dbPTM

RL35B_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL35B_YEAST
UniProt AC	P0CX85
Protein Name	60S ribosomal protein L35-B {ECO:0000303\|PubMed:9559554}
Gene Name	RPL35B {ECO:0000303\|PubMed:9559554}
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	120
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	MAGVKAYELRTKSKEQLASQLVDLKKELAELKVQKLSRPSLPKIKTVRKSIACVLTVINEQQREAVRQLYKGKKYQPKDLRAKKTRALRRALTKFEASQVTEKQRKKQIAFPQRKYAIKA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	VKAYELRTKSKEQLA CCHHHCCCCCHHHHH	52.90	30377154
13	Phosphorylation	AYELRTKSKEQLASQ HHHCCCCCHHHHHHH	40.59	21440633
14	Ubiquitination	YELRTKSKEQLASQL HHCCCCCHHHHHHHH	51.54	23749301
19	Phosphorylation	KSKEQLASQLVDLKK CCHHHHHHHHHHHHH	32.41	22369663
25	Ubiquitination	ASQLVDLKKELAELK HHHHHHHHHHHHHHH	39.47	23749301
26	Ubiquitination	SQLVDLKKELAELKV HHHHHHHHHHHHHHH	66.32	23749301
32	Ubiquitination	KKELAELKVQKLSRP HHHHHHHHHHHHCCC	33.84	23749301
35	Ubiquitination	LAELKVQKLSRPSLP HHHHHHHHHCCCCCC	51.95	22817900
37	Phosphorylation	ELKVQKLSRPSLPKI HHHHHHHCCCCCCCC	49.53	21440633
40	Phosphorylation	VQKLSRPSLPKIKTV HHHHCCCCCCCCHHH	57.08	22369663
45	Ubiquitination	RPSLPKIKTVRKSIA CCCCCCCHHHHHHHH	47.28	22817900
49	Ubiquitination	PKIKTVRKSIACVLT CCCHHHHHHHHHHHH	41.71	23749301
50	Phosphorylation	KIKTVRKSIACVLTV CCHHHHHHHHHHHHH	12.59	21440633
56	Phosphorylation	KSIACVLTVINEQQR HHHHHHHHHCCHHHH	10.03	30377154
73	Ubiquitination	VRQLYKGKKYQPKDL HHHHHCCCCCCCHHH	44.12	22817900
74	Ubiquitination	RQLYKGKKYQPKDLR HHHHCCCCCCCHHHH	58.76	22817900
78	Ubiquitination	KGKKYQPKDLRAKKT CCCCCCCHHHHHHHH	54.60	22817900
83	Ubiquitination	QPKDLRAKKTRALRR CCHHHHHHHHHHHHH	48.52	22817900
93	Phosphorylation	RALRRALTKFEASQV HHHHHHHHHHHHHHC	32.47	23749301
94	Ubiquitination	ALRRALTKFEASQVT HHHHHHHHHHHHHCC	41.90	23749301
98	Phosphorylation	ALTKFEASQVTEKQR HHHHHHHHHCCHHHH	20.27	23749301
101	Phosphorylation	KFEASQVTEKQRKKQ HHHHHHCCHHHHHHH	29.81	28889911
103	Ubiquitination	EASQVTEKQRKKQIA HHHHCCHHHHHHHCC	46.14	23749301

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 RL35B_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL35B_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 RL35B_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ARD1_YEAST	ARD1	physical	17541948
NACA_YEAST	EGD2	physical	26195668
RL13A_YEAST	RPL13A	physical	26195668

Drug and Disease Associations

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

Regulatory Network of RL35B_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-98, AND MASSSPECTROMETRY.	18407956 [Abstract]