT HLA-A2: possible implications for the generation of HLA polymorphism."; RL Proc. Natl. Acad. Sci. U.S.A. 79:3813-3817(1982). RN [37] RP FUNCTION (ALLELE A*03:01), AND CHARACTERIZATION OF VARIANT VAL-176. RX PubMed=2456340; RA Jelachich M.L., Cowan E.P., Turner R.V., Coligan J.E., Biddison W.E.; RT "Analysis of the molecular basis of HLA-A3 recognition by cytotoxic T cells RT using defined mutants of the HLA-A3 molecule."; RL J. Immunol. 141:1108-1113(1988). RN [38] RP FUNCTION (ALLELES A*02:01 AND A*68:01), INTERACTION WITH CD8A, DOMAIN, AND RP CHARACTERIZATION OF VARIANT VAL-269. RX PubMed=2784196; DOI=10.1038/338345a0; RA Salter R.D., Norment A.M., Chen B.P., Clayberger C., Krensky A.M., RA Littman D.R., Parham P.; RT "Polymorphism in the alpha 3 domain of HLA-A molecules affects binding to RT CD8."; RL Nature 338:345-347(1989). RN [39] RP FUNCTION (ALLELE A*01:01). RX PubMed=1402688; DOI=10.1084/jem.176.5.1453; RA Traversari C., van der Bruggen P., Luescher I.F., Lurquin C., Chomez P., RA Van Pel A., De Plaen E., Amar-Costesec A., Boon T.; RT "A nonapeptide encoded by human gene MAGE-1 is recognized on HLA-A1 by RT cytolytic T lymphocytes directed against tumor antigen MZ2-E."; RL J. Exp. Med. 176:1453-1457(1992). RN [40] RP FUNCTION (ALLELES A*01:01 AND A*03:01), AND INTERACTION WITH B2M AND RP PEPTIDE. RX PubMed=7504010; RA DiBrino M., Tsuchida T., Turner R.V., Parker K.C., Coligan J.E., RA Biddison W.E.; RT "HLA-A1 and HLA-A3 T cell epitopes derived from influenza virus proteins RT predicted from peptide binding motifs."; RL J. Immunol. 151:5930-5935(1993). RN [41] RP FUNCTION (ALLELE A*03:01), AND INTERACTION WITH B2M AND PEPTIDE. RX PubMed=7679507; DOI=10.1073/pnas.90.4.1508; RA DiBrino M., Parker K.C., Shiloach J., Knierman M., Lukszo J., Turner R.V., RA Biddison W.E., Coligan J.E.; RT "Endogenous peptides bound to HLA-A3 possess a specific combination of RT anchor residues that permit identification of potential antigenic RT peptides."; RL Proc. Natl. Acad. Sci. U.S.A. 90:1508-1512(1993). RN [42] RP FUNCTION (ALLELE A*01:01), AND INTERACTION WITH B2M AND PEPTIDE. RX PubMed=7506728; RA DiBrino M., Parker K.C., Shiloach J., Turner R.V., Tsuchida T., RA Garfield M., Biddison W.E., Coligan J.E.; RT "Endogenous peptides with distinct amino acid anchor residue motifs bind to RT HLA-A1 and HLA-B8."; RL J. Immunol. 152:620-631(1994). RN [43] RP FUNCTION (ALLELE A*02:01), MUTAGENESIS OF SER-156 AND THR-158, DOMAIN, RP INTERACTION WITH B2M, INTERACTION WITH TAP1-TAP2 COMPLEX, AND SUBCELLULAR RP LOCATION. RX PubMed=8805302; DOI=10.1016/s0960-9822(02)00611-5; RA Lewis J.W., Neisig A., Neefjes J., Elliott T.; RT "Point mutations in the alpha 2 domain of HLA-A2.1 define a functionally RT relevant interaction with TAP."; RL Curr. Biol. 6:873-883(1996). RN [44] RP FUNCTION (ALLELE A*02:01), INTERACTION WITH TAP1-TAP2 COMPLEX, AND RP MUTAGENESIS OF THR-158. RX PubMed=8630735; DOI=10.1016/s1074-7613(00)80416-1; RA Peace-Brewer A.L., Tussey L.G., Matsui M., Li G., Quinn D.G., RA Frelinger J.A.; RT "A point mutation in HLA-A*0201 results in failure to bind the TAP complex RT and to present virus-derived peptides to CTL."; RL Immunity 4:505-514(1996). RN [45] RP FUNCTION (ALLELE A*29:02). RX PubMed=8622959; DOI=10.1073/pnas.93.8.3466; RA Boisgerault F., Khalil I., Tieng V., Connan F., Tabary T., Cohen J.H., RA Choppin J., Charron D., Toubert A.; RT "Definition of the HLA-A29 peptide ligand motif allows prediction of RT potential T-cell epitopes from the retinal soluble antigen, a candidate RT autoantigen in birdshot retinopathy."; RL Proc. Natl. Acad. Sci. U.S.A. 93:3466-3470(1996). RN [46] RP FUNCTION (ALLELE A*24:02). RX PubMed=9047241; DOI=10.1016/s1074-7613(00)80426-4; RA Ikeda H., Lethe B.G., Lehmann F., van Baren N., Baurain J.-F., de Smet C., RA Chambost H., Vitale M., Moretta A., Boon T., Coulie P.G.; RT "Characterization of an antigen that is recognized on a melanoma showing RT partial HLA loss by CTL expressing an NK inhibitory receptor."; RL Immunity 6:199-208(1997). RN [47] RP FUNCTION (ALLELE A*03:01). RX PubMed=9862734; RA Kawakami Y., Robbins P.F., Wang X., Tupesis J.P., Parkhurst M.R., Kang X., RA Sakaguchi K., Appella E., Rosenberg S.A.; RT "Identification of new melanoma epitopes on melanosomal proteins recognized RT by tumor infiltrating T lymphocytes restricted by HLA-A1, -A2, and -A3 RT alleles."; RL J. Immunol. 161:6985-6992(1998). RN [48] RP FUNCTION (ALLELE A*11:01). RX PubMed=10449296; DOI=10.1097/00002030-199907300-00021; RA Fukada K., Chujoh Y., Tomiyama H., Miwa K., Kaneko Y., Oka S., RA Takiguchi M.; RT "HLA-A*1101-restricted cytotoxic T lymphocyte recognition of HIV-1 Pol RT protein."; RL AIDS 13:1413-1414(1999). RN [49] RP INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I (MICROBIAL INFECTION). RX PubMed=11390610; DOI=10.1128/jvi.75.13.6086-6094.2001; RA Johnson J.M., Nicot C., Fullen J., Ciminale V., Casareto L., Mulloy J.C., RA Jacobson S., Franchini G.; RT "Free major histocompatibility complex class I heavy chain is RT preferentially targeted for degradation by human T-cell RT leukemia/lymphotropic virus type 1 p12(I) protein."; RL J. Virol. 75:6086-6094(2001). RN [50] RP INTERACTION WITH HUMAN HERPESVIRUS 8 MIR1 PROTEIN (MICROBIAL INFECTION), RP AND UBIQUITINATION (MICROBIAL INFECTION). RX PubMed=12006494; DOI=10.1093/emboj/21.10.2418; RA Hewitt E.W., Duncan L., Mufti D., Baker J., Stevenson P.G., Lehner P.J.; RT "Ubiquitylation of MHC class I by the K3 viral protein signals RT internalization and TSG101-dependent degradation."; RL EMBO J. 21:2418-2429(2002). RN [51] RP FUNCTION (ALLELE A*02:01). RX PubMed=12138174; DOI=10.1073/pnas.112331099; RA Nagata Y., Ono S., Matsuo M., Gnjatic S., Valmori D., Ritter G., RA Garrett W., Old L.J., Mellman I.; RT "Differential presentation of a soluble exogenous tumor antigen, NY-ESO-1, RT by distinct human dendritic cell populations."; RL Proc. Natl. Acad. Sci. U.S.A. 99:10629-10634(2002). RN [52] RP FUNCTION (ALLELE A*24:02). RX PubMed=12393434; DOI=10.1182/blood-2002-04-1240; RA Kuzushima K., Hayashi N., Kudoh A., Akatsuka Y., Tsujimura K., RA Morishima Y., Tsurumi T.; RT "Tetramer-assisted identification and characterization of epitopes RT recognized by HLA A*2402-restricted Epstein-Barr virus-specific CD8+ T RT cells."; RL Blood 101:1460-1468(2003). RN [53] RP FUNCTION (ALLELE A*26:01). RX PubMed=15893615; DOI=10.1016/j.vaccine.2005.02.022; RA Satoh M., Takamiya Y., Oka S., Tokunaga K., Takiguchi M.; RT "Identification and characterization of HIV-1-specific CD8+ T cell epitopes RT presented by HLA-A*2601."; RL Vaccine 23:3783-3790(2005). RN [54] RP FUNCTION (ALLELE A*01:01). RX PubMed=17189421; DOI=10.1158/1078-0432.ccr-06-1337; RA Asemissen A.M., Keilholz U., Tenzer S., Mueller M., Walter S., RA Stevanovic S., Schild H., Letsch A., Thiel E., Rammensee H.G., RA Scheibenbogen C.; RT "Identification of a highly immunogenic HLA-A*01-binding T cell epitope of RT WT1."; RL Clin. Cancer Res. 12:7476-7482(2006). RN [55] RP FUNCTION (ALLELES A*23:01; A*24:02 AND A*32:01), AND INTERACTION WITH RP KIR3DL1. RX PubMed=17182537; DOI=10.4049/jimmunol.178.1.33; RA Thananchai H., Gillespie G., Martin M.P., Bashirova A., Yawata N., RA Yawata M., Easterbrook P., McVicar D.W., Maenaka K., Parham P., RA Carrington M., Dong T., Rowland-Jones S.; RT "Cutting Edge: Allele-specific and peptide-dependent interactions between RT KIR3DL1 and HLA-A and HLA-B."; RL J. Immunol. 178:33-37(2007). RN [56] RP FUNCTION (ALLELE A*02:01). RX PubMed=17079320; DOI=10.1128/jvi.01779-06; RA Robek M.D., Garcia M.L., Boyd B.S., Chisari F.V.; RT "Role of immunoproteasome catalytic subunits in the immune response to RT hepatitis B virus."; RL J. Virol. 81:483-491(2007). RN [57] RP FUNCTION (ALLELE A*24:02), AND INTERACTION WITH KIR3DL1. RX PubMed=18502829; DOI=10.1182/blood-2008-02-137521; RA Stern M., Ruggeri L., Capanni M., Mancusi A., Velardi A.; RT "Human leukocyte antigens A23, A24, and A32 but not A25 are ligands for RT KIR3DL1."; RL Blood 112:708-710(2008). RN [58] RP FUNCTION (ALLELE A*01:01). RX PubMed=18779413; DOI=10.1182/blood-2008-06-162883; RA Brennan R.M., Burrows S.R.; RT "A mechanism for the HLA-A*01-associated risk for EBV+ Hodgkin lymphoma and RT infectious mononucleosis."; RL Blood 112:2589-2590(2008). RN [59] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [60] RP FUNCTION (ALLELE A*03:01). RX PubMed=19543285; DOI=10.1038/nmeth.1345; RA Hadrup S.R., Bakker A.H., Shu C.J., Andersen R.S., van Veluw J., RA Hombrink P., Castermans E., Thor Straten P., Blank C., Haanen J.B., RA Heemskerk M.H., Schumacher T.N.; RT "Parallel detection of antigen-specific T-cell responses by RT multidimensional encoding of MHC multimers."; RL Nat. Methods 6:520-526(2009). RN [61] RP FUNCTION (ALLELE A*01:01). RX PubMed=20364150; DOI=10.1038/ni.1862; RA Parmentier N., Stroobant V., Colau D., de Diesbach P., Morel S., RA Chapiro J., van Endert P., Van den Eynde B.J.; RT "Production of an antigenic peptide by insulin-degrading enzyme."; RL Nat. Immunol. 11:449-454(2010). RN [62] 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 [63] RP INDUCTION BY IFNG, GLYCOSYLATION AT ASN-110, MUTAGENESIS OF ASN-110, RP SUBCELLULAR LOCATION, AND INTERACTION WITH TAPBP. RX PubMed=21263072; DOI=10.4049/jimmunol.1002959; RA Rizvi S.M., Del Cid N., Lybarger L., Raghavan M.; RT "Distinct functions for the glycans of tapasin and heavy chains in the RT assembly of MHC class I molecules."; RL J. Immunol. 186:2309-2320(2011). RN [64] RP FUNCTION (ALLELE A*74:01). RX PubMed=21498667; DOI=10.4049/jimmunol.1003711; RA Matthews P.C., Adland E., Listgarten J., Leslie A., Mkhwanazi N., RA Carlson J.M., Harndahl M., Stryhn A., Payne R.P., Ogwu A., Huang K.H., RA Frater J., Paioni P., Kloverpris H., Jooste P., Goedhals D., van Vuuren C., RA Steyn D., Riddell L., Chen F., Luzzi G., Balachandran T., Ndung'u T., RA Buus S., Carrington M., Shapiro R., Heckerman D., Goulder P.J.; RT "HLA-A*7401-mediated control of HIV viremia is independent of its linkage RT disequilibrium with HLA-B*5703."; RL J. Immunol. 186:5675-5686(2011). RN [65] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356 AND SER-359, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [66] RP FUNCTION (ALLELE A*24:02). RX PubMed=24192765; DOI=10.1038/srep03097; RA Shimizu A., Kawana-Tachikawa A., Yamagata A., Han C., Zhu D., Sato Y., RA Nakamura H., Koibuchi T., Carlson J., Martin E., Brumme C.J., Shi Y., RA Gao G.F., Brumme Z.L., Fukai S., Iwamoto A.; RT "Structure of TCR and antigen complexes at an immunodominant CTL epitope in RT HIV-1 infection."; RL Sci. Rep. 3:3097-3097(2013). RN [67] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343; TYR-344; SER-349; RP SER-350; SER-352; SER-356 AND SER-359, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [68] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [69] RP FUNCTION (ALLELE A*01:01), AND SUBCELLULAR LOCATION. RX PubMed=25880248; DOI=10.1111/tan.12565; RA Giam K., Ayala-Perez R., Illing P.T., Schittenhelm R.B., Croft N.P., RA Purcell A.W., Dudek N.L.; RT "A comprehensive analysis of peptides presented by HLA-A1."; RL Tissue Antigens 85:492-496(2015). RN [70] RP INTERACTION WITH TAPBPL. RX PubMed=26869717; DOI=10.1073/pnas.1519894113; RA Morozov G.I., Zhao H., Mage M.G., Boyd L.F., Jiang J., Dolan M.A., RA Venna R., Norcross M.A., McMurtrey C.P., Hildebrand W., Schuck P., RA Natarajan K., Margulies D.H.; RT "Interaction of TAPBPR, a tapasin homolog, with MHC-I molecules promotes RT peptide editing."; RL Proc. Natl. Acad. Sci. U.S.A. 113:E1006-E1015(2016). RN [71] RP FUNCTION (ALLELE A*02:01). RX PubMed=26929325; DOI=10.1073/pnas.1521812113; RA Tripathi S.C., Peters H.L., Taguchi A., Katayama H., Wang H., Momin A., RA Jolly M.K., Celiktas M., Rodriguez-Canales J., Liu H., Behrens C., RA Wistuba I.I., Ben-Jacob E., Levine H., Molldrem J.J., Hanash S.M., RA Ostrin E.J.; RT "Immunoproteasome deficiency is a feature of non-small cell lung cancer RT with a mesenchymal phenotype and is associated with a poor outcome."; RL Proc. Natl. Acad. Sci. U.S.A. 113:E1555-E1564(2016). RN [72] RP FUNCTION (ALLELE A*03:01). RX PubMed=27049119; DOI=10.1038/srep24032; RA Ebstein F., Textoris-Taube K., Keller C., Golnik R., Vigneron N., RA Van den Eynde B.J., Schuler-Thurner B., Schadendorf D., Lorenz F.K., RA Uckert W., Urban S., Lehmann A., Albrecht-Koepke N., Janek K., Henklein P., RA Niewienda A., Kloetzel P.M., Mishto M.; RT "Proteasomes generate spliced epitopes by two different mechanisms and as RT efficiently as non-spliced epitopes."; RL Sci. Rep. 6:24032-24032(2016). RN [73] RP FUNCTION (ALLELE A*01:01). RX PubMed=30530481; DOI=10.4049/jimmunol.1801003; RA Keib A., Mei Y.F., Cicin-Sain L., Busch D.H., Dennehy K.M.; RT "Measuring Antiviral Capacity of T Cell Responses to Adenovirus."; RL J. Immunol. 202:618-624(2019). RN [74] RP FUNCTION (ALLELES A*01:01; A*03:01 AND A*11:01). RX PubMed=32887977; DOI=10.1038/s41590-020-0782-6; RG Oxford Immunology Network Covid-19 Response T cell Consortium; RG ISARIC4C Investigators; RA Peng Y., Mentzer A.J., Liu G., Yao X., Yin Z., Dong D., Dejnirattisai W., RA Rostron T., Supasa P., Liu C., Lopez-Camacho C., Slon-Campos J., Zhao Y., RA Stuart D.I., Paesen G.C., Grimes J.M., Antson A.A., Bayfield O.W., RA Hawkins D.E.D.P., Ker D.S., Wang B., Turtle L., Subramaniam K., Thomson P., RA Zhang P., Dold C., Ratcliff J., Simmonds P., de Silva T., Sopp P., RA Wellington D., Rajapaksa U., Chen Y.L., Salio M., Napolitani G., Paes W., RA Borrow P., Kessler B.M., Fry J.W., Schwabe N.F., Semple M.G., Baillie J.K., RA Moore S.C., Openshaw P.J.M., Ansari M.A., Dunachie S., Barnes E., RA Frater J., Kerr G., Goulder P., Lockett T., Levin R., Zhang Y., Jing R., RA Ho L.P., Cornall R.J., Conlon C.P., Klenerman P., Screaton G.R., RA Mongkolsapaya J., McMichael A., Knight J.C., Ogg G., Dong T.; RT "Broad and strong memory CD4+ and CD8+ T cells induced by SARS-CoV-2 in UK RT convalescent individuals following COVID-19."; RL Nat. Immunol. 21:1336-1345(2020). RN [75] RP DOMAIN, CHARACTERIZATION OF VARIANTS PRO-5; VAL-10 AND LEU-14, AND RP POLYMORPHISM. RX PubMed=37264229; DOI=10.1038/s41590-023-01523-z; RA Lin Z., Bashirova A.A., Viard M., Garner L., Quastel M., Beiersdorfer M., RA Kasprzak W.K., Akdag M., Yuki Y., Ojeda P., Das S., Andresson T., RA Naranbhai V., Horowitz A., McMichael A.J., Hoelzemer A., Gillespie G.M., RA Garcia-Beltran W.F., Carrington M.; RT "HLA class I signal peptide polymorphism determines the level of CD94/NKG2- RT HLA-E-mediated regulation of effector cell responses."; RL Nat. Immunol. 24:1087-1097(2023). RN [76] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-294 (ALLELE A*68:01), AND RP FUNCTION (ALLELE A*68:01). RX PubMed=1448153; DOI=10.1038/360364a0; RA Guo H.-C., Jardetzky T.S., Garrett T.P.J., Lane W.S., Strominger J.L., RA Wiley D.C.; RT "Different length peptides bind to HLA-Aw68 similarly at their ends but RT bulge out in the middle."; RL Nature 360:364-366(1992). RN [77] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-294 (ALLELE A*68:01), AND RP FUNCTION (ALLELE A*68:01). RX PubMed=1448154; DOI=10.1038/360367a0; RA Silver M.L., Guo H.-C., Strominger J.L., Wiley D.C.; RT "Atomic structure of a human MHC molecule presenting an influenza virus RT peptide."; RL Nature 360:367-369(1992). RN [78] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 25-299 (ALLELE A*02:01) IN RP COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE A*02:01), DISULFIDE BOND, RP AND DOMAIN. RX PubMed=7694806; DOI=10.1016/0092-8674(93)90490-h; RA Madden D.R., Garboczi D.N., Wiley D.C.; RT "The antigenic identity of peptide-MHC complexes: a comparison of the RT conformations of five viral peptides presented by HLA-A2."; RL Cell 75:693-708(1993). RN [79] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 25-299 (ALLELE A*02:01) IN RP COMPLEX WITH B2M AND PEPTIDE, AND FUNCTION (ALLELE A*02:01). RX PubMed=7935798; DOI=10.1038/371626a0; RA Collins E.J., Garboczi D.N., Wiley D.C.; RT "Three-dimensional structure of a peptide extending from one end of a class RT I MHC binding site."; RL Nature 371:626-629(1994). RN [80] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 25-299 (ALLELE A*02:01) IN RP COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE A*02:01), AND DOMAIN. RX PubMed=8906788; DOI=10.1038/384134a0; RA Garboczi D.N., Ghosh P., Utz U., Fan Q.R., Biddison W.E., Wiley D.C.; RT "Structure of the complex between human T-cell receptor, viral peptide and RT HLA-A2."; RL Nature 384:134-141(1996). RN [81] RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 25-300 (ALLELE A*02:01) IN RP COMPLEX WITH B2M AND PEPTIDE, INTERACTION WITH CD8A, AND FUNCTION (ALLELE RP A*02:01). RX PubMed=9177355; DOI=10.1038/42523; RA Gao G.F., Tormo J., Gerth U.C., Wyer J.R., McMichael A.J., Stuart D.I., RA Bell J.I., Jones E.Y., Jakobsen B.K.; RT "Crystal structure of the complex between human CD8alpha(alpha) and HLA- RT A2."; RL Nature 387:630-634(1997). RN [82] RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 25-299 (ALLELE A*02:01) IN RP COMPLEX WITH B2M AND PEPTIDE, AND FUNCTION (ALLELE A*02:01). RX PubMed=11502003; DOI=10.1006/jmbi.2001.4816; RA Hillig R.C., Coulie P.G., Stroobant V., Saenger W., Ziegler A., RA Hulsmeyer M.; RT "High-resolution structure of HLA-A*0201 in complex with a tumour-specific RT antigenic peptide encoded by the MAGE-A4 gene."; RL J. Mol. Biol. 310:1167-1176(2001). RN [83] RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 25-300 (ALLELE A*02:01) IN RP COMPLEX WITH B2M AND PEPTIDE, INTERACTION WITH TCR, AND FUNCTION (ALLELE RP A*02:01). RX PubMed=12796775; DOI=10.1038/ni942; RA Stewart-Jones G.B.E., McMichael A.J., Bell J.I., Stuart D.I., Jones E.Y.; RT "A structural basis for immunodominant human T cell receptor recognition."; RL Nat. Immunol. 4:657-663(2003). RN [84] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 25-299 (ALLELE A*11:01) IN RP COMPLEX WITH SARS NUCLEOCAPSID PEPTIDE, AND DISULFIDE BONDS. RX PubMed=16041067; DOI=10.1107/s0907444905013090; RA Blicher T., Kastrup J.S., Buus S., Gajhede M.; RT "High-resolution structure of HLA-A*1101 in complex with SARS nucleocapsid RT peptide."; RL Acta Crystallogr. D 61:1031-1040(2005). RN [85] RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 25-300 (ALLELE A*02:01) IN RP COMPLEX WITH B2M AND PEPTIDE, INTERACTION WITH TCR, AND FUNCTION (ALLELE RP A*02:01). RX PubMed=18275829; DOI=10.1016/j.immuni.2007.12.018; RA Ishizuka J., Stewart-Jones G.B., van der Merwe A., Bell J.I., RA McMichael A.J., Jones E.Y.; RT "The structural dynamics and energetics of an immunodominant T cell RT receptor are programmed by its Vbeta domain."; RL Immunity 28:171-182(2008). RN [86] RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 25-298 (ALLELE A*02:01) IN RP COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE A*02:01), AND DOMAIN. RX PubMed=19542454; DOI=10.4049/jimmunol.0900556; RA Gras S., Saulquin X., Reiser J.B., Debeaupuis E., Echasserieau K., RA Kissenpfennig A., Legoux F., Chouquet A., Le Gorrec M., Machillot P., RA Neveu B., Thielens N., Malissen B., Bonneville M., Housset D.; RT "Structural bases for the affinity-driven selection of a public TCR against RT a dominant human cytomegalovirus epitope."; RL J. Immunol. 183:430-437(2009). RN [87] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 25-298 (ALLELE A*01:01) IN RP COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE A*01:01), DOMAIN, AND RP DISULFIDE BOND. RX PubMed=19177349; DOI=10.1002/pro.4; RA Kumar P., Vahedi-Faridi A., Saenger W., Ziegler A., Uchanska-Ziegler B.; RT "Conformational changes within the HLA-A1:MAGE-A1 complex induced by RT binding of a recombinant antibody fragment with TCR-like specificity."; RL Protein Sci. 18:37-49(2009). RN [88] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-298 (ALLELE A*24:02) IN COMPLEX RP WITH B2M AND WITH SARS NUCLEOCAPSID PEPTIDE, DISULFIDE BONDS, FUNCTION RP (ALLELE A*24:02), AND DOMAIN. RX PubMed=20844028; DOI=10.1128/jvi.01464-10; RA Liu J., Wu P., Gao F., Qi J., Kawana-Tachikawa A., Xie J., Vavricka C.J., RA Iwamoto A., Li T., Gao G.F.; RT "Novel immunodominant peptide presentation strategy: a featured HLA-A*2402- RT restricted cytotoxic T-lymphocyte epitope stabilized by intrachain hydrogen RT bonds from severe acute respiratory syndrome coronavirus nucleocapsid RT protein."; RL J. Virol. 84:11849-11857(2010). RN [89] RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 25-299 (ALLELE A*02:01) IN RP COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE A*02:01), AND DOMAIN. RX PubMed=20619457; DOI=10.1016/j.molimm.2010.06.005; RA Borbulevych O.Y., Do P., Baker B.M.; RT "Structures of native and affinity-enhanced WT1 epitopes bound to HLA- RT A*0201: implications for WT1-based cancer therapeutics."; RL Mol. Immunol. 47:2519-2524(2010). RN [90] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 25-298 (ALLELE A*03:01) IN COMPLEX RP WITH B2M AND PLP1 ANTIGENIC PEPTIDE, DISULFIDE BONDS, AND DOMAIN. RX PubMed=21543847; DOI=10.1107/s0907444911007888; RA McMahon R.M., Friis L., Siebold C., Friese M.A., Fugger L., Jones E.Y.; RT "Structure of HLA-A*0301 in complex with a peptide of proteolipid protein: RT insights into the role of HLA-A alleles in susceptibility to multiple RT sclerosis."; RL Acta Crystallogr. D 67:447-454(2011). RN [91] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 25-298 (ALLELE A*03:01) IN RP COMPLEX WITH B2M AND PEPTIDE, DISULFIDE BOND, DOMAIN, AND FUNCTION (ALLELE RP A*03:01). RX PubMed=21943705; DOI=10.1016/j.molimm.2011.08.015; RA Zhang S., Liu J., Cheng H., Tan S., Qi J., Yan J., Gao G.F.; RT "Structural basis of cross-allele presentation by HLA-A*0301 and HLA-A*1101 RT revealed by two HIV-derived peptide complexes."; RL Mol. Immunol. 49:395-401(2011). RN [92] RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 25-300 (ALLELE A*02:01) IN RP COMPLEX WITH B2M AND PEPTIDE, INTERACTION WITH TCR, FUNCTION (ALLELE RP A*02:01), DOMAIN, INDUCTION BY CYTOKINES, AND INVOLVEMENT IN IDDM (ALLELE RP A*02:01). RX PubMed=22245737; DOI=10.1038/ni.2206; RA Bulek A.M., Cole D.K., Skowera A., Dolton G., Gras S., Madura F., RA Fuller A., Miles J.J., Gostick E., Price D.A., Drijfhout J.W., Knight R.R., RA Huang G.C., Lissin N., Molloy P.E., Wooldridge L., Jakobsen B.K., RA Rossjohn J., Peakman M., Rizkallah P.J., Sewell A.K.; RT "Structural basis for the killing of human beta cells by CD8(+) T cells in RT type 1 diabetes."; RL Nat. Immunol. 13:283-289(2012). RN [93] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 25-308 (ALLELE A*01:01) IN RP COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE A*01:01), AND DOMAIN. RX PubMed=24395804; DOI=10.1073/pnas.1322229111; RA Quinones-Parra S., Grant E., Loh L., Nguyen T.H., Campbell K.A., Tong S.Y., RA Miller A., Doherty P.C., Vijaykrishna D., Rossjohn J., Gras S., RA Kedzierska K.; RT "Preexisting CD8+ T-cell immunity to the H7N9 influenza A virus varies RT across ethnicities."; RL Proc. Natl. Acad. Sci. U.S.A. 111:1049-1054(2014). RN [94] RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 25-298 (ALLELE A*01:01) IN RP COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE A*01:01), DOMAIN, AND RP DISULFIDE BOND. RX PubMed=26758806; DOI=10.1038/srep18851; RA Raman M.C., Rizkallah P.J., Simmons R., Donnellan Z., Dukes J., Bossi G., RA Le Provost G.S., Todorov P., Baston E., Hickman E., Mahon T., Hassan N., RA Vuidepot A., Sami M., Cole D.K., Jakobsen B.K.; RT "Direct molecular mimicry enables off-target cardiovascular toxicity by an RT enhanced affinity TCR designed for cancer immunotherapy."; RL Sci. Rep. 6:18851-18851(2016). RN [95] RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 25-299 (ALLELE A*02:01) IN RP COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE A*02:01), DOMAIN, AND RP DISULFIDE BOND. RX PubMed=28250417; DOI=10.1038/nsmb.3383; RA Song I., Gil A., Mishra R., Ghersi D., Selin L.K., Stern L.J.; RT "Broad TCR repertoire and diverse structural solutions for recognition of RT an immunodominant CD8+ T cell epitope."; RL Nat. Struct. Mol. Biol. 24:395-406(2017). RN [96] RP ASSOCIATION OF ALLELE A*29:02 WITH BIRDSHOT CHORIORETINOPATHY. RX PubMed=1728143; DOI=10.1016/s0002-9394(14)75749-6; RA LeHoang P., Ozdemir N., Benhamou A., Tabary T., Edelson C., Betuel H., RA Semiglia R., Cohen J.H.; RT "HLA-A29.2 subtype associated with birdshot retinochoroidopathy."; RL Am. J. Ophthalmol. 113:33-35(1992). RN [97] RP ASSOCIATION OF ALLELE A*03:01 WITH MULTIPLE SCLEROSIS. RX PubMed=10746785; DOI=10.1034/j.1399-0039.2000.550205.x; RA Fogdell-Hahn A., Ligers A., Groenning M., Hillert J., Olerup O.; RT "Multiple sclerosis: a modifying influence of HLA class I genes in an HLA RT class II associated autoimmune disease."; RL Tissue Antigens 55:140-148(2000). RN [98] RP ASSOCIATION OF ALLELE A*24:02 WITH IDDM. RX PubMed=16731854; DOI=10.2337/db05-1049; RA Nakanishi K., Inoko H.; RT "Combination of HLA-A24, -DQA1*03, and -DR9 contributes to acute-onset and RT early complete beta-cell destruction in type 1 diabetes: longitudinal study RT of residual beta-cell function."; RL Diabetes 55:1862-1868(2006). RN [99] RP ASSOCIATION OF ALLELE A*02:01 WITH IDDM. RX PubMed=18802479; DOI=10.1172/jci35449; RA Skowera A., Ellis R.J., Varela-Calvino R., Arif S., Huang G.C., RA Van-Krinks C., Zaremba A., Rackham C., Allen J.S., Tree T.I., Zhao M., RA Dayan C.M., Sewell A.K., Unger W.W., Unger W., Drijfhout J.W., RA Ossendorp F., Roep B.O., Peakman M.; RT "CTLs are targeted to kill beta cells in patients with type 1 diabetes RT through recognition of a glucose-regulated preproinsulin epitope."; RL J. Clin. Invest. 118:3390-3402(2008). RN [100] RP ASSOCIATION OF ALLELE A*03:01 WITH MULTIPLE SCLEROSIS. RX PubMed=18953350; DOI=10.1038/nm.1881; RA Friese M.A., Jakobsen K.B., Friis L., Etzensperger R., Craner M.J., RA McMahon R.M., Jensen L.T., Huygelen V., Jones E.Y., Bell J.I., Fugger L.; RT "Opposing effects of HLA class I molecules in tuning autoreactive CD8+ T RT cells in multiple sclerosis."; RL Nat. Med. 14:1227-1235(2008). RN [101] RP ASSOCIATION OF ALLELE A*24:02 WITH IDDM. RX PubMed=22522618; DOI=10.2337/db11-1520; RA Kronenberg D., Knight R.R., Estorninho M., Ellis R.J., Kester M.G., RA de Ru A., Eichmann M., Huang G.C., Powrie J., Dayan C.M., Skowera A., RA van Veelen P.A., Peakman M.; RT "Circulating preproinsulin signal peptide-specific CD8 T cells restricted RT by the susceptibility molecule HLA-A24 are expanded at onset of type 1 RT diabetes and kill beta-cells."; RL Diabetes 61:1752-1759(2012). RN [102] RP ASSOCIATION OF ALLELE A*31:01 WITH CARBAMAZEPINE-INDUCED HYPERSENSITIVITY RP REACTIONS. RX PubMed=21428769; DOI=10.1056/nejmoa1013297; RA McCormack M., Alfirevic A., Bourgeois S., Farrell J.J., Kasperaviciute D., RA Carrington M., Sills G.J., Marson T., Jia X., de Bakker P.I., RA Chinthapalli K., Molokhia M., Johnson M.R., O'Connor G.D., Chaila E., RA Alhusaini S., Shianna K.V., Radtke R.A., Heinzen E.L., Walley N., RA Pandolfo M., Pichler W., Park B.K., Depondt C., Sisodiya S.M., RA Goldstein D.B., Deloukas P., Delanty N., Cavalleri G.L., Pirmohamed M.; RT "HLA-A*3101 and carbamazepine-induced hypersensitivity reactions in RT Europeans."; RL N. Engl. J. Med. 364:1134-1143(2011). RN [103] RP ASSOCIATION OF ALLELE A*26:01 WITH BEHCET DISEASE. RX PubMed=30872678; DOI=10.1038/s41598-019-40824-y; RA Nakamura J., Meguro A., Ishii G., Mihara T., Takeuchi M., Mizuki Y., RA Yuda K., Yamane T., Kawagoe T., Ota M., Mizuki N.; RT "The association analysis between HLA-A*26 and Behcet's disease."; RL Sci. Rep. 9:4426-4426(2019). RN [104] RP POLYMORPHISM. RX PubMed=28650991; DOI=10.1371/journal.pgen.1006862; RA Robinson J., Guethlein L.A., Cereb N., Yang S.Y., Norman P.J., RA Marsh S.G.E., Parham P.; RT "Distinguishing functional polymorphism from random variation in the RT sequences of >10,000 HLA-A, -B and -C alleles."; RL PLoS Genet. 13:E1006862-E1006862(2017). CC -!