<p>An evidence describes the source of an annotation, e.g. an experiment that has been published in the scientific literature, an orthologous protein, a record from another database, etc.</p>
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<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli
<p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>
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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Antigen-presenting major histocompatibility complex class I (MHCI) molecule. In complex with B2M/beta 2 microglobulin displays primarily viral and tumor-derived peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-B-restricted CD8-positive T cells, guiding antigen-specific T cell immune response to eliminate infected or transformed cells (PubMed:25808313, PubMed:29531227, PubMed:9620674, PubMed:23209413). May also present self-peptides derived from the signal sequence of secreted or membrane proteins, although T cells specific for these peptides are usually inactivated to prevent autoreactivity (PubMed:7743181, PubMed:18991276). Both the peptide and the MHC molecule are recognized by TCR, the peptide is responsible for the fine specificity of antigen recognition and MHC residues account for the MHC restriction of T cells (PubMed:29531227, PubMed:9620674, PubMed:24600035). Typically presents intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via constitutive proteasome and IFNG-induced immunoproteasome (PubMed:23209413). Can bind different peptides containing allele-specific binding motifs, which are mainly defined by anchor residues at position 2 and 9 (PubMed:25808313, PubMed:29531227).7 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
Cited for: X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 25-300 (ALLELE B*51:01) IN COMPLEX WITH B2M AND PEPTIDE, INTERACTION WITH TCR, FUNCTION (ALLELE B*51:01).
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 25-300 (ALLELE B*07:02) IN COMPLEX WITH B2M AND HIV-1 PEPTIDES, DISULFIDE BOND, FUNCTION (ALLELE B*07:02), DOMAIN.
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) (ALLELE B*07:02) IN COMPLEX WITH B2M AND PEPTIDE, DISULFIDE BOND, INTERACTION WITH TCR, FUNCTION (ALLELE B*07:02).
Allele B*07:02: Displays peptides sharing a common signature motif, namely a Pro residue at position 2 and mainly a Leu anchor residue at the C-terminus (PubMed:7743181). Presents a long peptide (APRGPHGGAASGL) derived from the cancer-testis antigen CTAG1A/NY-ESO-1, eliciting a polyclonal CD8-positive T cell response against tumor cells (PubMed:29531227). Presents viral epitopes derived from HIV-1 gag-pol (TPQDLNTML) and Nef (RPQVPLRPM) (PubMed:25808313). Presents an immunodominant epitope derived from SARS-CoV-2 N/nucleoprotein (SPRWYFYYL) (PubMed:32887977). Displays self-peptides including a peptide derived from the signal sequence of HLA-DPB1 (APRTVALTA) (PubMed:7743181).4 Publications
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 25-300 (ALLELE B*07:02) IN COMPLEX WITH B2M AND HIV-1 PEPTIDES, DISULFIDE BOND, FUNCTION (ALLELE B*07:02), DOMAIN.
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) (ALLELE B*07:02) IN COMPLEX WITH B2M AND PEPTIDE, DISULFIDE BOND, INTERACTION WITH TCR, FUNCTION (ALLELE B*07:02).
Allele B*08:01: Presents to CD8-positive T cells viral epitopes derived from EBV/HHV-4 EBNA3 (QAKWRLQTL), eliciting cytotoxic T cell response.1 Publication
Cited for: FUNCTION (ALLELES B*08:01; B*27:05 AND B*44:02), INTERACTION WITH TAP1-TAP2, SUBCELLULAR LOCATION.
