dbPTM

RL13B_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL13B_YEAST
UniProt AC	P40212
Protein Name	60S ribosomal protein L13-B {ECO:0000303\|PubMed:9559554}
Gene Name	RPL13B {ECO:0000303\|PubMed:9559554}
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	199
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	MAISKNLPILKNHFRKHWQERVKVHFDQAGKKVSRRNARAARAAKIAPRPLDLLRPVVRAPTVKYNRKVRAGRGFTLAEVKAAGLTAAYARTIGIAVDHRRQNRNQEIFDANVQRLKEYQSKIIVFPRDGKAPEAEQVLSAAATFPIAQPATDVEARAVQDNGESAFRTLRLARSEKKFRGIREKRAREKAEAEAEKKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Ubiquitination	---MAISKNLPILKN ---CCCCCCCHHHHH	57.29	24961812
11	Succinylation	SKNLPILKNHFRKHW CCCCHHHHHHHHHHH	49.44	23954790
11	Acetylation	SKNLPILKNHFRKHW CCCCHHHHHHHHHHH	49.44	24489116
31	2-Hydroxyisobutyrylation	VHFDQAGKKVSRRNA HHHHHHCCHHHHHHH	53.68	-
31	Succinylation	VHFDQAGKKVSRRNA HHHHHHCCHHHHHHH	53.68	23954790
31	Ubiquitination	VHFDQAGKKVSRRNA HHHHHHCCHHHHHHH	53.68	22817900
31	Acetylation	VHFDQAGKKVSRRNA HHHHHHCCHHHHHHH	53.68	24489116
32	Ubiquitination	HFDQAGKKVSRRNAR HHHHHCCHHHHHHHH	44.52	22817900
45	Ubiquitination	ARAARAAKIAPRPLD HHHHHHHHHCCCCHH	38.11	23749301
62	Phosphorylation	RPVVRAPTVKYNRKV HCCCCCCCCCCCCEE	28.75	20377248
64	Acetylation	VVRAPTVKYNRKVRA CCCCCCCCCCCEECC	39.01	24489116
64	Ubiquitination	VVRAPTVKYNRKVRA CCCCCCCCCCCEECC	39.01	23749301
64	2-Hydroxyisobutyrylation	VVRAPTVKYNRKVRA CCCCCCCCCCCEECC	39.01	-
68	Ubiquitination	PTVKYNRKVRAGRGF CCCCCCCEECCCCCC	32.22	22817900
76	Phosphorylation	VRAGRGFTLAEVKAA ECCCCCCCHHHHHHH	28.07	22369663
81	Succinylation	GFTLAEVKAAGLTAA CCCHHHHHHHCHHHH	24.83	23954790
81	Ubiquitination	GFTLAEVKAAGLTAA CCCHHHHHHHCHHHH	24.83	23749301
81	Acetylation	GFTLAEVKAAGLTAA CCCHHHHHHHCHHHH	24.83	24489116
86	Phosphorylation	EVKAAGLTAAYARTI HHHHHCHHHHHHHHH	14.34	21440633
89	Phosphorylation	AAGLTAAYARTIGIA HHCHHHHHHHHHCHH	8.31	21082442
117	Acetylation	DANVQRLKEYQSKII HHHHHHHHHHHCCEE	57.47	24489116
117	Succinylation	DANVQRLKEYQSKII HHHHHHHHHHHCCEE	57.47	23954790
117	Ubiquitination	DANVQRLKEYQSKII HHHHHHHHHHHCCEE	57.47	23749301
122	Ubiquitination	RLKEYQSKIIVFPRD HHHHHHCCEEEECCC	22.41	24961812
122	2-Hydroxyisobutyrylation	RLKEYQSKIIVFPRD HHHHHHCCEEEECCC	22.41	-
122	Acetylation	RLKEYQSKIIVFPRD HHHHHHCCEEEECCC	22.41	24489116
131	Ubiquitination	IVFPRDGKAPEAEQV EEECCCCCCCHHHHH	66.12	23749301
131	Acetylation	IVFPRDGKAPEAEQV EEECCCCCCCHHHHH	66.12	24489116
140	Phosphorylation	PEAEQVLSAAATFPI CHHHHHHHHHHCCCC	19.60	22369663
144	Phosphorylation	QVLSAAATFPIAQPA HHHHHHHCCCCCCCC	25.80	22890988
152	Phosphorylation	FPIAQPATDVEARAV CCCCCCCCHHHHHHH	47.46	22369663
165	Phosphorylation	AVQDNGESAFRTLRL HHHCCCHHHHHHHHH	33.82	22369663
169	Phosphorylation	NGESAFRTLRLARSE CCHHHHHHHHHHHCH	15.13	24961812
175	Phosphorylation	RTLRLARSEKKFRGI HHHHHHHCHHHHHHH	48.43	24961812
190	Acetylation	REKRAREKAEAEAEK HHHHHHHHHHHHHHH	46.07	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 RL13B_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL13B_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 RL13B_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RL13B_YEAST !!

Drug and Disease Associations

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

Regulatory Network of RL13B_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND MASSSPECTROMETRY.	15665377 [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 THR-62, AND MASSSPECTROMETRY.	17287358 [Abstract]