- FUNCTION: Antigen-presenting major histocompatibility complex class I CC (MHCI) molecule. In complex with B2M/beta 2 microglobulin displays CC primarily viral and tumor-derived peptides on antigen-presenting cells CC for recognition by alpha-beta T cell receptor (TCR) on HLA-A-restricted CC CD8-positive T cells, guiding antigen-specific T cell immune response CC to eliminate infected or transformed cells (PubMed:2456340, CC PubMed:2784196, PubMed:1402688, PubMed:7504010, PubMed:9862734, CC PubMed:10449296, PubMed:12138174, PubMed:12393434, PubMed:15893615, CC PubMed:17189421, PubMed:19543285, PubMed:21498667, PubMed:24192765, CC PubMed:7694806, PubMed:24395804, PubMed:28250417). May also present CC self-peptides derived from the signal sequence of secreted or membrane CC proteins, although T cells specific for these peptides are usually CC inactivated to prevent autoreactivity (PubMed:25880248, PubMed:7506728, CC PubMed:7679507). Both the peptide and the MHC molecule are recognized CC by TCR, the peptide is responsible for the fine specificity of antigen CC recognition and MHC residues account for the MHC restriction of T cells CC (PubMed:12796775, PubMed:18275829, PubMed:19542454, PubMed:28250417). CC Typically presents intracellular peptide antigens of 8 to 13 amino CC acids that arise from cytosolic proteolysis via IFNG-induced CC immunoproteasome or via endopeptidase IDE/insulin-degrading enzyme CC (PubMed:17189421, PubMed:20364150, PubMed:17079320, PubMed:26929325, CC PubMed:27049119). Can bind different peptides containing allele- CC specific binding motifs, which are mainly defined by anchor residues at CC position 2 and 9 (PubMed:7504010, PubMed:9862734). CC {ECO:0000269|PubMed:10449296, ECO:0000269|PubMed:12138174, CC ECO:0000269|PubMed:12393434, ECO:0000269|PubMed:12796775, CC ECO:0000269|PubMed:1402688, ECO:0000269|PubMed:15893615, CC ECO:0000269|PubMed:17079320, ECO:0000269|PubMed:17189421, CC ECO:0000269|PubMed:18275829, ECO:0000269|PubMed:19542454, CC ECO:0000269|PubMed:19543285, ECO:0000269|PubMed:20364150, CC ECO:0000269|PubMed:21498667, ECO:0000269|PubMed:24192765, CC ECO:0000269|PubMed:24395804, ECO:0000269|PubMed:2456340, CC ECO:0000269|PubMed:25880248, ECO:0000269|PubMed:26929325, CC ECO:0000269|PubMed:27049119, ECO:0000269|PubMed:2784196, CC ECO:0000269|PubMed:28250417, ECO:0000269|PubMed:7504010, CC ECO:0000269|PubMed:7506728, ECO:0000269|PubMed:7679507, CC ECO:0000269|PubMed:7694806, ECO:0000269|PubMed:9862734}. CC -!- FUNCTION: Allele A*01:01: Presents a restricted peptide repertoire CC including viral epitopes derived from IAV NP/nucleoprotein (CTELKLSDY), CC IAV PB1/polymerase basic protein 1 (VSDGGPNLY), HAdV-11 capsid L3/hexon CC protein (LTDLGQNLLY), SARS-CoV-2 3a/ORF3a (FTSDYYQLY) as well as tumor CC peptide antigens including MAGE1 (EADPTGHSY), MAGEA3 (EVDPIGHLY) and CC WT1 (TSEKRPFMCAY), all having in common a canonical motif with a CC negatively charged Asp or Glu residue at position 3 and a Tyr anchor CC residue at the C-terminus (PubMed:1402688, PubMed:7504010, CC PubMed:17189421, PubMed:20364150, PubMed:25880248, PubMed:30530481, CC PubMed:19177349, PubMed:24395804, PubMed:26758806, PubMed:32887977). A CC number of HLA-A*01:01-restricted peptides carry a post-translational CC modification with oxidation and N-terminal acetylation being the most CC frequent (PubMed:25880248). Fails to present highly immunogenic CC peptides from the EBV latent antigens (PubMed:18779413). CC {ECO:0000269|PubMed:1402688, ECO:0000269|PubMed:17189421, CC ECO:0000269|PubMed:18779413, ECO:0000269|PubMed:19177349, CC ECO:0000269|PubMed:20364150, ECO:0000269|PubMed:24395804, CC ECO:0000269|PubMed:25880248, ECO:0000269|PubMed:26758806, CC ECO:0000269|PubMed:30530481, ECO:0000269|PubMed:7504010}. CC -!- FUNCTION: Allele A*02:01: A major allele in human populations, presents CC immunodominant viral epitopes derived from IAV M/matrix protein 1 CC (GILGFVFTL), HIV-1 env (TLTSCNTSV), HIV-1 gag-pol (ILKEPVHGV), HTLV-1 CC Tax (LLFGYPVYV), HBV C/core antigen (FLPSDFFPS), HCMV UL83/pp65 CC (NLVPMVATV) as well as tumor peptide antigens including MAGEA4 CC (GVYDGREHTV), WT1 (RMFPNAPYL) and CTAG1A/NY-ESO-1 (SLLMWITQC), all CC having in common hydrophobic amino acids at position 2 and at the C- CC terminal anchors. {ECO:0000269|PubMed:11502003, CC ECO:0000269|PubMed:12138174, ECO:0000269|PubMed:12796775, CC ECO:0000269|PubMed:17079320, ECO:0000269|PubMed:18275829, CC ECO:0000269|PubMed:19542454, ECO:0000269|PubMed:20619457, CC ECO:0000269|PubMed:22245737, ECO:0000269|PubMed:26929325, CC ECO:0000269|PubMed:2784196, ECO:0000269|PubMed:28250417, CC ECO:0000269|PubMed:7694806, ECO:0000269|PubMed:7935798, CC ECO:0000269|PubMed:8630735, ECO:0000269|PubMed:8805302, CC ECO:0000269|PubMed:8906788, ECO:0000269|PubMed:9177355}. CC -!- FUNCTION: Allele A*03:01: Presents viral epitopes derived from IAV NP CC (ILRGSVAHK), HIV-1 nef (QVPLRPMTYK), HIV-1 gag-pol (AIFQSSMTK), SARS- CC CoV-2 N/nucleoprotein (KTFPPTEPK) as well as tumor peptide antigens CC including PMEL (LIYRRRLMK), NODAL (HAYIQSLLK), TRP-2 (RMYNMVPFF), all CC having in common hydrophobic amino acids at position 2 and Lys or Arg CC anchor residues at the C-terminus (PubMed:7504010, PubMed:7679507, CC PubMed:9862734, PubMed:19543285, PubMed:21943705, PubMed:2456340, CC PubMed:32887977). May also display spliced peptides resulting from the CC ligation of two separate proteasomal cleavage products that are not CC contiguous in the parental protein (PubMed:27049119). CC {ECO:0000269|PubMed:19543285, ECO:0000269|PubMed:21943705, CC ECO:0000269|PubMed:2456340, ECO:0000269|PubMed:27049119, CC ECO:0000269|PubMed:7504010, ECO:0000269|PubMed:7679507, CC ECO:0000269|PubMed:9862734}. CC -!- FUNCTION: Allele A*11:01: Presents several immunodominant epitopes CC derived from HIV-1 gag-pol and HHV-4 EBNA4, containing the peptide CC motif with Val, Ile, Thr, Leu, Tyr or Phe at position 2 and Lys anchor CC residue at the C-terminus. Important in the control of HIV-1, EBV and CC HBV infections (PubMed:10449296). Presents an immunodominant epitope CC derived from SARS-CoV-2 N/nucleoprotein (KTFPPTEPK) (PubMed:32887977). CC {ECO:0000269|PubMed:10449296, ECO:0000269|PubMed:32887977}. CC -!- FUNCTION: Allele A*23:01: Interacts with natural killer (NK) cell CC receptor KIR3DL1 and may contribute to functional maturation of NK CC cells and self-nonself discrimination during innate immune response. CC {ECO:0000269|PubMed:17182537}. CC -!- FUNCTION: Allele A*24:02: Presents viral epitopes derived from HIV-1 CC nef (RYPLTFGWCF), EBV lytic- and latent-cycle antigens BRLF1 CC (TYPVLEEMF), BMLF1 (DYNFVKQLF) and LMP2 (IYVLVMLVL), SARS-CoV CC nucleocapsid/N (QFKDNVILL), as well as tumor peptide antigens including CC PRAME (LYVDSLFFL), all sharing a common signature motif, namely an CC aromatic residue Tyr or Phe at position 2 and a nonhydrophobic anchor CC residue Phe, Leu or Iso at the C-terminus (PubMed:9047241, CC PubMed:12393434, PubMed:24192765, PubMed:20844028). Interacts with CC natural killer (NK) cell receptor KIR3DL1 and may contribute to CC functional maturation of NK cells and self-nonself discrimination CC during innate immune response (PubMed:17182537, PubMed:18502829). CC {ECO:0000269|PubMed:12393434, ECO:0000269|PubMed:17182537, CC ECO:0000269|PubMed:18502829, ECO:0000269|PubMed:20844028, CC ECO:0000269|PubMed:24192765, ECO:0000269|PubMed:9047241}. CC -!- FUNCTION: Allele A*26:01: Presents several epitopes derived from HIV-1 CC gag-pol (EVIPMFSAL, ETKLGKAGY) and env (LVSDGGPNLY), carrying as anchor CC residues preferentially Glu at position 1, Val or Thr at position 2 and CC Tyr at the C-terminus. {ECO:0000269|PubMed:15893615}. CC -!- FUNCTION: Allele A*29:02: Presents peptides having a common motif, CC namely a Glu residue at position 2 and Tyr or Leu anchor residues at CC the C-terminus. {ECO:0000269|PubMed:8622959}. CC -!- FUNCTION: Allele A*32:01: Interacts with natural killer (NK) cell CC receptor KIR3DL1 and may contribute to functional maturation of NK CC cells and self-nonself discrimination during innate immune response. CC {ECO:0000269|PubMed:17182537}. CC -!- FUNCTION: Allele A*68:01: Presents viral epitopes derived from IAV NP CC (KTGGPIYKR) and HIV-1 tat (ITKGLGISYGR), having a common signature CC motif namely, Val or Thr at position 2 and positively charged residues CC Arg or Lys at the C-terminal anchor. {ECO:0000269|PubMed:1448153, CC ECO:0000269|PubMed:1448154, ECO:0000269|PubMed:2784196}. CC -!- FUNCTION: Allele A*74:01: Presents immunodominant HIV-1 epitopes CC derived from gag-pol (GQMVHQAISPR, QIYPGIKVR) and rev (RQIHSISER), CC carrying an aliphatic residue at position 2 and Arg anchor residue at CC the C-terminus. May contribute to viral load control in chronic HIV-1 CC infection. {ECO:0000269|PubMed:21498667}. CC -!- SUBUNIT: Heterotrimer that consists of an alpha chain HLA-A, a beta CC chain B2M and a peptide (peptide-HLA-A-B2M) (PubMed:7504010, CC PubMed:7679507, PubMed:21943705, PubMed:19177349, PubMed:24395804, CC PubMed:26758806, PubMed:7504010, PubMed:7506728, PubMed:8805302, CC PubMed:7694806, PubMed:7935798, PubMed:9177355, PubMed:18275829, CC PubMed:22245737, PubMed:28250417, PubMed:11502003, PubMed:8906788, CC PubMed:19542454). Early in biogenesis, HLA-A-B2M dimer interacts with CC the components of the peptide-loading complex composed of TAPBP, TAP1- CC TAP2, TAPBPL, PDIA3/ERP57 and CALR (PubMed:21263072). Interacts with CC TAP1-TAP2 transporter via TAPBP; this interaction is obligatory for the CC loading of peptide epitopes delivered to the ER by TAP1-TAP2 CC transporter (PubMed:8805302, PubMed:8630735, PubMed:21263072). CC Interacts with TAPBPL; TAPBPL binds peptide-free HLA-A-B2M complexes or CC those loaded with low affinity peptides, likely facilitating peptide CC exchange for higher affinity peptides (PubMed:26869717). Only optimally CC assembled peptide-HLA-B2M trimer translocates to the surface of CC antigen-presenting cells, where it interacts with TCR and CD8 CC coreceptor on the surface of T cells. HLA-A (via polymorphic alpha-1 CC and alpha-2 domains) interacts with antigen-specific TCR (via CDR3 CC domains) (PubMed:22245737, PubMed:12796775, PubMed:18275829). One HLA-A CC molecule (mainly via nonpolymorphic alpha-3 domain) interacts with one CC CD8A homodimer (via CDR-like loop); this interaction ensures peptide- CC HLA-A-B2M recognition by CD8-positive T cells only (PubMed:9177355, CC PubMed:2784196). Alleles A*23:01; A*24:02 and A*32:01 interact (via Bw4 CC motif) with KIR3DL1 on NK cells; this interaction is direct. CC {ECO:0000269|PubMed:11502003, ECO:0000269|PubMed:12796775, CC ECO:0000269|PubMed:17182537, ECO:0000269|PubMed:18275829, CC ECO:0000269|PubMed:18502829, ECO:0000269|PubMed:19177349, CC ECO:0000269|PubMed:21263072, ECO:0000269|PubMed:21943705, CC ECO:0000269|PubMed:22245737, ECO:0000269|PubMed:24395804, CC ECO:0000269|PubMed:26758806, ECO:0000269|PubMed:26869717, CC ECO:0000269|PubMed:2784196, ECO:0000269|PubMed:28250417, CC ECO:0000269|PubMed:7504010, ECO:0000269|PubMed:7506728, CC ECO:0000269|PubMed:7679507, ECO:0000269|PubMed:7694806, CC ECO:0000269|PubMed:7935798, ECO:0000269|PubMed:8630735, CC ECO:0000269|PubMed:8805302, ECO:0000269|PubMed:9177355}. CC -!- SUBUNIT: (Microbial infection) Interacts with HHV-8 MIR1 protein. CC {ECO:0000269|PubMed:12006494}. CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 accessory protein CC p12I. {ECO:0000269|PubMed:11390610}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21263072, CC ECO:0000269|PubMed:25880248, ECO:0000269|PubMed:8805302}; Single-pass CC type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane CC {ECO:0000305|PubMed:8805302}; Single-pass type I membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P04439-1; Sequence=Displayed; CC Name=2; CC IsoId=P04439-2; Sequence=VSP_060391, VSP_060392; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000305}. CC -!- INDUCTION: Up-regulated by IFNG, and pro-inflammatory cytokines IL1B CC and TNF. {ECO:0000269|PubMed:21263072, ECO:0000269|PubMed:22245737}. CC -!- DOMAIN: The alpha-1 domain is a structural part of the peptide-binding CC cleft. {ECO:0000269|PubMed:19177349, ECO:0000269|PubMed:19542454, CC ECO:0000269|PubMed:20619457, ECO:0000269|PubMed:20844028, CC ECO:0000269|PubMed:21943705, ECO:0000269|PubMed:22245737, CC ECO:0000269|PubMed:24395804, ECO:0000269|PubMed:26758806, CC ECO:0000269|PubMed:2784196, ECO:0000269|PubMed:7694806, CC ECO:0000269|PubMed:8906788}. CC -!- DOMAIN: The alpha-2 domain is a structural part of the peptide-binding CC cleft (PubMed:21543847, PubMed:21943705, PubMed:19177349, CC PubMed:26758806, PubMed:24395804, PubMed:7694806, PubMed:8906788, CC PubMed:2784196, PubMed:28250417, PubMed:22245737, PubMed:19542454, CC PubMed:20619457, PubMed:20844028). Mediates the interaction with TAP1- CC TAP2 complex (PubMed:8805302). {ECO:0000269|PubMed:19177349, CC ECO:0000269|PubMed:19542454, ECO:0000269|PubMed:20619457, CC ECO:0000269|PubMed:20844028, ECO:0000269|PubMed:21543847, CC ECO:0000269|PubMed:21943705, ECO:0000269|PubMed:22245737, CC ECO:0000269|PubMed:24395804, ECO:0000269|PubMed:26758806, CC ECO:0000269|PubMed:2784196, ECO:0000269|PubMed:28250417, CC ECO:0000269|PubMed:7694806, ECO:0000269|PubMed:8805302, CC ECO:0000269|PubMed:8906788}. CC -!- DOMAIN: The alpha-3 Ig-like domain mediates the interaction with CD8 CC coreceptor. {ECO:0000269|PubMed:2784196}. CC -!- DOMAIN: The VL9 peptide/epitope (VMAPRT[V/L][L/V/I/F]L) derived from CC the signal sequence is loaded onto HLA-E and enables HLA-E expression CC at the plasma membrane. Distinct VL9 peptides presented by HLA-E CC variably affect its recognition by KLRD1-KLRC1 or KLRD1-KLRC2 receptors CC on NK cells, setting NK cell activation threshold. Common HLA-A CC allotypes contain functional VL9 peptides (VMAPRTLLL, VMAPRTLVL and CC VPAPRTLLL). {ECO:0000269|PubMed:37264229}. CC -!- PTM: (Microbial infection) Polyubiquitinated in a post ER compartment CC by interaction with human herpesvirus 8 MIR1 protein. This targets the CC protein for rapid degradation via the ubiquitin system. CC {ECO:0000269|PubMed:12006494}. CC -!- PTM: N-linked glycosylation at Asn-110. {ECO:0000269|PubMed:19159218, CC ECO:0000269|PubMed:21263072}. CC -!