SIL1

From Wikipedia, the free encyclopedia

SIL1 homolog, endoplasmic reticulum chaperone (S. cerevisiae)

Identifiers

External IDs

OMIM: 608005 MGI: 1932040 HomoloGene: 32544

Gene ontology
Molecular Function:	• binding • unfolded protein binding
Cellular Component:	• endoplasmic reticulum
Biological Process:	• protein folding • protein targeting

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001037633 (mRNA)
NP_001032722 (protein)

NM_030749 (mRNA)
NP_109674 (protein)

Location

Chr 5: 138.31 - 138.56 Mb

Chr 18: 35.39 - 35.62 Mb

Pubmed search

[1]

[2]

SIL1 homolog, endoplasmic reticulum chaperone (S. cerevisiae), also known as SIL1, is a human gene.^[1]

This gene encodes a resident endoplasmic reticulum (ER), N-linked glycoprotein with an N-terminal ER targeting sequence, 2 putative N-glycosylation sites, and a C-terminal ER retention signal. This protein functions as a nucleotide exchange factor for another unfolded protein response protein. Mutations in this gene have been associated with Marinesco-Sjogren syndrome. Alternate transcriptional splice variants have been characterized.^[1]

[edit] References

^ ^a ^b Entrez Gene: SIL1 SIL1 homolog, endoplasmic reticulum chaperone (S. cerevisiae).

[edit] Further reading

Keats B, Ott J, Conneally M (1989). "Report of the committee on linkage and gene order.". Cytogenet. Cell Genet. 51 (1-4): 459-502. PMID 2791656.
Tyson JR, Stirling CJ (2001). "LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum.". EMBO J. 19 (23): 6440-52. doi:10.1093/emboj/19.23.6440. PMID 11101517.
Chung KT, Shen Y, Hendershot LM (2003). "BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP.". J. Biol. Chem. 277 (49): 47557-63. doi:10.1074/jbc.M208377200. PMID 12356756.
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.
Lagier-Tourenne C, Tranebaerg L, Chaigne D, et al. (2004). "Homozygosity mapping of Marinesco-Sjögren syndrome to 5q31.". Eur. J. Hum. Genet. 11 (10): 770-8. doi:10.1038/sj.ejhg.5201068. PMID 14512967.
Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway.". Genome Res. 14 (7): 1324-32. doi:10.1101/gr.2334104. PMID 15231748.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173-8. doi:10.1038/nature04209. PMID 16189514.
Senderek J, Krieger M, Stendel C, et al. (2006). "Mutations in SIL1 cause Marinesco-Sjögren syndrome, a cerebellar ataxia with cataract and myopathy.". Nat. Genet. 37 (12): 1312-4. doi:10.1038/ng1678. PMID 16282977.
Anttonen AK, Mahjneh I, Hämäläinen RH, et al. (2006). "The gene disrupted in Marinesco-Sjögren syndrome encodes SIL1, an HSPA5 cochaperone.". Nat. Genet. 37 (12): 1309-11. doi:10.1038/ng1677. PMID 16282978.
Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries.". DNA Res. 12 (2): 117-26. doi:10.1093/dnares/12.2.117. PMID 16303743.
Karim MA, Parsian AJ, Cleves MA, et al. (2006). "A novel mutation in BAP/SIL1 gene causes Marinesco-Sjögren syndrome in an extended pedigree.". Clin. Genet. 70 (5): 420-3. doi:10.1111/j.1399-0004.2006.00695.x. PMID 17026626.