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P01892

- 1A02_HUMAN

UniProt

P01892 - 1A02_HUMAN

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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: 5 out of 5- Experimental evidence at protein leveli

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. receptor binding Source: BHF-UCL
  5. TAP binding Source: UniProt
  6. 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
Complete GO annotation...

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
Complete GO annotation...

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

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[»]
4OV5X-ray2.20C/F/I/L/O/R128-141[»]
4UQ3X-ray2.10A/C25-299[»]
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

        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 CAA41022.1 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.
ENST00000547522; ENSP00000448077; ENSG00000227715.
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 [» ]
4OV5 X-ray 2.20 C/F/I/L/O/R 128-141 [» ]
4UQ3 X-ray 2.10 A/C 25-299 [» ]
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

PaxDbi P01892.
PRIDEi P01892.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000457879 ; ENSP00000403575 ; ENSG00000235657 .
ENST00000547271 ; ENSP00000447962 ; ENSG00000235657 .
ENST00000547522 ; ENSP00000448077 ; ENSG00000227715 .
GeneIDi 3105.
KEGGi hsa:3105.

Organism-specific databases

CTDi 3105.
GeneCardsi GC06P030186.
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.
GenomeRNAii 3105.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 171 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