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HLA class I histocompatibility antigen, A-2 alpha chain (Human leukocyte antigen A*02) (HLA-A*02)

 1A02_HUMAN              Reviewed;         365 AA.
P01892; O19619; P06338; P10313; P30444; P30445; P30446; P30514;
Q29680; Q29837; Q29899; Q95352; Q95380; Q9TPX8; Q9TPX9; Q9TPY0;
Q9TQH5; Q9TQI3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
31-JUL-2019, entry version 221.
RecName: Full=HLA class I histocompatibility antigen, A-2 alpha chain;
AltName: Full=Human leukocyte antigen A*02;
Short=HLA-A*02 {ECO:0000303|PubMed:20356336};
Flags: Precursor;
Name=HLA-A {ECO:0000312|HGNC:HGNC:4931}; Synonyms=HLAA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 39-365 (ALLELE A*02:01).
PubMed=3874058;
Krangel M.S.;
"Unusual RNA splicing generates a secreted form of HLA-A2 in a
mutagenized B lymphoblastoid cell line.";
EMBO J. 4:1205-1210(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 91-365.
PubMed=3863816;
Davidson W.F., Kress M., Khoury G., Jay G.;
"Comparison of HLA class I gene sequences. Derivation of locus-
specific oligonucleotide probes specific for HLA-A, HLA-B, and HLA-C
genes.";
J. Biol. Chem. 260:13414-13423(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A*02:03 AND A*02:05).
PubMed=3496393;
Holmes N., Ennis P., Wan A.M., Denney D.W., Parham P.;
"Multiple genetic mechanisms have contributed to the generation of the
HLA-A2/A28 family of class I MHC molecules.";
J. Immunol. 139:936-941(1987).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:10).
PubMed=2783680; DOI=10.1007/BF00395859;
Epstein H., Kennedy L., Holmes N.;
"An Oriental HLA-A2 subtype is closely related to a subset of
Caucasoid HLA-A2 alleles.";
Immunogenetics 29:112-116(1989).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:06).
PubMed=2715640;
Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.;
"Diversity and diversification of HLA-A,B,C alleles.";
J. Immunol. 142:3937-3950(1989).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:01).
PubMed=2320591; DOI=10.1073/pnas.87.7.2833;
Ennis P.D., Zemmour J., Salter R.D., Parham P.;
"Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction:
frequency and nature of errors produced in amplification.";
Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-365 (ALLELE A*02:04).
PubMed=1937577; DOI=10.1007/BF00211991;
Castano A.R., Lopez de Castro J.A.;
"Structure of the HLA-A*0204 antigen, found in South American Indians.
Spatial clustering of HLA-A2 subtype polymorphism.";
Immunogenetics 34:281-285(1991).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-365 (ALLELE A*02:11).
PubMed=1559719; DOI=10.1007/BF00189898;
Castano A.R., Lopez de Castro J.A.;
"Structure of the HLA-A*0211 (A2.5) subtype: further evidence for
selection-driven diversification of HLA-A2 antigens.";
Immunogenetics 35:344-346(1992).
[9]
NUCLEOTIDE SEQUENCE (ALLELES A*02:01; A*02:11 AND A*02:12).
PubMed=1317015; DOI=10.1038/357326a0;
Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J.,
Williams R.C., Luz R., Petzl-Erler M.L., Parham P.;
"Unusual HLA-B alleles in two tribes of Brazilian Indians.";
Nature 357:326-329(1992).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-365 (ALLELE A*02:04).
PubMed=1589035; DOI=10.1038/357329a0;
Watkins D.I., McAdam S.N., Liu X., Stang C.R., Milford E.L.,
Levine C.G., Garber T.L., Dogon A.L., Lord C.I., Ghim S.H.,
Troup G.M., Hughes A.L., Letvin N.L.;
"New recombinant HLA-B alleles in a tribe of South American
Amerindians indicate rapid evolution of MHC class I loci.";
Nature 357:329-333(1992).
[11]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:13).
PubMed=8168863; DOI=10.1007/BF00189243;
Barber D.F., Fernandez J.M., Lopez de Castro J.A.;
"Primary structure of a new HLA-A2 subtype: HLA-A*0213.";
Immunogenetics 39:378-378(1994).
[12]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:16).
PubMed=7759139; DOI=10.1007/BF00164000;
Barouch D., Krausa P., Bodmer J., Browning M.J., McMichael A.J.;
"Identification of a novel HLA-A2 subtype, HLA-A*0216.";
Immunogenetics 41:388-388(1995).
[13]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:17).
TISSUE=Blood;
PubMed=7652742; DOI=10.1111/j.1399-0039.1995.tb02464.x;
Selvakumar A., Granja C.B., Salazar M., Alosco S.M., Yunis E.J.,
Dupont B.;
"A novel subtype of A2 (A*0217) isolated from the South American
Indian B-cell line AMALA.";
Tissue Antigens 45:343-347(1995).
[14]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:20).
TISSUE=Blood;
PubMed=9008310; DOI=10.1111/j.1399-0039.1996.tb02691.x;
Fleischhauer K., Zino E., Mazzi B., Severini G.M., Benazzi E.,
Bordignon C.;
"HLA-A*02 subtype distribution in Caucasians from northern Italy:
identification of A*0220.";
Tissue Antigens 48:673-679(1996).
[15]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:18).
TISSUE=Blood;
Kashiwase K., Tokunaga K., Ishikawa Y., Oohashi H., Hashimoto M.,
Akaza T., Tadokoro K., Juji T.;
"A new A2 sequence HLA-A2K from Japanese.";
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
[16]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:21).
TISSUE=Blood;
Szmania S., Baxter-Lowe L.A.;
"Nucleotide sequence of a novel HLA-A2 gene.";
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
[17]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*02:01).
PubMed=2982951;
Koller B.H., Orr H.T.;
"Cloning and complete sequence of an HLA-A2 gene: analysis of two HLA-
A alleles at the nucleotide level.";
J. Immunol. 134:2727-2733(1985).
[18]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-298 (ALLELES A*02:02 AND
A*02:03).
PubMed=3497874; DOI=10.1007/BF00365911;
Mattson D.H., Handy D.E., Bradley D.A., Coligan J.E., Cowan E.P.,
Biddison W.E.;
"DNA sequences of the genes that encode the CTL-defined HLA-A2
variants M7 and DK1.";
Immunogenetics 26:190-192(1987).
[19]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*02:01).
TISSUE=Blood;
PubMed=7836067; DOI=10.1016/0198-8859(94)90087-6;
Balas A., Garcia-Sanchez F., Gomez-Reino F., Vicario J.L.;
"HLA class I allele (HLA-A2) expression defect associated with a
mutation in its enhancer B inverted CAT box in two families.";
Hum. Immunol. 41:69-73(1994).
[20]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE A*02:31).
PubMed=10689125; DOI=10.1016/S0198-8859(99)00155-X;
Ellis J.M., Henson V., Slack R., Ng J., Hartzman R.J., Hurley C.K.;
"Frequencies of HLA-A2 alleles in five U.S. population groups.
Predominance Of A*02011 and identification of HLA-A*0231.";
Hum. Immunol. 61:334-340(2000).
[21]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-298 (ALLELE A*02:34).
PubMed=10746792; DOI=10.1034/j.1399-0039.2000.550212.x;
Moses J.H., Greville W.D., Downes J., McClenahan W., Kennedy A.,
Dunckley H.;
"A new HLA-A*02 allele, A*0234, detected by polymerase chain reaction
using sequence-specific primers (PCR-SSP).";
Tissue Antigens 55:175-177(2000).
[22]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELES A*02:35; A*02:36
AND A*02:37).
PubMed=10852390; DOI=10.1034/j.1399-0039.2000.550412.x;
Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R.,
Ng J., Hartzman R.J., Hurley C.K.;
"Seventeen more novel HLA-A locus alleles.";
Tissue Antigens 55:369-373(2000).
[23]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*02:01).
Cox S.T.;
"Confirmation of HLA-A*0201.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[24]
PROTEIN SEQUENCE OF 25-295 (ALLELE A*02:01).
PubMed=92029; DOI=10.1073/pnas.76.9.4395;
Orr H.T., Lopez de Castro J.A., Parham P., Ploegh H.L.,
Strominger J.L.;
"Comparison of amino acid sequences of two human histocompatibility
antigens, HLA-A2 and HLA-B7: location of putative alloantigenic
sites.";
Proc. Natl. Acad. Sci. U.S.A. 76:4395-4399(1979).
[25]
PARTIAL PROTEIN SEQUENCE (ALLELE A*02:06).
PubMed=3489037;
Ezquerra A., Domenech N., van der Poel J., Strominger J.L., Vega M.A.,
Lopez de Castro J.A.;
"Molecular analysis of an HLA-A2 functional variant CLA defined by
cytolytic T lymphocytes.";
J. Immunol. 137:1642-1649(1986).
[26]
PARTIAL PROTEIN SEQUENCE (ALLELE A*02:08).
PubMed=2457548; DOI=10.1007/BF00375853;
Domenech N., Castano R., Goulmy E., Lopez de Castro J.A.;
"Molecular analysis of HLA-A2.4 functional variant KLO: close
structural and evolutionary relatedness to the HLA-A2.2 subtype.";
Immunogenetics 28:143-152(1988).
[27]
PARTIAL PROTEIN SEQUENCE (ALLELE A*02:07).
PubMed=2448239; DOI=10.1007/BF00346586;
Domenech N., Ezquerra A., Castano R., Lopez de Castro J.A.;
"Structural analysis of HLA-A2.4 functional variant KNE. Implications
for the mapping of HLA-A2-specific T-cell epitopes.";
Immunogenetics 27:196-202(1988).
[28]
PARTIAL PROTEIN SEQUENCE (ALLELE A*02:09).
PubMed=3258580; DOI=10.1007/BF00395130;
Castano R., Ezquerra A., Domenech N., Lopez de Castro J.A.;
"An HLA-A2 population variant with structural polymorphism in the
alpha 3 region.";
Immunogenetics 27:345-355(1988).
[29]
FUNCTION, INTERACTION WITH CD8A, MUTAGENESIS OF ALA-269, AND DOMAIN.
PubMed=2784196; DOI=10.1038/338345a0;
Salter R.D., Norment A.M., Chen B.P., Clayberger C., Krensky A.M.,
Littman D.R., Parham P.;
"Polymorphism in the alpha 3 domain of HLA-A molecules affects binding
to CD8.";
Nature 338:345-347(1989).
[30]
FUNCTION, MUTAGENESIS OF SER-156 AND THR-158, DOMAIN, INTERACTION WITH
B2M, INTERACTION WITH TAP1-TAP2 COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=8805302;
Lewis J.W., Neisig A., Neefjes J., Elliott T.;
"Point mutations in the alpha 2 domain of HLA-A2.1 define a
functionally relevant interaction with TAP.";
Curr. Biol. 6:873-883(1996).
[31]
FUNCTION, INTERACTION WITH TAP1-TAP2 COMPLEX, AND MUTAGENESIS OF
THR-158.
PubMed=8630735;
Peace-Brewer A.L., Tussey L.G., Matsui M., Li G., Quinn D.G.,
Frelinger J.A.;
"A point mutation in HLA-A*0201 results in failure to bind the TAP
complex and to present virus-derived peptides to CTL.";
Immunity 4:505-514(1996).
[32]
INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I (MICROBIAL INFECTION).
PubMed=11390610; DOI=10.1128/JVI.75.13.6086-6094.2001;
Johnson J.M., Nicot C., Fullen J., Ciminale V., Casareto L.,
Mulloy J.C., Jacobson S., Franchini G.;
"Free major histocompatibility complex class I heavy chain is
preferentially targeted for degradation by human T-cell
leukemia/lymphotropic virus type 1 p12(I) protein.";
J. Virol. 75:6086-6094(2001).
[33]
INTERACTION WITH HUMAN HERPESVIRUS 8 MIR1 PROTEIN (MICROBIAL
INFECTION), AND UBIQUITINATION.
PubMed=12006494; DOI=10.1093/emboj/21.10.2418;
Hewitt E.W., Duncan L., Mufti D., Baker J., Stevenson P.G.,
Lehner P.J.;
"Ubiquitylation of MHC class I by the K3 viral protein signals
internalization and TSG101-dependent degradation.";
EMBO J. 21:2418-2429(2002).
[34]
FUNCTION.
PubMed=12138174; DOI=10.1073/pnas.112331099;
Nagata Y., Ono S., Matsuo M., Gnjatic S., Valmori D., Ritter G.,
Garrett W., Old L.J., Mellman I.;
"Differential presentation of a soluble exogenous tumor antigen, NY-
ESO-1, by distinct human dendritic cell populations.";
Proc. Natl. Acad. Sci. U.S.A. 99:10629-10634(2002).
[35]
FUNCTION.
PubMed=17079320; DOI=10.1128/JVI.01779-06;
Robek M.D., Garcia M.L., Boyd B.S., Chisari F.V.;
"Role of immunoproteasome catalytic subunits in the immune response to
hepatitis B virus.";
J. Virol. 81:483-491(2007).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[38]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[39]
NOMENCLATURE.
PubMed=20356336; DOI=10.1111/j.1399-0039.2010.01466.x;
Marsh S.G., Albert E.D., Bodmer W.F., Bontrop R.E., Dupont B.,
Erlich H.A., Fernandez-Vina M., Geraghty D.E., Holdsworth R.,
Hurley C.K., Lau M., Lee K.W., Mach B., Maiers M., Mayr W.R.,
Mueller C.R., Parham P., Petersdorf E.W., Sasazuki T.,
Strominger J.L., Svejgaard A., Terasaki P.I., Tiercy J.M.,
Trowsdale J.;
"Nomenclature for factors of the HLA system, 2010.";
Tissue Antigens 75:291-455(2010).
[40]
INDUCTION BY IFNG, GLYCOSYLATION AT ASN-110, MUTAGENESIS OF ASN-110,
SUBCELLULAR LOCATION, AND INTERACTION WITH TAPBP.
PubMed=21263072; DOI=10.4049/jimmunol.1002959;
Rizvi S.M., Del Cid N., Lybarger L., Raghavan M.;
"Distinct functions for the glycans of tapasin and heavy chains in the
assembly of MHC class I molecules.";
J. Immunol. 186:2309-2320(2011).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356 AND SER-359, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350; SER-352; SER-356
AND SER-359, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[43]
INTERACTION WITH TAPBPL.
PubMed=26869717; DOI=10.1073/pnas.1519894113;
Morozov G.I., Zhao H., Mage M.G., Boyd L.F., Jiang J., Dolan M.A.,
Venna R., Norcross M.A., McMurtrey C.P., Hildebrand W., Schuck P.,
Natarajan K., Margulies D.H.;
"Interaction of TAPBPR, a tapasin homolog, with MHC-I molecules
promotes peptide editing.";
Proc. Natl. Acad. Sci. U.S.A. 113:E1006-E1015(2016).
[44]
FUNCTION.
PubMed=26929325; DOI=10.1073/pnas.1521812113;
Tripathi S.C., Peters H.L., Taguchi A., Katayama H., Wang H.,
Momin A., Jolly M.K., Celiktas M., Rodriguez-Canales J., Liu H.,
Behrens C., Wistuba I.I., Ben-Jacob E., Levine H., Molldrem J.J.,
Hanash S.M., Ostrin E.J.;
"Immunoproteasome deficiency is a feature of non-small cell lung
cancer with a mesenchymal phenotype and is associated with a poor
outcome.";
Proc. Natl. Acad. Sci. U.S.A. 113:E1555-E1564(2016).
[45]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 25-299 IN COMPLEX WITH B2M
AND PEPTIDE, FUNCTION, DISULFIDE BOND, AND DOMAIN.
PubMed=7694806; DOI=10.1016/0092-8674(93)90490-H;
Madden D.R., Garboczi D.N., Wiley D.C.;
"The antigenic identity of peptide-MHC complexes: a comparison of the
conformations of five viral peptides presented by HLA-A2.";
Cell 75:693-708(1993).
[46]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 25-299 IN COMPLEX WITH B2M
AND PEPTIDE, AND FUNCTION.
PubMed=7935798; DOI=10.1038/371626a0;
Collins E.J., Garboczi D.N., Wiley D.C.;
"Three-dimensional structure of a peptide extending from one end of a
class I MHC binding site.";
Nature 371:626-629(1994).
[47]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 25-299 IN COMPLEX WITH B2M
AND PEPTIDE, FUNCTION, AND DOMAIN.
PubMed=8906788; DOI=10.1038/384134a0;
Garboczi D.N., Ghosh P., Utz U., Fan Q.R., Biddison W.E., Wiley D.C.;
"Structure of the complex between human T-cell receptor, viral peptide
and HLA-A2.";
Nature 384:134-141(1996).
[48]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 25-300 IN COMPLEX WITH B2M
AND PEPTIDE, INTERACTION WITH CD8A, AND FUNCTION.
PubMed=9177355; DOI=10.1038/42523;
Gao G.F., Tormo J., Gerth U.C., Wyer J.R., McMichael A.J.,
Stuart D.I., Bell J.I., Jones E.Y., Jakobsen B.K.;
"Crystal structure of the complex between human CD8alpha(alpha) and
HLA-A2.";
Nature 387:630-634(1997).
[49]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 25-299 IN COMPLEX WITH B2M
AND PEPTIDE, AND FUNCTION.
PubMed=11502003; DOI=10.1006/jmbi.2001.4816;
Hillig R.C., Coulie P.G., Stroobant V., Saenger W., Ziegler A.,
Hulsmeyer M.;
"High-resolution structure of HLA-A*0201 in complex with a tumour-
specific antigenic peptide encoded by the MAGE-A4 gene.";
J. Mol. Biol. 310:1167-1176(2001).
[50]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 25-300 IN COMPLEX WITH B2M
AND PEPTIDE, INTERACTION WITH TCR, AND FUNCTION.
PubMed=12796775; DOI=10.1038/ni942;
Stewart-Jones G.B.E., McMichael A.J., Bell J.I., Stuart D.I.,
Jones E.Y.;
"A structural basis for immunodominant human T cell receptor
recognition.";
Nat. Immunol. 4:657-663(2003).
[51]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 25-300 IN COMPLEX WITH B2M
AND PEPTIDE, INTERACTION WITH TCR, AND FUNCTION.
PubMed=18275829; DOI=10.1016/J.IMMUNI.2007.12.018;
Ishizuka J., Stewart-Jones G.B., van der Merwe A., Bell J.I.,
McMichael A.J., Jones E.Y.;
"The structural dynamics and energetics of an immunodominant T cell
receptor are programmed by its Vbeta domain.";
Immunity 28:171-182(2008).
[52]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 25-298 IN COMPLEX WITH B2M
AND PEPTIDE, FUNCTION, AND DOMAIN.
PubMed=19542454; DOI=10.4049/jimmunol.0900556;
Gras S., Saulquin X., Reiser J.B., Debeaupuis E., Echasserieau K.,
Kissenpfennig A., Legoux F., Chouquet A., Le Gorrec M., Machillot P.,
Neveu B., Thielens N., Malissen B., Bonneville M., Housset D.;
"Structural bases for the affinity-driven selection of a public TCR
against a dominant human cytomegalovirus epitope.";
J. Immunol. 183:430-437(2009).
[53]
X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 25-299 IN COMPLEX WITH B2M
AND PEPTIDE, FUNCTION, AND DOMAIN.
PubMed=20619457; DOI=10.1016/j.molimm.2010.06.005;
Borbulevych O.Y., Do P., Baker B.M.;
"Structures of native and affinity-enhanced WT1 epitopes bound to HLA-
A*0201: implications for WT1-based cancer therapeutics.";
Mol. Immunol. 47:2519-2524(2010).
[54]
X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 25-300 IN COMPLEX WITH B2M
AND PEPTIDE, INTERACTION WITH TCR, FUNCTION, DOMAIN, INDUCTION BY
CYTOKINES, AND INVOLVEMENT IN IDDM.
PubMed=22245737; DOI=10.1038/ni.2206;
Bulek A.M., Cole D.K., Skowera A., Dolton G., Gras S., Madura F.,
Fuller A., Miles J.J., Gostick E., Price D.A., Drijfhout J.W.,
Knight R.R., Huang G.C., Lissin N., Molloy P.E., Wooldridge L.,
Jakobsen B.K., Rossjohn J., Peakman M., Rizkallah P.J., Sewell A.K.;
"Structural basis for the killing of human beta cells by CD8(+) T
cells in type 1 diabetes.";
Nat. Immunol. 13:283-289(2012).
[55]
X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 25-299 IN COMPLEX WITH B2M
AND PEPTIDE, FUNCTION, DOMAIN, AND DISULFIDE BOND.
