Gene_Locus Report

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Gene_locus Report for: human-PPT2

Homo sapiens (Human) 34.9 kda protein (palmitoyl-protein thioesterase-2)

Comment
A second form inactive is known Trembl 014799 genbank AF020544 differs by yhe C-terminal end


Relationship
Family|Palmitoyl-protein_thioesterase
Block| X
Position in NCBI Life Tree|Homo sapiens
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Metazoa: N E > Eumetazoa: N E > Bilateria: N E > Deuterostomia: N E > Chordata: N E > Craniata: N E > Vertebrata: N E > Gnathostomata: N E > Teleostomi: N E > Euteleostomi: N E > Sarcopterygii: N E > Dipnotetrapodomorpha: N E > Tetrapoda: N E > Amniota: N E > Mammalia: N E > Theria: N E > Eutheria: N E > Boreoeutheria: N E > Euarchontoglires: N E > Primates: N E > Haplorrhini: N E > Simiiformes: N E > Catarrhini: N E > Hominoidea: N E > Hominidae: N E > Homininae: N E > Homo: N E > Homo sapiens: N E


Molecular evidence
Database
No mutation
1 structure:
1PJA: The crystal structure of palmitoyl protein thioesterase-2 reveals the basis for divergent substrate specificities of the two lysosomal thioesterases (PPT1 and PPT2)
No kinetic





No Substrate
No inhibitor
>3 Genbank links 15 more: U89336, AF020543, AL110128
>3 UniProt links 4 more: Q9UMR5, Q5T0S4, B0S872
1 Structure : 1PJA
>3 UniProt links 3 more: Q9UMR5, Q5T0S4, A8K358
>3 Interpro links 3 more: Q9UMR5, Q5T0S4, A8K358
>3 Prodom links 3 more: Q9UMR5, Q5T0S4, A8K358
>3 Pfam links 3 more: Q9UMR5, Q5T0S4, A8K358
>3 PIRSF links 3 more: Q9UMR5, Q5T0S4, A8K358
>3 SUPERFAM links 3 more: Q9UMR5, Q5T0S4, A8K358
1 EntrezGene : 9374
1 SNP : 9374
1 UniGene : 332138
1 HUGO HGNC : 9326
1 OMIM : 603298
1 Ensembl : ENSG00000168452
Sequence
Graphical view for this peptide sequence: human-PPT2
Colored MSA for Palmitoyl-protein_thioesterase (raw)
MLGLWGQRLPAAWVLLLLPFLPLLLLAAPAPHRASYKPVIVVHGLFDSSY
SFRHLLEYINETHPGTVVTVLDLFDGRESLRPLWEQVQGFREAVVPIMAK
APQGVHLICYSQGGLVCRALLSVMDDHNVDSFISLSSPQMGQYGDTDYLK
WLFPTSMRSNLYRICYSPWGQEFSICNYWHDPHHDDLYLNASSFLALING
ERDHPNATVWRKNFLRVGHLVLIGGPDDGVITPWQSSFFGFYDANETVLE
MEEQLVYLRDSFGLKTLLARGAIVRCPMAGISHTAWHSNRTLYETCIEPW
LS
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA

MLGLWGQRLPAAWVLLLLPFLPLLLLAAPAPHRASYKPVIVVHGLFDSSY
SFRHLLEYINETHPGTVVTVLDLFDGRESLRPLWEQVQGFREAVVPIMAK
APQGVHLICYSQGGLVCRALLSVMDDHNVDSFISLSSPQMGQYGDTDYLK
WLFPTSMRSNLYRICYSPWGQEFSICNYWHDPHHDDLYLNASSFLALING
ERDHPNATVWRKNFLRVGHLVLIGGPDDGVITPWQSSFFGFYDANETVLE
MEEQLVYLRDSFGLKTLLARGAIVRCPMAGISHTAWHSNRTLYETCIEPW
LS


References
1 more
    Title: The crystal structure of palmitoyl protein thioesterase-2 (PPT2) reveals the basis for divergent substrate specificities of the two lysosomal thioesterases, PPT1 and PPT2
    Calero G, Gupta P, Nonato MC, Tandel S, Biehl ER, Hofmann SL, Clardy J
    Ref: Journal of Biological Chemistry, 278:37957, 2003 : PubMed

            

    Title: Characterization of a human MHC class III region gene product with S-thioesterase activity
    Aguado B, Campbell RD
    Ref: Biochemical Journal, 341 ( Pt 3):679, 1999 : PubMed

            

    Title: Molecular cloning and expression of palmitoyl-protein thioesterase 2 (PPT2), a homolog of lysosomal palmitoyl-protein thioesterase with a distinct substrate specificity
    Soyombo AA, Hofmann SL
    Ref: Journal of Biological Chemistry, 272:27456, 1997 : PubMed

            


Other Papers


Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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