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 02-OCT-2024, entry version 219.
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:10449296,
CC PubMed:12138174, PubMed:12393434, PubMed:1402688, PubMed:15893615,
CC PubMed:17189421, PubMed:19543285, PubMed:21498667, PubMed:24192765,
CC PubMed:24395804, PubMed:2456340, PubMed:2784196, PubMed:28250417,
CC PubMed:7504010, PubMed:7694806, PubMed:9862734). May also present self-
CC 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:17079320, PubMed:17189421, PubMed:20364150, 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:17189421,
CC PubMed:19177349, PubMed:20364150, PubMed:24395804, PubMed:25880248,
CC PubMed:26758806, PubMed:30530481, PubMed:32887977, PubMed:7504010). 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:19543285, PubMed:21943705,
CC PubMed:2456340, PubMed:32887977, PubMed:7504010, PubMed:7679507,
CC PubMed:9862734). 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:12393434,
CC PubMed:20844028, PubMed:24192765, PubMed:9047241). 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:11502003,
CC PubMed:18275829, PubMed:19177349, PubMed:19542454, PubMed:21943705,
CC PubMed:22245737, PubMed:24395804, PubMed:26758806, PubMed:28250417,
CC PubMed:7504010, PubMed:7506728, PubMed:7679507, PubMed:7694806,
CC PubMed:7935798, PubMed:8805302, PubMed:8906788, PubMed:9177355). Early
CC in biogenesis, HLA-A-B2M dimer interacts with the components of the
CC peptide-loading complex composed of TAPBP, TAP1-TAP2, TAPBPL,
CC PDIA3/ERP57 and CALR (PubMed:21263072). Interacts with TAP1-TAP2
CC transporter via TAPBP; this interaction is obligatory for the loading
CC of peptide epitopes delivered to the ER by TAP1-TAP2 transporter
CC (PubMed:21263072, PubMed:8630735, PubMed:8805302). Interacts with
CC TAPBPL; TAPBPL binds peptide-free HLA-A-B2M complexes or those loaded
CC with low affinity peptides, likely facilitating peptide exchange for
CC higher affinity peptides (PubMed:26869717). Only optimally assembled
CC peptide-HLA-B2M trimer translocates to the surface of antigen-
CC presenting cells, where it interacts with TCR and CD8 coreceptor on the
CC surface of T cells. HLA-A (via polymorphic alpha-1 and alpha-2 domains)
CC interacts with antigen-specific TCR (via CDR3 domains)
CC (PubMed:12796775, PubMed:18275829, PubMed:22245737). One HLA-A molecule
CC (mainly via nonpolymorphic alpha-3 domain) interacts with one CD8A
CC homodimer (via CDR-like loop); this interaction ensures peptide-HLA-A-
CC B2M recognition by CD8-positive T cells only (PubMed:2784196,
CC PubMed:9177355). 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:19177349, PubMed:19542454, PubMed:20619457,
CC PubMed:20844028, PubMed:21543847, PubMed:21943705, PubMed:22245737,
CC PubMed:24395804, PubMed:26758806, PubMed:2784196, PubMed:28250417,
CC PubMed:7694806, PubMed:8906788). 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:16731854, PubMed:18802479, PubMed:22245737, 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:18802479, PubMed:22245737). 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 ---------------------------------------------------------------------------
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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-26853; -.
DR EMDB; EMD-27181; -.
DR EMDB; EMD-27182; -.
DR EMDB; EMD-27183; -.
DR EMDB; EMD-27184; -.
DR EMDB; EMD-27185; -.
DR EMDB; EMD-3906; -.
DR SMR; P04439; -.
DR BioGRID; 109350; 405.
DR IntAct; P04439; 191.
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 DrugCentral; P04439; -.
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 jPOST; P04439; -.
DR MassIVE; 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; 1446 antibodies from 33 providers.
DR CPTC; P04439; 1 antibody.
DR DNASU; 3105; -.
DR Ensembl; ENST00000376809.10; ENSP00000366005.5; ENSG00000206503.15. [P04439-1]
DR Ensembl; ENST00000396634.5; ENSP00000379873.1; ENSG00000206503.15. [P04439-1]
DR Ensembl; ENST00000706901.1; ENSP00000516612.1; ENSG00000206503.15. [P04439-1]
DR Ensembl; ENST00000706903.1; ENSP00000516614.1; ENSG00000206503.15. [P04439-1]
DR Ensembl; ENST00000706905.1; ENSP00000516616.1; ENSG00000206503.15. [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; ENSGT01120000271826; -.
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 EvolutionaryTrace; P04439; -.
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; IPR050208; MHC_class-I_related.
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;
KW Proteomics identification; Reference proteome; Signal; Sulfation;
KW 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 KLRD1-
FT 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
//