PubMed=28250417; DOI=10.1038/nsmb.3383;
Song I., Gil A., Mishra R., Ghersi D., Selin L.K., Stern L.J.;
"Broad TCR repertoire and diverse structural solutions for recognition
of an immunodominant CD8+ T cell epitope.";
Nat. Struct. Mol. Biol. 24:395-406(2017).
[56]
INVOLVEMENT IN IDDM.
PubMed=18802479; DOI=10.1172/JCI35449;
Skowera A., Ellis R.J., Varela-Calvino R., Arif S., Huang G.C.,
Van-Krinks C., Zaremba A., Rackham C., Allen J.S., Tree T.I., Zhao M.,
Dayan C.M., Sewell A.K., Unger W.W., Unger W., Drijfhout J.W.,
Ossendorp F., Roep B.O., Peakman M.;
"CTLs are targeted to kill beta cells in patients with type 1 diabetes
through recognition of a glucose-regulated preproinsulin epitope.";
J. Clin. Invest. 118:3390-3402(2008).
[57]
VARIANT [LARGE SCALE ANALYSIS] GLU-176, VARIANT [LARGE SCALE ANALYSIS]
TRP-180, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[58]
VARIANT [LARGE SCALE ANALYSIS] GLU-176, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[59]
VARIANT GLY-89.
PubMed=26566883; DOI=10.1136/jmedgenet-2015-103179;
Rafiullah R., Aslamkhan M., Paramasivam N., Thiel C., Mustafa G.,
Wiemann S., Schlesner M., Wade R.C., Rappold G.A., Berkel S.;
"Homozygous missense mutation in the LMAN2L gene segregates with
intellectual disability in a large consanguineous Pakistani family.";
J. Med. Genet. 53:138-144(2016).
-!- FUNCTION: Antigen-presenting major histocompatibility complex
class I (MHCI) molecule, HLA-A*02 serotype. In complex with
B2M/beta 2 microglobulin displays primarily viral and tumor-
derived peptides on antigen-presenting cells for recognition by
alpha-beta T cell receptor (TCR) on HLA-A*02-restricted CD8-
positive T cells, guiding antigen-specific T cell immune response
to eliminate infected or transformed cells (PubMed:7694806,
PubMed:2784196, PubMed:12138174, PubMed:12796775, PubMed:28250417,
PubMed:8906788, PubMed:19542454, PubMed:20619457). May also
present self-peptides derived from the signal sequence of secreted
or membrane proteins, although T cells specific for these peptides
are usually inactivated to prevent autoreactivity
(PubMed:7935798). Both the peptide and the MHC molecule are
recognized by TCR, the peptide is responsible for the fine
specificity of antigen recognition and MHC residues account for
the MHC restriction of T cells (PubMed:12796775, PubMed:18275829,
PubMed:19542454, PubMed:28250417). Typically presents
intracellular peptide antigens of 8 to 11 amino acids that arise
from cytosolic proteolysis via IFNG-induced immunoproteasome
(PubMed:17079320, PubMed:26929325). Can bind different peptides
that share a common structural motif defined by the nature of the
peptide anchor residues (PubMed:7935798, PubMed:8906788,
PubMed:8805302, PubMed:8630735, PubMed:22245737). HLA-A*02:01, a
major allele in human populations, presents immunodominant viral
epitopes derived from IAV M/matrix protein 1 (GILGFVFTL), HIV-1
env (TLTSCNTSV), HIV-1 gag-pol (ILKEPVHGV), HTLV-1 Tax
(LLFGYPVYV), HBV C/core antigen (FLPSDFFPS), HCMV UL83/pp65
(NLVPMVATV) as well as tumor peptide antigens including MAGEA4
(GVYDGREHTV), WT1 (RMFPNAPYL) and CTAG1A/NY-ESO-1 (SLLMWITQC), all
having in common hydrophobic amino acids at position 2 and at C-
terminal anchors (PubMed:12796775, PubMed:8805302, PubMed:8630735,
PubMed:9177355, PubMed:20619457, PubMed:18275829, PubMed:28250417,
PubMed:7694806, PubMed:8906788, PubMed:11502003, PubMed:19542454,
PubMed:12138174). {ECO:0000269|PubMed:11502003,
ECO:0000269|PubMed:12138174, ECO:0000269|PubMed:12796775,
ECO:0000269|PubMed:17079320, ECO:0000269|PubMed:18275829,
ECO:0000269|PubMed:19542454, ECO:0000269|PubMed:20619457,
ECO:0000269|PubMed:22245737, ECO:0000269|PubMed:26929325,
ECO:0000269|PubMed:2784196, ECO:0000269|PubMed:28250417,
ECO:0000269|PubMed:7694806, ECO:0000269|PubMed:7935798,
ECO:0000269|PubMed:8630735, ECO:0000269|PubMed:8805302,
ECO:0000269|PubMed:8906788, ECO:0000269|PubMed:9177355}.
-!- SUBUNIT: Heterotrimer that consists of an alpha chain HLA-A*02, a
beta chain B2M and a peptide (peptide-HLA-A*02-B2M)
(PubMed:8805302, PubMed:7694806, PubMed:7935798, PubMed:9177355,
PubMed:18275829, PubMed:22245737, PubMed:28250417,
PubMed:11502003). Early in biogenesis, HLA-A*02-B2M dimer
interacts with the components of the peptide-loading complex
composed of TAPBP, TAP1-TAP2, TAPBPL, PDIA3/ERP57 and CALR
(PubMed:21263072). Interacts with TAP1-TAP2 transporter via TAPBP;
this interaction is obligatory for the loading of peptide epitopes
delivered to the ER by TAP1-TAP2 transporter (PubMed:8805302,
PubMed:8630735, PubMed:21263072). Interacts with TAPBPL; TAPBPL
binds peptide-free HLA-A*02-B2M complexes or those loaded with low
affinity peptides, likely facilitating peptide exchange for higher
affinity peptides (PubMed:26869717). Only optimally assembled
peptide-HLA-A*02-B2M trimer translocates to the surface of
antigen-presenting cells, where it interacts with TCR and CD8
coreceptor on the surface of T cells. HLA-A*02 (via polymorphic
alpha-1 and alpha-2 domains) interacts with antigen-specific TCR
(via CDR3 domains) (PubMed:22245737, PubMed:12796775,
PubMed:18275829). One HLA-A*02 molecule (mainly via nonpolymorphic
alpha-3 domain) interacts with one CD8A homodimer (via CDR-like
loop); this interaction insures peptide-HLA-A*02-B2M recognition
by CD8-positive T cells only (PubMed:9177355, PubMed:2784196).
{ECO:0000269|PubMed:11502003, ECO:0000269|PubMed:12796775,
ECO:0000269|PubMed:18275829, ECO:0000269|PubMed:21263072,
ECO:0000269|PubMed:22245737, ECO:0000269|PubMed:26869717,
ECO:0000269|PubMed:2784196, ECO:0000269|PubMed:28250417,
ECO:0000269|PubMed:7694806, ECO:0000269|PubMed:7935798,
ECO:0000269|PubMed:8630735, ECO:0000269|PubMed:8805302,
ECO:0000269|PubMed:9177355}.
-!- SUBUNIT: (Microbial infection) Interacts with HHV-8 MIR1 protein.
{ECO:0000269|PubMed:12006494}.
-!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 accessory
protein p12I. {ECO:0000269|PubMed:11390610}.
-!- INTERACTION:
P61769:B2M; NbExp=19; IntAct=EBI-2839473, EBI-714718;
O15533:TAPBP; NbExp=10; IntAct=EBI-2839473, EBI-874801;
Q9BX59:TAPBPL; NbExp=17; IntAct=EBI-2839473, EBI-12017416;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21263072,
ECO:0000269|PubMed:8805302}; Single-pass type I membrane protein
{ECO:0000255}. Endoplasmic reticulum membrane
{ECO:0000305|PubMed:8805302}; Single-pass type I membrane protein
{ECO:0000255}.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000305}.
-!- INDUCTION: Up-regulated by IFNG, and proinflammatory cytokines
IL1B and TNF. {ECO:0000269|PubMed:21263072,
ECO:0000269|PubMed:22245737}.
-!- DOMAIN: The alpha-1 domain is a structural part of the peptide-
binding cleft. {ECO:0000269|PubMed:19542454,
ECO:0000269|PubMed:20619457, ECO:0000269|PubMed:22245737,
ECO:0000269|PubMed:2784196, ECO:0000269|PubMed:7694806,
ECO:0000269|PubMed:8906788}.
-!- DOMAIN: The alpha-2 domain is a structural part of the peptide-
binding cleft (PubMed:7694806, PubMed:8906788, PubMed:2784196,
PubMed:28250417, PubMed:22245737, PubMed:19542454,
PubMed:20619457). Mediates the interaction with TAP1-TAP2 complex
(PubMed:8805302). {ECO:0000269|PubMed:19542454,
ECO:0000269|PubMed:20619457, ECO:0000269|PubMed:22245737,
ECO:0000269|PubMed:2784196, ECO:0000269|PubMed:28250417,
ECO:0000269|PubMed:7694806, ECO:0000269|PubMed:8805302,
ECO:0000269|PubMed:8906788}.
-!- DOMAIN: The alpha-3 Ig-like domain mediates the interaction with
CD8 coreceptor. {ECO:0000269|PubMed:2784196}.
-!- PTM: N-linked glycosylation at ASN-110.
{ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:21263072}.
-!- PTM: (Microbial infection) Polyubiquitinated in a post ER
compartment through interaction with human herpesvirus 8 MIR1
protein. This targets the protein for rapid degradation via the
ubiquitin system. {ECO:0000269|PubMed:12006494}.
-!- POLYMORPHISM: The HLA-A*02 allele group comprises at least 825
different alleles. Polymorphic residues encode for alpha-1 and
alpha-2 domains of the peptide-binding cleft, where they
contribute to variations in peptide binding and TCR recognition
among different alleles. The sequence shown is that of HLA-
A*02:01, which represents the major allele expressed in nearly
half of the human population worldwide. {ECO:0000305}.
-!- DISEASE: Note=May act as a susceptibility gene in Diabetes
mellitus, insulin-dependent (IDDM) (PubMed:22245737,
PubMed:18802479). In a glucose-dependent way, HLA-A*02:01 may
aberrantly present the signal peptide of preproinsulin
(ALWGPDPAAA) on the surface of pancreatic beta cells to
autoreactive CD8-positive T cells, potentially driving T-cell
mediated cytotoxicity in pancreatic islets (PubMed:22245737,
PubMed:18802479). {ECO:0000269|PubMed:18802479,
ECO:0000269|PubMed:22245737}.
