METAP1

Protein-coding gene in the species Homo sapiens
METAP1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2B3H, 2B3K, 2B3L, 2G6P, 2GZ5, 2NQ6, 2NQ7, 4FLI, 4FLJ, 4FLK, 4FLL, 4HXX, 4IKR, 4IKS, 4IKT, 4IKU, 4IU6, 4U1B, 4U69, 4U6C, 4U6E, 4U6J, 4U6W, 4U6Z, 4U70, 4U71, 4U73, 4U75, 4U76

Identifiers
AliasesMETAP1, MAP1A, MetAP1A, methionyl aminopeptidase 1
External IDsOMIM: 610151; MGI: 1922874; HomoloGene: 6488; GeneCards: METAP1; OMA:METAP1 - orthologs
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for METAP1
Genomic location for METAP1
Band4q23Start98,995,620 bp[1]
End99,062,813 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for METAP1
Genomic location for METAP1
Band3|3 G3Start138,164,717 bp[2]
End138,195,276 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • left testis

  • right testis

  • endometrium

  • Descending thoracic aorta

  • epithelium of nasopharynx

  • rectum

  • urinary bladder

  • gingival epithelium

  • hair follicle

  • oral cavity
Top expressed in
  • primitive streak

  • lens

  • vastus lateralis muscle

  • triceps brachii muscle

  • sternocleidomastoid muscle

  • temporal muscle

  • hair follicle

  • crypt of lieberkuhn of small intestine

  • digastric muscle

  • ciliary body
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • peptidase activity
  • aminopeptidase activity
  • metalloexopeptidase activity
  • hydrolase activity
  • metal ion binding
Cellular component
  • cytosol
  • cytoplasm
Biological process
  • peptidyl-methionine modification
  • platelet aggregation
  • N-terminal protein amino acid modification
  • regulation of translation
  • proteolysis
  • regulation of rhodopsin mediated signaling pathway
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

23173

75624

Ensembl

ENSG00000164024

ENSMUSG00000005813

UniProt

P53582

Q8BP48

RefSeq (mRNA)

NM_015143

NM_175224

RefSeq (protein)

NP_055958

NP_780433

Location (UCSC)Chr 4: 99 – 99.06 MbChr 3: 138.16 – 138.2 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Methionine aminopeptidase 1 is an enzyme that in humans is encoded by the METAP1 gene.[5][6][7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000164024 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000005813 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H, et al. (Jul 1995). "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1". DNA Res. 2 (1): 37–43. doi:10.1093/dnares/2.1.37. PMID 7788527.
  6. ^ Dummitt B, Fei Y, Chang YH (Jul 2002). "Functional expression of human methionine aminopeptidase type 1 in Saccharomyces cerevisiae". Protein Pept Lett. 9 (4): 295–303. doi:10.2174/0929866023408607. PMID 12144506.
  7. ^ "Entrez Gene: METAP1 methionyl aminopeptidase 1".

Further reading

  • 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • 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.
  • 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.
  • Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
  • Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
  • Addlagatta A, Hu X, Liu JO, Matthews BW (2006). "Structural basis for the functional differences between type I and type II human methionine aminopeptidases". Biochemistry. 44 (45): 14741–9. doi:10.1021/bi051691k. PMID 16274222.
  • Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Selvakumar P, Lakshmikuttyamma A, Dimmock JR, Sharma RK (2006). "Methionine aminopeptidase 2 and cancer". Biochim. Biophys. Acta. 1765 (2): 148–54. doi:10.1016/j.bbcan.2005.11.001. PMID 16386852.
  • Hu X, Addlagatta A, Lu J, et al. (2007). "Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression". Proc. Natl. Acad. Sci. U.S.A. 103 (48): 18148–53. doi:10.1073/pnas.0608389103. PMC 1838721. PMID 17114291.
  • Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

External links

  • PDBe-KB provides an overview of all the structure information available in the PDB for Human Methionine aminopeptidase 1
  • v
  • t
  • e
  • 2b3h: Crystal structure of Human Methionine Aminopeptidase Type I with a third cobalt in the active site
    2b3h: Crystal structure of Human Methionine Aminopeptidase Type I with a third cobalt in the active site
  • 2b3k: Crystal structure of Human Methionine Aminopeptidase Type I in the holo form
    2b3k: Crystal structure of Human Methionine Aminopeptidase Type I in the holo form
  • 2b3l: Crystal structure of type I human methionine aminopeptidase in the apo form
    2b3l: Crystal structure of type I human methionine aminopeptidase in the apo form
  • 2g6p: Crystal structure of truncated (delta 1-89) human methionine aminopeptidase Type 1 in complex with Pyridyl pyrimidine derivative
    2g6p: Crystal structure of truncated (delta 1-89) human methionine aminopeptidase Type 1 in complex with Pyridyl pyrimidine derivative
  • 2gz5: Human Type 1 methionine aminopeptidase in complex with ovalicin at 1.1 Ang
    2gz5: Human Type 1 methionine aminopeptidase in complex with ovalicin at 1.1 Ang
  • 2nq6: Crystal structure of human methionine aminopeptidase type 1 in complex with 3-tert-Butoxycarbonylaminopyridine-2-carboxylic acid thiazole-2-ylamide
    2nq6: Crystal structure of human methionine aminopeptidase type 1 in complex with 3-tert-Butoxycarbonylaminopyridine-2-carboxylic acid thiazole-2-ylamide
  • 2nq7: Crystal structure of type 1 human methionine aminopeptidase in complex with 3-(2,2-Dimethylpropionylamino)pyridine-2-carboxylic acid thiazole-2-ylamide
    2nq7: Crystal structure of type 1 human methionine aminopeptidase in complex with 3-(2,2-Dimethylpropionylamino)pyridine-2-carboxylic acid thiazole-2-ylamide
  • v
  • t
  • e
3.4.11-19: Exopeptidase
3.4.11
3.4.13
3.4.14
3.4.15
3.4.16
3.4.17
Other/ungrouped
3.4.21-25: Endopeptidase
3.4.99: Unknown
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