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Protein

HLA class I histocompatibility antigen, A-2 alpha chain

Gene

HLA-A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • beta-2-microglobulin binding Source: UniProtKB
  • peptide antigen binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • receptor binding Source: BHF-UCL
  • TAP binding Source: UniProtKB
  • T cell receptor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Immunity

Enzyme and pathway databases

ReactomeiR-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236977. Endosomal/Vacuolar pathway.
R-HSA-164940. Nef mediated downregulation of MHC class I complex cell surface expression.
R-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-877300. Interferon gamma signaling.
R-HSA-909733. Interferon alpha/beta signaling.
R-HSA-983170. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:4931. HLA-A.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 308284ExtracellularSequence analysisAdd
BLAST
Transmembranei309 – 33224HelicalSequence analysisAdd
BLAST
Topological domaini333 – 36533CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • early endosome membrane Source: Reactome
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum exit site Source: UniProtKB
  • ER to Golgi transport vesicle membrane Source: Reactome
  • Golgi apparatus Source: UniProtKB
  • Golgi medial cisterna Source: UniProtKB
  • Golgi membrane Source: Reactome
  • integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
  • MHC class I protein complex Source: UniProtKB
  • phagocytic vesicle membrane Source: Reactome
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane, MHC I

Pathology & Biotechi

Organism-specific databases

MalaCardsiHLA-A.

Polymorphism and mutation databases

DMDMi122138.

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 ↔ 188PROSITE-ProRule annotation1 Publication
Disulfide bondi227 ↔ 283PROSITE-ProRule annotation1 Publication
Modified residuei350 – 3501PhosphoserineCombined sources
Modified residuei352 – 3521PhosphoserineCombined sources
Modified residuei356 – 3561PhosphoserineCombined sources
Modified residuei359 – 3591PhosphoserineCombined sources

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

EPDiP01892.
PeptideAtlasiP01892.
PRIDEiP01892.

PTM databases

iPTMnetiP01892.
PhosphoSiteiP01892.
SwissPalmiP01892.

Expressioni

Gene expression databases

BgeeiENSG00000235657.
CleanExiHS_HLA-A.

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

GO - Molecular functioni

  • beta-2-microglobulin binding Source: UniProtKB
  • receptor binding Source: BHF-UCL
  • TAP binding Source: UniProtKB
  • T cell receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109350. 102 interactions.
IntActiP01892. 12 interactions.
MINTiMINT-5000859.

Structurei

Secondary structure

1
365
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 3610Combined sources
Beta strandi41 – 433Combined sources
Beta strandi45 – 528Combined sources
Beta strandi55 – 617Combined sources
Beta strandi64 – 663Combined sources
Beta strandi70 – 734Combined sources
Helixi74 – 785Combined sources
Helixi81 – 10828Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi118 – 12710Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi133 – 14210Combined sources
Beta strandi145 – 1506Combined sources
Beta strandi157 – 1593Combined sources
Helixi162 – 17312Combined sources
Helixi176 – 18510Combined sources
Helixi187 – 19812Combined sources
Helixi200 – 2034Combined sources
Beta strandi210 – 23526Combined sources
Beta strandi238 – 2436Combined sources
Beta strandi246 – 2483Combined sources
Helixi249 – 2513Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi265 – 27410Combined sources
Beta strandi275 – 2773Combined sources
Helixi278 – 2803Combined sources
Beta strandi281 – 2866Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi294 – 2963Combined sources
Beta strandi348 – 3503Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
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[»]
4NNXX-ray2.10A25-298[»]
4NNYX-ray1.90A25-298[»]
4NO0X-ray2.70A25-300[»]
4NO2X-ray2.00A25-298[»]
4NO3X-ray1.70A25-298[»]
4NO5X-ray2.10A25-299[»]
4OV5X-ray2.20C/F/I/L/O/R128-141[»]
4QOKX-ray3.00A25-300[»]
4U6XX-ray1.68A25-300[»]
4U6YX-ray1.47A25-300[»]
4UQ3X-ray2.10A/C25-299[»]
4WJ5X-ray1.65A/D25-299[»]
4WUUX-ray3.05A25-300[»]
4ZEZX-ray2.40A/D25-299[»]
5C07X-ray2.11A/F25-300[»]
5C08X-ray2.33A/F25-300[»]
5C09X-ray2.48A/F25-300[»]
5C0AX-ray2.46A/F25-300[»]
5C0BX-ray2.03A/F25-299[»]
5C0CX-ray1.97A/F25-300[»]
5C0DX-ray1.68A25-300[»]
5C0EX-ray1.49A25-300[»]
5C0FX-ray1.46A25-300[»]
5C0GX-ray1.37A25-300[»]
5C0HX-ray1.37A25-300[»]
5C0IX-ray1.53A25-300[»]
5C0JX-ray1.64A25-300[»]
5D2LX-ray3.51A/C/G/M25-299[»]
5D2NX-ray2.10A/H25-299[»]
5E9DX-ray2.51A/F25-299[»]
5EU3X-ray1.97A25-300[»]
5EU4X-ray2.12A/D25-300[»]
5EU5X-ray1.54A25-300[»]
5EU6X-ray2.02A25-300[»]
5HHMX-ray2.50A/F25-300[»]
5HHNX-ray2.03A25-298[»]
5HHOX-ray2.95A25-300[»]
5HHPX-ray1.90A25-298[»]
5HHQX-ray2.10A25-298[»]
5HYJX-ray3.06A/F25-300[»]
ProteinModelPortaliP01892.
SMRiP01892. Positions 25-298.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01892.

