Dbfetch

ID   1B40_HUMAN              Reviewed;         362 AA.
AC   Q04826; O19556; O19651; P01890; P30477; P30478; Q29762; Q29842;
AC   Q29855; Q30173; Q31603; Q9TPT6;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-OCT-2017, entry version 148.
DE   RecName: Full=HLA class I histocompatibility antigen, B-40 alpha chain;
DE   AltName: Full=Bw-60;
DE   AltName: Full=MHC class I antigen B*40;
DE   Flags: Precursor;
GN   Name=HLA-B; Synonyms=HLAB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ALLELE B*40:01).
RX   PubMed=2437025; DOI=10.1007/BF00404425;
RA   Ways J.W., Lawlor D.A., Wan A.M., Parham P.;
RT   "A transposable epitope of HLA-B7, B40 molecules.";
RL   Immunogenetics 25:323-328(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*40:01).
RX   PubMed=7517584; DOI=10.1111/j.1399-0039.1994.tb02294.x;
RA   Little A.-M., Domena J.D., Hildebrand W.H., Shen S.Y., Barber L.D.,
RA   Marsh S.G.E., Bias W.B., Parham P.;
RT   "HLA-B67: a member of the HLA-B16 family that expresses the ME1
RT   epitope.";
RL   Tissue Antigens 43:38-43(1994).
RN   [3]
RP   PROTEIN SEQUENCE OF 25-295 (B*40:01).
RX   PubMed=6193808; DOI=10.1021/bi00285a036;
RA   Lopez de Castro J.A., Bragado R., Strong D.M., Strominger J.L.;
RT   "Primary structure of papain-solubilized human histocompatibility
RT   antigen HLA-B40 (-Bw60). An outline of alloantigenic determinants.";
RL   Biochemistry 22:3961-3969(1983).
RN   [4]
RP   NUCLEOTIDE SEQUENCE (ALLELE B*40:02).
RX   PubMed=1362296; DOI=10.1111/j.1399-0039.1992.tb02053.x;
RA   Domena J.D., Johnston-Dow L., Parham P.;
RT   "The B*4002 allele encodes the B61 antigen: B40* is identical to
RT   B61.";
RL   Tissue Antigens 40:254-256(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE OF 13-318 (ALLELE B*40:02).
RC   TISSUE=Blood;
RX   PubMed=1481202; DOI=10.1111/j.1399-0039.1992.tb02054.x;
RA   Lin L., Watanabe Y., Tokunaga K., Kuwata S., Kohsaka T., Akaza T.;
RT   "A common Japanese haplotype HLA-A26-Cw3-B61-DR9-DQ3 carries HLA-
RT   B*4002.";
RL   Tissue Antigens 40:257-260(1992).
RN   [6]
RP   NUCLEOTIDE SEQUENCE (ALLELES B*40:03 AND B*40:04).
RX   PubMed=1317015; DOI=10.1038/357326a0;
RA   Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J.,
RA   Williams R.C., Luz R., Petzl-Erler M.L., Parham P.;
RT   "Unusual HLA-B alleles in two tribes of Brazilian Indians.";
RL   Nature 357:326-329(1992).
RN   [7]
RP   NUCLEOTIDE SEQUENCE (ALLELE B*40:05).
RX   PubMed=1385528;
RA   Hildebrand W.H., Madrigal J.A., Belich M.P., Zemmour J., Ward F.E.,
RA   Williams R.C., Parham P.;
RT   "Serologic cross-reactivities poorly reflect allelic relationships in
RT   the HLA-B12 and HLA-B21 groups. Dominant epitopes of the alpha 2
RT   helix.";
RL   J. Immunol. 149:3563-3568(1992).
RN   [8]
RP   NUCLEOTIDE SEQUENCE (ALLELE B*40:06).
RA   Herrero M.J.;
RL   Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE (ALLELE B*40:06).
RC   TISSUE=Blood;
RX   PubMed=12622774; DOI=10.1034/j.1399-0039.2003.610103.x;
RA   Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P.,
RA   Madrigal J.A., Little A.-M.;
RT   "Cloning and sequencing full-length HLA-B and -C genes.";
RL   Tissue Antigens 61:20-48(2003).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*40:08).
