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Q9UI32 (GLSL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutaminase liver isoform, mitochondrial

Short name=GLS
EC=3.5.1.2
Alternative name(s):
L-glutaminase
L-glutamine amidohydrolase
Gene names
Name:GLS2
Synonyms:GA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length602 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.6

Catalytic activity

L-glutamine + H2O = L-glutamate + NH3. HAMAP-Rule MF_00313

Subunit structure

Interacts with the PDZ domain of the syntrophin SNTA1. Interacts with the PDZ domain of TAX1BP3. Ref.5

Subcellular location

Mitochondrion Ref.6.

Tissue specificity

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. Ref.1 Ref.6

Induction

Up-regulated by P53 (at protein and mRNA level) under both stressed and non-stressed conditions. Ref.6

Sequence similarities

Belongs to the glutaminase family.

Contains 2 ANK repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1414Mitochondrion Potential
Chain15 – 602588Glutaminase liver isoform, mitochondrial HAMAP-Rule MF_00313
PRO_0000011625

Regions

Repeat518 – 55134ANK 1 HAMAP-Rule MF_00313
Repeat552 – 58534ANK 2 HAMAP-Rule MF_00313

Sites

Binding site2191Substrate By similarity
Binding site2681Substrate By similarity
Binding site3141Substrate By similarity
Binding site3211Substrate By similarity
Binding site3471Substrate By similarity
Binding site3991Substrate By similarity
Binding site4171Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue2531N6-succinyllysine By similarity
Modified residue2791N6-acetyllysine By similarity
Modified residue2841N6-acetyllysine By similarity
Modified residue3291N6-acetyllysine By similarity

Natural variations

Natural variant5811L → P. Ref.3
Corresponds to variant rs2657879 [ dbSNP | Ensembl ].
VAR_031615

Experimental info

Sequence conflict871I → T in AAF21933. Ref.1
Sequence conflict1401N → S in AAF21933. Ref.1
Sequence conflict2571N → D in AAF21933. Ref.1
Sequence conflict328 – 3292LK → HE in AAF21933. Ref.1
Sequence conflict5601A → V in AAF33826. Ref.3

Secondary structure

.............................................. 602
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UI32 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: 6D0E1EFF01BC3843

FASTA60266,323
        10         20         30         40         50         60 
MRSMKALQKA LSRAGSHCGR GGWGHPSRSP LLGGGVRHHL SEAAAQGRET PHSHQPQHQD 

        70         80         90        100        110        120 
HDSSESGMLS RLGDLLFYTI AEGQERIPIH KFTTALKATG LQTSDPRLRD CMSEMHRVVQ 

       130        140        150        160        170        180 
ESSSGGLLDR DLFRKCVSSN IVLLTQAFRK KFVIPDFEEF TGHVDRIFED VKELTGGKVA 

       190        200        210        220        230        240 
AYIPQLAKSN PDLWGVSLCT VDGQRHSVGH TKIPFCLQSC VKPLTYAISI STLGTDYVHK 

       250        260        270        280        290        300 
FVGKEPSGLR YNKLSLNEEG IPHNPMVNAG AIVVSSLIKM DCNKAEKFDF VLQYLNKMAG 

       310        320        330        340        350        360 
NEYMGFSNAT FQSEKETGDR NYAIGYYLKE KKCFPKGVDM MAALDLYFQL CSVEVTCESG 

       370        380        390        400        410        420 
SVMAATLANG GICPITGESV LSAEAVRNTL SLMHSCGMYD FSGQFAFHVG LPAKSAVSGA 

       430        440        450        460        470        480 
ILLVVPNVMG MMCLSPPLDK LGNSHRGTSF CQKLVSLFNF HNYDNLRHCA RKLDPRREGA 

       490        500        510        520        530        540 
EIRNKTVVNL LFAAYSGDVS ALRRFALSAM DMEQKDYDSR TALHVAAAEG HIEVVKFLIE 

       550        560        570        580        590        600 
ACKVNPFAKD RWGNIPLDDA VQFNHLEVVK LLQDYQDSYT LSETQAEAAA EALSKENLES 


MV 

« Hide

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001267727.1. NM_001280798.1.
NP_037399.2. NM_013267.3.
UniGeneHs.212606.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BQMX-ray2.18A/B154-479[»]
ProteinModelPortalQ9UI32.
SMRQ9UI32. Positions 72-601.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118044. 2 interactions.
IntActQ9UI32. 1 interaction.
MINTMINT-157952.
STRING9606.ENSP00000310447.

Chemistry

DrugBankDB00142. L-Glutamic Acid.
DB00130. L-Glutamine.

PTM databases

PhosphoSiteQ9UI32.

Polymorphism databases

DMDM145559477.

Proteomic databases

PaxDbQ9UI32.
PRIDEQ9UI32.

Protocols and materials databases

DNASU27165.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311966; ENSP00000310447; ENSG00000135423.
GeneID27165.
KEGGhsa:27165.
UCSCuc001slj.3. human.

Organism-specific databases

CTD27165.
GeneCardsGC12M056864.
HGNCHGNC:29570. GLS2.
HPAHPA038608.
MIM606365. gene.
neXtProtNX_Q9UI32.
PharmGKBPA134933506.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2066.
HOGENOMHOG000216891.
HOVERGENHBG005856.
InParanoidQ9UI32.
KOK01425.
OMAEGGEVRN.
OrthoDBEOG7S4X5F.
PhylomeDBQ9UI32.
TreeFamTF313359.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_13685. Neuronal System.
SABIO-RKQ9UI32.

Gene expression databases

ArrayExpressQ9UI32.
BgeeQ9UI32.
CleanExHS_GLS2.
GenevestigatorQ9UI32.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
3.40.710.10. 1 hit.
HAMAPMF_00313. Glutaminase.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR012338. Beta-lactam/transpept-like.
IPR015868. Glutaminase.
[Graphical view]
PANTHERPTHR12544. PTHR12544. 1 hit.
PfamPF12796. Ank_2. 1 hit.
PF04960. Glutaminase. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF56601. SSF56601. 1 hit.
TIGRFAMsTIGR03814. Gln_ase. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi27165.
NextBio49960.
PROQ9UI32.
SOURCESearch...

Entry information

Entry nameGLSL_HUMAN
AccessionPrimary (citable) accession number: Q9UI32
Secondary accession number(s): Q8IX91, Q9NYY2, Q9UI31
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: April 17, 2007
Last modified: April 16, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM