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P01911

- 2B1F_HUMAN

UniProt

P01911 - 2B1F_HUMAN

Protein

HLA class II histocompatibility antigen, DRB1-15 beta chain

Gene

HLA-DRB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.

    GO - Molecular functioni

    1. MHC class II protein complex binding Source: UniProt
    2. peptide antigen binding Source: UniProt

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    2. cytokine-mediated signaling pathway Source: Reactome
    3. interferon-gamma-mediated signaling pathway Source: Reactome
    4. polysaccharide assembly with MHC class II protein complex Source: UniProt
    5. T cell costimulation Source: Reactome
    6. T cell receptor signaling pathway Source: Reactome

    Keywords - Biological processi

    Immunity

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.
    REACT_12555. Downstream TCR signaling.
    REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
    REACT_12596. Translocation of ZAP-70 to Immunological synapse.
    REACT_12623. Generation of second messenger molecules.
    REACT_19324. PD-1 signaling.
    REACT_25078. Interferon gamma signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    HLA class II histocompatibility antigen, DRB1-15 beta chain
    Alternative name(s):
    DW2.2/DR2.2
    MHC class II antigen DRB1*15
    Gene namesi
    Name:HLA-DRB1
    Synonyms:HLA-DRB2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4948. HLA-DRB1.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Endoplasmic reticulum membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Golgi apparatustrans-Golgi network membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Endosome membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Lysosome membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Late endosome membrane 1 Publication; Single-pass type I membrane protein 1 Publication
    Note: The MHC class II complex transits through a number of intracellular compartments in the endocytic pathway until it reaches the cell membrane for antigen presentation.

    GO - Cellular componenti

    1. cell surface Source: UniProt
    2. clathrin-coated endocytic vesicle membrane Source: Reactome
    3. endocytic vesicle membrane Source: Reactome
    4. ER to Golgi transport vesicle membrane Source: Reactome
    5. extracellular vesicular exosome Source: UniProt
    6. Golgi membrane Source: Reactome
    7. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
    8. late endosome membrane Source: UniProtKB
    9. lysosomal membrane Source: UniProtKB
    10. membrane Source: UniProtKB
    11. MHC class II protein complex Source: UniProt
    12. plasma membrane Source: Reactome
    13. trans-Golgi network membrane Source: Reactome
    14. transport vesicle membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Endosome, Golgi apparatus, Lysosome, Membrane, MHC II

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35072.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 29292 PublicationsAdd
    BLAST
    Chaini30 – 266237HLA class II histocompatibility antigen, DRB1-15 beta chainPRO_0000080744Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi44 ↔ 108
    Glycosylationi48 – 481N-linked (GlcNAc...)
    Disulfide bondi146 ↔ 202
    Cross-linki254 – 254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

    Post-translational modificationi

    Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP01911.
    PRIDEiP01911.

    Expressioni

    Gene expression databases

    ArrayExpressiP01911.
    BgeeiP01911.
    CleanExiHS_HLA-DRB1.
    GenevestigatoriP01911.

    Organism-specific databases

    HPAiCAB015400.
    CAB034021.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit; also referred as MHC class II molecule. In the endoplasmic reticulum (ER) it forms a heterononamer; 3 MHC class II molecules bind to a CD74 homotrimer (also known as invariant chain or HLA class II histocompatibility antigen gamma chain). In the endosomal/lysosomal system; CD74 undergoes sequential degradation by various proteases; leaving a small fragment termed CLIP on each MHC class II molecule. MHC class II molecule interacts with HLA_DM, and HLA_DO in B-cells, in order to release CLIP and facilitate the binding of antigenic peptides.

    Protein-protein interaction databases

    BioGridi109368. 15 interactions.
    IntActiP01911. 1 interaction.

    Structurei

    Secondary structure

    1
    266
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 4712
    Turni48 – 514
    Beta strandi52 – 6110
    Beta strandi64 – 707
    Turni71 – 733
    Beta strandi75 – 806
    Helixi81 – 833
    Helixi84 – 929
    Helixi94 – 10613
    Helixi108 – 1158
    Turni116 – 1216
    Beta strandi127 – 1348
    Beta strandi142 – 15413
    Beta strandi157 – 1626
    Beta strandi165 – 1673
    Beta strandi169 – 1735
    Beta strandi180 – 1823
    Beta strandi184 – 1929
    Beta strandi199 – 2057
    Beta strandi209 – 2113
    Beta strandi213 – 2186

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BX2X-ray2.60B/E32-222[»]
    1YMMX-ray3.50B30-227[»]
    2WBJX-ray3.00B/F30-227[»]
    ProteinModelPortaliP01911.
    SMRiP01911. Positions 32-222.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01911.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini30 – 227198ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini249 – 26618CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei228 – 24821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini126 – 21489Ig-like C1-typeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 12495Beta-1Add
    BLAST
    Regioni125 – 227103Beta-2Add
    BLAST

    Sequence similaritiesi

    Belongs to the MHC class II family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOVERGENiHBG012730.
    InParanoidiP01911.
    KOiK06752.
    OMAiERISCGI.
    PhylomeDBiP01911.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.10.320.10. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003006. Ig/MHC_CS.
    IPR003597. Ig_C1-set.
    IPR011162. MHC_I/II-like_Ag-recog.
    IPR014745. MHC_II_a/b_N.
    IPR000353. MHC_II_b_N.
    [Graphical view]
    PfamiPF07654. C1-set. 1 hit.
    PF00969. MHC_II_beta. 1 hit.
    [Graphical view]
    ProDomiPD000328. MHC_II_b_N. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00407. IGc1. 1 hit.
    SM00921. MHC_II_beta. 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.

    P01911-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVCLKLPGGS CMTALTVTLM VLSSPLALSG DTRPRFLWQP KRECHFFNGT    50
    ERVRFLDRYF YNQEESVRFD SDVGEFRAVT ELGRPDAEYW NSQKDILEQA 100
    RAAVDTYCRH NYGVVESFTV QRRVQPKVTV YPSKTQPLQH HNLLVCSVSG 150
    FYPGSIEVRW FLNGQEEKAG MVSTGLIQNG DWTFQTLVML ETVPRSGEVY 200
    TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF 250
    RNQKGHSGLQ PTGFLS 266
    Length:266
    Mass (Da):29,966
    Last modified:January 15, 2008 - v2
    Checksum:i3B5912820A4654BE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti119 – 1191T → A in AAI08923. (PubMed:15489334)Curated
    Sequence conflicti154 – 1541G → A in AAA59801. (PubMed:3476943)Curated
    Sequence conflicti171 – 1711M → G AA sequence (PubMed:6947956)Curated
    Sequence conflicti179 – 1802NG → D AA sequence (PubMed:6947956)Curated

    Polymorphismi

    The following alleles of DRB1-15 are known: DRB1*15:01, DRB1*15:02, DRB1*15:03, DRB1*15:04, DRB1*15:05, DRB1*15:06, DRB1*15:07, DRB1*15:08, DRB1*15:09, DRB1*15:10, DRB1*15:11, DRB1*15:12, DRB1*15:13, DRB1*15:14, DRB1*15:15, DRB1*15:16, DRB1*15:18, DRB1*15:19, DRB1*15:20, DRB1*15:21, DRB1*15:22, DRB1*15:23, DRB1*15:24, DRB1*15:25, DRB1*15:26, DRB1*15:27, DRB1*15:28, DRB1*15:29, DRB1*15:30, DRB1*15:31 and DRB1*15:32. The sequence shown is that of DRB1*15:01.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51K → R.
    Corresponds to variant rs9270305 [ dbSNP | Ensembl ].
    VAR_050364
    Natural varianti55 – 551F → Y.
    Corresponds to variant rs16822516 [ dbSNP | Ensembl ].
    VAR_050365
    Natural varianti59 – 591Y → H in allele DRB1*15:03.
    VAR_038162
    Natural varianti96 – 961I → F in allele DRB1*15:04.
    Corresponds to variant rs17886918 [ dbSNP | Ensembl ].
    VAR_038163
    Natural varianti106 – 1061T → N.
    Corresponds to variant rs9269941 [ dbSNP | Ensembl ].
    VAR_050366
    Natural varianti115 – 1151V → G in allele DRB1*15:02.
    Corresponds to variant rs17885482 [ dbSNP | Ensembl ].
    VAR_038164
    Natural varianti164 – 1641G → S.
    Corresponds to variant rs1059633 [ dbSNP | Ensembl ].
    VAR_050367
    Natural varianti169 – 1691A → T.
    Corresponds to variant rs2308768 [ dbSNP | Ensembl ].
    VAR_050368
    Natural varianti236 – 2361V → M.
    Corresponds to variant rs2230816 [ dbSNP | Ensembl ].
    VAR_050369
    Natural varianti262 – 2621T → R.
    Corresponds to variant rs9269744 [ dbSNP | Ensembl ].
    VAR_050370

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20430 mRNA. Translation: AAA59831.1.
    AY663395 Genomic DNA. Translation: AAU87979.1.
    AY663406 Genomic DNA. Translation: AAU88008.1.
    AY663411 Genomic DNA. Translation: AAU88023.1.
    AY663414 Genomic DNA. Translation: AAU88033.1.
    AY961072 mRNA. Translation: AAX63460.1.
    AY961073 mRNA. Translation: AAX63461.1.
    AL713966 Genomic DNA. Translation: CAI18081.1.
    BC033827 mRNA. Translation: AAH33827.1.
    BC108922 mRNA. Translation: AAI08923.1.
    M28584 mRNA. Translation: AAA59681.1.
    M16957 mRNA. Translation: AAA36279.1.
    M17378 mRNA. Translation: AAA59801.1.
    CCDSiCCDS47409.1.
    PIRiI68734. HLHUWB.
    RefSeqiNP_002115.2. NM_002124.3.
    UniGeneiHs.534322.
    Hs.696211.
    Hs.736560.

    Genome annotation databases

    EnsembliENST00000360004; ENSP00000353099; ENSG00000196126.
    GeneIDi3123.
    KEGGihsa:3123.
    UCSCiuc003obp.4. human.

    Polymorphism databases

    DMDMi166214928.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20430 mRNA. Translation: AAA59831.1 .
    AY663395 Genomic DNA. Translation: AAU87979.1 .
    AY663406 Genomic DNA. Translation: AAU88008.1 .
    AY663411 Genomic DNA. Translation: AAU88023.1 .
    AY663414 Genomic DNA. Translation: AAU88033.1 .
    AY961072 mRNA. Translation: AAX63460.1 .
    AY961073 mRNA. Translation: AAX63461.1 .
    AL713966 Genomic DNA. Translation: CAI18081.1 .
    BC033827 mRNA. Translation: AAH33827.1 .
    BC108922 mRNA. Translation: AAI08923.1 .
    M28584 mRNA. Translation: AAA59681.1 .
    M16957 mRNA. Translation: AAA36279.1 .
    M17378 mRNA. Translation: AAA59801.1 .
    CCDSi CCDS47409.1.
    PIRi I68734. HLHUWB.
    RefSeqi NP_002115.2. NM_002124.3.
    UniGenei Hs.534322.
    Hs.696211.
    Hs.736560.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BX2 X-ray 2.60 B/E 32-222 [» ]
    1YMM X-ray 3.50 B 30-227 [» ]
    2WBJ X-ray 3.00 B/F 30-227 [» ]
    ProteinModelPortali P01911.
    SMRi P01911. Positions 32-222.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109368. 15 interactions.
    IntActi P01911. 1 interaction.

    Polymorphism databases

    DMDMi 166214928.

    Proteomic databases

    MaxQBi P01911.
    PRIDEi P01911.

    Protocols and materials databases

    DNASUi 3123.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360004 ; ENSP00000353099 ; ENSG00000196126 .
    GeneIDi 3123.
    KEGGi hsa:3123.
    UCSCi uc003obp.4. human.

    Organism-specific databases

    CTDi 3123.
    GeneCardsi GC06M032546.
    HGNCi HGNC:4948. HLA-DRB1.
    HPAi CAB015400.
    CAB034021.
    MIMi 142857. gene.
    neXtProti NX_P01911.
    PharmGKBi PA35072.
    GenAtlasi Search...

    Phylogenomic databases

    HOVERGENi HBG012730.
    InParanoidi P01911.
    KOi K06752.
    OMAi ERISCGI.
    PhylomeDBi P01911.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.
    REACT_12555. Downstream TCR signaling.
    REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
    REACT_12596. Translocation of ZAP-70 to Immunological synapse.
    REACT_12623. Generation of second messenger molecules.
    REACT_19324. PD-1 signaling.
    REACT_25078. Interferon gamma signaling.

    Miscellaneous databases

    ChiTaRSi HLA-DRB1. human.
    EvolutionaryTracei P01911.
    GeneWikii HLA-DRB1.
    GenomeRNAii 3123.
    NextBioi 12394.
    PROi P01911.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01911.
    Bgeei P01911.
    CleanExi HS_HLA-DRB1.
    Genevestigatori P01911.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.10.320.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003006. Ig/MHC_CS.
    IPR003597. Ig_C1-set.
    IPR011162. MHC_I/II-like_Ag-recog.
    IPR014745. MHC_II_a/b_N.
    IPR000353. MHC_II_b_N.
    [Graphical view ]
    Pfami PF07654. C1-set. 1 hit.
    PF00969. MHC_II_beta. 1 hit.
    [Graphical view ]
    ProDomi PD000328. MHC_II_b_N. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00407. IGc1. 1 hit.
    SM00921. MHC_II_beta. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*15:01).
      Tissue: B-cell.
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DRB1*15:01; DRB1*15:02 AND DRB1*15:03).
    3. "Group-specific amplification of cDNA from DRB1 genes. Complete coding sequences of partially defined alleles and identification of the new alleles DRB1*040602, DRB1*111102, DRB1*080103, and DRB1*0113."
      Balas A., Vilches C., Rodriguez M.A., Fernandez B., Martinez M.P., de Pablo R., Garcia-Sanchez F., Vicario J.L.
      Hum. Immunol. 67:1008-1016(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DRB1*15:03 AND DRB1*15:04).
      Tissue: Blood.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DRB1*15:01).
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELES DRB1*15:01 AND DRB1*15:02).
      Tissue: Leukocyte.
    6. "cDNA cloning and sequencing reveals that the electrophoretically constant DR beta 2 molecules, as well as the variable DR beta 1 molecules, from HLA-DR2 subtypes have different amino acid sequences including a hypervariable region for a functionally important epitope."
      Wu S.K., Yabe T., Madden M., Saunders T.L., Bach F.H.
      J. Immunol. 138:2953-2959(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-266 (ALLELE DRB1*15:02).
      Tissue: Lymphoblast.
    7. "HLA-DR2 subtypes form an additional supertypic family of DR beta alleles."
      Lee B.S.M., Rust N.A., McMichael A.J., McDevitt H.O.
      Proc. Natl. Acad. Sci. U.S.A. 84:4591-4595(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*15:01).
      Tissue: Lymphoblast.
    8. "Allelic variation in the DR subregion of the human major histocompatibility complex."
      Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A., McDevitt H.O.
      Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*15:01).
      Tissue: Lymphoblast.
    9. "Primary structure of class II human histocompatibility antigens. 1st communication. Amino acid sequence of the N-terminal 198 residues of the beta chain of a HLA-Dw2,2;DR2,2-alloantigen."
      Kratzin H., Yang C.-Y., Gotz H., Pauly E., Kolbel S., Egert G., Thinnes F.P., Wernet P., Altevogt P., Hilschmann N.
      Hoppe-Seyler's Z. Physiol. Chem. 362:1665-1669(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 30-228.
      Tissue: Lymphoblast.
    10. "N-terminal amino acid sequences of the alpha and beta chains of HLA-DR1 and HLA-DR2 antigens."
      Walker L.E., Hewick R., Hunkapiller M.W., Hood L.E., Dreyer W.J., Reisfeld R.A.
      Biochemistry 22:185-188(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 30-64.
      Tissue: B-cell.
    11. "Invariant chain structure and MHC class II function."
      Cresswell P.
      Cell 84:505-507(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    12. "Presentation of antigens by MHC class II molecules: getting the most out of them."
      Villadangos J.A.
      Mol. Immunol. 38:329-346(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    13. "Autophagy in MHC class II presentation: sampling from within."
      Menendez-Benito V., Neefjes J.
      Immunity 26:1-3(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    14. "MHC class II molecules on the move for successful antigen presentation."
      Rocha N., Neefjes J.
      EMBO J. 27:1-5(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    15. "MHC class II stabilization at the surface of human dendritic cells is the result of maturation-dependent MARCH I down-regulation."
      De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., Pierre P., Gatti E.
      Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY MARCH1, SUBCELLULAR LOCATION.
    16. "MHC class II transport at a glance."
      Berger A.C., Roche P.A.
      J. Cell Sci. 122:1-4(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    17. "CD74 in antigen presentation, inflammation, and cancers of the gastrointestinal tract."
      Beswick E.J., Reyes V.E.
      World J. Gastroenterol. 15:2855-2861(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Unconventional topology of self peptide-major histocompatibility complex binding by a human autoimmune T cell receptor."
      Hahn M., Nicholson M.J., Pyrdol J., Wucherpfennig K.W.
      Nat. Immunol. 6:490-496(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 30-227.

    Entry informationi

    Entry namei2B1F_HUMAN
    AccessioniPrimary (citable) accession number: P01911
    Secondary accession number(s): Q29790
    , Q29975, Q30142, Q30166, Q32MY7, Q56FN9, Q5Y7B0, Q5Y7B9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 124 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

    Miscellaneous

    The chain shown constituted about 70% of a pool of at least seven similar beta chains.

    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