- POLYMORPHISM: Highly polymorphic. Polymorphic residues encode for CC alpha-1 and alpha-2 domains of the peptide-binding cleft, where they CC contribute to variations in peptide binding and TCR recognition among CC different alleles. The human population is estimated to have millions CC of HLA-A alleles. But only 11 common HLA-A alleles are considered core CC alleles, representing all functionally significant variation CC (polymorphism) in alpha-1 and alpha-2 domains. These are: A*01:01; CC A*02:01; A*02:05; A*03:01; A*11:01; A*24:02; A*26:01; A*29:02; A*30:01; CC A*74:01 and A*80:01. Among these, A*02:01; A*11:01; A*24:02 and CC A*26:01, were likely passed by introgression from archaic to modern CC humans. Functional alleles of more recent origin (non-core) were CC derived by recombination (PubMed:28650991). The sequence shown is that CC of A*03:01. The sequences of core alleles and common representative CC alleles of serologically distinct allele groups are described as CC variants of A*03:01 (PubMed:28650991). Allelic variations of HLA-A CC signal peptide regulate HLA-E recognition by KLRD1-KLRC1 and KLRD1- CC KLRC2 receptors in viral infection and tumorigenesis by affecting its CC processing and by changing the affinity of HLA-E-VL9 complex for KLRD1- CC KLRC1 and KLRD1-KLRC2 receptors (PubMed:37264229). Allele A*31:01 is CC associated with carbamazepine-induced hypersensitivity reactions among CC subjects of Northern European ancestry [MIM:608579] (PubMed:21428769). CC {ECO:0000269|PubMed:21428769, ECO:0000269|PubMed:28650991, CC ECO:0000269|PubMed:37264229}. CC -!- DISEASE: Note=Alleles A*02:01 and A*24:02 are associated with increased CC susceptibility to diabetes mellitus, insulin-dependent (IDDM) CC (PubMed:22245737, PubMed:18802479, PubMed:16731854, PubMed:22522618). CC In a glucose-dependent way, allele A*02:01 may aberrantly present the CC signal peptide of preproinsulin (ALWGPDPAAA) on the surface of CC pancreatic beta cells to autoreactive CD8-positive T cells, potentially CC driving T-cell mediated cytotoxicity in pancreatic islets CC (PubMed:22245737, PubMed:18802479). Allele A*24:02 may present the CC signal peptide of preproinsulin (LWMRLLPLL) and contribute to acute CC pancreatic beta-cell destruction and early onset of IDDM CC (PubMed:16731854, PubMed:22522618). {ECO:0000269|PubMed:16731854, CC ECO:0000269|PubMed:18802479, ECO:0000269|PubMed:22245737, CC ECO:0000269|PubMed:22522618}. CC -!- DISEASE: Note=Allele A*03:01 is associated with increased CC susceptibility to multiple sclerosis (MS), an autoimmune disease of the CC central nervous system (PubMed:10746785). May contribute to the CC initiation phase of the disease by presenting myelin PLP1 self-peptide CC (KLIETYFSK) to autoreactive CD8-positive T cells capable of initiating CC the first autoimmune attacks (PubMed:18953350). CC {ECO:0000269|PubMed:10746785, ECO:0000269|PubMed:18953350}. CC -!- DISEASE: Note=Allele A*26:01 is associated with increased CC susceptibility to Behcet disease (BD) in the Northeast Asian CC population. Especially in the HLA-B*51-negative BD populations, HLA- CC A*26 is significantly associated with the onset of BD. CC {ECO:0000269|PubMed:30872678}. CC -!- DISEASE: Note=Allele A*29:02 is associated with increased CC susceptibility to birdshot chorioretinopathy (BSCR). May aberrantly CC present retinal autoantigens and induce autoimmune uveitis. CC {ECO:0000269|PubMed:1728143}. CC -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA25162.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305|PubMed:6609814}; 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; U03862; AAA03603.1; -; mRNA. DR EMBL; X13111; CAA31503.1; -; mRNA. DR EMBL; M23739; AAB47873.1; -; mRNA. DR EMBL; U83415; AAB53373.1; -; mRNA. DR EMBL; U83416; AAB53374.1; -; mRNA. DR EMBL; M30576; AAA59612.1; -; Genomic_DNA. DR EMBL; M30580; AAB47870.1; -; Genomic_DNA. DR EMBL; M24043; AAA59652.1; -; Genomic_DNA. DR EMBL; M84379; AAA59606.1; -; mRNA. DR EMBL; M32321; AAA36234.1; -; mRNA. DR EMBL; X60108; CAA42702.1; -; mRNA. DR EMBL; M64740; AAA59600.1; -; mRNA. DR EMBL; M64742; AAA03662.1; -; mRNA. DR EMBL; X61700; CAA43869.1; -; mRNA. DR EMBL; X61701; CAA43870.1; -; mRNA. DR EMBL; X61703; CAA43872.1; -; mRNA. DR EMBL; X61704; CAA43873.1; -; mRNA. DR EMBL; X61711; CAA43880.1; -; mRNA. DR EMBL; M84375; AAA59599.1; -; mRNA. DR EMBL; U03697; AAA03720.1; -; mRNA. DR EMBL; L18898; AAA17012.1; -; mRNA. DR EMBL; D14350; BAA03279.1; -; mRNA. DR EMBL; U03754; AAC04322.1; -; mRNA. DR EMBL; D16841; BAA04117.1; -; mRNA. DR EMBL; U07234; AAA70162.1; -; mRNA. DR EMBL; AY786587; AAV53345.1; -; mRNA. DR EMBL; X00492; CAA25162.1; ALT_SEQ; Genomic_DNA. DR EMBL; X03070; CAB56605.1; -; Genomic_DNA. DR EMBL; X03071; CAB56606.1; -; Genomic_DNA. DR EMBL; X03158; CAB56607.1; -; Genomic_DNA. DR EMBL; X03159; CAB56608.1; -; Genomic_DNA. DR EMBL; K02883; AAA98727.1; -; Genomic_DNA. DR EMBL; AH003070; AAA65449.1; -; Genomic_DNA. DR EMBL; X55710; CAA39243.1; -; Genomic_DNA. DR EMBL; U02935; AAA76608.2; -; Genomic_DNA. DR EMBL; L78918; AAB05976.1; -; Genomic_DNA. DR EMBL; Z72422; CAA96532.1; -; Genomic_DNA. DR EMBL; Z93949; CAB07989.1; -; Genomic_DNA. DR EMBL; EU445484; ACA35004.1; -; Genomic_DNA. DR EMBL; U03907; AAA03605.1; -; mRNA. DR EMBL; U17569; AAA56779.1; -; mRNA. DR EMBL; U17570; AAA56780.1; -; mRNA. DR EMBL; U32184; AAB63980.1; -; mRNA. DR EMBL; AJ748743; CAG38621.1; -; Genomic_DNA. DR EMBL; BC003069; AAH03069.1; -; mRNA. DR EMBL; BC008611; AAH08611.1; -; mRNA. DR EMBL; AL671277; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS34373.1; -. [P04439-1] DR RefSeq; NP_001229687.1; NM_001242758.1. DR RefSeq; NP_002107.3; NM_002116.7. [P04439-1] DR PDB; 1AKJ; X-ray; 2.65 A; A=25-300. DR PDB; 1AO7; X-ray; 2.60 A; A=25-299. DR PDB; 1AQD; X-ray; 2.45 A; C/F/I/L=127-141. DR PDB; 1B0G; X-ray; 2.50 A; A/D=25-299. DR PDB; 1B0R; X-ray; 2.90 A; A=25-299. DR PDB; 1BD2; X-ray; 2.50 A; A=25-299. DR PDB; 1DUY; X-ray; 2.15 A; A/D=25-299. DR PDB; 1DUZ; X-ray; 1.80 A; A/D=25-299. DR PDB; 1EEY; X-ray; 2.25 A; A/D=25-299. DR PDB; 1EEZ; X-ray; 2.30 A; A/D=25-299. DR PDB; 1HHG; X-ray; 2.60 A; A/D=25-299. DR PDB; 1HHH; X-ray; 3.00 A; A=25-299. DR PDB; 1HHI; X-ray; 2.50 A; A/D=25-299. DR PDB; 1HHJ; X-ray; 2.50 A; A/D=25-299. DR PDB; 1HHK; X-ray; 2.50 A; A/D=25-299. DR PDB; 1HLA; X-ray; 3.50 A; A=25-294. DR PDB; 1HSB; X-ray; 1.90 A; A=25-294. DR PDB; 1I1F; X-ray; 2.80 A; A/D=25-299. DR PDB; 1I1Y; X-ray; 2.20 A; A/D=25-299. DR PDB; 1I4F; X-ray; 1.40 A; A=25-299. DR PDB; 1I7R; X-ray; 2.20 A; A/D=25-299. DR PDB; 1I7T; X-ray; 2.80 A; A/D=25-299. DR PDB; 1I7U; X-ray; 1.80 A; A/D=25-299. DR PDB; 1IM3; X-ray; 2.20 A; A/E/I/M=25-299. DR PDB; 1JF1; X-ray; 1.85 A; A=25-299. DR PDB; 1JHT; X-ray; 2.15 A; A=25-299. DR PDB; 1LP9; X-ray; 2.00 A; A/H=25-299. DR PDB; 1OGA; X-ray; 1.40 A; A=25-300. DR PDB; 1P7Q; X-ray; 3.40 A; A=25-300. DR PDB; 1Q94; X-ray; 2.40 A; A/D=25-299. DR PDB; 1QEW; X-ray; 2.20 A; A=25-299. DR PDB; 1QR1; X-ray; 2.40 A; A/D=25-299. DR PDB; 1QRN; X-ray; 2.80 A; A=25-298. DR PDB; 1QSE; X-ray; 2.80 A; A=25-298. DR PDB; 1QSF; X-ray; 2.80 A; A=25-298. DR PDB; 1QVO; X-ray; 2.22 A; A/D=25-299. DR PDB; 1S8D; X-ray; 2.20 A; A=25-299. DR PDB; 1S9W; X-ray; 2.20 A; A=25-298. DR PDB; 1S9X; X-ray; 2.50 A; A=25-298. DR PDB; 1S9Y; X-ray; 2.30 A; A=25-298. DR PDB; 1T1W; X-ray; 2.20 A; A=25-299. DR PDB; 1T1X; X-ray; 2.20 A; A=25-299. DR PDB; 1T1Y; X-ray; 2.00 A; A=25-299. DR PDB; 1T1Z; X-ray; 1.90 A; A=25-299. DR PDB; 1T20; X-ray; 2.20 A; A=25-299. DR PDB; 1T21; X-ray; 2.19 A; A=25-299. DR PDB; 1T22; X-ray; 2.20 A; A=25-299. DR PDB; 1TMC; X-ray; 2.30 A; A=25-199. DR PDB; 1TVB; X-ray; 1.80 A; A/D=25-299. DR PDB; 1TVH; X-ray; 1.80 A; A/D=25-299. DR PDB; 1W72; X-ray; 2.15 A; A/D=25-298. DR PDB; 1X7Q; X-ray; 1.45 A; A=25-299. DR PDB; 2AV1; X-ray; 1.95 A; A/D=25-299. DR PDB; 2AV7; X-ray; 2.05 A; A/D=25-299. DR PDB; 2BCK; X-ray; 2.80 A; A/D=25-300. DR PDB; 2BNQ; X-ray; 1.70 A; A=25-300. DR PDB; 2BNR; X-ray; 1.90 A; A=25-300. DR PDB; 2C7U; X-ray; 2.38 A; A/D=25-300. DR PDB; 2CLR; X-ray; 2.00 A; A/D=25-299. DR PDB; 2F53; X-ray; 2.10 A; A=25-299. DR PDB; 2F54; X-ray; 2.70 A; A/F=25-298. DR PDB; 2GIT; X-ray; 1.70 A; A/D=25-299. DR PDB; 2GJ6; X-ray; 2.56 A; A=25-299. DR PDB; 2GT9; X-ray; 1.75 A; A/D=25-299. DR PDB; 2GTW; X-ray; 1.55 A; A/D=25-299. DR PDB; 2GTZ; X-ray; 1.70 A; A/D=25-299. DR PDB; 2GUO; X-ray; 1.90 A; A/D=25-299. DR PDB; 2HLA; X-ray; 2.60 A; A=25-294. DR PDB; 2HN7; X-ray; 1.60 A; A=25-299. DR PDB; 2J8U; X-ray; 2.88 A; A/H=25-299. DR PDB; 2JCC; X-ray; 2.50 A; A/H=25-299. DR PDB; 2P5E; X-ray; 1.89 A; A=25-300. DR PDB; 2P5W; X-ray; 2.20 A; A=25-300. DR PDB; 2PYE; X-ray; 2.30 A; A=25-300. DR PDB; 2UWE; X-ray; 2.40 A; A/H=25-299. DR PDB; 2V2W; X-ray; 1.60 A; A/D=25-300. DR PDB; 2V2X; X-ray; 1.60 A; A/D=25-300. DR PDB; 2VLJ; X-ray; 2.40 A; A=25-300. DR PDB; 2VLK; X-ray; 2.50 A; A=25-300. DR PDB; 2VLL; X-ray; 1.60 A; A/D=25-300. DR PDB; 2VLR; X-ray; 2.30 A; A/F=25-300. DR PDB; 2X4N; X-ray; 2.34 A; A/D=25-299. DR PDB; 2X4O; X-ray; 2.30 A; A/D=25-299. DR PDB; 2X4P; X-ray; 2.30 A; A/D=25-299. DR PDB; 2X4Q; X-ray; 1.90 A; A/D=25-299. DR PDB; 2X4R; X-ray; 2.30 A; A/D=25-299. DR PDB; 2X4S; X-ray; 2.55 A; A/D=25-299. DR PDB; 2X4T; X-ray; 2.30 A; A/D=25-299. DR PDB; 2X4U; X-ray; 2.10 A; A/D=25-299. DR PDB; 2X70; X-ray; 2.00 A; A/D=25-299. DR PDB; 2XPG; X-ray; 2.60 A; A=25-298. DR PDB; 3BGM; X-ray; 1.60 A; A=25-298. DR PDB; 3BH8; X-ray; 1.65 A; A=25-298. DR PDB; 3BH9; X-ray; 1.70 A; A=25-299. DR PDB; 3BHB; X-ray; 2.20 A; A=25-298. DR PDB; 3BO8; X-ray; 1.80 A; A=25-298. DR PDB; 3D25; X-ray; 1.30 A; A=25-298. DR PDB; 3D39; X-ray; 2.81 A; A=25-299. DR PDB; 3D3V; X-ray; 2.80 A; A=25-299. DR PDB; 3FQN; X-ray; 1.65 A; A=25-299. DR PDB; 3FQR; X-ray; 1.70 A; A=25-299. DR PDB; 3FQT; X-ray; 1.80 A; A=25-299. DR PDB; 3FQU; X-ray; 1.80 A; A=25-299. DR PDB; 3FQW; X-ray; 1.93 A; A=25-299. DR PDB; 3FQX; X-ray; 1.70 A; A=25-299. DR PDB; 3FT2; X-ray; 1.80 A; A=25-299. DR PDB; 3FT3; X-ray; 1.95 A; A=25-299. DR PDB; 3FT4; X-ray; 1.90 A; A=25-299. DR PDB; 3GIV; X-ray; 2.00 A; A/D=25-299. DR PDB; 3GJF; X-ray; 1.90 A; A/D=25-300. DR PDB; 3GSN; X-ray; 2.80 A; H=25-298. DR PDB; 3GSO; X-ray; 1.60 A; A=25-298. DR PDB; 3GSQ; X-ray; 2.12 A; A=25-298. DR PDB; 3GSR; X-ray; 1.95 A; A=25-298. DR PDB; 3GSU; X-ray; 1.80 A; A=25-299. DR PDB; 3GSV; X-ray; 1.90 A; A=25-299. DR PDB; 3GSW; X-ray; 1.81 A; A=25-298. DR PDB; 3GSX; X-ray; 2.10 A; A=25-298. DR PDB; 3H7B; X-ray; 1.88 A; A/D=25-299. DR PDB; 3H9H; X-ray; 2.00 A; A/D=25-299. DR PDB; 3H9S; X-ray; 2.70 A; A=25-299. DR PDB; 3HAE; X-ray; 2.90 A; A/D/J/P=25-300. DR PDB; 3HLA; X-ray; 2.60 A; A=25-294. DR PDB; 3HPJ; X-ray; 2.00 A; A/D=25-299. DR PDB; 3I6G; X-ray; 2.20 A; A/D=25-299. DR PDB; 3I6K; X-ray; 2.80 A; A/E=25-299. DR PDB; 3I6L; X-ray; 2.40 A; D=25-298. DR PDB; 3IXA; X-ray; 2.10 A; A/D=25-299. DR PDB; 3KLA; X-ray; 1.65 A; A/D=25-299. DR PDB; 3MGO; X-ray; 2.30 A; A/D/G/J=25-299. DR PDB; 3MGT; X-ray; 2.20 A; A/D/G/J=25-299. DR PDB; 3MR9; X-ray; 1.93 A; A=25-300. DR PDB; 3MRB; X-ray; 1.40 A; A=25-300. DR PDB; 3MRC; X-ray; 1.80 A; A=25-300. DR PDB; 3MRD; X-ray; 1.70 A; A=25-300. DR PDB; 3MRE; X-ray; 1.10 A; A=25-300. DR PDB; 3MRF; X-ray; 2.30 A; A=25-300. DR PDB; 3MRG; X-ray; 1.30 A; A=25-300. DR PDB; 3MRH; X-ray; 2.40 A; A=25-300. DR PDB; 3MRI; X-ray; 2.10 A; A=25-300. DR PDB; 3MRJ; X-ray; 1.87 A; A=25-300. DR PDB; 3MRK; X-ray; 1.40 A; A=25-300. DR PDB; 3MRL; X-ray; 2.41 A; A=25-300. DR PDB; 3MRM; X-ray; 1.90 A; A=25-300. DR PDB; 3MRN; X-ray; 2.30 A; A=25-300. DR PDB; 3MRO; X-ray; 2.35 A; A=25-300. DR PDB; 3MRP; X-ray; 2.10 A; A=25-300. DR PDB; 3MRQ; X-ray; 2.20 A; A=25-300. DR PDB; 3MRR; X-ray; 1.60 A; A=25-300. DR PDB; 3MYJ; X-ray; 1.89 A; A/D=25-299. DR PDB; 3NFN; X-ray; 2.39 A; A=25-298. DR PDB; 3O3A; X-ray; 1.80 A; A/D=25-299. DR PDB; 3O3B; X-ray; 1.90 A; A/D=25-299. DR PDB; 3O3D; X-ray; 1.70 A; A/D=25-299. DR PDB; 3O3E; X-ray; 1.85 A; A/D=25-299. DR PDB; 3O4L; X-ray; 2.54 A; A=25-300. DR PDB; 3PWJ; X-ray; 1.70 A; A/D=25-299. DR PDB; 3PWL; X-ray; 1.65 A; A/D=25-299. DR PDB; 3PWN; X-ray; 1.60 A; A/D=25-299. DR PDB; 3PWP; X-ray; 2.69 A; A=25-299. DR PDB; 3QDG; X-ray; 2.69 A; A=25-299. DR PDB; 3QDJ; X-ray; 2.30 A; A=25-299. DR PDB; 3QDM; X-ray; 2.80 A; A=25-299. DR PDB; 3QEQ; X-ray; 2.59 A; A=25-299. DR PDB; 3QFD; X-ray; 1.68 A; A/D=25-299. DR PDB; 3QFJ; X-ray; 2.29 A; A=25-299. DR PDB; 3QZW; X-ray; 2.80 A; A/D=25-298. DR PDB; 3REW; X-ray; 1.90 A; A/D=25-299. DR PDB; 3RL1; X-ray; 2.00 A; A=25-298. DR PDB; 3RL2; X-ray; 2.39 A; A=25-298. DR PDB; 3TO2; X-ray; 2.60 A; A=25-299. DR PDB; 3UTQ; X-ray; 1.67 A; A=25-300. DR PDB; 3UTS; X-ray; 2.71 A; A/F=25-300. DR PDB; 3UTT; X-ray; 2.60 A; A/F=25-299. DR PDB; 3V5D; X-ray; 2.00 A; A/D=25-299. DR PDB; 3V5H; X-ray; 1.63 A; A/D=25-299. DR PDB; 3V5K; X-ray; 2.31 A; A/D=25-299. DR PDB; 3VXM; X-ray; 2.50 A; A=25-298. DR PDB; 3VXN; X-ray; 1.95 A; A=25-298. DR PDB; 3VXO; X-ray; 2.61 A; A/D=25-298. DR PDB; 3VXP; X-ray; 2.50 A; A/D=25-298. DR PDB; 3VXR; X-ray; 2.40 A; A=25-298. DR PDB; 3VXS; X-ray; 1.80 A; A=25-298. DR PDB; 3VXU; X-ray; 2.70 A; A/F=25-298. DR PDB; 3W0W; X-ray; 2.60 A; A=25-298. DR PDB; 3WL9; X-ray; 1.66 A; A=25-298. DR PDB; 3WLB; X-ray; 2.00 A; A=25-298. DR PDB; 4E5X; X-ray; 1.95 A; A/D=25-299. DR PDB; 4EMZ; X-ray; 2.90 A; D/E=338-365. DR PDB; 4EN2; X-ray; 2.58 A; D/E=338-365. DR PDB; 4EUP; X-ray; 2.88 A; A/D=25-299. DR PDB; 4F7M; X-ray; 2.40 A; A/D=25-298. DR PDB; 4F7P; X-ray; 1.90 A; A=25-298. DR PDB; 4F7T; X-ray; 1.70 A; A/D=25-298. DR PDB; 4FTV; X-ray; 2.74 A; A=25-299. DR PDB; 4GKN; X-ray; 2.75 A; A/D=25-300. DR PDB; 4GKS; X-ray; 2.35 A; A/D=25-300. DR PDB; 4HWZ; X-ray; 2.40 A; A=25-298. DR PDB; 4HX1; X-ray; 1.80 A; A=25-296. DR PDB; 4I48; X-ray; 2.80 A; A=25-296. DR PDB; 4I4W; X-ray; 1.77 A; A=25-300. DR PDB; 4JFD; X-ray; 2.46 A; A=25-300. DR PDB; 4JFE; X-ray; 2.70 A; A=25-300. DR PDB; 4JFF; X-ray; 2.43 A; A=25-300. DR PDB; 4JFO; X-ray; 2.11 A; A/D=25-299. DR PDB; 4JFP; X-ray; 1.91 A; A/D=25-300. DR PDB; 4JFQ; X-ray; 1.90 A; A/D=25-300. DR PDB; 4K7F; X-ray; 2.00 A; A/D=25-299. DR PDB; 4L29; X-ray; 3.09 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y/a=25-300. DR PDB; 4L3C; X-ray; 2.64 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y/a=25-300. DR PDB; 4L3E; X-ray; 2.56 A; A=25-299. DR PDB; 4MJ5; X-ray; 2.40 A; A=25-298. DR PDB; 4MJ6; X-ray; 2.57 A; A=25-298. DR PDB; 4MNQ; X-ray; 2.74 A; A=25-300. DR PDB; 4N8V; X-ray; 2.50 A; A/D=25-298. DR PDB; 4NNX; X-ray; 2.10 A; A=25-298. DR PDB; 4NNY; X-ray; 1.90 A; A=25-298. DR PDB; 4NO0; X-ray; 2.70 A; A=25-300. DR PDB; 4NO2; X-ray; 2.00 A; A=25-298. DR PDB; 4NO3; X-ray; 1.70 A; A=25-298. DR PDB; 4NO5; X-ray; 2.10 A; A=25-299. DR PDB; 4NQV; X-ray; 2.39 A; A/C/E/G/I/K=25-298. DR PDB; 4NQX; X-ray; 2.00 A; A/C/E/G/I/K=25-308. DR PDB; 4OV5; X-ray; 2.20 A; C/F/I/L/O/R=128-141. DR PDB; 4QOK; X-ray; 3.00 A; A=25-300. DR PDB; 4U6X; X-ray; 1.68 A; A=25-300. DR PDB; 4U6Y; X-ray; 1.47 A; A=25-300. DR PDB; 4UQ2; X-ray; 2.43 A; A/C=25-299. DR PDB; 4UQ3; X-ray; 2.10 A; A/C=25-299. DR PDB; 4WJ5; X-ray; 1.65 A; A/D=25-299. DR PDB; 4WU5; X-ray; 2.40 A; A/D=25-298. DR PDB; 4WU7; X-ray; 2.30 A; A/D=25-298. DR PDB; 4WUU; X-ray; 3.05 A; A=25-300. DR PDB; 5BRZ; X-ray; 2.62 A; A=25-298. DR PDB; 5BS0; X-ray; 2.40 A; A=25-298. DR PDB; 5C07; X-ray; 2.11 A; A/F=25-300. DR PDB; 5C08; X-ray; 2.33 A; A/F=25-300. DR PDB; 5C09; X-ray; 2.48 A; A/F=25-300. DR PDB; 5C0A; X-ray; 2.46 A; A/F=25-300. DR PDB; 5C0B; X-ray; 2.03 A; A/F=25-299. DR PDB; 5C0C; X-ray; 1.97 A; A/F=25-300. DR PDB; 5C0D; X-ray; 1.68 A; A=25-300. DR PDB; 5C0E; X-ray; 1.49 A; A=25-300. DR PDB; 5C0F; X-ray; 1.46 A; A=25-300. DR PDB; 5C0G; X-ray; 1.37 A; A=25-300. DR PDB; 5C0I; X-ray; 1.53 A; A=25-300. DR PDB; 5C0J; X-ray; 1.64 A; A=25-300. DR PDB; 5D2L; X-ray; 3.51 A; A/C/G/M=25-299. DR PDB; 5D2N; X-ray; 2.10 A; A/H=25-299. DR PDB; 5D9S; X-ray; 1.87 A; A=25-298. DR PDB; 5DDH; X-ray; 1.50 A; A=25-298. DR PDB; 5E00; X-ray; 1.70 A; A=25-299. DR PDB; 5E6I; X-ray; 4.00 A; C/I/M/R=25-299. DR PDB; 5E9D; X-ray; 2.51 A; A/F=25-299. DR PDB; 5ENW; X-ray; 1.85 A; A=25-298. DR PDB; 5EOT; X-ray; 2.10 A; A=26-298. DR PDB; 5EU3; X-ray; 1.97 A; A=25-300. DR PDB; 5EU4; X-ray; 2.12 A; A/D=25-300. DR PDB; 5EU5; X-ray; 1.54 A; A=25-300. DR PDB; 5EU6; X-ray; 2.02 A; A=25-300. DR PDB; 5EUO; X-ray; 2.10 A; A/C=25-299. DR PDB; 5F7D; X-ray; 2.30 A; A=26-298. DR PDB; 5F9J; X-ray; 2.51 A; A=25-298. DR PDB; 5FA3; X-ray; 1.86 A; A=26-298. DR PDB; 5FA4; X-ray; 2.40 A; A=25-298. DR PDB; 5FDW; X-ray; 2.70 A; A=25-298. DR PDB; 5GRD; X-ray; 1.80 A; A=25-299. DR PDB; 5GRG; X-ray; 1.94 A; A=25-299. DR PDB; 5GSD; X-ray; 2.30 A; A=25-299. DR PDB; 5HGA; X-ray; 2.20 A; A/D=25-298. DR PDB; 5HGB; X-ray; 2.40 A; A/D/G/J=25-298. DR PDB; 5HGD; X-ray; 2.07 A; A/D=25-298. DR PDB; 5HGH; X-ray; 2.39 A; A=25-298. DR PDB; 5HHM; X-ray; 2.50 A; A/F=25-300. DR PDB; 5HHN; X-ray; 2.03 A; A=25-298. DR PDB; 5HHO; X-ray; 2.95 A; A=25-300. DR PDB; 5HHP; X-ray; 1.90 A; A=25-298. DR PDB; 5HHQ; X-ray; 2.10 A; A=25-298. DR PDB; 5HYJ; X-ray; 3.06 A; A/F=25-300. DR PDB; 5IRO; X-ray; 2.64 A; A/E/I/M/Q/U=25-299. DR PDB; 5ISZ; X-ray; 2.06 A; A=25-299. DR PDB; 5JHD; X-ray; 2.46 A; A/F=25-299. DR PDB; 5JZI; X-ray; 2.50 A; A/F=25-299. DR PDB; 5MEN; X-ray; 2.81 A; A=25-300. DR PDB; 5MEO; X-ray; 1.77 A; A=25-300. DR PDB; 5MEP; X-ray; 2.71 A; A/D=25-300. DR PDB; 5MEQ; X-ray; 2.27 A; A=25-300. DR PDB; 5MER; X-ray; 1.88 A; A/D=25-300. DR PDB; 5N1Y; X-ray; 1.39 A; A=25-300. DR PDB; 5N6B; X-ray; 1.71 A; A/D=25-300. DR PDB; 5NHT; X-ray; 3.20 A; H=25-300. DR PDB; 5NME; X-ray; 2.94 A; A/F=25-300. DR PDB; 5NMF; X-ray; 2.89 A; A/F=25-300. DR PDB; 5NMG; X-ray; 2.75 A; A/F=25-300. DR PDB; 5NMH; X-ray; 1.55 A; A=25-300. DR PDB; 5NMK; X-ray; 1.66 A; A=25-300. DR PDB; 5NQK; X-ray; 3.25 A; H=25-300. DR PDB; 5SWQ; X-ray; 2.00 A; A=25-300. DR PDB; 5TEZ; X-ray; 1.70 A; A=25-299. DR PDB; 5W1W; X-ray; 3.10 A; C/H/M/R=3-11. DR PDB; 5WJL; X-ray; 3.15 A; A/D/G=25-298. DR PDB; 5WJN; X-ray; 2.85 A; A/D/G=25-298. DR PDB; 5WKF; X-ray; 2.95 A; A/F=25-298. DR PDB; 5WKH; X-ray; 3.20 A; A/F=25-298. DR PDB; 5WSH; X-ray; 2.00 A; A=25-299. DR PDB; 5WWI; X-ray; 3.19 A; A=25-298. DR PDB; 5WWJ; X-ray; 2.29 A; A/C=25-298. DR PDB; 5WWU; X-ray; 2.79 A; A=25-298. DR PDB; 5WXC; X-ray; 2.29 A; A/C=25-298. DR PDB; 5WXD; X-ray; 3.29 A; A=25-298. DR PDB; 5XOV; X-ray; 2.68 A; A/D=25-298. DR PDB; 5YXN; X-ray; 2.03 A; C=25-299. DR PDB; 5YXU; X-ray; 2.70 A; C/E=25-299. DR PDB; 6AM5; X-ray; 2.39 A; A=25-299. DR PDB; 6AMT; X-ray; 2.50 A; A/D=25-299. DR PDB; 6AMU; X-ray; 2.15 A; A=26-298. DR PDB; 6APN; X-ray; 2.22 A; A/B=26-301. DR PDB; 6AT9; X-ray; 2.95 A; A=25-304. DR PDB; 6D78; X-ray; 2.35 A; A=25-299. DR PDB; 6D7G; X-ray; 2.75 A; A=25-299. DR PDB; 6DKP; X-ray; 2.97 A; A=25-299. DR PDB; 6EI2; X-ray; 1.61 A; A=25-299. DR PDB; 6ENY; EM; 5.80 A; F=25-365. DR PDB; 6EQA; X-ray; 3.16 A; A=25-300. DR PDB; 6EQB; X-ray; 2.81 A; A=25-300. DR PDB; 6EWA; X-ray; 2.39 A; A/E=25-300. DR PDB; 6EWC; X-ray; 3.20 A; A/E=25-300. DR PDB; 6EWO; X-ray; 2.30 A; A/E=25-300. DR PDB; 6G3J; X-ray; 2.45 A; A/D=25-300. DR PDB; 6G3K; X-ray; 2.90 A; A/D=25-300. DR PDB; 6ID4; X-ray; 2.40 A; A/E=25-299. DR PDB; 6J1W; X-ray; 1.50 A; A=25-298. DR PDB; 6J29; X-ray; 1.60 A; A=25-298. DR PDB; 6J2A; X-ray; 1.40 A; A=25-298. DR PDB; 6JOZ; X-ray; 1.35 A; A=25-299. DR PDB; 6JP3; X-ray; 1.66 A; A=25-299. DR PDB; 6MPP; NMR; -; A=25-303. DR PDB; 6NCA; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=25-299. DR PDB; 6O9B; X-ray; 2.20 A; A=25-304. DR PDB; 6O9C; X-ray; 2.45 A; A=25-304. DR PDB; 6OPD; X-ray; 1.79 A; A=25-299. DR PDB; 6PBH; X-ray; 1.89 A; A=25-302. DR PDB; 6PTB; X-ray; 2.15 A; A/D=25-299. DR PDB; 6PTE; X-ray; 1.90 A; A/E/H/K=25-299. DR PDB; 6Q3K; X-ray; 1.50 A; A=24-299. DR PDB; 6Q3S; X-ray; 2.50 A; A=25-300. DR PDB; 6R2L; X-ray; 2.30 A; A=25-299. DR PDB; 6RP9; X-ray; 3.12 A; A/F=25-299. DR PDB; 6RPA; X-ray; 2.56 A; A=25-299. DR PDB; 6RPB; X-ray; 2.50 A; A/F/K/P=25-299. DR PDB; 6RSY; X-ray; 2.95 A; A/F=25-299. DR PDB; 6SS7; X-ray; 2.50 A; A/D=25-299. DR PDB; 6SS8; X-ray; 2.24 A; A/D=25-299. DR PDB; 6SS9; X-ray; 2.70 A; A/D=25-299. DR PDB; 6SSA; X-ray; 2.11 A; A/D/G/J=25-299. DR PDB; 7L1B; X-ray; 2.04 A; A=25-298. DR PDB; 7L1C; X-ray; 1.96 A; A=25-298. DR PDB; 7L1D; X-ray; 3.11 A; A=25-298. DR PDB; 7MLE; X-ray; 2.20 A; A=25-301. DR PDB; 7PHR; EM; 3.08 A; H=25-304. DR PDB; 7QPD; EM; 3.73 A; M=25-365. DR PDB; 7RK7; X-ray; 2.54 A; A=25-299. DR PDB; 7RM4; X-ray; 3.33 A; A/F/K/P=25-299. DR PDB; 7RRG; X-ray; 2.12 A; A=25-298. DR PDB; 7STF; EM; 3.14 A; A=25-304. DR PDB; 7UC5; X-ray; 1.95 A; A/D=25-301. DR PDB; 7UX3; EM; 9.60 A; Y=334-365. DR PDB; 8D4C; EM; 9.30 A; P/Y=334-365. DR PDB; 8D4D; EM; 9.60 A; P/Y=334-365. DR PDB; 8D4E; EM; 9.20 A; Y=334-365. DR PDB; 8D4F; EM; 9.80 A; P/Y=334-365. DR PDB; 8D4G; EM; 11.60 A; P/Y=334-365. DR PDB; 8D9R; EM; 20.00 A; 0/1/2/Y/y/z=334-365. DR PDB; 8D9S; EM; 20.00 A; 0/1/2/Y/y/z=334-365. DR PDB; 8D9T; EM; 20.00 A; 0/1/Y/x/y/z=334-365. DR PDB; 8D9U; EM; 20.00 A; 0/1/Y/x/y/z=334-365. DR PDB; 8D9V; EM; 9.40 A; P/Y=334-365. DR PDB; 8D9W; EM; 9.30 A; Y/j=334-365. DR PDB; 8DVG; X-ray; 2.59 A; A=25-304. DR PDBsum; 1AKJ; -. DR PDBsum; 1AO7; -. DR PDBsum; 1AQD; -. DR PDBsum; 1B0G; -. DR PDBsum; 1B0R; -. DR PDBsum; 1BD2; -. DR PDBsum; 1DUY; -. DR PDBsum; 1DUZ; -. DR PDBsum; 1EEY; -. DR PDBsum; 1EEZ; -. DR PDBsum; 1HHG; -. DR PDBsum; 1HHH; -. DR PDBsum; 1HHI; -. DR PDBsum; 1HHJ; -. DR PDBsum; 1HHK; -. DR PDBsum; 1HLA; -. DR PDBsum; 1HSB; -. DR PDBsum; 1I1F; -. DR PDBsum; 1I1Y; -. DR PDBsum; 1I4F; -. DR PDBsum; 1I7R; -. DR PDBsum; 1I7T; -. DR PDBsum; 1I7U; -. DR PDBsum; 1IM3; -. DR PDBsum; 1JF1; -. DR PDBsum; 1JHT; -. DR PDBsum; 1LP9; -. DR PDBsum; 1OGA; -. DR PDBsum; 1P7Q; -. DR PDBsum; 1Q94; -. DR PDBsum; 1QEW; -. DR PDBsum; 1QR1; -. DR PDBsum; 1QRN; -. DR PDBsum; 1QSE; -. DR PDBsum; 1QSF; -. DR PDBsum; 1QVO; -. DR PDBsum; 1S8D; -. DR PDBsum; 1S9W; -. DR PDBsum; 1S9X; -. DR PDBsum; 1S9Y; -. DR PDBsum; 1T1W; -. DR PDBsum; 1T1X; -. DR PDBsum; 1T1Y; -. DR PDBsum; 1T1Z; -. DR PDBsum; 1T20; -. DR PDBsum; 1T21; -. DR PDBsum; 1T22; -. DR PDBsum; 1TMC; -. DR PDBsum; 1TVB; -. DR PDBsum; 1TVH; -. DR PDBsum; 1W72; -. DR PDBsum; 1X7Q; -. DR PDBsum; 2AV1; -. DR PDBsum; 2AV7; -. DR PDBsum; 2BCK; -. DR PDBsum; 2BNQ; -. DR PDBsum; 2BNR; -. DR PDBsum; 2C7U; -. DR PDBsum; 2CLR; -. DR PDBsum; 2F53; -. DR PDBsum; 2F54; -. DR PDBsum; 2GIT; -. DR PDBsum; 2GJ6; -. DR PDBsum; 2GT9; -. DR PDBsum; 2GTW; -. DR PDBsum; 2GTZ; -. DR PDBsum; 2GUO; -. DR PDBsum; 2HLA; -. DR PDBsum; 2HN7; -. DR PDBsum; 2J8U; -. DR PDBsum; 2JCC; -. DR PDBsum; 2P5E; -. DR PDBsum; 2P5W; -. DR PDBsum; 2PYE; -. DR PDBsum; 2UWE; -. DR PDBsum; 2V2W; -. DR PDBsum; 2V2X; -. DR PDBsum; 2VLJ; -. DR PDBsum; 2VLK; -. DR PDBsum; 2VLL; -. DR PDBsum; 2VLR; -. DR PDBsum; 2X4N; -. DR PDBsum; 2X4O; -. DR PDBsum; 2X4P; -. DR PDBsum; 2X4Q; -. DR PDBsum; 2X4R; -. DR PDBsum; 2X4S; -. DR PDBsum; 2X4T; -. DR PDBsum; 2X4U; -. DR PDBsum; 2X70; -. DR PDBsum; 2XPG; -. DR PDBsum; 3BGM; -. DR PDBsum; 3BH8; -. DR PDBsum; 3BH9; -. DR PDBsum; 3BHB; -. DR PDBsum; 3BO8; -. DR PDBsum; 3D25; -. DR PDBsum; 3D39; -. DR PDBsum; 3D3V; -. DR PDBsum; 3FQN; -. DR PDBsum; 3FQR; -. DR PDBsum; 3FQT; -. DR PDBsum; 3FQU; -. DR PDBsum; 3FQW; -. DR PDBsum; 3FQX; -. DR PDBsum; 3FT2; -. DR PDBsum; 3FT3; -. DR PDBsum; 3FT4; -. DR PDBsum; 3GIV; -. DR PDBsum; 3GJF; -. DR PDBsum; 3GSN; -. DR PDBsum; 3GSO; -. DR PDBsum; 3GSQ; -. DR PDBsum; 3GSR; -. DR PDBsum; 3GSU; -. DR PDBsum; 3GSV; -. DR PDBsum; 3GSW; -. DR PDBsum; 3GSX; -. DR PDBsum; 3H7B; -. DR PDBsum; 3H9H; -. DR PDBsum; 3H9S; -. DR PDBsum; 3HAE; -. DR PDBsum; 3HLA; -. DR PDBsum; 3HPJ; -. DR PDBsum; 3I6G; -. DR PDBsum; 3I6K; -. DR PDBsum; 3I6L; -. DR PDBsum; 3IXA; -. DR PDBsum; 3KLA; -. DR PDBsum; 3MGO; -. DR PDBsum; 3MGT; -. DR PDBsum; 3MR9; -. DR PDBsum; 3MRB; -. DR PDBsum; 3MRC; -. DR PDBsum; 3MRD; -. DR PDBsum; 3MRE; -. DR PDBsum; 3MRF; -. DR PDBsum; 3MRG; -. DR PDBsum; 3MRH; -. DR PDBsum; 3MRI; -. DR PDBsum; 3MRJ; -. DR PDBsum; 3MRK; -. DR PDBsum; 3MRL; -. DR PDBsum; 3MRM; -. DR PDBsum; 3MRN; -. DR PDBsum; 3MRO; -. DR PDBsum; 3MRP; -. DR PDBsum; 3MRQ; -. DR PDBsum; 3MRR; -. DR PDBsum; 3MYJ; -. DR PDBsum; 3NFN; -. DR PDBsum; 3O3A; -. DR PDBsum; 3O3B; -. DR PDBsum; 3O3D; -. DR PDBsum; 3O3E; -. DR PDBsum; 3O4L; -. DR PDBsum; 3PWJ; -. DR PDBsum; 3PWL; -. DR PDBsum; 3PWN; -. DR PDBsum; 3PWP; -. DR PDBsum; 3QDG; -. DR PDBsum; 3QDJ; -. DR PDBsum; 3QDM; -. DR PDBsum; 3QEQ; -. DR PDBsum; 3QFD; -. DR PDBsum; 3QFJ; -. DR PDBsum; 3QZW; -. DR PDBsum; 3REW; -. DR PDBsum; 3RL1; -. DR PDBsum; 3RL2; -. DR PDBsum; 3TO2; -. DR PDBsum; 3UTQ; -. DR PDBsum; 3UTS; -. DR PDBsum; 3UTT; -. DR PDBsum; 3V5D; -. DR PDBsum; 3V5H; -. DR PDBsum; 3V5K; -. DR PDBsum; 3VXM; -. DR PDBsum; 3VXN; -. DR PDBsum; 3VXO; -. DR PDBsum; 3VXP; -. DR PDBsum; 3VXR; -. DR PDBsum; 3VXS; -. DR PDBsum; 3VXU; -. DR PDBsum; 3W0W; -. DR PDBsum; 3WL9; -. DR PDBsum; 3WLB; -. DR PDBsum; 4E5X; -. DR PDBsum; 4EMZ; -. DR PDBsum; 4EN2; -. DR PDBsum; 4EUP; -. DR PDBsum; 4F7M; -. DR PDBsum; 4F7P; -. DR PDBsum; 4F7T; -. DR PDBsum; 4FTV; -. DR PDBsum; 4GKN; -. DR PDBsum; 4GKS; -. DR PDBsum; 4HWZ; -. DR PDBsum; 4HX1; -. DR PDBsum; 4I48; -. DR PDBsum; 4I4W; -. DR PDBsum; 4JFD; -. DR PDBsum; 4JFE; -. DR PDBsum; 4JFF; -. DR PDBsum; 4JFO; -. DR PDBsum; 4JFP; -. DR PDBsum; 4JFQ; -. DR PDBsum; 4K7F; -. DR PDBsum; 4L29; -. DR PDBsum; 4L3C; -. DR PDBsum; 4L3E; -. DR PDBsum; 4MJ5; -. DR PDBsum; 4MJ6; -. DR PDBsum; 4MNQ; -. DR PDBsum; 4N8V; -. DR PDBsum; 4NNX; -. DR PDBsum; 4NNY; -. DR PDBsum; 4NO0; -. DR PDBsum; 4NO2; -. DR PDBsum; 4NO3; -. DR PDBsum; 4NO5; -. DR PDBsum; 4NQV; -. DR PDBsum; 4NQX; -. DR PDBsum; 4OV5; -. DR PDBsum; 4QOK; -. DR PDBsum; 4U6X; -. DR PDBsum; 4U6Y; -. DR PDBsum; 4UQ2; -. DR PDBsum; 4UQ3; -. DR PDBsum; 4WJ5; -. DR PDBsum; 4WU5; -. DR PDBsum; 4WU7; -. DR PDBsum; 4WUU; -. DR PDBsum; 5BRZ; -. DR PDBsum; 5BS0; -. DR PDBsum; 5C07; -. DR PDBsum; 5C08; -. DR PDBsum; 5C09; -. DR PDBsum; 5C0A; -. DR PDBsum; 5C0B; -. DR PDBsum; 5C0C; -. DR PDBsum; 5C0D; -. DR PDBsum; 5C0E; -. DR PDBsum; 5C0F; -. DR PDBsum; 5C0G; -. DR PDBsum; 5C0I; -. DR PDBsum; 5C0J; -. DR PDBsum; 5D2L; -. DR PDBsum; 5D2N; -. DR PDBsum; 5D9S; -. DR PDBsum; 5DDH; -. DR PDBsum; 5E00; -. DR PDBsum; 5E6I; -. DR PDBsum; 5E9D; -. DR PDBsum; 5ENW; -. DR PDBsum; 5EOT; -. DR PDBsum; 5EU3; -. DR PDBsum; 5EU4; -. DR PDBsum; 5EU5; -. DR PDBsum; 5EU6; -. DR PDBsum; 5EUO; -. DR PDBsum; 5F7D; -. DR PDBsum; 5F9J; -. DR PDBsum; 5FA3; -. DR PDBsum; 5FA4; -. DR PDBsum; 5FDW; -. DR PDBsum; 5GRD; -. DR PDBsum; 5GRG; -. DR PDBsum; 5GSD; -. DR PDBsum; 5HGA; -. DR PDBsum; 5HGB; -. DR PDBsum; 5HGD; -. DR PDBsum; 5HGH; -. DR PDBsum; 5HHM; -. DR PDBsum; 5HHN; -. DR PDBsum; 5HHO; -. DR PDBsum; 5HHP; -. DR PDBsum; 5HHQ; -. DR PDBsum; 5HYJ; -. DR PDBsum; 5IRO; -. DR PDBsum; 5ISZ; -. DR PDBsum; 5JHD; -. DR PDBsum; 5JZI; -. DR PDBsum; 5MEN; -. DR PDBsum; 5MEO; -. DR PDBsum; 5MEP; -. DR PDBsum; 5MEQ; -. DR PDBsum; 5MER; -. DR PDBsum; 5N1Y; -. DR PDBsum; 5N6B; -. DR PDBsum; 5NHT; -. DR PDBsum; 5NME; -. DR PDBsum; 5NMF; -. DR PDBsum; 5NMG; -. DR PDBsum; 5NMH; -. DR PDBsum; 5NMK; -. DR PDBsum; 5NQK; -. DR PDBsum; 5SWQ; -. DR PDBsum; 5TEZ; -. DR PDBsum; 5W1W; -. DR PDBsum; 5WJL; -. DR PDBsum; 5WJN; -. DR PDBsum; 5WKF; -. DR PDBsum; 5WKH; -. DR PDBsum; 5WSH; -. DR PDBsum; 5WWI; -. DR PDBsum; 5WWJ; -. DR PDBsum; 5WWU; -. DR PDBsum; 5WXC; -. DR PDBsum; 5WXD; -. DR PDBsum; 5XOV; -. DR PDBsum; 5YXN; -. DR PDBsum; 5YXU; -. DR PDBsum; 6AM5; -. DR PDBsum; 6AMT; -. DR PDBsum; 6AMU; -. DR PDBsum; 6APN; -. DR PDBsum; 6AT9; -. DR PDBsum; 6D78; -. DR PDBsum; 6D7G; -. DR PDBsum; 6DKP; -. DR PDBsum; 6EI2; -. DR PDBsum; 6ENY; -. DR PDBsum; 6EQA; -. DR PDBsum; 6EQB; -. DR PDBsum; 6EWA; -. DR PDBsum; 6EWC; -. DR PDBsum; 6EWO; -. DR PDBsum; 6G3J; -. DR PDBsum; 6G3K; -. DR PDBsum; 6ID4; -. DR PDBsum; 6J1W; -. DR PDBsum; 6J29; -. DR PDBsum; 6J2A; -. DR PDBsum; 6JOZ; -. DR PDBsum; 6JP3; -. DR PDBsum; 6MPP; -. DR PDBsum; 6NCA; -. DR PDBsum; 6O9B; -. DR PDBsum; 6O9C; -. DR PDBsum; 6OPD; -. DR PDBsum; 6PBH; -. DR PDBsum; 6PTB; -. DR PDBsum; 6PTE; -. DR PDBsum; 6Q3K; -. DR PDBsum; 6Q3S; -. DR PDBsum; 6R2L; -. DR PDBsum; 6RP9; -. DR PDBsum; 6RPA; -. DR PDBsum; 6RPB; -. DR PDBsum; 6RSY; -. DR PDBsum; 6SS7; -. DR PDBsum; 6SS8; -. DR PDBsum; 6SS9; -. DR PDBsum; 6SSA; -. DR PDBsum; 7L1B; -. DR PDBsum; 7L1C; -. DR PDBsum; 7L1D; -. DR PDBsum; 7MLE; -. DR PDBsum; 7PHR; -. DR PDBsum; 7QPD; -. DR PDBsum; 7RK7; -. DR PDBsum; 7RM4; -. DR PDBsum; 7RRG; -. DR PDBsum; 7STF; -. DR PDBsum; 7UC5; -. DR PDBsum; 7UX3; -. DR PDBsum; 8D4C; -. DR PDBsum; 8D4D; -. DR PDBsum; 8D4E; -. DR PDBsum; 8D4F; -. DR PDBsum; 8D4G; -. DR PDBsum; 8D9R; -. DR PDBsum; 8D9S; -. DR PDBsum; 8D9T; -. DR PDBsum; 8D9U; -. DR PDBsum; 8D9V; -. DR PDBsum; 8D9W; -. DR PDBsum; 8DVG; -. DR AlphaFoldDB; P04439; -. DR EMDB; EMD-13427; -. DR EMDB; EMD-14119; -. DR EMDB; EMD-25427; -. DR EMDB; EMD-28571; -. DR EMDB; EMD-28572; -. DR EMDB; EMD-3906; -. DR SMR; P04439; -. DR BioGRID; 109350; 395. DR IntAct; P04439; 171. DR MINT; P04439; -. DR STRING; 9606.ENSP00000379873; -. DR BindingDB; P04439; -. DR ChEMBL; CHEMBL2632; -. DR DrugBank; DB02740; 3-Indolebutyric Acid. DR DrugBank; DB11294; Coccidioides immitis spherule. DR DrugBank; DB06226; Nelipepimut-S. DR TCDB; 9.A.75.1.2; the mhc ii receptor (mhc2r) family. DR TCDB; 9.A.75.1.3; the mhc ii receptor (mhc2r) family. DR GlyConnect; 1315; 3 N-Linked glycans (1 site). DR GlyConnect; 1316; 3 N-Linked glycans (1 site). DR GlyConnect; 1317; 4 N-Linked glycans (1 site). DR GlyConnect; 1318; 1 N-Linked glycan (1 site). DR GlyConnect; 1319; 3 N-Linked glycans (1 site). DR GlyConnect; 1320; 3 N-Linked glycans (1 site). DR