RL14A_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL14A_YEAST
• UniProt AC: P36105
• Protein Name: 60S ribosomal protein L14-A {ECO:0000303|PubMed:9559554}
• Gene Name: RPL14A {ECO:0000303|PubMed:9559554}
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 138
• 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: MSTDSIVKASNWRLVEVGRVVLIKKGQSAGKLAAIVEIIDQKKVLIDGPKAGVPRQAINLGQVVLTPLTFALPRGARTATVSKKWAAAAVCEKWAASSWAKKIAQRERRAALTDFERFQVMVLRKQKRYTVKKALAKA

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
2	Phosphorylation	------MSTDSIVKA ------CCHHHHHHH	40.70	19795423
2	Acetylation	------MSTDSIVKA ------CCHHHHHHH	40.70	10601260
3	Phosphorylation	-----MSTDSIVKAS -----CCHHHHHHHC	32.25	19795423
5	Phosphorylation	---MSTDSIVKASNW ---CCHHHHHHHCCE	29.39	19795423
8	Acetylation	MSTDSIVKASNWRLV CCHHHHHHHCCEEEE	44.41	24489116
8	Ubiquitination	MSTDSIVKASNWRLV CCHHHHHHHCCEEEE	44.41	24961812
8	Succinylation	MSTDSIVKASNWRLV CCHHHHHHHCCEEEE	44.41	23954790
8	2-Hydroxyisobutyrylation	MSTDSIVKASNWRLV CCHHHHHHHCCEEEE	44.41	-
10	Phosphorylation	TDSIVKASNWRLVEV HHHHHHHCCEEEEEE	31.07	17287358
31	Ubiquitination	KKGQSAGKLAAIVEI ECCCCCCHHHHHEEE	34.37	23749301
31	Acetylation	KKGQSAGKLAAIVEI ECCCCCCHHHHHEEE	34.37	24489116
42	Ubiquitination	IVEIIDQKKVLIDGP HEEEECCCCEEECCC	40.89	22817900
42	Succinylation	IVEIIDQKKVLIDGP HEEEECCCCEEECCC	40.89	23954790
42	Acetylation	IVEIIDQKKVLIDGP HEEEECCCCEEECCC	40.89	24489116
43	2-Hydroxyisobutyrylation	VEIIDQKKVLIDGPK EEEECCCCEEECCCC	36.32	-
43	Ubiquitination	VEIIDQKKVLIDGPK EEEECCCCEEECCCC	36.32	23749301
50	2-Hydroxyisobutyrylation	KVLIDGPKAGVPRQA CEEECCCCCCCCHHH	64.40	-
50	Ubiquitination	KVLIDGPKAGVPRQA CEEECCCCCCCCHHH	64.40	23749301
50	Acetylation	KVLIDGPKAGVPRQA CEEECCCCCCCCHHH	64.40	24489116
50	Succinylation	KVLIDGPKAGVPRQA CEEECCCCCCCCHHH	64.40	23954790
78	Phosphorylation	ALPRGARTATVSKKW ECCCCCCEEECCHHH	26.58	21440633
82	Phosphorylation	GARTATVSKKWAAAA CCCEEECCHHHHHHH	24.94	21440633
83	Ubiquitination	ARTATVSKKWAAAAV CCEEECCHHHHHHHH	48.26	22817900
83	Succinylation	ARTATVSKKWAAAAV CCEEECCHHHHHHHH	48.26	23954790
83	2-Hydroxyisobutyrylation	ARTATVSKKWAAAAV CCEEECCHHHHHHHH	48.26	-
84	Ubiquitination	RTATVSKKWAAAAVC CEEECCHHHHHHHHH	34.26	23749301
84	Acetylation	RTATVSKKWAAAAVC CEEECCHHHHHHHHH	34.26	25381059
93	Ubiquitination	AAAAVCEKWAASSWA HHHHHHHHHHHHHHH	36.69	23749301
93	Acetylation	AAAAVCEKWAASSWA HHHHHHHHHHHHHHH	36.69	24489116
97	Phosphorylation	VCEKWAASSWAKKIA HHHHHHHHHHHHHHH	20.75	22369663
98	Phosphorylation	CEKWAASSWAKKIAQ HHHHHHHHHHHHHHH	26.73	21440633
101	Succinylation	WAASSWAKKIAQRER HHHHHHHHHHHHHHH	38.15	23954790
101	Ubiquitination	WAASSWAKKIAQRER HHHHHHHHHHHHHHH	38.15	23749301
101	2-Hydroxyisobutyrylation	WAASSWAKKIAQRER HHHHHHHHHHHHHHH	38.15	-
101	Acetylation	WAASSWAKKIAQRER HHHHHHHHHHHHHHH	38.15	24489116
102	Ubiquitination	AASSWAKKIAQRERR HHHHHHHHHHHHHHH	35.21	22817900
127	Ubiquitination	VMVLRKQKRYTVKKA HHHHHHCCCHHHHHH	50.86	22817900
132	Ubiquitination	KQKRYTVKKALAKA- HCCCHHHHHHHHCC-	25.24	22817900
133	Ubiquitination	QKRYTVKKALAKA-- CCCHHHHHHHHCC--	44.27	22817900
137	Ubiquitination	TVKKALAKA------ HHHHHHHCC------	56.32	22817900

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

Oops, there are no upstream regulatory protein records of RL14A_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RL14A_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 RL14A_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UPPS_YEAST	NUS1	genetic	20101242
ACT_YEAST	ACT1	genetic	20101242
RPAB4_YEAST	RPC10	genetic	20101242
TCPB_YEAST	CCT2	genetic	20101242
RS5_YEAST	RPS5	genetic	20101242
SEC23_YEAST	SEC23	genetic	20101242
RL14B_YEAST	RPL14B	genetic	22377630

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"The action of N-terminal acetyltransferases on yeast ribosomalproteins.";
Arnold R.J., Polevoda B., Reilly J.P., Sherman F.;
J. Biol. Chem. 274:37035-37040(1999).
Cited for: CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2 BY NATA.
PubMed: 10601260