UniProt ID | RL13_HUMAN | |
---|---|---|
UniProt AC | P26373 | |
Protein Name | 60S ribosomal protein L13 | |
Gene Name | RPL13 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 211 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MAPSRNGMVLKPHFHKDWQRRVATWFNQPARKIRRRKARQAKARRIAPRPASGPIRPIVRCPTVRYHTKVRAGRGFSLEELRVAGIHKKVARTIGISVDPRRRNKSTESLQANVQRLKEYRSKLILFPRKPSAPKKGDSSAEELKLATQLTGPVMPVRNVYKKEKARVITEEEKNFKAFASLRMARANARLFGIRAKRAKEAAEQDVEKKK | |
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 |
---|---|---|---|---|---|
11 | Acetylation | SRNGMVLKPHFHKDW CCCCEEECCCCCHHH | 25.65 | 25953088 | |
11 | Ubiquitination | SRNGMVLKPHFHKDW CCCCEEECCCCCHHH | 25.65 | - | |
16 | Ubiquitination | VLKPHFHKDWQRRVA EECCCCCHHHHHHHH | 60.77 | 19608861 | |
16 | Acetylation | VLKPHFHKDWQRRVA EECCCCCHHHHHHHH | 60.77 | 19608861 | |
52 | Phosphorylation | RIAPRPASGPIRPIV HHCCCCCCCCCCCCE | 48.02 | 23403867 | |
74 | Methylation | HTKVRAGRGFSLEEL ECCCCCCCCCCHHHH | 41.83 | 54558869 | |
77 | Phosphorylation | VRAGRGFSLEELRVA CCCCCCCCHHHHHHC | 37.38 | 23927012 | |
82 | Methylation | GFSLEELRVAGIHKK CCCHHHHHHCCHHHH | 21.37 | 115491663 | |
88 | 2-Hydroxyisobutyrylation | LRVAGIHKKVARTIG HHHCCHHHHHHHHHC | 47.20 | - | |
88 | Ubiquitination | LRVAGIHKKVARTIG HHHCCHHHHHHHHHC | 47.20 | - | |
93 | Phosphorylation | IHKKVARTIGISVDP HHHHHHHHHCCCCCC | 17.51 | 20068231 | |
93 (in isoform 2) | Phosphorylation | - | 17.51 | 29743597 | |
97 | Phosphorylation | VARTIGISVDPRRRN HHHHHCCCCCCCCCC | 18.43 | 24670416 | |
101 | Methylation | IGISVDPRRRNKSTE HCCCCCCCCCCCCHH | 45.81 | 115491671 | |
105 | 2-Hydroxyisobutyrylation | VDPRRRNKSTESLQA CCCCCCCCCHHHHHH | 57.87 | - | |
105 | Ubiquitination | VDPRRRNKSTESLQA CCCCCCCCCHHHHHH | 57.87 | 21890473 | |
105 | Ubiquitination | VDPRRRNKSTESLQA CCCCCCCCCHHHHHH | 57.87 | 21890473 | |
105 | Acetylation | VDPRRRNKSTESLQA CCCCCCCCCHHHHHH | 57.87 | 26051181 | |
106 | Phosphorylation | DPRRRNKSTESLQAN CCCCCCCCHHHHHHH | 40.74 | 22167270 | |
107 | Phosphorylation | PRRRNKSTESLQANV CCCCCCCHHHHHHHH | 31.07 | 30266825 | |
109 | Phosphorylation | RRNKSTESLQANVQR CCCCCHHHHHHHHHH | 26.35 | 30266825 | |
122 | Phosphorylation | QRLKEYRSKLILFPR HHHHHHHHHEEEECC | 30.80 | - | |
123 | Ubiquitination | RLKEYRSKLILFPRK HHHHHHHHEEEECCC | 30.46 | 21890473 | |
123 | 2-Hydroxyisobutyrylation | RLKEYRSKLILFPRK HHHHHHHHEEEECCC | 30.46 | - | |
123 | Sumoylation | RLKEYRSKLILFPRK HHHHHHHHEEEECCC | 30.46 | 28112733 | |
123 | Sumoylation | RLKEYRSKLILFPRK HHHHHHHHEEEECCC | 30.46 | - | |
123 | Ubiquitination | RLKEYRSKLILFPRK HHHHHHHHEEEECCC | 30.46 | 21890473 | |
123 | Acetylation | RLKEYRSKLILFPRK HHHHHHHHEEEECCC | 30.46 | 25953088 | |
130 | Acetylation | KLILFPRKPSAPKKG HEEEECCCCCCCCCC | 43.49 | 19608861 | |
130 | Ubiquitination | KLILFPRKPSAPKKG HEEEECCCCCCCCCC | 43.49 | 19608861 | |
132 | Phosphorylation | ILFPRKPSAPKKGDS EEECCCCCCCCCCCC | 61.31 | 20860994 | |
136 | Acetylation | RKPSAPKKGDSSAEE CCCCCCCCCCCCHHH | 67.88 | 25953088 | |
136 | Ubiquitination | RKPSAPKKGDSSAEE CCCCCCCCCCCCHHH | 67.88 | 21890473 | |
139 | Phosphorylation | SAPKKGDSSAEELKL CCCCCCCCCHHHHHH | 39.87 | 29255136 | |
140 | Phosphorylation | APKKGDSSAEELKLA CCCCCCCCHHHHHHH | 44.43 | 29255136 | |
145 | Sumoylation | DSSAEELKLATQLTG CCCHHHHHHHHHCCC | 39.08 | 28112733 | |
145 | Acetylation | DSSAEELKLATQLTG CCCHHHHHHHHHCCC | 39.08 | 25953088 | |
145 | Ubiquitination | DSSAEELKLATQLTG CCCHHHHHHHHHCCC | 39.08 | 21890473 | |
148 | Phosphorylation | AEELKLATQLTGPVM HHHHHHHHHCCCCCC | 34.25 | 30108239 | |
151 | Phosphorylation | LKLATQLTGPVMPVR HHHHHHCCCCCCCCC | 29.62 | 30108239 | |
155 | Sulfoxidation | TQLTGPVMPVRNVYK HHCCCCCCCCCCCCH | 2.60 | 28465586 | |
158 | Acetylation | TGPVMPVRNVYKKEK CCCCCCCCCCCHHHH | 22.49 | 19608861 | |
158 | Ubiquitination | TGPVMPVRNVYKKEK CCCCCCCCCCCHHHH | 22.49 | 19608861 | |
162 | Sumoylation | MPVRNVYKKEKARVI CCCCCCCHHHHCEEE | 50.61 | - | |
170 | Phosphorylation | KEKARVITEEEKNFK HHHCEEECHHHHHHH | 34.19 | - | |
174 | Ubiquitination | RVITEEEKNFKAFAS EEECHHHHHHHHHHH | 71.60 | 21890473 | |
174 | Sumoylation | RVITEEEKNFKAFAS EEECHHHHHHHHHHH | 71.60 | 25114211 | |
174 | Acetylation | RVITEEEKNFKAFAS EEECHHHHHHHHHHH | 71.60 | 23749302 | |
174 | Ubiquitination | RVITEEEKNFKAFAS EEECHHHHHHHHHHH | 71.60 | 21890473 | |
177 | Ubiquitination | TEEEKNFKAFASLRM CHHHHHHHHHHHHHH | 52.57 | 21890473 | |
177 | Ubiquitination | TEEEKNFKAFASLRM CHHHHHHHHHHHHHH | 52.57 | 21890473 | |
177 | Methylation | TEEEKNFKAFASLRM CHHHHHHHHHHHHHH | 52.57 | 19608861 | |
177 | Acetylation | TEEEKNFKAFASLRM CHHHHHHHHHHHHHH | 52.57 | 19608861 | |
177 | Sumoylation | TEEEKNFKAFASLRM CHHHHHHHHHHHHHH | 52.57 | - | |
177 | Sumoylation | TEEEKNFKAFASLRM CHHHHHHHHHHHHHH | 52.57 | 28112733 | |
181 | Phosphorylation | KNFKAFASLRMARAN HHHHHHHHHHHHHHH | 15.28 | 22199227 | |
200 | Acetylation | GIRAKRAKEAAEQDV CHHHHHHHHHHHHHH | 52.50 | 26051181 | |
200 | Ubiquitination | GIRAKRAKEAAEQDV CHHHHHHHHHHHHHH | 52.50 | 21890473 | |
200 | Methylation | GIRAKRAKEAAEQDV CHHHHHHHHHHHHHH | 52.50 | 21679131 | |
210 | Acetylation | AEQDVEKKK------ HHHHHHHCC------ | 50.65 | 23749302 | |
211 | Acetylation | EQDVEKKK------- HHHHHHCC------- | 76.32 | 12435169 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RL13_HUMAN !! |
* 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 RL13_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16 AND LYS-177, AND MASSSPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-106, AND MASSSPECTROMETRY. | |
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY. |