Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutaminase kidney isoform, mitochondrial

Gene

GLS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate in the brain. Isoform 2 lacks catalytic activity.

Catalytic activityi

L-glutamine + H2O = L-glutamate + NH3.1 Publication

Enzyme regulationi

Isoform 1 and isoform 3 are activated by phosphate. Inhibited by BPTES. BPTES binds between subunits and favors dissociation of the tetramer into dimers.1 Publication

Kineticsi

  1. KM=1.9 mM for glutamine (isoform 1)1 Publication
  2. KM=1.4 mM for glutamine (isoform 3)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei286 – 2861Substrate
    Binding sitei335 – 3351Substrate
    Binding sitei381 – 3811Substrate
    Binding sitei388 – 3881Substrate
    Binding sitei414 – 4141Substrate
    Binding sitei466 – 4661Substrate
    Binding sitei484 – 4841Substrate; via amide nitrogen

    GO - Molecular functioni

    • glutaminase activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BRENDAi3.5.1.2. 2681.
    ReactomeiREACT_12591. Glutamate Neurotransmitter Release Cycle.
    REACT_238. Amino acid synthesis and interconversion (transamination).
    REACT_355377. TP53 Regulates Metabolic Genes.
    SABIO-RKO94925.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutaminase kidney isoform, mitochondrial (EC:3.5.1.2)
    Short name:
    GLS
    Alternative name(s):
    K-glutaminase
    L-glutamine amidohydrolase
    Gene namesi
    Name:GLS
    Synonyms:GLS1, KIAA0838
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:4331. GLS.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB-SubCell
    • mitochondrial matrix Source: Reactome
    • mitochondrion Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi318 – 3181F → Y: No effect on catalytic activity. Loss of inhibition by BPTES; when associated with S-322. 1 Publication
    Mutagenesisi322 – 3221F → S: No effect on catalytic activity. Loss of inhibition by BPTES; when associated with Y-318. 1 Publication
    Mutagenesisi394 – 3941Y → L: No effect on catalytic activity. Loss of inhibition by BPTES. 1 Publication

    Organism-specific databases

    PharmGKBiPA28734.

    Chemistry

    DrugBankiDB00130. L-Glutamine.

    Polymorphism and mutation databases

    BioMutaiGLS.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1616MitochondrionBy similarityAdd
    BLAST
    Chaini17 – 669653Glutaminase kidney isoform, mitochondrialPRO_0000011622Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei130 – 1301N6-succinyllysineBy similarity
    Modified residuei164 – 1641N6-succinyllysineBy similarity
    Modified residuei311 – 3111N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO94925.
    PaxDbiO94925.
    PeptideAtlasiO94925.
    PRIDEiO94925.

    PTM databases

    PhosphoSiteiO94925.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 3 are detected in brain cortex. Isoform 3 is highly expressed in astrocytoma, ganglioglioma and ependymoma. Isoform 1 is highly expressed in brain and kidney, but not detected in liver. Isoform 3 is highly expressed in heart and pancreas, detected at lower levels in placenta, lung, pancreas and kidney, but is not detected in liver. Isoform 2 is expressed in cardiac and skeletal muscle.1 Publication

    Gene expression databases

    BgeeiO94925.
    CleanExiHS_GLS.
    ExpressionAtlasiO94925. baseline and differential.
    GenevisibleiO94925. HS.

    Organism-specific databases

    HPAiHPA036223.

    Interactioni

    Subunit structurei

    Heterotetramer. Interacts with ATCAY; the interaction is direct and may control GLS localization, negatively regulating its activity.3 Publications

    Protein-protein interaction databases

    BioGridi109006. 20 interactions.
    DIPiDIP-50591N.
    IntActiO94925. 2 interactions.
    MINTiMINT-4096121.
    STRINGi9606.ENSP00000317379.

