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P04229

- 2B11_HUMAN

UniProt

P04229 - 2B11_HUMAN

Protein

HLA class II histocompatibility antigen, DRB1-1 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 145 (01 Oct 2014)
      Sequence version 2 (29 Aug 2003)
      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: UniProtKB

    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. detection of bacterium Source: UniProtKB
    4. humoral immune response mediated by circulating immunoglobulin Source: UniProtKB
    5. immune response Source: UniProtKB
    6. immunoglobulin production involved in immunoglobulin mediated immune response Source: UniProtKB
    7. inflammatory response to antigenic stimulus Source: UniProtKB
    8. interferon-gamma-mediated signaling pathway Source: Reactome
    9. negative regulation of interferon-gamma production Source: UniProtKB
    10. negative regulation of T cell proliferation Source: UniProtKB
    11. positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
    12. protein tetramerization Source: UniProtKB
    13. regulation of interleukin-10 secretion Source: UniProtKB
    14. regulation of interleukin-4 production Source: UniProtKB
    15. T cell costimulation Source: Reactome
    16. T cell receptor signaling pathway Source: Reactome
    17. T-helper 1 type immune response Source: UniProtKB

    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, DRB1-1 beta chain
    Alternative name(s):
    MHC class II antigen DRB1*1
    Short name:
    DR-1
    Short name:
    DR1
    Gene namesi
    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. clathrin-coated endocytic vesicle membrane Source: Reactome
    2. endocytic vesicle membrane Source: Reactome
    3. ER to Golgi transport vesicle membrane Source: Reactome
    4. external side of plasma membrane Source: UniProtKB
    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. MHC class II protein complex Source: UniProt
    11. plasma membrane Source: Reactome
    12. trans-Golgi network membrane Source: Reactome
    13. transport vesicle membrane Source: Reactome

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Sarcoidosis 1 (SS1) [MIM:181000]: An idiopathic, systemic, inflammatory disease characterized by the formation of immune granulomas in involved organs. Granulomas predominantly invade the lungs and the lymphatic system, but also skin, liver, spleen, eyes and other organs may be involved.
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi181000. phenotype.
    Orphaneti703. Bullous pemphigoid.
    555. Celiac disease.
    243377. Diabetes mellitus type 1.
    220393. Diffuse cutaneous systemic sclerosis.
    545. Follicular lymphoma.
    220402. Limited cutaneous systemic sclerosis.
    220407. Limited systemic sclerosis.
    802. Multiple sclerosis.
    83465. Narcolepsy without cataplexy.
    2073. Narcolepsy-cataplexy.
    284130. Rheumatoid arthritis.
    797. Sarcoidosis.
    536. Systemic lupus erythematosus.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 29291 PublicationAdd
    BLAST
    Chaini30 – 266237HLA class II histocompatibility antigen, DRB1-1 beta chainPRO_0000018949Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi44 ↔ 108PROSITE-ProRule annotation
    Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi146 ↔ 202PROSITE-ProRule annotation
    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

    PaxDbiP04229.
    PRIDEiP04229.

    PTM databases

    PhosphoSiteiP04229.

    Expressioni

    Gene expression databases

    ArrayExpressiP04229.
    BgeeiP04229.
    CleanExiHS_HLA-DRB1.
    GenevestigatoriP04229.

    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

    DIPiDIP-6143N.
    IntActiP04229. 6 interactions.
    MINTiMINT-203282.

    Structurei

    Secondary structure

    1
    266
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 4712
    Turni48 – 514
    Beta strandi52 – 6312
    Beta strandi65 – 706
    Turni71 – 733
    Beta strandi75 – 806
    Helixi81 – 833
    Helixi84 – 918
    Helixi94 – 10613
    Helixi108 – 1158
    Helixi116 – 1183
    Turni119 – 1213
    Beta strandi127 – 1326
    Beta strandi135 – 1395
    Beta strandi142 – 15413
    Beta strandi157 – 1626
    Beta strandi165 – 1673
    Beta strandi169 – 1735
    Beta strandi180 – 1823
    Beta strandi184 – 1929
    Beta strandi199 – 2057
    Beta strandi213 – 2186

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AQDX-ray2.45B/E/H/K30-227[»]
    1DLHX-ray2.80B/E32-219[»]
    1FYTX-ray2.60B30-221[»]
    1HXYX-ray2.60B30-219[»]
    1JWMX-ray2.70B30-219[»]
    1JWSX-ray2.60B30-219[»]
    1JWUX-ray2.30B30-219[»]
    1KG0X-ray2.65B32-219[»]
    1KLGX-ray2.40B30-219[»]
    1KLUX-ray1.93B30-219[»]
    1LO5X-ray3.20B30-219[»]
    1PYWX-ray2.10B30-219[»]
    1R5IX-ray2.60B/F30-219[»]
    1SEBX-ray2.70B/F30-221[»]
    1SJEX-ray2.45B30-219[»]
    1SJHX-ray2.25B30-219[»]
    1T5WX-ray2.40B/E30-219[»]
    1T5XX-ray2.50B30-219[»]
    2FSEX-ray3.10B/D33-219[»]
    2G9HX-ray2.00B30-219[»]
    2IAMX-ray2.80B30-219[»]
    2IANX-ray2.80B/G/L/Q30-219[»]
    2ICWX-ray2.41B/E30-219[»]
    2IPKX-ray2.30B30-219[»]
    2OJEX-ray3.00B/F30-219[»]
    2XN9X-ray2.30E30-219[»]
    3L6FX-ray2.10B30-221[»]
    3PDOX-ray1.95B30-227[»]
    3PGCX-ray2.66B/E30-227[»]
    3PGDX-ray2.72B/E30-227[»]
    3QXAX-ray2.71B/E30-219[»]
    3QXDX-ray2.30B/E30-219[»]
    3S4SX-ray2.40B/E30-221[»]
    3S5LX-ray2.10B/E30-221[»]
    4AENX-ray2.20B30-227[»]
    4AH2X-ray2.36B30-227[»]
    4E41X-ray2.60B/G30-219[»]
    4FQXX-ray2.60B30-221[»]
    4GBXX-ray3.00B30-220[»]
    4I5BX-ray2.12B/E31-222[»]
    ProteinModelPortaliP04229.
    SMRiP04229. Positions 30-219.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04229.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini30 – 227198ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini251 – 26616CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei228 – 25023HelicalSequence 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

    eggNOGiNOG68200.
    HOVERGENiHBG012730.
    InParanoidiP04229.
    OrthoDBiEOG7PS1GV.

    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.

    P04229-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVCLKLPGGS CMTALTVTLM VLSSPLALAG DTRPRFLWQL KFECHFFNGT    50
    ERVRLLERCI YNQEESVRFD SDVGEYRAVT ELGRPDAEYW NSQKDLLEQR 100
    RAAVDTYCRH NYGVGESFTV QRRVEPKVTV YPSKTQPLQH HNLLVCSVSG 150
    FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY 200
    TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF 250
    RNQKGHSGLQ PTGFLS 266
    Length:266
    Mass (Da):29,914
    Last modified:August 29, 2003 - v2
    Checksum:iCC9CC7E2D0DD036C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251P → R in AAA59781. (PubMed:3858829)Curated
    Sequence conflicti36 – 361F → S AA sequence (PubMed:6600932)Curated
    Sequence conflicti58 – 592RC → LF AA sequence (PubMed:6600932)Curated
    Sequence conflicti80 – 801T → E in AAA59781. (PubMed:3858829)Curated
    Sequence conflicti100 – 1034RRAA → KRGQ in AAA59781. (PubMed:3858829)Curated
    Sequence conflicti192 – 1921T → I in AAA59781. (PubMed:3858829)Curated

    Polymorphismi

    The following alleles of DRB1-1 are known: DRB1*01:01; DRB1*01:02; DRB1*01:03; DRB1*01:04; DRB1*01:05; DRB1*01:06; DRB1*01:07; DRB1*01:08; DRB1*01:09; DRB1*01:10; DRB1*01:11; DRB1*01:12; DRB1*01:13; DRB1*01:14; DRB1*01:15; DRB1*01:16; DRB1*01:17; DRB1*01:18; DRB1*01:19; DRB1*01:20 and DRB1*01:21. The sequence shown is that of DRB1*01:01.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51K → R.
    Corresponds to variant rs9270305 [ dbSNP | Ensembl ].
    VAR_056527
    Natural varianti13 – 131T → A.
    Corresponds to variant rs1059553 [ dbSNP | Ensembl ].
    VAR_033377
    Natural varianti29 – 291A → S.
    Corresponds to variant rs9270299 [ dbSNP | Ensembl ].
    VAR_033378
    Natural varianti33 – 331R → K.
    Corresponds to variant rs34716432 [ dbSNP | Ensembl ].
    VAR_033379
    Natural varianti33 – 331R → Q.
    Corresponds to variant rs34716432 [ dbSNP | Ensembl ].
    VAR_033380
    Natural varianti39 – 391Q → E in allele DRB1*01:07.
    VAR_016740
    Natural varianti66 – 661S → Y.
    Corresponds to variant rs16822820 [ dbSNP | Ensembl ].
    VAR_033381
    Natural varianti74 – 741G → R in allele DRB1*01:05.
    VAR_016741
    Natural varianti76 – 761Y → F.
    Corresponds to variant rs1060346 [ dbSNP | Ensembl ].
    VAR_033382
    Natural varianti89 – 891Y → S.
    Corresponds to variant rs36074728 [ dbSNP | Ensembl ].
    VAR_033383
    Natural varianti96 – 961L → I in allele DRB1*01:03.
    VAR_016710
    Natural varianti99 – 991Q → D in allele DRB1*01:03; requires 2 nucleotide substitutions.
    VAR_016711
    Natural varianti99 – 991Q → E.
    Corresponds to variant rs17881965 [ dbSNP | Ensembl ].
    VAR_033384
    Natural varianti99 – 991Q → H.
    Corresponds to variant rs17879599 [ dbSNP | Ensembl ].
    VAR_033385
    Natural varianti100 – 1001R → A in allele DRB1*01:06; requires 2 nucleotide substitutions.
    VAR_016742
    Natural varianti100 – 1001R → E in allele DRB1*01:03; requires 2 nucleotide substitutions.
    VAR_016712
    Natural varianti102 – 1021A → G.
    Corresponds to variant rs17878857 [ dbSNP | Ensembl ].
    VAR_033386
    Natural varianti103 – 1031A → E.
    Corresponds to variant rs16822805 [ dbSNP | Ensembl ].
    VAR_033387
    Natural varianti106 – 1061T → N in allele DRB1*01:04.
    Corresponds to variant rs16822752 [ dbSNP | Ensembl ].
    VAR_016713
    Natural varianti107 – 1071Y → H.
    Corresponds to variant rs16822512 [ dbSNP | Ensembl ].
    VAR_033388
    Natural varianti114 – 1141V → A in allele DRB1*01:02.
    Corresponds to variant rs17424145 [ dbSNP | Ensembl ].
    VAR_016714
    Natural varianti115 – 1151G → V in allele DRB1*01:02, allele DRB1*01:04 and allele DRB1*01:06.
    Corresponds to variant rs2230810 [ dbSNP | Ensembl ].
    VAR_016715
    Natural varianti164 – 1641G → D.
    Corresponds to variant rs1059633 [ dbSNP | Ensembl ].
    VAR_033389
    Natural varianti169 – 1691A → T.
    Corresponds to variant rs2308768 [ dbSNP | Ensembl ].
    VAR_033390
    Natural varianti171 – 1711V → M.
    Corresponds to variant rs701829 [ dbSNP | Ensembl ].
    VAR_033391
    Natural varianti178 – 1781Q → H.
    Corresponds to variant rs701830 [ dbSNP | Ensembl ].
    VAR_033392
    Natural varianti195 – 1951R → Q.
    Corresponds to variant rs3205588 [ dbSNP | Ensembl ].
    VAR_033393
    Natural varianti210 – 2101T → I.
    Corresponds to variant rs17423930 [ dbSNP | Ensembl ].
    VAR_033394
    Natural varianti236 – 2361V → M.
    Corresponds to variant rs2230816 [ dbSNP | Ensembl ].
    VAR_033395
    Natural varianti253 – 2531Q → E in allele DRB1*01:02.
    VAR_016716
    Natural varianti262 – 2621T → R.1 Publication
    Corresponds to variant rs9269744 [ dbSNP | Ensembl ].
    VAR_056528

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03069 mRNA. Translation: CAA26873.1.
    M11161 mRNA. Translation: AAA59781.1.
    M33600 mRNA. Translation: AAA59782.1.
    AY663400 Genomic DNA. Translation: AAU87993.1.
    AM419948 Genomic DNA. Translation: CAL99240.1.
    AK289463 mRNA. Translation: BAF82152.1.
    X64547 Genomic DNA. Translation: CAA45845.1.
    X99896 mRNA. Translation: CAA68171.1.
    AF089723 Genomic DNA. Translation: AAD51131.1.
    AJ276206 Genomic DNA. Translation: CAC27123.1.
    AB015184 Genomic DNA. Translation: BAA28761.1.
    AJ303118 Genomic DNA. Translation: CAC19693.1.
    Z50871 Genomic DNA. No translation available.
    M21008 mRNA. Translation: AAA59780.1.
    AF029288 Genomic DNA. Translation: AAF65497.1.
    AF029293 Genomic DNA. Translation: AAF65502.1.
    PIRiA19197.
    D24669. HLHU1B.
    I56072.
    PH0147.
    UniGeneiHs.534322.
    Hs.696211.
    Hs.736560.

    Genome annotation databases

    EnsembliENST00000360004; ENSP00000353099; ENSG00000196126.

    Polymorphism databases

    DMDMi34395916.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03069 mRNA. Translation: CAA26873.1 .
    M11161 mRNA. Translation: AAA59781.1 .
    M33600 mRNA. Translation: AAA59782.1 .
    AY663400 Genomic DNA. Translation: AAU87993.1 .
    AM419948 Genomic DNA. Translation: CAL99240.1 .
    AK289463 mRNA. Translation: BAF82152.1 .
    X64547 Genomic DNA. Translation: CAA45845.1 .
    X99896 mRNA. Translation: CAA68171.1 .
    AF089723 Genomic DNA. Translation: AAD51131.1 .
    AJ276206 Genomic DNA. Translation: CAC27123.1 .
    AB015184 Genomic DNA. Translation: BAA28761.1 .
    AJ303118 Genomic DNA. Translation: CAC19693.1 .
    Z50871 Genomic DNA. No translation available.
    M21008 mRNA. Translation: AAA59780.1 .
    AF029288 Genomic DNA. Translation: AAF65497.1 .
    AF029293 Genomic DNA. Translation: AAF65502.1 .
    PIRi A19197.
    D24669. HLHU1B.
    I56072.
    PH0147.
    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
    1AQD X-ray 2.45 B/E/H/K 30-227 [» ]
    1DLH X-ray 2.80 B/E 32-219 [» ]
    1FYT X-ray 2.60 B 30-221 [» ]
    1HXY X-ray 2.60 B 30-219 [» ]
    1JWM X-ray 2.70 B 30-219 [» ]
    1JWS X-ray 2.60 B 30-219 [» ]
    1JWU X-ray 2.30 B 30-219 [» ]
    1KG0 X-ray 2.65 B 32-219 [» ]
    1KLG X-ray 2.40 B 30-219 [» ]
    1KLU X-ray 1.93 B 30-219 [» ]
    1LO5 X-ray 3.20 B 30-219 [» ]
    1PYW X-ray 2.10 B 30-219 [» ]
    1R5I X-ray 2.60 B/F 30-219 [» ]
    1SEB X-ray 2.70 B/F 30-221 [» ]
    1SJE X-ray 2.45 B 30-219 [» ]
    1SJH X-ray 2.25 B 30-219 [» ]
    1T5W X-ray 2.40 B/E 30-219 [» ]
    1T5X X-ray 2.50 B 30-219 [» ]
    2FSE X-ray 3.10 B/D 33-219 [» ]
    2G9H X-ray 2.00 B 30-219 [» ]
    2IAM X-ray 2.80 B 30-219 [» ]
    2IAN X-ray 2.80 B/G/L/Q 30-219 [» ]
    2ICW X-ray 2.41 B/E 30-219 [» ]
    2IPK X-ray 2.30 B 30-219 [» ]
    2OJE X-ray 3.00 B/F 30-219 [» ]
    2XN9 X-ray 2.30 E 30-219 [» ]
    3L6F X-ray 2.10 B 30-221 [» ]
    3PDO X-ray 1.95 B 30-227 [» ]
    3PGC X-ray 2.66 B/E 30-227 [» ]
    3PGD X-ray 2.72 B/E 30-227 [» ]
    3QXA X-ray 2.71 B/E 30-219 [» ]
    3QXD X-ray 2.30 B/E 30-219 [» ]
    3S4S X-ray 2.40 B/E 30-221 [» ]
    3S5L X-ray 2.10 B/E 30-221 [» ]
    4AEN X-ray 2.20 B 30-227 [» ]
    4AH2 X-ray 2.36 B 30-227 [» ]
    4E41 X-ray 2.60 B/G 30-219 [» ]
    4FQX X-ray 2.60 B 30-221 [» ]
    4GBX X-ray 3.00 B 30-220 [» ]
    4I5B X-ray 2.12 B/E 31-222 [» ]
    ProteinModelPortali P04229.
    SMRi P04229. Positions 30-219.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6143N.
    IntActi P04229. 6 interactions.
    MINTi MINT-203282.

    Chemistry

    BindingDBi P04229.
    ChEMBLi CHEMBL1943.
    DrugBanki DB05259. Glatiramer Acetate.

    PTM databases

    PhosphoSitei P04229.

    Polymorphism databases

    DMDMi 34395916.

    Proteomic databases

    PaxDbi P04229.
    PRIDEi P04229.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360004 ; ENSP00000353099 ; ENSG00000196126 .

    Organism-specific databases

    GeneCardsi GC06M032546.
    HGNCi HGNC:4948. HLA-DRB1.
    HPAi CAB015400.
    CAB034021.
    MIMi 142857. gene.
    181000. phenotype.
    neXtProti NX_P04229.
    Orphaneti 703. Bullous pemphigoid.
    555. Celiac disease.
    243377. Diabetes mellitus type 1.
    220393. Diffuse cutaneous systemic sclerosis.
    545. Follicular lymphoma.
    220402. Limited cutaneous systemic sclerosis.
    220407. Limited systemic sclerosis.
    802. Multiple sclerosis.
    83465. Narcolepsy without cataplexy.
    2073. Narcolepsy-cataplexy.
    284130. Rheumatoid arthritis.
    797. Sarcoidosis.
    536. Systemic lupus erythematosus.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG68200.
    HOVERGENi HBG012730.
    InParanoidi P04229.
    OrthoDBi EOG7PS1GV.

    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 P04229.
    PROi P04229.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04229.
    Bgeei P04229.
    CleanExi HS_HLA-DRB1.
    Genevestigatori P04229.

    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. "DO beta: a new beta chain gene in HLA-D with a distinct regulation of expression."
      Tonnelle C., Demars R., Long E.O.
      EMBO J. 4:2839-2847(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*01:01).
    2. "DNA sequence and characterization of human class II major histocompatibility complex beta chains from the DR1 haplotype."
      Bell J.I., Estess P., St John T., Saiki R., Watling D.L., Erlich H.A., McDevitt H.O.
      Proc. Natl. Acad. Sci. U.S.A. 82:3405-3409(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*01:01).
    3. "Evolution of the HLA-DR1 gene family. Structural and functional analysis of the new allele 'DR-BON'."
      Coppin H.L., Avoustin P., Fabron J., Huchenq A., Garnier J.-M., Thomsen M., De Preval C.
      J. Immunol. 144:984-989(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*01:03).
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Full-length sequence analysis of the HLA-DRB1 locus suggests a recent origin of alleles."
      von Salome J., Gyllensten U., Bergstroem T.F.
      Immunogenetics 59:261-271(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRB1*01:01), VARIANT ARG-262.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cerebellum.
    7. "Polymorphism in the regulatory region of HLA-DRB genes correlating with haplotype evolution."
      Louis P., Eliaou J.F., Kerlan-Candon S., Pinet V., Vincent R., Clot J.
      Immunogenetics 38:21-26(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
      Tissue: B-cell.
    8. Middleton D., Versluis L.F., Tilanus M.G.J.
      Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*01:04).
    9. "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.
    10. "Identification of a novel DRB1-allele (DRB1*0106) by sequence-based typing."
      Palou E., Mongay L., Arias M.T., Isart F., Suarez B., Masso M., Fabregat V., Martorell J., Gaya A.
      Tissue Antigens 53:308-310(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:06).
    11. "Identification of three new DRB1 alleles, DRB1*0107, *0425 and *13012 and confirmation of DRB4*01033."
      Voorter C.E.M., Hepkema B.G., Lems S.P.M., van den Berg-Loonen E.M.
      Tissue Antigens 61:398-402(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:07).
    12. "HLA-DRB1 new alleles."
      Kashiwase K., Akaza T., Juji T.
      Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:05).
    13. "A new HLA-DRB1*01 allele."
      Dormoy A., Froelich N., Leisenbach R., Tongio M.M.
      Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:07).
    14. "Identification and sequencing of a novel DRB1*01 allele."
      Hashemi S., Couture C., Cole R., Buyse I.
      Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELE DRB1*01:02).
      Tissue: Blood.
    15. "Polymorphism of the HLA-DR1 haplotype in American blacks. Identification of a DR1 beta-chain determinant recognized in the mixed lymphocyte reaction."
      Hurley C.K., Ziff B.L., Silver J., Gregersen P.K., Hartzman R., Johnson A.H.
      J. Immunol. 140:4019-4023(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-266 (ALLELE DRB1*01:02).
    16. "HLA class II polymorphism."
      Arnaiz-Villena A.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-115 (ALLELES DRB1*01:01 AND DRB1*01:02).
      Tissue: Blood.
    17. Cited for: DISEASE.
    18. "Invariant chain structure and MHC class II function."
      Cresswell P.
      Cell 84:505-507(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    19. "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.
    20. "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.
    21. "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.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "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.
    24. "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.
    25. "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.
    26. "Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1."
      Brown J.H., Jardetzky T.S., Gorga J.C., Stern L.J., Urban R.G., Strominger J.L., Wiley D.C.
      Nature 364:33-39(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 32-219.
    27. "Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide."
      Stern L.J., Brown J.H., Jardetzky T.J., Gorga J.C., Urban R.G., Strominger J.L., Wiley D.C.
      Nature 368:215-221(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 32-219.
    28. "Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen."
      Jardetzky T.S., Brown J.H., Gorga J.C., Stern L.J., Urban R.G., Chi Y.I., Stauffacher C., Strominger J.L., Wiley D.C.
      Nature 368:711-718(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH SEB.

    Entry informationi

    Entry namei2B11_HUMAN
    AccessioniPrimary (citable) accession number: P04229
    Secondary accession number(s): A4F5N0
    , A8K098, O62869, P13758, Q06662, Q30116, Q30117, Q5Y7E9, Q7M2H4, Q95461, Q9BCL7, Q9GIK5, Q9MXZ0, Q9MXZ5, Q9TQ91
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: August 29, 2003
    Last modified: October 1, 2014
    This is version 145 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