GLSK_HUMAN - dbPTM
GLSK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLSK_HUMAN
UniProt AC O94925
Protein Name Glutaminase kidney isoform, mitochondrial
Gene Name GLS
Organism Homo sapiens (Human).
Sequence Length 669
Subcellular Localization Isoform 1: Cytoplasm, cytosol.
Isoform 3: Mitochondrion.
Protein 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..
Protein Sequence MMRLRGSGMLRDLLLRSPAGVSATLRRAQPLVTLCRRPRGGGRPAAGPAAAARLHPWWGGGGWPAEPLARGLSSSPSEILQELGKGSTHPQPGVSPPAAPAAPGPKDGPGETDAFGNSEGKELVASGENKIKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDNGKENQTVHKNLDGLL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
17PhosphorylationLRDLLLRSPAGVSAT
HHHHHHHCCCCHHHH		21.04-
73PhosphorylationEPLARGLSSSPSEIL
HHHHHHCCCCHHHHH		31.4320068231
74PhosphorylationPLARGLSSSPSEILQ
HHHHHCCCCHHHHHH		51.8420068231
75PhosphorylationLARGLSSSPSEILQE
HHHHCCCCHHHHHHH		29.1220068231
77PhosphorylationRGLSSSPSEILQELG
HHCCCCHHHHHHHHC		38.9420068231
87PhosphorylationLQELGKGSTHPQPGV
HHHHCCCCCCCCCCC		27.3320068231
88PhosphorylationQELGKGSTHPQPGVS
HHHCCCCCCCCCCCC		46.3620068231
95PhosphorylationTHPQPGVSPPAAPAA
CCCCCCCCCCCCCCC		30.9520068231
112PhosphorylationPKDGPGETDAFGNSE
CCCCCCCCCCCCCCC		38.2420068231
118PhosphorylationETDAFGNSEGKELVA
CCCCCCCCCCCEEHH		48.3720068231
121UbiquitinationAFGNSEGKELVASGE
CCCCCCCCEEHHCCC		43.7721890473
121 (in isoform 1)Ubiquitination-43.7721890473
121 (in isoform 2)Ubiquitination-43.7721890473
121 (in isoform 3)Ubiquitination-43.7721890473
1212-HydroxyisobutyrylationAFGNSEGKELVASGE
CCCCCCCCEEHHCCC		43.77-
126PhosphorylationEGKELVASGENKIKQ
CCCEEHHCCCCHHHC		38.8828857561
130SuccinylationLVASGENKIKQGLLP
EHHCCCCHHHCCCCC		47.15-
130SuccinylationLVASGENKIKQGLLP
EHHCCCCHHHCCCCC		47.15-
158AcetylationQEKIPVHKFITALKS
CCCCCHHHHHHHHHH		38.4025825284
1582-HydroxyisobutyrylationQEKIPVHKFITALKS
CCCCCHHHHHHHHHH		38.40-
158MalonylationQEKIPVHKFITALKS
CCCCCHHHHHHHHHH		38.4026320211
158 (in isoform 1)Ubiquitination-38.4021890473
158UbiquitinationQEKIPVHKFITALKS
CCCCCHHHHHHHHHH		38.402189047
158 (in isoform 3)Ubiquitination-38.4021890473
164MalonylationHKFITALKSTGLRTS
HHHHHHHHHCCCCCC		43.4326320211
164SuccinylationHKFITALKSTGLRTS
HHHHHHHHHCCCCCC		43.43-
164UbiquitinationHKFITALKSTGLRTS
HHHHHHHHHCCCCCC		43.43-
164SuccinylationHKFITALKSTGLRTS
HHHHHHHHHCCCCCC		43.4327452117
164 (in isoform 3)Ubiquitination-43.43-
164AcetylationHKFITALKSTGLRTS
HHHHHHHHHCCCCCC		43.4323954790
1762-HydroxyisobutyrylationRTSDPRLKECMDMLR
CCCCHHHHHHHHHHH		50.58-
176MalonylationRTSDPRLKECMDMLR
CCCCHHHHHHHHHHH		50.5826320211
176UbiquitinationRTSDPRLKECMDMLR
CCCCHHHHHHHHHHH		50.58-
176AcetylationRTSDPRLKECMDMLR
CCCCHHHHHHHHHHH		50.587706877
176 (in isoform 3)Ubiquitination-50.58-
185PhosphorylationCMDMLRLTLQTTSDG
HHHHHHHHHHCCCCC		15.4724505115
188 (in isoform 3)Phosphorylation-31.2321406692
188PhosphorylationMLRLTLQTTSDGVML
HHHHHHHCCCCCCEE		31.2324505115
189 (in isoform 3)Phosphorylation-16.3221406692
189PhosphorylationLRLTLQTTSDGVMLD
HHHHHHCCCCCCEEC		16.3228857561
190PhosphorylationRLTLQTTSDGVMLDK
HHHHHCCCCCCEECH		35.4421406692
1972-HydroxyisobutyrylationSDGVMLDKDLFKKCV
CCCCEECHHHHHHHH		52.98-
197AcetylationSDGVMLDKDLFKKCV
CCCCEECHHHHHHHH		52.9823236377
203S-palmitoylationDKDLFKKCVQSNIVL
CHHHHHHHHHCHHHH		3.2929575903
245MalonylationAKKQSGGKVADYIPQ
HHHHCCCCHHHHHHH		37.4626320211
249PhosphorylationSGGKVADYIPQLAKF
CCCCHHHHHHHHHHC		12.5528857561
266S-palmitoylationDLWGVSVCTVDGQRH
CCCEEEEEEECCCCC		2.0929575903
279UbiquitinationRHSTGDTKVPFCLQS
CCCCCCCCCCCHHHH		53.29-
279MalonylationRHSTGDTKVPFCLQS
CCCCCCCCCCCHHHH		53.2926320211
279AcetylationRHSTGDTKVPFCLQS
CCCCCCCCCCCHHHH		53.2923236377
289AcetylationFCLQSCVKPLKYAIA
CHHHHCCCCCCEEEE		49.3026051181
289UbiquitinationFCLQSCVKPLKYAIA
CHHHHCCCCCCEEEE		49.30-
2922-HydroxyisobutyrylationQSCVKPLKYAIAVND
HHCCCCCCEEEEECC		40.96-
302PhosphorylationIAVNDLGTEYVHRYV
EEECCCCHHHHHHHC		31.2928152594
304PhosphorylationVNDLGTEYVHRYVGK
ECCCCHHHHHHHCCC		11.0328152594
311UbiquitinationYVHRYVGKEPSGLRF
HHHHHCCCCCCCCCE		57.3019608861
311 (in isoform 3)Ubiquitination-57.30-
3112-HydroxyisobutyrylationYVHRYVGKEPSGLRF
HHHHHCCCCCCCCCE		57.30-
311MalonylationYVHRYVGKEPSGLRF
HHHHHCCCCCCCCCE		57.3026320211
311AcetylationYVHRYVGKEPSGLRF
HHHHHCCCCCCCCCE		57.3019608861
311SuccinylationYVHRYVGKEPSGLRF
HHHHHCCCCCCCCCE		57.3023954790
314PhosphorylationRYVGKEPSGLRFNKL
HHCCCCCCCCCEEEE		52.10-
320AcetylationPSGLRFNKLFLNEDD
CCCCCEEEEECCCCC		37.5925953088
343PhosphorylationAGAIVVTSLIKQGVN
CHHHHHHHHHHHCCC		19.2524719451
357PhosphorylationNNAEKFDYVMQFLNK
CCHHHHHHHHHHHHH		10.85-
370PhosphorylationNKMAGNEYVGFSNAT
HHHCCCCCCCCCCCE		15.18-
374PhosphorylationGNEYVGFSNATFQSE
CCCCCCCCCCEEEHH		21.4530387612
387MethylationSERESGDRNFAIGYY
HHHHHCCCCEEHHHH		43.63-
393PhosphorylationDRNFAIGYYLKEKKC
CCCEEHHHHHCCCCC		10.26-
394PhosphorylationRNFAIGYYLKEKKCF
CCEEHHHHHCCCCCC		13.1930387612
396MalonylationFAIGYYLKEKKCFPE
EEHHHHHCCCCCCCC		51.9026320211
449PhosphorylationITGERVLSPEAVRNT
CCCCCCCCHHHHHHH		20.1725850435
523PhosphorylationHFCHDLVSLCNFHNY
HHCHHHHHHHHCCCH		34.21-
539UbiquitinationNLRHFAKKLDPRREG
HHHHHHHHCCCCCCC		55.48-
552 (in isoform 3)Phosphorylation-40.9930108239
558 (in isoform 3)Phosphorylation-2.0726471730
560 (in isoform 3)Phosphorylation-10.2627251275
568 (in isoform 3)Ubiquitination-12.63-
574 (in isoform 3)Ubiquitination-2.85-
652PhosphorylationQYTPQGDSDNGKENQ
EECCCCCCCCCCCCC		39.54-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
314SPhosphorylationKinasePRKCEQ02156
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLSK_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of GLSK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNTA1_HUMANSNTA1physical
11163757
SIR5_HUMANSIRT5physical
25700560
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00130L-Glutamine
Regulatory Network of GLSK_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-311, AND MASS SPECTROMETRY.

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