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Q9UI32

- GLSL_HUMAN

UniProt

Q9UI32 - GLSL_HUMAN

Protein

Glutaminase liver isoform, mitochondrial

Gene

GLS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (17 Apr 2007)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

    L-glutamine + H2O = L-glutamate + NH3.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei219 – 2191SubstrateBy similarity
    Binding sitei268 – 2681SubstrateBy similarity
    Binding sitei314 – 3141SubstrateBy similarity
    Binding sitei321 – 3211SubstrateBy similarity
    Binding sitei347 – 3471SubstrateBy similarity
    Binding sitei399 – 3991SubstrateBy similarity
    Binding sitei417 – 4171Substrate; via amide nitrogenBy similarity

    GO - Molecular functioni

    1. glutaminase activity Source: ProtInc
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular amino acid biosynthetic process Source: Reactome
    2. cellular amino acid metabolic process Source: ProtInc
    3. cellular nitrogen compound metabolic process Source: Reactome
    4. glutamate secretion Source: Reactome
    5. glutamine metabolic process Source: InterPro
    6. neurotransmitter secretion Source: Reactome
    7. reactive oxygen species metabolic process Source: MGI
    8. regulation of apoptotic process Source: MGI
    9. small molecule metabolic process Source: Reactome
    10. synaptic transmission Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    ReactomeiREACT_12591. Glutamate Neurotransmitter Release Cycle.
    REACT_238. Amino acid synthesis and interconversion (transamination).
    SABIO-RKQ9UI32.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutaminase liver isoform, mitochondrial (EC:3.5.1.2)
    Short name:
    GLS
    Alternative name(s):
    L-glutaminase
    L-glutamine amidohydrolase
    Gene namesi
    Name:GLS2
    Synonyms:GA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:29570. GLS2.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134933506.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1414MitochondrionSequence AnalysisAdd
    BLAST
    Chaini15 – 602588Glutaminase liver isoform, mitochondrialPRO_0000011625Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei253 – 2531N6-succinyllysineBy similarity
    Modified residuei279 – 2791N6-acetyllysineBy similarity
    Modified residuei284 – 2841N6-acetyllysineBy similarity
    Modified residuei329 – 3291N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9UI32.
    PaxDbiQ9UI32.
    PRIDEiQ9UI32.

    PTM databases

    PhosphoSiteiQ9UI32.

    Expressioni

    Tissue specificityi

    Highly expressed in liver. Expressed in brain and pancreas. Not observed in heart, placenta, lung, skeletal muscle and kidney. Expression is significantly reduced in hepatocellular carcinomas.2 Publications

    Inductioni

    Up-regulated by P53 (at protein and mRNA level) under both stressed and non-stressed conditions.1 Publication

    Gene expression databases

    ArrayExpressiQ9UI32.
    BgeeiQ9UI32.
    CleanExiHS_GLS2.
    GenevestigatoriQ9UI32.

    Organism-specific databases

    HPAiHPA038608.

    Interactioni

    Subunit structurei

    Interacts with the PDZ domain of the syntrophin SNTA1. Interacts with the PDZ domain of TAX1BP3.1 Publication

    Protein-protein interaction databases

    BioGridi118044. 2 interactions.
    IntActiQ9UI32. 1 interaction.
    MINTiMINT-157952.
    STRINGi9606.ENSP00000310447.

    Structurei

    Secondary structure

    1
    602
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi157 – 17115
    Beta strandi195 – 2006
    Beta strandi205 – 2106
    Helixi218 – 2214
    Helixi222 – 23312
    Helixi235 – 2384
    Turni239 – 2413
    Helixi268 – 27710
    Turni278 – 2814
    Helixi284 – 29815
    Turni299 – 3013
    Helixi308 – 31710
    Helixi319 – 33012
    Helixi340 – 35112
    Beta strandi353 – 3553
    Helixi357 – 36812
    Turni369 – 3713
    Turni374 – 3763
    Helixi383 – 39614
    Helixi399 – 4013
    Helixi402 – 4087
    Beta strandi413 – 4153
    Beta strandi419 – 4257
    Turni426 – 4283
    Beta strandi429 – 4346
    Beta strandi442 – 4443
    Helixi445 – 45814

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4BQMX-ray2.18A/B154-479[»]
    ProteinModelPortaliQ9UI32.
    SMRiQ9UI32. Positions 72-479, 490-572.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati518 – 55134ANK 1Add
    BLAST
    Repeati552 – 58534ANK 2Add
    BLAST

