| UniProt ID | RL10_HUMAN | |
|---|---|---|
| UniProt AC | P27635 | |
| Protein Name | 60S ribosomal protein L10 {ECO:0000305} | |
| Gene Name | RPL10 {ECO:0000312|HGNC:HGNC:10298} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 214 | |
| Subcellular Localization | ||
| Protein Description | Component of the large ribosomal subunit. [PubMed: 26290468 Plays a role in the formation of actively translating ribosomes] | |
| Protein Sequence | MGRRPARCYRYCKNKPYPKSRFCRGVPDAKIRIFDLGRKKAKVDEFPLCGHMVSDEYEQLSSEALEAARICANKYMVKSCGKDGFHIRVRLHPFHVIRINKMLSCAGADRLQTGMRGAFGKPQGTVARVHIGQVIMSIRTKLQNKEHVIEALRRAKFKFPGRQKIHISKKWGFTKFNADEFEDMVAEKRLIPDGCGVKYIPNRGPLDKWRALHS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 9 | Phosphorylation | GRRPARCYRYCKNKP CCCCHHHHHHHCCCC | 10.08 | 20068231 | |
| 13 | Ubiquitination | ARCYRYCKNKPYPKS HHHHHHHCCCCCCHH | 60.10 | - | |
| 17 | Phosphorylation | RYCKNKPYPKSRFCR HHHCCCCCCHHHCCC | 25.54 | - | |
| 19 | Ubiquitination | CKNKPYPKSRFCRGV HCCCCCCHHHCCCCC | 48.71 | - | |
| 24 | Methylation | YPKSRFCRGVPDAKI CCHHHCCCCCCCCEE | 46.56 | - | |
| 30 | Sumoylation | CRGVPDAKIRIFDLG CCCCCCCEEEEEECC | 39.64 | - | |
| 30 | Ubiquitination | CRGVPDAKIRIFDLG CCCCCCCEEEEEECC | 39.64 | 21890473 | |
| 30 | 2-Hydroxyisobutyrylation | CRGVPDAKIRIFDLG CCCCCCCEEEEEECC | 39.64 | - | |
| 30 | Sumoylation | CRGVPDAKIRIFDLG CCCCCCCEEEEEECC | 39.64 | - | |
| 32 | Citrullination | GVPDAKIRIFDLGRK CCCCCEEEEEECCCC | 23.86 | - | |
| 32 | Methylation | GVPDAKIRIFDLGRK CCCCCEEEEEECCCC | 23.86 | - | |
| 32 | Citrullination | GVPDAKIRIFDLGRK CCCCCEEEEEECCCC | 23.86 | - | |
| 39 | Sumoylation | RIFDLGRKKAKVDEF EEEECCCCCCCCCCC | 56.11 | - | |
| 42 | Acetylation | DLGRKKAKVDEFPLC ECCCCCCCCCCCCCC | 60.13 | 26051181 | |
| 42 | Ubiquitination | DLGRKKAKVDEFPLC ECCCCCCCCCCCCCC | 60.13 | - | |
| 49 | Glutathionylation | KVDEFPLCGHMVSDE CCCCCCCCCCCCCHH | 3.42 | 22555962 | |
| 52 | Sulfoxidation | EFPLCGHMVSDEYEQ CCCCCCCCCCHHHHH | 1.55 | 30846556 | |
| 54 | Phosphorylation | PLCGHMVSDEYEQLS CCCCCCCCHHHHHHC | 19.70 | 26126808 | |
| 57 | Phosphorylation | GHMVSDEYEQLSSEA CCCCCHHHHHHCHHH | 17.61 | 28796482 | |
| 61 | Phosphorylation | SDEYEQLSSEALEAA CHHHHHHCHHHHHHH | 26.31 | - | |
| 71 | S-nitrosocysteine | ALEAARICANKYMVK HHHHHHHHHHHHHHH | 2.59 | - | |
| 71 | S-nitrosylation | ALEAARICANKYMVK HHHHHHHHHHHHHHH | 2.59 | 19483679 | |
| 74 | Sumoylation | AARICANKYMVKSCG HHHHHHHHHHHHHCC | 19.05 | - | |
| 74 | Ubiquitination | AARICANKYMVKSCG HHHHHHHHHHHHHCC | 19.05 | 21890473 | |
| 74 | Sumoylation | AARICANKYMVKSCG HHHHHHHHHHHHHCC | 19.05 | - | |
| 74 | Acetylation | AARICANKYMVKSCG HHHHHHHHHHHHHCC | 19.05 | 25825284 | |
| 75 | Phosphorylation | ARICANKYMVKSCGK HHHHHHHHHHHHCCC | 13.62 | - | |
| 78 | Acetylation | CANKYMVKSCGKDGF HHHHHHHHHCCCCCE | 24.41 | 27178108 | |
| 78 | 2-Hydroxyisobutyrylation | CANKYMVKSCGKDGF HHHHHHHHHCCCCCE | 24.41 | - | |
| 78 | Ubiquitination | CANKYMVKSCGKDGF HHHHHHHHHCCCCCE | 24.41 | - | |
| 80 | S-palmitoylation | NKYMVKSCGKDGFHI HHHHHHHCCCCCEEE | 6.95 | 21044946 | |
| 82 | Ubiquitination | YMVKSCGKDGFHIRV HHHHHCCCCCEEEEE | 60.03 | 21906983 | |
| 82 | Acetylation | YMVKSCGKDGFHIRV HHHHHCCCCCEEEEE | 60.03 | 26051181 | |
| 82 | 2-Hydroxyisobutyrylation | YMVKSCGKDGFHIRV HHHHHCCCCCEEEEE | 60.03 | - | |
| 82 | Sumoylation | YMVKSCGKDGFHIRV HHHHHCCCCCEEEEE | 60.03 | - | |
| 88 | Methylation | GKDGFHIRVRLHPFH CCCCEEEEEEECCCE | 10.03 | 115491543 | |
| 101 | 2-Hydroxyisobutyrylation | FHVIRINKMLSCAGA CEEEEHHCCHHHCCH | 38.56 | - | |
| 101 | Acetylation | FHVIRINKMLSCAGA CEEEEHHCCHHHCCH | 38.56 | 25953088 | |
| 101 | Ubiquitination | FHVIRINKMLSCAGA CEEEEHHCCHHHCCH | 38.56 | 21890473 | |
| 102 | Sulfoxidation | HVIRINKMLSCAGAD EEEEHHCCHHHCCHH | 2.62 | 21406390 | |
| 104 | Phosphorylation | IRINKMLSCAGADRL EEHHCCHHHCCHHHH | 9.83 | 21815630 | |
| 105 | Glutathionylation | RINKMLSCAGADRLQ EHHCCHHHCCHHHHH | 3.40 | 22555962 | |
| 110 | Methylation | LSCAGADRLQTGMRG HHHCCHHHHHCCCCC | 28.32 | - | |
| 121 | Acetylation | GMRGAFGKPQGTVAR CCCCCCCCCCCCEEE | 27.93 | 19608861 | |
| 121 | Malonylation | GMRGAFGKPQGTVAR CCCCCCCCCCCCEEE | 27.93 | 26320211 | |
| 121 | Sumoylation | GMRGAFGKPQGTVAR CCCCCCCCCCCCEEE | 27.93 | - | |
| 121 | Ubiquitination | GMRGAFGKPQGTVAR CCCCCCCCCCCCEEE | 27.93 | - | |
| 125 | Phosphorylation | AFGKPQGTVARVHIG CCCCCCCCEEEEEHH | 13.02 | 23312004 | |
| 136 | Sulfoxidation | VHIGQVIMSIRTKLQ EEHHHHHHHHHHHHC | 2.60 | 30846556 | |
| 137 | Phosphorylation | HIGQVIMSIRTKLQN EHHHHHHHHHHHHCC | 9.59 | 28450419 | |
| 145 | Ubiquitination | IRTKLQNKEHVIEAL HHHHHCCHHHHHHHH | 35.91 | 21890473 | |
| 145 | 2-Hydroxyisobutyrylation | IRTKLQNKEHVIEAL HHHHHCCHHHHHHHH | 35.91 | - | |
| 153 | Methylation | EHVIEALRRAKFKFP HHHHHHHHHCCCCCC | 43.49 | - | |
| 156 | Ubiquitination | IEALRRAKFKFPGRQ HHHHHHCCCCCCCCC | 47.47 | - | |
| 158 | Ubiquitination | ALRRAKFKFPGRQKI HHHHCCCCCCCCCEE | 50.36 | - | |
| 158 | Acetylation | ALRRAKFKFPGRQKI HHHHCCCCCCCCCEE | 50.36 | 26051181 | |
| 158 | Sumoylation | ALRRAKFKFPGRQKI HHHHCCCCCCCCCEE | 50.36 | - | |
| 164 | Acetylation | FKFPGRQKIHISKKW CCCCCCCEEEEECCC | 34.59 | 7491835 | |
| 168 | Phosphorylation | GRQKIHISKKWGFTK CCCEEEEECCCCCCC | 17.64 | 12138090 | |
| 170 | Ubiquitination | QKIHISKKWGFTKFN CEEEEECCCCCCCCC | 45.84 | - | |
| 170 | Methylation | QKIHISKKWGFTKFN CEEEEECCCCCCCCC | 45.84 | 110874759 | |
| 170 | Acetylation | QKIHISKKWGFTKFN CEEEEECCCCCCCCC | 45.84 | 25825284 | |
| 170 | Sumoylation | QKIHISKKWGFTKFN CEEEEECCCCCCCCC | 45.84 | - | |
| 175 | Ubiquitination | SKKWGFTKFNADEFE ECCCCCCCCCHHHHH | 34.07 | 21906983 | |
| 175 | Acetylation | SKKWGFTKFNADEFE ECCCCCCCCCHHHHH | 34.07 | 21466224 | |
| 175 | Sumoylation | SKKWGFTKFNADEFE ECCCCCCCCCHHHHH | 34.07 | 28112733 | |
| 175 | Sumoylation | SKKWGFTKFNADEFE ECCCCCCCCCHHHHH | 34.07 | - | |
| 184 | Sulfoxidation | NADEFEDMVAEKRLI CHHHHHHHHHHHCCC | 2.12 | 21406390 | |
| 188 | Ubiquitination | FEDMVAEKRLIPDGC HHHHHHHHCCCCCCC | 42.65 | 18781797 | |
| 188 | 2-Hydroxyisobutyrylation | FEDMVAEKRLIPDGC HHHHHHHHCCCCCCC | 42.65 | - | |
| 188 | Sumoylation | FEDMVAEKRLIPDGC HHHHHHHHCCCCCCC | 42.65 | - | |
| 188 | Acetylation | FEDMVAEKRLIPDGC HHHHHHHHCCCCCCC | 42.65 | 23236377 | |
| 195 | S-nitrosylation | KRLIPDGCGVKYIPN HCCCCCCCCCEECCC | 8.05 | 19483679 | |
| 195 | S-nitrosocysteine | KRLIPDGCGVKYIPN HCCCCCCCCCEECCC | 8.05 | - | |
| 198 | 2-Hydroxyisobutyrylation | IPDGCGVKYIPNRGP CCCCCCCEECCCCCC | 23.81 | - | |
| 198 | Acetylation | IPDGCGVKYIPNRGP CCCCCCCEECCCCCC | 23.81 | 26051181 | |
| 208 | 2-Hydroxyisobutyrylation | PNRGPLDKWRALHS- CCCCCHHHHHHHCC- | 46.38 | - | |
| 208 | Ubiquitination | PNRGPLDKWRALHS- CCCCCHHHHHHHCC- | 46.38 | 19608861 | |
| 208 | Acetylation | PNRGPLDKWRALHS- CCCCCHHHHHHHCC- | 46.38 | 23954790 |
| 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 RL10_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RL10_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 RL10_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| OMIM Disease | ||||||
| 300847 | Autism, X-linked 5 (AUTSX5) | |||||
| Kegg Drug | ||||||
| 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-121 AND LYS-208, AND MASSSPECTROMETRY. | |
| Ubiquitylation | |
| Reference | PubMed |
| "Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-188, AND MASSSPECTROMETRY. | |