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P03989

- 1B27_HUMAN

UniProt

P03989 - 1B27_HUMAN

Protein

HLA class I histocompatibility antigen, B-27 alpha chain

Gene

HLA-B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (13 Aug 1987)
      Previous versions | rss
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    Functioni

    Involved in the presentation of foreign antigens to the immune system.

    GO - Molecular functioni

    1. peptide antigen 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. defense response Source: UniProtKB
    8. detection of bacterium Source: UniProtKB
    9. immune response Source: UniProtKB
    10. interferon-gamma-mediated signaling pathway Source: Reactome
    11. positive regulation of T cell mediated cytotoxicity Source: InterPro
    12. regulation of immune response Source: Reactome
    13. type I interferon signaling pathway Source: Reactome
    14. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, Immunity

    Enzyme and pathway databases

    ReactomeiREACT_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, B-27 alpha chain
    Alternative name(s):
    MHC class I antigen B*27
    Gene namesi
    Name:HLA-B
    Synonyms:HLAB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:4932. HLA-B.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: UniProt
    2. early endosome membrane Source: Reactome
    3. endoplasmic reticulum Source: UniProt
    4. ER to Golgi transport vesicle membrane Source: Reactome
    5. extracellular vesicular exosome Source: UniProt
    6. Golgi apparatus Source: UniProt
    7. Golgi membrane Source: Reactome
    8. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
    9. membrane Source: UniProtKB
    10. MHC class I protein complex Source: UniProt
    11. phagocytic vesicle membrane Source: Reactome
    12. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane, MHC I

    Pathology & Biotechi

    Involvement in diseasei

    Spondyloarthropathy 1 (SPDA1) [MIM:106300]: A 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.
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. A restricted number of HLA-B27 subtypes can be associated with ankylosing spondylitis and other B27-related diseases, and an elevated frequency of the B*2702 allele in ankylosing spondylitis patients is identified. The allele B*2707 seems to have a protective role some populations because it was found only in the healthy controls.

    Organism-specific databases

    MIMi106300. phenotype.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 362338HLA class I histocompatibility antigen, B-27 alpha chainPRO_0000018839Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi110 – 1101N-linked (GlcNAc...)1 Publication
    Disulfide bondi125 ↔ 188
    Disulfide bondi227 ↔ 283

    Post-translational modificationi

    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.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP03989.
    PRIDEiP03989.

    Expressioni

    Gene expression databases

    CleanExiHS_HLA-B.
    GenevestigatoriP03989.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). Interacts with human herpesvirus 8 MIR1 protein By similarity.By similarity

    Protein-protein interaction databases

    DIPiDIP-6188N.
    IntActiP03989. 1 interaction.
    MINTiMINT-247525.

    Structurei

    Secondary structure

    1
    362
    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
    Helixi74 – 763
    Helixi81 – 10828
    Beta strandi113 – 1153
    Beta strandi118 – 12710
    Beta strandi133 – 14210
    Beta strandi145 – 1506
    Beta strandi157 – 1615
    Helixi162 – 17312
    Helixi176 – 18510
    Helixi187 – 19812
    Turni199 – 2046
    Beta strandi210 – 21910
    Beta strandi222 – 23514
    Beta strandi238 – 2436
    Helixi249 – 2513
    Beta strandi252 – 2543
    Beta strandi261 – 2633
    Beta strandi265 – 27410
    Helixi278 – 2803
    Beta strandi281 – 2866
    Beta strandi290 – 2923
    Beta strandi294 – 2963

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HSAX-ray2.10A/D25-300[»]
    1JGDX-ray1.90A25-300[»]
    1JGEX-ray2.10A25-300[»]
    1K5NX-ray1.09A25-300[»]
    1OF2X-ray2.20A25-300[»]
    1OGTX-ray1.47A25-300[»]
    1ROGmodel-A25-206[»]
    1ROHmodel-A25-206[»]
    1ROImodel-A25-206[»]
    1ROJmodel-A25-206[»]
    1ROKmodel-A25-206[»]
    1ROLmodel-A25-206[»]
    1UXSX-ray1.55A25-300[»]
    1UXWX-ray1.71A25-300[»]
    1W0VX-ray2.27A25-300[»]
    1W0WX-ray2.10A25-300[»]
    2A83X-ray1.40A25-300[»]
    2BSRX-ray2.30A25-300[»]
    2BSSX-ray2.00A25-300[»]
    2BSTX-ray2.10A25-300[»]
    3B3IX-ray1.86A25-300[»]
    3B6SX-ray1.80A25-300[»]
    3BP4X-ray1.85A25-300[»]
    3BP7X-ray1.80A25-300[»]
    3CZFX-ray1.20A25-300[»]
    3D18X-ray1.74A25-300[»]
    3DTXX-ray2.10A25-300[»]
    3HCVX-ray1.95A25-300[»]
    3LV3X-ray1.94A25-300[»]
    4G8GX-ray2.40A25-300[»]
    4G8IX-ray1.60A25-300[»]
    4G9DX-ray1.60A25-300[»]
    4G9FX-ray1.90A25-300[»]
    ProteinModelPortaliP03989.
    SMRiP03989. Positions 25-300.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03989.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 308284ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini333 – 36230CytoplasmicSequence 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.
    InParanoidiP03989.
    PhylomeDBiP03989.

    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.

    P03989-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFITVG    50
    YVDDTLFVRF DSDAASPREE PRAPWIEQEG PEYWDRETQI CKAKAQTDRE 100
    DLRTLLRYYN QSEAGSHTLQ NMYGCDVGPD GRLLRGYHQD AYDGKDYIAL 150
    NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGECVE WLRRYLENGK 200
    ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ 250
    DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP 300
    SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS 350
    DSAQGSDVSL TA 362
    Length:362
    Mass (Da):40,428
    Last modified:August 13, 1987 - v2
    Checksum:iC8D2F154E3292031
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti206 – 2061A → V(PubMed:3485286)Curated
    Sequence conflicti266 – 2661Q → E AA sequence (PubMed:2408663)Curated

    Polymorphismi

    The following alleles of B-27 are known: B*27:01=B*27:05, B*27:02 (B27.2; B-27k; B27e), B*27:03 (B27d), B*27:04, B*27:06, B*27:07, B*27:08 (B7Qui) and B*27:09 (B27-ci). The sequence shown is that of B*27:01.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti65 – 651A → T.1 Publication
    Corresponds to variant rs1050529 [ dbSNP | Ensembl ].
    VAR_056341
    Natural varianti83 – 831Y → H in allele B*27:03.
    VAR_016379
    Natural varianti101 – 1011D → N in allele B*27:02.
    VAR_016380
    Natural varianti101 – 1011D → S in allele B*27:04, allele B*27:06 and allele B*27:08; requires 2 nucleotide substitutions.
    VAR_016381
    Natural varianti104 – 1052TL → IA in allele B*27:02.
    VAR_016382
    Natural varianti104 – 1041T → N in allele B*27:08.
    VAR_016383
    Natural varianti106 – 1072LR → RG in allele B*27:08.
    VAR_016384
    Natural varianti121 – 1211N → S in allele B*27:07.
    VAR_016385
    Natural varianti137 – 1382YH → HN in allele B*27:07.
    VAR_016386
    Natural varianti138 – 1381H → D in allele B*27:06.
    VAR_016387
    Natural varianti140 – 1401D → H in allele B*27:09.
    VAR_016388
    Natural varianti140 – 1401D → Y in allele B*27:06 and allele B*27:07.
    VAR_016389
    Natural varianti155 – 1551S → R in allele B*27:07.
    VAR_016390
    Natural varianti176 – 1761V → E in allele B*27:04 and allele B*27:06.
    VAR_016391
    Natural varianti235 – 2351A → G in allele B*27:04 and allele B*27:06.
    VAR_016392
    Natural varianti306 – 3061V → I.
    Corresponds to variant rs1131500 [ dbSNP | Ensembl ].
    VAR_056342
    Natural varianti329 – 3291A → T.
    Corresponds to variant rs1051488 [ dbSNP | Ensembl ].
    VAR_056343
    Natural varianti349 – 3491C → S.
    Corresponds to variant rs2308655 [ dbSNP | Ensembl ].
    VAR_061402
    Natural varianti349 – 3491C → Y.
    Corresponds to variant rs2308655 [ dbSNP | Ensembl ].
    VAR_061403

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03945 Genomic DNA. Translation: CAA27578.1. Sequence problems.
    X03664, X03667 Genomic DNA. Translation: CAA27301.1.
    L38504 mRNA. Translation: AAA69724.1.
    M54883 Genomic DNA. Translation: AAA59616.1.
    X03665, X03666 Genomic DNA. Translation: CAA27302.1.
    M12967 Genomic DNA. Translation: AAA36221.1.
    U27608 mRNA. Translation: AAC50444.1.
    U35734 mRNA. Translation: AAC50447.1.
    M14013 Genomic DNA. Translation: AAA59643.1.
    X73578 mRNA. Translation: CAA51980.1.
    M62852 mRNA. Translation: AAA59647.1.
    L19923 mRNA. Translation: AAA59658.1.
    Z33453 mRNA. Translation: CAA83876.1.
    PIRiI37515.
    I56116.
    S07441. HLHUB2.
    UniGeneiHs.654404.
    Hs.77961.

    Genome annotation databases

    EnsembliENST00000435618; ENSP00000405178; ENSG00000224608.

    Polymorphism databases

    DMDMi34305677.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03945 Genomic DNA. Translation: CAA27578.1 . Sequence problems.
    X03664 , X03667 Genomic DNA. Translation: CAA27301.1 .
    L38504 mRNA. Translation: AAA69724.1 .
    M54883 Genomic DNA. Translation: AAA59616.1 .
    X03665 , X03666 Genomic DNA. Translation: CAA27302.1 .
    M12967 Genomic DNA. Translation: AAA36221.1 .
    U27608 mRNA. Translation: AAC50444.1 .
    U35734 mRNA. Translation: AAC50447.1 .
    M14013 Genomic DNA. Translation: AAA59643.1 .
    X73578 mRNA. Translation: CAA51980.1 .
    M62852 mRNA. Translation: AAA59647.1 .
    L19923 mRNA. Translation: AAA59658.1 .
    Z33453 mRNA. Translation: CAA83876.1 .
    PIRi I37515.
    I56116.
    S07441. HLHUB2.
    UniGenei Hs.654404.
    Hs.77961.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HSA X-ray 2.10 A/D 25-300 [» ]
    1JGD X-ray 1.90 A 25-300 [» ]
    1JGE X-ray 2.10 A 25-300 [» ]
    1K5N X-ray 1.09 A 25-300 [» ]
    1OF2 X-ray 2.20 A 25-300 [» ]
    1OGT X-ray 1.47 A 25-300 [» ]
    1ROG model - A 25-206 [» ]
    1ROH model - A 25-206 [» ]
    1ROI model - A 25-206 [» ]
    1ROJ model - A 25-206 [» ]
    1ROK model - A 25-206 [» ]
    1ROL model - A 25-206 [» ]
    1UXS X-ray 1.55 A 25-300 [» ]
    1UXW X-ray 1.71 A 25-300 [» ]
    1W0V X-ray 2.27 A 25-300 [» ]
    1W0W X-ray 2.10 A 25-300 [» ]
    2A83 X-ray 1.40 A 25-300 [» ]
    2BSR X-ray 2.30 A 25-300 [» ]
    2BSS X-ray 2.00 A 25-300 [» ]
    2BST X-ray 2.10 A 25-300 [» ]
    3B3I X-ray 1.86 A 25-300 [» ]
    3B6S X-ray 1.80 A 25-300 [» ]
    3BP4 X-ray 1.85 A 25-300 [» ]
    3BP7 X-ray 1.80 A 25-300 [» ]
    3CZF X-ray 1.20 A 25-300 [» ]
    3D18 X-ray 1.74 A 25-300 [» ]
    3DTX X-ray 2.10 A 25-300 [» ]
    3HCV X-ray 1.95 A 25-300 [» ]
    3LV3 X-ray 1.94 A 25-300 [» ]
    4G8G X-ray 2.40 A 25-300 [» ]
    4G8I X-ray 1.60 A 25-300 [» ]
    4G9D X-ray 1.60 A 25-300 [» ]
    4G9F X-ray 1.90 A 25-300 [» ]
    ProteinModelPortali P03989.
    SMRi P03989. Positions 25-300.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6188N.
    IntActi P03989. 1 interaction.
    MINTi MINT-247525.

    Polymorphism databases

    DMDMi 34305677.

    Proteomic databases

    PaxDbi P03989.
    PRIDEi P03989.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000435618 ; ENSP00000405178 ; ENSG00000224608 .

    Organism-specific databases

    GeneCardsi GC06M031321.
    GC06Ml31364.
    HGNCi HGNC:4932. HLA-B.
    MIMi 106300. phenotype.
    142830. gene.
    neXtProti NX_P03989.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG42056.
    HOVERGENi HBG016709.
    InParanoidi P03989.
    PhylomeDBi P03989.

    Enzyme and pathway databases

    Reactomei 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-B. human.
    EvolutionaryTracei P03989.
    SOURCEi Search...

    Gene expression databases

    CleanExi HS_HLA-B.
    Genevestigatori P03989.

    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

    1. "Organization, sequence and expression of the HLA-B27 gene: a molecular approach to analyze HLA and disease associations."
      Weiss E.H., Kuon W., Doerner C., Lang M., Riethmueller G.
      Immunobiology 170:367-380(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*27:01).
    2. "Complete sequence of HLA-B27 cDNA identified through the characterization of structural markers unique to the HLA-A, -B, and -C allelic series."
      Szoets H., Riethmueller G., Weiss E., Meo T.
      Proc. Natl. Acad. Sci. U.S.A. 83:1428-1432(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-361 (ALLELE B*27:01).
    3. "Primary structure of papain-solubilized human histocompatibility antigen HLA-B27."
      Ezquerra A., Bragado R., Vega M.A., Strominger J.L., Woody J., Lopez de Castro J.A.
      Biochemistry 24:1733-1741(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-295 (B*27:01).
    4. "Gene conversion-like mechanisms may generate polymorphism in human class I genes."
      Seemann G.H.A., Rein R.S., Brown C.S., Ploegh H.L.
      EMBO J. 5:547-552(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES B*27:01 AND B*27:02).
    5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*27:02).
    6. "Structural analysis of an HLA-B27 functional variant: identification of residues that contribute to the specificity of recognition by cytolytic T lymphocytes."
      Vega M.A., Ezquerra A., Rojo S., Aparicio P., Bragado R., Lopez de Castro J.A.
      Proc. Natl. Acad. Sci. U.S.A. 82:7394-7398(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 86-107 AND 171-181 (B*27:02).
    7. "Molecular analysis of the variant alloantigen HLA-B27d (HLA-B*2703) identifies a unique single amino acid substitution."
      Choo S.Y., St John T., Orr H.T., Hansen J.A.
      Hum. Immunol. 21:209-219(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*27:03).
    8. "The nucleotide sequence of HLA-B*2704 reveals a new amino acid substitution in exon 4 which is also present in HLA-B*2706."
      Rudwaleit M., Bowness P., Wordsworth P.
      Immunogenetics 43:160-162(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*27:04 AND B*27:06).
    9. "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).
    10. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*27:06).
    11. "A novel HLA-B27 allele maps B27 allospecificity to the region around position 70 in the alpha 1 domain."
      Choo Y.S., Fan L.A., Hansen J.A.
      J. Immunol. 147:174-180(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*27:07).
    12. "The HLA-B7Qui antigen is encoded by a new subtype of HLA-B27 (B*2708)."
      Hildebrand W.H., Domena J.D., Shen S.Y., Marsh S.G.E., Bunce M., Guttridge M.G., Darke C., Parham P.
      Tissue Antigens 44:47-51(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*27:08).
    13. "Identification of a novel HLA-B27 subtype by restriction analysis of a cytotoxic gamma/delta T cell clone."
      Del Porto P., D'Amato M., Fiorillo M.T., Tuosto L., Piccolella E., Sorrentino R.
      J. Immunol. 153:3093-3100(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*27:09).
      Tissue: Blood.
    14. "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.
    15. "The three-dimensional structure of HLA-B27 at 2.1-A resolution suggests a general mechanism for tight peptide binding to MHC."
      Madden D.R., Gorga J.C., Strominger J.L., Wiley D.C.
      Cell 70:1035-1048(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-300.
    16. "The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation."
      Madden D.R., Gorga J.C., Strominger J.L., Wiley D.C.
      Nature 353:321-325(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-300.
    17. "HLA-B27 subtypes differentially associated with disease exhibit subtle structural alterations."
      Hulsmeyer M., Hillig R.C., Volz A., Ruhl M., Schroder W., Saenger W., Ziegler A., Uchanska-Ziegler B.
      J. Biol. Chem. 277:47844-47853(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-300.
    18. "Rational design of nonnatural peptides as high-affinity ligands for the HLA-B*2705 human leukocyte antigen."
      Rognan D., Scapozza L., Folkers G., Daser A.
      Proc. Natl. Acad. Sci. U.S.A. 92:753-757(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 115-206.
    19. "HLA-B27 in the Greek Cypriot population: distribution of subtypes in patients with ankylosing spondylitis and other HLA-B27-related diseases. The possible protective role of B*2707."
      Varnavidou-Nicolaidou A., Karpasitou K., Georgiou D., Stylianou G., Kokkofitou A., Michalis C., Constantina C., Gregoriadou C., Kyriakides G.
      Hum. Immunol. 65:1451-1454(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISEASE, POSSIBLE PROTECTIVE ROLE OF ALLELE B*27:07.
    20. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry namei1B27_HUMAN
    AccessioniPrimary (citable) accession number: P03989
    Secondary accession number(s): O19692
    , P10317, P10318, P19373, P30467, Q08136, Q29693, Q29846, Q29961
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 1986
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 153 of the entry and version 2 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