Endophilin-B2 (SH3GLB2)
The protein contains 395 amino acids for an estimated molecular weight of 43974 Da.
No function (updated: Feb. 4, 2015)
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.
- 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.
- 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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- 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.
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| Variant | Description |
|---|---|
| dbSNP:rs17455482 | |
| dbSNP:rs17455475 |
Biological Process
The reference OMIM entry for this protein is 609288
Sh3 domain, grb2-like, endophilin b2; sh3glb2
Endophilin b2
Kiaa1848
CLONING
Using SH3GLB1 (609287) as bait in a yeast 2-hybrid screen of skeletal muscle and adipocyte cDNA libraries, Pierrat et al. (2001) cloned SH3GLB2. The deduced 395-amino acid protein contains an N-terminal domain, a central coiled-coil region, and a C-terminal SH3 domain. SH3GLB2 shares 65% amino acid identity with SH3GLB1, but it has a 23-amino acid extension following the coiled-coil region that is not present in SH3GLB1. RT-PCR and EST database analysis indicated that SH3GLB2 is expressed in many tissues, including skeletal muscle, adipocytes, brain, lung, colon, and mammary gland. SH3GLB2 was expressed in the cytoplasm of transfected HeLa cells and was excluded from nuclei. By sequencing clones obtained from a size-fractionated adult brain cDNA library, Nagase et al. (2001) cloned SH3GLB2, which they designated KIAA1848. The deduced protein contains 378 amino acids. RT-PCR ELISA detected highest expression in adult and fetal brain, adult lung, ovary, and spinal cord, and in all specific brain regions examined. Intermediate expression was detected in all other tissues examined.GENE FUNCTION
By Western blot analysis, Pierrat et al. (2001) confirmed that SH3GLB2 could form homodimers and heterodimers with SH3GLB1 in vitro. Mutation analysis indicated that the core coiled-coil region was required for the formation of SH3GLB homodimers and heterodimers, but the SH3 domain was not.MAPPING
By analysis of a human-rodent hybrid panel, Nagase et al. (2001) mapped the SH3GLB2 gene to chromosome 9. ... More on the omim web site
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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 609288 was added.