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Gene_locus Report for: human-PPME1

Homo sapiens (Human) protein phosphatase PP2A methylesterase-1 (EC 3.1.1.-) (pme-1)

Comment
PP2A dimethyl-esterase (PME-1). human Q9NVT5 CDNA FLJ10519 fis, clone NT2RP2000816, similar to a chelatase is identical to PME-1 Q9UI18 pro0750


Relationship
Family|PPase_methylesterase_euk
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
2 structures: 3C5V, 3C5W
No kinetic





No Substrate
1 inhbitor:
ABL-127
>3 Genbank links 3 more: AF157028, AK001381, AF111853
1 UniProt : Q9Y570
2 Structure : 3C5W, 3C5V
1 UniProt : Q9Y570
1 Interpro : Q9Y570
1 Prodom : Q9Y570
1 Pfam : Q9Y570
1 PIRSF : Q9Y570
1 SUPERFAM : Q9Y570
1 EntrezGene : 51400
1 SNP : 51400
1 UniGene : 503251
1 HUGO HGNC : 30178
1 IUPHAR : 2875
1 OMIM : 611117
1 Ensembl : ENSG00000189311
Sequence
Graphical view for this peptide sequence: human-PPME1
Colored MSA for PPase_methylesterase_euk (raw)
MSALEKSMHLGRLPSRPPLPGSGGSQSGAKMRMGPGRKRDFSPVPWSQYF
ESMEDVEVENETGKDTFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAII
SRVQCRIVALDLRSHGETKVKNPEDLSAETMAKDVGNVVEAMYGDLPPPI
MLIGHSMGGAIAVHTASSNLVPSLLGLCMIDVVEGTAMDALNSMQNFLRG
RPKTFKSLENAIEWSVKSGQIRNLESARVSMVGQVKQCEGITSPEGSKSI
VEGIIEEEEEDEEGSESISKRKKEDDMETKKDHPYTWRIELAKTEKYWDG
WFRGLSNLFLSCPIPKLLLLAGVDRLDKDLTIGQMQGKFQMQVLPQCGHA
VHEDAPDKVAEAVATFLIRHRFAEPIGGFQCVFPGC
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

MSALEKSMHLGRLPSRPPLPGSGGSQSGAKMRMGPGRKRDFSPVPWSQYF
ESMEDVEVENETGKDTFRVYKSGSEGPVLLLLHGGGHSALSWAVFTAAII
SRVQCRIVALDLRSHGETKVKNPEDLSAETMAKDVGNVVEAMYGDLPPPI
MLIGHSMGGAIAVHTASSNLVPSLLGLCMIDVVEGTAMDALNSMQNFLRG
RPKTFKSLENAIEWSVKSGQIRNLESARVSMVGQVKQCEGITSPEGSKSI
VEGIIEEEEEDEEGSESISKRKKEDDMETKKDHPYTWRIELAKTEKYWDG
WFRGLSNLFLSCPIPKLLLLAGVDRLDKDLTIGQMQGKFQMQVLPQCGHA
VHEDAPDKVAEAVATFLIRHRFAEPIGGFQCVFPGC


References
6 more
    Title: Spatial control of protein phosphatase 2A (de)methylation
    Longin S, Zwaenepoel K, Martens E, Louis JV, Rondelez E, Goris J, Janssens V
    Ref: Experimental Cell Research, 314:68, 2008 : PubMed

            

    Title: Structural mechanism of demethylation and inactivation of protein phosphatase 2A
    Xing Y, Li Z, Chen Y, Stock JB, Jeffrey PD, Shi Y
    Ref: Cell, 133:154, 2008 : PubMed

            

    Title: A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A
    Ogris E, Du X, Nelson KC, Mak EK, Yu XX, Lane WS, Pallas DC
    Ref: Journal of Biological Chemistry, 274:14382, 1999 : PubMed

            


Other Papers


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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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