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P01892

- 1A02_HUMAN

UniProt

P01892 - 1A02_HUMAN

Protein

HLA class I histocompatibility antigen, A-2 alpha chain

Gene

HLA-A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    Functioni

    Involved in the presentation of foreign antigens to the immune system.

    GO - Molecular functioni

    1. beta-2-microglobulin binding Source: UniProt
    2. peptide antigen binding Source: UniProt
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. receptor binding Source: BHF-UCL
    6. TAP binding Source: UniProt
    7. T cell receptor binding Source: UniProt

    GO - Biological processi

    1. antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent Source: UniProt
    2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
    3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
    4. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent Source: Reactome
    5. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    6. cytokine-mediated signaling pathway Source: Reactome
    7. interferon-gamma-mediated signaling pathway Source: Reactome
    8. positive regulation of interferon-gamma production Source: UniProt
    9. positive regulation of memory T cell activation Source: UniProt
    10. positive regulation of T cell mediated cytotoxicity Source: UniProt
    11. regulation of defense response to virus by virus Source: Reactome
    12. regulation of immune response Source: Reactome
    13. type I interferon signaling pathway Source: Reactome
    14. viral process Source: Reactome

    Keywords - Biological processi

    Host-virus interaction, Immunity

    Enzyme and pathway databases

    ReactomeiREACT_11103. Nef mediated downregulation of MHC class I complex cell surface expression.
    REACT_111168. Endosomal/Vacuolar pathway.
    REACT_111178. ER-Phagosome pathway.
    REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.
    REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    HLA class I histocompatibility antigen, A-2 alpha chain
    Alternative name(s):
    MHC class I antigen A*2
    Gene namesi
    Name:HLA-A
    Synonyms:HLAA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:4931. HLA-A.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: UniProt
    2. early endosome membrane Source: Reactome
    3. endoplasmic reticulum Source: UniProt
    4. endoplasmic reticulum exit site Source: UniProt
    5. ER to Golgi transport vesicle membrane Source: Reactome
    6. Golgi apparatus Source: UniProt
    7. Golgi medial cisterna Source: UniProt
    8. Golgi membrane Source: Reactome
    9. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
    10. MHC class I protein complex Source: UniProt
    11. phagocytic vesicle membrane Source: Reactome
    12. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane, MHC I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 365341HLA class I histocompatibility antigen, A-2 alpha chainPRO_0000018814Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi110 – 1101N-linked (GlcNAc...)1 Publication
    Disulfide bondi125 ↔ 1881 PublicationPROSITE-ProRule annotation
    Disulfide bondi227 ↔ 2831 PublicationPROSITE-ProRule annotation
    Modified residuei356 – 3561Phosphoserine1 Publication

    Post-translational modificationi

    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.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP01892.
    PaxDbiP01892.
    PRIDEiP01892.

    PTM databases

    PhosphoSiteiP01892.

    Expressioni

    Gene expression databases

    CleanExiHS_HLA-A.
    GenevestigatoriP01892.

    Interactioni

    Subunit structurei

    Dimer of alpha chain and a beta chain (beta-2-microglobulin). Interacts with human herpesvirus 8 MIR1 protein. Interacts with HTLV-1 accessory protein p12I.3 Publications

    Protein-protein interaction databases

    DIPiDIP-6085N.
    IntActiP01892. 12 interactions.
    MINTiMINT-5000859.

    Structurei

    Secondary structure

    1
    365
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi27 – 3610
    Beta strandi41 – 433
    Beta strandi45 – 528
    Beta strandi55 – 617
    Beta strandi64 – 663
    Beta strandi70 – 734
    Helixi74 – 785
    Helixi81 – 10828
    Beta strandi113 – 1153
    Beta strandi118 – 12710
    Beta strandi131 – 14212
    Beta strandi145 – 1506
    Beta strandi157 – 1593
    Helixi162 – 17312
    Helixi176 – 1849
    Helixi187 – 19812
    Helixi200 – 2034
    Beta strandi210 – 23526
    Beta strandi238 – 2436
    Beta strandi246 – 2483
    Helixi249 – 2513
    Beta strandi252 – 2543
    Beta strandi261 – 2633
    Beta strandi265 – 27410
    Beta strandi275 – 2773
    Helixi278 – 2803
    Beta strandi281 – 2866
    Beta strandi290 – 2923
    Beta strandi294 – 2974
    Beta strandi348 – 3503

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AKJX-ray2.65A25-300[»]
    1AO7X-ray2.60A25-299[»]
    1AQDX-ray2.45C/F/I/L127-141[»]
    1B0GX-ray2.50A/D25-299[»]
    1B0RX-ray2.90A25-299[»]
    1BD2X-ray2.50A25-299[»]
    1DUYX-ray2.15A/D25-299[»]
    1DUZX-ray1.80A/D25-299[»]
    1EEYX-ray2.25A/D25-299[»]
    1EEZX-ray2.30A/D25-299[»]
    1HHGX-ray2.60A/D25-299[»]
    1HHHX-ray3.00A25-299[»]
    1HHIX-ray2.50A/D25-299[»]
    1HHJX-ray2.50A/D25-299[»]
    1HHKX-ray2.50A/D25-299[»]
    1HLAX-ray3.50A25-294[»]
    1I1FX-ray2.80A/D25-299[»]
    1I1YX-ray2.20A/D25-299[»]
    1I4FX-ray1.40A25-299[»]
    1I7RX-ray2.20A/D25-299[»]
    1I7TX-ray2.80A/D25-299[»]
    1I7UX-ray1.80A/D25-299[»]
    1IM3X-ray2.20A/E/I/M25-299[»]
    1JF1X-ray1.85A25-299[»]
    1JHTX-ray2.15A25-299[»]
    1LP9X-ray2.00A/H25-299[»]
    1OGAX-ray1.40A25-300[»]
    1P7QX-ray3.40A25-300[»]
    1QEWX-ray2.20A25-299[»]
    1QR1X-ray2.40A/D25-299[»]
    1QRNX-ray2.80A25-298[»]
    1QSEX-ray2.80A25-298[»]
    1QSFX-ray2.80A25-298[»]
    1S8DX-ray2.20A25-299[»]
    1S9WX-ray2.20A25-298[»]
    1S9XX-ray2.50A25-298[»]
    1S9YX-ray2.30A25-298[»]
    1T1WX-ray2.20A25-299[»]
    1T1XX-ray2.20A25-299[»]
    1T1YX-ray2.00A25-299[»]
    1T1ZX-ray1.90A25-299[»]
    1T20X-ray2.20A25-299[»]
    1T21X-ray2.19A25-299[»]
    1T22X-ray2.20A25-299[»]
    1TVBX-ray1.80A/D25-299[»]
    1TVHX-ray1.80A/D25-299[»]
    1UR7model-A25-299[»]
    2AV1X-ray1.95A/D25-299[»]
    2AV7X-ray2.05A/D25-299[»]
    2BNQX-ray1.70A25-300[»]
    2BNRX-ray1.90A25-300[»]
    2C7UX-ray2.38A/D25-300[»]
    2CLRX-ray2.00A/D25-299[»]
    2F53X-ray2.10A25-299[»]
    2F54X-ray2.70A/F25-298[»]
    2GITX-ray1.70A/D25-299[»]
    2GJ6X-ray2.56A25-299[»]
    2GT9X-ray1.75A/D25-299[»]
    2GTWX-ray1.55A/D25-299[»]
    2GTZX-ray1.70A/D25-299[»]
    2GUOX-ray1.90A/D25-299[»]
    2J8UX-ray2.88A/H25-299[»]
    2JCCX-ray2.50A/H25-299[»]
    2P5EX-ray1.89A25-300[»]
    2P5WX-ray2.20A25-300[»]
    2PYEX-ray2.30A25-300[»]
    2UWEX-ray2.40A/H25-299[»]
    2V2WX-ray1.60A/D25-300[»]
    2V2XX-ray1.60A/D25-300[»]
    2VLJX-ray2.40A25-300[»]
    2VLKX-ray2.50A25-300[»]
    2VLLX-ray1.60A/D25-300[»]
    2VLRX-ray2.30A/F25-300[»]
    2X4NX-ray2.34A/D25-299[»]
    2X4OX-ray2.30A/D25-299[»]
    2X4PX-ray2.30A/D25-299[»]
    2X4QX-ray1.90A/D25-299[»]
    2X4RX-ray2.30A/D25-299[»]
    2X4SX-ray2.55A/D25-299[»]
    2X4TX-ray2.30A/D25-299[»]
    2X4UX-ray2.10A/D25-299[»]
    2X70X-ray2.00A/D25-299[»]
    3BGMX-ray1.60A25-298[»]
    3BH8X-ray1.65A25-298[»]
    3BH9X-ray1.70A25-299[»]
    3BHBX-ray2.20A25-298[»]
    3D25X-ray1.30A25-298[»]
    3D39X-ray2.81A25-299[»]
    3D3VX-ray2.80A25-299[»]
    3FQNX-ray1.65A25-299[»]
    3FQRX-ray1.70A25-299[»]
    3FQTX-ray1.80A25-299[»]
    3FQUX-ray1.80A25-299[»]
    3FQWX-ray1.93A25-299[»]
    3FQXX-ray1.70A25-299[»]
    3FT2X-ray1.80A25-299[»]
    3FT3X-ray1.95A25-299[»]
    3FT4X-ray1.90A25-299[»]
    3GIVX-ray2.00A/D25-299[»]
    3GJFX-ray1.90A/D25-300[»]
    3GSNX-ray2.80H25-298[»]
    3GSOX-ray1.60A25-298[»]
    3GSQX-ray2.12A25-298[»]
    3GSRX-ray1.95A25-298[»]
    3GSUX-ray1.80A25-299[»]
    3GSVX-ray1.90A25-299[»]
    3GSWX-ray1.81A25-298[»]
    3GSXX-ray2.10A25-298[»]
    3H7BX-ray1.88A/D25-299[»]
    3H9HX-ray2.00A/D25-299[»]
    3H9SX-ray2.70A25-299[»]
    3HAEX-ray2.90A/D/J/P25-300[»]
    3HLAX-ray2.60A25-294[»]
    3HPJX-ray2.00A/D25-299[»]
    3I6GX-ray2.20A/D25-299[»]
    3I6KX-ray2.80A/E25-299[»]
    3IXAX-ray2.10A/D25-299[»]
    3KLAX-ray1.65A/D25-299[»]
    3MGOX-ray2.30A/D/G/J25-299[»]
    3MGTX-ray2.20A/D/G/J25-299[»]
    3MR9X-ray1.93A25-300[»]
    3MRBX-ray1.40A25-300[»]
    3MRCX-ray1.80A25-300[»]
    3MRDX-ray1.70A25-300[»]
    3MREX-ray1.10A25-300[»]
    3MRFX-ray2.30A25-300[»]
    3MRGX-ray1.30A25-300[»]
    3MRHX-ray2.40A25-300[»]
    3MRIX-ray2.10A25-300[»]
    3MRJX-ray1.87A25-300[»]
    3MRKX-ray1.40A25-300[»]
    3MRLX-ray2.41A25-300[»]
    3MRMX-ray1.90A25-300[»]
    3MRNX-ray2.30A25-300[»]
    3MROX-ray2.35A25-300[»]
    3MRPX-ray2.10A25-300[»]
    3MRQX-ray2.20A25-300[»]
    3MRRX-ray1.60A25-300[»]
    3MYJX-ray1.89A/D25-299[»]
    3O3AX-ray1.80A/D25-299[»]
    3O3BX-ray1.90A/D25-299[»]
    3O3DX-ray1.70A/D25-299[»]
    3O3EX-ray1.85A/D25-299[»]
    3O4LX-ray2.54A25-300[»]
    3PWJX-ray1.70A/D25-299[»]
    3PWLX-ray1.65A/D25-299[»]
    3PWNX-ray1.60A/D25-299[»]
    3PWPX-ray2.69A25-299[»]
    3QDGX-ray2.69A25-299[»]
    3QDJX-ray2.30A25-299[»]
    3QDMX-ray2.80A25-299[»]
    3QEQX-ray2.59A25-299[»]
    3QFDX-ray1.68A/D25-299[»]
    3QFJX-ray2.29A25-299[»]
    3REWX-ray1.90A/D25-299[»]
    3TO2X-ray2.60A25-299[»]
    3UTQX-ray1.67A25-300[»]
    3UTSX-ray2.71A/F25-300[»]
    3UTTX-ray2.60A/F25-299[»]
    3V5DX-ray2.00A/D25-299[»]
    3V5HX-ray1.63A/D25-299[»]
    3V5KX-ray2.31A/D25-299[»]
    4E5XX-ray1.95A/D25-299[»]
    4EMZX-ray2.90D/E338-365[»]
    4EN2X-ray2.58D/E338-365[»]
    4EUPX-ray2.88A/D25-299[»]
    4EUQX-ray2.69A/D25-299[»]
    4FTVX-ray2.74A25-299[»]
    4GKNX-ray2.75A/D25-300[»]
    4GKSX-ray2.35A/D25-300[»]
    4I4WX-ray1.77A25-300[»]
    4JFDX-ray2.46A25-300[»]
    4JFEX-ray2.70A25-300[»]
    4JFFX-ray2.43A25-300[»]
    4JFOX-ray2.11A/D25-299[»]
    4JFPX-ray1.91A/D25-300[»]
    4JFQX-ray1.90A/D25-300[»]
    4K7FX-ray2.00A/D25-299[»]
    4L29X-ray3.09A/C/E/G/I/K/M/O/Q/S/U/W/Y/a25-300[»]
    4L3CX-ray2.64A/C/E/G/I/K/M/O/Q/S/U/W/Y/a25-300[»]
    4L3EX-ray2.56A25-299[»]
    4MNQX-ray2.74A25-300[»]
    ProteinModelPortaliP01892.
    SMRiP01892. Positions 25-298.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01892.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 308284ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini333 – 36533CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei309 – 33224HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini209 – 29587Ig-like C1-typeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni25 – 11490Alpha-1Add
    BLAST
    Regioni115 – 20692Alpha-2Add
    BLAST
    Regioni207 – 29892Alpha-3Add
    BLAST
    Regioni299 – 30810Connecting peptide

