UniProt ID | RL16A_YEAST | |
---|---|---|
UniProt AC | P26784 | |
Protein Name | 60S ribosomal protein L16-A {ECO:0000303|PubMed:14562095} | |
Gene Name | RPL16A {ECO:0000303|PubMed:14562095} | |
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 | MSVEPVVVIDGKGHLVGRLASVVAKQLLNGQKIVVVRAEELNISGEFFRNKLKYHDFLRKATAFNKTRGPFHFRAPSRIFYKALRGMVSHKTARGKAALERLKVFEGIPPPYDKKKRVVVPQALRVLRLKPGRKYTTLGKLSTSVGWKYEDVVAKLEAKRKVSSAEYYAKKRAFTKKVASANATAAESDVAKQLAALGY | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSVEPVVVI ------CCCCCEEEE | 34.88 | 27717283 | |
2 | Acetylation | ------MSVEPVVVI ------CCCCCEEEE | 34.88 | 1544921 | |
12 | Acetylation | PVVVIDGKGHLVGRL CEEEECCCCCHHHHH | 39.13 | 24489116 | |
12 | Ubiquitination | PVVVIDGKGHLVGRL CEEEECCCCCHHHHH | 39.13 | 24961812 | |
21 | Phosphorylation | HLVGRLASVVAKQLL CHHHHHHHHHHHHHH | 23.01 | 21440633 | |
25 | Acetylation | RLASVVAKQLLNGQK HHHHHHHHHHHCCCE | 29.84 | 24489116 | |
25 | Ubiquitination | RLASVVAKQLLNGQK HHHHHHHHHHHCCCE | 29.84 | 23749301 | |
32 | Acetylation | KQLLNGQKIVVVRAE HHHHCCCEEEEEEEE | 38.58 | 24489116 | |
51 | Ubiquitination | SGEFFRNKLKYHDFL CHHHHHHHHHHHHHH | 41.94 | 22817900 | |
53 | 2-Hydroxyisobutyrylation | EFFRNKLKYHDFLRK HHHHHHHHHHHHHHH | 41.99 | - | |
53 | Acetylation | EFFRNKLKYHDFLRK HHHHHHHHHHHHHHH | 41.99 | 24489116 | |
53 | Ubiquitination | EFFRNKLKYHDFLRK HHHHHHHHHHHHHHH | 41.99 | 23749301 | |
60 | 2-Hydroxyisobutyrylation | KYHDFLRKATAFNKT HHHHHHHHHHHCCCC | 52.84 | - | |
66 | 2-Hydroxyisobutyrylation | RKATAFNKTRGPFHF HHHHHCCCCCCCCCC | 32.90 | - | |
66 | Ubiquitination | RKATAFNKTRGPFHF HHHHHCCCCCCCCCC | 32.90 | 23749301 | |
66 | Acetylation | RKATAFNKTRGPFHF HHHHHCCCCCCCCCC | 32.90 | 24489116 | |
82 | Acetylation | APSRIFYKALRGMVS CCHHHHHHHHHHHHC | 30.14 | 24489116 | |
91 | 2-Hydroxyisobutyrylation | LRGMVSHKTARGKAA HHHHHCCCHHHCHHH | 36.05 | - | |
91 | Ubiquitination | LRGMVSHKTARGKAA HHHHHCCCHHHCHHH | 36.05 | 23749301 | |
103 | Acetylation | KAALERLKVFEGIPP HHHHHHHHHCCCCCC | 51.61 | 24489116 | |
114 | Acetylation | GIPPPYDKKKRVVVP CCCCCCCCCCCEECC | 55.11 | 24489116 | |
114 | Succinylation | GIPPPYDKKKRVVVP CCCCCCCCCCCEECC | 55.11 | 23954790 | |
114 | Ubiquitination | GIPPPYDKKKRVVVP CCCCCCCCCCCEECC | 55.11 | 22817900 | |
115 | Ubiquitination | IPPPYDKKKRVVVPQ CCCCCCCCCCEECCH | 42.80 | 22817900 | |
116 | Ubiquitination | PPPYDKKKRVVVPQA CCCCCCCCCEECCHH | 57.05 | 22817900 | |
130 | Ubiquitination | ALRVLRLKPGRKYTT HHHHHCCCCCCCEEE | 38.70 | 22817900 | |
134 | Ubiquitination | LRLKPGRKYTTLGKL HCCCCCCCEEECCCC | 53.52 | 23749301 | |
134 | Acetylation | LRLKPGRKYTTLGKL HCCCCCCCEEECCCC | 53.52 | 25381059 | |
136 | Phosphorylation | LKPGRKYTTLGKLST CCCCCCEEECCCCCC | 20.69 | 27214570 | |
137 | Phosphorylation | KPGRKYTTLGKLSTS CCCCCEEECCCCCCC | 30.35 | 30377154 | |
140 | Ubiquitination | RKYTTLGKLSTSVGW CCEEECCCCCCCCCC | 42.23 | 23749301 | |
140 | Acetylation | RKYTTLGKLSTSVGW CCEEECCCCCCCCCC | 42.23 | 24489116 | |
144 | Phosphorylation | TLGKLSTSVGWKYED ECCCCCCCCCCCHHH | 18.43 | 21440633 | |
148 | Acetylation | LSTSVGWKYEDVVAK CCCCCCCCHHHHHHH | 32.60 | 24489116 | |
148 | Methylation | LSTSVGWKYEDVVAK CCCCCCCCHHHHHHH | 32.60 | 20137074 | |
155 | Acetylation | KYEDVVAKLEAKRKV CHHHHHHHHHHHHCC | 34.94 | 24489116 | |
155 | Ubiquitination | KYEDVVAKLEAKRKV CHHHHHHHHHHHHCC | 34.94 | 23749301 | |
155 | Succinylation | KYEDVVAKLEAKRKV CHHHHHHHHHHHHCC | 34.94 | 23954790 | |
159 | Ubiquitination | VVAKLEAKRKVSSAE HHHHHHHHHCCCHHH | 43.29 | 22817900 | |
161 | Ubiquitination | AKLEAKRKVSSAEYY HHHHHHHCCCHHHHH | 45.84 | 23749301 | |
161 | 2-Hydroxyisobutyrylation | AKLEAKRKVSSAEYY HHHHHHHCCCHHHHH | 45.84 | - | |
163 | Phosphorylation | LEAKRKVSSAEYYAK HHHHHCCCHHHHHHH | 27.19 | 23749301 | |
164 | Phosphorylation | EAKRKVSSAEYYAKK HHHHCCCHHHHHHHH | 28.27 | 28889911 | |
170 | Acetylation | SSAEYYAKKRAFTKK CHHHHHHHHHHHHHH | 27.03 | 24489116 | |
170 | Ubiquitination | SSAEYYAKKRAFTKK CHHHHHHHHHHHHHH | 27.03 | 23749301 | |
170 | Succinylation | SSAEYYAKKRAFTKK CHHHHHHHHHHHHHH | 27.03 | 23954790 | |
171 | Ubiquitination | SAEYYAKKRAFTKKV HHHHHHHHHHHHHHH | 40.56 | 22817900 | |
176 | Ubiquitination | AKKRAFTKKVASANA HHHHHHHHHHHHCCC | 38.50 | 22817900 | |
177 | Ubiquitination | KKRAFTKKVASANAT HHHHHHHHHHHCCCC | 39.72 | 23749301 | |
180 | Phosphorylation | AFTKKVASANATAAE HHHHHHHHCCCCHHH | 25.66 | 21440633 | |
188 | Phosphorylation | ANATAAESDVAKQLA CCCCHHHHHHHHHHH | 32.43 | 24909858 | |
192 | Acetylation | AAESDVAKQLAALGY HHHHHHHHHHHHCCC | 45.77 | 24489116 | |
192 | Ubiquitination | AAESDVAKQLAALGY HHHHHHHHHHHHCCC | 45.77 | 23749301 |
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 RL16A_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RL16A_YEAST !! |
* 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 RL16A_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...