    Sequence similaritiesi

    Belongs to the glutaminase family.Curated
    Contains 2 ANK repeats.Curated

    Keywords - Domaini

    ANK repeat, Repeat, Transit peptide

    Phylogenomic databases

    eggNOGiCOG2066.
    HOGENOMiHOG000216891.
    HOVERGENiHBG005856.
    InParanoidiQ9UI32.
    KOiK01425.
    OMAiCVKPLTY.
    OrthoDBiEOG7S4X5F.
    PhylomeDBiQ9UI32.
    TreeFamiTF313359.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    3.40.710.10. 1 hit.
    HAMAPiMF_00313. Glutaminase.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR012338. Beta-lactam/transpept-like.
    IPR015868. Glutaminase.
    [Graphical view]
    PANTHERiPTHR12544. PTHR12544. 1 hit.
    PfamiPF12796. Ank_2. 1 hit.
    PF04960. Glutaminase. 1 hit.
    [Graphical view]
    SMARTiSM00248. ANK. 2 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    SSF56601. SSF56601. 1 hit.
    TIGRFAMsiTIGR03814. Gln_ase. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9UI32-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRSMKALQKA LSRAGSHCGR GGWGHPSRSP LLGGGVRHHL SEAAAQGRET    50
    PHSHQPQHQD HDSSESGMLS RLGDLLFYTI AEGQERIPIH KFTTALKATG 100
    LQTSDPRLRD CMSEMHRVVQ ESSSGGLLDR DLFRKCVSSN IVLLTQAFRK 150
    KFVIPDFEEF TGHVDRIFED VKELTGGKVA AYIPQLAKSN PDLWGVSLCT 200
    VDGQRHSVGH TKIPFCLQSC VKPLTYAISI STLGTDYVHK FVGKEPSGLR 250
    YNKLSLNEEG IPHNPMVNAG AIVVSSLIKM DCNKAEKFDF VLQYLNKMAG 300
    NEYMGFSNAT FQSEKETGDR NYAIGYYLKE KKCFPKGVDM MAALDLYFQL 350
    CSVEVTCESG SVMAATLANG GICPITGESV LSAEAVRNTL SLMHSCGMYD 400
    FSGQFAFHVG LPAKSAVSGA ILLVVPNVMG MMCLSPPLDK LGNSHRGTSF 450
    CQKLVSLFNF HNYDNLRHCA RKLDPRREGA EIRNKTVVNL LFAAYSGDVS 500
    ALRRFALSAM DMEQKDYDSR TALHVAAAEG HIEVVKFLIE ACKVNPFAKD 550
    RWGNIPLDDA VQFNHLEVVK LLQDYQDSYT LSETQAEAAA EALSKENLES 600
    MV 602
    Length:602
    Mass (Da):66,323
    Last modified:April 17, 2007 - v2
    Checksum:i6D0E1EFF01BC3843
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti87 – 871I → T in AAF21933. (PubMed:10620514)Curated
    Sequence conflicti140 – 1401N → S in AAF21933. (PubMed:10620514)Curated
    Sequence conflicti257 – 2571N → D in AAF21933. (PubMed:10620514)Curated
    Sequence conflicti328 – 3292LK → HE in AAF21933. (PubMed:10620514)Curated
    Sequence conflicti560 – 5601A → V in AAF33826. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti581 – 5811L → P.1 Publication
    Corresponds to variant rs2657879 [ dbSNP | Ensembl ].
    VAR_031615

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF110330 mRNA. Translation: AAF21933.1.
    AF110331 mRNA. Translation: AAF21934.1.
    AF348119 Genomic DNA. Translation: AAO13298.2.
    AF223944 mRNA. Translation: AAF33826.1.
    CH471054 Genomic DNA. Translation: EAW96943.1.
    CCDSiCCDS8921.1.
    RefSeqiNP_001267727.1. NM_001280798.1.
    NP_037399.2. NM_013267.3.
    UniGeneiHs.212606.

    Genome annotation databases

    EnsembliENST00000311966; ENSP00000310447; ENSG00000135423.
    GeneIDi27165.
    KEGGihsa:27165.
    UCSCiuc001slj.3. human.

    Polymorphism databases

    DMDMi145559477.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF110330 mRNA. Translation: AAF21933.1 .
    AF110331 mRNA. Translation: AAF21934.1 .
    AF348119 Genomic DNA. Translation: AAO13298.2 .
    AF223944 mRNA. Translation: AAF33826.1 .
    CH471054 Genomic DNA. Translation: EAW96943.1 .
    CCDSi CCDS8921.1.
    RefSeqi NP_001267727.1. NM_001280798.1.
    NP_037399.2. NM_013267.3.
    UniGenei Hs.212606.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4BQM X-ray 2.18 A/B 154-479 [» ]
    ProteinModelPortali Q9UI32.
    SMRi Q9UI32. Positions 72-479, 490-572.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118044. 2 interactions.
    IntActi Q9UI32. 1 interaction.
    MINTi MINT-157952.
    STRINGi 9606.ENSP00000310447.

    Chemistry

    DrugBanki DB00142. L-Glutamic Acid.
    DB00130. L-Glutamine.

    PTM databases

    PhosphoSitei Q9UI32.

    Polymorphism databases

    DMDMi 145559477.

    Proteomic databases

    MaxQBi Q9UI32.
    PaxDbi Q9UI32.
    PRIDEi Q9UI32.

    Protocols and materials databases

    DNASUi 27165.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311966 ; ENSP00000310447 ; ENSG00000135423 .
    GeneIDi 27165.
    KEGGi hsa:27165.
    UCSCi uc001slj.3. human.

    Organism-specific databases

    CTDi 27165.
    GeneCardsi GC12M056864.
    HGNCi HGNC:29570. GLS2.
    HPAi HPA038608.
    MIMi 606365. gene.
    neXtProti NX_Q9UI32.
    PharmGKBi PA134933506.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2066.
    HOGENOMi HOG000216891.
    HOVERGENi HBG005856.
    InParanoidi Q9UI32.
    KOi K01425.
    OMAi CVKPLTY.
    OrthoDBi EOG7S4X5F.
    PhylomeDBi Q9UI32.
    TreeFami TF313359.

    Enzyme and pathway databases

    Reactomei REACT_12591. Glutamate Neurotransmitter Release Cycle.
    REACT_238. Amino acid synthesis and interconversion (transamination).
    SABIO-RK Q9UI32.

    Miscellaneous databases

    GenomeRNAii 27165.
    NextBioi 49960.
    PROi Q9UI32.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UI32.
    Bgeei Q9UI32.
    CleanExi HS_GLS2.
    Genevestigatori Q9UI32.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    3.40.710.10. 1 hit.
    HAMAPi MF_00313. Glutaminase.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR012338. Beta-lactam/transpept-like.
    IPR015868. Glutaminase.
    [Graphical view ]
    PANTHERi PTHR12544. PTHR12544. 1 hit.
    Pfami PF12796. Ank_2. 1 hit.
    PF04960. Glutaminase. 1 hit.
    [Graphical view ]
    SMARTi SM00248. ANK. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    SSF56601. SSF56601. 1 hit.
    TIGRFAMsi TIGR03814. Gln_ase. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, sequencing and expression studies of the human breast cancer cell glutaminase."
      Gomez-Fabre P.M., Aledo J.C., del Castillo-Olivares A., Alonso F.J., Nunez de Castro I., Campos J.A., Marquez J.
      Biochem. J. 345:365-375(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Brain and Mammary cancer.
    2. "Genomic organization and transcriptional analysis of the human l-glutaminase gene."
      Perez-Gomez C., Mates J.M., Gomez-Fabre P.M., del Castillo-Olivares A., Alonso F.J., Marquez J.
      Biochem. J. 370:771-784(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Brain and Mammary cancer.
    3. "Identification and expression of human renal and hepatic glutaminase isoforms."
      Chavez R.A., Wang C., Cong R., Hawkinson J.E., Forsayeth J.R.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-581.
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The C-terminus of human glutaminase L mediates association with PDZ domain-containing proteins."
      Olalla L., Aledo J.C., Bannenberg G., Marquez J.
      FEBS Lett. 488:116-122(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNTA1 AND TAX1BP3.
    6. "Glutaminase 2, a novel p53 target gene regulating energy metabolism and antioxidant function."
      Hu W., Zhang C., Wu R., Sun Y., Levine A., Feng Z.
      Proc. Natl. Acad. Sci. U.S.A. 107:7455-7460(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.

    Entry informationi

    Entry nameiGLSL_HUMAN
    AccessioniPrimary (citable) accession number: Q9UI32
    Secondary accession number(s): Q8IX91, Q9NYY2, Q9UI31
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3