    Structurei

    Secondary structure

    1
    669
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi139 – 14810Combined sources
    Beta strandi152 – 1554Combined sources
    Helixi156 – 16510Combined sources
    Helixi173 – 1753Combined sources
    Helixi176 – 18813Combined sources
    Helixi197 – 2048Combined sources
    Helixi205 – 2073Combined sources
    Helixi208 – 2169Combined sources
    Beta strandi219 – 2235Combined sources
    Helixi224 – 23916Combined sources
    Beta strandi244 – 2463Combined sources
    Helixi251 – 2544Combined sources
    Beta strandi262 – 2676Combined sources
    Beta strandi272 – 2776Combined sources
    Helixi285 – 2873Combined sources
    Helixi288 – 30518Combined sources
    Turni306 – 3083Combined sources
    Beta strandi315 – 3173Combined sources
    Helixi335 – 3428Combined sources
    Turni343 – 3486Combined sources
    Helixi351 – 36515Combined sources
    Turni366 – 3683Combined sources
    Beta strandi371 – 3733Combined sources
    Helixi375 – 3839Combined sources
    Helixi386 – 39712Combined sources
    Helixi407 – 41812Combined sources
    Beta strandi420 – 4223Combined sources
    Helixi424 – 43512Combined sources
    Turni436 – 4383Combined sources
    Turni441 – 4433Combined sources
    Helixi450 – 46314Combined sources
    Helixi466 – 4683Combined sources
    Helixi469 – 4757Combined sources
    Beta strandi480 – 4823Combined sources
    Beta strandi486 – 4927Combined sources
    Turni493 – 4953Combined sources
    Beta strandi496 – 5016Combined sources
    Beta strandi503 – 5053Combined sources
    Beta strandi509 – 5113Combined sources
    Helixi512 – 52514Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CZDX-ray2.40A221-533[»]
    3UNWX-ray2.56A/B/C/D71-597[»]
    3UO9X-ray2.30A/B/C/D71-597[»]
    3VOYX-ray2.20A221-533[»]
    3VOZX-ray2.40A221-533[»]
    3VP0X-ray2.40A221-533[»]
    3VP1X-ray2.30A221-533[»]
    3VP2X-ray2.70A221-533[»]
    3VP3X-ray2.70A221-533[»]
    3VP4X-ray2.45A221-533[»]
    4O7DX-ray2.30A221-531[»]
    ProteinModelPortaliO94925.
    SMRiO94925. Positions 137-641.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO94925.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati585 – 61430ANK 1Add
    BLAST
    Repeati619 – 64830ANK 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.
    GeneTreeiENSGT00390000010463.
    HOGENOMiHOG000216891.
    HOVERGENiHBG005856.
    InParanoidiO94925.
    KOiK01425.
    OMAiQCCSMEA.
    OrthoDBiEOG7S4X5F.
    PhylomeDBiO94925.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: O94925-1) [UniParc]FASTAAdd to basket

