dbPTM

RMT2_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RMT2_YEAST
UniProt AC	Q03305
Protein Name	Protein arginine N-methyltransferase 2 {ECO:0000303\|PubMed:9873020}
Gene Name	RMT2 {ECO:0000303\|PubMed:9873020}
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	412
Subcellular Localization	Cytoplasm . Nucleus . Appears often very close to the nuclear membrane and the nuclear pores.
Protein Description	S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that methylates the delta-nitrogen atom of arginine residues to form N5-methylarginine (type IV) in target proteins. [PubMed: 9873020 Monomethylates ribosomal protein L12 (RPL12A/RPL12B) at 'Arg-67']
Protein Sequence	MSELHALLTFPERPISQSYYVPKLQHFLKSGIPATYTLEQVAAFEHEEKNRNGDKEFRESTDDNKTSNTTPLHVLARSLPLDIKDEELQVVMDMMNILFEYGAGWNFIDYEDKTVGDLFLERNQSRESPLYRRLVEAGVSAELLLRKLNGGDVEFLDTDELIGIEPEESVQTAVDGQKEESVGSDDDATAANQQVYLKTELEYKDDALITKENKDGVMMDWETKIMELASETLFPDPEATNSATILNIGFGMGIIDTFIQARKPYRHYICEAHPDVLAKMKMDGWYEKDNVVILEGRWQDTLNNLLDKGEVFFDGIYYDTFSEHYQDILDLYDVVVGLIKPEGVFSFFNGLGADRSLCYDVYKEIVEIDVATYGMKCDYTRYSLDEQLPDWNDVKRSYFNCNYYYHPRITFA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSELHALLT ------CCCCCHHHC	49.19	30377154
49	Acetylation	AAFEHEEKNRNGDKE HCCCHHHHCCCCCHH	59.22	24489116
60	Phosphorylation	GDKEFRESTDDNKTS CCHHHHHCCCCCCCC	32.64	19779198
61	Phosphorylation	DKEFRESTDDNKTSN CHHHHHCCCCCCCCC	42.49	27717283
181	Phosphorylation	VDGQKEESVGSDDDA CCCCCEECCCCCCCC	32.63	22369663
184	Phosphorylation	QKEESVGSDDDATAA CCEECCCCCCCCHHH	35.39	22369663
189	Phosphorylation	VGSDDDATAANQQVY CCCCCCCHHHHHEEE	33.04	22890988
204	Acetylation	LKTELEYKDDALITK EEEEEEECCCEEEEE	39.49	24489116

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of RMT2_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RMT2_YEAST !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of RMT2_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NU116_YEAST	NUP116	physical	17448464
NU100_YEAST	NUP100	physical	17448464
NUP57_YEAST	NUP57	physical	17448464
NUP49_YEAST	NUP49	physical	17448464
SLX8_YEAST	SLX8	genetic	20093466
RTG2_YEAST	RTG2	genetic	20093466
ASK10_YEAST	ASK10	genetic	20093466
PHB2_YEAST	PHB2	genetic	20093466
SNF6_YEAST	SNF6	genetic	20093466
MDM35_YEAST	MDM35	genetic	20093466
DIA2_YEAST	DIA2	genetic	20093466
FIT3_YEAST	FIT3	genetic	20093466
TGS1_YEAST	TGS1	genetic	20093466
GGPPS_YEAST	BTS1	genetic	20093466
MRM2_YEAST	MRM2	genetic	27708008
ASK10_YEAST	ASK10	genetic	27708008
SIN3_YEAST	SIN3	genetic	27708008
PP2C1_YEAST	PTC1	genetic	27708008
SLX5_YEAST	SLX5	genetic	27708008
OSW7_YEAST	OSW7	genetic	27708008
ATG1_YEAST	ATG1	genetic	27708008
RTG2_YEAST	RTG2	genetic	27708008
RL11B_YEAST	RPL11B	genetic	27708008
MDM35_YEAST	MDM35	genetic	27708008
MMM1_YEAST	MMM1	genetic	27708008
PET8_YEAST	PET8	genetic	27708008
LSM7_YEAST	LSM7	genetic	27708008
DIA2_YEAST	DIA2	genetic	27708008
PMA2_YEAST	PMA2	genetic	27708008
GGPPS_YEAST	BTS1	genetic	27708008
TGS1_YEAST	TGS1	genetic	27708008
BRR1_YEAST	BRR1	genetic	27708008
RL36A_YEAST	RPL36A	genetic	29158977

Drug and Disease Associations

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

Regulatory Network of RMT2_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-181 AND SER-184, ANDMASS SPECTROMETRY.	18407956 [Abstract]
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-184, ANDMASS SPECTROMETRY.	17330950 [Abstract]