PDF (gene)

Peptide deformylase, mitochondrial is an enzyme that in humans is encoded by the PDF gene.[4][5][6]

PDF
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 3G5K, 3G5P
Identifiers
Aliases	PDF, peptide deformylase (mitochondrial), peptide deformylase, mitochondrial
External IDs	MGI: 1915273 HomoloGene: 69354 GeneCards: PDF
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16q22.1 Start 69,326,913 bp[1] End 69,330,588 bp[1]
Gene ontology Molecular function • hydrolase activity • metal ion binding • peptide deformylase activity Cellular component • mitochondrion Biological process • peptidyl-methionine modification • N-terminal protein amino acid modification • protein biosynthesis • positive regulation of cell proliferation • co-translational protein modification Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	64146	68023
Ensembl	ENSG00000258429	n/a
UniProt	Q9HBH1	n/a
RefSeq (mRNA)	NM_022341	NM_026513
RefSeq (protein)	NP_071736	n/a
Location (UCSC)	Chr 16: 69.33 – 69.33 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

See also

• Period (gene)
• Timeless (gene)

References

1. GRCh38: Ensembl release 89: ENSG00000258429 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Giglione C, Serero A, Pierre M, Boisson B, Meinnel T (Nov 2000). "Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms". EMBO J. 19 (21): 5916–29. doi:10.1093/emboj/19.21.5916. PMC 305796. PMID 11060042.
5. Lee MD, She Y, Soskis MJ, Borella CP, Gardner JR, Hayes PA, Dy BM, Heaney ML, Philips MR, Bornmann WG, Sirotnak FM, Scheinberg DA (Oct 2004). "Human mitochondrial peptide deformylase, a new anticancer target of actinonin-based antibiotics". J Clin Invest. 114 (8): 1107–16. doi:10.1172/JCI22269. PMC 522256. PMID 15489958.
6. "Entrez Gene: PDF peptide deformylase (mitochondrial)".

Further reading

• 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.
• Lee MD, Antczak C, Li Y, et al. (2004). "A new human peptide deformylase inhibitable by actinonin". Biochem. Biophys. Res. Commun. 312 (2): 309–15. doi:10.1016/j.bbrc.2003.10.123. PMID 14637138.
• Serero A, Giglione C, Sardini A, et al. (2004). "An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathway". J. Biol. Chem. 278 (52): 52953–63. doi:10.1074/jbc.M309770200. PMID 14532271.
• Nguyen KT, Hu X, Colton C, et al. (2003). "Characterization of a human peptide deformylase: implications for antibacterial drug design". Biochemistry. 42 (33): 9952–8. doi:10.1021/bi0346446. PMID 12924944.
• 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.
• Chagnon P, Michaud J, Mitchell G, et al. (2003). "A missense mutation (R565W) in cirhin (FLJ14728) in North American Indian childhood cirrhosis". Am. J. Hum. Genet. 71 (6): 1443–9. doi:10.1086/344580. PMC 378590. PMID 12417987.

External links

• Overview of all the structural information available in the PDB for UniProt: Q9HBH1 (Human Peptide deformylase, mitochondrial) at the PDBe-KB.