Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Leucine carboxyl methyltransferase 1

Gene

PPM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues. Acts on the two major protein phosphatase 2A catalytic subunits, PPH21 and PPH22.2 Publications

Catalytic activityi

S-adenosyl-L-methionine + [phosphatase 2A protein]-leucine = S-adenosyl-L-homocysteine + [phosphatase 2A protein]-leucine methyl ester.

Enzyme regulationi

Inhibited by S-adenosyl-L-homocysteine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei81 – 811S-adenosyl-L-methionine
Binding sitei105 – 1051S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei128 – 1281S-adenosyl-L-methionine
Binding sitei201 – 2011S-adenosyl-L-methionine; via carbonyl oxygen

GO - Molecular functioni

  1. protein C-terminal leucine carboxyl O-methyltransferase activity Source: SGD

GO - Biological processi

  1. cellular protein complex assembly Source: SGD
  2. C-terminal protein methylation Source: SGD
  3. regulation of autophagy Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:YDR435C-MONOMER.
BRENDAi2.1.1.233. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine carboxyl methyltransferase 1 (EC:2.1.1.233)
Alternative name(s):
Protein phosphatase methyltransferase 1
[Phosphatase 2A protein]-leucine-carboxy methyltransferase 1
Gene namesi
Name:PPM1
Ordered Locus Names:YDR435C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDR435c.
SGDiS000002843. PPM1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328Leucine carboxyl methyltransferase 1PRO_0000226135Add
BLAST

Proteomic databases

MaxQBiQ04081.
PaxDbiQ04081.
PeptideAtlasiQ04081.

Expressioni

Gene expression databases

GenevestigatoriQ04081.

Interactioni

Protein-protein interaction databases

BioGridi32491. 94 interactions.
DIPiDIP-5435N.
MINTiMINT-517778.
STRINGi4932.YDR435C.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64Combined sources
Helixi8 – 2215Combined sources
Turni28 – 325Combined sources
Helixi35 – 5521Combined sources
Helixi57 – 6812Combined sources
Helixi72 – 9524Combined sources
Beta strandi97 – 1048Combined sources
Helixi112 – 1187Combined sources
Beta strandi122 – 1287Combined sources
Helixi130 – 14213Combined sources
Helixi144 – 1507Combined sources
Beta strandi162 – 1654Combined sources
Beta strandi167 – 1737Combined sources
Beta strandi176 – 1783Combined sources
Helixi179 – 1879Combined sources
Beta strandi192 – 1943Combined sources
Beta strandi196 – 2027Combined sources
Helixi204 – 2063Combined sources
Helixi209 – 22214Combined sources
Beta strandi224 – 23310Combined sources
Helixi243 – 25513Combined sources
Turni260 – 2656Combined sources
Helixi268 – 2725Combined sources
Helixi273 – 2753Combined sources
Beta strandi278 – 2858Combined sources
Helixi286 – 2927Combined sources
Helixi296 – 3038Combined sources
Helixi311 – 3188Combined sources
Beta strandi321 – 3288Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RJDX-ray1.80A/B/C1-328[»]
1RJEX-ray2.00A/B/C1-328[»]
1RJFX-ray2.25A/B/C1-328[»]
1RJGX-ray2.61A1-328[»]
2OB1X-ray1.90A/B/C10-328[»]
2OB2X-ray1.92A/B/C2-328[»]
SMRiQ04081. Positions 2-328.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04081.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni175 – 1773S-adenosyl-L-methionine binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG329644.
HOGENOMiHOG000113293.
InParanoidiQ04081.
KOiK18203.
OMAiWISYDPI.
OrthoDBiEOG70611J.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR007213. LCM_MeTrfase.
IPR016651. Leu_CO_MeTrfase_LCMT1.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR13600. PTHR13600. 1 hit.
PfamiPF04072. LCM. 1 hit.
[Graphical view]
PIRSFiPIRSF016305. LCM_mtfrase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

