CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001499
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutaminase kidney isoform, mitochondrial 
Protein Synonyms/Alias
 GLS; K-glutaminase; L-glutamine amidohydrolase 
Gene Name
 GLS 
Gene Synonyms/Alias
 GLS1; KIAA0838 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
121AFGNSEGKELVASGEubiquitination[1]
158QEKIPVHKFITALKSubiquitination[1]
164HKFITALKSTGLRTSacetylation[2]
176RTSDPRLKECMDMLRubiquitination[3]
197SDGVMLDKDLFKKCVacetylation[4]
279RHSTGDTKVPFCLQSubiquitination[5]
289FCLQSCVKPLKYAIAubiquitination[5]
311YVHRYVGKEPSGLRFacetylation[6]
539NLRHFAKKLDPRREGubiquitination[5]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 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. 
Sequence Annotation
 REPEAT 585 614 ANK 1.
 REPEAT 619 648 ANK 2.
 BINDING 286 286 Substrate.
 BINDING 335 335 Substrate.
 BINDING 381 381 Substrate.
 BINDING 388 388 Substrate.
 BINDING 414 414 Substrate.
 BINDING 466 466 Substrate.
 BINDING 484 484 Substrate; via amide nitrogen.
 MOD_RES 311 311 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; ANK repeat; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Mitochondrion; Polymorphism; Reference proteome; Repeat; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 669 AA 
Protein Sequence
MMRLRGSGML RDLLLRSPAG VSATLRRAQP LVTLCRRPRG GGRPAAGPAA AARLHPWWGG 60
GGWPAEPLAR GLSSSPSEIL QELGKGSTHP QPGVSPPAAP AAPGPKDGPG ETDAFGNSEG 120
KELVASGENK IKQGLLPSLE DLLFYTIAEG QEKIPVHKFI TALKSTGLRT SDPRLKECMD 180
MLRLTLQTTS DGVMLDKDLF KKCVQSNIVL LTQAFRRKFV IPDFMSFTSH IDELYESAKK 240
QSGGKVADYI PQLAKFSPDL WGVSVCTVDG QRHSTGDTKV PFCLQSCVKP LKYAIAVNDL 300
GTEYVHRYVG KEPSGLRFNK LFLNEDDKPH NPMVNAGAIV VTSLIKQGVN NAEKFDYVMQ 360
FLNKMAGNEY VGFSNATFQS ERESGDRNFA IGYYLKEKKC FPEGTDMVGI LDFYFQLCSI 420
EVTCESASVM AATLANGGFC PITGERVLSP EAVRNTLSLM HSCGMYDFSG QFAFHVGLPA 480
KSGVAGGILL VVPNVMGMMC WSPPLDKMGN SVKGIHFCHD LVSLCNFHNY DNLRHFAKKL 540
DPRREGGDQR VKSVINLLFA AYTGDVSALR RFALSAMDME QRDYDSRTAL HVAAAEGHVE 600
VVKFLLEACK VNPFPKDRWN NTPMDEALHF GHHDVFKILQ EYQVQYTPQG DSDNGKENQT 660
VHKNLDGLL 669 
Gene Ontology
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0004359; F:glutaminase activity; IDA:UniProtKB.
 GO:0007610; P:behavior; IEA:Compara.
 GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
 GO:0006537; P:glutamate biosynthetic process; IDA:UniProtKB.
 GO:0014047; P:glutamate secretion; TAS:Reactome.
 GO:0006543; P:glutamine catabolic process; IDA:UniProtKB.
 GO:0007269; P:neurotransmitter secretion; TAS:Reactome.
 GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
 GO:0002087; P:regulation of respiratory gaseous exchange by neurological system process; IEA:Compara. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR012338; Beta-lactam/transpept-like.
 IPR015868; Glutaminase. 
Pfam
 PF12796; Ank_2
 PF04960; Glutaminase 
SMART
 SM00248; ANK 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT 
PRINTS