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O94925

- GLSK_HUMAN

UniProt

O94925 - GLSK_HUMAN

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Protein
Glutaminase kidney isoform, mitochondrial
Gene
GLS, GLS1, KIAA0838
Organism
Homo sapiens (Human)
Status
Reviewed - 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.UniRule annotation

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)

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

  1. glutaminase activity Source: UniProtKB
  2. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. cellular amino acid biosynthetic process Source: Reactome
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. glutamate biosynthetic process Source: UniProtKB
  4. glutamate secretion Source: Reactome
  5. glutamine catabolic process Source: UniProtKB
  6. neurotransmitter secretion Source: Reactome
  7. protein homotetramerization Source: UniProtKB
  8. regulation of respiratory gaseous exchange by neurological system process Source: Ensembl
  9. small molecule metabolic process Source: Reactome
  10. suckling behavior Source: Ensembl
  11. synaptic transmission Source: Reactome
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).

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: Chromosome 2

Organism-specific databases

HGNCiHGNC:4331. GLS.

Subcellular locationi

Isoform 1 : Cytoplasmcytosol 2 Publications
Isoform 3 : Mitochondrion 2 Publications

GO - Cellular componenti

  1. cytosol Source: UniProtKB-SubCell
  2. mitochondrial matrix Source: Reactome
  3. 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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1616Mitochondrion By similarity
Add
BLAST
Chaini17 – 669653Glutaminase kidney isoform, mitochondrialUniRule annotation
PRO_0000011622Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei130 – 1301N6-succinyllysine By similarity
Modified residuei164 – 1641N6-succinyllysine By 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.2 Publications

Gene expression databases

ArrayExpressiO94925.
BgeeiO94925.
CleanExiHS_GLS.
GenevestigatoriO94925.

Organism-specific databases

HPAiHPA036223.

Interactioni

Subunit structurei

Heterotetramer. Interacts with ATCAY; the interaction is direct and may control GLS localization, negatively regulating its activity.2 Publications

Protein-protein interaction databases

BioGridi109006. 12 interactions.
DIPiDIP-50591N.
IntActiO94925. 2 interactions.
MINTiMINT-4096121.
STRINGi9606.ENSP00000317379.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiO94925.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati585 – 61430ANK 1UniRule annotation
Add
BLAST
Repeati619 – 64830ANK 2UniRule annotation
Add
BLAST

Sequence similaritiesi

Belongs to the glutaminase family.
Contains 2 ANK repeats.

Keywords - Domaini

ANK repeat, Repeat, Transit peptide

Phylogenomic databases

eggNOGiCOG2066.
HOGENOMiHOG000216891.
HOVERGENiHBG005856.
InParanoidiO94925.
KOiK01425.
OMAiGMDMEQR.
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. Align

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

MMRLRGSGML RDLLLRSPAG VSATLRRAQP LVTLCRRPRG GGRPAAGPAA    50
AARLHPWWGG GGWPAEPLAR GLSSSPSEIL QELGKGSTHP QPGVSPPAAP 100
AAPGPKDGPG ETDAFGNSEG KELVASGENK IKQGLLPSLE DLLFYTIAEG 150
QEKIPVHKFI TALKSTGLRT SDPRLKECMD MLRLTLQTTS DGVMLDKDLF 200
KKCVQSNIVL LTQAFRRKFV IPDFMSFTSH IDELYESAKK QSGGKVADYI 250
PQLAKFSPDL WGVSVCTVDG QRHSTGDTKV PFCLQSCVKP LKYAIAVNDL 300
GTEYVHRYVG KEPSGLRFNK LFLNEDDKPH NPMVNAGAIV VTSLIKQGVN 350
NAEKFDYVMQ FLNKMAGNEY VGFSNATFQS ERESGDRNFA IGYYLKEKKC 400
FPEGTDMVGI LDFYFQLCSI EVTCESASVM AATLANGGFC PITGERVLSP 450
EAVRNTLSLM HSCGMYDFSG QFAFHVGLPA KSGVAGGILL VVPNVMGMMC 500
WSPPLDKMGN SVKGIHFCHD LVSLCNFHNY DNLRHFAKKL DPRREGGDQR 550
VKSVINLLFA AYTGDVSALR RFALSAMDME QRDYDSRTAL HVAAAEGHVE 600
VVKFLLEACK VNPFPKDRWN NTPMDEALHF GHHDVFKILQ EYQVQYTPQG 650
DSDNGKENQT VHKNLDGLL 669
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.

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.
VSP_001765
Alternative sequencei170 – 669500Missing in isoform 2.
VSP_001766Add
BLAST
Alternative sequencei551 – 669119VKSVI…LDGLL → HSFGPLDYESLQQELALKET VWKKVSPESNEDISTTVVYR MESLGEKS in isoform 3.
VSP_001767Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61G → S in AAF00090. 1 Publication
Sequence conflicti66 – 661E → D in AAF00090. 1 Publication
Sequence conflicti219 – 2191F → L in AAG47842. 1 Publication
Sequence conflicti268 – 2681V → A in AAD47056. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2308.1. [O94925-1 ]
CCDS58744.1. [O94925-3 ]
RefSeqi NP_001243239.1. NM_001256310.1. [O94925-3 ]
NP_055720.3. NM_014905.4. [O94925-1 ]
UniGenei Hs.116448.
Hs.737608.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3CZD X-ray 2.40 A 221-533 [» ]
3UNW X-ray 2.56 A/B/C/D 71-597 [» ]
3UO9 X-ray 2.30 A/B/C/D 71-597 [» ]
3VOY X-ray 2.20 A 221-533 [» ]
3VOZ X-ray 2.40 A 221-533 [» ]
3VP0 X-ray 2.40 A 221-533 [» ]
3VP1 X-ray 2.30 A 221-533 [» ]
3VP2 X-ray 2.70 A 221-533 [» ]
3VP3 X-ray 2.70 A 221-533 [» ]
3VP4 X-ray 2.45 A 221-533 [» ]
4O7D X-ray 2.30 A 221-531 [» ]
ProteinModelPortali O94925.
SMRi O94925. Positions 137-641.
ModBasei Search...

Protein-protein interaction databases

BioGridi 109006. 12 interactions.
DIPi DIP-50591N.
IntActi O94925. 2 interactions.
MINTi MINT-4096121.
STRINGi 9606.ENSP00000317379.

Chemistry

ChEMBLi CHEMBL2146302.
DrugBanki DB00142. L-Glutamic Acid.
DB00130. L-Glutamine.

PTM databases

PhosphoSitei O94925.

Proteomic databases

MaxQBi O94925.
PaxDbi O94925.
PeptideAtlasi O94925.
PRIDEi O94925.

Protocols and materials databases

DNASUi 2744.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000320717 ; ENSP00000317379 ; ENSG00000115419 . [O94925-1 ]
ENST00000338435 ; ENSP00000340689 ; ENSG00000115419 . [O94925-3 ]
GeneIDi 2744.
KEGGi hsa:2744.
UCSCi uc002usd.2. human. [O94925-2 ]
uc002use.3. human. [O94925-3 ]
uc002usf.3. human. [O94925-1 ]

Organism-specific databases

CTDi 2744.
GeneCardsi GC02P191709.
H-InvDB HIX0161645.
HGNCi HGNC:4331. GLS.
HPAi HPA036223.
MIMi 138280. gene.
neXtProti NX_O94925.
PharmGKBi PA28734.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2066.
HOGENOMi HOG000216891.
HOVERGENi HBG005856.
InParanoidi O94925.
KOi K01425.
OMAi GMDMEQR.
OrthoDBi EOG7S4X5F.
PhylomeDBi O94925.
TreeFami TF313359.

Enzyme and pathway databases

BRENDAi 3.5.1.2. 2681.
Reactomei REACT_12591. Glutamate Neurotransmitter Release Cycle.
REACT_238. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

ChiTaRSi GLS. human.
EvolutionaryTracei O94925.
GenomeRNAii 2744.
NextBioi 10816.
PROi O94925.
SOURCEi Search...

Gene expression databases

ArrayExpressi O94925.
Bgeei O94925.
CleanExi HS_GLS.
Genevestigatori O94925.

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

« 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. "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.
  15. "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: September 3, 2014
This is version 146 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 (1 Publication), but has been shown to be well expressed (1 Publication and 1 Publication) and the encoded protein is detected in mitochondria (1 Publication).
A report observed N-glycosylation at Asn-620 (1 Publication). However, as the protein is mitochondrial, additional evidences are required to confirm this result.

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

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