HLA-DRB3
entrez
3125
canonical
uniprot
P79483
canonical
ensembl
ENSG00000196101
resolver
ensembl
ENSG00000231679
resolver
ensp
ENSP00000302517
resolver
ensp
ENSP00000372607
resolver
enst
ENST00000307137
resolver
enst
ENST00000383126
resolver
genesymbol
HLA-DRB3
resolver
hgnc
HGNC:4951
resolver
uniprot
A0ZXY9
resolver
uniprot
A7MA46
resolver
uniprot
B5AU12
resolver
uniprot
B5AU13
resolver
uniprot
B5AU14
resolver
uniprot
B8YAC6
resolver
uniprot
C6H115
resolver
uniprot
C6H116
resolver
uniprot
O02875
resolver
uniprot
O19590
resolver
uniprot
O46701
resolver
uniprot
O46794
resolver
uniprot
O78049
resolver
uniprot
O78162
resolver
uniprot
P01913
resolver
uniprot
P79663
resolver
uniprot
Q29721
resolver
uniprot
Q29809
resolver
uniprot
Q2PPD0
resolver
uniprot
Q30144
resolver
uniprot
Q507L8
resolver
uniprot
Q5SP44
resolver
uniprot
Q5STE0
resolver
uniprot
Q6YJU6
resolver
uniprot
Q70M87
resolver
uniprot
Q7YQ62
resolver
uniprot
Q860I9
resolver
uniprot
Q8SP69
resolver
uniprot
Q8WLT7
resolver
uniprot
Q8WLT8
resolver
uniprot
Q95359
resolver
uniprot
Q95HM8
resolver
uniprot
Q95IE5
resolver
uniprot
Q96H16
resolver
uniprot
Q9BCP3
resolver
uniprot
Q9BD18
resolver
uniprot
Q9MYA4
resolver
uniprot
Q9MYH3
resolver
uniprot
Q9MYH4
resolver
uniprot
Q9TP01
resolver
uniprot
Q9TP02
resolver
uniprot
Q9TPB5
resolver
uniprot
Q9TQ21
resolver
uniprot
Q9UIN3
resolver
uniprot
Q9UIN5
resolver
uniprot_entry
DRB3_HUMAN
resolver
uniprot_sec
A0ZXY9
resolver
uniprot_sec
A7MA46
resolver
uniprot_sec
B5AU12
resolver
uniprot_sec
B5AU13
resolver
uniprot_sec
B5AU14
resolver
uniprot_sec
B8YAC6
resolver
uniprot_sec
C6H115
resolver
uniprot_sec
C6H116
resolver
uniprot_sec
O02875
resolver
uniprot_sec
O19590
resolver
uniprot_sec
O46701
resolver
uniprot_sec
O46794
resolver
uniprot_sec
O78049
resolver
uniprot_sec
O78162
resolver
uniprot_sec
P01913
resolver
uniprot_sec
P79663
resolver
uniprot_sec
Q29721
resolver
uniprot_sec
Q29809
resolver
uniprot_sec
Q2PPD0
resolver
uniprot_sec
Q30144
resolver
uniprot_sec
Q507L8
resolver
uniprot_sec
Q5SP44
resolver
uniprot_sec
Q5STE0
resolver
uniprot_sec
Q6YJU6
resolver
uniprot_sec
Q70M87
resolver
uniprot_sec
Q7YQ62
resolver
uniprot_sec
Q860I9
resolver
uniprot_sec
Q8SP69
resolver
uniprot_sec
Q8WLT7
resolver
uniprot_sec
Q8WLT8
resolver
uniprot_sec
Q95359
resolver
uniprot_sec
Q95HM8
resolver
uniprot_sec
Q95IE5
resolver
uniprot_sec
Q96H16
resolver
uniprot_sec
Q9BCP3
resolver
uniprot_sec
Q9BD18
resolver
uniprot_sec
Q9MYA4
resolver
uniprot_sec
Q9MYH3
resolver
uniprot_sec
Q9MYH4
resolver
uniprot_sec
Q9TP01
resolver
uniprot_sec
Q9TP02
resolver
uniprot_sec
Q9TPB5
resolver
uniprot_sec
Q9TQ21
resolver
uniprot_sec
Q9UIN3
resolver
uniprot_sec
Q9UIN5
resolver
amino_acid_sequence
MVCLKLPGGSSLAALTVTLMVLSSRLAFAGDTRPRFLELRKSECHFFNGTERVRYLDRYFHNQEEFLRFDSDVGEYRAVTELGRPVAESWNSQKDLLEQKRGRVDNYCRHNYGVGESFTVQRRVHPQVTVYPAKTQPLQHHNLLVCSVSGFYPGSIEVRWFRNGQEEKAGVVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSVTSALTVEWRARSESAQSKMLSGVGGFVLGLLFLGAGLFIYFRNQKGHSGLQPTGFLS
uniprot
proteins
function
FUNCTION: 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-DRB3-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. Typically presents extracellular peptide antigens of 10 to 30 amino acids that arise from proteolysis of endocytosed antigens in lysosomes (PubMed:16148104, PubMed:19531622, PubMed:19830726, PubMed:20368442, PubMed:22929521, PubMed:23569328, PubMed:2463305, PubMed:2788702, PubMed:30282837, PubMed:31020640, PubMed:31308093, PubMed:31333679). 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 (By similarity). 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 (By similarity). 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. 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 (By similarity). {ECO:0000250|UniProtKB:P01911, ECO:0000269|PubMed:16148104, ECO:0000269|PubMed:19531622, ECO:0000269|PubMed:19830726, ECO:0000269|PubMed:20368442, ECO:0000269|PubMed:22929521, ECO:0000269|PubMed:23569328, ECO:0000269|PubMed:2463305, ECO:0000269|PubMed:2788702, ECO:0000269|PubMed:30282837, ECO:0000269|PubMed:31020640, ECO:0000269|PubMed:31308093, ECO:0000269|PubMed:31333679}.; FUNCTION: ALLELE DRB3*01:01: Exclusively presents several immunogenic epitopes derived from C.tetani neurotoxin tetX, playing a significant role in immune recognition and long-term protection (PubMed:19830726, PubMed:2463305, PubMed:2788702). Presents viral epitopes derived from HHV-6B U11, TRX2/U56 and U85 antigens to polyfunctional CD4-positive T cells with cytotoxic activity implicated in control of HHV-6B infection (PubMed:31020640). {ECO:0000269|PubMed:19830726, ECO:0000269|PubMed:2463305, ECO:0000269|PubMed:2788702, ECO:0000269|PubMed:31020640}.; FUNCTION: ALLELE DRB3*02:02 Exclusively presents several immunogenic epitopes derived from C.tetani neurotoxin tetX, playing a significant role in immune recognition and long-term protection (PubMed:19830726, PubMed:2788702). Upon EBV infection, presents to CD4-positive T cells latent antigen EBNA2 (PRSPTVFYNIPPMPLPPSQL) and lytic antigen BZLF1 (LTAYHVSTAPTGSWF) peptides, driving oligoclonal expansion and selection of virus-specific memory T cell subsets with cytotoxic potential to directly eliminate virus-infected B cells (PubMed:23569328, PubMed:31308093). Presents viral epitopes derived from HHV-6B U11, gB/U39 and gH/U48 antigens to polyfunctional CD4-positive T cells with cytotoxic activity implicated in control of HHV-6B infection (PubMed:31020640). Plays a minor role in CD4-positive T cell immune response against Dengue virus by presenting conserved peptides from capsid and non-structural NS3 proteins (PubMed:31333679). Displays peptides derived from IAV matrix protein M, implying a role in protection against IAV infection (PubMed:19830726). In the context of tumor immunesurveillance, may present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (KRYFKLSHLQMHSRKH), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies (PubMed:22929521). Presents to Vbeta2-positive T-helper 1 cells specifically an immunodominant peptide derived from tumor antigen CTAG1A/NY-ESO-1(PGVLLKEFTVSGNILTIRLTAADHR) and confers protective memory response (PubMed:19531622, PubMed:20368442). In metastatic epithelial tumors, presents to intratumoral CD4-positive T cells a TP53 neoantigen (HYNYMCNSSCMGSMNRRPILTIITL) carrying G245S hotspot driver mutation and may mediate tumor regression (PubMed:30282837). {ECO:0000269|PubMed:19531622, ECO:0000269|PubMed:19830726, ECO:0000269|PubMed:20368442, ECO:0000269|PubMed:22929521, ECO:0000269|PubMed:23569328, ECO:0000269|PubMed:2788702, ECO:0000269|PubMed:30282837, ECO:0000269|PubMed:31020640, ECO:0000269|PubMed:31308093, ECO:0000269|PubMed:31333679}.; FUNCTION: ALLELE DRB3*03:01: Presents a series of conserved peptides derived from the M.tuberculosis PPE family of proteins, in particular PPE29 and PPE33, known to be highly immunogenic (PubMed:32341563). Presents immunogenic epitopes derived from C.tetani neurotoxin tetX, playing a role in immune recognition and long-term protection (PubMed:2788702). Displays immunodominant viral peptides from HCV non-structural protein NS2, as part of a broad range T-helper response to resolve infection (PubMed:16148104). {ECO:0000269|PubMed:16148104, ECO:0000269|PubMed:2788702, ECO:0000269|PubMed:32341563}.
uniprot
proteins
mass_dalton
29962
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by MARCHF1 and MARCHF8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II. {ECO:0000305|PubMed:18305173}.
uniprot
proteins
protein_family
MHC class II family
uniprot
proteins
pubmed
10599892
uniprot
proteins
pubmed
10902611
uniprot
proteins
pubmed
10958362
uniprot
proteins
pubmed
11098940
uniprot
proteins
pubmed
11380956
uniprot
proteins
pubmed
11894954
uniprot
proteins
pubmed
11972885
uniprot
proteins
pubmed
12944060
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15104685
uniprot
proteins
pubmed
15140047
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15496209
uniprot
proteins
pubmed
16148104
uniprot
proteins
pubmed
17583734
uniprot
proteins
pubmed
18305173
uniprot
proteins
pubmed
18697946
uniprot
proteins
pubmed
18764810
uniprot
proteins
pubmed
19000136
uniprot
proteins
pubmed
19494351
uniprot
proteins
pubmed
19531622
uniprot
proteins
pubmed
19535639
uniprot
proteins
pubmed
19706888
uniprot
proteins
pubmed
19830726
uniprot
proteins
pubmed
20368442
uniprot
proteins
pubmed
22929521
uniprot
proteins
pubmed
23510415
uniprot
proteins
pubmed
23569328
uniprot
proteins
pubmed
2463305
uniprot
proteins
pubmed
2471740
uniprot
proteins
pubmed
2788702
uniprot
proteins
pubmed
30282837
uniprot
proteins
pubmed
31020640
uniprot
proteins
pubmed
31308093
uniprot
proteins
pubmed
31333679
uniprot
proteins
pubmed
32341563
uniprot
proteins
pubmed
3459965
uniprot
proteins
pubmed
3476943
uniprot
proteins
pubmed
6414998
uniprot
proteins
pubmed
9162096
uniprot
proteins
pubmed
9234492
uniprot
proteins
pubmed
9234494
uniprot
proteins
pubmed
9243765
uniprot
proteins
pubmed
9389331
uniprot
proteins
pubmed
9802612
uniprot
proteins
sequence_length
266
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173, ECO:0000269|PubMed:19531622, ECO:0000269|PubMed:19830726}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein {ECO:0000255}. Autolysosome membrane {ECO:0000250|UniProtKB:P01911}; Single-pass type I membrane protein {ECO:0000255}. 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 (PubMed:18305173). Component of immunological synapses at the interface between T cell and APC. {ECO:0000250|UniProtKB:P01911}.
uniprot
proteins
transmembrane_region
TRANSMEM 228..248; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins