RS27B_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RS27B_YEAST
• UniProt AC: P38711
• Protein Name: 40S ribosomal protein S27-B {ECO:0000303|PubMed:9559554}
• Gene Name: RPS27B {ECO:0000303|PubMed:9559554}
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 82
• 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..
• Protein Sequence: MVLVQDLLHPTAASEARKHKLKTLVQGPRSYFLDVKCPGCLNITTVFSHAQTAVTCESCSTVLCTPTGGKAKLSEGTSFRRK

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
11	Phosphorylation	VQDLLHPTAASEARK CCCCCCHHHHHHHHH	24.90	28889911
14	Phosphorylation	LLHPTAASEARKHKL CCCHHHHHHHHHHHH	29.35	28889911
18	Ubiquitination	TAASEARKHKLKTLV HHHHHHHHHHHHHHH	52.73	22817900
20	Ubiquitination	ASEARKHKLKTLVQG HHHHHHHHHHHHHCC	55.50	22817900
22	Ubiquitination	EARKHKLKTLVQGPR HHHHHHHHHHHCCCC	44.62	23749301
23	Phosphorylation	ARKHKLKTLVQGPRS HHHHHHHHHHCCCCC	42.47	22369663
30	Phosphorylation	TLVQGPRSYFLDVKC HHHCCCCCEECCCCC	24.30	28889911
31	Phosphorylation	LVQGPRSYFLDVKCP HHCCCCCEECCCCCC	14.94	21440633
36	Ubiquitination	RSYFLDVKCPGCLNI CCEECCCCCCCCEEE	34.09	15699485
70	Ubiquitination	LCTPTGGKAKLSEGT EECCCCCCEECCCCC	43.63	22817900
72	Ubiquitination	TPTGGKAKLSEGTSF CCCCCCEECCCCCCC	56.91	23749301
74	Phosphorylation	TGGKAKLSEGTSFRR CCCCEECCCCCCCCC	33.02	22369663
77	Phosphorylation	KAKLSEGTSFRRK-- CEECCCCCCCCCC--	22.20	22369663
78	Phosphorylation	AKLSEGTSFRRK--- EECCCCCCCCCC---	27.84	21440633

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

Oops, there are no upstream regulatory protein records of RS27B_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RS27B_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 RS27B_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RS8A_YEAST	RPS8A	genetic	27708008
RS8B_YEAST	RPS8A	genetic	27708008
DBP7_YEAST	DBP7	genetic	27708008
THTR_YEAST	TUM1	genetic	27708008
SNC2_YEAST	SNC2	genetic	27708008
PUT4_YEAST	PUT4	genetic	27708008
AP3D_YEAST	APL5	genetic	27708008
TREB_YEAST	NTH2	genetic	27708008
RCR1_YEAST	RCR1	genetic	27708008
TPS1_YEAST	TPS1	genetic	27708008
CCZ1_YEAST	CCZ1	genetic	27708008
UBX3_YEAST	UBX3	genetic	27708008
IME1_YEAST	IME1	genetic	27708008
FKBP_YEAST	FPR1	genetic	27708008
YNO0_YEAST	YNL140C	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-14 AND THR-77, AND MASSSPECTROMETRY.
PubMed: 18407956