Allele B*13:02: Presents multiple HIV-1 epitopes derived from gag (RQANFLGKI, GQMREPRGSDI), nef (RQDILDLWI), gag-pol (RQYDQILIE, GQGQWTYQI) and rev (LQLPPLERL), all having in common a Gln residue at position 2 and mainly hydrophobic amino acids Leu, Ile or Val at the C-terminus. Associated with succesful control of HIV-1 infection.1 Publication
Allele B*18:01: Preferentially presents octomeric and nonameric peptides sharing a common motif, namely a Glu at position 2 and Phe or Tyr anchor residues at the C-terminus (PubMed:14978097, PubMed:23749632, PubMed:18991276). Presents an EBV/HHV-4 epitope derived from BZLF1 (SELEIKRY) (PubMed:23749632). May present to CD8-positive T cells an antigenic peptide derived from MAGEA3 (MEVDPIGHLY), triggering an anti-tumor immune response (PubMed:12366779). May display a broad repertoire of self-peptides with a preference for peptides derived from RNA-binding proteins (PubMed:14978097).4 Publications
Allele B*27:05: Presents to CD8-positive T cells immunodominant viral epitopes derived from HCV POLG (ARMILMTHF), HIV-1 gag (KRWIILGLNK), IAV NP (SRYWAIRTR), SARS-CoV-2 N/nucleoprotein (QRNAPRITF), EBV/HHV-4 EBNA4 (HRCQAIRKK) and EBV/HHV-4 EBNA6 (RRIYDLIEL), confering longterm protection against viral infection (PubMed:19139562, PubMed:18385228, PubMed:15113903, PubMed:9620674, PubMed:32887977). Can present self-peptides derived from cytosolic and nuclear proteins. All peptides carry an Arg at position 2 (PubMed:1922338). The peptide-bound form interacts with NK cell inhibitory receptor KIR3DL1 and inhibits NK cell activation in a peptide-specific way, being particularly sensitive to the nature of the amino acid side chain at position 8 of the antigenic peptide (PubMed:8879234, PubMed:15657948). KIR3DL1 fails to recognize HLA-B*27:05 in complex with B2M and EBV/HHV-4 EBNA6 (RRIYDLIEL) peptide, which can lead to increased activation of NK cells during infection (PubMed:15657948). May present an altered repertoire of peptides in the absence of TAP1-TAP2 and TAPBPL (PubMed:9620674).7 Publications
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 25-300 (ALLELE B*27:05) IN COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE B*27:05).
Allele B*40:01: Presents immunodominant viral epitopes derived from EBV/HHV-4 LMP2 (IEDPPFNSL) and SARS-CoV-2 N/nucleoprotein (MEVTPSGTWL), triggering memory CD8-positive T cell response (PubMed:18991276, PubMed:32887977). Displays self-peptides sharing a signature motif, namely a Glu at position 2 and a Leu anchor residue at the C-terminus (PubMed:18991276).2 Publications
Cited for: FUNCTION (ALLELES B*07:02; B*27:05 AND B*40:01).
Allele B*41:01: Displays self-peptides sharing a signature motif, namely a Glu at position 2 and Ala or Pro anchor residues at the C-terminus.1 Publication
Cited for: FUNCTION (ALLELES B*18:01; B*40:01; B*41:01; B*44:02; B*45:01; B*47:01; B*49:01 AND B*50:01).
Allele B*44:02: Presents immunodominant viral epitopes derived from EBV/HHV-4 EBNA4 (VEITPYKPTW) and EBNA6 (AEGGVGWRHW, EENLLDFVRF), triggering memory CD8-positive T cell response (PubMed:9620674, PubMed:18991276). Displays self-peptides sharing a signature motif, namely a Glu at position 2 and Phe, Tyr or Trp anchor residues at the C-terminus (PubMed:18991276).2 Publications
Cited for: FUNCTION (ALLELES B*18:01; B*40:01; B*41:01; B*44:02; B*45:01; B*47:01; B*49:01 AND B*50:01).
Allele B*45:01: Displays self-peptides sharing a signature motif, namely a Glu at position 2 and Ala or Pro anchor residues at the C-terminus.1 Publication
Cited for: FUNCTION (ALLELES B*18:01; B*40:01; B*41:01; B*44:02; B*45:01; B*47:01; B*49:01 AND B*50:01).
