dbPTM

RL25_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL25_YEAST
UniProt AC	P04456
Protein Name	60S ribosomal protein L25 {ECO:0000303\|PubMed:9559554}
Gene Name	RPL25 {ECO:0000303\|PubMed:9559554}
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	142
Subcellular Localization	Cytoplasm .
Protein Description	Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. uL23 is a major component of the universal docking site for these factors at the polypeptide exit tunnel..
Protein Sequence	MAPSAKATAAKKAVVKGTNGKKALKVRTSATFRLPKTLKLARAPKYASKAVPHYNRLDSYKVIEQPITSETAMKKVEDGNILVFQVSMKANKYQIKKAVKELYEVDVLKVNTLVRPNGTKKAYVRLTADYDALDIANRIGYI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MAPSAKATAAK ----CCCCHHHHHHH	32.63	19795423
8	Phosphorylation	MAPSAKATAAKKAVV CCCCHHHHHHHHHHE	26.83	19795423
25	2-Hydroxyisobutyrylation	TNGKKALKVRTSATF CCCCEEEEEEECCEE	34.23	-
28	Phosphorylation	KKALKVRTSATFRLP CEEEEEEECCEECCC	26.21	29136822
29	Phosphorylation	KALKVRTSATFRLPK EEEEEEECCEECCCC	18.10	19823750
31	Phosphorylation	LKVRTSATFRLPKTL EEEEECCEECCCCHH	14.73	29136822
36	Ubiquitination	SATFRLPKTLKLARA CCEECCCCHHHHHCC	71.70	22817900
39	Ubiquitination	FRLPKTLKLARAPKY ECCCCHHHHHCCCCH	45.38	22817900
45	Acetylation	LKLARAPKYASKAVP HHHHCCCCHHHHCCC	53.08	24489116
45	Ubiquitination	LKLARAPKYASKAVP HHHHCCCCHHHHCCC	53.08	22817900
49	Acetylation	RAPKYASKAVPHYNR CCCCHHHHCCCCCCC	45.27	24489116
49	Ubiquitination	RAPKYASKAVPHYNR CCCCHHHHCCCCCCC	45.27	22817900
59	Phosphorylation	PHYNRLDSYKVIEQP CCCCCCCCCEEEECC	31.29	17287358
60	Phosphorylation	HYNRLDSYKVIEQPI CCCCCCCCEEEECCC	14.67	21440633
61	Sumoylation	YNRLDSYKVIEQPIT CCCCCCCEEEECCCC	40.46	15542864
61	Succinylation	YNRLDSYKVIEQPIT CCCCCCCEEEECCCC	40.46	23954790
61	Acetylation	YNRLDSYKVIEQPIT CCCCCCCEEEECCCC	40.46	24489116
61	Ubiquitination	YNRLDSYKVIEQPIT CCCCCCCEEEECCCC	40.46	23749301
61	Sumoylation	YNRLDSYKVIEQPIT CCCCCCCEEEECCCC	40.46	-
68	Phosphorylation	KVIEQPITSETAMKK EEEECCCCCHHHCEE	27.48	24961812
69	Phosphorylation	VIEQPITSETAMKKV EEECCCCCHHHCEEC	33.40	24961812
71	Phosphorylation	EQPITSETAMKKVED ECCCCCHHHCEECCC	31.64	28889911
74	2-Hydroxyisobutyrylation	ITSETAMKKVEDGNI CCCHHHCEECCCCCE	51.72	-
74	Succinylation	ITSETAMKKVEDGNI CCCHHHCEECCCCCE	51.72	23954790
74	Ubiquitination	ITSETAMKKVEDGNI CCCHHHCEECCCCCE	51.72	23749301
74	Acetylation	ITSETAMKKVEDGNI CCCHHHCEECCCCCE	51.72	24489116
75	Ubiquitination	TSETAMKKVEDGNIL CCHHHCEECCCCCEE	37.46	23749301
92	Acetylation	QVSMKANKYQIKKAV EEEECCCHHHHHHHH	43.31	25381059
96	2-Hydroxyisobutyrylation	KANKYQIKKAVKELY CCCHHHHHHHHHHHH	21.10	-
96	Ubiquitination	KANKYQIKKAVKELY CCCHHHHHHHHHHHH	21.10	22817900
97	Acetylation	ANKYQIKKAVKELYE CCHHHHHHHHHHHHC	61.10	24489116
97	Ubiquitination	ANKYQIKKAVKELYE CCHHHHHHHHHHHHC	61.10	22817900
100	Succinylation	YQIKKAVKELYEVDV HHHHHHHHHHHCCCE	47.03	23954790
100	Ubiquitination	YQIKKAVKELYEVDV HHHHHHHHHHHCCCE	47.03	23749301
100	Acetylation	YQIKKAVKELYEVDV HHHHHHHHHHHCCCE	47.03	24489116
100	2-Hydroxyisobutyrylation	YQIKKAVKELYEVDV HHHHHHHHHHHCCCE	47.03	-
109	Acetylation	LYEVDVLKVNTLVRP HHCCCEEEEEEEECC	33.03	24489116
112	Phosphorylation	VDVLKVNTLVRPNGT CCEEEEEEEECCCCC	29.62	21440633
119	Phosphorylation	TLVRPNGTKKAYVRL EEECCCCCCCEEEEE	35.69	21440633

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 RL25_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL25_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 RL25_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STM1_YEAST	STM1	physical	12166649
GBLP_YEAST	ASC1	physical	12166649
NMD3_YEAST	NMD3	physical	20584915
MEX67_YEAST	MEX67	physical	21852791
NMD3_YEAST	NMD3	physical	21852791
NOP3_YEAST	NPL3	physical	21852791
SLF1_YEAST	SLF1	physical	24838188
SSBP1_YEAST	SBP1	physical	24838188
NAM7_YEAST	NAM7	physical	23801788
PABP_YEAST	PAB1	physical	23801788
RS2_YEAST	RPS2	physical	24100011
MEX67_YEAST	MEX67	physical	26872259
DBP5_YEAST	DBP5	physical	26872259
RS3_YEAST	RPS3	physical	26872259
SPB1_YEAST	SPB1	physical	25404745
NOP2_YEAST	NOP2	physical	25404745
PESC_YEAST	NOP7	physical	25404745
NOG1_YEAST	NOG1	physical	25404745
NUG1_YEAST	NUG1	physical	25404745
EBP2_YEAST	EBP2	physical	25404745
NOG2_YEAST	NOG2	physical	25404745
NLE1_YEAST	RSA4	physical	25404745
HAS1_YEAST	HAS1	physical	25404745
CIC1_YEAST	CIC1	physical	25404745
RL3_YEAST	RPL3	physical	25404745
RPF2_YEAST	RPF2	physical	25404745
RLP7_YEAST	RLP7	physical	25404745
RL4A_YEAST	RPL4A	physical	25404745
NSA2_YEAST	NSA2	physical	25404745
NOP15_YEAST	NOP15	physical	25404745

Drug and Disease Associations

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

Regulatory Network of RL25_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-29, AND MASSSPECTROMETRY.	18407956 [Abstract]
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-59, AND MASSSPECTROMETRY.	17287358 [Abstract]
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASSSPECTROMETRY.	11875433 [Abstract]
Sumoylation
Reference	PubMed
"A proteomic strategy for gaining insights into protein sumoylation inyeast."; Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D.,Gygi S.P.; Mol. Cell. Proteomics 4:246-254(2005). Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-61, AND MASS SPECTROMETRY.	15542864 [Abstract]