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P30685

- 1B35_HUMAN

UniProt

P30685 - 1B35_HUMAN

Protein

HLA class I histocompatibility antigen, B-35 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 138 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      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 exogenous peptide antigen via MHC class I Source: Reactome
    2. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
    3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent Source: Reactome
    4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    5. cytokine-mediated signaling pathway Source: Reactome
    6. interferon-gamma-mediated signaling pathway Source: Reactome
    7. positive regulation of T cell mediated cytotoxicity Source: InterPro
    8. regulation of immune response Source: Reactome
    9. type I interferon signaling pathway Source: Reactome
    10. 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-35 alpha chain
    Alternative name(s):
    MHC class I antigen B*35
    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. Golgi apparatus Source: UniProt
    6. Golgi membrane Source: Reactome
    7. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
    8. MHC class I protein complex Source: UniProt
    9. phagocytic vesicle membrane Source: Reactome
    10. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane, MHC I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Add
    BLAST
    Chaini25 – 362338HLA class I histocompatibility antigen, B-35 alpha chainPRO_0000018840Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi110 – 1101N-linked (GlcNAc...)By similarity
    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

    PRIDEiP30685.

    Expressioni

    Gene expression databases

    CleanExiHS_HLA-B.
    GenevestigatoriP30685.

    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

    IntActiP30685. 1 interaction.
    MINTiMINT-1516663.

    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
    Beta strandi69 – 713
    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
    Helixi200 – 2034
    Beta strandi210 – 2178
    Beta strandi219 – 23517
    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
    1A1NX-ray2.00A25-300[»]
    1A9BX-ray3.20A/D25-301[»]
    1A9EX-ray2.50A25-301[»]
    1CG9X-ray2.70A25-301[»]
    1XH3X-ray1.48A25-300[»]
    1ZHKX-ray1.60A25-300[»]
    1ZHLX-ray1.50A25-300[»]
    1ZSDX-ray1.70A25-300[»]
    2AK4X-ray2.50A/F/K/Q25-300[»]
    2AXFX-ray1.80A25-300[»]
    2AXGX-ray2.00A25-300[»]
    2CIKX-ray1.75A25-300[»]
    2FYYX-ray1.50A25-300[»]
    2FZ3X-ray1.90A25-300[»]
    2H6PX-ray1.90A25-300[»]
    2NW3X-ray1.70A25-300[»]
    2NX5X-ray2.70A/F/K/Q25-300[»]
    3BW9X-ray1.75A25-300[»]
    3BWAX-ray1.30A25-300[»]
    3KWWX-ray2.18A25-300[»]
    3KXFX-ray3.10A/C/I/K25-300[»]
    3LKNX-ray2.00A25-300[»]
    3LKOX-ray1.80A25-300[»]
    3LKPX-ray1.80A25-300[»]
    3LKQX-ray1.80A25-300[»]
    3LKRX-ray2.00A25-300[»]
    3LKSX-ray1.90A25-300[»]
    3MV7X-ray2.00A25-300[»]
    3MV8X-ray2.10A25-300[»]
    3MV9X-ray2.70A25-300[»]
    3VFSX-ray1.85A25-300[»]
    3VFTX-ray1.95A25-300[»]
    3VFUX-ray1.65A25-300[»]
    3VFVX-ray1.55A25-300[»]
    3VFWX-ray2.30A25-300[»]
    4PR5X-ray1.80A25-300[»]
    4PRNX-ray1.65A25-300[»]
    ProteinModelPortaliP30685.
    SMRiP30685. Positions 25-300.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30685.

    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

    HOVERGENiHBG016709.
    InParanoidiP30685.

    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.

    P30685-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG    50
    YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE 100
    SLRNLRGYYN QSEAGSHIIQ RMYGCDLGPD GRLLRGHDQS AYDGKDYIAL 150
    NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK 200
    ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ 250
    DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP 300
    SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS 350
    DSAQGSDVSL TA 362
    Length:362
    Mass (Da):40,455
    Last modified:April 1, 1993 - v1
    Checksum:i52906854FC43E7A6
    GO

    Polymorphismi

    The following alleles of B-35 are known: B*35:01, B*35:02, B*35:03, B*35:04, B*35:05 (B35-G), B*35:06 (B35-K), B*35:07, B*35:08, B*35:25, B*35:28, B*35:29 (B*KG), B*35:30, B*35:32 (B*TMUL) and B*35:36. The sequence shown is that of B*35:01.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401G → V in allele B*35:07.
    VAR_016393
    Natural varianti48 – 481A → S in allele B*35:25.
    VAR_016394
    Natural varianti69 – 691T → E in allele B*35:25; requires 2 nucleotide substitutions.
    VAR_016395
    Natural varianti87 – 871N → E in allele B*35:28; requires 2 nucleotide substitutions.
    VAR_016396
    Natural varianti91 – 911F → S in allele B*35:28.
    VAR_016397
    Natural varianti98 – 981Y → D in allele B*35:29.
    VAR_016398
    Natural varianti107 – 1071G → D in allele B*35:36.
    VAR_016399
    Natural varianti118 – 1192II → TL in allele B*35:05 and allele B*35:32.
    VAR_016400
    Natural varianti121 – 1211R → S in allele B*35:05 and allele B*35:30.
    VAR_016401
    Natural varianti127 – 1271L → V in allele B*35:32.
    VAR_016402
    Natural varianti133 – 1331L → F in allele B*35:02.
    VAR_016403
    Natural varianti138 – 1381D → N in allele B*35:02, allele B*35:04 and allele B*35:06.
    VAR_016404
    Natural varianti140 – 1401S → F in allele B*35:06 and allele B*35:36.
    VAR_016405
    Natural varianti140 – 1401S → Y in allele B*35:02, allele B*35:03 and allele B*35:04. 1 Publication
    VAR_016406
    Natural varianti180 – 1801L → R in allele B*35:08.
    VAR_016407

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28115
    , M28109, M28110, M28111, M28112, M28113, M28114 Genomic DNA. Translation: AAA59617.1.
    M63454 Genomic DNA. Translation: AAA59682.1.
    M81798 mRNA. Translation: AAA59684.1.
    D50299 mRNA. Translation: BAA08828.1.
    M84385 mRNA. Translation: AAA59635.1.
    M84381 mRNA. Translation: AAA59631.1.
    L04695 mRNA. Translation: AAA59694.1.
    L04696 mRNA. Translation: AAA52674.1.
    Z22651 mRNA. Translation: CAA80366.1.
    M86403 mRNA. No translation available.
    AH007565 Genomic DNA. Translation: AAD23460.1.
    AH007706 Genomic DNA. Translation: AAD30277.1.
    AH006372 Genomic DNA. Translation: AAC32570.1.
    AH007604 Genomic DNA. Translation: AAD27538.1.
    AH008126 Genomic DNA. Translation: AAD51745.1.
    AH007584 Genomic DNA. Translation: AAD26151.1.
    AH009759 Genomic DNA. Translation: AAG01819.1.
    PIRiA45880.
    I54298.
    I56133.
    I61904.
    I61907.
    I81233.
    UniGeneiHs.654404.
    Hs.77961.

    Genome annotation databases

    EnsembliENST00000359635; ENSP00000352656; ENSG00000206450.

