HLA-DMB

HLA class II histocompatibility antigen, DM beta chain is a protein that in humans is encoded by the HLA-DMB gene.

HLA-DMB
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1HDM, 2BC4, 4FQX, 4GBX, 4I0P
Identifiers
Aliases	HLA-DMB, D6S221E, RING7, major histocompatibility complex, class II, DM beta
External IDs	OMIM: 142856; MGI: 95922; HomoloGene: 68231; GeneCards: HLA-DMB; OMA:HLA-DMB - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6p21.32 Start 32,934,629 bp End 32,941,028 bp
Gene location (Mouse) Chr. Chromosome 17 (mouse) Band 17 B1|17 17.98 cM Start 34,372,046 bp End 34,379,204 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte granulocyte lymph node appendix spleen duodenum gallbladder right lung upper lobe of left lung rectum Top expressed in mesenteric lymph nodes spleen blood right kidney ankle joint superior surface of tongue thymus sciatic nerve lip subcutaneous adipose tissue More reference expression data BioGPS More reference expression data
Gene ontology Molecular function MHC class II protein complex binding protein binding Cellular component lysosomal membrane lysosome membrane endosome late endosome membrane integral component of membrane MHC class II protein complex Biological process positive regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell antigen processing and presentation MHC class II protein complex assembly positive regulation of T cell proliferation antigen processing and presentation of peptide or polysaccharide antigen via MHC class II peptide antigen assembly with MHC class II protein complex immune system process antigen processing and presentation of exogenous peptide antigen via MHC class II immune response adaptive immune response Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3109 14999 Ensembl ENSG00000241674 ENSG00000226264 ENSG00000242574 ENSG00000239329 ENSG00000234154 ENSG00000242386 ENSG00000242092 ENSG00000241296 ENSMUSG00000079547 UniProt P28068 P35737 Q31094 RefSeq (mRNA) NM_002118 NM_010387 RefSeq (protein) NP_002109 NP_034517 Location (UCSC) Chr 6: 32.93 – 32.94 Mb Chr 17: 34.37 – 34.38 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

HLA-DMB belongs to the HLA class II beta chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DMA) and a beta (DMB) chain, both anchored in the membrane. It is located in intracellular vesicles. DM plays a central role in the peptide loading of MHC class II molecules by helping to release the CLIP (class II-associated invariant chain peptide) molecule from the peptide binding site. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The beta chain is approximately 26–28 kDa and its gene contains 6 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and exon 5 encodes the cytoplasmic tail.

Clinical significance

HLA-DMB is upregulated in tumor tissue of Caucasian but not African patients. Its role in tumor immunology is undefined but has been shown to positively correlated with increased T-cell infiltration and improved prognosis in ovarian cancer. Differential immune processes mediated by HLA-DMB may contribute to the disparity in cancer outcome.

