YME1L1
From Wikipedia, the free encyclopedia
| YME1-like 1 (S. cerevisiae) | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | YME1L1; FTSH; MEG4; PAMP; YME1L | ||||||||||||
| External IDs | OMIM: 607472 MGI: 1351651 HomoloGene: 31996 GeneCards: YME1L1 Gene | ||||||||||||
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| RNA expression pattern | |||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 10730 | 27377 | |||||||||||
| Ensembl | ENSG00000136758 | ENSMUSG00000026775 | |||||||||||
| UniProt | Q96TA2 | Q8C597 | |||||||||||
| RefSeq (mRNA) | NM_014263.2 | NM_013771.5 | |||||||||||
| RefSeq (protein) | NP_055078.1 | NP_038799.1 | |||||||||||
| Location (UCSC) | Chr 10: 27.4 – 27.44 Mb |
Chr 2: 23.01 – 23.05 Mb |
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| PubMed search | [1] | [2] | |||||||||||
ATP-dependent metalloprotease YME1L1 is an enzyme that in humans is encoded by the YME1L1 gene.[1]
The protein encoded by this gene is the human ortholog of yeast mitochondrial AAA metalloprotease, Yme1p. It is localized in the mitochondria and can functionally complement a yme1 disruptant yeast strain. It is proposed that this gene plays a role in mitochondrial protein metabolism and could be involved in mitochondrial pathologies. Two transcript variants encoding different isoforms have been found for this gene.[1]
[edit] References
[edit] Further reading
- Coppola M, Pizzigoni A, Banfi S et al (2000). "Identification and characterization of YME1L1, a novel paraplegin-related gene". Genomics 66 (1): 48–54. doi:10.1006/geno.2000.6136. PMID 10843804.
- Shah ZH, Hakkaart GA, Arku B et al (2000). "The human homologue of the yeast mitochondrial AAA metalloprotease Yme1p complements a yeast yme1 disruptant". FEBS Lett. 478 (3): 267–70. doi:10.1016/S0014-5793(00)01859-7. PMID 10930580.
- Zhang QH, Ye M, Wu XY et al (2001). "Cloning and Functional Analysis of cDNAs with Open Reading Frames for 300 Previously Undefined Genes Expressed in CD34+ Hematopoietic Stem/Progenitor Cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=310934.
- Pellegrini L, Passer BJ, Canelles M et al (2001). "PAMP and PARL, two novel putative metalloproteases interacting with the COOH-terminus of Presenilin-1 and -2". Journal of Alzheimer's disease : JAD 3 (2): 181–190. PMID 12214059.
- 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- 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. PMC 403697. PMID 12975309. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=403697.
- 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.
- Deloukas P, Earthrowl ME, Grafham DV et al (2004). "The DNA sequence and comparative analysis of human chromosome 10". Nature 429 (6990): 375–81. doi:10.1038/nature02462. PMID 15164054.
- 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. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
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