    Sequence similaritiesi

    Belongs to the MHC class I family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG42056.
    HOVERGENiHBG016709.
    KOiK06751.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.30.500.10. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003006. Ig/MHC_CS.
    IPR003597. Ig_C1-set.
    IPR011161. MHC_I-like_Ag-recog.
    IPR011162. MHC_I/II-like_Ag-recog.
    IPR027648. MHC_I_a.
    IPR001039. MHC_I_a_a1/a2.
    IPR010579. MHC_I_a_C.
    [Graphical view]
    PfamiPF07654. C1-set. 1 hit.
    PF00129. MHC_I. 1 hit.
    PF06623. MHC_I_C. 1 hit.
    [Graphical view]
    PRINTSiPR01638. MHCCLASSI.
    SMARTiSM00407. IGc1. 1 hit.
    [Graphical view]
    SUPFAMiSSF54452. SSF54452. 1 hit.
    PROSITEiPS50835. IG_LIKE. 1 hit.
    PS00290. IG_MHC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P01892-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG    50
    YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDGETRK VKAHSQTHRV 100
    DLGTLRGYYN QSEAGSHTVQ RMYGCDVGSD WRFLRGYHQY AYDGKDYIAL 150
    KEDLRSWTAA DMAAQTTKHK WEAAHVAEQL RAYLEGTCVE WLRRYLENGK 200
    ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ 250
    DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP 300
    SSQPTIPIVG IIAGLVLFGA VITGAVVAAV MWRRKSSDRK GGSYSQAASS 350
    DSAQGSDVSL TACKV 365
    Length:365
    Mass (Da):40,922
    Last modified:August 13, 1987 - v1
    Checksum:iB54A97B24B337C08
    GO

    Sequence cautioni

    The sequence CAA41022.1 differs from that shown. Reason: The sequence differs from that shown extensively.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti115 – 1151G → V in AAA52656. (PubMed:3863816)Curated
    Sequence conflicti140 – 1401Y → V in AAA52656. (PubMed:3863816)Curated
    Sequence conflicti277 – 2771Q → E in AAA52656. (PubMed:3863816)Curated
    Sequence conflicti318 – 3181F → L in AAA52656. (PubMed:3863816)Curated

    Polymorphismi

    The following alleles of A-2 are known: A*02:01, A*02:02, A*02:03, A*02:04, A*02:05, A*02:06 (A2.4A), A*02:07, A*02:08, A*02:09, A*02:10, A*02:11 (A2.5), A*02:12, A*02:13 (A*02SLU), A*02:16, A*02:17, A*02:18 (A2K), A*02:19, A*02:20, A*02:21, A*02:31, A*02:34 (A*AAT), A*02:35, A*02:36 and A*02:37. The sequence shown is that of A*02:01.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti33 – 331F → Y in allele A*02:05, allele A*02:06, allele A*02:08, allele A*02:10 and allele A*02:21.
    VAR_004334
    Natural varianti54 – 541D → N in allele A*02:21.
    VAR_004335
    Natural varianti65 – 651A → G in allele A*02:31.
    VAR_016726
    Natural varianti67 – 671Q → R in allele A*02:02, allele A*02:05 and allele A*02:08.
    VAR_004336
    Natural varianti90 – 901K → N in allele A*02:08 and allele A*02:20.
    VAR_004337
    Natural varianti94 – 941H → Q in allele A*02:34 and allele A*02:35.
    VAR_016727
    Natural varianti97 – 971T → I in allele A*02:11.
    VAR_004338
    Natural varianti98 – 981H → D in allele A*02:11 and allele A*02:35.
    VAR_016728
    Natural varianti119 – 1191V → L in allele A*02:02, allele A*02:05, allele A*02:08 and allele A*02:17.
    VAR_004339
    Natural varianti121 – 1211R → M in allele A*02:04 and allele A*02:17.
    VAR_004340
    Natural varianti123 – 1231Y → C in allele A*02:07 and allele A*02:18.
    VAR_004341
    Natural varianti123 – 1231Y → F in allele A*02:10 and allele A*02:17.
    VAR_004342
    Natural varianti131 – 1311W → G in allele A*02:10.
    VAR_004343
    Natural varianti162 – 1621M → K in allele A*02:18.
    VAR_004344
    Natural varianti173 – 1731A → T in allele A*02:03.
    VAR_004345
    Natural varianti176 – 1761V → E in allele A*02:03 and allele A*02:13. 1 Publication
    VAR_004346
    Natural varianti180 – 1801L → Q in allele A*02:12, allele A*02:13 and allele A*02:37.
    VAR_004348
    Natural varianti180 – 1801L → W in allele A*02:02, allele A*02:03, allele A*02:05 and allele A*02:08. 1 Publication
    VAR_004347
    Natural varianti187 – 1871T → E in allele A*02:16; requires 2 nucleotide substitutions.
    VAR_004349
    Natural varianti190 – 1901E → D in allele A*02:36 and allele A*02:37.
    VAR_016729
    Natural varianti191 – 1911W → G in allele A*02:36 and allele A*02:37.
    VAR_016730
    Natural varianti260 – 2601A → E in allele A*02:09.
    VAR_004350

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02883 Genomic DNA. Translation: AAA98727.1.
    M84379 mRNA. Translation: AAA59606.1.
    X02457 mRNA. Translation: CAA26297.1.
    M11887 mRNA. Translation: AAA52656.1.
    M19670 Genomic DNA. Translation: AAA03683.2.
    AH003586 Genomic DNA. Translation: AAB02120.1.
    U03863 mRNA. Translation: AAA03604.1.
    M86404 mRNA. No translation available.
    X57954 mRNA. Translation: CAA41022.1. Sequence problems.
    U02935 Genomic DNA. Translation: AAA76608.2.
    AJ555412 Genomic DNA. Translation: CAD87771.1.
    U03862 mRNA. Translation: AAA03603.1.
    M24042 mRNA. Translation: AAA59653.1.
    Z23071 mRNA. Translation: CAA80612.1.
    M84377 mRNA. Translation: AAA59603.1.
    X60764 mRNA. No translation available.
    M84378 mRNA. Translation: AAA59604.1.
    Z27120 mRNA. Translation: CAA81644.1.
    Z46633 mRNA. Translation: CAA86602.1.
    U18930 mRNA. Translation: AAA87076.1.
    D83515 mRNA. Translation: BAA11935.1.
    X96724 mRNA. Translation: CAA65501.1.
    U56825 mRNA. Translation: AAB17465.1.
    AH007560 Genomic DNA. Translation: AAD23437.1.
    AH007704 Genomic DNA. Translation: AAD30272.1.
    AH008013 Genomic DNA. Translation: AAD45690.1.
    AH008012 Genomic DNA. Translation: AAD45689.1.
    AH008007 Genomic DNA. Translation: AAD45324.1.
    PIRiB24512. HLHU10.
    I37470.
    I37542.
    I38418.
    I38442.
    I38443.
    I55948. HLHUA2.
    I61857.
    I61902.
    I84448.
    RefSeqiXP_006725814.1. XM_006725751.1.
    UniGeneiHs.181244.
    Hs.713441.

    Genome annotation databases

    EnsembliENST00000457879; ENSP00000403575; ENSG00000235657.
    ENST00000547271; ENSP00000447962; ENSG00000235657.
    GeneIDi3105.
    KEGGihsa:3105.

    Polymorphism databases

    DMDMi122138.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02883 Genomic DNA. Translation: AAA98727.1 .
    M84379 mRNA. Translation: AAA59606.1 .
    X02457 mRNA. Translation: CAA26297.1 .
    M11887 mRNA. Translation: AAA52656.1 .
    M19670 Genomic DNA. Translation: AAA03683.2 .
    AH003586 Genomic DNA. Translation: AAB02120.1 .
    U03863 mRNA. Translation: AAA03604.1 .
    M86404 mRNA. No translation available.
    X57954 mRNA. Translation: CAA41022.1 . Sequence problems.
    U02935 Genomic DNA. Translation: AAA76608.2 .
    AJ555412 Genomic DNA. Translation: CAD87771.1 .
    U03862 mRNA. Translation: AAA03603.1 .
    M24042 mRNA. Translation: AAA59653.1 .
    Z23071 mRNA. Translation: CAA80612.1 .
    M84377 mRNA. Translation: AAA59603.1 .
    X60764 mRNA. No translation available.
    M84378 mRNA. Translation: AAA59604.1 .
    Z27120 mRNA. Translation: CAA81644.1 .
    Z46633 mRNA. Translation: CAA86602.1 .
    U18930 mRNA. Translation: AAA87076.1 .
    D83515 mRNA. Translation: BAA11935.1 .
    X96724 mRNA. Translation: CAA65501.1 .
    U56825 mRNA. Translation: AAB17465.1 .
    AH007560 Genomic DNA. Translation: AAD23437.1 .
    AH007704 Genomic DNA. Translation: AAD30272.1 .
    AH008013 Genomic DNA. Translation: AAD45690.1 .
    AH008012 Genomic DNA. Translation: AAD45689.1 .
    AH008007 Genomic DNA. Translation: AAD45324.1 .
    PIRi B24512. HLHU10.
    I37470.
    I37542.
    I38418.
    I38442.
    I38443.
    I55948. HLHUA2.
    I61857.
    I61902.
    I84448.
    RefSeqi XP_006725814.1. XM_006725751.1.
    UniGenei Hs.181244.
    Hs.713441.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AKJ X-ray 2.65 A 25-300 [» ]
    1AO7 X-ray 2.60 A 25-299 [» ]
    1AQD X-ray 2.45 C/F/I/L 127-141 [» ]
    1B0G X-ray 2.50 A/D 25-299 [» ]
    1B0R X-ray 2.90 A 25-299 [» ]
    1BD2 X-ray 2.50 A 25-299 [» ]
    1DUY X-ray 2.15 A/D 25-299 [» ]
    1DUZ X-ray 1.80 A/D 25-299 [» ]
    1EEY X-ray 2.25 A/D 25-299 [» ]
    1EEZ X-ray 2.30 A/D 25-299 [» ]
    1HHG X-ray 2.60 A/D 25-299 [» ]
    1HHH X-ray 3.00 A 25-299 [» ]
    1HHI X-ray 2.50 A/D 25-299 [» ]
    1HHJ X-ray 2.50 A/D 25-299 [» ]
    1HHK X-ray 2.50 A/D 25-299 [» ]
    1HLA X-ray 3.50 A 25-294 [» ]
    1I1F X-ray 2.80 A/D 25-299 [» ]
    1I1Y X-ray 2.20 A/D 25-299 [» ]
    1I4F X-ray 1.40 A 25-299 [» ]
    1I7R X-ray 2.20 A/D 25-299 [» ]
    1I7T X-ray 2.80 A/D 25-299 [» ]
    1I7U X-ray 1.80 A/D 25-299 [» ]
    1IM3 X-ray 2.20 A/E/I/M 25-299 [» ]
    1JF1 X-ray 1.85 A 25-299 [» ]
    1JHT X-ray 2.15 A 25-299 [» ]
    1LP9 X-ray 2.00 A/H 25-299 [» ]
    1OGA X-ray 1.40 A 25-300 [» ]
    1P7Q X-ray 3.40 A 25-300 [» ]
    1QEW X-ray 2.20 A 25-299 [» ]
    1QR1 X-ray 2.40 A/D 25-299 [» ]
    1QRN X-ray 2.80 A 25-298 [» ]
    1QSE X-ray 2.80 A 25-298 [» ]
    1QSF X-ray 2.80 A 25-298 [» ]
    1S8D X-ray 2.20 A 25-299 [» ]
    1S9W X-ray 2.20 A 25-298 [» ]
    1S9X X-ray 2.50 A 25-298 [» ]
    1S9Y X-ray 2.30 A 25-298 [» ]
    1T1W X-ray 2.20 A 25-299 [» ]
    1T1X X-ray 2.20 A 25-299 [» ]
    1T1Y X-ray 2.00 A 25-299 [» ]
    1T1Z X-ray 1.90 A 25-299 [» ]
    1T20 X-ray 2.20 A 25-299 [» ]
    1T21 X-ray 2.19 A 25-299 [» ]
    1T22 X-ray 2.20 A 25-299 [» ]
    1TVB X-ray 1.80 A/D 25-299 [» ]
    1TVH X-ray 1.80 A/D 25-299 [» ]
    1UR7 model - A 25-299 [» ]
    2AV1 X-ray 1.95 A/D 25-299 [» ]
    2AV7 X-ray 2.05 A/D 25-299 [» ]
    2BNQ X-ray 1.70 A 25-300 [» ]
    2BNR X-ray 1.90 A 25-300 [» ]
    2C7U X-ray 2.38 A/D 25-300 [» ]
    2CLR X-ray 2.00 A/D 25-299 [» ]
    2F53 X-ray 2.10 A 25-299 [» ]
    2F54 X-ray 2.70 A/F 25-298 [» ]
    2GIT X-ray 1.70 A/D 25-299 [» ]
    2GJ6 X-ray 2.56 A 25-299 [» ]
    2GT9 X-ray 1.75 A/D 25-299 [» ]
    2GTW X-ray 1.55 A/D 25-299 [» ]
    2GTZ X-ray 1.70 A/D 25-299 [» ]
    2GUO X-ray 1.90 A/D 25-299 [» ]
    2J8U X-ray 2.88 A/H 25-299 [» ]
    2JCC X-ray 2.50 A/H 25-299 [» ]
    2P5E X-ray 1.89 A 25-300 [» ]
    2P5W X-ray 2.20 A 25-300 [» ]
    2PYE X-ray 2.30 A 25-300 [» ]
    2UWE X-ray 2.40 A/H 25-299 [» ]
    2V2W X-ray 1.60 A/D 25-300 [» ]
    2V2X X-ray 1.60 A/D 25-300 [» ]
    2VLJ X-ray 2.40 A 25-300 [» ]
    2VLK X-ray 2.50 A 25-300 [» ]
    2VLL X-ray 1.60 A/D 25-300 [» ]
    2VLR X-ray 2.30 A/F 25-300 [» ]
    2X4N X-ray 2.34 A/D 25-299 [» ]
    2X4O X-ray 2.30 A/D 25-299 [» ]
    2X4P X-ray 2.30 A/D 25-299 [» ]
    2X4Q X-ray 1.90 A/D 25-299 [» ]
    2X4R X-ray 2.30 A/D 25-299 [» ]
    2X4S X-ray 2.55 A/D 25-299 [» ]
    2X4T X-ray 2.30 A/D 25-299 [» ]
    2X4U X-ray 2.10 A/D 25-299 [» ]
    2X70 X-ray 2.00 A/D 25-299 [» ]
    3BGM X-ray 1.60 A 25-298 [» ]
    3BH8 X-ray 1.65 A 25-298 [» ]
    3BH9 X-ray 1.70 A 25-299 [» ]
    3BHB X-ray 2.20 A 25-298 [» ]
    3D25 X-ray 1.30 A 25-298 [» ]
    3D39 X-ray 2.81 A 25-299 [» ]
    3D3V X-ray 2.80 A 25-299 [» ]
    3FQN X-ray 1.65 A 25-299 [» ]
    3FQR X-ray 1.70 A 25-299 [» ]
    3FQT X-ray 1.80 A 25-299 [» ]
    3FQU X-ray 1.80 A 25-299 [» ]
    3FQW X-ray 1.93 A 25-299 [» ]
    3FQX X-ray 1.70 A 25-299 [» ]
    3FT2 X-ray 1.80 A 25-299 [» ]
    3FT3 X-ray 1.95 A 25-299 [» ]
    3FT4 X-ray 1.90 A 25-299 [» ]
    3GIV X-ray 2.00 A/D 25-299 [» ]
    3GJF X-ray 1.90 A/D 25-300 [» ]
    3GSN X-ray 2.80 H 25-298 [» ]
    3GSO X-ray 1.60 A 25-298 [» ]
    3GSQ X-ray 2.12 A 25-298 [» ]
    3GSR X-ray 1.95 A 25-298 [» ]
    3GSU X-ray 1.80 A 25-299 [» ]
    3GSV X-ray 1.90 A 25-299 [» ]
    3GSW X-ray 1.81 A 25-298 [» ]
    3GSX X-ray 2.10 A 25-298 [» ]
    3H7B X-ray 1.88 A/D 25-299 [» ]
    3H9H X-ray 2.00 A/D 25-299 [» ]
    3H9S X-ray 2.70 A 25-299 [» ]
    3HAE X-ray 2.90 A/D/J/P 25-300 [» ]
    3HLA X-ray 2.60 A 25-294 [» ]
    3HPJ X-ray 2.00 A/D 25-299 [» ]
    3I6G X-ray 2.20 A/D 25-299 [» ]
    3I6K X-ray 2.80 A/E 25-299 [» ]
    3IXA X-ray 2.10 A/D 25-299 [» ]
    3KLA X-ray 1.65 A/D 25-299 [» ]
    3MGO X-ray 2.30 A/D/G/J 25-299 [» ]
    3MGT X-ray 2.20 A/D/G/J 25-299 [» ]
    3MR9 X-ray 1.93 A 25-300 [» ]
    3MRB X-ray 1.40 A 25-300 [» ]
    3MRC X-ray 1.80 A 25-300 [» ]
    3MRD X-ray 1.70 A 25-300 [» ]
    3MRE X-ray 1.10 A 25-300 [» ]
    3MRF X-ray 2.30 A 25-300 [» ]
    3MRG X-ray 1.30 A 25-300 [» ]
    3MRH X-ray 2.40 A 25-300 [» ]
    3MRI X-ray 2.10 A 25-300 [» ]
    3MRJ X-ray 1.87 A 25-300 [» ]
    3MRK X-ray 1.40 A 25-300 [» ]
    3MRL X-ray 2.41 A 25-300 [» ]
    3MRM X-ray 1.90 A 25-300 [» ]
    3MRN X-ray 2.30 A 25-300 [» ]
    3MRO X-ray 2.35 A 25-300 [» ]
    3MRP X-ray 2.10 A 25-300 [» ]
    3MRQ X-ray 2.20 A 25-300 [» ]
    3MRR X-ray 1.60 A 25-300 [» ]
    3MYJ X-ray 1.89 A/D 25-299 [» ]
    3O3A X-ray 1.80 A/D 25-299 [» ]
    3O3B X-ray 1.90 A/D 25-299 [» ]
    3O3D X-ray 1.70 A/D 25-299 [» ]
    3O3E X-ray 1.85 A/D 25-299 [» ]
    3O4L X-ray 2.54 A 25-300 [» ]
    3PWJ X-ray 1.70 A/D 25-299 [» ]
    3PWL X-ray 1.65 A/D 25-299 [» ]
    3PWN X-ray 1.60 A/D 25-299 [» ]
    3PWP X-ray 2.69 A 25-299 [» ]
    3QDG X-ray 2.69 A 25-299 [» ]
    3QDJ X-ray 2.30 A 25-299 [» ]
    3QDM X-ray 2.80 A 25-299 [» ]
    3QEQ X-ray 2.59 A 25-299 [» ]
    3QFD X-ray 1.68 A/D 25-299 [» ]
    3QFJ X-ray 2.29 A 25-299 [» ]
    3REW X-ray 1.90 A/D 25-299 [» ]
    3TO2 X-ray 2.60 A 25-299 [» ]
    3UTQ X-ray 1.67 A 25-300 [» ]
    3UTS X-ray 2.71 A/F 25-300 [» ]
    3UTT X-ray 2.60 A/F 25-299 [» ]
    3V5D X-ray 2.00 A/D 25-299 [» ]
    3V5H X-ray 1.63 A/D 25-299 [» ]
    3V5K X-ray 2.31 A/D 25-299 [» ]
    4E5X X-ray 1.95 A/D 25-299 [» ]
    4EMZ X-ray 2.90 D/E 338-365 [» ]
    4EN2 X-ray 2.58 D/E 338-365 [» ]
    4EUP X-ray 2.88 A/D 25-299 [» ]
    4EUQ X-ray 2.69 A/D 25-299 [» ]
    4FTV X-ray 2.74 A 25-299 [» ]
    4GKN X-ray 2.75 A/D 25-300 [» ]
    4GKS X-ray 2.35 A/D 25-300 [» ]
    4I4W X-ray 1.77 A 25-300 [» ]
    4JFD X-ray 2.46 A 25-300 [» ]
    4JFE X-ray 2.70 A 25-300 [» ]
    4JFF X-ray 2.43 A 25-300 [» ]
    4JFO X-ray 2.11 A/D 25-299 [» ]
    4JFP X-ray 1.91 A/D 25-300 [» ]
    4JFQ X-ray 1.90 A/D 25-300 [» ]
    4K7F X-ray 2.00 A/D 25-299 [» ]
    4L29 X-ray 3.09 A/C/E/G/I/K/M/O/Q/S/U/W/Y/a 25-300 [» ]
    4L3C X-ray 2.64 A/C/E/G/I/K/M/O/Q/S/U/W/Y/a 25-300 [» ]
    4L3E X-ray 2.56 A 25-299 [» ]
    4MNQ X-ray 2.74 A 25-300 [» ]
    ProteinModelPortali P01892.
    SMRi P01892. Positions 25-298.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6085N.
    IntActi P01892. 12 interactions.
    MINTi MINT-5000859.

