Reviewed,
UniProtKB/Swiss-Prot Q9HBH1 (DEFM_HUMAN)
Last modified
November 3, 2009.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Peptide deformylase, mitochondrial EC=3.5.1.88 Alternative name(s): Polypeptide deformylase | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 243 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Removes the formyl group from the N-terminal Met of newly synthesized proteins By similarity. |
| Catalytic activity | Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. |
| Cofactor | Binds 1 Fe2+ ion By similarity. |
| Subcellular location | Mitochondrion Potential. |
| Tissue specificity | Ubiquitous. |
| Sequence similarities | Belongs to the polypeptide deformylase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Mitochondrion |
| Coding sequence diversity | Polymorphism |
| Domain | Transit peptide |
| Ligand | Iron Metal-binding |
| Molecular function | Hydrolase |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | N-terminal protein amino acid modification Inferred from direct assay. Source: HGNC peptidyl-methionine modificationInferred from direct assay. Source: HGNC positive regulation of cell proliferationInferred from mutant phenotype. Source: HGNC translationInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrion Inferred from direct assay. Source: HGNC |
| Molecular function | iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW peptide deformylase activityInferred from direct assay. Source: HGNC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 39 | 39 | Mitochondrion Probable | ||||||||||||||||||||||||||||||||||
| Chain | 40 – 243 | 204 | Peptide deformylase, mitochondrial | PRO_0000006729 | |||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||
| Active site | 215 | 1 | By similarity | ||||||||||||||||||||||||||||||||||
| Metal binding | 172 | 1 | Iron By similarity | ||||||||||||||||||||||||||||||||||
| Metal binding | 214 | 1 | Iron By similarity | ||||||||||||||||||||||||||||||||||
| Metal binding | 218 | 1 | Iron By similarity | ||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||
| Natural variant | 11 | 1 | W → R: dbSNP rs8057004. Ref.3 | VAR_060122 | |||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||
| Helix | 73 – 75 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 84 – 86 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 91 – 105 | 15 | |||||||||||||||||||||||||||||||||||
| Helix | 113 – 115 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 120 – 127 | 8 | |||||||||||||||||||||||||||||||||||
| Helix | 129 – 133 | 5 | |||||||||||||||||||||||||||||||||||
| Helix | 137 – 143 | 7 | |||||||||||||||||||||||||||||||||||
| Beta strand | 148 – 155 | 8 | |||||||||||||||||||||||||||||||||||
| Beta strand | 157 – 170 | 14 | |||||||||||||||||||||||||||||||||||
| Beta strand | 179 – 191 | 13 | |||||||||||||||||||||||||||||||||||
| Beta strand | 202 – 204 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 208 – 219 | 12 | |||||||||||||||||||||||||||||||||||
| Helix | 224 – 226 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 230 – 232 | 3 | |||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms." Giglione C., Serero A., Pierre M., Boisson B., Meinnel T. EMBO J. 19:5916-5929(2000) [PubMed: 11060042] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "A human homolog of bacterial peptide deformylases." Lonetto M.A., Zhu Y., Li X., Southan C. Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-11. Tissue: Placenta. |
| [4] | "An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathway." Serero A., Giglione C., Sardini A., Martinez-Sanz J., Meinnel T. J. Biol. Chem. 278:52953-52963(2003) [PubMed: 14532271] [Abstract] Cited for: MITOCHONDRIAL TRANSIT PEPTIDE. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AF239156 mRNA. Translation: AAG33968.1. AF322879 mRNA. Translation: AAK15624.1. BC019912 mRNA. Translation: AAH19912.1. | |||||||||||||||||||
| IPI | IPI00007060. | ||||||||||||||||||
| RefSeq | NP_071736.1. | ||||||||||||||||||
| UniGene | Hs.130849 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| STRING | Q9HBH1. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PeptideAtlas | Q9HBH1. | ||||||||||||||||||
| PRIDE | Q9HBH1. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENST00000288022; ENSP00000288022; ENSG00000157312; Homo sapiens. [Genome view] | ||||||||||||||||||
| GeneID | 64146. | ||||||||||||||||||
| KEGG | hsa:64146. | ||||||||||||||||||
| NMPDR | fig|9606.3.peg.12472. | ||||||||||||||||||
| UCSC | uc002ewx.1. human. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 64146. | ||||||||||||||||||
| GeneCards | GC16M067920. | ||||||||||||||||||
| HGNC | HGNC:30012. PDF. | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOVERGEN | Q9HBH1. | ||||||||||||||||||
| OMA | LYPSRIT. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BRENDA | 3.5.1.88. 247. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | Q9HBH1. | ||||||||||||||||||
| Bgee | Q9HBH1. | ||||||||||||||||||
| Genevestigator | Q9HBH1. | ||||||||||||||||||
| GermOnline | ENSG00000157312. Homo sapiens. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR000181. Fmet_deformylase. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:3.90.45.10. Fmet_deformylase. 1 hit. | ||||||||||||||||||
| PANTHER | PTHR10458. Fmet_deformylase. 1 hit. | ||||||||||||||||||
| Pfam | PF01327. Pep_deformylase. 1 hit. [Graphical view] | ||||||||||||||||||
| PRINTS | PR01576. PDEFORMYLASE. | ||||||||||||||||||
| ProDom | PD003844. Fmet_deformylase. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other Resources | |||||||||||||||||||
| NextBio | 66046. | ||||||||||||||||||
Entry information
| Entry name | DEFM_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9HBH1 Secondary accession number(s): Q8WUN6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 16 Human chromosome 16: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


