UniProt ID | ASNS_MOUSE | |
---|---|---|
UniProt AC | Q61024 | |
Protein Name | Asparagine synthetase [glutamine-hydrolyzing] | |
Gene Name | Asns | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 561 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQPIRVRKYPYLWLCYNGEIYNHKALQQRFEFEYQTNVDGEIILHLYDKGGIEKTICMLDGVFAFILLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVSLKHSTTPFLKVEPFLPGHYEVLDLKPNGKVASVEMVKYHHCTDEPLHAIYDSVEKLFPGFDLETVKNNLRILFDNAIKKRLMTDRRIGCLLSGGLDSSLVAASLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVANYIGSEHHEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVVIFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLKELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPDMRIPKNGIEKHLLRETFEDCNLLPKEILWRPKEAFSDGITSVKNSWFKILQDYVEHQVDDEMMSAASQKFPFNTPKTKEGYFYRQIFERHYPGRADWLTHYWMPKWINATDPSARTLTHYKSAAKA | |
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 |
---|---|---|---|---|---|
168 | Ubiquitination | AKGLVSLKHSTTPFL CCCCEEECCCCCCCE | 28.18 | - | |
168 | Acetylation | AKGLVSLKHSTTPFL CCCCEEECCCCCCCE | 28.18 | 22826441 | |
204 | Phosphorylation | ASVEMVKYHHCTDEP EEEEEEEEECCCCCC | 5.84 | 25777480 | |
207 | S-nitrosylation | EMVKYHHCTDEPLHA EEEEEECCCCCCHHH | 3.06 | 20925432 | |
207 | S-nitrosocysteine | EMVKYHHCTDEPLHA EEEEEECCCCCCHHH | 3.06 | - | |
208 | Phosphorylation | MVKYHHCTDEPLHAI EEEEECCCCCCHHHH | 38.75 | 25777480 | |
216 | Phosphorylation | DEPLHAIYDSVEKLF CCCHHHHHHHHHHHC | 11.71 | 26745281 | |
218 | Phosphorylation | PLHAIYDSVEKLFPG CHHHHHHHHHHHCCC | 18.40 | 26824392 | |
221 | Ubiquitination | AIYDSVEKLFPGFDL HHHHHHHHHCCCCCH | 53.96 | - | |
272 | Ubiquitination | LVAASLLKQLKEAQV HHHHHHHHHHHHHCC | 59.90 | - | |
281 | Phosphorylation | LKEAQVQYPLQTFAI HHHHCCCCCCCCEEC | 13.67 | 29899451 | |
342 | Phosphorylation | DITTVRASVGMYLIS CCCCHHHHHHHHHHH | 14.51 | 20495213 | |
350 | Acetylation | VGMYLISKYIRKNTD HHHHHHHHHHHCCCC | 37.39 | 22826441 | |
382 | Phosphorylation | IYFHKAPSPEKAEEE EEEECCCCHHHHHHH | 51.02 | 26824392 | |
385 | Acetylation | HKAPSPEKAEEESER ECCCCHHHHHHHHHH | 65.56 | - | |
395 | Ubiquitination | EESERLLKELYLFDV HHHHHHHHHHHHHHH | 50.71 | - | |
395 | Acetylation | EESERLLKELYLFDV HHHHHHHHHHHHHHH | 50.71 | 22826441 | |
455 | Glutathionylation | LRETFEDCNLLPKEI HHHHHHHCCCCCHHH | 2.81 | 24333276 | |
471 | Phosphorylation | WRPKEAFSDGITSVK CCCHHHHCCCCCCHH | 41.81 | 28066266 | |
475 | Phosphorylation | EAFSDGITSVKNSWF HHHCCCCCCHHHHHH | 32.75 | 28066266 | |
478 | Ubiquitination | SDGITSVKNSWFKIL CCCCCCHHHHHHHHH | 45.06 | 27667366 | |
504 | Ubiquitination | MMSAASQKFPFNTPK HHHHHHCCCCCCCCC | 53.13 | - | |
513 | Acetylation | PFNTPKTKEGYFYRQ CCCCCCCCCCCHHHH | 56.09 | 22826441 | |
545 | Phosphorylation | MPKWINATDPSARTL CCCCCCCCCCCHHHH | 43.91 | - | |
556 | Acetylation | ARTLTHYKSAAKA-- HHHHHHHHHHHCC-- | 26.47 | 23806337 | |
556 | Ubiquitination | ARTLTHYKSAAKA-- HHHHHHHHHHHCC-- | 26.47 | - | |
557 | Phosphorylation | RTLTHYKSAAKA--- HHHHHHHHHHCC--- | 26.71 | - |
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 ASNS_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ASNS_MOUSE !! |
* 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 ASNS_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ASNS_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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