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Protein

Ribosomal lysine N-methyltransferase 2

Gene

RKM2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that trimethylates 60S ribosomal protein L12 (RPL12A and RPL12B) at 'Lys-4' and 'Lys-11'.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei324 – 3241S-adenosyl-L-methioninePROSITE-ProRule annotation

GO - Molecular functioni

  • protein-lysine N-methyltransferase activity Source: SGD

GO - Biological processi

  • peptidyl-lysine monomethylation Source: SGD
  • peptidyl-lysine trimethylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-29784-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal lysine N-methyltransferase 21 Publication (EC:2.1.1.-1 Publication)
Gene namesi
Name:RKM21 Publication
Ordered Locus Names:YDR198CImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR198C.
SGDiS000002606. RKM2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 479479Ribosomal lysine N-methyltransferase 2PRO_0000253809Add
BLAST

Proteomic databases

MaxQBiQ03942.

Interactioni

Protein-protein interaction databases

BioGridi32250. 19 interactions.
DIPiDIP-6397N.
IntActiQ03942. 2 interactions.
MINTiMINT-686952.

Structurei

3D structure databases

ProteinModelPortaliQ03942.
SMRiQ03942. Positions 21-52.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 325304SETPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. RKM2 family.PROSITE-ProRule annotationCurated
Contains 1 SET domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000001042.
InParanoidiQ03942.
OMAiINSRCLY.
OrthoDBiEOG7XSTQQ.

Family and domain databases

InterProiIPR001214. SET_dom.
IPR016852. SET_MeTrfase.
[Graphical view]
PIRSFiPIRSF027158. Lys_MTase_YDR198C_prd. 1 hit.
PROSITEiPS50280. SET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03942-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGKVDVLLT WLKKSDKFYI APNISICESP ETGRGIVLSH GSIRKNDIIV
60 70 80 90 100
SVPSSKQLNF HTILYHISKF NKELNIPGIT IDRKPINYED NIIEAENKAW
110 120 130 140 150
ADPRYGLYSE LSKEFLLSLS SFQLVSFYIL VENFLLPKWT HNEIYSDWKP
160 170 180 190 200
FFDVWPSMEE LRSIPAIWNC DPNSRYHSLI EYLPAASRKH MARISGLVRE
210 220 230 240 250
DWETISEVVL KWNEIYGSLS CTKNSDKFTS DELFSLFVHV YFIINSRCLY
260 270 280 290 300
AKIPLKIEDS PSNFTLVPYV DFMNHICESD LHCYPQLSPQ LRSEGENIIG
310 320 330 340 350
IGQFTIRCGD HLYDNINEEL FLNYGAHSND FLLNEYGFVV DGNKWNYLDI
360 370 380 390 400
SDEIIELIDD DKKEVKTFLL EHDYWGDYTI NETDISYRIF VALNYYVTRD
410 420 430 440 450
ERRVRKFIEG YISEDYFKPK ISSVLKELLV SLTAKYTKTL SELTEKVSNL
460 470
ENNLCLQNLI TIYKGYIKIL TQHLQDLQS
Length:479
Mass (Da):55,950
Last modified:November 1, 1996 - v1
Checksum:i4E19ADFADEE1A0A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48784 Genomic DNA. Translation: CAA88711.1.
BK006938 Genomic DNA. Translation: DAA12041.1.
PIRiS52705.
RefSeqiNP_010484.1. NM_001180506.1.

Genome annotation databases

EnsemblFungiiYDR198C; YDR198C; YDR198C.
GeneIDi851779.
KEGGisce:YDR198C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48784 Genomic DNA. Translation: CAA88711.1.
BK006938 Genomic DNA. Translation: DAA12041.1.
PIRiS52705.
RefSeqiNP_010484.1. NM_001180506.1.

3D structure databases

ProteinModelPortaliQ03942.
SMRiQ03942. Positions 21-52.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32250. 19 interactions.
DIPiDIP-6397N.
IntActiQ03942. 2 interactions.
MINTiMINT-686952.

Proteomic databases

MaxQBiQ03942.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR198C; YDR198C; YDR198C.
GeneIDi851779.
KEGGisce:YDR198C.

Organism-specific databases

EuPathDBiFungiDB:YDR198C.
SGDiS000002606. RKM2.

Phylogenomic databases

HOGENOMiHOG000001042.
InParanoidiQ03942.
OMAiINSRCLY.
OrthoDBiEOG7XSTQQ.

Enzyme and pathway databases

BioCyciYEAST:G3O-29784-MONOMER.

Miscellaneous databases

NextBioi969585.
PROiQ03942.

Family and domain databases

InterProiIPR001214. SET_dom.
IPR016852. SET_MeTrfase.
[Graphical view]
PIRSFiPIRSF027158. Lys_MTase_YDR198C_prd. 1 hit.
PROSITEiPS50280. SET. 1 hit.
[Graphical view]
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(1997) [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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  4. "A novel SET domain methyltransferase in yeast: Rkm2-dependent trimethylation of ribosomal protein L12ab at lysine 10."
    Porras-Yakushi T.R., Whitelegge J.P., Clarke S.
    J. Biol. Chem. 281:35835-35845(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Identification of two SET domain proteins required for methylation of lysine residues in yeast ribosomal protein Rpl42ab."
    Webb K.J., Laganowsky A., Whitelegge J.P., Clarke S.G.
    J. Biol. Chem. 283:35561-35568(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiRKM2_YEAST
AccessioniPrimary (citable) accession number: Q03942
Secondary accession number(s): D6VSI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 768 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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 one 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.