Immunoglobulin heavy constant gamma 1 (IGHG1)
The protein contains 330 amino acids for an estimated molecular weight of 36106 Da.
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). (updated: Jan. 31, 2018)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in UniProt.
(right-click above to access to more options from the contextual menu)
| Variant | Description |
|---|---|
| IMGT allele IGHG1*03 | |
| IMGT allele IGHG1*03 | |
| IMGT allele IGHG1*03 |
No binding partner found
Biological Process
B cell receptor signaling pathway
Complement activation
Complement activation, classical pathway
Cytokine-mediated signaling pathway
Defense response to bacterium
Fc-gamma receptor signaling pathway involved in phagocytosis
Innate immune response
Negative regulation of inflammatory response to antigenic stimulus
Opsonization
Peptide cross-linking
Phagocytosis, engulfment
Phagocytosis, recognition
Positive regulation of B cell activation
Regulation of complement activation
Cellular Component
Blood microparticle
External side of plasma membrane
Extracellular exosome
Extracellular region
Extracellular space
Immunoglobulin complex, circulating
Molecular Function
Antigen binding
Immunoglobulin receptor binding
Serine-type endopeptidase activity
The reference OMIM entry for this protein is 147100
Igg heavy chain locus; ighg1
Immunoglobulin gm1 ighg1/ccnd1 fusion gene, included
Ighg1/lhx4 fusion gene, included
At least 2 separate autosomal loci determining serologic type of gamma globulin were identified in the 1950s and 1960s. One was referred to as the Gm locus and the other as the Inv locus. The genetics of the gamma globulins has been as revealing of general principles as has been that of the hemoglobins. The Gm system is associated with the heavy chains of the IgG molecules encoded, as was later found, by chromosome 14; the Inv system is associated with the kappa light chains (147200). (See Anonymous, 1966 for recommended notation for Gm and Inv types.) Hood and Ein (1968) presented evidence that antibody light chains are an exception to the rule of 'one gene, one polypeptide chain.' Two separate loci (a specific region locus and a common region locus) appeared to code for a single, continuous polypeptide chain. Three closely linked loci (IgG1, IgG2 and IgG3) were thought to be responsible for the Gm specificities. Van Loghem et al. (1970) presented evidence on the linkage relationship of immunoglobulin markers (gamma 1, 2, 3, Am). That the gamma-G3 and gamma-G1 loci are closely linked was indicated by the findings in a Lepore-type myeloma protein (Kunkel et al., 1969). A fourth IgG locus (gamma-G4) was identifiable in the cluster. A family possibly supporting the sequence (beginning at the N terminus) of alpha-2, gamma-4, gamma-2, gamma-3, and gamma-1 was presented by Lefranc et al. (1977). Gedde-Dahl et al. (1972, 1975) presented data on the linkage of Gm-Pi (AAT; 107400). They considered heterogeneity of recombination fraction among males of different Pi type to be very likely. The major difference seemed to be between the Pi(Z) and other alleles. Possible explanations included a chromosomal deletion, inversion or locus regulation recombination in linkage disequilibrium with the Pi locus. Bender et al. (1979) excluded Gm, Pi and C3 from the segment 6q25-qter and Gm and Pi from 6p. See 182870 for evidence of linkage to hereditary spherocytosis. Croce et al. (1979) studied somatic cell hybrids between mouse myeloma cells and either human peripheral lymphocytes or human lymphoblastoid or myeloma cells. They observed that the presence or absence of chromosome 14 correlated with formation of human mu, gamma, and alpha heavy chains. Smith et al. (1981) confirmed assignment of the immunoglobulin heavy chain family of genes to chromosome 14. Green (1979) reviewed the genetics of the immunoglobulins in mice and proposed a nomenclature. From study of somatic cell hybrids, Hengartner et al. (1978) concluded that the loci for immunoglobulin heavy chains are on chromosome 12 in the mouse. Meo et al. (1980) reported the conclusive mapping of the Igh-1 and the linked prealbumin locus to mouse chromosome 12. In the mouse, the heavy chain variable and constant regions, Igh-V and Igh-C (Green, 1979), occupy a chromosomal segment at least 7-11 units long (Pisetsky and Sachs, 1977), and are linked, probably at the Igh-C end, with the serum prealbumin locus at a distance of about 11 units (Taylor et al., 1975). Steinberg et al. (1975) described polymorphism of both Gm and Inv in baboons of Kenya. In man and in mouse, fine mapping of the immunoglobulin gene progressed faster than chromosomal and regional assignment. The immunoglobulin loci were thought to be located in three different chromosomal regions carrying heavy chain, kappa light chain and lambda light chain loci. Each region was thought to contain one or more loci specifying the constant region an ... More on the omim web site
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for IGHG1
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 147100 was added.