Allele B*46:01: Preferentially presents nonameric peptides sharing a signature motif, namely Ala and Leu at position 2 and Tyr, Phe, Leu, or Met anchor residues at the C-terminus. The peptide-bound form interacts with KIR2DL3 and inhibits NK cell cytotoxic response in a peptide-specific way.1 Publication
Cited for: FUNCTION (ALLELE B*46:01), INTERACTION WITH KIR2DL3.
Allele B*47:01: Displays self-peptides sharing a signature motif, namely an Asp at position 2 and Leu or Met anchor residues at the C-terminus.1 Publication
Cited for: FUNCTION (ALLELES B*18:01; B*40:01; B*41:01; B*44:02; B*45:01; B*47:01; B*49:01 AND B*50:01).
Allele B*49:01: Displays self-peptides sharing a signature motif, namely a Glu at position 2 and Ile or Val anchor residues at the C-terminus.1 Publication
Cited for: FUNCTION (ALLELES B*18:01; B*40:01; B*41:01; B*44:02; B*45:01; B*47:01; B*49:01 AND B*50:01).
Allele B*50:01: Displays self-peptides sharing a signature motif, namely a Glu at position 2 and Ala or Pro anchor residues at the C-terminus.1 Publication
Cited for: FUNCTION (ALLELES B*18:01; B*40:01; B*41:01; B*44:02; B*45:01; B*47:01; B*49:01 AND B*50:01).
Allele B*51:01: Presents an octomeric HIV-1 epitope derived from gag-pol (TAFTIPSI) to the public TRAV17/TRBV7-3 TCR clonotype, strongly suppressing HIV-1 replication.1 Publication
Cited for: X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 25-300 (ALLELE B*51:01) IN COMPLEX WITH B2M AND PEPTIDE, INTERACTION WITH TCR, FUNCTION (ALLELE B*51:01).
Allele B*54:01: Displays peptides sharing a common signature motif, namely a Pro residue at position 2 and Ala anchor residue at the C-terminus.1 Publication
Cited for: FUNCTION (ALLELES B*07:02; B*54:01; B*55:01; B*56:01 AND B*67:01).
Allele B*55:01: Displays peptides sharing a common signature motif, namely a Pro residue at position 2 and Ala anchor residue at the C-terminus.1 Publication
Cited for: FUNCTION (ALLELES B*07:02; B*54:01; B*55:01; B*56:01 AND B*67:01).
Allele B*56:01: Displays peptides sharing a common signature motif, namely a Pro residue at position 2 and Ala anchor residue at the C-terminus.1 Publication
Cited for: FUNCTION (ALLELES B*08:01 AND B*57:01), DOMAIN, BW4 AND BW6 MOTIFS, INTERACTION WITH KIR3DL1, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS ILE-104 AND ARG-107.
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 25-299 (ALLELE B*57:01) IN COMPLEX WITH B2M AND SELF-PEPTIDE, INTERACTION WITH KIR3DL1, DOMAIN, BW4 MOTIF, FUNCTION (ALLELE B*57:01).
Allele B*67:01: Displays peptides sharing a common signature motif, namely a Pro residue at position 2 and Leu anchor residue at the C-terminus.1 Publication
Cited for: FUNCTION (ALLELES B*07:02; B*54:01; B*55:01; B*56:01 AND B*67:01).
Sites
Feature key
Position(s)
DescriptionActions
Graphical view
Length
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 25-300 (ALLELE B*07:02) IN COMPLEX WITH B2M AND HIV-1 PEPTIDES, DISULFIDE BOND, FUNCTION (ALLELE B*07:02), DOMAIN.
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 25-300 (ALLELE B*07:02) IN COMPLEX WITH B2M AND HIV-1 PEPTIDES, DISULFIDE BOND, FUNCTION (ALLELE B*07:02), DOMAIN.
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 25-300 (ALLELE B*07:02) IN COMPLEX WITH B2M AND HIV-1 PEPTIDES, DISULFIDE BOND, FUNCTION (ALLELE B*07:02), DOMAIN.