RX   PubMed=8525480; DOI=10.1111/j.1399-0039.1995.tb03120.x;
RA   Adams E.J., Little A.-M., Arnett K.L., Leushner J., Parham P.;
RT   "Identification of a novel HLA-B40 allele (B*4008) in a patient with
RT   leukemia.";
RL   Tissue Antigens 46:204-205(1995).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 26-206 (ALLELE B*40:09).
RX   PubMed=10372543; DOI=10.1034/j.1399-0039.1999.530504.x;
RA   Marcos C.Y., Fernandez-Vina M.A., Lazaro A.M., Moraes M.E.,
RA   Moraes J.R., Stastny P.;
RT   "Novel HLA-A and HLA-B alleles in South American Indians.";
RL   Tissue Antigens 53:476-485(1999).
RN   [12]
RP   NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*40:16).
RX   PubMed=11098929; DOI=10.1034/j.1399-0039.2000.560401.x;
RA   Ellis J.M., Mack S.J., Leke R.F.G., Quakyi I., Johnson A.H.,
RA   Hurley C.K.;
RT   "Diversity is demonstrated in class I HLA-A and HLA-B alleles in
RT   Cameroon, Africa: description of HLA-A*03012, *2612, *3006 and HLA-
RT   B*1403, *4016, *4703.";
RL   Tissue Antigens 56:291-302(2000).
RN   [13]
RP   NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*40:27).
RA   Pimtanothai N., Hurley C.K.;
RT   "Novel HLA-B allele.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [15]
RP   VARIANT [LARGE SCALE ANALYSIS] ASP-138, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [16]
RP   VARIANT [LARGE SCALE ANALYSIS] SER-155, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: Involved in the presentation of foreign antigens to the
CC       immune system.
CC   -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-
CC       microglobulin). Interacts with human herpesvirus 8 MIR1 protein
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- PTM: Polyubiquitinated in a post ER compartment by interaction
CC       with human herpesvirus 8 MIR1 protein. This targets the protein
CC       for rapid degradation via the ubiquitin system (By similarity).
CC       {ECO:0000250}.
CC   -!- POLYMORPHISM: The following alleles of B-40 are known: B*40:01,
CC       B*40:02, B*40:03 (B40-G1), B*40:04 (B40-G2), B*40:05 (BN21),
CC       B*40:06, B*40:08, B*40:09, B*40:16 and B*40:27. The sequence shown
CC       is that of B*40:02.
CC   -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U03698; AAA03719.1; -; mRNA.
DR   EMBL; L41628; AAA65040.1; -; Genomic_DNA.
DR   EMBL; L09736; AAA36224.1; -; mRNA.
DR   EMBL; D14343; BAA03277.1; -; mRNA.
DR   EMBL; M84383; AAA59633.1; -; mRNA.
DR   EMBL; M84384; AAA59634.1; -; mRNA.
DR   EMBL; M84694; AAA03661.1; -; mRNA.
DR   EMBL; X84725; CAA59215.1; -; mRNA.
DR   EMBL; AJ300180; CAC15501.1; -; Genomic_DNA.
DR   EMBL; AJ292253; CAC29021.1; -; Genomic_DNA.
DR   EMBL; L41353; AAC41923.1; -; Genomic_DNA.
DR   EMBL; L76934; AAA96270.1; -; mRNA.
DR   EMBL; AH005563; AAB70252.1; -; Genomic_DNA.
DR   EMBL; AH008232; AAD56943.1; -; Genomic_DNA.
DR   PIR; I38437; HLHU40.
DR   PIR; I56149; I56149.
DR   PIR; I59655; I59655.
DR   PIR; I61905; I61905.
DR   PIR; I61906; I61906.
DR   PIR; S52486; S52486.
DR   UniGene; Hs.654404; -.
DR   UniGene; Hs.726974; -.
DR   UniGene; Hs.77961; -.
DR   PDB; 5IEH; X-ray; 1.50 A; A=25-300.
DR   PDB; 5IEK; X-ray; 1.80 A; A=25-300.
DR   PDBsum; 5IEH; -.
DR   PDBsum; 5IEK; -.
DR   ProteinModelPortal; Q04826; -.
DR   SMR; Q04826; -.
DR   SwissPalm; Q04826; -.
DR   DMDM; 416557; -.
DR   EPD; Q04826; -.
DR   MaxQB; Q04826; -.
