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Reference

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A reference for what the literature reports. Not medical advice.

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Proteins/UNIPROT:Q9HBH1

PDF

Protein·UNIPROT:Q9HBH1Peptide deformylase, mitochondrial

Open in the graph

Removes the formyl group from the N-terminal Met of newly synthesized proteins..

Function from UniProtKB (Q9HBH1), read 2026-09-23. CC BY 4.0.

Curated compounds routed: 0

What the reference databases state

Inferred

Inferred — not reported by a source. Evidence key

Statements

5 statements

5 statements · 4 reference databases · Subject: PDF · Sources: gene ontology, Hetionet, Rhea, UniProt

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PDF covaries with GOLT1AProteinHetionet hetionet:covaries:127845-64146Inferred only
H2BC14 covaries with PDFProteinHetionet hetionet:covaries:64146-8342Inferred only
PDF regulates positive regulation of cell population proliferationBiological processgene ontology Q9HBH1|GO:0008284Inferred only
PDF requires the cofactor Co(2+)CompoundUniProt Q9HBH1Inferred only
formate is a substrate of PDFCompoundRhea RHEA:24420Inferred only

Reactions

2 reactions

MAM01838c+waterformic acid+proton+MAM02472c
Catalysed by PDF
Reaction pageLeft to rightBalance undeterminableEC 3.5.1.88cytosol
Human-GEM MAR09551CC BY 4.0Reference data
N-terminal N-formyl-L-methionyl-[peptide]+waterN-terminal L-methionyl-[peptide]+formate
Catalysed by PDF
Reaction pageDirection not assertedBalance undeterminable
Rhea RHEA:24420

Other names

2 names

Resolves to: PDF

Also called: PDF1APolypeptide deformylase

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CC BY 4.0

Reference data