-!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA41022.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown extensively.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=IPD-IMGT/HLA; Note=Immuno Polymorphism
Database-ImMunoGeneTics/HLA;
URL="https://www.ebi.ac.uk/ipd/imgt/hla/";
-!- WEB RESOURCE: Name=IEDB; Note=The Immune Epitope Database;
URL="https://www.iedb.org/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X02457; CAA26297.1; -; mRNA.
EMBL; M11887; AAA52656.1; -; mRNA.
EMBL; U03862; AAA03603.1; -; mRNA.
EMBL; U03863; AAA03604.1; -; mRNA.
EMBL; Z23071; CAA80612.1; -; mRNA.
EMBL; M24042; AAA59653.1; -; mRNA.
EMBL; M84379; AAA59606.1; -; mRNA.
EMBL; X57954; CAA41022.1; ALT_SEQ; mRNA.
EMBL; X60764; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; M84377; AAA59603.1; -; mRNA.
EMBL; M84378; AAA59604.1; -; mRNA.
EMBL; M86404; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; Z27120; CAA81644.1; -; mRNA.
EMBL; Z46633; CAA86602.1; -; mRNA.
EMBL; U18930; AAA87076.1; -; mRNA.
EMBL; X96724; CAA65501.1; -; mRNA.
EMBL; D83515; BAA11935.1; -; mRNA.
EMBL; U56825; AAB17465.1; -; mRNA.
EMBL; K02883; AAA98727.1; -; Genomic_DNA.
EMBL; AH003586; AAB02120.1; -; Genomic_DNA.
EMBL; AH000042; AAA03683.2; -; Genomic_DNA.
EMBL; U02935; AAA76608.2; -; Genomic_DNA.
EMBL; AH007560; AAD23437.1; -; Genomic_DNA.
EMBL; AH007704; AAD30272.1; -; Genomic_DNA.
EMBL; AH008013; AAD45690.1; -; Genomic_DNA.
EMBL; AH008012; AAD45689.1; -; Genomic_DNA.
EMBL; AH008007; AAD45324.1; -; Genomic_DNA.
EMBL; AJ555412; CAD87771.1; -; Genomic_DNA.
PIR; B24512; HLHU10.
PIR; I37470; I37470.
PIR; I37542; I37542.
PIR; I38418; I38418.
PIR; I38442; I38442.
PIR; I38443; I38443.
PIR; I55948; HLHUA2.
PIR; I61857; I61857.
PIR; I61902; I61902.
PIR; I84448; I84448.
PDB; 1AKJ; X-ray; 2.65 A; A=25-300.
PDB; 1AO7; X-ray; 2.60 A; A=25-299.
PDB; 1AQD; X-ray; 2.45 A; C/F/I/L=127-141.
PDB; 1B0G; X-ray; 2.50 A; A/D=25-299.
PDB; 1B0R; X-ray; 2.90 A; A=25-299.
PDB; 1BD2; X-ray; 2.50 A; A=25-299.
PDB; 1DUY; X-ray; 2.15 A; A/D=25-299.
PDB; 1DUZ; X-ray; 1.80 A; A/D=25-299.
PDB; 1EEY; X-ray; 2.25 A; A/D=25-299.
PDB; 1EEZ; X-ray; 2.30 A; A/D=25-299.
PDB; 1HHG; X-ray; 2.60 A; A/D=25-299.
PDB; 1HHH; X-ray; 3.00 A; A=25-299.
PDB; 1HHI; X-ray; 2.50 A; A/D=25-299.
PDB; 1HHJ; X-ray; 2.50 A; A/D=25-299.
PDB; 1HHK; X-ray; 2.50 A; A/D=25-299.
PDB; 1HLA; X-ray; 3.50 A; A=25-294.
PDB; 1I1F; X-ray; 2.80 A; A/D=25-299.
PDB; 1I1Y; X-ray; 2.20 A; A/D=25-299.
PDB; 1I4F; X-ray; 1.40 A; A=25-299.
PDB; 1I7R; X-ray; 2.20 A; A/D=25-299.
PDB; 1I7T; X-ray; 2.80 A; A/D=25-299.
PDB; 1I7U; X-ray; 1.80 A; A/D=25-299.
PDB; 1IM3; X-ray; 2.20 A; A/E/I/M=25-299.
PDB; 1JF1; X-ray; 1.85 A; A=25-299.
PDB; 1JHT; X-ray; 2.15 A; A=25-299.
PDB; 1LP9; X-ray; 2.00 A; A/H=25-299.
PDB; 1OGA; X-ray; 1.40 A; A=25-300.
PDB; 1P7Q; X-ray; 3.40 A; A=25-300.
PDB; 1QEW; X-ray; 2.20 A; A=25-299.
PDB; 1QR1; X-ray; 2.40 A; A/D=25-299.
PDB; 1QRN; X-ray; 2.80 A; A=25-298.
PDB; 1QSE; X-ray; 2.80 A; A=25-298.
PDB; 1QSF; X-ray; 2.80 A; A=25-298.
PDB; 1S8D; X-ray; 2.20 A; A=25-299.
PDB; 1S9W; X-ray; 2.20 A; A=25-298.
PDB; 1S9X; X-ray; 2.50 A; A=25-298.
PDB; 1S9Y; X-ray; 2.30 A; A=25-298.
PDB; 1T1W; X-ray; 2.20 A; A=25-299.
PDB; 1T1X; X-ray; 2.20 A; A=25-299.
PDB; 1T1Y; X-ray; 2.00 A; A=25-299.
PDB; 1T1Z; X-ray; 1.90 A; A=25-299.
PDB; 1T20; X-ray; 2.20 A; A=25-299.
PDB; 1T21; X-ray; 2.19 A; A=25-299.
PDB; 1T22; X-ray; 2.20 A; A=25-299.
PDB; 1TVB; X-ray; 1.80 A; A/D=25-299.
PDB; 1TVH; X-ray; 1.80 A; A/D=25-299.
PDB; 1UR7; Model; -; A=25-299.
PDB; 2AV1; X-ray; 1.95 A; A/D=25-299.
PDB; 2AV7; X-ray; 2.05 A; A/D=25-299.
PDB; 2BNQ; X-ray; 1.70 A; A=25-300.
PDB; 2BNR; X-ray; 1.90 A; A=25-300.
PDB; 2C7U; X-ray; 2.38 A; A/D=25-300.
PDB; 2CLR; X-ray; 2.00 A; A/D=25-299.
PDB; 2F53; X-ray; 2.10 A; A=25-299.
PDB; 2F54; X-ray; 2.70 A; A/F=25-298.
PDB; 2GIT; X-ray; 1.70 A; A/D=25-299.
PDB; 2GJ6; X-ray; 2.56 A; A=25-299.
PDB; 2GT9; X-ray; 1.75 A; A/D=25-299.
PDB; 2GTW; X-ray; 1.55 A; A/D=25-299.
PDB; 2GTZ; X-ray; 1.70 A; A/D=25-299.
PDB; 2GUO; X-ray; 1.90 A; A/D=25-299.
PDB; 2J8U; X-ray; 2.88 A; A/H=25-299.
PDB; 2JCC; X-ray; 2.50 A; A/H=25-299.
PDB; 2P5E; X-ray; 1.89 A; A=25-300.
PDB; 2P5W; X-ray; 2.20 A; A=25-300.
PDB; 2PYE; X-ray; 2.30 A; A=25-300.
PDB; 2UWE; X-ray; 2.40 A; A/H=25-299.
PDB; 2V2W; X-ray; 1.60 A; A/D=25-300.
PDB; 2V2X; X-ray; 1.60 A; A/D=25-300.
PDB; 2VLJ; X-ray; 2.40 A; A=25-300.
PDB; 2VLK; X-ray; 2.50 A; A=25-300.
PDB; 2VLL; X-ray; 1.60 A; A/D=25-300.
PDB; 2VLR; X-ray; 2.30 A; A/F=25-300.
PDB; 2X4N; X-ray; 2.34 A; A/D=25-299.
PDB; 2X4O; X-ray; 2.30 A; A/D=25-299.
PDB; 2X4P; X-ray; 2.30 A; A/D=25-299.
PDB; 2X4Q; X-ray; 1.90 A; A/D=25-299.
PDB; 2X4R; X-ray; 2.30 A; A/D=25-299.
PDB; 2X4S; X-ray; 2.55 A; A/D=25-299.
PDB; 2X4T; X-ray; 2.30 A; A/D=25-299.
PDB; 2X4U; X-ray; 2.10 A; A/D=25-299.
PDB; 2X70; X-ray; 2.00 A; A/D=25-299.
PDB; 3BGM; X-ray; 1.60 A; A=25-298.
PDB; 3BH8; X-ray; 1.65 A; A=25-298.
PDB; 3BH9; X-ray; 1.70 A; A=25-299.
PDB; 3BHB; X-ray; 2.20 A; A=25-298.
PDB; 3D25; X-ray; 1.30 A; A=25-298.
PDB; 3D39; X-ray; 2.81 A; A=25-299.
PDB; 3D3V; X-ray; 2.80 A; A=25-299.
PDB; 3FQN; X-ray; 1.65 A; A=25-299.
PDB; 3FQR; X-ray; 1.70 A; A=25-299.
PDB; 3FQT; X-ray; 1.80 A; A=25-299.
PDB; 3FQU; X-ray; 1.80 A; A=25-299.
PDB; 3FQW; X-ray; 1.93 A; A=25-299.
PDB; 3FQX; X-ray; 1.70 A; A=25-299.
PDB; 3FT2; X-ray; 1.80 A; A=25-299.
PDB; 3FT3; X-ray; 1.95 A; A=25-299.
PDB; 3FT4; X-ray; 1.90 A; A=25-299.
PDB; 3GIV; X-ray; 2.00 A; A/D=25-299.
PDB; 3GJF; X-ray; 1.90 A; A/D=25-300.
PDB; 3GSN; X-ray; 2.80 A; H=25-298.
PDB; 3GSO; X-ray; 1.60 A; A=25-298.
PDB; 3GSQ; X-ray; 2.12 A; A=25-298.
PDB; 3GSR; X-ray; 1.95 A; A=25-298.
PDB; 3GSU; X-ray; 1.80 A; A=25-299.
PDB; 3GSV; X-ray; 1.90 A; A=25-299.
PDB; 3GSW; X-ray; 1.81 A; A=25-298.
PDB; 3GSX; X-ray; 2.10 A; A=25-298.
PDB; 3H7B; X-ray; 1.88 A; A/D=25-299.
PDB; 3H9H; X-ray; 2.00 A; A/D=25-299.
PDB; 3H9S; X-ray; 2.70 A; A=25-299.
PDB; 3HAE; X-ray; 2.90 A; A/D/J/P=25-300.
PDB; 3HLA; X-ray; 2.60 A; A=25-294.
PDB; 3HPJ; X-ray; 2.00 A; A/D=25-299.
PDB; 3I6G; X-ray; 2.20 A; A/D=25-299.
PDB; 3I6K; X-ray; 2.80 A; A/E=25-299.
PDB; 3IXA; X-ray; 2.10 A; A/D=25-299.
PDB; 3KLA; X-ray; 1.65 A; A/D=25-299.
PDB; 3MGO; X-ray; 2.30 A; A/D/G/J=25-299.
PDB; 3MGT; X-ray; 2.20 A; A/D/G/J=25-299.
PDB; 3MR9; X-ray; 1.93 A; A=25-300.
PDB; 3MRB; X-ray; 1.40 A; A=25-300.
PDB; 3MRC; X-ray; 1.80 A; A=25-300.
PDB; 3MRD; X-ray; 1.70 A; A=25-300.
PDB; 3MRE; X-ray; 1.10 A; A=25-300.
PDB; 3MRF; X-ray; 2.30 A; A=25-300.
PDB; 3MRG; X-ray; 1.30 A; A=25-300.
PDB; 3MRH; X-ray; 2.40 A; A=25-300.
PDB; 3MRI; X-ray; 2.10 A; A=25-300.
PDB; 3MRJ; X-ray; 1.87 A; A=25-300.
PDB; 3MRK; X-ray; 1.40 A; A=25-300.
PDB; 3MRL; X-ray; 2.41 A; A=25-300.
PDB; 3MRM; X-ray; 1.90 A; A=25-300.
PDB; 3MRN; X-ray; 2.30 A; A=25-300.
PDB; 3MRO; X-ray; 2.35 A; A=25-300.
PDB; 3MRP; X-ray; 2.10 A; A=25-300.
PDB; 3MRQ; X-ray; 2.20 A; A=25-300.
PDB; 3MRR; X-ray; 1.60 A; A=25-300.
PDB; 3MYJ; X-ray; 1.89 A; A/D=25-299.
PDB; 3O3A; X-ray; 1.80 A; A/D=25-299.
PDB; 3O3B; X-ray; 1.90 A; A/D=25-299.
PDB; 3O3D; X-ray; 1.70 A; A/D=25-299.
PDB; 3O3E; X-ray; 1.85 A; A/D=25-299.
PDB; 3O4L; X-ray; 2.54 A; A=25-300.
PDB; 3PWJ; X-ray; 1.70 A; A/D=25-299.
PDB; 3PWL; X-ray; 1.65 A; A/D=25-299.
PDB; 3PWN; X-ray; 1.60 A; A/D=25-299.
PDB; 3PWP; X-ray; 2.69 A; A=25-299.
PDB; 3QDG; X-ray; 2.69 A; A=25-299.
PDB; 3QDJ; X-ray; 2.30 A; A=25-299.
PDB; 3QDM; X-ray; 2.80 A; A=25-299.
PDB; 3QEQ; X-ray; 2.59 A; A=25-299.
PDB; 3QFD; X-ray; 1.68 A; A/D=25-299.
PDB; 3QFJ; X-ray; 2.29 A; A=25-299.
PDB; 3REW; X-ray; 1.90 A; A/D=25-299.
PDB; 3TO2; X-ray; 2.60 A; A=25-299.
PDB; 3UTQ; X-ray; 1.67 A; A=25-300.
PDB; 3UTS; X-ray; 2.71 A; A/F=25-300.
PDB; 3UTT; X-ray; 2.60 A; A/F=25-299.
PDB; 3V5D; X-ray; 2.00 A; A/D=25-299.
PDB; 3V5H; X-ray; 1.63 A; A/D=25-299.
PDB; 3V5K; X-ray; 2.31 A; A/D=25-299.
PDB; 4E5X; X-ray; 1.95 A; A/D=25-299.
PDB; 4EMZ; X-ray; 2.90 A; D/E=338-365.
PDB; 4EN2; X-ray; 2.58 A; D/E=338-365.
PDB; 4EUP; X-ray; 2.88 A; A/D=25-299.
PDB; 4FTV; X-ray; 2.74 A; A=25-299.
PDB; 4GKN; X-ray; 2.75 A; A/D=25-300.
PDB; 4GKS; X-ray; 2.35 A; A/D=25-300.
PDB; 4I4W; X-ray; 1.77 A; A=25-300.
PDB; 4JFD; X-ray; 2.46 A; A=25-300.
PDB; 4JFE; X-ray; 2.70 A; A=25-300.
PDB; 4JFF; X-ray; 2.43 A; A=25-300.
PDB; 4JFO; X-ray; 2.11 A; A/D=25-299.
PDB; 4JFP; X-ray; 1.91 A; A/D=25-300.
PDB; 4JFQ; X-ray; 1.90 A; A/D=25-300.
PDB; 4K7F; X-ray; 2.00 A; A/D=25-299.
PDB; 4L29; X-ray; 3.09 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y/a=25-300.
PDB; 4L3C; X-ray; 2.64 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y/a=25-300.
PDB; 4L3E; X-ray; 2.56 A; A=25-299.
PDB; 4MNQ; X-ray; 2.74 A; A=25-300.
PDB; 4NNX; X-ray; 2.10 A; A=25-298.
PDB; 4NNY; X-ray; 1.90 A; A=25-298.
PDB; 4NO0; X-ray; 2.70 A; A=25-300.
PDB; 4NO2; X-ray; 2.00 A; A=25-298.
PDB; 4NO3; X-ray; 1.70 A; A=25-298.
PDB; 4NO5; X-ray; 2.10 A; A=25-299.
PDB; 4OV5; X-ray; 2.20 A; C/F/I/L/O/R=128-141.
PDB; 4QOK; X-ray; 3.00 A; A=25-300.
PDB; 4U6X; X-ray; 1.68 A; A=25-300.
PDB; 4U6Y; X-ray; 1.47 A; A=25-300.
PDB; 4UQ3; X-ray; 2.10 A; A/C=25-299.
PDB; 4WJ5; X-ray; 1.65 A; A/D=25-299.
PDB; 4WUU; X-ray; 3.05 A; A=25-300.
PDB; 5C07; X-ray; 2.11 A; A/F=25-300.
PDB; 5C08; X-ray; 2.33 A; A/F=25-300.
PDB; 5C09; X-ray; 2.48 A; A/F=25-300.
PDB; 5C0A; X-ray; 2.46 A; A/F=25-300.
PDB; 5C0B; X-ray; 2.03 A; A/F=25-299.
PDB; 5C0C; X-ray; 1.97 A; A/F=25-300.
PDB; 5C0D; X-ray; 1.68 A; A=25-300.
PDB; 5C0E; X-ray; 1.49 A; A=25-300.
PDB; 5C0F; X-ray; 1.46 A; A=25-300.
PDB; 5C0G; X-ray; 1.37 A; A=25-300.
PDB; 5C0I; X-ray; 1.53 A; A=25-300.
PDB; 5C0J; X-ray; 1.64 A; A=25-300.
PDB; 5D2L; X-ray; 3.51 A; A/C/G/M=25-299.
PDB; 5D2N; X-ray; 2.10 A; A/H=25-299.
PDB; 5D9S; X-ray; 1.87 A; A=25-298.
PDB; 5DDH; X-ray; 1.50 A; A=25-298.
PDB; 5E00; X-ray; 1.70 A; A=25-299.
PDB; 5E6I; X-ray; 4.00 A; C/I/M/R=25-299.
PDB; 5E9D; X-ray; 2.51 A; A/F=25-299.
PDB; 5ENW; X-ray; 1.85 A; A=25-298.
PDB; 5EOT; X-ray; 2.10 A; A=26-298.
PDB; 5EU3; X-ray; 1.97 A; A=25-300.
PDB; 5EU4; X-ray; 2.12 A; A/D=25-300.
PDB; 5EU5; X-ray; 1.54 A; A=25-300.
PDB; 5EU6; X-ray; 2.02 A; A=25-300.
PDB; 5EUO; X-ray; 2.10 A; A/C=25-299.
PDB; 5F7D; X-ray; 2.30 A; A=26-298.
PDB; 5F9J; X-ray; 2.51 A; A=25-298.
PDB; 5FA3; X-ray; 1.86 A; A=26-298.
PDB; 5FA4; X-ray; 2.40 A; A=25-298.
PDB; 5FDW; X-ray; 2.70 A; A=25-298.
PDB; 5HHM; X-ray; 2.50 A; A/F=25-300.
PDB; 5HHN; X-ray; 2.03 A; A=25-298.
PDB; 5HHO; X-ray; 2.95 A; A=25-300.
PDB; 5HHP; X-ray; 1.90 A; A=25-298.
PDB; 5HHQ; X-ray; 2.10 A; A=25-298.
PDB; 5HYJ; X-ray; 3.06 A; A/F=25-300.
PDB; 5IRO; X-ray; 2.64 A; A/E/I/M/Q/U=25-299.
PDB; 5ISZ; X-ray; 2.06 A; A=25-299.
PDB; 5JHD; X-ray; 2.46 A; A/F=25-299.
PDB; 5JZI; X-ray; 2.50 A; A/F=25-299.
PDB; 5MEN; X-ray; 2.81 A; A=25-300.
PDB; 5MEO; X-ray; 1.77 A; A=25-300.
PDB; 5MEP; X-ray; 2.71 A; A/D=25-300.
PDB; 5MEQ; X-ray; 2.27 A; A=25-300.
PDB; 5MER; X-ray; 1.88 A; A/D=25-300.
PDB; 5N1Y; X-ray; 1.39 A; A=25-300.
PDB; 5N6B; X-ray; 1.71 A; A/D=25-300.
PDB; 5NHT; X-ray; 3.20 A; H=25-300.
PDB; 5NME; X-ray; 2.94 A; A/F=25-300.
PDB; 5NMF; X-ray; 2.89 A; A/F=25-300.
PDB; 5NMG; X-ray; 2.75 A; A/F=25-300.
PDB; 5NMH; X-ray; 1.55 A; A=25-300.
PDB; 5NMK; X-ray; 1.66 A; A=25-300.
PDB; 5NQK; X-ray; 3.25 A; H=25-300.