Q04081-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERIIQQTDY DALSCKLAAI SVGYLPSSGL QRLSVDLSKK YTEWHRSYLI
60 70 80 90 100
TLKKFSRRAF GKVDKAMRSS FPVMNYGTYL RTVGIDAAIL EFLVANEKVQ
110 120 130 140 150
VVNLGCGSDL RMLPLLQMFP HLAYVDIDYN ESVELKNSIL RESEILRISL
160 170 180 190 200
GLSKEDTAKS PFLIDQGRYK LAACDLNDIT ETTRLLDVCT KREIPTIVIS
210 220 230 240 250
ECLLCYMHNN ESQLLINTIM SKFSHGLWIS YDPIGGSQPN DRFGAIMQSN
260 270 280 290 300
LKESRNLEMP TLMTYNSKEK YASRWSAAPN VIVNDMWEIF NAQIPESERK
310 320
RLRSLQFLDE LEELKVMQTH YILMKAQW
Length:328
Mass (Da):37,695
Last modified:October 31, 1996 - v1
Checksum:i5FAB5B9F8B04D154
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33007 Genomic DNA. Translation: AAB64876.1.
BK006938 Genomic DNA. Translation: DAA12272.1.
PIRiS69715.
RefSeqiNP_010723.1. NM_001180743.1.

Genome annotation databases

EnsemblFungiiYDR435C; YDR435C; YDR435C.
GeneIDi852045.
KEGGisce:YDR435C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33007 Genomic DNA. Translation: AAB64876.1.
BK006938 Genomic DNA. Translation: DAA12272.1.
PIRiS69715.
RefSeqiNP_010723.1. NM_001180743.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RJDX-ray1.80A/B/C1-328[»]
1RJEX-ray2.00A/B/C1-328[»]
1RJFX-ray2.25A/B/C1-328[»]
1RJGX-ray2.61A1-328[»]
2OB1X-ray1.90A/B/C10-328[»]
2OB2X-ray1.92A/B/C2-328[»]
SMRiQ04081. Positions 2-328.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32491. 94 interactions.
DIPiDIP-5435N.
MINTiMINT-517778.
STRINGi4932.YDR435C.

Proteomic databases

MaxQBiQ04081.
PaxDbiQ04081.
PeptideAtlasiQ04081.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR435C; YDR435C; YDR435C.
GeneIDi852045.
KEGGisce:YDR435C.

Organism-specific databases

CYGDiYDR435c.
SGDiS000002843. PPM1.

Phylogenomic databases

eggNOGiNOG329644.
HOGENOMiHOG000113293.
InParanoidiQ04081.
KOiK18203.
OMAiWISYDPI.
OrthoDBiEOG70611J.

Enzyme and pathway databases

BioCyciYEAST:YDR435C-MONOMER.
BRENDAi2.1.1.233. 984.

Miscellaneous databases

EvolutionaryTraceiQ04081.
NextBioi970296.
PROiQ04081.

Gene expression databases

GenevestigatoriQ04081.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR007213. LCM_MeTrfase.
IPR016651. Leu_CO_MeTrfase_LCMT1.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR13600. PTHR13600. 1 hit.
PfamiPF04072. LCM. 1 hit.
[Graphical view]
PIRSFiPIRSF016305. LCM_mtfrase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo."
    Wu J., Tolstykh T., Lee J., Boyd K., Stock J.B., Broach J.R.
    EMBO J. 19:5672-5681(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Protein phosphatase methyltransferase 1 (Ppm1p) is the sole activity responsible for modification of the major forms of protein phosphatase 2A in yeast."
    Kalhor H.R., Luk K., Ramos A., Zobel-Thropp P., Clarke S.
    Arch. Biochem. Biophys. 395:239-245(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Structure of protein phosphatase methyltransferase 1 (PPM1), a leucine carboxyl methyltransferase involved in the regulation of protein phosphatase 2A activity."
    Leulliot N., Quevillon-Cheruel S., Sorel I., de La Sierra-Gallay I.L., Collinet B., Graille M., Blondeau K., Bettache N., Poupon A., Janin J., van Tilbeurgh H.
    J. Biol. Chem. 279:8351-8358(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH S-ADENOSYL-L-METHIONINE AND S-ADENOSYL-L-HOMOCYSTEINE.

Entry informationi

Entry nameiLCMT1_YEAST
AccessioniPrimary (citable) accession number: Q04081
Secondary accession number(s): D6VT62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2006
Last sequence update: October 31, 1996
Last modified: March 31, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.