    PTM databases

    PhosphoSitei P01892.

    Polymorphism databases

    DMDMi 122138.

    Proteomic databases

    MaxQBi P01892.
    PaxDbi P01892.
    PRIDEi P01892.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000457879 ; ENSP00000403575 ; ENSG00000235657 .
    ENST00000547271 ; ENSP00000447962 ; ENSG00000235657 .
    GeneIDi 3105.
    KEGGi hsa:3105.

    Organism-specific databases

    CTDi 3105.
    GeneCardsi GC06P029949.
    GC06Pk29899.
    HGNCi HGNC:4931. HLA-A.
    MIMi 142800. gene.
    neXtProti NX_P01892.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG42056.
    HOVERGENi HBG016709.
    KOi K06751.

    Enzyme and pathway databases

    Reactomei REACT_11103. Nef mediated downregulation of MHC class I complex cell surface expression.
    REACT_111168. Endosomal/Vacuolar pathway.
    REACT_111178. ER-Phagosome pathway.
    REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.
    REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

    Miscellaneous databases

    ChiTaRSi HLA-A. human.
    EvolutionaryTracei P01892.
    SOURCEi Search...

    Gene expression databases

    CleanExi HS_HLA-A.
    Genevestigatori P01892.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.30.500.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003006. Ig/MHC_CS.
    IPR003597. Ig_C1-set.
    IPR011161. MHC_I-like_Ag-recog.
    IPR011162. MHC_I/II-like_Ag-recog.
    IPR027648. MHC_I_a.
    IPR001039. MHC_I_a_a1/a2.
    IPR010579. MHC_I_a_C.
    [Graphical view ]
    Pfami PF07654. C1-set. 1 hit.
    PF00129. MHC_I. 1 hit.
    PF06623. MHC_I_C. 1 hit.
    [Graphical view ]
    PRINTSi PR01638. MHCCLASSI.
    SMARTi SM00407. IGc1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54452. SSF54452. 1 hit.
    PROSITEi PS50835. IG_LIKE. 1 hit.
    PS00290. IG_MHC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and complete sequence of an HLA-A2 gene: analysis of two HLA-A alleles at the nucleotide level."
      Koller B.H., Orr H.T.
      J. Immunol. 134:2727-2733(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*02:01).
    2. "Three new class I HLA alleles: structure of mRNAs and alternative mechanisms of processing."
      Cianetti L., Testa U., Scotto L., la Valle R., Simeone A., Boccoli G., Giannella G., Peschle C., Boncinelli E.
      Immunogenetics 29:80-91(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ALLELE A*02:01).
    3. "Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction: frequency and nature of errors produced in amplification."
      Ennis P.D., Zemmour J., Salter R.D., Parham P.
      Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ALLELE A*02:01).
    4. "Comparison of HLA class I gene sequences. Derivation of locus-specific oligonucleotide probes specific for HLA-A, HLA-B, and HLA-C genes."
      Davidson W.F., Kress M., Khoury G., Jay G.
      J. Biol. Chem. 260:13414-13423(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 91-365.
    5. Cited for: NUCLEOTIDE SEQUENCE (ALLELES A*02:01; A*02:11 AND A*02:12).
    6. "Unusual RNA splicing generates a secreted form of HLA-A2 in a mutagenized B lymphoblastoid cell line."
      Krangel M.S.
      EMBO J. 4:1205-1210(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 39-365 (ALLELE A*02:01).
    7. "Comparison of amino acid sequences of two human histocompatibility antigens, HLA-A2 and HLA-B7: location of putative alloantigenic sites."
      Orr H.T., Lopez de Castro J.A., Parham P., Ploegh H.L., Strominger J.L.
      Proc. Natl. Acad. Sci. U.S.A. 76:4395-4399(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-295 (ALLELE A*02:01).
    8. "Structure of crossreactive human histocompatibility antigens HLA-A28 and HLA-A2: possible implications for the generation of HLA polymorphism."
      Lopez de Castro J.A., Strominger J.L., Strong D.M., Orr H.T.
      Proc. Natl. Acad. Sci. U.S.A. 79:3813-3817(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION (ALLELE A*02:01).
    9. "HLA class I allele (HLA-A2) expression defect associated with a mutation in its enhancer B inverted CAT box in two families."
      Balas A., Garcia-Sanchez F., Gomez-Reino F., Vicario J.L.
      Hum. Immunol. 41:69-73(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*02:01).
      Tissue: Blood.
    10. Balas A.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    11. "Confirmation of HLA-A*0201."
      Cox S.T.
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE (ALLELE A*02:01).
    12. "DNA sequences of the genes that encode the CTL-defined HLA-A2 variants M7 and DK1."
      Mattson D.H., Handy D.E., Bradley D.A., Coligan J.E., Cowan E.P., Biddison W.E.
      Immunogenetics 26:190-192(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-298 (ALLELES A*02:02 AND A*02:03).
    13. "Multiple genetic mechanisms have contributed to the generation of the HLA-A2/A28 family of class I MHC molecules."
      Holmes N., Ennis P., Wan A.M., Denney D.W., Parham P.
      J. Immunol. 139:936-941(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ALLELES A*02:03 AND A*02:05).
    14. Domena J.D.
      Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE (ALLELES A*02:03 AND A*02:05).
    15. "Structure of the HLA-A*0204 antigen, found in South American Indians. Spatial clustering of HLA-A2 subtype polymorphism."
      Castano A.R., Lopez de Castro J.A.
      Immunogenetics 34:281-285(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-365 (ALLELE A*02:04).
    16. "New recombinant HLA-B alleles in a tribe of South American Amerindians indicate rapid evolution of MHC class I loci."
      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.
      Nature 357:329-333(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 9-365 (ALLELE A*02:04).
    17. "Diversity and diversification of HLA-A,B,C alleles."
      Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.
      J. Immunol. 142:3937-3950(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ALLELE A*02:06).
    18. "Molecular analysis of an HLA-A2 functional variant CLA defined by cytolytic T lymphocytes."
      Ezquerra A., Domenech N., van der Poel J., Strominger J.L., Vega M.A., Lopez de Castro J.A.
      J. Immunol. 137:1642-1649(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE (ALLELE A*02:06).
    19. "Structural analysis of HLA-A2.4 functional variant KNE. Implications for the mapping of HLA-A2-specific T-cell epitopes."
      Domenech N., Ezquerra A., Castano R., Lopez de Castro J.A.
      Immunogenetics 27:196-202(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE (ALLELE A*02:07).
    20. "Molecular analysis of HLA-A2.4 functional variant KLO: close structural and evolutionary relatedness to the HLA-A2.2 subtype."
      Domenech N., Castano R., Goulmy E., Lopez de Castro J.A.
      Immunogenetics 28:143-152(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE (ALLELE A*02:08).
    21. "An HLA-A2 population variant with structural polymorphism in the alpha 3 region."
      Castano R., Ezquerra A., Domenech N., Lopez de Castro J.A.
      Immunogenetics 27:345-355(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE (ALLELE A*02:09).
    22. "An Oriental HLA-A2 subtype is closely related to a subset of Caucasoid HLA-A2 alleles."
      Epstein H., Kennedy L., Holmes N.
      Immunogenetics 29:112-116(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ALLELE A*02:10).
    23. "Structure of the HLA-A*0211 (A2.5) subtype: further evidence for selection-driven diversification of HLA-A2 antigens."
      Castano A.R., Lopez de Castro J.A.
      Immunogenetics 35:344-346(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-365 (ALLELE A*02:11).
    24. "Primary structure of a new HLA-A2 subtype: HLA-A*0213."
      Barber D.F., Fernandez J.M., Lopez de Castro J.A.
      Immunogenetics 39:378-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:13).
    25. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:16).
    26. "A novel subtype of A2 (A*0217) isolated from the South American Indian B-cell line AMALA."
      Selvakumar A., Granja C.B., Salazar M., Alosco S.M., Yunis E.J., Dupont B.
      Tissue Antigens 45:343-347(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:17).
      Tissue: Blood.
    27. "A new A2 sequence HLA-A2K from Japanese."
      Kashiwase K., Tokunaga K., Ishikawa Y., Oohashi H., Hashimoto M., Akaza T., Tadokoro K., Juji T.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE (ALLELE A*02:18).
      Tissue: Blood.
    28. "HLA-A*02 subtype distribution in Caucasians from northern Italy: identification of A*0220."
      Fleischhauer K., Zino E., Mazzi B., Severini G.M., Benazzi E., Bordignon C.
      Tissue Antigens 48:673-679(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:20).
      Tissue: Blood.
    29. "Nucleotide sequence of a novel HLA-A2 gene."
      Szmania S., Baxter-Lowe L.A.
      Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE (ALLELE A*02:21).
      Tissue: Blood.
    30. "Frequencies of HLA-A2 alleles in five U.S. population groups. Predominance Of A*02011 and identification of HLA-A*0231."
      Ellis J.M., Henson V., Slack R., Ng J., Hartzman R.J., Hurley C.K.
      Hum. Immunol. 61:334-340(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*02:31).
    31. "A new HLA-A*02 allele, A*0234, detected by polymerase chain reaction using sequence-specific primers (PCR-SSP)."
      Moses J.H., Greville W.D., Downes J., McClenahan W., Kennedy A., Dunckley H.
      Tissue Antigens 55:175-177(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-298 (ALLELE A*02:34).
    32. Cited for: NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES A*02:35; A*02:36 AND A*02:37).
    33. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    34. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    35. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110.
      Tissue: Liver.
    36. "Structure of the human class I histocompatibility antigen, HLA-A2."
      Bjorkman P.J., Saper M.A., Samraoui B., Bennett W.S., Strominger J.L., Wiley D.C.
      Nature 329:506-512(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF A*02:01.
    37. "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."
      Johnson J.M., Nicot C., Fullen J., Ciminale V., Casareto L., Mulloy J.C., Jacobson S., Franchini G.
      J. Virol. 75:6086-6094(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I.
    38. "Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation."
      Hewitt E.W., Duncan L., Mufti D., Baker J., Stevenson P.G., Lehner P.J.
      EMBO J. 21:2418-2429(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN HERPESVIRUS 8 MIR1 PROTEIN, UBIQUITINATION.
    39. "A structural basis for immunodominant human T cell receptor recognition."
      Stewart-Jones G.B.E., McMichael A.J., Bell J.I., Stuart D.I., Jones E.Y.
      Nat. Immunol. 4:657-663(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 25-300 OF HLA-A/B2M HETERODIMER IN COMPLEX WITH TRAC AND TRBC1, DISULFIDE BONDS.
    40. "Refined structure of the human histocompatibility antigen HLA-A2 at 2.6-A resolution."
      Saper M.A., Bjorkman P.J., Wiley D.C.
      J. Mol. Biol. 219:277-319(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF A*02:01.
    41. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-176, VARIANT [LARGE SCALE ANALYSIS] TRP-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry namei1A02_HUMAN
    AccessioniPrimary (citable) accession number: P01892
    Secondary accession number(s): O19619
    , P06338, P10313, P30444, P30445, P30446, P30514, Q29680, Q29837, Q29899, Q95352, Q95380, Q9TPX8, Q9TPX9, Q9TPY0, Q9TQH5, Q9TQI3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 170 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3