TOM1

From Wikipedia, the free encyclopedia

Target of myb1 (chicken)

PDB rendering based on 1elk.

Available structures: 1elk, 1wrd

Identifiers

Symbol(s)

TOM1; FLJ33404

External IDs

OMIM: 604700 HomoloGene: 88453

Gene ontology
Molecular Function:	• protein binding
Cellular Component:	• intracellular • lysosome • endosome • early endosome • cytosol • membrane
Biological Process:	• intracellular protein transport • endocytosis • endosome transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

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Refseq

NM_005488 (mRNA)
NP_005479 (protein)

n/a (mRNA)
n/a (protein)

Location

Chr 22: 34.03 - 34.07 Mb

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Pubmed search

[1]

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Target of myb1 (chicken), also known as TOM1, is a human gene.^[1]

The specific function of this gene has not yet been determined, yet it may involve the translocation of growth factor receptor complexes to the lysosome for degradation. This gene is localized to 22q13.1, with HMOX1 and MCM5 distally and HMG2L1 proximally positioned.^[1]

[edit] References

^ ^a ^b Entrez Gene: TOM1 target of myb1 (chicken).

[edit] Further reading

Seroussi E, Kedra D, Kost-Alimova M, et al. (1999). "TOM1 genes map to human chromosome 22q13.1 and mouse chromosome 8C1 and encode proteins similar to the endosomal proteins HGS and STAM.". Genomics 57 (3): 380–8. doi:10.1006/geno.1998.5739. PMID 10329004.
Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22.". Nature 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
Misra S, Beach BM, Hurley JH (2000). "Structure of the VHS domain of human Tom1 (target of myb 1): insights into interactions with proteins and membranes.". Biochemistry 39 (37): 11282–90. PMID 10985773.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMID 12975309.
Yamakami M, Yoshimori T, Yokosawa H (2004). "Tom1, a VHS domain-containing protein, interacts with tollip, ubiquitin, and clathrin.". J. Biol. Chem. 278 (52): 52865–72. doi:10.1074/jbc.M306740200. PMID 14563850.
Seet LF, Liu N, Hanson BJ, Hong W (2004). "Endofin recruits TOM1 to endosomes.". J. Biol. Chem. 279 (6): 4670–9. doi:10.1074/jbc.M311228200. PMID 14613930.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Katoh Y, Shiba Y, Mitsuhashi H, et al. (2004). "Tollip and Tom1 form a complex and recruit ubiquitin-conjugated proteins onto early endosomes.". J. Biol. Chem. 279 (23): 24435–43. doi:10.1074/jbc.M400059200. PMID 15047686.
Collins JE, Wright CL, Edwards CA, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome.". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMID 15461802.
Seet LF, Hong W (2005). "Endofin recruits clathrin to early endosomes via TOM1.". J. Cell. Sci. 118 (Pt 3): 575–87. doi:10.1242/jcs.01628. PMID 15657082.
Schmid EM, Ford MG, Burtey A, et al. (2007). "Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly.". PLoS Biol. 4 (9): e262. doi:10.1371/journal.pbio.0040262. PMID 16903783.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.