PPM1/YDR435C Protein Information

Standard Name	Ppm1p 1
Systematic Name	Ydr435cp
ORF Classification	Verified
Description	Carboxyl methyltransferase, methylates the C terminus of the protein phosphatase 2A catalytic subunit (Pph21p or Pph22p), which is important for complex formation with regulatory subunits (1, 2, 3)
Name Description	Protein Phosphatase Methyltransferase 1

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	328
Molecular Weight (Da)	37,694
Isoelectric Point (pI)	7.34

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Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Ppm1p (InterPro)
Physical Interactions	There are 1 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000006B82C \| Q04081 MIPS: YDR435C NCBI: 126031467 \| 126031468 \| 126031469 \| 126031470 \| 126031471 \| 126031472 \| 39654870 \| 39654871 \| 39654872 \| 39654873 \| 39654874 \| 39654875 \| 39654876 \| 39654877 \| 39654878 \| 39654879 \| 6320643 \| 74583444 \| 927710 \| NP_010723.1 GenBank/EMBL/DDBJ: DAA12272.1 \| U33007
External Classifications	EC: 2.1.1.- [Transferases transferring one-carbon groups methyltransferases] EC: 2.1.1.233 [[Phosphatase 2A protein]-leucine-carboxy methyltransferase]

Amino Acid Sequence (or in FASTA format)
1 MERIIQQTDY DALSCKLAAI SVGYLPSSGL QRLSVDLSKK YTEWHRSYLI 51 TLKKFSRRAF GKVDKAMRSS FPVMNYGTYL RTVGIDAAIL EFLVANEKVQ 101 VVNLGCGSDL RMLPLLQMFP HLAYVDIDYN ESVELKNSIL RESEILRISL 151 GLSKEDTAKS PFLIDQGRYK LAACDLNDIT ETTRLLDVCT KREIPTIVIS 201 ECLLCYMHNN ESQLLINTIM SKFSHGLWIS YDPIGGSQPN DRFGAIMQSN 251 LKESRNLEMP TLMTYNSKEK YASRWSAAPN VIVNDMWEIF NAQIPESERK 301 RLRSLQFLDE LEELKVMQTH YILMKAQW*

Amino Acid Sequence (or in FASTA format)

       1  MERIIQQTDY DALSCKLAAI SVGYLPSSGL QRLSVDLSKK YTEWHRSYLI
      51  TLKKFSRRAF GKVDKAMRSS FPVMNYGTYL RTVGIDAAIL EFLVANEKVQ
     101  VVNLGCGSDL RMLPLLQMFP HLAYVDIDYN ESVELKNSIL RESEILRISL
     151  GLSKEDTAKS PFLIDQGRYK LAACDLNDIT ETTRLLDVCT KREIPTIVIS
     201  ECLLCYMHNN ESQLLINTIM SKFSHGLWIS YDPIGGSQPN DRFGAIMQSN
     251  LKESRNLEMP TLMTYNSKEK YASRWSAAPN VIVNDMWEIF NAQIPESERK
     301  RLRSLQFLDE LEELKVMQTH YILMKAQW*

external links for Ppm1p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	Organelle DB
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YPL+
Candida (CGD)	BioPIXIE	MIPS	YeastGFP
Candida (CandidaDB)	CYC2008 (complexes)	Pfam domains
YGOB	Complexome	YeastRC Structure Prediction (Seattle)
YOGY	DIP
	GeneMANIA
	YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Ppm1p

1)	Wu J, et al. (2000) Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo. EMBO J 19(21):5672-81
2)	Wei H, et al. (2001) Carboxymethylation of the PP2A catalytic subunit in Saccharomyces cerevisiae is required for efficient interaction with the B-type subunits Cdc55p and Rts1p. J Biol Chem 276(2):1570-7
3)	Kalhor HR, et al. (2001) Protein phosphatase methyltransferase 1 (Ppm1p) is the sole activity responsible for modification of the major forms of protein phosphatase 2A in yeast. Arch Biochem Biophys 395(2):239-45