    Polymorphism databases

    DMDMi231390.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28115
    , M28109 , M28110 , M28111 , M28112 , M28113 , M28114 Genomic DNA. Translation: AAA59617.1 .
    M63454 Genomic DNA. Translation: AAA59682.1 .
    M81798 mRNA. Translation: AAA59684.1 .
    D50299 mRNA. Translation: BAA08828.1 .
    M84385 mRNA. Translation: AAA59635.1 .
    M84381 mRNA. Translation: AAA59631.1 .
    L04695 mRNA. Translation: AAA59694.1 .
    L04696 mRNA. Translation: AAA52674.1 .
    Z22651 mRNA. Translation: CAA80366.1 .
    M86403 mRNA. No translation available.
    AH007565 Genomic DNA. Translation: AAD23460.1 .
    AH007706 Genomic DNA. Translation: AAD30277.1 .
    AH006372 Genomic DNA. Translation: AAC32570.1 .
    AH007604 Genomic DNA. Translation: AAD27538.1 .
    AH008126 Genomic DNA. Translation: AAD51745.1 .
    AH007584 Genomic DNA. Translation: AAD26151.1 .
    AH009759 Genomic DNA. Translation: AAG01819.1 .
    PIRi A45880.
    I54298.
    I56133.
    I61904.
    I61907.
    I81233.
    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
    1A1N X-ray 2.00 A 25-300 [» ]
    1A9B X-ray 3.20 A/D 25-301 [» ]
    1A9E X-ray 2.50 A 25-301 [» ]
    1CG9 X-ray 2.70 A 25-301 [» ]
    1XH3 X-ray 1.48 A 25-300 [» ]
    1ZHK X-ray 1.60 A 25-300 [» ]
    1ZHL X-ray 1.50 A 25-300 [» ]
    1ZSD X-ray 1.70 A 25-300 [» ]
    2AK4 X-ray 2.50 A/F/K/Q 25-300 [» ]
    2AXF X-ray 1.80 A 25-300 [» ]
    2AXG X-ray 2.00 A 25-300 [» ]
    2CIK X-ray 1.75 A 25-300 [» ]
    2FYY X-ray 1.50 A 25-300 [» ]
    2FZ3 X-ray 1.90 A 25-300 [» ]
    2H6P X-ray 1.90 A 25-300 [» ]
    2NW3 X-ray 1.70 A 25-300 [» ]
    2NX5 X-ray 2.70 A/F/K/Q 25-300 [» ]
    3BW9 X-ray 1.75 A 25-300 [» ]
    3BWA X-ray 1.30 A 25-300 [» ]
    3KWW X-ray 2.18 A 25-300 [» ]
    3KXF X-ray 3.10 A/C/I/K 25-300 [» ]
    3LKN X-ray 2.00 A 25-300 [» ]
    3LKO X-ray 1.80 A 25-300 [» ]
    3LKP X-ray 1.80 A 25-300 [» ]
    3LKQ X-ray 1.80 A 25-300 [» ]
    3LKR X-ray 2.00 A 25-300 [» ]
    3LKS X-ray 1.90 A 25-300 [» ]
    3MV7 X-ray 2.00 A 25-300 [» ]
    3MV8 X-ray 2.10 A 25-300 [» ]
    3MV9 X-ray 2.70 A 25-300 [» ]
    3VFS X-ray 1.85 A 25-300 [» ]
    3VFT X-ray 1.95 A 25-300 [» ]
    3VFU X-ray 1.65 A 25-300 [» ]
    3VFV X-ray 1.55 A 25-300 [» ]
    3VFW X-ray 2.30 A 25-300 [» ]
    4PR5 X-ray 1.80 A 25-300 [» ]
    4PRN X-ray 1.65 A 25-300 [» ]
    ProteinModelPortali P30685.
    SMRi P30685. Positions 25-300.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P30685. 1 interaction.
    MINTi MINT-1516663.

    Polymorphism databases

    DMDMi 231390.

    Proteomic databases

    PRIDEi P30685.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359635 ; ENSP00000352656 ; ENSG00000206450 .

    Organism-specific databases

    GeneCardsi GC06M031321.
    GC06Mn31311.
    H-InvDB HIX0167180.
    HGNCi HGNC:4932. HLA-B.
    MIMi 142830. gene.
    neXtProti NX_P30685.
    GenAtlasi Search...

    Phylogenomic databases

    HOVERGENi HBG016709.
    InParanoidi P30685.

    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 P30685.
    SOURCEi Search...

    Gene expression databases

    CleanExi HS_HLA-B.
    Genevestigatori P30685.

    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. "The structure of HLA-B35 suggests that it is derived from HLA-Bw58 by two genetic mechanisms."
      Ooba T., Hayashi H., Karaki S., Tanabe M., Kano K., Takiguchi M.
      Immunogenetics 30:76-80(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*35:01).
    2. "Complete nucleotide sequence of a genomic clone encoding HLA-B35 isolated from a Caucasian individual of Hispanic origin. Identification of a new variant of HLA-B35."
      Chertkoff L.P., Herrera M., Fainboim L., Satz M.L.
      Hum. Immunol. 31:153-158(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*35:02).
    3. "The HLA-A,B 'negative' mutant cell line C1R expresses a novel HLA-B35 allele, which also has a point mutation in the translation initiation codon."
      Zemmour J., Little A.-M., Schendel D.J., Parham P.
      J. Immunol. 148:1941-1948(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*35:03).
    4. "Polymorphism of human minor histocompatibility antigens: T cell recognition of human minor histocompatibility peptides presented by HLA-B35 subtype molecules."
      Beck Y., Satz L., Takamiya Y., Nakayama S., Ling L., Ishikawa Y., Nagao T., Uchida H., Tokunaga K., Mueller C., Juji T., Takiguchi M.
      J. Exp. Med. 181:2037-2048(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ALLELE B*35:03).
      Tissue: Blood.
    5. Cited for: NUCLEOTIDE SEQUENCE (ALLELES B*35:05 AND B*35:06).
    6. "Isolation and characterization of two new functional subtypes of HLA-B35."
      Theiler G., Pando M., Delfino J.M., Takiguchi M., Satz M.L.
      Tissue Antigens 41:143-147(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*35:07 AND B*35:08).
    7. "Microheterogeneity in HLA-B35 alleles influences peptide-dependent allorecognition by cytotoxic T cells but not binding of a peptide-restricted monoclonal antibody."
      Steinle A., Reinhardt C., Noessner E., Uchanska-Ziegler B., Ziegler A., Schendel D.J.
      Hum. Immunol. 38:261-269(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*35:08).
    8. "New recombinant HLA-B alleles in a tribe of South American Amerindians indicate rapid evolution of MHC class I loci."
      Watkins D.I., McAdam S.N., Liu X., Stang C.R., Milford E.L., Levine C.G., Garber T.L., Dogon A.L., Lord C.I., Ghim S.H., Troup G.M., Hughes A.L., Letvin N.L.
      Nature 357:329-333(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 9-362 (ALLELE B*35:04).
    9. "Routine HLA-B genotyping with PCR-sequence-specific oligonucleotides (PCR-SSO) detects eight new alleles: B*0807, B*0809, B*1551, B*3529, B*3532, B*4025, B*5304 and B*5508."
      Kennedy C.T., Dodd R., Le T., Wallace R., Ng G., Greville W.D., Kennedy A., Taverniti A., Moses J.H., Clow N., Watson N., Dunckley H.
      Tissue Antigens 55:266-270(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELES B*35:29 AND B*35:32).
    10. Cited for: NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES B*35:25; B*35:28; B*35:29; B*35:30 AND B*35:36).
    11. "An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501."
      Smith K.J., Reid S.W., Stuart D.I., McMichael A.J., Jones E.Y., Bell J.I.
      Immunity 4:203-214(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-300.
    12. "Decamer-like conformation of a nona-peptide bound to HLA-B*3501 due to non-standard positioning of the C-terminus."
      Menssen R., Orth P., Ziegler A., Saenger W.
      J. Mol. Biol. 285:645-653(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    13. Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry namei1B35_HUMAN
    AccessioniPrimary (citable) accession number: P30685
    Secondary accession number(s): O62919
    , P30468, P30469, P30470, P30471, P30472, P30473, P30474, Q9GJM7, Q9TPV2, Q9TQH3, Q9TQH9, Q9TQN4, Q9TQN6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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