| UniProt ID | GLSL_HUMAN | |
|---|---|---|
| UniProt AC | Q9UI32 | |
| Protein Name | Glutaminase liver isoform, mitochondrial | |
| Gene Name | GLS2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 602 | |
| Subcellular Localization | Mitochondrion . | |
| Protein Description | Plays an important role in the regulation of glutamine catabolism. Promotes mitochondrial respiration and increases ATP generation in cells by catalyzing the synthesis of glutamate and alpha-ketoglutarate. Increases cellular anti-oxidant function via NADH and glutathione production. May play a role in preventing tumor proliferation.. | |
| Protein Sequence | MRSMKALQKALSRAGSHCGRGGWGHPSRSPLLGGGVRHHLSEAAAQGRETPHSHQPQHQDHDSSESGMLSRLGDLLFYTIAEGQERIPIHKFTTALKATGLQTSDPRLRDCMSEMHRVVQESSSGGLLDRDLFRKCVSSNIVLLTQAFRKKFVIPDFEEFTGHVDRIFEDVKELTGGKVAAYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHKFVGKEPSGLRYNKLSLNEEGIPHNPMVNAGAIVVSSLIKMDCNKAEKFDFVLQYLNKMAGNEYMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMMAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFHNYDNLRHCARKLDPRREGAEIRNKTVVNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACKVNPFAKDRWGNIPLDDAVQFNHLEVVKLLQDYQDSYTLSETQAEAAAEALSKENLESMV | |
| 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 |
|---|---|---|---|---|---|
| 122 | Phosphorylation | MHRVVQESSSGGLLD HHHHHHHCCCCCCCC | 16.83 | 22210691 | |
| 136 | S-nitrosylation | DRDLFRKCVSSNIVL CHHHHHHHHHCCHHH | 2.90 | 24105792 | |
| 138 | Phosphorylation | DLFRKCVSSNIVLLT HHHHHHHHCCHHHHC | 27.43 | 30576142 | |
| 139 | Phosphorylation | LFRKCVSSNIVLLTQ HHHHHHHCCHHHHCH | 15.35 | 30576142 | |
| 145 | Phosphorylation | SSNIVLLTQAFRKKF HCCHHHHCHHHHHCC | 17.43 | 30576142 | |
| 253 | Succinylation | PSGLRYNKLSLNEEG CCCCCCCCCCCCCCC | 30.44 | - | |
| 253 | Succinylation | PSGLRYNKLSLNEEG CCCCCCCCCCCCCCC | 30.44 | - | |
| 276 | Phosphorylation | AGAIVVSSLIKMDCN HHHEEEECHHHCCCC | 23.62 | 24719451 | |
| 279 | Acetylation | IVVSSLIKMDCNKAE EEEECHHHCCCCHHH | 33.70 | - | |
| 284 | Acetylation | LIKMDCNKAEKFDFV HHHCCCCHHHHHHHH | 65.34 | - | |
| 303 | Phosphorylation | NKMAGNEYMGFSNAT HHHCCCCCCCCCCCE | 13.41 | - | |
| 310 | Phosphorylation | YMGFSNATFQSEKET CCCCCCCEEECCHHH | 26.85 | - | |
| 317 | Phosphorylation | TFQSEKETGDRNYAI EEECCHHHCCCCEEH | 56.29 | 25072903 | |
| 322 | Phosphorylation | KETGDRNYAIGYYLK HHHCCCCEEHHHHHC | 10.65 | 25072903 | |
| 326 | Phosphorylation | DRNYAIGYYLKEKKC CCCEEHHHHHCCCCC | 10.26 | 26434776 | |
| 327 | Phosphorylation | RNYAIGYYLKEKKCF CCEEHHHHHCCCCCC | 13.19 | 26434776 | |
| 329 | Acetylation | YAIGYYLKEKKCFPK EEHHHHHCCCCCCCC | 51.90 | - | |
| 485 | Ubiquitination | EGAEIRNKTVVNLLF CCCHHCCHHHHHHHH | 32.61 | - | |
| 486 | Phosphorylation | GAEIRNKTVVNLLFA CCHHCCHHHHHHHHH | 32.98 | 22210691 | |
| 495 | Phosphorylation | VNLLFAAYSGDVSAL HHHHHHHHCCCHHHH | 15.12 | 22210691 |
| 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 GLSL_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GLSL_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
| 310 | Phosphorylation | 316 (6) | L ⇒ P | rs2657879 |
| 21886157 24816252 26068415 27005778 |
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| GRHPR_HUMAN | GRHPR | physical | 21988832 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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