YME1L1

YME1-like 1 ATPase

Identifiers

YME1L1 ; FTSH; MEG4; PAMP; YME1L

External IDs

OMIM: 607472 MGI: 1351651 HomoloGene: 31996 GeneCards: YME1L1 Gene

Gene ontology
Molecular function	• metalloendopeptidase activity • ATP binding • nucleoside-triphosphatase activity • metal ion binding
Cellular component	• mitochondrial inner membrane • membrane • integral component of membrane
Biological process	• misfolded or incompletely synthesized protein catabolic process • mitochondrion organization • cell proliferation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

ENSG00000136758

ENSMUSG00000026775

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 10:
27.4 – 27.44 Mb

Chr 2:
23.16 – 23.2 Mb

PubMed search

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]

References

↑ 1.0 1.1 "Entrez Gene: YME1L1 YME1-like 1 (S. cerevisiae)".

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.
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.
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.
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.