HLA-DRB5
entrez
3127
canonical
uniprot
Q30154
canonical
ensembl
ENSG00000198502
resolver
ensp
ENSP00000364114
resolver
ensp
ENSP00000667954
resolver
enst
ENST00000374975
resolver
genesymbol
HLA-DRB5
resolver
hgnc
HGNC:4953
resolver
uniprot
B2RBV6
resolver
uniprot
C7C4X3
resolver
uniprot
O00157
resolver
uniprot
O00283
resolver
uniprot
O46700
resolver
uniprot
Q29703
resolver
uniprot
Q29787
resolver
uniprot
Q29788
resolver
uniprot
Q30126
resolver
uniprot
Q30150
resolver
uniprot
Q30199
resolver
uniprot
Q6SJR2
resolver
uniprot
Q7M2H9
resolver
uniprot
Q8HWS7
resolver
uniprot
Q8WLR5
resolver
uniprot
Q9MY54
resolver
uniprot
Q9XRX6
resolver
uniprot_entry
DRB5_HUMAN
resolver
uniprot_sec
B2RBV6
resolver
uniprot_sec
C7C4X3
resolver
uniprot_sec
O00157
resolver
uniprot_sec
O00283
resolver
uniprot_sec
O46700
resolver
uniprot_sec
Q29703
resolver
uniprot_sec
Q29787
resolver
uniprot_sec
Q29788
resolver
uniprot_sec
Q30126
resolver
uniprot_sec
Q30150
resolver
uniprot_sec
Q30199
resolver
uniprot_sec
Q6SJR2
resolver
uniprot_sec
Q7M2H9
resolver
uniprot_sec
Q8HWS7
resolver
uniprot_sec
Q8WLR5
resolver
uniprot_sec
Q9MY54
resolver
uniprot_sec
Q9XRX6
resolver
amino_acid_sequence
MVCLKLPGGSYMAKLTVTLMVLSSPLALAGDTRPRFLQQDKYECHFFNGTERVRFLHRDIYNQEEDLRFDSDVGEYRAVTELGRPDAEYWNSQKDFLEDRRAAVDTYCRHNYGVGESFTVQRRVEPKVTVYPARTQTLQHHNLLVCSVNGFYPGSIEVRWFRNSQEEKAGVVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSVTSPLTVEWRAQSESAQSKMLSGVGGFVLGLLFLGAGLFIYFKNQKGHSGLHPTGLVS
uniprot
proteins
function
FUNCTION: 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.
uniprot
proteins
mass_dalton
30056
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to down-regulation of MHC class II. {ECO:0000305|PubMed:18305173}.
uniprot
proteins
protein_family
MHC class II family
uniprot
proteins
pubmed
11080454
uniprot
proteins
pubmed
11163233
uniprot
proteins
pubmed
11684289
uniprot
proteins
pubmed
12244309
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14617041
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1471145
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16079912
uniprot
proteins
pubmed
16671952
uniprot
proteins
pubmed
17241953
uniprot
proteins
pubmed
18046453
uniprot
proteins
pubmed
18305173
uniprot
proteins
pubmed
19092054
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19533806
uniprot
proteins
pubmed
2001975
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2885840
uniprot
proteins
pubmed
3099214
uniprot
proteins
pubmed
3259543
uniprot
proteins
pubmed
3476943
uniprot
proteins
pubmed
3571980
uniprot
proteins
pubmed
6576979
uniprot
proteins
pubmed
8598037
uniprot
proteins
pubmed
8773325
uniprot
proteins
pubmed
9162096
uniprot
proteins
pubmed
9226128
uniprot
proteins
pubmed
9458128
uniprot
proteins
pubmed
9694360
uniprot
proteins
sequence_length
266
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein {ECO:0000269|PubMed:18305173, ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein {ECO:0000269|PubMed:18305173, ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein {ECO:0000269|PubMed:18305173, ECO:0000305}. Endosome membrane {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein {ECO:0000269|PubMed:18305173, ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein {ECO:0000269|PubMed:18305173, ECO:0000305}. Late endosome membrane {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein {ECO:0000269|PubMed:18305173, ECO:0000305}. 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.
uniprot
proteins
transmembrane_region
TRANSMEM 228..248; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins