General Information of Target

Target ID LDTP01909
Target Name Immunoglobulin heavy constant mu (IGHM)
Gene Name IGHM
Synonyms
Immunoglobulin heavy constant mu; Ig mu chain C region; Ig mu chain C region BOT; Ig mu chain C region GAL; Ig mu chain C region OU
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
GSASAPTLFPLVSCENSPSDTSSVAVGCLAQDFLPDSITFSWKYKNNSDISSTRGFPSVL
RGGKYAATSQVLLPSKDVMQGTDEHVVCKVQHPNGNKEKNVPLPVIAELPPKVSVFVPPR
DGFFGNPRKSKLICQATGFSPRQIQVSWLREGKQVGSGVTTDQVQAEAKESGPTTYKVTS
TLTIKESDWLGQSMFTCRVDHRGLTFQQNASSMCVPDQDTAIRVFAIPPSFASIFLTKST
KLTCLVTDLTTYDSVTISWTRQNGEAVKTHTNISESHPNATFSAVGEASICEDDWNSGER
FTCTVTHTDLPSPLKQTISRPKGVALHRPDVYLLPPAREQLNLRESATITCLVTGFSPAD
VFVQWMQRGQPLSPEKYVTSAPMPEPQAPGRYFAHSILTVSEEEWNTGETYTCVVAHEAL
PNRVTERTVDKSTEGEVSADEEGFENLWATASTFIVLFLLSLFYSTTVTLFKVK
Target Bioclass
Immunoglobulin
Subcellular location
Secreted; Cell membrane
Function
Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.; [Isoform 1]: Constant region of secreted IgM (sIgM), also known as the Fc region of IgM antibody. Able to multimerize, forms high order polymers, mainly pentamers and occasionally hexamers, providing for multivalency and high avidity recognition of antigens. Natural sIgM are polyreactive and recognize conserved self- and pathogen-derived structures, whereas immune sIgM are secreted only upon exposure to pathogens and are antigen-specific. Both natural and immune sIgM are required for an efficient humoral immune response to infection. Mediates sIgM effector functions mostly via Fc receptors and the complement system. On lymphoid cells binds high-affinity Fc receptor FCMR and promotes induction of an efficient neutralizing IgG response while maintaining tolerance to self-antigens. Recruits C1q complement component to initiate the classical complement pathway, facilitating the recognition and neutralization of pathogens by the host. Together with C1q and mannose-binding lectin promotes the phagocytosis of apoptotic cells by macrophages, ensuring the clearance of potential autoimmune epitopes from tissues. Involved in mucosal immunity. It is transported by transcytosis across mucosal epithelium by PIGR and secreted on the apical side in complex with PIGR secretory component to scan mucosal lining for pathogens. IgM-antigen complexes undergo FCMR-mediated retrotranscytosis across mucosal M cells toward antigen-presenting cells in mucosal lymphoid tissues.; [Isoform 2]: Constant region of membrane-bound IgM, part of the B cell receptor complex (BCR). IgM BCR provides constitutive tonic signaling for B cell survival. Mediates pre-BCR signaling that regulates B cell selection and rearrangement of Ig genes via allelic exclusion.
Uniprot ID
P01871
Ensemble ID
ENST00000390559.6
HGNC ID
HGNC:5541

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 4 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
STPyne
 Probe Info 
K131(12.55)  LDD2218  [1]
DBIA
 Probe Info 
C88(2.44); C134(3.09)  LDD3339  [2]
IA-alkyne
 Probe Info 
6.79  LDD0433  [3]
NAIA_5
 Probe Info 
C244(0.00); 0.00  LDD2223  [4]

