UniProt ID | RM46_HUMAN | |
---|---|---|
UniProt AC | Q9H2W6 | |
Protein Name | 39S ribosomal protein L46, mitochondrial | |
Gene Name | MRPL46 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 279 | |
Subcellular Localization | Mitochondrion . | |
Protein Description | ||
Protein Sequence | MAAPVRRTLLGVAGGWRRFERLWAGSLSSRSLALAAAPSSNGSPWRLLGALCLQRPPVVSKPLTPLQEEMASLLQQIEIERSLYSDHELRALDENQRLAKKKADLHDEEDEQDILLAQDLEDMWEQKFLQFKLGARITEADEKNDRTSLNRKLDRNLVLLVREKFGDQDVWILPQAEWQPGETLRGTAERTLATLSENNMEAKFLGNAPCGHYTFKFPQAMRTESNLGAKVFFFKALLLTGDFSQAGNKGHHVWVTKDELGDYLKPKYLAQVRRFVSDL | |
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 |
---|---|---|---|---|---|
8 | Phosphorylation | MAAPVRRTLLGVAGG CCCCHHHHHHHHHCC | 18.77 | - | |
26 | Phosphorylation | FERLWAGSLSSRSLA HHHHHCCCCCCCHHH | 19.82 | 23025827 | |
60 | Phosphorylation | LQRPPVVSKPLTPLQ CCCCCCCCCCCCHHH | 28.87 | 24719451 | |
82 | Phosphorylation | QQIEIERSLYSDHEL HHHHHHHHCCCHHHH | 20.90 | 23186163 | |
84 | Phosphorylation | IEIERSLYSDHELRA HHHHHHCCCHHHHHH | 17.19 | 25884760 | |
85 | Phosphorylation | EIERSLYSDHELRAL HHHHHCCCHHHHHHH | 37.47 | 25003641 | |
127 | Ubiquitination | LEDMWEQKFLQFKLG HHHHHHHHHHHHHHC | 36.21 | 22817900 | |
132 | Ubiquitination | EQKFLQFKLGARITE HHHHHHHHHCCCCCC | 32.81 | 22817900 | |
194 | Phosphorylation | TAERTLATLSENNME HHHHHHHHHCCCCCE | 33.65 | 22210691 | |
200 | Sulfoxidation | ATLSENNMEAKFLGN HHHCCCCCEEEECCC | 8.81 | 21406390 | |
203 | Ubiquitination | SENNMEAKFLGNAPC CCCCCEEEECCCCCC | 28.02 | 21890473 | |
216 | Acetylation | PCGHYTFKFPQAMRT CCCCEEEECCCHHCC | 48.62 | 25953088 | |
230 | Ubiquitination | TESNLGAKVFFFKAL CCCHHHCHHHHHHHH | 37.46 | 22817900 | |
230 | Acetylation | TESNLGAKVFFFKAL CCCHHHCHHHHHHHH | 37.46 | 19608861 | |
235 | Ubiquitination | GAKVFFFKALLLTGD HCHHHHHHHHHHHCC | 32.73 | 22817900 | |
249 | Malonylation | DFSQAGNKGHHVWVT CHHHCCCCCCEEEEE | 59.72 | 26320211 | |
263 | Phosphorylation | TKDELGDYLKPKYLA EHHHHHHHCCHHHHH | 18.15 | 20068231 | |
265 | Ubiquitination | DELGDYLKPKYLAQV HHHHHHCCHHHHHHH | 32.98 | 19608861 | |
265 | Acetylation | DELGDYLKPKYLAQV HHHHHHCCHHHHHHH | 32.98 | 23236377 | |
267 | Acetylation | LGDYLKPKYLAQVRR HHHHCCHHHHHHHHH | 51.84 | 23236377 | |
267 | Malonylation | LGDYLKPKYLAQVRR HHHHCCHHHHHHHHH | 51.84 | 26320211 |
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 RM46_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RM46_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 RM46_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
VPP1_HUMAN | ATP6V0A1 | physical | 22939629 | |
RM48_HUMAN | MRPL48 | physical | 26186194 | |
RM40_HUMAN | MRPL40 | physical | 26186194 | |
ETFR1_HUMAN | LYRM5 | physical | 26186194 | |
RM55_HUMAN | MRPL55 | physical | 26186194 | |
MGME1_HUMAN | MGME1 | physical | 26186194 | |
ACPM_HUMAN | NDUFAB1 | physical | 26186194 | |
RM40_HUMAN | MRPL40 | physical | 26344197 | |
RM55_HUMAN | MRPL55 | physical | 26344197 | |
RM40_HUMAN | MRPL40 | physical | 28514442 | |
RM55_HUMAN | MRPL55 | physical | 28514442 | |
RM48_HUMAN | MRPL48 | physical | 28514442 | |
MGME1_HUMAN | MGME1 | physical | 28514442 | |
CGL_HUMAN | CTH | physical | 28514442 | |
ACPM_HUMAN | NDUFAB1 | physical | 28514442 |
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-230 AND LYS-265, AND MASSSPECTROMETRY. |