DR   PeptideAtlas; Q04826; -.
DR   PRIDE; Q04826; -.
DR   Ensembl; ENST00000359635; ENSP00000352656; ENSG00000206450.
DR   DisGeNET; 3106; -.
DR   GeneCards; HLA-B; -.
DR   HGNC; HGNC:4932; HLA-B.
DR   MalaCards; HLA-B; -.
DR   MIM; 142830; gene.
DR   neXtProt; NX_Q04826; -.
DR   HOVERGEN; HBG016709; -.
DR   OrthoDB; EOG091G09OH; -.
DR   Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR   Reactome; R-HSA-1236977; Endosomal/Vacuolar pathway.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-HSA-877300; Interferon gamma signaling.
DR   Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR   Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR   ChiTaRS; HLA-B; human.
DR   Proteomes; UP000005640; Chromosome 6.
DR   CleanEx; HS_HLA-B; -.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0042612; C:MHC class I protein complex; ISS:UniProtKB.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome.
DR   GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB.
DR   GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR   GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome.
DR   GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
DR   GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
DR   GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.30.500.10; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003006; Ig/MHC_CS.
DR   InterPro; IPR003597; Ig_C1-set.
DR   InterPro; IPR011161; MHC_I-like_Ag-recog.
DR   InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR   InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR   InterPro; IPR001039; MHC_I_a_a1/a2.
DR   InterPro; IPR010579; MHC_I_a_C.
DR   Pfam; PF07654; C1-set; 1.
DR   Pfam; PF00129; MHC_I; 1.
DR   Pfam; PF06623; MHC_I_C; 1.
DR   PRINTS; PR01638; MHCCLASSI.
DR   SMART; SM00407; IGc1; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF54452; SSF54452; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00290; IG_MHC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Host-virus interaction; Immunity;
KW   Membrane; MHC I; Polymorphism; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL        1     24       {ECO:0000269|PubMed:6193808}.
FT   CHAIN        25    362       HLA class I histocompatibility antigen,
FT                                B-40 alpha chain.
FT                                /FTId=PRO_0000018844.
FT   TOPO_DOM     25    308       Extracellular. {ECO:0000255}.
FT   TRANSMEM    309    332       Helical. {ECO:0000255}.
FT   TOPO_DOM    333    362       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      209    295       Ig-like C1-type.
FT   REGION       25    114       Alpha-1.
FT   REGION      115    206       Alpha-2.
FT   REGION      207    298       Alpha-3.
FT   REGION      299    308       Connecting peptide.
FT   CARBOHYD    110    110       N-linked (GlcNAc...) asparagine.
FT   DISULFID    125    188
FT   DISULFID    227    283
FT   VARIANT       9      9       L -> V (in allele B*40:01).
FT                                /FTId=VAR_016435.
FT   VARIANT      14     15       WG -> SA (in allele B*40:01).
FT                                /FTId=VAR_016436.
FT   VARIANT      17     17       V -> L (in allele B*40:01).
FT                                /FTId=VAR_016437.
FT   VARIANT      35     36       SV -> AM (in allele B*40:01 and allele
FT                                B*40:16).
FT                                /FTId=VAR_016438.
FT   VARIANT      87     87       E -> N (in allele B*40:08; requires 2
FT                                nucleotide substitutions).
FT                                /FTId=VAR_016439.
FT   VARIANT      91     91       S -> F (in allele B*40:08).
FT                                /FTId=VAR_016440.
FT   VARIANT     101    101       S -> N (in dbSNP:rs1050388).
FT                                /FTId=VAR_056363.
FT   VARIANT     118    119       TL -> II (in allele B*40:03).
FT                                /FTId=VAR_016441.
FT   VARIANT     119    119       L -> W (in allele B*40:06).
FT                                /FTId=VAR_016442.
FT   VARIANT     121    121       S -> R (in allele B*40:01 and allele
FT                                B*40:03).
FT                                /FTId=VAR_016443.
FT   VARIANT     121    121       S -> T (in allele B*40:06).
FT                                /FTId=VAR_016444.
FT   VARIANT     127    127       V -> L (in allele B*40:03).
FT                                /FTId=VAR_016445.
FT   VARIANT     137    137       H -> Y (in allele B*40:09;
FT                                dbSNP:rs1050379).
FT                                /FTId=VAR_016658.