Further reading

• Vogt AB, Kropshofer H (1999). "HLA-DM - an endosomal and lysosomal chaperone for the immune system". Trends Biochem. Sci. 24 (4): 150–4. doi:10.1016/S0968-0004(99)01364-X. PMID 10322421.
• Kropshofer H, Hämmerling GJ, Vogt AB (2000). "The impact of the non-classical MHC proteins HLA-DM and HLA-DO on loading of MHC class II molecules". Immunol. Rev. 172: 267–78. doi:10.1111/j.1600-065X.1999.tb01371.x. PMID 10631952. S2CID 22216172.
• Piatier-Tonneau D, Gastinel LN, Amblard F, et al. (1991). "Interaction of CD4 with HLA class II antigens and HIV gp120". Immunogenetics. 34 (2): 121–8. doi:10.1007/BF00211424. PMID 1869305. S2CID 10116507.
• Rosenstein Y, Burakoff SJ, Herrmann SH (1990). "HIV-gp120 can block CD4-class II MHC-mediated adhesion". J. Immunol. 144 (2): 526–31. doi:10.4049/jimmunol.144.2.526. PMID 1967269.
• Bowman MR, MacFerrin KD, Schreiber SL, Burakoff SJ (1991). "Identification and structural analysis of residues in the V1 region of CD4 involved in interaction with human immunodeficiency virus envelope glycoprotein gp120 and class II major histocompatibility complex molecules". Proc. Natl. Acad. Sci. U.S.A. 87 (22): 9052–6. doi:10.1073/pnas.87.22.9052. PMC 55099. PMID 1978941.
• Clayton LK, Sieh M, Pious DA, Reinherz EL (1989). "Identification of human CD4 residues affecting class II MHC versus HIV-1 gp120 binding". Nature. 339 (6225): 548–51. Bibcode:1989Natur.339..548C. doi:10.1038/339548a0. PMID 2543930. S2CID 4246781.
• Diamond DC, Sleckman BP, Gregory T, et al. (1988). "Inhibition of CD4+ T cell function by the HIV envelope protein, gp120". J. Immunol. 141 (11): 3715–7. doi:10.4049/jimmunol.141.11.3715. PMID 2846691.
• Andrieu JM, Even P, Venet A (1986). "AIDS and related syndromes as a viral-induced autoimmune disease of the immune system: an anti-MHC II disorder. Therapeutic implications". AIDS Research. 2 (3): 163–74. doi:10.1089/aid.1.1986.2.163. PMID 3489470.
• Houlgatte R, Scarmato P, el Marhomy S, et al. (1994). "HLA class II antigens and the HIV envelope glycoprotein gp120 bind to the same face of CD4". J. Immunol. 152 (9): 4475–88. doi:10.4049/jimmunol.152.9.4475. PMID 7512597.
• Shaman J, von Scheven E, Morris P, et al. (1995). "Analysis of HLA-DMB mutants and -DMB genomic structure". Immunogenetics. 41 (2–3): 117–24. doi:10.1007/BF00182322. PMID 7528727. S2CID 40078535.
• Chirmule N, McCloskey TW, Hu R, et al. (1995). "HIV gp120 inhibits T cell activation by interfering with expression of costimulatory molecules CD40 ligand and CD80 (B71)". J. Immunol. 155 (2): 917–24. doi:10.4049/jimmunol.155.2.917. PMID 7541827.
• Rowell JF, Stanhope PE, Siliciano RF (1995). "Endocytosis of endogenously synthesized HIV-1 envelope protein. Mechanism and role in processing for association with class II MHC". J. Immunol. 155 (1): 473–88. doi:10.4049/jimmunol.155.1.473. PMID 7602119. S2CID 19994352.
• Sherman MA, Weber DA, Jensen PE (1995). "DM enhances peptide binding to class II MHC by release of invariant chain-derived peptide". Immunity. 3 (2): 197–205. doi:10.1016/1074-7613(95)90089-6. PMID 7648393.
• Radley E, Alderton RP, Kelly A, et al. (1994). "Genomic organization of HLA-DMA and HLA-DMB. Comparison of the gene organization of all six class II families in the human major histocompatibility complex". J. Biol. Chem. 269 (29): 18834–8. doi:10.1016/S0021-9258(17)32242-1. PMID 8034636.
• Chen YH, Böck G, Vornhagen R, et al. (1994). "HIV-1 gp41 binding proteins and antibodies to gp41 could inhibit enhancement of human Raji cell MHC class I and II expression by gp41". Mol. Immunol. 31 (13): 977–82. doi:10.1016/0161-5890(94)90092-2. PMID 8084338.
• Fling SP, Arp B, Pious D (1994). "HLA-DMA and -DMB genes are both required for MHC class II/peptide complex formation in antigen-presenting cells". Nature. 368 (6471): 554–8. Bibcode:1994Natur.368..554F. doi:10.1038/368554a0. PMID 8139690. S2CID 4307699.
• Chirmule N, Wang XP, Hu R, et al. (1994). "Envelope glycoproteins of HIV-1 interfere with T-cell-dependent B cell differentiation: role of CD4-MHC class II interaction in the effector phase of T cell help". Cell. Immunol. 155 (1): 169–82. doi:10.1006/cimm.1994.1110. PMID 8168144.
• Sanderson F, Powis SH, Kelly AP, Trowsdale J (1993). "Limited polymorphism in HLA-DM does not involve the peptide binding groove". Immunogenetics. 39 (1): 56–8. doi:10.1007/bf00171797. PMID 8225438. S2CID 27369392.
• Callahan KM, Rowell JF, Soloski MJ, et al. (1993). "HIV-1 envelope protein is expressed on the surface of infected cells before its processing and presentation to class II-restricted T lymphocytes". J. Immunol. 151 (6): 2928–42. doi:10.4049/jimmunol.151.6.2928. PMID 8376762.