    Also known as: KGA

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MMRLRGSGML RDLLLRSPAG VSATLRRAQP LVTLCRRPRG GGRPAAGPAA
    60 70 80 90 100
    AARLHPWWGG GGWPAEPLAR GLSSSPSEIL QELGKGSTHP QPGVSPPAAP
    110 120 130 140 150
    AAPGPKDGPG ETDAFGNSEG KELVASGENK IKQGLLPSLE DLLFYTIAEG
    160 170 180 190 200
    QEKIPVHKFI TALKSTGLRT SDPRLKECMD MLRLTLQTTS DGVMLDKDLF
    210 220 230 240 250
    KKCVQSNIVL LTQAFRRKFV IPDFMSFTSH IDELYESAKK QSGGKVADYI
    260 270 280 290 300
    PQLAKFSPDL WGVSVCTVDG QRHSTGDTKV PFCLQSCVKP LKYAIAVNDL
    310 320 330 340 350
    GTEYVHRYVG KEPSGLRFNK LFLNEDDKPH NPMVNAGAIV VTSLIKQGVN
    360 370 380 390 400
    NAEKFDYVMQ FLNKMAGNEY VGFSNATFQS ERESGDRNFA IGYYLKEKKC
    410 420 430 440 450
    FPEGTDMVGI LDFYFQLCSI EVTCESASVM AATLANGGFC PITGERVLSP
    460 470 480 490 500
    EAVRNTLSLM HSCGMYDFSG QFAFHVGLPA KSGVAGGILL VVPNVMGMMC
    510 520 530 540 550
    WSPPLDKMGN SVKGIHFCHD LVSLCNFHNY DNLRHFAKKL DPRREGGDQR
    560 570 580 590 600
    VKSVINLLFA AYTGDVSALR RFALSAMDME QRDYDSRTAL HVAAAEGHVE
    610 620 630 640 650
    VVKFLLEACK VNPFPKDRWN NTPMDEALHF GHHDVFKILQ EYQVQYTPQG
    660
    DSDNGKENQT VHKNLDGLL
    Length:669
    Mass (Da):73,461
    Last modified:May 1, 1999 - v1
    Checksum:i4E5E63505E84E0B7
    GO
    Isoform 2 (identifier: O94925-2) [UniParc]FASTAAdd to basket

    Also known as: GAM

    The sequence of this isoform differs from the canonical sequence as follows:
         162-169: ALKSTGLR → VSFYIFLS
         170-669: Missing.

    Show »
    Length:169
    Mass (Da):17,738
    Checksum:i869F0D4A9B2B3AEE
    GO
    Isoform 3 (identifier: O94925-3) [UniParc]FASTAAdd to basket

    Also known as: Glutaminase C, GAC

    The sequence of this isoform differs from the canonical sequence as follows:
         551-669: VKSVINLLFA...TVHKNLDGLL → HSFGPLDYES...YRMESLGEKS

    Show »
    Length:598
    Mass (Da):65,460
    Checksum:i3076ED034A79ABA5
    GO

    Sequence cautioni

    The sequence BAA74861.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61G → S in AAF00090 (PubMed:11015561).Curated
    Sequence conflicti66 – 661E → D in AAF00090 (PubMed:11015561).Curated
    Sequence conflicti219 – 2191F → L in AAG47842 (PubMed:10719215).Curated
    Sequence conflicti268 – 2681V → A in AAD47056 (PubMed:11015561).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti254 – 2541A → P.
    Corresponds to variant rs16833035 [ dbSNP | Ensembl ].
    VAR_049188

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei162 – 1698ALKSTGLR → VSFYIFLS in isoform 2. CuratedVSP_001765
    Alternative sequencei170 – 669500Missing in isoform 2. CuratedVSP_001766Add
    BLAST
    Alternative sequencei551 – 669119VKSVI…LDGLL → HSFGPLDYESLQQELALKET VWKKVSPESNEDISTTVVYR MESLGEKS in isoform 3. 1 PublicationVSP_001767Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF158555 mRNA. Translation: AAD47056.1.
    AF097492 mRNA. Translation: AAF00088.1.
    AF097493 mRNA. Translation: AAF00089.1.
    AF097495 mRNA. Translation: AAF00090.1.
    AB020645 mRNA. Translation: BAA74861.2. Different initiation.
    AF223943 mRNA. Translation: AAF33825.1.
    AF327434 mRNA. Translation: AAG47842.1.
    BC038507 mRNA. Translation: AAH38507.2.
    AF279697 mRNA. Translation: AAG17700.1.
    CCDSiCCDS2308.1. [O94925-1]
    CCDS58744.1. [O94925-3]
    RefSeqiNP_001243239.1. NM_001256310.1. [O94925-3]
    NP_055720.3. NM_014905.4. [O94925-1]
    UniGeneiHs.116448.
    Hs.737608.

    Genome annotation databases

    EnsembliENST00000320717; ENSP00000317379; ENSG00000115419. [O94925-1]
    ENST00000338435; ENSP00000340689; ENSG00000115419. [O94925-3]
    GeneIDi2744.
    KEGGihsa:2744.
    UCSCiuc002usd.2. human. [O94925-2]
    uc002use.3. human. [O94925-3]
    uc002usf.3. human. [O94925-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF158555 mRNA. Translation: AAD47056.1.
    AF097492 mRNA. Translation: AAF00088.1.
    AF097493 mRNA. Translation: AAF00089.1.
    AF097495 mRNA. Translation: AAF00090.1.
    AB020645 mRNA. Translation: BAA74861.2. Different initiation.
    AF223943 mRNA. Translation: AAF33825.1.
    AF327434 mRNA. Translation: AAG47842.1.
    BC038507 mRNA. Translation: AAH38507.2.
    AF279697 mRNA. Translation: AAG17700.1.
    CCDSiCCDS2308.1. [O94925-1]
    CCDS58744.1. [O94925-3]
    RefSeqiNP_001243239.1. NM_001256310.1. [O94925-3]
    NP_055720.3. NM_014905.4. [O94925-1]
    UniGeneiHs.116448.
    Hs.737608.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CZDX-ray2.40A221-533[»]
    3UNWX-ray2.56A/B/C/D71-597[»]
    3UO9X-ray2.30A/B/C/D71-597[»]
    3VOYX-ray2.20A221-533[»]
    3VOZX-ray2.40A221-533[»]
    3VP0X-ray2.40A221-533[»]
    3VP1X-ray2.30A221-533[»]
    3VP2X-ray2.70A221-533[»]
    3VP3X-ray2.70A221-533[»]
    3VP4X-ray2.45A221-533[»]
    4O7DX-ray2.30A221-531[»]
    ProteinModelPortaliO94925.
    SMRiO94925. Positions 137-641.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi109006. 20 interactions.
    DIPiDIP-50591N.
    IntActiO94925. 2 interactions.
    MINTiMINT-4096121.
    STRINGi9606.ENSP00000317379.

    Chemistry

    BindingDBiO94925.
    ChEMBLiCHEMBL2146302.
    DrugBankiDB00130. L-Glutamine.

    PTM databases

    PhosphoSiteiO94925.

    Polymorphism and mutation databases

    BioMutaiGLS.

    Proteomic databases

    MaxQBiO94925.
    PaxDbiO94925.
    PeptideAtlasiO94925.
    PRIDEiO94925.

    Protocols and materials databases

    DNASUi2744.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000320717; ENSP00000317379; ENSG00000115419. [O94925-1]
    ENST00000338435; ENSP00000340689; ENSG00000115419. [O94925-3]
    GeneIDi2744.
    KEGGihsa:2744.
    UCSCiuc002usd.2. human. [O94925-2]
    uc002use.3. human. [O94925-3]
    uc002usf.3. human. [O94925-1]

    Organism-specific databases

    CTDi2744.
    GeneCardsiGC02P191709.
    H-InvDBHIX0161645.
    HGNCiHGNC:4331. GLS.
    HPAiHPA036223.
    MIMi138280. gene.
    neXtProtiNX_O94925.
    PharmGKBiPA28734.
    HUGEiSearch...
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG2066.
    GeneTreeiENSGT00390000010463.
    HOGENOMiHOG000216891.
    HOVERGENiHBG005856.
    InParanoidiO94925.
    KOiK01425.
    OMAiQCCSMEA.
    OrthoDBiEOG7S4X5F.
    PhylomeDBiO94925.
    TreeFamiTF313359.

    Enzyme and pathway databases

    BRENDAi3.5.1.2. 2681.
    ReactomeiREACT_12591. Glutamate Neurotransmitter Release Cycle.
    REACT_238. Amino acid synthesis and interconversion (transamination).
    REACT_355377. TP53 Regulates Metabolic Genes.
    SABIO-RKO94925.

    Miscellaneous databases

    ChiTaRSiGLS. human.
    EvolutionaryTraceiO94925.
    GenomeRNAii2744.
    NextBioi10816.
    PROiO94925.
    SOURCEiSearch...

    Gene expression databases

    BgeeiO94925.
    CleanExiHS_GLS.
    ExpressionAtlasiO94925. baseline and differential.
    GenevisibleiO94925. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and analysis of unique human glutaminase isoforms generated by tissue-specific alternative splicing."
      Elgadi K.M., Meguid R.A., Qian M., Souba W.W., Abcouwer S.F.
      Physiol. Genomics 1:51-62(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
      Tissue: Placenta.
    2. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    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] (ISOFORM 1).
      Tissue: Brain.
    4. "Isolation, characterization and expression of a human brain mitochondrial glutaminase cDNA."
      Holcomb T., Taylor L., Trohkimoinen J., Curthoys N.P.
      Brain Res. Mol. Brain Res. 76:56-63(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    6. "Adenoma and carcinoma cell lines derived from colorectal tumours express different isoforms of glutaminase."
      Turner A., McGivan J.D.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 225-466.
      Tissue: Colon carcinoma.
    7. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    8. "Brain-specific BNIP-2-homology protein Caytaxin relocalises glutaminase to neurite terminals and reduces glutamate levels."
      Buschdorf J.P., Li Chew L., Zhang B., Cao Q., Liang F.Y., Liou Y.C., Zhou Y.T., Low B.C.
      J. Cell Sci. 119:3337-3350(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATCAY, SUBCELLULAR LOCATION.
    9. "Relative expression of mRNAs coding for glutaminase isoforms in CNS tissues and CNS tumors."
      Szeliga M., Matyja E., Obara M., Grajkowska W., Czernicki T., Albrecht J.
      Neurochem. Res. 33:808-813(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY (ISOFORM 1 AND ISOFORM 3).
    10. Cited for: IDENTIFICATION.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Mitochondrial localization and structure-based phosphate activation mechanism of glutaminase C with implications for cancer metabolism."
      Cassago A., Ferreira A.P., Ferreira I.M., Fornezari C., Gomes E.R., Greene K.S., Pereira H.M., Garratt R.C., Dias S.M., Ambrosio A.L.
      Proc. Natl. Acad. Sci. U.S.A. 109:1092-1097(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    15. "Full-length human glutaminase in complex with an allosteric inhibitor."
      DeLaBarre B., Gross S., Fang C., Gao Y., Jha A., Jiang F., Song J.J., Wei W., Hurov J.B.
      Biochemistry 50:10764-10770(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 71-550 (ISOFORM 3) IN COMPLEXES WITH GLUTAMATE AND SYNTHETIC INHIBITOR BPTES, PROTEIN SEQUENCE OF N-TERMINUS, CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-318; PHE-322 AND TYR-394, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
    16. "Human glutaminase in complex with L-glutamate."
      Structural genomics consortium (SGC)
      Submitted (JUL-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 221-533 IN COMPLEX WITH GLUTAMATE.

    Entry informationi

    Entry nameiGLSK_HUMAN
    AccessioniPrimary (citable) accession number: O94925
    Secondary accession number(s): Q9UL05
    , Q9UL06, Q9UL07, Q9UN40
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: May 1, 1999
    Last modified: June 24, 2015
    This is version 154 of the entry and version 1 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

    Caution

    Isoform 3 is predicted to be expressed at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay (PubMed:14759258), but has been shown to be well expressed (PubMed:17940881 and PubMed:11015561) and the encoded protein is detected in mitochondria (PubMed:22228304).2 Publications
    A report observed N-glycosylation at Asn-620 (PubMed:19139490). However, as the protein is mitochondrial, additional evidences are required to confirm this result.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.