RKM1_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RKM1_YEAST
• UniProt AC: Q08961
• Protein Name: Ribosomal lysine N-methyltransferase 1 {ECO:0000303|PubMed:16096273}
• Gene Name: RKM1 {ECO:0000303|PubMed:16096273}
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 583
• Subcellular Localization: Cytoplasm . Nucleus .
• Protein Description: S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates ribosomal protein S18 (RPS18A and RPS18B) at 'Lys-48' and dimethylates ribosomal protein L23 (RPL23A and RPL23B) at 'Lys-106' and 'Lys-110'..
• Protein Sequence: MSSDALKALLQWGASFGVIVPEELKFLYTDLKGIICVCEKDIDNPSIKIPPEIVISRNLPMKFFGLSESTKNINGWLKLFFAKIKFDRDNDTIVDNVRVNDKFKPYLDALPSRLNSPLVWNPSELKRLSSTNIGNSIHEKFEGIFKEWFELVSSSDMFDLERVADDVQTFHNLDELTYEALYEKILKITELQRPTIWYSFPAFLWSHLIFISRAFPEYVLNRNCPDNSIVLLPIVDLLNHDYRSKVKWYPENGWFCYEKIGTASQSRELSNNYGGKGNEELLSGYGFVLEDNIFDSVALKVKLPLDVVSTILETEPSLKLPLLSDYTTYAFENKDCVQQEKKATRSATDYINGVTYFINIQNEQCLEPLLDLFTYLSKAEEEDLHDLRARLQGIQMLRNALQSKLNSITGPPATDDSYAIDPYRVYCADVYTKGQKQILKEALTRLKKLEKTMLSENKHQLLTMSKILKNDPAFAETELPSLFSNEDGEEVIFESTYDLLILWILLKTKKNSYPTKYEWVGQQYTNFKQTAYISDDAKAFHTAYFEKQDDVDLAEVDHAIQFVVDNSFTRTSSTTEETILVRK

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
67	Phosphorylation	PMKFFGLSESTKNIN CCCEECCCCCCCCCC	29.85	19684113
69	Phosphorylation	KFFGLSESTKNINGW CEECCCCCCCCCCHH	41.11	28889911
129	Phosphorylation	PSELKRLSSTNIGNS HHHHHHHHCCCCCHH	38.87	22369663
130	Phosphorylation	SELKRLSSTNIGNSI HHHHHHHCCCCCHHH	30.02	22369663
131	Phosphorylation	ELKRLSSTNIGNSIH HHHHHHCCCCCHHHH	27.72	22369663
136	Phosphorylation	SSTNIGNSIHEKFEG HCCCCCHHHHHHHHH	21.80	22369663
327	Phosphorylation	LPLLSDYTTYAFENK CCCCCCCCEEEECCC	20.51	27017623
328	Phosphorylation	PLLSDYTTYAFENKD CCCCCCCEEEECCCH	13.46	27017623
329	Phosphorylation	LLSDYTTYAFENKDC CCCCCCEEEECCCHH	11.07	27017623
452	Phosphorylation	RLKKLEKTMLSENKH HHHHHHHHHCCCCHH	17.61	27017623
455	Phosphorylation	KLEKTMLSENKHQLL HHHHHHCCCCHHHHH	28.44	27017623
458	Acetylation	KTMLSENKHQLLTMS HHHCCCCHHHHHHHH	28.77	24489116
465	Phosphorylation	KHQLLTMSKILKNDP HHHHHHHHHHHHCCC	16.00	27017623
510	Acetylation	WILLKTKKNSYPTKY HHHHHHCCCCCCCCC	57.25	24489116
516	Acetylation	KKNSYPTKYEWVGQQ CCCCCCCCCEECCCC	36.35	24489116
573	Phosphorylation	NSFTRTSSTTEETIL CCCCCCCCCCEEEEE	38.44	27214570
575	Phosphorylation	FTRTSSTTEETILVR CCCCCCCCEEEEEEE	33.50	25752575

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RKM1_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RKM1_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RKM1_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UTP22_YEAST	UTP22	physical	16554755
SLM1_YEAST	SLM1	physical	16554755
YMR1_YEAST	YMR1	physical	16554755
SP382_YEAST	SPP382	physical	16554755
ARP7_YEAST	ARP7	physical	16554755
ASK10_YEAST	ASK10	genetic	20093466
SDS3_YEAST	SDS3	genetic	20093466
VRP1_YEAST	VRP1	genetic	20093466
SNF5_YEAST	SNF5	genetic	27708008
SAS4_YEAST	SAS4	genetic	27708008
ACE2_YEAST	ACE2	genetic	27708008

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND MASSSPECTROMETRY.
PubMed: 18407956