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 25-300 (ALLELE B*07:02) IN COMPLEX WITH B2M AND HIV-1 PEPTIDES, DISULFIDE BOND, FUNCTION (ALLELE B*07:02), DOMAIN.
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 25-300 (ALLELE B*07:02) IN COMPLEX WITH B2M AND HIV-1 PEPTIDES, DISULFIDE BOND, FUNCTION (ALLELE B*07:02), DOMAIN.
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 25-300 (ALLELE B*07:02) IN COMPLEX WITH B2M AND HIV-1 PEPTIDES, DISULFIDE BOND, FUNCTION (ALLELE B*07:02), DOMAIN.
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 25-300 (ALLELE B*07:02) IN COMPLEX WITH B2M AND HIV-1 PEPTIDES, DISULFIDE BOND, FUNCTION (ALLELE B*07:02), DOMAIN.
1
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
chaperone binding Source: UniProtKB
<p>Inferred from Physical Interaction</p>
<p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p>
Inferred from physical interactioni
peptide antigen binding Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
defense response Source: UniProtKB
<p>Traceable Author Statement</p>
<p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p>
Traceable author statementi
detection of bacterium Source: UniProtKB
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
HLA class I histocompatibility antigen, B alpha chain
Alternative name(s):
Human leukocyte antigen B
Short name:
HLA-B
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
<p>Manually validated information which has been imported from another database.</p>
<p><a href="/manual/evidences#ECO:0000312">More...</a></p>
Manual assertion inferred from database entriesi
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
UP000005640
<p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Cited for: FUNCTION (ALLELES B*08:01 AND B*57:01), DOMAIN, BW4 AND BW6 MOTIFS, INTERACTION WITH KIR3DL1, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS ILE-104 AND ARG-107.
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p>
<p><a href="/manual/evidences#ECO:0000305">More...</a></p>
Manual assertion inferred by curator fromi
integral component of plasma membrane Source: UniProtKB
<p>Non-traceable Author Statement</p>
<p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#nas">GO evidence code guide</a></p>
Non-traceable author statementi
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Disease susceptibility is associated with variants affecting the gene represented in this entry. Increased susceptibility to Stevens-Johnson syndrome is conferred by allele B*15:02.1 Publication
Cited for: ASSOCIATION OF ALLELE B*15:02 WITH STEVENS-JOHNSON SYNDROME.
Disease descriptionA rare blistering mucocutaneous disease that share clinical and histopathologic features with toxic epidermal necrolysis. Both disorders are characterized by high fever, malaise, and a rapidly developing blistering exanthema of macules and target-like lesions accompanied by mucosal involvement. Stevens-Johnson syndrome is a milder disease characterized by destruction and detachment of the skin epithelium and mucous membranes involving less than 10% of the body surface area. Ocular symptoms include ulcerative conjunctivitis, keratitis, iritis, uveitis and sometimes blindness. It can be caused by a severe adverse reaction to particular types of medication, although Mycoplasma infections may induce some cases.
Disease susceptibility is associated with variants affecting the gene represented in this entry. A restricted number of HLA-B*27 subtypes can be associated with ankylosing spondylitis and other B*27-related diseases, and an elevated frequency of the B*27:02 allele in ankylosing spondylitis patients is identified. The allele B*27:07 seems to have a protective role in some populations because it was found only in the healthy controls.1 Publication
Cited for: ASSOCIATION WITH SPDA1, POSSIBLE PROTECTIVE ROLE OF ALLELE B*27:07.
Disease descriptionA chronic rheumatic disease with multifactorial inheritance. It includes a spectrum of related disorders comprising ankylosing spondylitis, a subset of psoriatic arthritis, reactive arthritis (e.g. Reiter syndrome), arthritis associated with inflammatory bowel disease and undifferentiated spondyloarthropathy. These disorders may occur simultaneously or sequentially in the same patient, probably representing various phenotypic expressions of the same disease. Ankylosing spondylitis is the form of rheumatoid arthritis affecting the spine and is considered the prototype of seronegative spondyloarthropathies. It produces pain and stiffness as a result of inflammation of the sacroiliac, intervertebral, and costovertebral joints.
