Glutaminase liver isoform, mitochondrial precursor

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Q9UI32 (GLSL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	602 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	ANK repeat Repeat Transit peptide
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular amino acid biosynthetic process Traceable author statement. Source: Reactome cellular nitrogen compound metabolic process Traceable author statement. Source: Reactome glutamate secretion Traceable author statement. Source: Reactome glutamine metabolic process Inferred from electronic annotation. Source: InterPro neurotransmitter secretion Traceable author statement. Source: Reactome reactive oxygen species metabolic process Inferred from mutant phenotype PubMed 20351271. Source: MGI regulation of apoptotic process Inferred from mutant phenotype PubMed 20351271. Source: MGI
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome
Molecular_function	glutaminase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 14

Mitochondrion Potential

Chain

15 – 602

588

Glutaminase liver isoform, mitochondrial

PRO_0000011625

Regions

Repeat

518 – 551

ANK 1

Repeat

552 – 585

ANK 2

Sites

Binding site

219

Substrate By similarity

Binding site

268

Substrate By similarity

Binding site

314

Substrate By similarity

Binding site

321

Substrate By similarity

Binding site

347

Substrate By similarity

Binding site

399

Substrate By similarity

Binding site

417

Substrate; via amide nitrogen By similarity

Natural variations

Natural variant

581

L → P. Ref.3
Corresponds to variant rs2657879 [ dbSNP | Ensembl ].

VAR_031615

Experimental info

Sequence conflict

I → T in AAF21933. Ref.1

Sequence conflict

140

N → S in AAF21933. Ref.1

Sequence conflict

257

N → D in AAF21933. Ref.1

Sequence conflict

328 – 329

LK → HE in AAF21933. Ref.1

Sequence conflict

560

A → V in AAF33826. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q9UI32 [UniParc].

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

602

66,323

        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' referencesShow '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. 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.
IPI	IPI00296219.
RefSeq	NP_037399.2. NM_013267.2.
UniGene	Hs.212606.
3D structure databases
ProteinModelPortal	Q9UI32.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UI32. 1 interaction.
STRING	9606.ENSP00000310447.
PTM databases
PhosphoSite	Q9UI32.
Polymorphism databases
DMDM	145559477.
Proteomic databases
PaxDb	Q9UI32.
PRIDE	Q9UI32.
Protocols and materials databases
DNASU	27165.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000311966; ENSP00000310447; ENSG00000135423.
GeneID	27165.
KEGG	hsa:27165.
UCSC	uc001slj.3. human.
Organism-specific databases
CTD	27165.
GeneCards	GC12M056864.
HGNC	HGNC:29570. GLS2.
HPA	HPA038608.
MIM	606365. gene.
neXtProt	NX_Q9UI32.
PharmGKB	PA134933506.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2066.
HOGENOM	HOG000216891.
HOVERGEN	HBG005856.
InParanoid	Q9UI32.
KO	K01425.
OMA	CQKLVSL.
OrthoDB	EOG4ZS92W.
PhylomeDB	Q9UI32.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_13685. Neuronal System.
SABIO-RK	Q9UI32.
Gene expression databases
ArrayExpress	Q9UI32.
Bgee	Q9UI32.
CleanEx	HS_GLS2.
Genevestigator	Q9UI32.
GermOnline	ENSG00000135423. Homo sapiens.
Family and domain databases
Gene3D	1.25.40.20. 1 hit. 3.40.710.10. 1 hit.
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR012338. Beta-lactam/transpept-like. IPR015868. Glutaminase. [Graphical view]
PANTHER	PTHR12544. PTHR12544. 1 hit.
Pfam	PF12796. Ank_2. 1 hit. PF04960. Glutaminase. 1 hit. [Graphical view]
SMART	SM00248. ANK. 2 hits. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit. SSF56601. PBP_transp_fold. 1 hit.
TIGRFAMs	TIGR03814. Gln_ase. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00142. L-Glutamic Acid. DB00130. L-Glutamine.
GenomeRNAi	27165.
NextBio	49960.
SOURCE	Search...

Entry information

Entry name

GLSL_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

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

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents