General Information of Target

Target ID LDTP01919
Target Name HLA class II histocompatibility antigen, DQ beta 1 chain (HLA-DQB1)
Gene Name HLA-DQB1
Gene ID 3119
Synonyms
HLA-DQB; HLA class II histocompatibility antigen, DQ beta 1 chain; MHC class II antigen DQB1
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
MSWKKALRIPGGLRAATVTLMLAMLSTPVAEGRDSPEDFVYQFKAMCYFTNGTERVRYVT
RYIYNREEYARFDSDVEVYRAVTPLGPPDAEYWNSQKEVLERTRAELDTVCRHNYQLELR
TTLQRRVEPTVTISPSRTEALNHHNLLVCSVTDFYPAQIKVRWFRNDQEETTGVVSTPLI
RNGDWTFQILVMLEMTPQHGDVYTCHVEHPSLQNPITVEWRAQSESAQSKMLSGIGGFVL
GLIFLGLGLIIHHRSQKGLLH
Target Bioclass
Immunoglobulin
Family
MHC class II family
Subcellular location
Cell membrane
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 ID
P01920
Ensemble ID
ENST00000399088.8
HGNC ID
HGNC:4944

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 2 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
DBIA
 Probe Info 
C111(1.26)  LDD1510  [1]
IPM
 Probe Info 
N.A.  LDD2156  [2]

Competitor(s) Related to This Target

Competitor ID Name Cell line Binding Site(Ratio) Interaction ID Ref
 LDCM0237  AC12 HEK-293T C111(1.26)  LDD1510  [1]
 LDCM0259  AC14 HEK-293T C111(1.32)  LDD1512  [1]
 LDCM0270  AC15 HEK-293T C111(0.81)  LDD1513  [1]
 LDCM0280  AC20 HEK-293T C111(0.98)  LDD1519  [1]
 LDCM0282  AC22 HEK-293T C111(1.10)  LDD1521  [1]
 LDCM0283  AC23 HEK-293T C111(0.63)  LDD1522  [1]
 LDCM0288  AC28 HEK-293T C111(1.25)  LDD1527  [1]
 LDCM0291  AC30 HEK-293T C111(0.97)  LDD1530  [1]
 LDCM0292  AC31 HEK-293T C111(0.78)  LDD1531  [1]
 LDCM0297  AC36 HEK-293T C111(1.34)  LDD1536  [1]
 LDCM0299  AC38 HEK-293T C111(1.01)  LDD1538  [1]
 LDCM0300  AC39 HEK-293T C111(1.08)  LDD1539  [1]
 LDCM0301  AC4 HEK-293T C111(1.07)  LDD1540  [1]
 LDCM0306  AC44 HEK-293T C111(1.33)  LDD1545  [1]
 LDCM0308  AC46 HEK-293T C111(1.04)  LDD1547  [1]
 LDCM0309  AC47 HEK-293T C111(1.02)  LDD1548  [1]
 LDCM0315  AC52 HEK-293T C111(1.39)  LDD1554  [1]
 LDCM0317  AC54 HEK-293T C111(1.37)  LDD1556  [1]
 LDCM0318  AC55 HEK-293T C111(1.08)  LDD1557  [1]
 LDCM0323  AC6 HEK-293T C111(1.17)  LDD1562  [1]
 LDCM0324  AC60 HEK-293T C111(1.24)  LDD1563  [1]
 LDCM0326  AC62 HEK-293T C111(1.15)  LDD1565  [1]
 LDCM0327  AC63 HEK-293T C111(1.00)  LDD1566  [1]
 LDCM0334  AC7 HEK-293T C111(1.00)  LDD1568  [1]
 LDCM0367  CL1 HEK-293T C111(1.13)  LDD1571  [1]
 LDCM0368  CL10 HEK-293T C111(1.22)  LDD1572  [1]
 LDCM0370  CL101 HEK-293T C111(1.17)  LDD1574  [1]
 LDCM0374  CL105 HEK-293T C111(0.82)  LDD1578  [1]
 LDCM0378  CL109 HEK-293T C111(0.96)  LDD1582  [1]
 LDCM0379  CL11 HEK-293T C111(1.01)  LDD1583  [1]
 LDCM0383  CL113 HEK-293T C111(0.96)  LDD1587  [1]
 LDCM0387  CL117 HEK-293T C111(0.97)  LDD1591  [1]
 LDCM0392  CL121 HEK-293T C111(0.93)  LDD1596  [1]
 LDCM0396  CL125 HEK-293T C111(0.90)  LDD1600  [1]
 LDCM0400  CL13 HEK-293T C111(1.13)  LDD1604  [1]
 LDCM0408  CL20 HEK-293T C111(1.91)  LDD1612  [1]
 LDCM0410  CL22 HEK-293T C111(1.60)  LDD1614  [1]
 LDCM0411  CL23 HEK-293T C111(1.39)  LDD1615  [1]
 LDCM0413  CL25 HEK-293T C111(1.17)  LDD1617  [1]
 LDCM0421  CL32 HEK-293T C111(1.50)  LDD1625  [1]
 LDCM0423  CL34 HEK-293T C111(1.11)  LDD1627  [1]
 LDCM0424  CL35 HEK-293T C111(0.96)  LDD1628  [1]
 LDCM0426  CL37 HEK-293T C111(1.01)  LDD1630  [1]
 LDCM0434  CL44 HEK-293T C111(1.64)  LDD1638  [1]
 LDCM0436  CL46 HEK-293T C111(1.36)  LDD1640  [1]
 LDCM0437  CL47 HEK-293T C111(0.97)  LDD1641  [1]
 LDCM0439  CL49 HEK-293T C111(1.02)  LDD1643  [1]
 LDCM0447  CL56 HEK-293T C111(1.51)  LDD1650  [1]
 LDCM0449  CL58 HEK-293T C111(1.19)  LDD1652  [1]
 LDCM0450  CL59 HEK-293T C111(0.83)  LDD1653  [1]
 LDCM0453  CL61 HEK-293T C111(0.82)  LDD1656  [1]
 LDCM0460  CL68 HEK-293T C111(1.44)  LDD1663  [1]
 LDCM0463  CL70 HEK-293T C111(1.02)  LDD1666  [1]
 LDCM0464  CL71 HEK-293T C111(0.99)  LDD1667  [1]
 LDCM0466  CL73 HEK-293T C111(1.03)  LDD1669  [1]
 LDCM0473  CL8 HEK-293T C111(1.64)  LDD1676  [1]
 LDCM0474  CL80 HEK-293T C111(1.92)  LDD1677  [1]
 LDCM0476  CL82 HEK-293T C111(1.61)  LDD1679  [1]
 LDCM0477  CL83 HEK-293T C111(0.94)  LDD1680  [1]
 LDCM0479  CL85 HEK-293T C111(0.97)  LDD1682  [1]
 LDCM0487  CL92 HEK-293T C111(1.53)  LDD1690  [1]
 LDCM0489  CL94 HEK-293T C111(1.22)  LDD1692  [1]
 LDCM0490  CL95 HEK-293T C111(0.73)  LDD1693  [1]
 LDCM0492  CL97 HEK-293T C111(0.70)  LDD1695  [1]
 LDCM0022  KB02 HG-3 C111(1.41)  LDD2355  [3]
 LDCM0023  KB03 MEC-1 C111(3.54)  LDD2876  [3]
 LDCM0024  KB05 MEC-1 C111(3.30)  LDD3293  [3]

The Interaction Atlas With This Target

The Protein(s) Related To This Target

Immunoglobulin
Click To Hide/Show 1 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
HLA class II histocompatibility antigen, DQ alpha 1 chain (HLA-DQA1) MHC class II family P01909

References

1 Accelerating multiplexed profiling of protein-ligand interactions: High-throughput plate-based reactive cysteine profiling with minimal input. Cell Chem Biol. 2024 Mar 21;31(3):565-576.e4. doi: 10.1016/j.chembiol.2023.11.015. Epub 2023 Dec 19.
Mass spectrometry data entry: PXD044402
2 Benchmarking Cleavable Biotin Tags for Peptide-Centric Chemoproteomics. J Proteome Res. 2022 May 6;21(5):1349-1358. doi: 10.1021/acs.jproteome.2c00174. Epub 2022 Apr 25.
Mass spectrometry data entry: PXD031019
3 DrugMap: A quantitative pan-cancer analysis of cysteine ligandability. Cell. 2024 May 9;187(10):2536-2556.e30. doi: 10.1016/j.cell.2024.03.027. Epub 2024 Apr 22.
Mass spectrometry data entry: PXD047840