There is evidence that HLA-B*51 is associated with susceptibility to Behcet disease (BD). However, it is not certain whether HLA-B*51 itself or a closely linked gene is responsible for susceptibility. The world distribution of HLA-B*51 in healthy people corresponds to the global distribution of BD; in Southern hemisphere countries (Africa, South Pacific, etc.) and in some parts of Europe, the prevalence of HLA-B*51 in healthy people is low or null, corresponding to a low prevalence of BD. The wide variation that exists in the relative risk of HLA-B*51 would support other nongenetic risk factors.1 Publication
Cited for: ASSOCIATION WITH ABACAVIR HYPERSENSITIVITY.
Allele group B*08 is associated with increased susceptibility to rheumatoid arthritis, where affected individuals have antibodies to cyclic citrullinated peptide (anti-CCP-positive rheumatoid arthritis).1 Publication
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000018833
HLA class I histocompatibility antigen, B alpha chainAddBLAST
338
Amino acid modifications
Feature key
Position(s)
DescriptionActions
Graphical view
Length
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110.
1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p>
<p><a href="/manual/evidences#ECO:0000255">More...</a></p>
Manual assertion according to rulesi
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 25-300 (ALLELE B*07:02) IN COMPLEX WITH B2M AND HIV-1 PEPTIDES, DISULFIDE BOND, FUNCTION (ALLELE B*07:02), DOMAIN.
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) (ALLELE B*07:02) IN COMPLEX WITH B2M AND PEPTIDE, DISULFIDE BOND, INTERACTION WITH TCR, FUNCTION (ALLELE B*07:02).
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 25-300 (ALLELE B*07:02) IN COMPLEX WITH B2M AND HIV-1 PEPTIDES, DISULFIDE BOND, FUNCTION (ALLELE B*07:02), DOMAIN.
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) (ALLELE B*07:02) IN COMPLEX WITH B2M AND PEPTIDE, DISULFIDE BOND, INTERACTION WITH TCR, FUNCTION (ALLELE B*07:02).
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Heterotrimer that consists of an alpha chain HLA-B, a beta chain B2M and a peptide (peptide-HLA-B-B2M) (PubMed:25808313, PubMed:29531227, PubMed:15657948, PubMed:17057332, PubMed:22020283, PubMed:24600035). Early in biogenesis, HLA-B-B2M dimer interacts with the components of the peptide-loading complex composed of TAPBP, TAP1-TAP2, TAPBPL, PDIA3/ERP57 and CALR (PubMed:9036970, PubMed:9620674, PubMed:26439010, PubMed:26416272).
Interacts with TAP1-TAP2 transporter via TAPBP; this interaction is obligatory for the loading of peptide epitopes delivered to the ER by TAP1-TAP2 transporter (PubMed:9036970, PubMed:9620674).
Interacts with TAPBPL; TAPBPL binds peptide-free HLA-B-B2M complexes or those loaded with low affinity peptides, likely facilitating peptide exchange for higher affinity peptides (PubMed:26439010). Only optimally assembled peptide-HLA-B-B2M trimer translocates to the surface of antigen-presenting cells, where it interacts with TCR and CD8 coreceptor on the surface of T cells. HLA-B (via polymorphic alpha-1 and alpha-2 domains) interacts with antigen-specific TCR (via CDR1, CDR2 and CDR3 domains) (PubMed:29531227, PubMed:24600035). One HLA-B molecule (mainly via nonpolymorphic alpha-3 domain) interacts with one CD8A homodimer (via CDR-like loop); this interaction insures peptide-HLA-B-B2M recognition by CD8-positive T cells only (PubMed:29531227). Allele B*57:01 interacts (via Bw4 motif) with KIR3DL1 (via Ig-like C2-type domain); this interaction may interfere with peptide binding (PubMed:22020283, PubMed:25480565). Allele B*46:01 interacts with KIR2DL3 (PubMed:28514659).
