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HLA-DRB1

Chr 6p21.32

major histocompatibility complex, class II, DR beta 1

MANE:
ENST00000360004.6

Annotations refreshed 10 hours ago.

Predicted protein structure

Clinical relevance (Genomics England PanelApp)

Diagnostic Grade (Green)

  • COVID-19 research

    Unknown
  • Cerebral vascular malformations

    Unknown
  • Familial Meniere Disease

  • Gastrointestinal epithelial barrier disorders

  • Pneumothorax - familial

Disease associations (Open Targets)

  • rheumatoid arthritis

    0.40
  • multiple sclerosis

    0.40
  • Pulmonary artery atresia

    0.33
  • neurodegenerative disease

    0.21
  • myeloid sarcoma

    0.12
  • type 1 diabetes mellitus

    0.12
  • systemic lupus erythematosus

    0.12
  • systemic sclerosis

    0.11
  • non-Hodgkin lymphoma

    0.11
  • autoimmune hepatitis

    0.11

Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.

Protein function (UniProt)

HLA class II histocompatibility antigen, DRB1 beta chain

A beta chain of antigen-presenting major histocompatibility complex class II (MHCII) molecule. In complex with the alpha chain HLA-DRA, displays antigenic peptides on professional antigen presenting cells (APCs) for recognition by alpha-beta T cell receptor (TCR) on HLA-DRB1-restricted CD4-positive T cells. This guides antigen-specific T-helper effector functions, both antibody-mediated immune response and macrophage activation, to ultimately eliminate the infectious agents and transformed cells (PubMed:15265931, PubMed:16148104, PubMed:22327072, PubMed:27591323, PubMed:29884618, PubMed:31495665, PubMed:8642306). Typically presents extracellular peptide antigens of 10 to 30 amino acids that arise from proteolysis of endocytosed antigens in lysosomes (PubMed:8145819). In the tumor microenvironment, presents antigenic peptides that are primarily generated in tumor-resident APCs likely via phagocytosis of apoptotic tumor cells or macropinocytosis of secreted tumor proteins (PubMed:31495665). Presents peptides derived from intracellular proteins that are trapped in autolysosomes after macroautophagy, a mechanism especially relevant for T cell selection in the thymus and central immune tolerance (PubMed:17182262, PubMed:23783831). The selection of the immunodominant epitopes follows two processing modes: 'bind first, cut/trim later' for pathogen-derived antigenic peptides and 'cut first, bind later' for autoantigens/self-peptides (PubMed:25413013). The anchor residue at position 1 of the peptide N-terminus, usually a large hydrophobic residue, is essential for high affinity interaction with MHCII molecules (PubMed:8145819)

Data sources: HGNC (CC BY 4.0), AlphaFold (CC BY 4.0, Jumper et al. Nature 2021), Genomics England PanelApp (CC BY 4.0), ClinGen, Open Targets (CC0), UniProt.

Not for sole clinical decision-making. Always verify against primary sources.