dbPTM

RL32_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL32_YEAST
UniProt AC	P38061
Protein Name	60S ribosomal protein L32 {ECO:0000303\|PubMed:9559554}
Gene Name	RPL32 {ECO:0000303\|PubMed:9559554}
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	130
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	MASLPHPKIVKKHTKKFKRHHSDRYHRVAENWRKQKGIDSVVRRRFRGNISQPKIGYGSNKKTKFLSPSGHKTFLVANVKDLETLTMHTKTYAAEIAHNISAKNRVVILARAKALGIKVTNPKGRLALEA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MASLPHPKIV -----CCCCCCHHHH	40.93	19795423
34	Ubiquitination	RVAENWRKQKGIDSV HHHHHHHHHCCCCHH	48.23	22817900
36	Ubiquitination	AENWRKQKGIDSVVR HHHHHHHCCCCHHHH	61.95	22817900
36	2-Hydroxyisobutyrylation	AENWRKQKGIDSVVR HHHHHHHCCCCHHHH	61.95	-
36	Acetylation	AENWRKQKGIDSVVR HHHHHHHCCCCHHHH	61.95	24489116
40	Phosphorylation	RKQKGIDSVVRRRFR HHHCCCCHHHHHHHC	22.16	17287358
51	Phosphorylation	RRFRGNISQPKIGYG HHHCCCCCCCCCCCC	44.42	23749301
54	Ubiquitination	RGNISQPKIGYGSNK CCCCCCCCCCCCCCC	40.92	23749301
59	Phosphorylation	QPKIGYGSNKKTKFL CCCCCCCCCCCCEEE	36.67	23749301
61	Ubiquitination	KIGYGSNKKTKFLSP CCCCCCCCCCEEECC	64.61	23749301
61	Succinylation	KIGYGSNKKTKFLSP CCCCCCCCCCEEECC	64.61	23954790
61	Acetylation	KIGYGSNKKTKFLSP CCCCCCCCCCEEECC	64.61	25381059
62	Ubiquitination	IGYGSNKKTKFLSPS CCCCCCCCCEEECCC	62.29	22817900
64	Acetylation	YGSNKKTKFLSPSGH CCCCCCCEEECCCCC	53.86	24489116
64	Ubiquitination	YGSNKKTKFLSPSGH CCCCCCCEEECCCCC	53.86	23749301
67	Phosphorylation	NKKTKFLSPSGHKTF CCCCEEECCCCCCEE	21.83	22369663
69	Phosphorylation	KTKFLSPSGHKTFLV CCEEECCCCCCEEEE	50.59	22369663
72	Acetylation	FLSPSGHKTFLVANV EECCCCCCEEEEEEC	44.49	24489116
72	Succinylation	FLSPSGHKTFLVANV EECCCCCCEEEEEEC	44.49	23954790
72	Ubiquitination	FLSPSGHKTFLVANV EECCCCCCEEEEEEC	44.49	24961812
73	Phosphorylation	LSPSGHKTFLVANVK ECCCCCCEEEEEECC	19.27	21440633
80	Acetylation	TFLVANVKDLETLTM EEEEEECCCHHHHCC	57.30	24489116
80	Succinylation	TFLVANVKDLETLTM EEEEEECCCHHHHCC	57.30	23954790
80	Ubiquitination	TFLVANVKDLETLTM EEEEEECCCHHHHCC	57.30	23749301
84	Phosphorylation	ANVKDLETLTMHTKT EECCCHHHHCCCCHH	34.52	23749301
86	Phosphorylation	VKDLETLTMHTKTYA CCCHHHHCCCCHHHH	17.83	21440633
89	Phosphorylation	LETLTMHTKTYAAEI HHHHCCCCHHHHHHH	17.79	21440633
90	Ubiquitination	ETLTMHTKTYAAEIA HHHCCCCHHHHHHHH	25.51	23749301
90	Acetylation	ETLTMHTKTYAAEIA HHHCCCCHHHHHHHH	25.51	24489116
91	Phosphorylation	TLTMHTKTYAAEIAH HHCCCCHHHHHHHHH	21.39	22369663
92	Phosphorylation	LTMHTKTYAAEIAHN HCCCCHHHHHHHHHH	12.84	21440633
101	Phosphorylation	AEIAHNISAKNRVVI HHHHHHCCCCCCEEE	38.21	21440633
103	Ubiquitination	IAHNISAKNRVVILA HHHHCCCCCCEEEEE	38.20	23749301
103	Acetylation	IAHNISAKNRVVILA HHHHCCCCCCEEEEE	38.20	24489116
103	2-Hydroxyisobutyrylation	IAHNISAKNRVVILA HHHHCCCCCCEEEEE	38.20	-
103	Succinylation	IAHNISAKNRVVILA HHHHCCCCCCEEEEE	38.20	23954790
113	Ubiquitination	VVILARAKALGIKVT EEEEEEHHHHCCEEE	38.29	22817900
113	2-Hydroxyisobutyrylation	VVILARAKALGIKVT EEEEEEHHHHCCEEE	38.29	-
118	Ubiquitination	RAKALGIKVTNPKGR EHHHHCCEEECCCCC	41.00	22817900
118	2-Hydroxyisobutyrylation	RAKALGIKVTNPKGR EHHHHCCEEECCCCC	41.00	-
123	Ubiquitination	GIKVTNPKGRLALEA CCEEECCCCCEEECC	59.75	22817900
123	Succinylation	GIKVTNPKGRLALEA CCEEECCCCCEEECC	59.75	23954790

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 RL32_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL32_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 RL32_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RL32_YEAST !!

Drug and Disease Associations

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

Regulatory Network of RL32_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-40 AND SER-51, 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-40, AND MASSSPECTROMETRY.	17287358 [Abstract]