FT   VARIANT     138    138       N -> D (in allele B*40:04 and allele
FT                                B*40:09). {ECO:0000244|PubMed:21269460}.
FT                                /FTId=VAR_016446.
FT   VARIANT     140    140       Y -> N (in allele B*40:27).
FT                                /FTId=VAR_016447.
FT   VARIANT     140    140       Y -> S (in allele B*40:04).
FT                                /FTId=VAR_016448.
FT   VARIANT     155    155       R -> S (in dbSNP:rs1050654).
FT                                {ECO:0000244|PubMed:25944712}.
FT                                /FTId=VAR_056364.
FT   VARIANT     167    167       T -> S (in allele B*40:01).
FT                                /FTId=VAR_016449.
FT   VARIANT     171    171       W -> L (in allele B*40:01).
FT                                /FTId=VAR_016450.
FT   VARIANT     176    176       V -> E (in allele B*40:05 and allele
FT                                B*40:16).
FT                                /FTId=VAR_016451.
FT   VARIANT     180    180       L -> R (in allele B*40:16).
FT                                /FTId=VAR_016655.
FT   VARIANT     187    187       E -> L (in allele B*40:05; requires 2
FT                                nucleotide substitutions).
FT                                /FTId=VAR_016452.
FT   VARIANT     201    202       ET -> DK (in allele B*40:01 and allele
FT                                B*40:16).
FT                                /FTId=VAR_016453.
FT   VARIANT     204    204       Q -> E (in allele B*40:01 and allele
FT                                B*40:16).
FT                                /FTId=VAR_016454.
FT   VARIANT     306    306       V -> I (in dbSNP:rs1131500).
FT                                /FTId=VAR_056365.
FT   VARIANT     329    329       A -> T (in dbSNP:rs1051488).
FT                                /FTId=VAR_056366.
FT   VARIANT     349    349       C -> S (in dbSNP:rs2308655).
FT                                /FTId=VAR_061413.
FT   VARIANT     349    349       C -> Y (in dbSNP:rs2308655).
FT                                /FTId=VAR_061414.
FT   CONFLICT    167    167       Missing (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   STRAND       27     36       {ECO:0000244|PDB:5IEH}.
FT   STRAND       41     43       {ECO:0000244|PDB:5IEK}.
FT   STRAND       45     52       {ECO:0000244|PDB:5IEH}.
FT   STRAND       55     61       {ECO:0000244|PDB:5IEH}.
FT   STRAND       64     66       {ECO:0000244|PDB:5IEH}.
FT   HELIX        74     76       {ECO:0000244|PDB:5IEH}.
FT   HELIX        81    108       {ECO:0000244|PDB:5IEH}.
FT   STRAND      118    127       {ECO:0000244|PDB:5IEH}.
FT   STRAND      133    142       {ECO:0000244|PDB:5IEH}.
FT   STRAND      145    150       {ECO:0000244|PDB:5IEH}.
FT   STRAND      157    161       {ECO:0000244|PDB:5IEH}.
FT   HELIX       162    173       {ECO:0000244|PDB:5IEH}.
FT   HELIX       176    185       {ECO:0000244|PDB:5IEH}.
FT   HELIX       187    198       {ECO:0000244|PDB:5IEH}.
FT   HELIX       200    203       {ECO:0000244|PDB:5IEH}.
FT   STRAND      210    217       {ECO:0000244|PDB:5IEH}.
FT   STRAND      219    235       {ECO:0000244|PDB:5IEH}.
FT   STRAND      238    243       {ECO:0000244|PDB:5IEH}.
FT   HELIX       249    251       {ECO:0000244|PDB:5IEH}.
FT   STRAND      261    263       {ECO:0000244|PDB:5IEH}.
FT   STRAND      265    274       {ECO:0000244|PDB:5IEH}.
FT   HELIX       278    280       {ECO:0000244|PDB:5IEH}.
FT   STRAND      281    286       {ECO:0000244|PDB:5IEH}.
FT   STRAND      294    296       {ECO:0000244|PDB:5IEH}.
SQ   SEQUENCE   362 AA;  40505 MW;  7D66503ACD865152 CRC64;
     MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFITVG YVDDTLFVRF
     DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTLQ
     SMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARVAEQL
     RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT
     WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP
     SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL
     TA
//