Target of Myb protein 1 (TOM1)
The protein contains 492 amino acids for an estimated molecular weight of 53818 Da.
May be involved in intracellular trafficking. Probable association with membranes. (updated: March 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.
- 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.
This protein is annotated as membranous in Gene Ontology.
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| Variant | Description |
|---|---|
| dbSNP:rs11558473 | |
| dbSNP:rs34371697 |
Biological Process
Endocytosis
Endosomal transport
Intracellular protein transport
Neutrophil degranulation
Protein transport
Signal transduction
The reference OMIM entry for this protein is 604700
Target of myb1, chicken, homolog of; tom1
DESCRIPTION
TOM1 is the founding member of a family of proteins involved in endocytosis. These proteins have an N-terminal Vps27/HGS (604375)/STAM (601899) (VHS) domain, followed by a GGA (see 606004)/TOM1 (GAT) domain (Katoh et al., 2006).CLONING
The retroviral oncogene v-myb of avian myeloblastosis virus (AMV) and avian leukemia virus E26 is a mutated and truncated version of the c-myb protooncogene (see 189990), which encodes a transcription factor. In a differential display study of v-myb oncogene-transformed chicken myelomonocytic cells, Burk et al. (1997) identified the tom1 gene as a specific target of the v-myb oncogene. By assembling the sequences of a group of human TOM1 ESTs, Seroussi et al. (1999) determined a full-length TOM1 coding sequence. The deduced 492-amino acid TOM1 protein has an N-terminal domain that shares sequence similarity to the N-terminal domains of human HGS (604375), human STAM (601899), and yeast VPS27, all of which are proteins associated with vesicular trafficking at the endosome. TOM1 also has a predicted central coiled-coil domain. Human TOM1 shares 76% amino acid sequence identity with chicken tom1 and 89% identity with mouse Tom1, the cDNA of which Seroussi et al. (1999) also cloned. Northern blot analysis of human tissues detected a ubiquitously expressed 2.3-kb TOM1 transcript, with the highest expression in skeletal muscle, placenta, heart, and liver, and lower expression in brain, lung, kidney, and pancreas. In situ hybridization of a 17.5-day mouse embryo showed ubiquitous Tom1 expression, with the highest level in the intestines. In situ hybridization of a section from the mesencephalic level of adult mouse brain detected Tom1 expression throughout brain, with high levels in the thalamic area, cerebellum, hippocampal formation, and medial lemniscus. In the cerebellum, Tom1 was expressed strongly in Purkinje cells and the granular layers. By PCR of a human liver cDNA library, Katoh et al. (2006) cloned human TOM1. The deduced 492-amino acid protein has an N-terminal VHS domain, a central GAT domain, and a C-terminal domain with a clathrin (see 118955) box sequence.GENE FUNCTION
Using yeast 2-hybrid analysis with the C-terminal portion of endofin (608880) as bait against a human brain cDNA library, Seet et al. (2004) identified TOM1 as an endofin binding partner. GST pull-down and coimmunoprecipitation assays confirmed that the C-terminal region of endofin binds to the C-terminal region of TOM1. While immunofluorescence showed a cytosolic distribution of TOM1, density gradient analysis showed partially overlapping expression of TOM1 and endofin in early endosomes. Overexpression of endofin recruits TOM1 to endosomal aggregates. Katoh et al. (2006) stated that the GAT domain of human TOM1 interacts with the endosomal protein TOLLIP (606277) and that the C-terminal domain TOM1 interacts with clathrin heavy chain (CLTC; 118955). They found that the related proteins TOM1L1 (604701) and TOM1L2 (615519) also interacted with TOLLIP and clathrin. When coexpressed, TOM1 and TOM1L1 were recruited onto TOLLIP-positive endosomes. Katoh et al. (2006) concluded that, in conjunction with TOLLIP, TOM1 family proteins recruit clathrin onto endosomes and modulate endosomal function.GENE STRUCTURE
Seroussi et al. (1999) determined that the TOM1 gene contains 15 exons, with a 17.9-kb first intron.MAPPING
Seroussi et al. (1999) characterized a 190.3-kb cont ... 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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 604700 was added.
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed