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Identification
HMDB Protein ID HMDBP12428
Secondary Accession Numbers None
Name Immunoglobulin heavy constant mu
Synonyms
  1. Ig mu chain C region
  2. Ig mu chain C region BOT
  3. Ig mu chain C region GAL
  4. Ig mu chain C region OU
Gene Name IGHM
Protein Type Unknown
Biological Properties
General Function Not Available
Specific 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 (PubMed:22158414, PubMed:20176268). 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 (PubMed:17576170, PubMed:20176268). IgM antibodies play an important role in primary defense mechanisms. They have been shown to be involved in early recognition of external invaders like bacteria and viruses, cellular waste and modified self, as well as in recognition and elimination of precancerous and cancerous lesions. The membrane-bound form is found in the majority of normal B-cells alongside with IgD. Membrane-bound IgM induces the phosphorylation of CD79A and CD79B by the Src family of protein tyrosine kinases. It may cause death of cells by apoptosis. It is also found in soluble form, which represents about 30% of the total serum immunoglobulins where it is found almost exclusively as a homopentamer. After the antigen binds to the B-cell receptor, the secreted form is secreted in large amounts (PubMed:3137579, PubMed:16895553).
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
B cell receptor signaling pathway
defense response to bacterium
leukocyte migration
complement activation, classical pathway
phagocytosis, engulfment
phagocytosis, recognition
positive regulation of B cell activation
innate immune response
adaptive immune response
defense response to Gram-negative bacterium
antibacterial humoral response
Cellular Component
cell surface
extracellular vesicular exosome
plasma membrane
blood microparticle
hexameric IgM immunoglobulin complex
immunoglobulin complex, circulating
pentameric IgM immunoglobulin complex
extracellular space
external side of plasma membrane
integral to membrane
Molecular Function
antigen binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues Not Available
Molecular Weight 49439.37
Theoretical pI Not Available
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P01871
UniProtKB/Swiss-Prot Entry Name IGHM_HUMAN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
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  3. Bunkenborg J, Pilch BJ, Podtelejnikov AV, Wisniewski JR: Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics. 2004 Feb;4(2):454-65. [PubMed:14760718 ]
  4. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [PubMed:21269460 ]
  5. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [PubMed:24275569 ]
  6. Putnam FW, Florent G, Paul C, Shinoda T, Shimizu A: Complete amino acid sequence of the Mu heavy chain of a human IgM immunoglobulin. Science. 1973 Oct 19;182(4109):287-91. doi: 10.1126/science.182.4109.287. [PubMed:4742735 ]
  7. Geisberger R, Lamers M, Achatz G: The riddle of the dual expression of IgM and IgD. Immunology. 2006 Aug;118(4):429-37. doi: 10.1111/j.1365-2567.2006.02386.x. [PubMed:16895553 ]
  8. Teng G, Papavasiliou FN: Immunoglobulin somatic hypermutation. Annu Rev Genet. 2007;41:107-20. doi: 10.1146/annurev.genet.41.110306.130340. [PubMed:17576170 ]
  9. Schroeder HW Jr, Cavacini L: Structure and function of immunoglobulins. J Allergy Clin Immunol. 2010 Feb;125(2 Suppl 2):S41-52. doi: 10.1016/j.jaci.2009.09.046. [PubMed:20176268 ]
  10. McHeyzer-Williams M, Okitsu S, Wang N, McHeyzer-Williams L: Molecular programming of B cell memory. Nat Rev Immunol. 2011 Dec 9;12(1):24-34. doi: 10.1038/nri3128. [PubMed:22158414 ]
  11. Watanabe S, Barnikol HU, Horn J, Bertram J, Hilschmann N: [The primary structure of a monoclonal IgM-immunoglobulin (macroglobulin Gal.), II: the amino acid sequence of the H-chain (mu-type), subgroup H III. Architecture of the complete IgM-molecule (author's transl)]. Hoppe Seylers Z Physiol Chem. 1973 Oct-Nov;354(10-11):1505-9. [PubMed:4803843 ]
  12. Mihaesco E, Barnikol-Watanabe S, Barnikol HU, Mihaesco C, Hilschmann N: The primary structure of the constant part of mu-chain-disease protein BOT. Eur J Biochem. 1980 Oct;111(1):275-86. doi: 10.1111/j.1432-1033.1980.tb06103.x. [PubMed:6777162 ]
  13. Dorai H, Gillies SD: The complete nucleotide sequence of a human immunoglobulin genomic C mu gene. Nucleic Acids Res. 1989 Aug 11;17(15):6412. doi: 10.1093/nar/17.15.6412. [PubMed:2505237 ]
  14. Friedlander RM, Nussenzweig MC, Leder P: Complete nucleotide sequence of the membrane form of the human IgM heavy chain. Nucleic Acids Res. 1990 Jul 25;18(14):4278. doi: 10.1093/nar/18.14.4278. [PubMed:2115996 ]
  15. Barnikol-Watanabe S, Mihaesco E, Mihaesco C, Barnikol HU, Hilschmann N: The primary structure of mu-chain-disease protein BOT. Peculiar amino-acid sequence of the N-terminal 42 positions. Hoppe Seylers Z Physiol Chem. 1984 Jan;365(1):105-18. doi: 10.1515/bchm2.1984.365.1.105. [PubMed:6425189 ]
  16. Dolby TW, Devuono J, Croce CM: Cloning and partial nucleotide sequence of human immunoglobulin mu chain cDNA from B cells and mouse-human hybridomas. Proc Natl Acad Sci U S A. 1980 Oct;77(10):6027-31. doi: 10.1073/pnas.77.10.6027. [PubMed:6777778 ]
  17. Rabbitts TH, Forster A, Milstein CP: Human immunoglobulin heavy chain genes: evolutionary comparisons of C mu, C delta and C gamma genes and associated switch sequences. Nucleic Acids Res. 1981 Sep 25;9(18):4509-24. doi: 10.1093/nar/9.18.4509. [PubMed:6795593 ]
  18. Tisch R, Roifman CM, Hozumi N: Functional differences between immunoglobulins M and D expressed on the surface of an immature B-cell line. Proc Natl Acad Sci U S A. 1988 Sep;85(18):6914-8. doi: 10.1073/pnas.85.18.6914. [PubMed:3137579 ]
  19. Jia W, Lu Z, Fu Y, Wang HP, Wang LH, Chi H, Yuan ZF, Zheng ZB, Song LN, Han HH, Liang YM, Wang JL, Cai Y, Zhang YK, Deng YL, Ying WT, He SM, Qian XH: A strategy for precise and large scale identification of core fucosylated glycoproteins. Mol Cell Proteomics. 2009 May;8(5):913-23. doi: 10.1074/mcp.M800504-MCP200. Epub 2009 Jan 12. [PubMed:19139490 ]
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  21. Graille M, Stura EA, Housden NG, Beckingham JA, Bottomley SP, Beale D, Taussig MJ, Sutton BJ, Gore MG, Charbonnier JB: Complex between Peptostreptococcus magnus protein L and a human antibody reveals structural convergence in the interaction modes of Fab binding proteins. Structure. 2001 Aug;9(8):679-87. doi: 10.1016/s0969-2126(01)00630-x. [PubMed:11587642 ]
  22. Ramsland PA, Terzyan SS, Cloud G, Bourne CR, Farrugia W, Tribbick G, Geysen HM, Moomaw CR, Slaughter CA, Edmundson AB: Crystal structure of a glycosylated Fab from an IgM cryoglobulin with properties of a natural proteolytic antibody. Biochem J. 2006 May 1;395(3):473-81. doi: 10.1042/BJ20051739. [PubMed:16422668 ]