GGT7_HUMAN - dbPTM
GGT7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GGT7_HUMAN
UniProt AC Q9UJ14
Protein Name Glutathione hydrolase 7
Gene Name GGT7
Organism Homo sapiens (Human).
Sequence Length 662
Subcellular Localization Membrane
Single-pass type II membrane protein.
Protein Description Cleaves glutathione conjugates..
Protein Sequence MAAENEASQESALGAYSPVDYMSITSFPRLPEDEPAPAAPLRGRKDEDAFLGDPDTDPDSFLKSARLQRLPSSSSEMGSQDGSPLRETRKDPFSAAAAECSCRQDGLTVIVTACLTFATGVTVALVMQIYFGDPQIFQQGAVVTDAARCTSLGIEVLSKQGSSVDAAVAAALCLGIVAPHSSGLGGGGVMLVHDIRRNESHLIDFRESAPGALREETLQRSWETKPGLLVGVPGMVKGLHEAHQLYGRLPWSQVLAFAAAVAQDGFNVTHDLARALAEQLPPNMSERFRETFLPSGRPPLPGSLLHRPDLAEVLDVLGTSGPAAFYAGGNLTLEMVAEAQHAGGVITEEDFSNYSALVEKPVCGVYRGHLVLSPPPPHTGPALISALNILEGFNLTSLVSREQALHWVAETLKIALALASRLGDPVYDSTITESMDDMLSKVEAAYLRGHINDSQAAPAPLLPVYELDGAPTAAQVLIMGPDDFIVAMVSSLNQPFGSGLITPSGILLNSQMLDFSWPNRTANHSAPSLENSVQPGKRPLSFLLPTVVRPAEGLCGTYLALGANGAARGLSGLTQVLLNVLTLNRNLSDSLARGRLHPDLQSNLLQVDSEFTEEEIEFLEARGHHVEKVDVLSWVHGSRRTNNFIIAVKDPRSPDAAGATIL
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
8PhosphorylationMAAENEASQESALGA
CCCCCHHHHHHHCCC		28.44-
11PhosphorylationENEASQESALGAYSP
CCHHHHHHHCCCCCC		22.58-
17PhosphorylationESALGAYSPVDYMSI
HHHCCCCCCCCCEEC		20.22-
21PhosphorylationGAYSPVDYMSITSFP
CCCCCCCCEECCCCC		7.9325884760
45UbiquitinationAAPLRGRKDEDAFLG
CCCCCCCCCCCCCCC		69.19-
56PhosphorylationAFLGDPDTDPDSFLK
CCCCCCCCCHHHHHH		55.6127732954
60PhosphorylationDPDTDPDSFLKSARL
CCCCCHHHHHHHHHH		37.5622617229
63UbiquitinationTDPDSFLKSARLQRL
CCHHHHHHHHHHHCC		39.81-
64PhosphorylationDPDSFLKSARLQRLP
CHHHHHHHHHHHCCC		22.2923312004
72PhosphorylationARLQRLPSSSSEMGS
HHHHCCCCCCHHCCC		47.6629255136
72 (in isoform 5)Phosphorylation-47.66-
73PhosphorylationRLQRLPSSSSEMGSQ
HHHCCCCCCHHCCCC		35.6227273156
74PhosphorylationLQRLPSSSSEMGSQD
HHCCCCCCHHCCCCC		34.3530266825
75PhosphorylationQRLPSSSSEMGSQDG
HCCCCCCHHCCCCCC		33.2830266825
79PhosphorylationSSSSEMGSQDGSPLR
CCCHHCCCCCCCCCC		24.6429255136
83PhosphorylationEMGSQDGSPLRETRK
HCCCCCCCCCCCCCC		29.1129255136
88PhosphorylationDGSPLRETRKDPFSA
CCCCCCCCCCCCCHH		36.2629523821
108PhosphorylationSCRQDGLTVIVTACL
CCCCCCCEEEHHHHH		17.4524043423
112PhosphorylationDGLTVIVTACLTFAT
CCCEEEHHHHHHHHH		10.6724043423
116PhosphorylationVIVTACLTFATGVTV
EEHHHHHHHHHCHHH		15.8824043423
119PhosphorylationTACLTFATGVTVALV
HHHHHHHHCHHHHHH		28.1724043423
122PhosphorylationLTFATGVTVALVMQI
HHHHHCHHHHHHHHH		11.0424043423
130PhosphorylationVALVMQIYFGDPQIF
HHHHHHHHHCCHHHH		5.6624043423
144PhosphorylationFQQGAVVTDAARCTS
HCCCCEECCHHHHHH		17.2024043423
162PhosphorylationEVLSKQGSSVDAAVA
HHHHCCCCCHHHHHH		25.3724043423
163PhosphorylationVLSKQGSSVDAAVAA
HHHCCCCCHHHHHHH		30.7324043423
181PhosphorylationLGIVAPHSSGLGGGG
HHHHCCCCCCCCCCC		25.6624043423
182PhosphorylationGIVAPHSSGLGGGGV
HHHCCCCCCCCCCCE		34.7024043423
198N-linked_GlycosylationLVHDIRRNESHLIDF
EEEECCCCCCCEEEH		45.32UniProtKB CARBOHYD
225UbiquitinationLQRSWETKPGLLVGV
HHHHHCCCCCEEECC		26.10-
267N-linked_GlycosylationAVAQDGFNVTHDLAR
HHHCCCCCHHHHHHH		43.22UniProtKB CARBOHYD
283N-linked_GlycosylationLAEQLPPNMSERFRE
HHHHCCCCHHHHHHH		44.68UniProtKB CARBOHYD
295PhosphorylationFRETFLPSGRPPLPG
HHHHHCCCCCCCCCC		49.9724043423
330N-linked_GlycosylationAAFYAGGNLTLEMVA
CEEEECCCEEHHHHH		29.00UniProtKB CARBOHYD
353N-linked_GlycosylationITEEDFSNYSALVEK
CCHHHHCCCHHHCCC		34.47UniProtKB CARBOHYD
394N-linked_GlycosylationLNILEGFNLTSLVSR
HHHHHCCCCHHHCCH		53.95UniProtKB CARBOHYD
420PhosphorylationKIALALASRLGDPVY
HHHHHHHHHHCCCCC		28.9621406692
427PhosphorylationSRLGDPVYDSTITES
HHHCCCCCCCCCCCC		15.0121406692
429PhosphorylationLGDPVYDSTITESMD
HCCCCCCCCCCCCHH		12.2021406692
430PhosphorylationGDPVYDSTITESMDD
CCCCCCCCCCCCHHH		29.0821406692
432PhosphorylationPVYDSTITESMDDML
CCCCCCCCCCHHHHH		23.3021406692
434PhosphorylationYDSTITESMDDMLSK
CCCCCCCCHHHHHHH		20.8921406692
440PhosphorylationESMDDMLSKVEAAYL
CCHHHHHHHHHHHHH		28.1921406692
452N-linked_GlycosylationAYLRGHINDSQAAPA
HHHHCCCCCCCCCCC		36.89UniProtKB CARBOHYD
519N-linked_GlycosylationMLDFSWPNRTANHSA
CCCCCCCCCCCCCCC		47.91UniProtKB CARBOHYD
523N-linked_GlycosylationSWPNRTANHSAPSLE
CCCCCCCCCCCCCHH		29.09UniProtKB CARBOHYD
586N-linked_GlycosylationNVLTLNRNLSDSLAR
HHHHHCCCHHHHHHH		42.71UniProtKB CARBOHYD
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

Oops, there are no upstream regulatory protein records of GGT7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GGT7_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 GGT7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GGT7_HUMANGGT7physical
15943911
GPR25_HUMANGPR25physical
25416956
MALL_HUMANMALLphysical
25416956
LHPL5_HUMANLHFPL5physical
25416956
TM242_HUMANTMEM242physical
25416956
NALD2_HUMANNAALAD2physical
28514442
PIGB_HUMANPIGBphysical
28514442
ALG12_HUMANALG12physical
28514442
DDX11_HUMANDDX11physical
28514442
MANEA_HUMANMANEAphysical
28514442
POMT1_HUMANPOMT1physical
28514442
FA69A_HUMANFAM69Aphysical
28514442
ZDHC9_HUMANZDHHC9physical
28514442
ABHEA_HUMANABHD14Aphysical
28514442
GOLI_HUMANRNF130physical
28514442
ALG9_HUMANALG9physical
28514442
MPZL1_HUMANMPZL1physical
28514442
ENTP6_HUMANENTPD6physical
28514442
MANEL_HUMANMANEALphysical
28514442
LSR_HUMANLSRphysical
28514442
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
D02755 Acivicin (USAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GGT7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND MASSSPECTROMETRY.

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