12 Publications
Manual assertion based on experiment ini
Ref.56
"Prominence of beta 2-microglobulin, class I heavy chain conformation, and tapasin in the interactions of class I heavy chain with calreticulin and the transporter associated with antigen processing." Solheim J.C., Harris M.R., Kindle C.S., Hansen T.H. J. Immunol. 158:2236-2241(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH B2M, INTERACTION WITH CALR AND TAP1-TAP2.
Cited for: FUNCTION (ALLELES B*08:01 AND B*57:01), DOMAIN, BW4 AND BW6 MOTIFS, INTERACTION WITH KIR3DL1, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS ILE-104 AND ARG-107.
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 25-299 (ALLELE B*57:01) IN COMPLEX WITH B2M AND SELF-PEPTIDE, INTERACTION WITH KIR3DL1, DOMAIN, BW4 MOTIF, FUNCTION (ALLELE B*57:01).
Cited for: X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 25-300 (ALLELE B*51:01) IN COMPLEX WITH B2M AND PEPTIDE, INTERACTION WITH TCR, FUNCTION (ALLELE B*51:01).
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 25-300 (ALLELE B*07:02) IN COMPLEX WITH B2M AND HIV-1 PEPTIDES, DISULFIDE BOND, FUNCTION (ALLELE B*07:02), DOMAIN.
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) (ALLELE B*07:02) IN COMPLEX WITH B2M AND PEPTIDE, DISULFIDE BOND, INTERACTION WITH TCR, FUNCTION (ALLELE B*07:02).
(Microbial infection) Interacts with HTLV-1 accessory protein p12I.
Cited for: INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I (MICROBIAL INFECTION).
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More...</a></p>
Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
Feature key
Position(s)
DescriptionActions
Graphical view
Length
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi
Cited for: FUNCTION (ALLELES B*08:01 AND B*57:01), DOMAIN, BW4 AND BW6 MOTIFS, INTERACTION WITH KIR3DL1, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS ILE-104 AND ARG-107.
7
<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
The alpha-1 domain is a structural part of the peptide-binding cleft (PubMed:25808313). Residues 101-107 determine Bw4/Bw6 motifs, which serologically distinguish HLA-B alleles. Each HLA-B allele posseses either the Bw4 or Bw6 motif. Only HLA-B alleles bearing the Bw4 epitope are recognized by NK cell inhibitory receptor KIR3DL1 (PubMed:25480565, PubMed:22020283).3 Publications
Cited for: FUNCTION (ALLELES B*08:01 AND B*57:01), DOMAIN, BW4 AND BW6 MOTIFS, INTERACTION WITH KIR3DL1, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS ILE-104 AND ARG-107.
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 25-299 (ALLELE B*57:01) IN COMPLEX WITH B2M AND SELF-PEPTIDE, INTERACTION WITH KIR3DL1, DOMAIN, BW4 MOTIF, FUNCTION (ALLELE B*57:01).
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 25-300 (ALLELE B*07:02) IN COMPLEX WITH B2M AND HIV-1 PEPTIDES, DISULFIDE BOND, FUNCTION (ALLELE B*07:02), DOMAIN.
The alpha-2 domain is a structural part of the peptide-binding cleft (PubMed:25808313). Mediates the interaction with TAP1-TAP2 complex (By similarity).By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p>
<p><a href="/manual/evidences#ECO:0000250">More...</a></p>
Manual assertion inferred from sequence similarity toi
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 25-300 (ALLELE B*07:02) IN COMPLEX WITH B2M AND HIV-1 PEPTIDES, DISULFIDE BOND, FUNCTION (ALLELE B*07:02), DOMAIN.
