UniProt ID | SYSM_HUMAN | |
---|---|---|
UniProt AC | Q9NP81 | |
Protein Name | Serine--tRNA ligase, mitochondrial | |
Gene Name | SARS2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 518 | |
Subcellular Localization | Mitochondrion matrix . | |
Protein Description | Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).. | |
Protein Sequence | MAASMARRLWPLLTRRGFRPRGGCISNDSPRRSFTTEKRNRNLLYEYAREGYSALPQLDIERFCACPEEAAHALELRKGELRSADLPAIISTWQELRQLQEQIRSLEEEKAAVTEAVRALLANQDSGEVQQDPKYQGLRARGREIRKELVHLYPREAQLEEQFYLQALKLPNQTHPDVPVGDESQARVLHMVGDKPVFSFQPRGHLEIGEKLDIIRQKRLSHVSGHRSYYLRGAGALLQHGLVNFTFNKLLRRGFTPMTVPDLLRGAVFEGCGMTPNANPSQIYNIDPARFKDLNLAGTAEVGLAGYFMDHTVAFRDLPVRMVCSSTCYRAETNTGQEPRGLYRVHHFTKVEMFGVTGPGLEQSSQLLEEFLSLQMEILTELGLHFRVLDMPTQELGLPAYRKFDIEAWMPGRGRFGEVTSASNCTDFQSRRLHIMFQTEAGELQFAHTVNATACAVPRLLIALLESNQQKDGSVLVPPALQSYLGTDRITAPTHVPLQYIGPNQPRKPGLPGQPAVS | |
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 |
---|---|---|---|---|---|
4 | Phosphorylation | ----MAASMARRLWP ----CHHHHHHHHHH | 11.93 | 28509920 | |
14 | Phosphorylation | RRLWPLLTRRGFRPR HHHHHHHHCCCCCCC | 26.46 | 28509920 | |
52 | Phosphorylation | YEYAREGYSALPQLD HHHHHHCCCCCCCCC | 5.99 | 28152594 | |
53 | Phosphorylation | EYAREGYSALPQLDI HHHHHCCCCCCCCCH | 33.90 | 28152594 | |
110 | Acetylation | IRSLEEEKAAVTEAV HHHHHHHHHHHHHHH | 44.95 | 23954790 | |
110 | Succinylation | IRSLEEEKAAVTEAV HHHHHHHHHHHHHHH | 44.95 | 23954790 | |
110 | Malonylation | IRSLEEEKAAVTEAV HHHHHHHHHHHHHHH | 44.95 | 26320211 | |
126 | Phosphorylation | ALLANQDSGEVQQDP HHHHCCCCCCCCCCC | 27.39 | 29507054 | |
134 | Acetylation | GEVQQDPKYQGLRAR CCCCCCCCHHHHHHH | 59.50 | 23236377 | |
134 | Ubiquitination | GEVQQDPKYQGLRAR CCCCCCCCHHHHHHH | 59.50 | 29967540 | |
134 | 2-Hydroxyisobutyrylation | GEVQQDPKYQGLRAR CCCCCCCCHHHHHHH | 59.50 | - | |
135 | Phosphorylation | EVQQDPKYQGLRARG CCCCCCCHHHHHHHH | 17.13 | 29083192 | |
147 | Malonylation | ARGREIRKELVHLYP HHHHHHHHHHHHHCC | 62.15 | 26320211 | |
184 | O-linked_Glycosylation | DVPVGDESQARVLHM CCCCCCHHHHEEEEE | 33.60 | 23301498 | |
195 | Acetylation | VLHMVGDKPVFSFQP EEEEECCCCCEEECC | 36.83 | 25953088 | |
195 | Malonylation | VLHMVGDKPVFSFQP EEEEECCCCCEEECC | 36.83 | 26320211 | |
195 | Succinylation | VLHMVGDKPVFSFQP EEEEECCCCCEEECC | 36.83 | - | |
195 | Ubiquitination | VLHMVGDKPVFSFQP EEEEECCCCCEEECC | 36.83 | 21890473 | |
195 | Succinylation | VLHMVGDKPVFSFQP EEEEECCCCCEEECC | 36.83 | - | |
197 | Ubiquitination | HMVGDKPVFSFQPRG EEECCCCCEEECCCC | 8.48 | 21890473 | |
197 | Ubiquitination | HMVGDKPVFSFQPRG EEECCCCCEEECCCC | 8.48 | 21890473 | |
211 | Malonylation | GHLEIGEKLDIIRQK CCCCHHHHHHHHHHH | 46.37 | 26320211 | |
211 | Acetylation | GHLEIGEKLDIIRQK CCCCHHHHHHHHHHH | 46.37 | 25953088 | |
221 | Phosphorylation | IIRQKRLSHVSGHRS HHHHHCHHCCCCCHH | 26.35 | 23312004 | |
224 | Phosphorylation | QKRLSHVSGHRSYYL HHCHHCCCCCHHHCH | 24.37 | 23312004 | |
256 | Phosphorylation | KLLRRGFTPMTVPDL HHHHCCCCCCCHHHH | 18.25 | 21406692 | |
259 | Phosphorylation | RRGFTPMTVPDLLRG HCCCCCCCHHHHHCC | 30.04 | 21406692 | |
325 | Phosphorylation | LPVRMVCSSTCYRAE CCCEEEEECEEEEEE | 19.78 | 25219547 | |
326 | Phosphorylation | PVRMVCSSTCYRAET CCEEEEECEEEEEEC | 19.85 | 25219547 | |
327 | Phosphorylation | VRMVCSSTCYRAETN CEEEEECEEEEEECC | 9.39 | 25219547 | |
329 | Phosphorylation | MVCSSTCYRAETNTG EEEECEEEEEECCCC | 16.97 | 25219547 | |
343 | Phosphorylation | GQEPRGLYRVHHFTK CCCCCCEEEEEEEEE | 17.26 | - | |
401 | Phosphorylation | QELGLPAYRKFDIEA HHCCCCCHHCCCEEE | 16.64 | 30576142 | |
500 | Phosphorylation | PTHVPLQYIGPNQPR CCCCCCCCCCCCCCC | 18.61 | - | |
518 | Phosphorylation | LPGQPAVS------- CCCCCCCC------- | 36.29 | 20068231 |
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 SYSM_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SYSM_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 SYSM_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SYHM_HUMAN | HARS2 | physical | 26344197 | |
SBDS_HUMAN | SBDS | physical | 26344197 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
613845 | Hyperuricemia, pulmonary hypertension, renal failure, and alkalosis syndrome (HUPRAS) | |||||
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-110, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, AND MASSSPECTROMETRY. |