RS31_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RS31_YEAST
• UniProt AC: P05759
• Protein Name: Ubiquitin-40S ribosomal protein S31
• Gene Name: RPS31 {ECO:0000303|PubMed:24524803}
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 152
• Subcellular Localization: Ubiquitin: Cytoplasm. Nucleus.; 40S ribosomal protein S31: Cytoplasm .
• Protein Description: Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).; 40S ribosomal protein S31: 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: MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGGKKRKKKVYTTPKKIKHKHKKVKLAVLSYYKVDAEGKVTKLRRECSNPTCGAGVFLANHKDRLYCGKCHSVYKVNA

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
6	2-Hydroxyisobutyrylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE		-
6	Ubiquitination	--MQIFVKTLTGKTI --CEEEEEECCCCEE		23749301
11	Ubiquitination	FVKTLTGKTITLEVE EEEECCCCEEEEEEE		23749301
12	Phosphorylation	VKTLTGKTITLEVES EEECCCCEEEEEEEC		23749301
14	Phosphorylation	TLTGKTITLEVESSD ECCCCEEEEEEECCC		23749301
19	Phosphorylation	TITLEVESSDTIDNV EEEEEEECCCCHHHH		23749301
22	Phosphorylation	LEVESSDTIDNVKSK EEEECCCCHHHHHHH		23749301
27	Succinylation	SDTIDNVKSKIQDKE CCCHHHHHHHCCCCC		23954790
27	Ubiquitination	SDTIDNVKSKIQDKE CCCHHHHHHHCCCCC		23749301
29	2-Hydroxyisobutyrylation	TIDNVKSKIQDKEGI CHHHHHHHCCCCCCC		-
29	Ubiquitination	TIDNVKSKIQDKEGI CHHHHHHHCCCCCCC		22817900
33	Ubiquitination	VKSKIQDKEGIPPDQ HHHHCCCCCCCCHHH		23749301
33	Acetylation	VKSKIQDKEGIPPDQ HHHHCCCCCCCCHHH		24489116
33	2-Hydroxyisobutyrylation	VKSKIQDKEGIPPDQ HHHHCCCCCCCCHHH		-
48	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC		23749301
48	Succinylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC		23954790
48	2-Hydroxyisobutyrylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC		-
48	Acetylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC		24489116
55	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC		22369663
57	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH		22369663
59	Phosphorylation	DGRTLSDYNIQKEST CCCCCCCCCCCCHHE		22369663
63	Succinylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE		23954790
63	Acetylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE		24489116
63	Ubiquitination	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE		23749301
65	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE		23749301
66	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE		23749301
78	Ubiquitination	LRLRGGGKKRKKKVY EEECCCCCCCCCEEE		22817900
79	Ubiquitination	RLRGGGKKRKKKVYT EECCCCCCCCCEEEC		22817900
81	Ubiquitination	RGGGKKRKKKVYTTP CCCCCCCCCEEECCC		22817900
82	Ubiquitination	GGGKKRKKKVYTTPK CCCCCCCCEEECCCH		22817900
83	Ubiquitination	GGKKRKKKVYTTPKK CCCCCCCEEECCCHH		22817900
85	Phosphorylation	KKRKKKVYTTPKKIK CCCCCEEECCCHHHC		28889911
86	Phosphorylation	KRKKKVYTTPKKIKH CCCCEEECCCHHHCC		23749301
87	Phosphorylation	RKKKVYTTPKKIKHK CCCEEECCCHHHCCC		16445868
89	Acetylation	KKVYTTPKKIKHKHK CEEECCCHHHCCCCC		25381059
89	Succinylation	KKVYTTPKKIKHKHK CEEECCCHHHCCCCC		23954790
94	Ubiquitination	TPKKIKHKHKKVKLA CCHHHCCCCCCCEEE		22817900
96	Ubiquitination	KKIKHKHKKVKLAVL HHHCCCCCCCEEEEE		22817900
97	Ubiquitination	KIKHKHKKVKLAVLS HHCCCCCCCEEEEEE		22817900
99	Ubiquitination	KHKHKKVKLAVLSYY CCCCCCCEEEEEEEE		23749301
99	Acetylation	KHKHKKVKLAVLSYY CCCCCCCEEEEEEEE		24489116
99	2-Hydroxyisobutyrylation	KHKHKKVKLAVLSYY CCCCCCCEEEEEEEE		-
104	Phosphorylation	KVKLAVLSYYKVDAE CCEEEEEEEEEECCC		22369663
105	Phosphorylation	VKLAVLSYYKVDAEG CEEEEEEEEEECCCC		23749301
106	Phosphorylation	KLAVLSYYKVDAEGK EEEEEEEEEECCCCC		22369663
107	Succinylation	LAVLSYYKVDAEGKV EEEEEEEEECCCCCE		23954790
107	Acetylation	LAVLSYYKVDAEGKV EEEEEEEEECCCCCE		24489116
107	2-Hydroxyisobutyrylation	LAVLSYYKVDAEGKV EEEEEEEEECCCCCE		-
107	Ubiquitination	LAVLSYYKVDAEGKV EEEEEEEEECCCCCE		23749301
113	2-Hydroxyisobutyrylation	YKVDAEGKVTKLRRE EEECCCCCEEEEHHH		-
113	Ubiquitination	YKVDAEGKVTKLRRE EEECCCCCEEEEHHH		23749301
115	Phosphorylation	VDAEGKVTKLRRECS ECCCCCEEEEHHHCC		23749301
116	2-Hydroxyisobutyrylation	DAEGKVTKLRRECSN CCCCCEEEEHHHCCC		-
116	Ubiquitination	DAEGKVTKLRRECSN CCCCCEEEEHHHCCC		22817900
122	Phosphorylation	TKLRRECSNPTCGAG EEEHHHCCCCCCCCC		21082442
125	Phosphorylation	RRECSNPTCGAGVFL HHHCCCCCCCCCEEE		19779198
136	Acetylation	GVFLANHKDRLYCGK CEEEECCCCCEEECC		24489116
136	Ubiquitination	GVFLANHKDRLYCGK CEEEECCCCCEEECC		23749301
143	Acetylation	KDRLYCGKCHSVYKV CCCEEECCCCEEEEE		25381059
143	Ubiquitination	KDRLYCGKCHSVYKV CCCEEECCCCEEEEE		23749301
146	Phosphorylation	LYCGKCHSVYKVNA- EEECCCCEEEEECC-		21440633
149	Ubiquitination	GKCHSVYKVNA---- CCCCEEEEECC----		23749301

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

Oops, there are no upstream regulatory protein records of RS31_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RS31_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 RS31_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RS31_YEAST	RPS31	physical	19210616
CACO2_HUMAN	CALCOCO2	physical	27107014

Drug and Disease Associations

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