The alpha-3 Ig-like domain mediates the interaction with CD8 coreceptor.By similarity
Manual assertion inferred from sequence similarity toi
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry has 1 described isoform and 25 potential isoforms that are computationally mapped.Show allAlign All
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i5E5A7BDE031403D6
<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi
HLA class I histocompatibility antigen B alpha chain (HLA class I histocompatibility antigen, B alpha chain) (Leukocyte antigen (HLA) class I molecule) (Lymphocyte antigen) (MHC class I antigen) (MHC class I protein) (Major histocompatibility complex, class I, B)
HLA-B HLA-B*4403, HLA-B*44031, HLA-B*44032
362
Annotation score:
Annotation score:2 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
HLA class I antigen (HLA class I histocompatibility antigen) (HLA class I histocompatibility antigen, B alpha chain) (MHC class I antigen) (MICA protein)
HLA-B MICA
362
Annotation score:
Annotation score:2 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
HLA class I histocompatibility antigen (HLA class I histocompatibility antigen, B alpha chain) (HLA-B*18:01:01:NEW) (MHC class I antigen) (MHC class I protein)
HLA-B HLA B
362
Annotation score:
Annotation score:2 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
HLA class I histocompatibility antigen, B alpha chain
HLA-B
363
Annotation score:
Annotation score:2 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
HLA class I antigen (HLA class I histocompatibility antigen B alpha chain) (HLA class I histocompatibility antigen, B alpha chain) (MHC class I antigen) (MHC class I protein) (MHC class I protein (HLA-B))
HLA-B
362
Annotation score:
Annotation score:2 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
HLA class I histocompatibility antigen B alpha chain (HLA class I histocompatibility antigen, B alpha chain) (MHC class I antigen) (MHC class I protein)
HLA-B
362
Annotation score:
Annotation score:2 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
HLA class I histocompatibility antigen, B alpha chain
HLA-B
241
Annotation score:
Annotation score:2 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
HLA class I histocompatibility antigen, B alpha chain
HLA-B
241
Annotation score:
Annotation score:2 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
HLA class I histocompatibility antigen, B alpha chain
HLA-B
241
Annotation score:
Annotation score:1 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
HLA class I histocompatibility antigen, B alpha chain
HLA-B
241
Annotation score:
Annotation score:1 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
<p>This subsection of the 'Sequence' section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement%5Fin%5Fdisease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi
The most polymorphic of the mammalian genome. Polymorphic residues encode for alpha-1 and alpha-2 domains of the peptide-binding cleft, where they contribute to variations in peptide binding and TCR recognition among different alleles. The human population is estimated to have millions of HLA-B alleles. But only 17 common HLA-A alleles are considered core alleles, representing all functionally significant variation (polymorphism) in alpha-1 and alpha-2 domains. These are: B*07:02; B*08:01; B*13:02; B*15:01; B*18:01; B*27:05; B*35:01; B*37:01; B*38:01; B*40:01; B*44:02; B*45:01; B*51:01; B*54:01; B*57:01 and B*73:01. Among these, B*07:02; B*15:01; B*18:01; B*37:01; B*51:01; B*54:01; B*57:01 and B*73:01, were likely passed by introgression from archaic to modern humans. Functional alleles of more recent origin (non-core) were derived by recombination (PubMed:28650991). The sequence shown is that of B*07:02. The sequences of core alleles and common representative alleles of serologically distinct allele groups are described as variants of B*07:02.1 Publication
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_082483
"Absence of polymorphism between HLA-B27 genomic exon sequences isolated from normal donors and ankylosing spondylitis patients." Coppin H.L., McDevitt H.O. J. Immunol. 137:2168-2172(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-298 (ALLELE B*27:05).
"Oncology, C.W.Bill Young DoD Marrow Donor Recruitment and Research Program, 11333 Woodglen Dr, Rockville, MD 20852, USA." Lazaro A.M., Hou L., Enriquez E., Persaud M., Hurley C.K. Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases
"Absence of polymorphism between HLA-B27 genomic exon sequences isolated from normal donors and ankylosing spondylitis patients." Coppin H.L., McDevitt H.O. J. Immunol. 137:2168-2172(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-298 (ALLELE B*27:05).
