Sorting and assembly machinery component 50 homolog (SAMM50)
The protein contains 469 amino acids for an estimated molecular weight of 51976 Da.
Plays a crucial role in the maintenance of the structure of mitochondrial cristae and the proper assembly of the mitochondrial respiratory chain complexes (PubMed:22252321, PubMed:25781180). Required for the assembly of TOMM40 into the TOM complex (PubMed:15644312). (updated: Oct. 25, 2017)
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.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
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:rs3761472 | |
| dbSNP:rs8418 |
Biological Process
Cellular protein metabolic process
Cellular protein-containing complex assembly
Cristae formation
Inner mitochondrial membrane organization
Mitochondrial respiratory chain complex assembly
Protein insertion into mitochondrial outer membrane
Protein targeting to mitochondrion
Protein-containing complex assembly
Cellular Component
Extracellular exosome
Integral component of membrane
MIB complex
Mitochondrial inner membrane
Mitochondrial outer membrane
Mitochondrion
SAM complex
Molecular Function
The reference OMIM entry for this protein is 612058
Sorting and assembly machinery component 50, s. cerevisiae, homolog of; samm50
Sam50
DESCRIPTION
SAMM50 is a component of the sorting and assembly machinery (SAM) complex of the outer mitochondrial membrane. The SAM complex has a role in integrating beta-barrel proteins into the outer mitochondrial membrane (Humphries et al., 2005).GENE FUNCTION
Humphries et al. (2005) found that continued expression of fluorescence-tagged human SAM50 in COS-7 cells impaired mitochondrial morphology and shortened cellular life span, indicating that the fusion protein was toxic. SAM50 was associated with a 200-kD protein complex that was distinct from the 380-kD translocase of the outer mitochondrial membrane (TOM) complex. RNA interference against SAM50 in human embryonic kidney cells reduced assembly of TOM40 (TOMM40; 608061), an essential component of the TOM complex involved in translocation and sorting of proteins into mitochondria. Using a monoclonal antibody directed against the mitochondrial inner membrane protein mitofilin (IMMT; 600378), followed by SDS-PAGE and mass spectrometry, Xie et al. (2007) identified a protein complex in human heart mitochondria that, in addition to mitofilin, included SAMM50, metaxin-1 (MTX1; 600605), metaxin-2 (MTX2; 608555), CHCHD3 (613748), CHCHD6 (615634), and DNAJC11 (614827).MAPPING
Hartz (2014) mapped the SAMM50 gene to chromosome 22q13.31 based on an alignment of the SAMM50 sequence (GenBank GENBANK AF151809) with the genomic sequence (GRCh37). ... 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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 612058 was added.