Competitor(s) Related to This Target

Competitor ID Name Cell line Binding Site(Ratio) Interaction ID Ref
 LDCM0625  F8 Ramos C88(1.09); C134(0.76); C214(1.36)  LDD2187  [5]
 LDCM0572  Fragment10 Ramos C88(1.22); C134(1.41); C214(1.07)  LDD2189  [5]
 LDCM0573  Fragment11 Ramos C88(0.41); C134(6.81)  LDD2190  [5]
 LDCM0574  Fragment12 Ramos C88(0.94); C134(1.05); C214(0.94)  LDD2191  [5]
 LDCM0575  Fragment13 Ramos C88(1.26); C134(1.02)  LDD2192  [5]
 LDCM0576  Fragment14 Ramos C88(1.15); C134(1.41); C214(0.66)  LDD2193  [5]
 LDCM0579  Fragment20 Ramos C88(1.18); C134(1.65); C214(0.86)  LDD2194  [5]
 LDCM0580  Fragment21 Ramos C88(0.93); C134(0.99); C214(1.48)  LDD2195  [5]
 LDCM0582  Fragment23 Ramos C88(0.85); C134(0.87); C214(1.20)  LDD2196  [5]
 LDCM0578  Fragment27 Ramos C88(1.02); C134(0.94)  LDD2197  [5]
 LDCM0586  Fragment28 Ramos C88(1.23); C134(0.87)  LDD2198  [5]
 LDCM0588  Fragment30 Ramos C88(1.19); C134(0.92); C214(1.57)  LDD2199  [5]
 LDCM0589  Fragment31 Ramos C88(1.12); C134(1.09); C214(0.96)  LDD2200  [5]
 LDCM0590  Fragment32 Ramos C88(2.19); C134(1.22)  LDD2201  [5]
 LDCM0468  Fragment33 Ramos C88(1.07); C134(0.96); C214(1.60)  LDD2202  [5]
 LDCM0596  Fragment38 Ramos C88(0.87); C134(0.89)  LDD2203  [5]
 LDCM0566  Fragment4 Ramos C88(1.06); C134(1.00); C214(0.65)  LDD2184  [5]
 LDCM0610  Fragment52 Ramos C88(1.16); C134(1.23)  LDD2204  [5]
 LDCM0614  Fragment56 Ramos C88(1.15); C134(1.20)  LDD2205  [5]
 LDCM0569  Fragment7 Ramos C88(1.23); C134(1.13); C214(1.04)  LDD2186  [5]
 LDCM0571  Fragment9 Ramos C88(0.82)  LDD2188  [5]
 LDCM0022  KB02 Ramos C88(1.47); C214(0.88)  LDD2182  [5]
 LDCM0023  KB03 Ramos C88(0.98); C134(1.38); C214(0.85)  LDD2183  [5]
 LDCM0024  KB05 NALM-6 C88(2.44); C134(3.09)  LDD3339  [2]
 LDCM0170  Structure8 Ramos 6.79  LDD0433  [3]

The Interaction Atlas With This Target

The Drug(s) Related To This Target

Approved
Click To Hide/Show 2 Drug(s) Interacting with This Target
Drug Name Drug Type External ID
Zinc . DB01593
Zinc Acetate . DB14487

References

1 Global profiling of lysine reactivity and ligandability in the human proteome. Nat Chem. 2017 Dec;9(12):1181-1190. doi: 10.1038/nchem.2826. Epub 2017 Jul 31.
2 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
3 2-Sulfonylpyridines as Tunable, Cysteine-Reactive Electrophiles. J Am Chem Soc. 2020 May 13;142(19):8972-8979. doi: 10.1021/jacs.0c02721. Epub 2020 Apr 29.
4 N-Acryloylindole-alkyne (NAIA) enables imaging and profiling new ligandable cysteines and oxidized thiols by chemoproteomics. Nat Commun. 2023 Jun 15;14(1):3564. doi: 10.1038/s41467-023-39268-w.
Mass spectrometry data entry: PXD041264
5 Site-specific quantitative cysteine profiling with data-independent acquisition-based mass spectrometry. Methods Enzymol. 2023;679:295-322. doi: 10.1016/bs.mie.2022.07.037. Epub 2022 Sep 7.
Mass spectrometry data entry: PXD027578