GlyConnect; 1321; 1 N-Linked glycan (1 site). DR GlyConnect; 1322; 1 N-Linked glycan (1 site). DR GlyConnect; 1323; 4 N-Linked glycans (1 site). DR GlyConnect; 1324; 3 N-Linked glycans (1 site). DR GlyConnect; 1325; 4 N-Linked glycans (1 site). DR GlyConnect; 1326; 4 N-Linked glycans (1 site). DR GlyConnect; 1327; 1 N-Linked glycan (1 site). DR GlyConnect; 1328; 3 N-Linked glycans (1 site). DR GlyConnect; 1329; 1 N-Linked glycan (1 site). DR GlyCosmos; P04439; 2 sites, 3 glycans. DR GlyGen; P04439; 2 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; P04439; -. DR PhosphoSitePlus; P04439; -. DR SwissPalm; P04439; -. DR BioMuta; HLA-A; -. DR DMDM; 13124681; -. DR EPD; P04439; -. DR jPOST; P04439; -. DR MassIVE; P04439; -. DR MaxQB; P04439; -. DR PaxDb; 9606-ENSP00000379873; -. DR PeptideAtlas; P04439; -. DR ProteomicsDB; 51505; -. DR ProteomicsDB; 51506; -. DR ProteomicsDB; 51714; -. DR ProteomicsDB; 51843; -. DR ProteomicsDB; 52596; -. DR ProteomicsDB; 52597; -. DR ProteomicsDB; 52979; -. DR ProteomicsDB; 52980; -. DR ProteomicsDB; 53320; -. DR ProteomicsDB; 53321; -. DR ProteomicsDB; 53322; -. DR ProteomicsDB; 53564; -. DR ProteomicsDB; 54669; -. DR ProteomicsDB; 54670; -. DR ProteomicsDB; 54671; -. DR ProteomicsDB; 54672; -. DR ProteomicsDB; 54673; -. DR ProteomicsDB; 54674; -. DR ProteomicsDB; 54675; -. DR ProteomicsDB; 54676; -. DR ProteomicsDB; 54707; -. DR ProteomicsDB; 58716; -. DR Pumba; P04439; -. DR ABCD; P04439; 62 sequenced antibodies. DR Antibodypedia; 26136; 1459 antibodies from 32 providers. DR CPTC; P04439; 1 antibody. DR DNASU; 3105; -. DR Ensembl; ENST00000376809.10; ENSP00000366005.5; ENSG00000206503.14. [P04439-1] DR Ensembl; ENST00000396634.5; ENSP00000379873.1; ENSG00000206503.14. [P04439-1] DR Ensembl; ENST00000706901.1; ENSP00000516612.1; ENSG00000206503.14. [P04439-1] DR Ensembl; ENST00000706903.1; ENSP00000516614.1; ENSG00000206503.14. [P04439-1] DR Ensembl; ENST00000706905.1; ENSP00000516616.1; ENSG00000206503.14. [P04439-1] DR GeneID; 3105; -. DR KEGG; hsa:3105; -. DR MANE-Select; ENST00000376809.10; ENSP00000366005.5; NM_002116.8; NP_002107.3. DR UCSC; uc021zos.2; human. DR AGR; HGNC:4931; -. DR CTD; 3105; -. DR DisGeNET; 3105; -. DR GeneCards; HLA-A; -. DR HGNC; HGNC:4931; HLA-A. DR HPA; ENSG00000206503; Low tissue specificity. DR MalaCards; HLA-A; -. DR MIM; 126200; phenotype. DR MIM; 142800; gene. DR MIM; 222100; phenotype. DR neXtProt; NX_P04439; -. DR OpenTargets; ENSG00000206503; -. DR Orphanet; 179; Birdshot chorioretinopathy. DR PharmGKB; PA35055; -. DR VEuPathDB; HostDB:ENSG00000206503; -. DR eggNOG; ENOG502RQEK; Eukaryota. DR GeneTree; ENSGT00980000198488; -. DR InParanoid; P04439; -. DR OMA; EGSCMEW; -. DR OrthoDB; 3840485at2759; -. DR PhylomeDB; P04439; -. DR TreeFam; TF336617; -. DR PathwayCommons; P04439; -. DR Reactome; R-HSA-1236974; ER-Phagosome pathway. DR Reactome; R-HSA-1236977; Endosomal/Vacuolar pathway. DR Reactome; R-HSA-164940; Nef mediated downregulation of MHC class I complex cell surface expression. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins. DR Reactome; R-HSA-909733; Interferon alpha/beta signaling. DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses. DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC. DR SignaLink; P04439; -. DR SIGNOR; P04439; -. DR BioGRID-ORCS; 3105; 27 hits in 1067 CRISPR screens. DR ChiTaRS; HLA-A; human. DR GeneWiki; HLA-A; -. DR GenomeRNAi; 3105; -. DR Pharos; P04439; Tclin. DR PRO; PR:P04439; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000206503; Expressed in blood and 104 other cell types or tissues. DR ExpressionAtlas; P04439; baseline and differential. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum 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; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0005797; C:Golgi medial cisterna; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0098553; C:lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0042824; C:MHC class I peptide loading complex; IDA:UniProtKB. DR GO; GO:0042612; C:MHC class I protein complex; IDA:UniProtKB. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome. DR GO; GO:0030881; F:beta-2-microglobulin binding; IDA:UniProtKB. DR GO; GO:0042610; F:CD8 receptor binding; IDA:UniProtKB. DR GO; GO:0042605; F:peptide antigen binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL. DR GO; GO:0042608; F:T cell receptor binding; IDA:UniProtKB. DR GO; GO:0046977; F:TAP binding; IDA:UniProtKB. DR GO; GO:0062061; F:TAP complex binding; IDA:UniProtKB. DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB. DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IDA:UniProtKB. DR GO; GO:0002485; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent; IMP:UniProtKB. DR GO; GO:0002486; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent; IDA:UniProtKB. DR GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; IBA:GO_Central. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; IDA:UniProtKB. DR GO; GO:0036037; P:CD8-positive, alpha-beta T cell activation; IDA:UniProtKB. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB. DR GO; GO:0016045; P:detection of bacterium; IMP:UniProtKB. DR GO; GO:0006955; P:immune response; IMP:UniProtKB. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0002502; P:peptide antigen assembly with MHC class I protein complex; IDA:UniProt. DR GO; GO:2001187; P:positive regulation of CD8-positive, alpha-beta T cell activation; IDA:BHF-UCL. DR GO; GO:2000566; P:positive regulation of CD8-positive, alpha-beta T cell proliferation; IDA:UniProtKB. DR GO; GO:2000568; P:positive regulation of memory T cell activation; IDA:UniProtKB. DR GO; GO:0002726; P:positive regulation of T cell cytokine production; IDA:BHF-UCL. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:UniProtKB. DR GO; GO:0032729; P:positive regulation of type II interferon production; IDA:UniProtKB. DR GO; GO:0042270; P:protection from natural killer cell mediated cytotoxicity; IDA:UniProtKB. DR GO; GO:0001913; P:T cell mediated cytotoxicity; IDA:UniProtKB. DR GO; GO:0002419; P:T cell mediated cytotoxicity directed against tumor cell target; IDA:UniProtKB. DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB. DR CDD; cd21026; IgC1_MHC_Ia_HLA-B; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 3.30.500.10; MHC class I-like antigen recognition-like; 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; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR037055; MHC_I-like_Ag-recog_sf. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR001039; MHC_I_a_a1/a2. DR InterPro; IPR010579; MHC_I_a_C. DR PANTHER; PTHR16675:SF229; HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A ALPHA CHAIN; 1. DR PANTHER; PTHR16675; MHC CLASS I-RELATED; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR SUPFAM; SSF54452; MHC antigen-recognition domain; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane; KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; KW Glycoprotein; Host-virus interaction; Immunity; Immunoglobulin domain; KW Innate immunity; Membrane; MHC I; Phosphoprotein; Reference proteome; KW Signal; Sulfation; Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1..24 FT /evidence="ECO:0000269|PubMed:92029" FT CHAIN 25..365 FT /note="HLA class I histocompatibility antigen, A alpha FT chain" FT /id="PRO_0000018815" FT TOPO_DOM 25..308 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 309..332 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 333..365 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 209..295 FT /note="Ig-like C1-type" FT /evidence="ECO:0000255" FT REGION 3..11 FT /note="VL9 epitope" FT /evidence="ECO:0000269|PubMed:37264229" FT REGION 25..114 FT /note="Alpha-1" FT /evidence="ECO:0000255" FT REGION 115..206 FT /note="Alpha-2" FT /evidence="ECO:0000255" FT REGION 207..298 FT /note="Alpha-3" FT /evidence="ECO:0000255" FT REGION 299..308 FT /note="Connecting peptide" FT /evidence="ECO:0000255" FT REGION 339..365 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 341..359 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 31 FT /ligand="a peptide antigen" FT /ligand_id="ChEBI:CHEBI:166823" FT /ligand_label="1" FT /ligand_note="pathogen-derived peptide antigen" FT /evidence="ECO:0000269|PubMed:21943705" FT BINDING 97 FT /ligand="a peptide antigen" FT /ligand_id="ChEBI:CHEBI:166823" FT /ligand_label="1" FT /ligand_note="pathogen-derived peptide antigen" FT /evidence="ECO:0000269|PubMed:21943705" FT BINDING 108 FT /ligand="a peptide antigen" FT /ligand_id="ChEBI:CHEBI:166823" FT /ligand_label="1" FT /ligand_note="pathogen-derived peptide antigen" FT /evidence="ECO:0000269|PubMed:21943705" FT BINDING 140 FT /ligand="a peptide antigen" FT /ligand_id="ChEBI:CHEBI:166823" FT /ligand_label="2" FT /ligand_note="self-peptide antigen" FT /evidence="ECO:0000269|PubMed:21543847" FT BINDING 167 FT /ligand="a peptide antigen" FT /ligand_id="ChEBI:CHEBI:166823" FT /ligand_label="1" FT /ligand_note="pathogen-derived peptide antigen" FT /evidence="ECO:0000269|PubMed:21943705" FT BINDING 170 FT /ligand="a peptide antigen" FT /ligand_id="ChEBI:CHEBI:166823" FT /ligand_label="1" FT /ligand_note="pathogen-derived peptide antigen" FT /evidence="ECO:0000269|PubMed:21943705" FT BINDING 183 FT /ligand="a peptide antigen" FT /ligand_id="ChEBI:CHEBI:166823" FT /ligand_label="1" FT /ligand_note="pathogen-derived peptide antigen" FT /evidence="ECO:0000269|PubMed:21943705" FT BINDING 183 FT /ligand="a peptide antigen" FT /ligand_id="ChEBI:CHEBI:166823" FT /ligand_label="2" FT /ligand_note="self-peptide antigen" FT /evidence="ECO:0000269|PubMed:21543847" FT BINDING 195 FT /ligand="a peptide antigen" FT /ligand_id="ChEBI:CHEBI:166823" FT /ligand_label="1" FT /ligand_note="pathogen-derived peptide antigen" FT /evidence="ECO:0000269|PubMed:21943705" FT MOD_RES 83 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 343 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 344 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 349 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 350 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 352 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 356 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 359 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT CARBOHYD 110 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT DISULFID 125..188 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:16041067, ECO:0000269|PubMed:19177349, FT ECO:0000269|PubMed:20844028, ECO:0000269|PubMed:21543847, FT ECO:0000269|PubMed:21943705, ECO:0000269|PubMed:26758806, FT ECO:0000269|PubMed:28250417, ECO:0000269|PubMed:7694806" FT DISULFID 227..283 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:16041067, ECO:0000269|PubMed:19177349, FT ECO:0000269|PubMed:20844028, ECO:0000269|PubMed:21543847, FT ECO:0000269|PubMed:21943705, ECO:0000269|PubMed:26758806, FT ECO:0000269|PubMed:28250417, ECO:0000269|PubMed:7694806" FT VAR_SEQ 176..187 FT /note="EAEQLRAYLDGT -> AAEQQRAYLEGR (in isoform 2)" FT /id="VSP_060391" FT VAR_SEQ 337 FT /note="S -> SGGEGVK (in isoform 2)" FT /id="VSP_060392" FT VARIANT 3 FT /note="V -> I (in allele A*34:01)" FT /evidence="ECO:0000269|PubMed:1431115" FT /id="VAR_082315" FT VARIANT 5 FT /note="A -> P (in allele A*80:01; does not alter the FT affinity of VL9 peptide for HLA-E or HLA-E expression at FT the plasma membrane; facilitates KLRD1-KLRC1 and FT KLRD1-KLRC2 receptor engagement and signaling)" FT /evidence="ECO:0000269|PubMed:37264229, FT ECO:0000269|PubMed:8188325, ECO:0000269|PubMed:8284791" FT /id="VAR_082316" FT VARIANT 10 FT /note="L -> V (in allele A*02:01, allele A*02:05, allele FT A*23:01, allele A*24:02, allele A*25:01, allele A*26:01, FT allele A*34:01, allele A*43:01, allele A*66:01, allele FT A*68:01 and allele A*69:01; does not alter the affinity of FT VL9 peptide for HLA-E or HLA-E expression at the plasma FT membrane; decreases KLRD1-KLRC1 and KLRD1-KLRC2 receptor FT engagement and signaling)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:1729171, ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393, FT ECO:0000269|PubMed:37264229, ECO:0000269|PubMed:3877632, FT ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:8026990, FT ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:9349616" FT /id="VAR_082317" FT VARIANT 14 FT /note="S -> L (in allele A*29:02, allele A*31:01, allele FT A*32:01, allele A*33:01 and allele A*74:01; impairs VL9 FT peptide processing and HLA-E expression at the plasma FT membrane)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566, FT ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623, FT ECO:0000269|PubMed:37264229, ECO:0000269|PubMed:8795145, FT ECO:0000269|Ref.29" FT /id="VAR_082318" FT VARIANT 23 FT /note="W -> R (in allele A*74:01)" FT /evidence="ECO:0000269|PubMed:1431115" FT /id="VAR_082319" FT VARIANT 33 FT /note="F -> S (in allele A*23:01, allele A*24:02 and allele FT A*30:01; dbSNP:rs2075684)" FT /evidence="ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:7871528, FT ECO:0000269|PubMed:9349616" FT /id="VAR_082320" FT VARIANT 33 FT /note="F -> T (in allele A*29:02, allele A*31:01 and allele FT A*33:01; requires 2 nucleotide substitutions)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2478623, FT ECO:0000269|PubMed:8795145" FT /id="VAR_082321" FT VARIANT 33 FT /note="F -> Y (in allele A*02:05, allele A*11:01, allele FT A*25:01, allele A*26:01, allele A*34:01, allele A*43:01, FT allele A*66:01, allele A*68:01 and allele A*69:01; FT dbSNP:rs2075684)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2437024, FT ECO:0000269|PubMed:2460344, ECO:0000269|PubMed:3496393, FT ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:8016845, FT ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8475492" FT /id="VAR_082322" FT VARIANT 41 FT /note="R -> S (in allele A*30:01; dbSNP:rs1059423)" FT /evidence="ECO:0000269|PubMed:2478623, FT ECO:0000269|PubMed:7871528" FT /id="VAR_082323" FT VARIANT 55 FT /note="T -> S (in allele A*80:01)" FT /evidence="ECO:0000269|PubMed:8188325, FT ECO:0000269|PubMed:8284791" FT /id="VAR_082324" FT VARIANT 59 FT /note="R -> Q (in allele A*80:01)" FT /evidence="ECO:0000269|PubMed:8188325, FT ECO:0000269|PubMed:8284791" FT /id="VAR_082325" FT VARIANT 67 FT /note="Q -> R (in allele A*02:05; dbSNP:rs41559117)" FT /evidence="ECO:0000269|PubMed:3496393" FT /id="VAR_082326" FT VARIANT 68 FT /note="R -> K (in alleles A*01:01 and allele A*36:01)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:9349617" FT /id="VAR_082327" FT VARIANT 80 FT /note="G -> E (in allele A*80:01)" FT /evidence="ECO:0000269|PubMed:8188325, FT ECO:0000269|PubMed:8284791" FT /id="VAR_082328" FT VARIANT 80 FT /note="G -> R (in allele A*30:01 and allele A*31:01; FT dbSNP:rs1059449)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:7871528, FT ECO:0000269|PubMed:8795145" FT /id="VAR_082329" FT VARIANT 86 FT /note="Q -> E (in allele A*23:01, allele 24:02 and allele FT A*80:01)" FT /evidence="ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:8188325, ECO:0000269|PubMed:8284791, FT ECO:0000269|PubMed:9349616" FT /id="VAR_082330" FT VARIANT 86 FT /note="Q -> G (in allele A*02:01 and allele A*02:05; FT requires 2 nucleotide substitutions)" FT /evidence="ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393, FT ECO:0000269|PubMed:7836067" FT /id="VAR_082331" FT VARIANT 86 FT /note="Q -> L (in alleles A*29:02 and allele A*43:01)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:1782566" FT /id="VAR_082332" FT VARIANT 86 FT /note="Q -> R (in allele A*25:01, allele A*26:01, allele FT A*33:01, allele A*34:01, allele A*66:01, allele A*68:01 and FT allele A*69:01)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2478623, FT ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:8026990, FT ECO:0000269|PubMed:8475492" FT /id="VAR_082333" FT VARIANT 87 FT /note="E -> N (in alleles A*25:01, allele A*26:01, allele FT A*33:01, allele A*34:01, allele A*66:01, allele A*68:01 and FT allele A*69:01; requires 2 nucleotide substitutions)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2478623, FT ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:8026990, FT ECO:0000269|PubMed:8475492" FT /id="VAR_082334" FT VARIANT 87 FT /note="E -> Q (in allele A*29:02 and allele A*43:01)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:1782566" FT /id="VAR_082335" FT VARIANT 89 FT /note="R -> G (in allele A*23:01 and allele 24:02; FT dbSNP:rs199474430)" FT /evidence="ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:9349616" FT /id="VAR_082336" FT VARIANT 90 FT /note="N -> K (in allele A*02:01, allele A*02:05, allele FT A*23:01, allele 24:02 and allele A*34:01; FT dbSNP:rs199474436)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:1729171, ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393, FT ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:9349616" FT /id="VAR_082337" FT VARIANT 91 FT /note="V -> M (in allele A*01:01 and allele A*36:01)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:9349617" FT /id="VAR_082338" FT VARIANT 94 FT /note="Q -> H (in allele A*01:01, allele A*02:01, allele FT A*02:05, allele A*23:01, allele 24:02, allele A*25:01, FT allele A*26:01, allele A*31:01, allele A*32:01, allele FT A*33:01, allele A*36:01, allele A*43:01, allele A*74:01 and FT allele A*80:01; dbSNP:rs78306866)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623, FT ECO:0000269|PubMed:2715640, ECO:0000269|PubMed:2982951, FT ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:7836067, FT ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8188325, FT ECO:0000269|PubMed:8284791, ECO:0000269|PubMed:8475492, FT ECO:0000269|PubMed:8795145, ECO:0000269|PubMed:9349616, FT ECO:0000269|PubMed:9349617, ECO:0000269|Ref.29" FT /id="VAR_082339" FT VARIANT 97 FT /note="T -> I (in allele A*31:01 and allele A*33:01; FT dbSNP:rs199474457)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:8795145" FT /id="VAR_082340" FT VARIANT 98 FT /note="D -> H (in allele A*02:01 and allele A*02:05)" FT /evidence="ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393, FT ECO:0000269|PubMed:7836067" FT /id="VAR_082341" FT VARIANT 98 FT /note="D -> N (in allele A*80:01)" FT /evidence="ECO:0000269|PubMed:8188325, FT ECO:0000269|PubMed:8284791" FT /id="VAR_082342" FT VARIANT 100 FT /note="V -> A (in allele A*01:01, allele A*26:01, allele FT A*29:02, allele A*36:01, allele A*43:01 and allele FT A*80:01)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2251137, FT ECO:0000269|PubMed:2715640, ECO:0000269|PubMed:8026990, FT ECO:0000269|PubMed:8188325, ECO:0000269|PubMed:8284791, FT ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:9349617" FT /id="VAR_082343" FT VARIANT 100 FT /note="V -> E (in allele A*23:01, allele A*24:02, allele FT A*25:01 and allele A*32:01; dbSNP:rs1071742)" FT /evidence="ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040, FT ECO:0000269|PubMed:9349616, ECO:0000269|Ref.29" FT /id="VAR_082344" FT VARIANT 101 FT /note="D -> N (allele A*01:01, allele A*23:01, allele FT A*24:02, allele A*26:01, allele A*29:02, allele A*36:01, FT allele A*43:01 and allele A*80:01; dbSNP:rs1136688)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:1729171, ECO:0000269|PubMed:1782566, FT ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8188325, FT ECO:0000269|PubMed:8284791, ECO:0000269|PubMed:8475492, FT ECO:0000269|PubMed:9349616, ECO:0000269|PubMed:9349617" FT /id="VAR_082345" FT VARIANT 101 FT /note="D -> S (in allele A*25:01 and allele A*32:01; FT requires 2 nucleotide substitutions)" FT /evidence="ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2431040, ECO:0000269|Ref.29" FT /id="VAR_082346" FT VARIANT 103..107 FT /note="GTLRG -> RIALR (in allele A*23:01, allele A*24:02, FT allele A*25:01 and allele A*32:01; Bw4 motif RIALR is FT involved in the recognition of NK cell inhibitory receptor FT KIR3DL1)" FT /evidence="ECO:0000269|PubMed:17182537, FT ECO:0000269|PubMed:1729171, ECO:0000269|PubMed:18502829, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040, FT ECO:0000269|PubMed:9349616, ECO:0000269|Ref.29" FT /id="VAR_082347" FT VARIANT 114 FT /note="A -> D (in allele A*01:01, allele A*11:01, allele FT A*25:01, allele A*26:01, allele A*34:01, allele A*36:01, FT allele A*43:01, allele A*66:01 and allele A*80:01; FT dbSNP:rs1136692)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2437024, ECO:0000269|PubMed:2460344, FT ECO:0000269|PubMed:2715640, ECO:0000269|PubMed:8016845, FT ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8188325, FT ECO:0000269|PubMed:8284791, ECO:0000269|PubMed:8475492, FT ECO:0000269|PubMed:9349617" FT /id="VAR_082348" FT VARIANT 119 FT /note="I -> L (in allele A*02:05, allele A*23:01 and allele FT 24:02; dbSNP:rs1071743)" FT /evidence="ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:9349616" FT /id="VAR_082349" FT VARIANT 119 FT /note="I -> V (in allele A*02:01 and allele A*69:01)" FT /evidence="ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3877632, FT ECO:0000269|PubMed:7836067" FT /id="VAR_082350" FT VARIANT 121 FT /note="I -> M (in allele A*23:01, allele 24:02, allele FT A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, FT allele A*68:01 and allele A*74:01; dbSNP:rs1136695)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2431040, FT ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:3877632, FT ECO:0000269|PubMed:8795145, ECO:0000269|PubMed:9349616, FT ECO:0000269|Ref.29" FT /id="VAR_082351" FT VARIANT 121 FT /note="I -> R (in allele A*02:01, allele A*02:05, allele FT A*25:01, allele A*26:01, allele A*34:01, allele A*43:01, FT allele A*66:01 and allele A*69:01)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2982951, FT ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632, FT ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:8026990, FT ECO:0000269|PubMed:8475492" FT /id="VAR_082352" FT VARIANT 123 FT /note="Y -> F (in allele A*23:01, allele 24:02; FT dbSNP:rs1136697)" FT /evidence="ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:9349616" FT /id="VAR_082353" FT VARIANT 129 FT /note="S -> P (in allele A*01:01, allele A*11:01, allele FT A*25:01, allele A*26:01, allele A*32:01, allele A*34:01, FT allele A*36:01, allele A*43:01, allele A*66:01 and allele FT A*74:01; dbSNP:rs1136700)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2437024, FT ECO:0000269|PubMed:2460344, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:8016845, ECO:0000269|PubMed:8026990, FT ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:9349617, FT ECO:0000269|Ref.29" FT /id="VAR_082354" FT VARIANT 131 FT /note="G -> W (in allele A*02:01, allele A*02:05 and allele FT A*69:01; dbSNP:rs1136702)" FT /evidence="ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393, FT ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:7836067" FT /id="VAR_082355" FT VARIANT 133 FT /note="F -> L (in allele A*32:01 and allele A*74:01; FT dbSNP:rs1059488)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:2431040, ECO:0000269|Ref.29" FT /id="VAR_082356" FT VARIANT 138 FT /note="R -> E (in allele A*30:01; requires 2 nucleotide FT substitutions)" FT /evidence="ECO:0000269|PubMed:2478623, FT ECO:0000269|PubMed:7871528" FT /id="VAR_082357" FT VARIANT 138 FT /note="R -> H (in allele A*02:01, allele A*02:05, allele FT A*23:01, allele A*24:02, allele A*69:01)" FT /evidence="ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2982951, FT ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632, FT ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:9349616" FT /id="VAR_082358" FT VARIANT 138 FT /note="R -> Q (in allele A*25:01, allele A*26:01, allele FT A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, FT allele A*43:01, allele A*66:01, allele A*74:01)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623, FT ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8475492, FT ECO:0000269|PubMed:8795145, ECO:0000269|Ref.29" FT /id="VAR_082359" FT VARIANT 140 FT /note="D -> H (in allele A*30:01)" FT /evidence="ECO:0000269|PubMed:2478623, FT ECO:0000269|PubMed:7871528" FT /id="VAR_082360" FT VARIANT 140 FT /note="D -> Y (in allele A*02:01, allele A*02:05, allele FT A*23:01, allele A*24:02 and allele A*69:01)" FT /evidence="ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2982951, FT ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632, FT ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:9349616" FT /id="VAR_082361" FT VARIANT 151 FT /note="N -> K (in allele A*02:01, allele A*02:05, allele FT A*23:01, allele A*24:02, allele A*68:01 and allele A*69:01; FT dbSNP:rs1059509)" FT /evidence="ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2982951, FT ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632, FT ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:9349616" FT /id="VAR_082362" FT VARIANT 166 FT /note="I -> T (in allele A*02:01, allele A*02:05, allele FT A*68:01 and allele A*69:01; dbSNP:rs1059516)" FT /evidence="ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393, FT ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:7836067" FT /id="VAR_082363" FT VARIANT 168 FT /note="K -> Q (in allele A*23:01, allele A*25:01, allele FT A*26:01, allele A*29:02, allele A*30:01, allele A*31:01, FT allele A*32:01, allele A*33:01, allele A*34:01, allele FT A*43:01, allele A*66:01 and allele A*74:01)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623, FT ECO:0000269|PubMed:7871528, ECO:0000269|PubMed:8026990, FT ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:8795145, FT ECO:0000269|Ref.29" FT /id="VAR_082364" FT VARIANT 169 FT /note="R -> H (in allele A*02:01, allele A*02:05, allele FT A*68:01 and allele A*69:01; dbSNP:rs1059520)" FT /evidence="ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393, FT ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:7836067" FT /id="VAR_082365" FT VARIANT 173 FT /note="A -> T (in allele A*25:01, allele A*26:01, allele FT A*34:01, allele A*43:01 and allele A*66:01; FT dbSNP:rs1059526)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:8026990, FT ECO:0000269|PubMed:8475492" FT /id="VAR_082366" FT VARIANT 174 FT /note="A -> V (in allele A*01:01 and allele A*36:01)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:9349617" FT /id="VAR_082367" FT VARIANT 175 FT /note="H -> R (in allele A*23:01, allele A*29:02, allele FT A*30:01, allele A*31:01, allele A*32:01, allele A*33:01, FT allele A*74:01 and allele A*80:01)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2431040, FT ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:7871528, FT ECO:0000269|PubMed:8188325, ECO:0000269|PubMed:8284791, FT ECO:0000269|PubMed:8795145, ECO:0000269|Ref.29" FT /id="VAR_082368" FT VARIANT 176 FT /note="E -> A (in allele A*01:01, allele A*11:01 and allele FT A*36:01)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2437024, FT ECO:0000269|PubMed:2460344, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:8016845, ECO:0000269|PubMed:9349617" FT /id="VAR_082369" FT VARIANT 176 FT /note="E -> R (in allele A*80:01; requires 2 nucleotide FT substitutions)" FT /evidence="ECO:0000269|PubMed:8188325, FT ECO:0000269|PubMed:8284791" FT /id="VAR_082370" FT VARIANT 176 FT /note="E -> V (in allele A*02:01, allele A*02:05, allele FT A*23:01, allele A*24:02, allele A*29:02, allele A*31:01, FT allele A*32:01, allele A*33:01, allele A*68:01, allele FT A*69:01 and allele A*74:01; results in inefficient T cell FT recognition of epitopes derived from influenza A virus.; FT dbSNP:rs9256983)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2456340, FT ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:2982951, FT ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632, FT ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:8795145, FT ECO:0000269|PubMed:9349616, ECO:0000269|Ref.29" FT /id="VAR_082371" FT VARIANT 176 FT /note="E -> W (in allele A*30:01; requires 2 nucleotide FT substitutions)" FT /evidence="ECO:0000269|PubMed:2478623, FT ECO:0000269|PubMed:7871528" FT /id="VAR_082372" FT VARIANT 180 FT /note="L -> Q (in allele A*11:01 and allele A*24:02)" FT /evidence="ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:2437024, ECO:0000269|PubMed:2460344, FT ECO:0000269|PubMed:8016845, ECO:0000269|PubMed:9349616" FT /id="VAR_082373" FT VARIANT 180 FT /note="L -> R (in allele A*01:01 and allele A*36:01)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:9349617" FT /id="VAR_082374" FT VARIANT 180 FT /note="L -> W (in allele A*02:05, allele A*25:01, allele FT A*26:01, allele A*34:01, allele A*43:01, allele A*66:01, FT allele A*68:01; dbSNP:rs9260156)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:3496393, FT ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:8026990, FT ECO:0000269|PubMed:8475492" FT /id="VAR_082375" FT VARIANT 182 FT /note="A -> V (in allele A*01:01 and allele A*36:01)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:9349617" FT /id="VAR_082376" FT VARIANT 185 FT /note="D -> E (in allele A*01:01, allele A*02:01, allele FT A*02:05, allele A*11:01, allele A*23:01, allele A*24:02, FT allele A*25:01, allele A*26:01, allele A*29:02, allele FT A*30:01, allele A*31:01, allele A*32:01, allele A*33:01, FT allele A*34:01, allele A*36:01, allele A*43:01, allele FT A*66:01, allele A*68:01, allele A*69:01, allele A*74:01 and FT allele A*80:01; dbSNP:rs1059542)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2251137, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040, FT ECO:0000269|PubMed:2437024, ECO:0000269|PubMed:2460344, FT ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393, FT ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:7836067, FT ECO:0000269|PubMed:7871528, ECO:0000269|PubMed:8016845, FT ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8188325, FT ECO:0000269|PubMed:8284791, ECO:0000269|PubMed:8475492, FT ECO:0000269|PubMed:8795145, ECO:0000269|PubMed:9349616, FT ECO:0000269|PubMed:9349617, ECO:0000269|Ref.29" FT /id="VAR_082377" FT VARIANT 187 FT /note="T -> E (in allele A*80:01; requires 2 nucleotide FT substitutions)" FT /evidence="ECO:0000269|PubMed:8188325, FT ECO:0000269|PubMed:8284791" FT /id="VAR_082378" FT VARIANT 187 FT /note="T -> R (in allele A*01:01, allele A*11:01, allele FT A*25:01, allele A*26:01, allele A*43:01 and allele FT A*66:01)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2437024, ECO:0000269|PubMed:2460344, FT ECO:0000269|PubMed:2715640, ECO:0000269|PubMed:8016845, FT ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8475492, FT ECO:0000269|PubMed:9349617" FT /id="VAR_082379" FT VARIANT 190 FT /note="E -> D (in allele A*01:01, allele A*23:01, allele FT A*24:02 and allele A*80:01; dbSNP:rs879577815)" FT /evidence="ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:8188325, ECO:0000269|PubMed:8284791, FT ECO:0000269|PubMed:9349616, ECO:0000269|PubMed:9349617" FT /id="VAR_082380" FT VARIANT 191 FT /note="W -> G (in allele A*01:01, allele A*23:01, allele FT A*24:02 and allele A*80:01; dbSNP:rs3098019)" FT /evidence="ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:2251137, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:8188325, ECO:0000269|PubMed:8284791, FT ECO:0000269|PubMed:9349616, ECO:0000269|PubMed:9349617" FT /id="VAR_082381" FT VARIANT 195 FT /note="Y -> H (in allele A*33:01)" FT /evidence="ECO:0000269|PubMed:2478623" FT /id="VAR_082382" FT VARIANT 208 FT /note="P -> A (in allele A*02:01, allele A*02:05, allele FT A*25:01, allele A*26:01, allele A*29:02, allele A*32:01, FT allele A*34:01, allele A*43:01, allele A*66:01, allele FT A*68:01, allele A*69:01 and allele A*74:01)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2982951, FT ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632, FT ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:8026990, FT ECO:0000269|PubMed:8475492, ECO:0000269|Ref.29" FT /id="VAR_082383" FT VARIANT 210 FT /note="K -> R (in allele A*33:01)" FT /evidence="ECO:0000269|PubMed:2478623" FT /id="VAR_082384" FT VARIANT 217 FT /note="P -> A (in allele A*02:01, allele A*02:05, allele FT A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, FT allele A*32:01, allele A*33:01, allele A*34:01, allele FT A*43:01, allele A*66:01, allele A*68:01, allele A*69:01, FT allele A*74:01)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040, FT ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:2982951, FT ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632, FT ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:8026990, FT ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:8795145, FT ECO:0000269|Ref.29" FT /id="VAR_082385" FT VARIANT 218 FT /note="I -> V (in allele A*02:01, allele A*02:05, allele FT A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, FT allele A*32:01, allele A*33:01, allele A*34:01, allele FT A*43:01, allele A*66:01, allele A*68:01, allele A*69:01 and FT allele A*74:01)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040, FT ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:2982951, FT ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632, FT ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:8026990, FT ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:8795145, FT ECO:0000269|Ref.29" FT /id="VAR_082386" FT VARIANT 231 FT /note="G -> S (in allele A*02:01, allele A*02:05, allele FT A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, FT allele A*32:01, allele A*33:01, allele A*34:01, allele FT A*43:01, allele A*66:01, allele A*68:01, allele A*69:01, FT allele A*74:01 and allele A*80:01)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040, FT ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:2982951, FT ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632, FT ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:8026990, FT ECO:0000269|PubMed:8188325, ECO:0000269|PubMed:8284791, FT ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:8795145, FT ECO:0000269|Ref.29" FT /id="VAR_082387" FT VARIANT 269 FT /note="A -> V (in allele A*68:01; impairs binding to CD8A FT and reduces recognition by antigen-specific CD8-positive T FT cells)" FT /evidence="ECO:0000269|PubMed:2784196, FT ECO:0000269|PubMed:3877632" FT /id="VAR_082388" FT VARIANT 270 FT /note="A -> S (in allele A*25:01, allele A*26:01, allele FT A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, FT allele A*34:01, allele A*43:01, allele A*66:01 and allele FT A*74:01)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623, FT ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8475492, FT ECO:0000269|Ref.29" FT /id="VAR_082389" FT VARIANT 277 FT /note="E -> K (in allele A*80:01)" FT /evidence="ECO:0000269|PubMed:8188325, FT ECO:0000269|PubMed:8284791" FT /id="VAR_082390" FT VARIANT 277 FT /note="E -> Q (in allele A*02:01, allele A*02:05, allele FT A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, FT allele A*32:01, allele A*33:01, allele A*34:01, allele FT A*43:01, allele A*66:01, allele A*68:01, allele A*69:01 and FT allele A*74:01)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040, FT ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:2982951, FT ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632, FT ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:8026990, FT ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:8795145, FT ECO:0000269|Ref.29" FT /id="VAR_082391" FT VARIANT 279 FT /note="Q -> K (in allele A*80:01)" FT /evidence="ECO:0000269|PubMed:8188325, FT ECO:0000269|PubMed:8284791" FT /id="VAR_082392" FT VARIANT 292 FT /note="K -> E (in allele A*80:01)" FT /evidence="ECO:0000269|PubMed:8188325, FT ECO:0000269|PubMed:8284791" FT /id="VAR_082393" FT VARIANT 300 FT /note="L -> P (in allele A*02:01, allele A*02:05, allele FT A*23:01, allele A*24:02, allele A*25:01, allele A*26:01, FT allele A*29:02, allele A*31:01, allele A*32:01, allele FT A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, FT allele A*68:01, allele A*69:01, allele A*74:01 and allele FT A*80:01)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623, FT ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393, FT ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:7836067, FT ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8188325, FT ECO:0000269|PubMed:8284791, ECO:0000269|PubMed:8475492, FT ECO:0000269|PubMed:8795145, ECO:0000269|PubMed:9349616, FT ECO:0000269|Ref.29" FT /id="VAR_082394" FT VARIANT 306 FT /note="I -> V (in allele A*23:01 and allele A*24:02)" FT /evidence="ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:9349616" FT /id="VAR_082395" FT VARIANT 307 FT /note="P -> H (in allele A*23:01)" FT /evidence="ECO:0000269|PubMed:1729171" FT /id="VAR_082396" FT VARIANT 312 FT /note="I -> L (in allele A*34:01)" FT /evidence="ECO:0000269|PubMed:1431115" FT /id="VAR_082397" FT VARIANT 318 FT /note="L -> F (in allele A*02:01, allele A*02:05, allele FT A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, FT allele A*32:01, allele A*33:01, allele A*34:01, allele FT A*43:01, allele A*66:01, allele A*68:01, allele A*69:01 and FT allele A*74:01)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040, FT ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:2982951, FT ECO:0000269|PubMed:3496393, ECO:0000269|PubMed:3877632, FT ECO:0000269|PubMed:7836067, ECO:0000269|PubMed:8026990, FT ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:8795145, FT ECO:0000269|Ref.29" FT /id="VAR_082398" FT VARIANT 321 FT /note="V -> M (in allele A*32:01 and allele A*74:01)" FT /evidence="ECO:0000269|PubMed:1431115, FT ECO:0000269|PubMed:2431040, ECO:0000269|Ref.29" FT /id="VAR_082399" FT VARIANT 322 FT /note="I -> F (in allele A*29:02, allele A*31:01, allele FT A*32:01, allele A*33:01 and allele A*74:01)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566, FT ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623, FT ECO:0000269|PubMed:8795145, ECO:0000269|Ref.29" FT /id="VAR_082400" FT VARIANT 323 FT /note="T -> A (in allele A*25:01, allele A*26:01, allele FT A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, FT allele A*34:01, allele A*43:01, allele A*66:01, allele FT A*74:01 and allele A*80:01)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040, FT ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:8026990, FT ECO:0000269|PubMed:8188325, ECO:0000269|PubMed:8284791, FT ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:8795145, FT ECO:0000269|Ref.29" FT /id="VAR_082401" FT VARIANT 331 FT /note="M -> R (in allele A*29:02, allele A*31:01, allele FT A*32:01, allele A*33:01 and allele A*74:01)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566, FT ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623, FT ECO:0000269|PubMed:8795145, ECO:0000269|Ref.29" FT /id="VAR_082402" FT VARIANT 334 FT /note="R -> K (allele A*80:01)" FT /evidence="ECO:0000269|PubMed:8188325, FT ECO:0000269|PubMed:8284791" FT /id="VAR_082403" FT VARIANT 335 FT /note="K -> N (in allele A*23:01 and allele A*24:02)" FT /evidence="ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:9349616" FT /id="VAR_082404" FT VARIANT 338 FT /note="D -> V (allele A*80:01)" FT /evidence="ECO:0000269|PubMed:8188325, FT ECO:0000269|PubMed:8284791" FT /id="VAR_082405" FT VARIANT 345 FT /note="T -> S (in allele A*02:01, allele A*02:05, allele FT A*23:01, allele A*24:02, allele A*25:01, allele A*26:01, FT allele A*29:02, allele A*31:01, allele A*32:01, allele FT A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, FT allele A*68:01 allele A*69:01, allele A*74:01 and allele FT A*80:01)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1729171, FT ECO:0000269|PubMed:1782566, ECO:0000269|PubMed:2320591, FT ECO:0000269|PubMed:2431040, ECO:0000269|PubMed:2478623, FT ECO:0000269|PubMed:2982951, ECO:0000269|PubMed:3496393, FT ECO:0000269|PubMed:3877632, ECO:0000269|PubMed:7836067, FT ECO:0000269|PubMed:8026990, ECO:0000269|PubMed:8188325, FT ECO:0000269|PubMed:8284791, ECO:0000269|PubMed:8475492, FT ECO:0000269|PubMed:8795145, ECO:0000269|PubMed:9349616, FT ECO:0000269|Ref.29" FT /id="VAR_082406" FT VARIANT 358 FT /note="V -> M (in allele A*25:01, allele A*26:01, allele FT A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, FT allele A*34:01, allele A*43:01, allele A*66:01 and allele FT A*74:01)" FT /evidence="ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1431115, ECO:0000269|PubMed:1782566, FT ECO:0000269|PubMed:2320591, ECO:0000269|PubMed:2431040, FT ECO:0000269|PubMed:2478623, ECO:0000269|PubMed:8026990, FT ECO:0000269|PubMed:8475492, ECO:0000269|PubMed:8795145, FT ECO:0000269|Ref.29" FT /id="VAR_082407" FT MUTAGEN 110 FT /note="N->Q: Impairs the recruitment of HLA-A*02 in the FT peptide-loading complex." FT /evidence="ECO:0000269|PubMed:21263072" FT MUTAGEN 156 FT /note="S->C: Impairs the maturation of a peptide-receptive FT HLA-A*02-B2M complex." FT /evidence="ECO:0000269|PubMed:8805302" FT MUTAGEN 158 FT /note="T->K: Impairs binding to TAP1-TAP2 transporter, FT resulting in impaired presentation of intracellular FT peptides." FT /evidence="ECO:0000269|PubMed:8630735, FT ECO:0000269|PubMed:8805302" FT STRAND 27..36 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 41..43 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 45..52 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 55..61 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 70..73 FT /evidence="ECO:0007829|PDB:4F7T" FT HELIX 74..78 FT /evidence="ECO:0007829|PDB:3MRE" FT HELIX 81..108 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:3D25" FT STRAND 118..127 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 131..142 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 145..150 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 152..155 FT /evidence="ECO:0007829|PDB:6EWA" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:3MRE" FT HELIX 162..173 FT /evidence="ECO:0007829|PDB:3MRE" FT HELIX 176..184 FT /evidence="ECO:0007829|PDB:3MRE" FT HELIX 187..198 FT /evidence="ECO:0007829|PDB:3MRE" FT HELIX 200..203 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 210..235 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 238..243 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:3MRE" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:2GTW" FT STRAND 252..254 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 261..263 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 265..274 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 275..277 FT /evidence="ECO:0007829|PDB:4JFD" FT HELIX 278..280 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 281..286 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 290..292 FT /evidence="ECO:0007829|PDB:2V2X" FT STRAND 294..297 FT /evidence="ECO:0007829|PDB:3MRE" FT STRAND 348..350 FT /evidence="ECO:0007829|PDB:4EN2" SQ SEQUENCE 365 AA; 40841 MW; DEDFCEC4450E0580 CRC64; MAVMAPRTLL LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDQETRN VKAQSQTDRV DLGTLRGYYN QSEAGSHTIQ IMYGCDVGSD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAAHEAEQL RAYLDGTCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEL SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV //