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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.
SIGNORiP01892.

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)DescriptionActionsGraphical viewLength
Topological domaini25 – 308ExtracellularSequence analysisAdd BLAST284
Transmembranei309 – 332HelicalSequence analysisAdd BLAST24
Topological domaini333 – 365CytoplasmicSequence analysisAdd BLAST33

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

DisGeNETi3105.
MalaCardsiHLA-A.
OpenTargetsiENSG00000235657.

Polymorphism and mutation databases

DMDMi122138.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000001881425 – 365HLA class I histocompatibility antigen, A-2 alpha chainAdd BLAST341

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi110N-linked (GlcNAc...)1 Publication1
Disulfide bondi125 ↔ 188PROSITE-ProRule annotation1 Publication
Disulfide bondi227 ↔ 283PROSITE-ProRule annotation1 Publication
Modified residuei350PhosphoserineCombined sources1
Modified residuei352PhosphoserineCombined sources1
Modified residuei356PhosphoserineCombined sources1
Modified residuei359PhosphoserineCombined sources1

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.
PhosphoSitePlusiP01892.
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 interactors.
IntActiP01892. 12 interactors.
MINTiMINT-5000859.

Structurei

Secondary structure

1365
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 36Combined sources10
Beta strandi41 – 43Combined sources3
Beta strandi45 – 52Combined sources8
Beta strandi55 – 61Combined sources7
Beta strandi64 – 66Combined sources3
Beta strandi70 – 73Combined sources4
Helixi74 – 78Combined sources5
Helixi81 – 108Combined sources28
Beta strandi113 – 115Combined sources3
Beta strandi118 – 127Combined sources10
Beta strandi129 – 131Combined sources3
Beta strandi133 – 142Combined sources10
Beta strandi145 – 150Combined sources6
Beta strandi152 – 155Combined sources4
Beta strandi157 – 159Combined sources3
Helixi162 – 173Combined sources12
Helixi176 – 185Combined sources10
Helixi187 – 198Combined sources12
Helixi200 – 203Combined sources4
Beta strandi210 – 235Combined sources26
Beta strandi238 – 243Combined sources6
Beta strandi246 – 248Combined sources3
Helixi249 – 251Combined sources3
Beta strandi252 – 254Combined sources3
Beta strandi261 – 263Combined sources3
Beta strandi265 – 274Combined sources10
Beta strandi275 – 277Combined sources3
Helixi278 – 280Combined sources3
Beta strandi281 – 286Combined sources6
Beta strandi290 – 292Combined sources3
Beta strandi294 – 296Combined sources3
Beta strandi348 – 350Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5D9SX-ray1.87A25-298[»]
5DDHX-ray1.50A25-298[»]
5E6IX-ray4.00C/I/M/R25-299[»]
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[»]
5IROX-ray2.64A/E/I/M/Q/U25-299[»]
5SWQX-ray2.00A25-300[»]
ProteinModelPortaliP01892.
SMRiP01892.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01892.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini209 – 295Ig-like C1-typeAdd BLAST87

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni25 – 114Alpha-1Add BLAST90
Regioni115 – 206Alpha-2Add BLAST92
Regioni207 – 298Alpha-3Add BLAST92
Regioni299 – 308Connecting peptide10

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)DescriptionActionsGraphical viewLength
Sequence conflicti115G → V in AAA52656 (PubMed:3863816).Curated1
Sequence conflicti140Y → V in AAA52656 (PubMed:3863816).Curated1
Sequence conflicti277Q → E in AAA52656 (PubMed:3863816).Curated1
Sequence conflicti318F → L in AAA52656 (PubMed:3863816).Curated1

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_00433433F → 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 rs2075684dbSNPEnsembl.1
Natural variantiVAR_00433554D → N in allele A*02:21. Corresponds to variant rs41549215dbSNPEnsembl.1
Natural variantiVAR_01672665A → G in allele A*02:31. Corresponds to variant rs41557613dbSNPEnsembl.1
Natural variantiVAR_00433667Q → R in allele A*02:02, allele A*02:05 and allele A*02:08. Corresponds to variant rs41559117dbSNPEnsembl.1
Natural variantiVAR_07644689R → G Polymorphism. 1 PublicationCorresponds to variant rs199474430dbSNPEnsembl.1
Natural variantiVAR_00433790K → N in allele A*02:08 and allele A*02:20. Corresponds to variant rs199474436dbSNPEnsembl.1
Natural variantiVAR_01672794H → Q in allele A*02:34 and allele A*02:35. Corresponds to variant rs78306866dbSNPEnsembl.1
Natural variantiVAR_00433897T → I in allele A*02:11. Corresponds to variant rs199474457dbSNPEnsembl.1
Natural variantiVAR_01672898H → D in allele A*02:11 and allele A*02:35. Corresponds to variant rs1136683dbSNPEnsembl.1
Natural variantiVAR_004339119V → L in allele A*02:02, allele A*02:05, allele A*02:08 and allele A*02:17. Corresponds to variant rs1071743dbSNPEnsembl.1
Natural variantiVAR_004340121R → M in allele A*02:04 and allele A*02:17. Corresponds to variant rs199474485dbSNPEnsembl.1
Natural variantiVAR_004341123Y → C in allele A*02:07 and allele A*02:18. Corresponds to variant rs1136697dbSNPEnsembl.1
Natural variantiVAR_004342123Y → F in allele A*02:10 and allele A*02:17. Corresponds to variant rs1136697dbSNPEnsembl.1
Natural variantiVAR_004343131W → G in allele A*02:10. Corresponds to variant rs1136702dbSNPEnsembl.1
Natural variantiVAR_004344162M → K in allele A*02:18. Corresponds to variant rs41549316dbSNPEnsembl.1
Natural variantiVAR_004345173A → T in allele A*02:03. Corresponds to variant rs1059526dbSNPEnsembl.1
Natural variantiVAR_004346176V → E in allele A*02:03 and allele A*02:13. Combined sourcesCorresponds to variant rs9256983dbSNPEnsembl.1
Natural variantiVAR_004348180L → Q in allele A*02:12, allele A*02:13 and allele A*02:37. 1
Natural variantiVAR_004347180L → W in allele A*02:02, allele A*02:03, allele A*02:05 and allele A*02:08. Combined sourcesCorresponds to variant rs9260156dbSNPEnsembl.1
Natural variantiVAR_004349187T → E in allele A*02:16; requires 2 nucleotide substitutions. 1
Natural variantiVAR_016729190E → D in allele A*02:36 and allele A*02:37. 1
Natural variantiVAR_016730191W → G in allele A*02:36 and allele A*02:37. Corresponds to variant rs3098019dbSNPEnsembl.1
Natural variantiVAR_004350260A → E in allele A*02:09. Corresponds to variant rs41540417dbSNPEnsembl.1

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
PDB 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[»]
5D9SX-ray1.87A25-298[»]
5DDHX-ray1.50A25-298[»]
5E6IX-ray4.00C/I/M/R25-299[»]
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[»]
5IROX-ray2.64A/E/I/M/Q/U25-299[»]
5SWQX-ray2.00A25-300[»]
ProteinModelPortaliP01892.
SMRiP01892.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP01892.
PhosphoSitePlusiP01892.
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

DisGeNETi3105.
GeneCardsiHLA-A.
HGNCiHGNC:4931. HLA-A.
MalaCardsiHLA-A.
MIMi142800. gene.
neXtProtiNX_P01892.
OpenTargetsiENSG00000235657.
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.
SIGNORiP01892.

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: November 30, 2016
This is version 193 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.