PDB; 5SWQ; X-ray; 2.00 A; A=25-300.
PDB; 5TEZ; X-ray; 1.70 A; A=25-299.
PDB; 5W1W; X-ray; 3.10 A; C/H/M/R=3-11.
PDB; 5WSH; X-ray; 2.00 A; A=25-299.
PDB; 5YXN; X-ray; 2.03 A; C=25-299.
PDB; 5YXU; X-ray; 2.70 A; C/E=25-299.
PDB; 6AM5; X-ray; 2.39 A; A=25-299.
PDB; 6AMT; X-ray; 2.50 A; A/D=25-299.
PDB; 6AMU; X-ray; 2.15 A; A=26-298.
PDB; 6APN; X-ray; 2.22 A; A/B=26-301.
PDB; 6D78; X-ray; 2.35 A; A=25-299.
PDB; 6D7G; X-ray; 2.75 A; A=25-299.
PDB; 6DKP; X-ray; 2.97 A; A=25-299.
PDB; 6EQA; X-ray; 3.16 A; A=25-300.
PDB; 6EQB; X-ray; 2.81 A; A=25-300.
PDB; 6EWA; X-ray; 2.39 A; A/E=25-300.
PDB; 6EWC; X-ray; 3.20 A; A/E=25-300.
PDB; 6EWO; X-ray; 2.30 A; A/E=25-300.
PDB; 6G3J; X-ray; 2.45 A; A/D=25-300.
PDBsum; 1AKJ; -.
PDBsum; 1AO7; -.
PDBsum; 1AQD; -.
PDBsum; 1B0G; -.
PDBsum; 1B0R; -.
PDBsum; 1BD2; -.
PDBsum; 1DUY; -.
PDBsum; 1DUZ; -.
PDBsum; 1EEY; -.
PDBsum; 1EEZ; -.
PDBsum; 1HHG; -.
PDBsum; 1HHH; -.
PDBsum; 1HHI; -.
PDBsum; 1HHJ; -.
PDBsum; 1HHK; -.
PDBsum; 1HLA; -.
PDBsum; 1I1F; -.
PDBsum; 1I1Y; -.
PDBsum; 1I4F; -.
PDBsum; 1I7R; -.
PDBsum; 1I7T; -.
PDBsum; 1I7U; -.
PDBsum; 1IM3; -.
PDBsum; 1JF1; -.
PDBsum; 1JHT; -.
PDBsum; 1LP9; -.
PDBsum; 1OGA; -.
PDBsum; 1P7Q; -.
PDBsum; 1QEW; -.
PDBsum; 1QR1; -.
PDBsum; 1QRN; -.
PDBsum; 1QSE; -.
PDBsum; 1QSF; -.
PDBsum; 1S8D; -.
PDBsum; 1S9W; -.
PDBsum; 1S9X; -.
PDBsum; 1S9Y; -.
PDBsum; 1T1W; -.
PDBsum; 1T1X; -.
PDBsum; 1T1Y; -.
PDBsum; 1T1Z; -.
PDBsum; 1T20; -.
PDBsum; 1T21; -.
PDBsum; 1T22; -.
PDBsum; 1TVB; -.
PDBsum; 1TVH; -.
PDBsum; 1UR7; -.
PDBsum; 2AV1; -.
PDBsum; 2AV7; -.
PDBsum; 2BNQ; -.
PDBsum; 2BNR; -.
PDBsum; 2C7U; -.
PDBsum; 2CLR; -.
PDBsum; 2F53; -.
PDBsum; 2F54; -.
PDBsum; 2GIT; -.
PDBsum; 2GJ6; -.
PDBsum; 2GT9; -.
PDBsum; 2GTW; -.
PDBsum; 2GTZ; -.
PDBsum; 2GUO; -.
PDBsum; 2J8U; -.
PDBsum; 2JCC; -.
PDBsum; 2P5E; -.
PDBsum; 2P5W; -.
PDBsum; 2PYE; -.
PDBsum; 2UWE; -.
PDBsum; 2V2W; -.
PDBsum; 2V2X; -.
PDBsum; 2VLJ; -.
PDBsum; 2VLK; -.
PDBsum; 2VLL; -.
PDBsum; 2VLR; -.
PDBsum; 2X4N; -.
PDBsum; 2X4O; -.
PDBsum; 2X4P; -.
PDBsum; 2X4Q; -.
PDBsum; 2X4R; -.
PDBsum; 2X4S; -.
PDBsum; 2X4T; -.
PDBsum; 2X4U; -.
PDBsum; 2X70; -.
PDBsum; 3BGM; -.
PDBsum; 3BH8; -.
PDBsum; 3BH9; -.
PDBsum; 3BHB; -.
PDBsum; 3D25; -.
PDBsum; 3D39; -.
PDBsum; 3D3V; -.
PDBsum; 3FQN; -.
PDBsum; 3FQR; -.
PDBsum; 3FQT; -.
PDBsum; 3FQU; -.
PDBsum; 3FQW; -.
PDBsum; 3FQX; -.
PDBsum; 3FT2; -.
PDBsum; 3FT3; -.
PDBsum; 3FT4; -.
PDBsum; 3GIV; -.
PDBsum; 3GJF; -.
PDBsum; 3GSN; -.
PDBsum; 3GSO; -.
PDBsum; 3GSQ; -.
PDBsum; 3GSR; -.
PDBsum; 3GSU; -.
PDBsum; 3GSV; -.
PDBsum; 3GSW; -.
PDBsum; 3GSX; -.
PDBsum; 3H7B; -.
PDBsum; 3H9H; -.
PDBsum; 3H9S; -.
PDBsum; 3HAE; -.
PDBsum; 3HLA; -.
PDBsum; 3HPJ; -.
PDBsum; 3I6G; -.
PDBsum; 3I6K; -.
PDBsum; 3IXA; -.
PDBsum; 3KLA; -.
PDBsum; 3MGO; -.
PDBsum; 3MGT; -.
PDBsum; 3MR9; -.
PDBsum; 3MRB; -.
PDBsum; 3MRC; -.
PDBsum; 3MRD; -.
PDBsum; 3MRE; -.
PDBsum; 3MRF; -.
PDBsum; 3MRG; -.
PDBsum; 3MRH; -.
PDBsum; 3MRI; -.
PDBsum; 3MRJ; -.
PDBsum; 3MRK; -.
PDBsum; 3MRL; -.
PDBsum; 3MRM; -.
PDBsum; 3MRN; -.
PDBsum; 3MRO; -.
PDBsum; 3MRP; -.
PDBsum; 3MRQ; -.
PDBsum; 3MRR; -.
PDBsum; 3MYJ; -.
PDBsum; 3O3A; -.
PDBsum; 3O3B; -.
PDBsum; 3O3D; -.
PDBsum; 3O3E; -.
PDBsum; 3O4L; -.
PDBsum; 3PWJ; -.
PDBsum; 3PWL; -.
PDBsum; 3PWN; -.
PDBsum; 3PWP; -.
PDBsum; 3QDG; -.
PDBsum; 3QDJ; -.
PDBsum; 3QDM; -.
PDBsum; 3QEQ; -.
PDBsum; 3QFD; -.
PDBsum; 3QFJ; -.
PDBsum; 3REW; -.
PDBsum; 3TO2; -.
PDBsum; 3UTQ; -.
PDBsum; 3UTS; -.
PDBsum; 3UTT; -.
PDBsum; 3V5D; -.
PDBsum; 3V5H; -.
PDBsum; 3V5K; -.
PDBsum; 4E5X; -.
PDBsum; 4EMZ; -.
PDBsum; 4EN2; -.
PDBsum; 4EUP; -.
PDBsum; 4FTV; -.
PDBsum; 4GKN; -.
PDBsum; 4GKS; -.
PDBsum; 4I4W; -.
PDBsum; 4JFD; -.
PDBsum; 4JFE; -.
PDBsum; 4JFF; -.
PDBsum; 4JFO; -.
PDBsum; 4JFP; -.
PDBsum; 4JFQ; -.
PDBsum; 4K7F; -.
PDBsum; 4L29; -.
PDBsum; 4L3C; -.
PDBsum; 4L3E; -.
PDBsum; 4MNQ; -.
PDBsum; 4NNX; -.
PDBsum; 4NNY; -.
PDBsum; 4NO0; -.
PDBsum; 4NO2; -.
PDBsum; 4NO3; -.
PDBsum; 4NO5; -.
PDBsum; 4OV5; -.
PDBsum; 4QOK; -.
PDBsum; 4U6X; -.
PDBsum; 4U6Y; -.
PDBsum; 4UQ3; -.
PDBsum; 4WJ5; -.
PDBsum; 4WUU; -.
PDBsum; 5C07; -.
PDBsum; 5C08; -.
PDBsum; 5C09; -.
PDBsum; 5C0A; -.
PDBsum; 5C0B; -.
PDBsum; 5C0C; -.
PDBsum; 5C0D; -.
PDBsum; 5C0E; -.
PDBsum; 5C0F; -.
PDBsum; 5C0G; -.
PDBsum; 5C0I; -.
PDBsum; 5C0J; -.
PDBsum; 5D2L; -.
PDBsum; 5D2N; -.
PDBsum; 5D9S; -.
PDBsum; 5DDH; -.
PDBsum; 5E00; -.
PDBsum; 5E6I; -.
PDBsum; 5E9D; -.
PDBsum; 5ENW; -.
PDBsum; 5EOT; -.
PDBsum; 5EU3; -.
PDBsum; 5EU4; -.
PDBsum; 5EU5; -.
PDBsum; 5EU6; -.
PDBsum; 5EUO; -.
PDBsum; 5F7D; -.
PDBsum; 5F9J; -.
PDBsum; 5FA3; -.
PDBsum; 5FA4; -.
PDBsum; 5FDW; -.
PDBsum; 5HHM; -.
PDBsum; 5HHN; -.
PDBsum; 5HHO; -.
PDBsum; 5HHP; -.
PDBsum; 5HHQ; -.
PDBsum; 5HYJ; -.
PDBsum; 5IRO; -.
PDBsum; 5ISZ; -.
PDBsum; 5JHD; -.
PDBsum; 5JZI; -.
PDBsum; 5MEN; -.
PDBsum; 5MEO; -.
PDBsum; 5MEP; -.
PDBsum; 5MEQ; -.
PDBsum; 5MER; -.
PDBsum; 5N1Y; -.
PDBsum; 5N6B; -.
PDBsum; 5NHT; -.
PDBsum; 5NME; -.
PDBsum; 5NMF; -.
PDBsum; 5NMG; -.
PDBsum; 5NMH; -.
PDBsum; 5NMK; -.
PDBsum; 5NQK; -.
PDBsum; 5SWQ; -.
PDBsum; 5TEZ; -.
PDBsum; 5W1W; -.
PDBsum; 5WSH; -.
PDBsum; 5YXN; -.
PDBsum; 5YXU; -.
PDBsum; 6AM5; -.
PDBsum; 6AMT; -.
PDBsum; 6AMU; -.
PDBsum; 6APN; -.
PDBsum; 6D78; -.
PDBsum; 6D7G; -.
PDBsum; 6DKP; -.
PDBsum; 6EQA; -.
PDBsum; 6EQB; -.
PDBsum; 6EWA; -.
PDBsum; 6EWC; -.
PDBsum; 6EWO; -.
PDBsum; 6G3J; -.
SMR; P01892; -.
BioGrid; 109350; 101.
IntAct; P01892; 33.
MINT; P01892; -.
DrugBank; DB02740; 3-Indolebutyric Acid.
GlyConnect; 1319; -.
iPTMnet; P01892; -.
PhosphoSitePlus; P01892; -.
SwissPalm; P01892; -.
BioMuta; HLA-A; -.
DMDM; 122138; -.
EPD; P01892; -.
jPOST; P01892; -.
PeptideAtlas; P01892; -.
PRIDE; P01892; -.
ProteomicsDB; 51506; -.
ABCD; P01892; -.
Ensembl; ENST00000457879; ENSP00000403575; ENSG00000235657.
Ensembl; ENST00000547271; ENSP00000447962; ENSG00000235657.
Ensembl; ENST00000547522; ENSP00000448077; ENSG00000227715.
DisGeNET; 3105; -.
GeneCards; HLA-A; -.
HGNC; HGNC:4931; HLA-A.
MalaCards; HLA-A; -.
MIM; 142800; gene.
neXtProt; NX_P01892; -.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236977; Endosomal/Vacuolar pathway.
Reactome; R-HSA-164940; Nef mediated downregulation of MHC class I complex cell surface expression.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
SIGNOR; P01892; -.
ChiTaRS; HLA-A; human.
EvolutionaryTrace; P01892; -.
Proteomes; UP000005640; Chromosome 6.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005797; C:Golgi medial cisterna; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0042824; C:MHC class I peptide loading complex; IDA:UniProtKB.
GO; GO:0042612; C:MHC class I protein complex; IDA:UniProtKB.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
GO; GO:0030881; F:beta-2-microglobulin binding; IDA:UniProtKB.
GO; GO:0042610; F:CD8 receptor binding; IDA:UniProtKB.
GO; GO:0042605; F:peptide antigen binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
GO; GO:0042608; F:T cell receptor binding; IDA:UniProtKB.
GO; GO:0046977; F:TAP binding; IDA:UniProtKB.
GO; GO:0062061; F:TAP complex binding; IDA:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IDA:BHF-UCL.
GO; GO:0002485; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent; IMP:UniProtKB.
GO; GO:0002486; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent; IDA:UniProtKB.
GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; IDA:UniProtKB.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome.
GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
GO; GO:0036037; P:CD8-positive, alpha-beta T cell activation; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:2001187; P:positive regulation of CD8-positive, alpha-beta T cell activation; IDA:BHF-UCL.
GO; GO:2000566; P:positive regulation of CD8-positive, alpha-beta T cell proliferation; IDA:UniProtKB.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:2000568; P:positive regulation of memory T cell activation; IDA:UniProtKB.
GO; GO:0002726; P:positive regulation of T cell cytokine production; IDA:BHF-UCL.
GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:UniProtKB.
GO; GO:0051290; P:protein heterotetramerization; IDA:CAFA.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.30.500.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
InterPro; IPR011161; MHC_I-like_Ag-recog.
InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
InterPro; IPR011162; MHC_I/II-like_Ag-recog.
InterPro; IPR001039; MHC_I_a_a1/a2.
InterPro; IPR010579; MHC_I_a_C.
Pfam; PF07654; C1-set; 1.
Pfam; PF00129; MHC_I; 1.
Pfam; PF06623; MHC_I_C; 1.
PRINTS; PR01638; MHCCLASSI.
SMART; SM00407; IGc1; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF54452; SSF54452; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Cell membrane; Complete proteome;
Diabetes mellitus; Direct protein sequencing; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Host-virus interaction; Immunity;
Membrane; MHC I; Phosphoprotein; Polymorphism; Reference proteome;
Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 24 {ECO:0000269|PubMed:92029}.
CHAIN 25 365 HLA class I histocompatibility antigen,
A-2 alpha chain.
/FTId=PRO_0000018814.
TOPO_DOM 25 308 Extracellular. {ECO:0000255}.
TRANSMEM 309 332 Helical. {ECO:0000255}.
TOPO_DOM 333 365 Cytoplasmic. {ECO:0000255}.
DOMAIN 209 295 Ig-like C1-type. {ECO:0000255}.
REGION 25 114 Alpha-1. {ECO:0000255}.
REGION 115 206 Alpha-2. {ECO:0000255}.
REGION 207 298 Alpha-3. {ECO:0000255}.
REGION 299 308 Connecting peptide. {ECO:0000255}.
BINDING 31 31 Self- and pathogen-derived peptide
antigen. {ECO:0000269|PubMed:20619457,
ECO:0000269|PubMed:7694806}.
BINDING 87 87 Pathogen-derived peptide antigen.
{ECO:0000269|PubMed:7694806}.
BINDING 89 89 Pathogen-derived peptide antigen.
{ECO:0000269|PubMed:7694806,
ECO:0000269|PubMed:9177355}.
BINDING 90 90 Self- and pathogen-derived peptide
antigen. {ECO:0000269|PubMed:22245737,
ECO:0000269|PubMed:7694806}.
BINDING 101 101 Pathogen-derived peptide antigen.
{ECO:0000269|PubMed:19542454}.
BINDING 108 108 Self- and pathogen-derived peptide
antigen. {ECO:0000269|PubMed:11502003,
ECO:0000269|PubMed:20619457,
ECO:0000269|PubMed:22245737,
ECO:0000269|PubMed:7694806}.
BINDING 123 123 Self-peptide antigen.
{ECO:0000269|PubMed:7935798}.
BINDING 166 166 Self- and pathogen-derived peptide
antigen. {ECO:0000269|PubMed:11502003,
ECO:0000269|PubMed:19542454,
ECO:0000269|PubMed:20619457,
ECO:0000269|PubMed:22245737,
ECO:0000269|PubMed:28250417,
ECO:0000269|PubMed:7694806,
ECO:0000269|PubMed:8906788}.
BINDING 170 170 Self- and pathogen-derived peptide
antigen. {ECO:0000269|PubMed:20619457,
ECO:0000269|PubMed:28250417}.
BINDING 171 171 Self- and pathogen-derived peptide
antigen. {ECO:0000269|PubMed:20619457,
ECO:0000269|PubMed:22245737,
ECO:0000269|PubMed:8906788}.
BINDING 183 183 Self- and pathogen-derived peptide
antigen. {ECO:0000269|PubMed:11502003,
ECO:0000269|PubMed:19542454,
ECO:0000269|PubMed:20619457,
ECO:0000269|PubMed:22245737,
ECO:0000269|PubMed:28250417,
ECO:0000269|PubMed:7694806,
ECO:0000269|PubMed:7935798,
ECO:0000269|PubMed:9177355}.
BINDING 195 195 Self- and pathogen-derived peptide
antigen. {ECO:0000269|PubMed:11502003,
ECO:0000269|PubMed:19542454,
ECO:0000269|PubMed:20619457,
ECO:0000269|PubMed:22245737,
ECO:0000269|PubMed:28250417,
ECO:0000269|PubMed:7694806,
ECO:0000269|PubMed:7935798,
ECO:0000269|PubMed:8906788}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000250|UniProtKB:P18462}.
MOD_RES 344 344 Phosphotyrosine.
{ECO:0000250|UniProtKB:P18462}.
MOD_RES 345 345 Phosphoserine.
{ECO:0000250|UniProtKB:P18462}.
MOD_RES 349 349 Phosphoserine.
{ECO:0000250|UniProtKB:P18462}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 356 356 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 359 359 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 125 188 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:28250417,
ECO:0000269|PubMed:7694806}.
DISULFID 227 283 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:28250417,
ECO:0000269|PubMed:7694806}.
VARIANT 33 33 F -> Y (in allele A*02:05, allele
A*02:06, allele A*02:08, allele A*02:10
and allele A*02:21; dbSNP:rs2075684).
/FTId=VAR_004334.
VARIANT 54 54 D -> N (in allele A*02:21;
dbSNP:rs41549215).
/FTId=VAR_004335.
VARIANT 65 65 A -> G (in allele A*02:31;
dbSNP:rs41557613).
/FTId=VAR_016726.
VARIANT 67 67 Q -> R (in allele A*02:02, allele A*02:05
and allele A*02:08; dbSNP:rs41559117).
/FTId=VAR_004336.
VARIANT 89 89 R -> G (polymorphism; dbSNP:rs199474430).
{ECO:0000269|PubMed:26566883}.
/FTId=VAR_076446.
VARIANT 90 90 K -> N (in allele A*02:08 and allele
A*02:20; dbSNP:rs199474436).
/FTId=VAR_004337.
VARIANT 94 94 H -> Q (in allele A*02:34 and allele
A*02:35; dbSNP:rs78306866).
/FTId=VAR_016727.
VARIANT 97 97 T -> I (in allele A*02:11;
dbSNP:rs199474457).
/FTId=VAR_004338.
VARIANT 98 98 H -> D (in allele A*02:11 and allele
A*02:35; dbSNP:rs1136683).
/FTId=VAR_016728.
VARIANT 119 119 V -> L (in allele A*02:02, allele
A*02:05, allele A*02:08 and allele
A*02:17; dbSNP:rs1071743).
/FTId=VAR_004339.
VARIANT 121 121 R -> M (in allele A*02:04 and allele
A*02:17; dbSNP:rs199474485).
/FTId=VAR_004340.
VARIANT 123 123 Y -> C (in allele A*02:07 and allele
A*02:18; dbSNP:rs1136697).
/FTId=VAR_004341.
VARIANT 123 123 Y -> F (in allele A*02:10 and allele
A*02:17; dbSNP:rs1136697).
/FTId=VAR_004342.
