Protein transport protein Sec24B (SEC24B)
The protein contains 1268 amino acids for an estimated molecular weight of 137418 Da.
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex (PubMed:17499046, PubMed:20427317, PubMed:18843296). Plays a central role in cargo selection within the COPII complex and together with SEC24A may have a different specificity compared to SEC24C and SEC24D. May package preferentially cargos with cytoplasmic DxE or LxxLE motifs and may also recognize conformational epitopes (PubMed:17499046, PubMed:18843296). (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
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.
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| Variant | Description |
|---|---|
| dbSNP:rs35705351 |
Biological Process
Antigen processing and presentation of exogenous peptide antigen via MHC class II
Antigen processing and presentation of peptide antigen via MHC class I
Aorta morphogenesis
Auditory receptor cell stereocilium organization
Cochlear nucleus development
COPII vesicle coating
COPII-coated vesicle cargo loading
Coronary artery morphogenesis
Endoplasmic reticulum to Golgi vesicle-mediated transport
Intracellular protein transport
Lung lobe morphogenesis
Neural tube closure
Outflow tract morphogenesis
Pulmonary artery morphogenesis
Regulation of cargo loading into COPII-coated vesicle
Regulation of establishment of planar polarity involved in neural tube closure
The reference OMIM entry for this protein is 607184
Sec24-related gene family, member b; sec24b
DESCRIPTION
In yeast, the Sec23-Sec24 complex is a component of coat protein II (COPII; see 601924)-coated vesicles that mediate protein transport from the endoplasmic reticulum. SEC24B is 1 of several mammalian proteins that show structural and functional homology to yeast Sec24.CLONING
By searching an EST database for homologs of yeast Sec24 proteins and screening a size-selected B-lymphocyte cDNA library, Pagano et al. (1999) isolated a full-length cDNA encoding SEC24B. The deduced 1,268-amino acid protein has a calculated molecular mass of about 137 kD. RNase protection assays demonstrated that SEC24A (607183), SEC24B, and SEC24C (607185) were expressed simultaneously in several cell lines, including lines originating from fibroblasts, hepatocytes, and lymphocytes. The major difference in expression was a constant 2- to 3-fold lower level of expression of SEC24B compared with SEC24A and SEC24C. Immunofluorescence localization indicated that endogenous SEC24B is expressed in various human cell lines throughout the cytoplasm, with more intense perinuclear staining. Tang et al. (1999) determined that SEC24A and SEC24B share about 56% sequence identity, while SEC24C and SEC24D (607186) share about 52% identity. However, the identity shared between these 2 pairs is only about 20%.GENE FUNCTION
By gel filtration analysis, Pagano et al. (1999) determined that SEC24B and SEC24C elute in the same fractions, corresponding to a molecular mass of 400 kD. Coimmunoprecipitation experiments showed no evidence for direct interaction between SEC24B and SEC24C, although both coimmunoprecipitated with SEC23A. Yeast 2-hybrid assays confirmed the interaction between SEC24C and SEC23A. The authors determined that the interacting domain of SEC24C includes the conserved SEC24 family domain, and the interacting domain SEC23A includes the N terminus up to amino acid 543.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SEC24A gene to chromosome 4 (TMAP RH33784). ... More on the omim web site
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 607184 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).