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Q9UI32

- GLSL_HUMAN

UniProt

Q9UI32 - GLSL_HUMAN

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Protein

Glutaminase liver isoform, mitochondrial

Gene

GLS2

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

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9UI32.
CleanExiHS_GLS2.
ExpressionAtlasiQ9UI32. baseline and differential.
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 – 17115Combined sources
Beta strandi195 – 2006Combined sources
Beta strandi205 – 2106Combined sources
Helixi218 – 2214Combined sources
Helixi222 – 23312Combined sources
Helixi235 – 2384Combined sources
Turni239 – 2413Combined sources
Helixi268 – 27710Combined sources
Turni278 – 2814Combined sources
Helixi284 – 29815Combined sources
Turni299 – 3013Combined sources
Helixi308 – 31710Combined sources
Helixi319 – 33012Combined sources
Helixi340 – 35112Combined sources
Beta strandi353 – 3553Combined sources
Helixi357 – 36812Combined sources
Turni369 – 3713Combined sources
Turni374 – 3763Combined sources
Helixi383 – 39614Combined sources
Helixi399 – 4013Combined sources
Helixi402 – 4087Combined sources
Beta strandi413 – 4153Combined sources
Beta strandi419 – 4257Combined sources
Turni426 – 4283Combined sources
Beta strandi429 – 4346Combined sources
Beta strandi442 – 4443Combined sources
Helixi445 – 45814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000010463.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UI32-1) [UniParc]FASTAAdd to Basket

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
MRSMKALQKA LSRAGSHCGR GGWGHPSRSP LLGGGVRHHL SEAAAQGRET
60 70 80 90 100
PHSHQPQHQD HDSSESGMLS RLGDLLFYTI AEGQERIPIH KFTTALKATG
110 120 130 140 150
LQTSDPRLRD CMSEMHRVVQ ESSSGGLLDR DLFRKCVSSN IVLLTQAFRK
160 170 180 190 200
KFVIPDFEEF TGHVDRIFED VKELTGGKVA AYIPQLAKSN PDLWGVSLCT
210 220 230 240 250
VDGQRHSVGH TKIPFCLQSC VKPLTYAISI STLGTDYVHK FVGKEPSGLR
260 270 280 290 300
YNKLSLNEEG IPHNPMVNAG AIVVSSLIKM DCNKAEKFDF VLQYLNKMAG
310 320 330 340 350
NEYMGFSNAT FQSEKETGDR NYAIGYYLKE KKCFPKGVDM MAALDLYFQL
360 370 380 390 400
CSVEVTCESG SVMAATLANG GICPITGESV LSAEAVRNTL SLMHSCGMYD
410 420 430 440 450
FSGQFAFHVG LPAKSAVSGA ILLVVPNVMG MMCLSPPLDK LGNSHRGTSF
460 470 480 490 500
CQKLVSLFNF HNYDNLRHCA RKLDPRREGA EIRNKTVVNL LFAAYSGDVS
510 520 530 540 550
ALRRFALSAM DMEQKDYDSR TALHVAAAEG HIEVVKFLIE ACKVNPFAKD
560 570 580 590 600
RWGNIPLDDA VQFNHLEVVK LLQDYQDSYT LSETQAEAAA EALSKENLES

MV
Length:602
Mass (Da):66,323
Last modified:April 17, 2007 - v2
Checksum:i6D0E1EFF01BC3843
GO
Isoform 2 (identifier: Q9UI32-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     136-209: CVSSNIVLLT...TVDGQRHSVG → HSERSLSFLI...QRSPSACSPV
     210-602: Missing.

Note: No experimental confirmation available

Show »
Length:209
Mass (Da):23,055
Checksum:iC3D6450C81DD26AD
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei136 – 20974CVSSN…RHSVG → HSERSLSFLILRSSRAMWIA SLRMSKSSLEAKWQPTSLSW PSQTQTCGVSPCALWMVNGT LWATQRSPSACSPV in isoform 2. 1 PublicationVSP_057009Add
BLAST
Alternative sequencei210 – 602393Missing in isoform 2. 1 PublicationVSP_057010Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF110330 mRNA. Translation: AAF21933.1.
AF110331 mRNA. Translation: AAF21934.1.
AF348119 Genomic DNA. Translation: AAO13298.2.
AF223944 mRNA. Translation: AAF33826.1.
AK303772 mRNA. Translation: BAH14045.1.
AC097104 Genomic DNA. No translation available.
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. [Q9UI32-1]
ENST00000486896; ENSP00000419661; ENSG00000135423. [Q9UI32-2]
GeneIDi27165.
KEGGihsa:27165.
UCSCiuc001slj.3. human. [Q9UI32-1]

Polymorphism databases

DMDMi145559477.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF110330 mRNA. Translation: AAF21933.1 .
AF110331 mRNA. Translation: AAF21934.1 .
AF348119 Genomic DNA. Translation: AAO13298.2 .
AF223944 mRNA. Translation: AAF33826.1 .
AK303772 mRNA. Translation: BAH14045.1 .
AC097104 Genomic DNA. No translation available.
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:
PDBei
RCSB PDBi
PDBji
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 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 . [Q9UI32-1 ]
ENST00000486896 ; ENSP00000419661 ; ENSG00000135423 . [Q9UI32-2 ]
GeneIDi 27165.
KEGGi hsa:27165.
UCSCi uc001slj.3. human. [Q9UI32-1 ]

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.
GeneTreei ENSGT00390000010463.
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

ChiTaRSi GLS2. human.
GenomeRNAii 27165.
NextBioi 49960.
PROi Q9UI32.
SOURCEi Search...

Gene expression databases

Bgeei Q9UI32.
CleanExi HS_GLS2.
ExpressionAtlasi Q9UI32. baseline and differential.
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

« Hide 'large scale' publications
  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] (ISOFORM 1), 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] (ISOFORM 1), VARIANT PRO-581.
    Tissue: Brain.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Liver.
  5. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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.
  8. "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): B7Z8Q9
, Q8IX91, Q9NYY2, Q9UI31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: April 17, 2007
Last modified: November 26, 2014
This is version 134 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