VARIANT 131 131 W -> G (in allele A*02:10;
dbSNP:rs1136702).
/FTId=VAR_004343.
VARIANT 162 162 M -> K (in allele A*02:18;
dbSNP:rs41549316).
/FTId=VAR_004344.
VARIANT 173 173 A -> T (in allele A*02:03;
dbSNP:rs1059526).
/FTId=VAR_004345.
VARIANT 176 176 V -> E (in allele A*02:03 and allele
A*02:13; dbSNP:rs9256983).
{ECO:0000244|PubMed:21269460,
ECO:0000244|PubMed:25944712}.
/FTId=VAR_004346.
VARIANT 180 180 L -> Q (in allele A*02:12, allele A*02:13
and allele A*02:37).
/FTId=VAR_004348.
VARIANT 180 180 L -> W (in allele A*02:02, allele
A*02:03, allele A*02:05 and allele
A*02:08; dbSNP:rs9260156).
{ECO:0000244|PubMed:21269460}.
/FTId=VAR_004347.
VARIANT 187 187 T -> E (in allele A*02:16; requires 2
nucleotide substitutions).
/FTId=VAR_004349.
VARIANT 190 190 E -> D (in allele A*02:36 and allele
A*02:37; dbSNP:rs879577815).
/FTId=VAR_016729.
VARIANT 191 191 W -> G (in allele A*02:36 and allele
A*02:37; dbSNP:rs3098019).
/FTId=VAR_016730.
VARIANT 260 260 A -> E (in allele A*02:09;
dbSNP:rs41540417).
/FTId=VAR_004350.
MUTAGEN 110 110 N->Q: Impairs the recruitment of HLA-A*02
in the peptide-loading complex.
{ECO:0000269|PubMed:21263072}.
MUTAGEN 156 156 S->C: Impairs the maturation of a
peptide-receptive HLA-A*02-B2M complex.
{ECO:0000269|PubMed:8805302}.
MUTAGEN 158 158 T->K: Impairs binding to TAP1-TAP2
transporter, resulting in impaired
presentation of intracellular peptides.
{ECO:0000269|PubMed:8630735,
ECO:0000269|PubMed:8805302}.
MUTAGEN 269 269 A->V: Impairs binding to CD8A and reduces
recognition by antigen-specific CD8-
positive T cells.
{ECO:0000269|PubMed:2784196}.
CONFLICT 115 115 G -> V (in Ref. 2; AAA52656).
{ECO:0000305}.
CONFLICT 140 140 Y -> V (in Ref. 2; AAA52656).
{ECO:0000305}.
CONFLICT 277 277 Q -> E (in Ref. 2; AAA52656).
{ECO:0000305}.
CONFLICT 318 318 F -> L (in Ref. 2; AAA52656).
{ECO:0000305}.
STRAND 27 36 {ECO:0000244|PDB:3D25}.
STRAND 41 43 {ECO:0000244|PDB:5C0G}.
STRAND 45 52 {ECO:0000244|PDB:3D25}.
STRAND 55 61 {ECO:0000244|PDB:3D25}.
STRAND 64 66 {ECO:0000244|PDB:3D25}.
STRAND 70 73 {ECO:0000244|PDB:4E5X}.
HELIX 74 78 {ECO:0000244|PDB:3D25}.
HELIX 81 108 {ECO:0000244|PDB:3D25}.
STRAND 113 115 {ECO:0000244|PDB:3D25}.
STRAND 118 127 {ECO:0000244|PDB:3D25}.
STRAND 129 131 {ECO:0000244|PDB:1B0R}.
STRAND 133 142 {ECO:0000244|PDB:3D25}.
STRAND 145 150 {ECO:0000244|PDB:3D25}.
STRAND 152 155 {ECO:0000244|PDB:6EWA}.
STRAND 157 159 {ECO:0000244|PDB:3D25}.
HELIX 162 173 {ECO:0000244|PDB:3D25}.
HELIX 176 185 {ECO:0000244|PDB:3D25}.
HELIX 187 198 {ECO:0000244|PDB:3D25}.
HELIX 200 203 {ECO:0000244|PDB:3D25}.
STRAND 210 235 {ECO:0000244|PDB:3D25}.
STRAND 238 243 {ECO:0000244|PDB:3D25}.
STRAND 246 248 {ECO:0000244|PDB:3D25}.
HELIX 249 251 {ECO:0000244|PDB:2GTW}.
STRAND 252 254 {ECO:0000244|PDB:3D25}.
STRAND 261 263 {ECO:0000244|PDB:3D25}.
STRAND 265 274 {ECO:0000244|PDB:3D25}.
STRAND 275 277 {ECO:0000244|PDB:4JFD}.
HELIX 278 280 {ECO:0000244|PDB:3D25}.
STRAND 281 286 {ECO:0000244|PDB:3D25}.
STRAND 290 292 {ECO:0000244|PDB:2V2X}.
STRAND 294 296 {ECO:0000244|PDB:3D25}.
STRAND 348 350 {ECO:0000244|PDB:4EN2}.
SEQUENCE 365 AA; 40922 MW; B54A97B24B337C08 CRC64;
MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF
DSDAASQRME PRAPWIEQEG PEYWDGETRK VKAHSQTHRV DLGTLRGYYN QSEAGSHTVQ
RMYGCDVGSD WRFLRGYHQY AYDGKDYIAL KEDLRSWTAA DMAAQTTKHK WEAAHVAEQL
RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT
WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP
SSQPTIPIVG IIAGLVLFGA VITGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDVSL
TACKV


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[HLA-A HLAA] HLA class I histocompatibility antigen, A-2 alpha chain (Human leukocyte antigen A*02) (HLA-A*02)
[HLA-A HLAA] HLA class I histocompatibility antigen, A-1 alpha chain (Human leukocyte antigen A*01) (HLA-A*01)
[HLA-A HLAA] HLA class I histocompatibility antigen, A-3 alpha chain (Human leukocyte antigen A*03) (HLA-A*03)
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[HLA-E HLA-6.2 HLAE] HLA class I histocompatibility antigen, alpha chain E (MHC class I antigen E) [Cleaved into: Soluble HLA class I histocompatibility antigen, alpha chain E (sHLA-E)]
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[HLA-DQA1] HLA class II histocompatibility antigen, DQ alpha 1 chain (DC-1 alpha chain) (DC-alpha) (HLA-DCA) (MHC class II DQA1)
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[HLA-DQB1 HLA-DQB] HLA class II histocompatibility antigen, DQ beta 1 chain (MHC class II antigen DQB1)
[HLA-DRB1 HLA-DRB2] HLA class II histocompatibility antigen, DRB1-15 beta chain (DW2.2/DR2.2) (MHC class II antigen DRB1*15)
[HLA-B HLAB] HLA class I histocompatibility antigen, B-27 alpha chain (MHC class I antigen B*27)
[HLA-DRB1] HLA class II histocompatibility antigen, DRB1-13 beta chain (MHC class II antigen DRB1*13) (DR-13) (DR13)
[HLA-DRB1] HLA class II histocompatibility antigen, DRB1-14 beta chain (MHC class II antigen DRB1*14) (DR-14) (DR14)
[HLA-DRB1] HLA class II histocompatibility antigen, DRB1-8 beta chain (MHC class II antigen DRB1*8) (DR-8) (DR8) (DRw8)
[HLA-DQB2 HLA-DXB] HLA class II histocompatibility antigen, DQ beta 2 chain (HLA class II histocompatibility antigen, DX beta chain) (MHC class II antigen DQB2)
[HLA-DRB3] HLA class II histocompatibility antigen, DR beta 3 chain (MHC class II antigen DRB3)
[HLA-DRB4] HLA class II histocompatibility antigen, DR beta 4 chain (MHC class II antigen DRB4)
[CD74 DHLAG] HLA class II histocompatibility antigen gamma chain (HLA-DR antigens-associated invariant chain) (Ia antigen-associated invariant chain) (Ii) (p33) (CD antigen CD74)
[HLA-B HLAB] HLA class I histocompatibility antigen, B-51 alpha chain (MHC class I antigen B*51)
[HLA-DRB1] HLA class II histocompatibility antigen, DRB1-1 beta chain (MHC class II antigen DRB1*1) (DR-1) (DR1)
[HLA-C HLAC] HLA class I histocompatibility antigen, Cw-5 alpha chain (MHC class I antigen Cw*5)
[HLA-DRB1] HLA class II histocompatibility antigen, DRB1-4 beta chain (MHC class II antigen DRB1*4) (DR-4) (DR4)
[HLA-DRB1] HLA class II histocompatibility antigen, DRB1-16 beta chain (MHC class II antigen DRB1*16) (DR-16) (DR16)
[HLA-DRB1] HLA class II histocompatibility antigen, DRB1-3 chain (Clone P2-beta-3) (MHC class II antigen DRB1*3)
[HLA-DRB1] HLA class II histocompatibility antigen, DRB1-12 beta chain (MHC class II antigen DRB1*12) (DR-12) (DR12)
[HLA-DRB1] HLA class II histocompatibility antigen, DRB1-9 beta chain (MHC class II antigen DRB1*9) (DR-9) (DR9)
[HLA-DRB1] HLA class II histocompatibility antigen, DRB1-10 beta chain (DRw10) (MHC class II antigen DRB1*10)
[HLA-DRB1] HLA class II histocompatibility antigen, DRB1-11 beta chain (DR-5) (DR5) (DRw11) (MHC class II antigen DRB1*11)

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[30664875] A Missense Variant in PTPN22 is a Risk Factor for Drug-induced Liver Injury.
[30201808] Phenotypic and Functional Signatures of Herpes Simplex Virus-Specific Effector Memory CD73CD45RACCR7CD8 T and CD73CD45RACCR7CD8 T Cells Are Associated with Asymptomatic Ocular Herpes.
[30115740] Identification of non-mutated neoantigens presented by TAP-deficient tumors.
[30007228] Generation of a T cell receptor (TCR)-like single domain antibody (sDAb) against a Mycobacterium Tuberculosis (Mtb) heat shock protein (HSP) 16kDa antigen presented by Human Leukocyte Antigen (HLA)-A*02.
[30006605] Nonstimulatory peptide-MHC enhances human T-cell antigen-specific responses by amplifying proximal TCR signaling.
[29970406] Organic solvents and MS susceptibility: Interaction with MS risk HLA genes.
[29967002] Humanized Mouse Model to Study Type 1 Diabetes.
[29950410] CD8 T-Cell Response-Associated Evolution of Hepatitis B Virus Core Protein and Disease Progress.
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