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HLA class I histocompatibility antigen, B-52 alpha chain (Bw-52) (HLA class I histocompatibility antigen, B-5 alpha chain) (MHC class I antigen B*52)

 1B52_HUMAN              Reviewed;         362 AA.
P30490; Q9MY75; Q9TPT4;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
08-MAY-2019, entry version 144.
RecName: Full=HLA class I histocompatibility antigen, B-52 alpha chain;
AltName: Full=Bw-52;
AltName: Full=HLA class I histocompatibility antigen, B-5 alpha chain;
AltName: Full=MHC class I antigen B*52;
Flags: Precursor;
Name=HLA-B; Synonyms=HLAB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*52:01).
PubMed=2909619;
Hayashi H., Ennis P.D., Ariga H., Salter R.D., Parham P., Kano K.,
Takiguchi M.;
"HLA-B51 and HLA-Bw52 differ by only two amino acids which are in the
helical region of the alpha 1 domain.";
J. Immunol. 142:306-311(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*52:02).
Jones P.F., Hurley C.K.;
"Novel HLA-B allele.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*52:03).
Gans C.P., Hurley C.K.;
"Novel HLA-B allele.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Involved in the presentation of foreign antigens to the
immune system.
-!- SUBUNIT: Dimer of alpha chain and a beta chain (beta-2-
microglobulin). {ECO:0000250|UniProtKB:P01892}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- PTM: Polyubiquitinated in a post ER compartment by interaction
with human herpesvirus 8 MIR1 protein. This targets the protein
for rapid degradation via the ubiquitin system (By similarity).
{ECO:0000250}.
-!- POLYMORPHISM: The following alleles of B-52 are known: B*52:01,
B*52:02 (B*52012V) and B*52:03. The sequence shown is that of
B*52:01.
-!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M22799; AAA59645.1; ALT_SEQ; Genomic_DNA.
EMBL; M22793; AAA59645.1; JOINED; Genomic_DNA.
EMBL; M22794; AAA59645.1; JOINED; Genomic_DNA.
EMBL; M22795; AAA59645.1; JOINED; Genomic_DNA.
EMBL; M22796; AAA59645.1; JOINED; Genomic_DNA.
EMBL; M22797; AAA59645.1; JOINED; Genomic_DNA.
EMBL; M22798; AAA59645.1; JOINED; Genomic_DNA.
EMBL; AH008246; AAF00933.1; -; Genomic_DNA.
EMBL; AH009592; AAF81610.1; -; Genomic_DNA.
PIR; B30345; B30345.
PDB; 3W39; X-ray; 3.10 A; A/D=25-300.
PDBsum; 3W39; -.
SMR; P30490; -.
SwissPalm; P30490; -.
BioMuta; HLA-B; -.
EPD; P30490; -.
jPOST; P30490; -.
MaxQB; P30490; -.
PeptideAtlas; P30490; -.
PRIDE; P30490; -.
Ensembl; ENST00000450871; ENSP00000388208; ENSG00000232126.
UCSC; uc011hpp.3; human.
DisGeNET; 3106; -.
GeneCards; HLA-B; -.
HGNC; HGNC:4932; HLA-B.
MalaCards; HLA-B; -.
MIM; 142830; gene.
neXtProt; NX_P30490; -.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236977; Endosomal/Vacuolar pathway.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
ChiTaRS; HLA-B; human.
Proteomes; UP000005640; Chromosome 6.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0042612; C:MHC class I protein complex; ISS:UniProtKB.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome.
GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.30.500.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
InterPro; IPR011161; MHC_I-like_Ag-recog.
InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
InterPro; IPR011162; MHC_I/II-like_Ag-recog.
InterPro; IPR001039; MHC_I_a_a1/a2.
InterPro; IPR010579; MHC_I_a_C.
Pfam; PF07654; C1-set; 1.
Pfam; PF00129; MHC_I; 1.
Pfam; PF06623; MHC_I_C; 1.
PRINTS; PR01638; MHCCLASSI.
SMART; SM00407; IGc1; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF54452; SSF54452; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Glycoprotein;
Immunity; Membrane; MHC I; Polymorphism; Reference proteome; Signal;
Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 24
CHAIN 25 362 HLA class I histocompatibility antigen,
B-52 alpha chain.
/FTId=PRO_0000018855.
TOPO_DOM 25 308 Extracellular. {ECO:0000255}.
TRANSMEM 309 332 Helical. {ECO:0000255}.
TOPO_DOM 333 362 Cytoplasmic. {ECO:0000255}.
DOMAIN 209 295 Ig-like C1-type.
REGION 25 114 Alpha-1.
REGION 115 206 Alpha-2.
REGION 207 298 Alpha-3.
REGION 299 308 Connecting peptide.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 125 188 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 227 283 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VARIANT 69 70 TE -> MA (in allele B*52:02).
/FTId=VAR_016521.
VARIANT 176 176 E -> V (in allele B*52:03).
/FTId=VAR_016522.
VARIANT 195 195 H -> Y (in allele B*52:03).
/FTId=VAR_016523.
STRAND 27 36 {ECO:0000244|PDB:3W39}.
STRAND 39 41 {ECO:0000244|PDB:3W39}.
STRAND 45 52 {ECO:0000244|PDB:3W39}.
STRAND 55 61 {ECO:0000244|PDB:3W39}.
STRAND 64 66 {ECO:0000244|PDB:3W39}.
TURN 75 78 {ECO:0000244|PDB:3W39}.
HELIX 81 109 {ECO:0000244|PDB:3W39}.
STRAND 118 127 {ECO:0000244|PDB:3W39}.
STRAND 133 142 {ECO:0000244|PDB:3W39}.
STRAND 145 150 {ECO:0000244|PDB:3W39}.
HELIX 162 172 {ECO:0000244|PDB:3W39}.
TURN 173 175 {ECO:0000244|PDB:3W39}.
HELIX 176 185 {ECO:0000244|PDB:3W39}.
HELIX 187 198 {ECO:0000244|PDB:3W39}.
HELIX 200 203 {ECO:0000244|PDB:3W39}.
STRAND 212 217 {ECO:0000244|PDB:3W39}.
STRAND 219 221 {ECO:0000244|PDB:3W39}.
STRAND 223 235 {ECO:0000244|PDB:3W39}.
STRAND 238 247 {ECO:0000244|PDB:3W39}.
HELIX 249 251 {ECO:0000244|PDB:3W39}.
STRAND 252 254 {ECO:0000244|PDB:3W39}.
STRAND 261 263 {ECO:0000244|PDB:3W39}.
STRAND 265 273 {ECO:0000244|PDB:3W39}.
HELIX 277 280 {ECO:0000244|PDB:3W39}.
STRAND 281 286 {ECO:0000244|PDB:3W39}.
SEQUENCE 362 AA; 40521 MW; A32E36370FD84F91 CRC64;
MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF
DSDAASPRTE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE NLRIALRYYN QSEAGSHTWQ
TMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL
RAYLEGLCVE WLRRHLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT
WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP
SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL
TA


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