"Oncology, C.W.Bill Young DoD Marrow Donor Recruitment and Research Program, 11333 Woodglen Dr, Rockville, MD 20852, USA." Lazaro A.M., Hou L., Enriquez E., Persaud M., Hurley C.K. Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases
"Absence of polymorphism between HLA-B27 genomic exon sequences isolated from normal donors and ankylosing spondylitis patients." Coppin H.L., McDevitt H.O. J. Immunol. 137:2168-2172(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-298 (ALLELE B*27:05).
"Oncology, C.W.Bill Young DoD Marrow Donor Recruitment and Research Program, 11333 Woodglen Dr, Rockville, MD 20852, USA." Lazaro A.M., Hou L., Enriquez E., Persaud M., Hurley C.K. Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases
"Absence of polymorphism between HLA-B27 genomic exon sequences isolated from normal donors and ankylosing spondylitis patients." Coppin H.L., McDevitt H.O. J. Immunol. 137:2168-2172(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-298 (ALLELE B*27:05).
"Oncology, C.W.Bill Young DoD Marrow Donor Recruitment and Research Program, 11333 Woodglen Dr, Rockville, MD 20852, USA." Lazaro A.M., Hou L., Enriquez E., Persaud M., Hurley C.K. Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases
"Absence of polymorphism between HLA-B27 genomic exon sequences isolated from normal donors and ankylosing spondylitis patients." Coppin H.L., McDevitt H.O. J. Immunol. 137:2168-2172(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-298 (ALLELE B*27:05).
"Oncology, C.W.Bill Young DoD Marrow Donor Recruitment and Research Program, 11333 Woodglen Dr, Rockville, MD 20852, USA." Lazaro A.M., Hou L., Enriquez E., Persaud M., Hurley C.K. Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases
"Absence of polymorphism between HLA-B27 genomic exon sequences isolated from normal donors and ankylosing spondylitis patients." Coppin H.L., McDevitt H.O. J. Immunol. 137:2168-2172(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-298 (ALLELE B*27:05).
"Oncology, C.W.Bill Young DoD Marrow Donor Recruitment and Research Program, 11333 Woodglen Dr, Rockville, MD 20852, USA." Lazaro A.M., Hou L., Enriquez E., Persaud M., Hurley C.K. Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region." Shiina S., Tamiya G., Oka A., Inoko H. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
"Absence of polymorphism between HLA-B27 genomic exon sequences isolated from normal donors and ankylosing spondylitis patients." Coppin H.L., McDevitt H.O. J. Immunol. 137:2168-2172(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-298 (ALLELE B*27:05).
"Oncology, C.W.Bill Young DoD Marrow Donor Recruitment and Research Program, 11333 Woodglen Dr, Rockville, MD 20852, USA." Lazaro A.M., Hou L., Enriquez E., Persaud M., Hurley C.K. Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region." Shiina S., Tamiya G., Oka A., Inoko H. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region." Shiina S., Tamiya G., Oka A., Inoko H. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
"Absence of polymorphism between HLA-B27 genomic exon sequences isolated from normal donors and ankylosing spondylitis patients." Coppin H.L., McDevitt H.O. J. Immunol. 137:2168-2172(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-298 (ALLELE B*27:05).
"Oncology, C.W.Bill Young DoD Marrow Donor Recruitment and Research Program, 11333 Woodglen Dr, Rockville, MD 20852, USA." Lazaro A.M., Hou L., Enriquez E., Persaud M., Hurley C.K. Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases
"Absence of polymorphism between HLA-B27 genomic exon sequences isolated from normal donors and ankylosing spondylitis patients." Coppin H.L., McDevitt H.O. J. Immunol. 137:2168-2172(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-298 (ALLELE B*27:05).
"Oncology, C.W.Bill Young DoD Marrow Donor Recruitment and Research Program, 11333 Woodglen Dr, Rockville, MD 20852, USA." Lazaro A.M., Hou L., Enriquez E., Persaud M., Hurley C.K. Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases