| Identification |
|---|
| HMDB Protein ID
| HMDBP00675 |
| Secondary Accession Numbers
| - 5948
- HMDBP02424
- HMDBP04869
|
| Name
| Glutaminase liver isoform, mitochondrial |
| Synonyms
|
- GLS
- L-glutaminase
- L-glutamine amidohydrolase
- SubName: L-glutaminase
|
| Gene Name
| GLS2 |
| Protein Type
| Enzyme |
| Biological Properties |
|---|
| General Function
| Involved in glutaminase activity |
| Specific Function
| 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.
|
| Pathways
|
- 2-Hydroxyglutric Aciduria (D And L Form)
- 4-Hydroxybutyric Aciduria/Succinic Semialdehyde Dehydrogenase Deficiency
- Alanine, aspartate and glutamate metabolism
- Arginine and proline metabolism
- Argininemia
- Argininosuccinic Aciduria
- Carbamoyl Phosphate Synthetase Deficiency
- Citrullinemia Type I
- D-Glutamine and D-glutamate metabolism
- GABAergic synapse
- Glutamate Metabolism
- Glutamatergic synapse
- Glutaminolysis and Cancer
- Homocarnosinosis
- Hyperinsulinism-Hyperammonemia Syndrome
- Nitrogen metabolism
- Ornithine Transcarbamylase Deficiency (OTC Deficiency)
- Proximal tubule bicarbonate reclamation
- Succinic semialdehyde dehydrogenase deficiency
- The oncogenic action of 2-hydroxyglutarate
- The oncogenic action of D-2-hydroxyglutarate in Hydroxygluaricaciduria
- The oncogenic action of L-2-hydroxyglutarate in Hydroxygluaricaciduria
- Urea Cycle
- Warburg Effect
|
| Reactions
|
| Glutamine + Water → Glutamic acid + Ammonia |
details
|
| D-Glutamine + Water → D-Glutamic acid + Ammonia |
details
|
|
| GO Classification
|
| Biological Process |
| cellular nitrogen compound metabolic process |
| glutamine metabolic process |
| reactive oxygen species metabolic process |
| cellular amino acid biosynthetic process |
| regulation of apoptotic process |
| neurotransmitter secretion |
| glutamate secretion |
| Cellular Component |
| mitochondrial matrix |
| Function |
| catalytic activity |
| hydrolase activity |
| hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| glutaminase activity |
| hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| Molecular Function |
| glutaminase activity |
| Process |
| metabolic process |
| cellular metabolic process |
| glutamine metabolic process |
| glutamine family amino acid metabolic process |
| cellular amino acid and derivative metabolic process |
| cellular amino acid metabolic process |
|
| Cellular Location
|
- Cytoplasmic
- Mitochondrion
|
| Gene Properties |
|---|
| Chromosome Location
| 12 |
| Locus
| 12q13 |
| SNPs
| GLS2 |
| Gene Sequence
|
>1809 bp
ATGCGCTCCATGAAGGCTCTGCAGAAGGCCCTGAGCCGGGCTGGCAGTCACTGCGGGCGA
GGAGGCTGGGGTCACCCGAGCCGGAGCCCCCTCCTTGGCGGGGGCGTCCGGCACCACCTC
AGTGAGGCCGCGGCGCAGGGCAGAGAGACGCCACACAGCCACCAGCCGCAGCACCAGGAT
CATGATTCATCAGAAAGTGGCATGCTGTCCCGCCTGGGTGATTTGCTCTTTTACACTATT
GCTGAAGGACAGGAACGAACCCCTATCCACAAGTTCACCACTGCACTAAAGGCCACTGGA
CTGCAGACATCAGATCCTCGGCTCCGAGACTGCATGAGCGAGATGCACCGCGTGGTCCAA
GAGTCCAGTAGTGGTGGCCTCTTGGACCGAGATCTCTTCCGAAAGTGTGTGAGCAGCAGC
ATTGTGCTCCTGACCCAGGCATTCCGAAAGAAGTTTGTCATTCCTGATTTTGAGGAGTTC
ACGGGCCATGTGGATCGCATCTTTGAGGATGTCAAAGAGCTCACTGGAGGCAAAGTGGCA
GCCTACATCCCTCAGCTGGCCAAGTCAAACCCAGACCTGTGGGGTGTCTCCCTGTGCACT
GTGGATGGTCAACGGCACTCTGTGGGCCACACAAAGATCCCCTTCTGCCTGCAGTCCTGT
GTGAAGCCCCTCACCTATGCCATCTCCATAAGCACCCTAGGCACTGACTACGTGCACAAG
TTTGTGGGCAAAGAGCCAAGTGGCCTGCGCTACAACAAGCTCTCCCTCGATGAGGAAGGA
ATCCCCCATAACCCCATGGTCAATGCTGGTGCCATTGTTGTCAGCTCCCTGATCAAGATG
GACTGTAACAAAGCAGAGAAGTTTGATTTTGTGTTGCAGTATCTCAACAAAATGGCTGGG
AATGAATACATGGGTTTCAGCAATGCCACATTCCAGTCAGAGAAGGAAACAGGGGATCGG
AATTATGCCATCGGCTATTATCACGAGGAAAAGAAGTGCTTTCCTAAGGGGGTGGACATG
ATGGCTGCCCTTGATCTCTACTTCCAGCTGTGTTCTGTGGAGGTCACTTGTGAATCAGGC
AGTGTCATGGCAGCCACCCTCGCCAACGGTGGGATTTGCCCCATCACAGGCGAGAGTGTG
CTGAGTGCTGAAGCAGTGCGCAACACCCTCAGCCTCATGCATTCCTGCGGCATGTATGAC
TTCTCTGGCCAGTTTGCCTTCCACGTGGGCCTGCCAGCCAAGTCAGCTGTATCAGGAGCC
ATCCTCCTGGTGGTACCCAATGTCATGGGAATGATGTGCCTGTCACCCCCATTGGACAAG
CTGGGGAACAGCCATAGGGGGACCAGCTTCTGCCAGAAGTTGGTGTCTCTCTTCAATTTC
CACAACTATGACAACCTGAGGCACTGTGCTCGGAAGTTAGACCCACGGCGTGAAGGGGCA
GAAATTCGGAACAAGACTGTGGTCAACCTGTTATTTGCTGCCTATAGTGGCGATGTCTCA
GCTCTTCGAAGGTTTGCCTTGTCAGCCATGGATATGGAACAGAAAGACTATGACTCGCGC
ACAGCTCTGCATGTTGCTGCAGCTGAAGGACACATCGAAGTTGTTAAATTCCTGATCGAG
GCTTGCAAAGTGAATCCTTTTGCCAAGGACAGGTGGGGCAACATTCCCCTGGATGATGCT
GTGCAGTTCAACCATCTGGAGGTGGTCAAACTGCTTCAAGATTACCAGGACTCCTACACA
CTCTCTGAAACTCAGGCTGAGGCAGCAGCTGAGGCCCTGTCCAAAGAGAACTTAGAAAGC
ATGGTATGA
|
| Protein Properties |
|---|
| Number of Residues
| 602 |
| Molecular Weight
| 66322.225 |
| Theoretical pI
| 7.301 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
>Glutaminase liver isoform, mitochondrial
MRSMKALQKALSRAGSHCGRGGWGHPSRSPLLGGGVRHHLSEAAAQGRETPHSHQPQHQD
HDSSESGMLSRLGDLLFYTIAEGQERIPIHKFTTALKATGLQTSDPRLRDCMSEMHRVVQ
ESSSGGLLDRDLFRKCVSSNIVLLTQAFRKKFVIPDFEEFTGHVDRIFEDVKELTGGKVA
AYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHK
FVGKEPSGLRYNKLSLNEEGIPHNPMVNAGAIVVSSLIKMDCNKAEKFDFVLQYLNKMAG
NEYMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMMAALDLYFQLCSVEVTCESG
SVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGA
ILLVVPNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFHNYDNLRHCARKLDPRREGA
EIRNKTVVNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIE
ACKVNPFAKDRWGNIPLDDAVQFNHLEVVKLLQDYQDSYTLSETQAEAAAEALSKENLES
MV
|
| External Links |
|---|
| GenBank ID Protein
| 6650606 |
| UniProtKB/Swiss-Prot ID
| Q9UI32 |
| UniProtKB/Swiss-Prot Entry Name
| GLSL_HUMAN |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| AF110330 |
| GeneCard ID
| GLS2 |
| GenAtlas ID
| GLS2 |
| HGNC ID
| HGNC:29570 |
| References |
|---|
| General References
| - Gomez-Fabre PM, Aledo JC, Del Castillo-Olivares A, Alonso FJ, Nunez De Castro I, Campos JA, Marquez J: Molecular cloning, sequencing and expression studies of the human breast cancer cell glutaminase. Biochem J. 2000 Jan 15;345 Pt 2:365-75. [PubMed:10620514 ]
- Olalla L, Aledo JC, Bannenberg G, Marquez J: The C-terminus of human glutaminase L mediates association with PDZ domain-containing proteins. FEBS Lett. 2001 Jan 19;488(3):116-22. [PubMed:11163757 ]
- Perez-Gomez C, Mates JM, Gomez-Fabre PM, del Castillo-Olivares A, Alonso FJ, Marquez J: Genomic organization and transcriptional analysis of the human l-glutaminase gene. Biochem J. 2003 Mar 15;370(Pt 3):771-84. [PubMed:12444921 ]
|