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

HOVERGENiHBG016709.

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.
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]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF54452. 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

        10         20         30         40         50
MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG
60 70 80 90 100
YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDGETRK VKAHSQTHRV
110 120 130 140 150
DLGTLRGYYN QSEAGSHTVQ RMYGCDVGSD WRFLRGYHQY AYDGKDYIAL
160 170 180 190 200
KEDLRSWTAA DMAAQTTKHK WEAAHVAEQL RAYLEGTCVE WLRRYLENGK
210 220 230 240 250
ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ
260 270 280 290 300
DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP
310 320 330 340 350
SSQPTIPIVG IIAGLVLFGA VITGAVVAAV MWRRKSSDRK GGSYSQAASS
360
DSAQGSDVSL TACKV
Length:365
Mass (Da):40,922
Last modified:August 13, 1987 - v1
Checksum:iB54A97B24B337C08
GO

Sequence cautioni

The sequence CAA41022 differs from that shown.The sequence differs from that shown extensively.Curated

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.
Corresponds to variant rs2075684 [ dbSNP | Ensembl ].
VAR_004334
Natural varianti54 – 541D → N in allele A*02:21.
Corresponds to variant rs41549215 [ dbSNP | Ensembl ].
VAR_004335
Natural varianti65 – 651A → G in allele A*02:31.
Corresponds to variant rs41557613 [ dbSNP | Ensembl ].
VAR_016726
Natural varianti67 – 671Q → R in allele A*02:02, allele A*02:05 and allele A*02:08.
Corresponds to variant rs41559117 [ dbSNP | Ensembl ].
VAR_004336
Natural varianti89 – 891R → G Polymorphism; found in a patient with MRT52. 1 Publication
VAR_076446
Natural varianti90 – 901K → N in allele A*02:08 and allele A*02:20.
Corresponds to variant rs199474436 [ dbSNP | Ensembl ].
VAR_004337
Natural varianti94 – 941H → Q in allele A*02:34 and allele A*02:35.
Corresponds to variant rs78306866 [ dbSNP | Ensembl ].
VAR_016727
Natural varianti97 – 971T → I in allele A*02:11.
Corresponds to variant rs199474457 [ dbSNP | Ensembl ].
VAR_004338
Natural varianti98 – 981H → D in allele A*02:11 and allele A*02:35.
Corresponds to variant rs1136683 [ dbSNP | Ensembl ].
VAR_016728
Natural varianti119 – 1191V → L in allele A*02:02, allele A*02:05, allele A*02:08 and allele A*02:17.
Corresponds to variant rs1071743 [ dbSNP | Ensembl ].
VAR_004339
Natural varianti121 – 1211R → M in allele A*02:04 and allele A*02:17.
Corresponds to variant rs199474485 [ dbSNP | Ensembl ].
VAR_004340
Natural varianti123 – 1231Y → C in allele A*02:07 and allele A*02:18.
Corresponds to variant rs1136697 [ dbSNP | Ensembl ].
VAR_004341
Natural varianti123 – 1231Y → F in allele A*02:10 and allele A*02:17.
Corresponds to variant rs1136697 [ dbSNP | Ensembl ].
VAR_004342
Natural varianti131 – 1311W → G in allele A*02:10.
Corresponds to variant rs1136702 [ dbSNP | Ensembl ].
VAR_004343
Natural varianti162 – 1621M → K in allele A*02:18.
Corresponds to variant rs41549316 [ dbSNP | Ensembl ].
VAR_004344
Natural varianti173 – 1731A → T in allele A*02:03.
Corresponds to variant rs1059526 [ dbSNP | Ensembl ].
VAR_004345
Natural varianti176 – 1761V → E in allele A*02:03 and allele A*02:13. Combined sources
Corresponds to variant rs9256983 [ dbSNP | Ensembl ].
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. Combined sources
Corresponds to variant rs9260156 [ dbSNP | Ensembl ].
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.
Corresponds to variant rs3098019 [ dbSNP | Ensembl ].
VAR_016730
Natural varianti260 – 2601A → E in allele A*02:09.
Corresponds to variant rs41540417 [ dbSNP | Ensembl ].
VAR_004350

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
UniGeneiHs.181244.
Hs.713441.

Genome annotation databases

EnsembliENST00000457879; ENSP00000403575; ENSG00000235657.
ENST00000547271; ENSP00000447962; ENSG00000235657.
ENST00000547522; ENSP00000448077; ENSG00000227715.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
UniGeneiHs.181244.
Hs.713441.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
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[»]
4NNXX-ray2.10A25-298[»]
4NNYX-ray1.90A25-298[»]
4NO0X-ray2.70A25-300[»]
4NO2X-ray2.00A25-298[»]
4NO3X-ray1.70A25-298[»]
4NO5X-ray2.10A25-299[»]
4OV5X-ray2.20C/F/I/L/O/R128-141[»]
4QOKX-ray3.00A25-300[»]
4U6XX-ray1.68A25-300[»]
4U6YX-ray1.47A25-300[»]
4UQ3X-ray2.10A/C25-299[»]
4WJ5X-ray1.65A/D25-299[»]
4WUUX-ray3.05A25-300[»]
4ZEZX-ray2.40A/D25-299[»]
5C07X-ray2.11A/F25-300[»]
5C08X-ray2.33A/F25-300[»]
5C09X-ray2.48A/F25-300[»]
5C0AX-ray2.46A/F25-300[»]
5C0BX-ray2.03A/F25-299[»]
5C0CX-ray1.97A/F25-300[»]
5C0DX-ray1.68A25-300[»]
5C0EX-ray1.49A25-300[»]
5C0FX-ray1.46A25-300[»]
5C0GX-ray1.37A25-300[»]
5C0HX-ray1.37A25-300[»]
5C0IX-ray1.53A25-300[»]
5C0JX-ray1.64A25-300[»]
5D2LX-ray3.51A/C/G/M25-299[»]
5D2NX-ray2.10A/H25-299[»]
5E9DX-ray2.51A/F25-299[»]
5EU3X-ray1.97A25-300[»]
5EU4X-ray2.12A/D25-300[»]
5EU5X-ray1.54A25-300[»]
5EU6X-ray2.02A25-300[»]
5HHMX-ray2.50A/F25-300[»]
5HHNX-ray2.03A25-298[»]
5HHOX-ray2.95A25-300[»]
5HHPX-ray1.90A25-298[»]
5HHQX-ray2.10A25-298[»]
5HYJX-ray3.06A/F25-300[»]
ProteinModelPortaliP01892.
SMRiP01892. Positions 25-298.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109350. 102 interactions.
IntActiP01892. 12 interactions.
MINTiMINT-5000859.

PTM databases

iPTMnetiP01892.
PhosphoSiteiP01892.
SwissPalmiP01892.

Polymorphism and mutation databases

DMDMi122138.

Proteomic databases

EPDiP01892.
PeptideAtlasiP01892.
PRIDEiP01892.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000457879; ENSP00000403575; ENSG00000235657.
ENST00000547271; ENSP00000447962; ENSG00000235657.
ENST00000547522; ENSP00000448077; ENSG00000227715.

Organism-specific databases

GeneCardsiHLA-A.
HGNCiHGNC:4931. HLA-A.
MalaCardsiHLA-A.
MIMi142800. gene.
neXtProtiNX_P01892.
GenAtlasiSearch...

Phylogenomic databases

HOVERGENiHBG016709.

Enzyme and pathway databases

ReactomeiR-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236977. Endosomal/Vacuolar pathway.
R-HSA-164940. Nef mediated downregulation of MHC class I complex cell surface expression.
R-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-877300. Interferon gamma signaling.
R-HSA-909733. Interferon alpha/beta signaling.
R-HSA-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

ChiTaRSiHLA-A. human.
EvolutionaryTraceiP01892.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000235657.
CleanExiHS_HLA-A.

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.
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]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF54452. SSF54452. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: September 7, 2016
This is version 190 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.