GSHB_HUMAN - dbPTM
GSHB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GSHB_HUMAN
UniProt AC P48637
Protein Name Glutathione synthetase
Gene Name GSS
Organism Homo sapiens (Human).
Sequence Length 474
Subcellular Localization
Protein Description
Protein Sequence MATNWGSLLQDKQQLEELARQAVDRALAEGVLLRTSQEPTSSEVVSYAPFTLFPSLVPSALLEQAYAVQMDFNLLVDAVSQNAAFLEQTLSSTIKQDDFTARLFDIHKQVLKEGIAQTVFLGLNRSDYMFQRSADGSPALKQIEINTISASFGGLASRTPAVHRHVLSVLSKTKEAGKILSNNPSKGLALGIAKAWELYGSPNALVLLIAQEKERNIFDQRAIENELLARNIHVIRRTFEDISEKGSLDQDRRLFVDGQEIAVVYFRDGYMPRQYSLQNWEARLLLERSHAAKCPDIATQLAGTKKVQQELSRPGMLEMLLPGQPEAVARLRATFAGLYSLDVGEEGDQAIAEALAAPSRFVLKPQREGGGNNLYGEEMVQALKQLKDSEERASYILMEKIEPEPFENCLLRPGSPARVVQCISELGIFGVYVRQEKTLVMNKHVGHLLRTKAIEHADGGVAAGVAVLDNPYPV
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
2Acetylation------MATNWGSLL
------CCCCHHHHH		15.0522223895
12UbiquitinationWGSLLQDKQQLEELA
HHHHHHCHHHHHHHH		27.30-
1082-HydroxyisobutyrylationARLFDIHKQVLKEGI
HHHHHHHHHHHHHCC		42.30-
108UbiquitinationARLFDIHKQVLKEGI
HHHHHHHHHHHHHCC		42.3021890473
112UbiquitinationDIHKQVLKEGIAQTV
HHHHHHHHHCCCHHH		55.8521890473
137PhosphorylationFQRSADGSPALKQIE
CEECCCCCHHHCEEE		13.9323312004
141UbiquitinationADGSPALKQIEINTI
CCCCHHHCEEEEEEE		51.8721890473
147PhosphorylationLKQIEINTISASFGG
HCEEEEEEEEECCCC		23.2120068231
149PhosphorylationQIEINTISASFGGLA
EEEEEEEEECCCCHH		18.8020068231
151PhosphorylationEINTISASFGGLASR
EEEEEEECCCCHHHC		20.0326657352
157PhosphorylationASFGGLASRTPAVHR
ECCCCHHHCCHHHHH		41.5522673903
168PhosphorylationAVHRHVLSVLSKTKE
HHHHHHHHHHHCCHH		21.6621406692
171PhosphorylationRHVLSVLSKTKEAGK
HHHHHHHHCCHHHHH		35.8021406692
172UbiquitinationHVLSVLSKTKEAGKI
HHHHHHHCCHHHHHH		60.50-
178UbiquitinationSKTKEAGKILSNNPS
HCCHHHHHHHCCCCC		47.74-
181PhosphorylationKEAGKILSNNPSKGL
HHHHHHHCCCCCCCC		37.7328857561
185PhosphorylationKILSNNPSKGLALGI
HHHCCCCCCCCHHHH		41.2922673903
186MalonylationILSNNPSKGLALGIA
HHCCCCCCCCHHHHH		60.2326320211
186AcetylationILSNNPSKGLALGIA
HHCCCCCCCCHHHHH		60.2388347
186UbiquitinationILSNNPSKGLALGIA
HHCCCCCCCCHHHHH		60.23-
199PhosphorylationIAKAWELYGSPNALV
HHHHHHHHCCCCEEE		12.21-
213UbiquitinationVLLIAQEKERNIFDQ
EEHHHHHHHCCCCCH		50.3121890473
230MethylationIENELLARNIHVIRR
HHHHHHHHHHHHHHH		42.47-
238PhosphorylationNIHVIRRTFEDISEK
HHHHHHHHHHHHHHC		22.8720068231
245UbiquitinationTFEDISEKGSLDQDR
HHHHHHHCCCCCCCC		47.1921890473
252MethylationKGSLDQDRRLFVDGQ
CCCCCCCCEEEECCE		31.41-
270PhosphorylationVVYFRDGYMPRQYSL
EEEECCCCCCCCHHC		14.2926356563
293UbiquitinationLERSHAAKCPDIATQ
HHHHHHHCCCCHHHH		47.27-
305UbiquitinationATQLAGTKKVQQELS
HHHHCCCHHHHHHHC		50.45-
306UbiquitinationTQLAGTKKVQQELSR
HHHCCCHHHHHHHCC		45.15-
364UbiquitinationAPSRFVLKPQREGGG
CCCCEEECCCCCCCC		33.53-
384UbiquitinationEEMVQALKQLKDSEE
HHHHHHHHHHCCHHH		57.5121890473
394PhosphorylationKDSEERASYILMEKI
CCHHHHHHHHHHHCC		20.9421406692
395PhosphorylationDSEERASYILMEKIE
CHHHHHHHHHHHCCC		9.3321406692
400UbiquitinationASYILMEKIEPEPFE
HHHHHHHCCCCCCCC		38.10-
415PhosphorylationNCLLRPGSPARVVQC
CCCCCCCCHHHHHHH		20.3330266825
443UbiquitinationEKTLVMNKHVGHLLR
CCEEEECHHHHHHHH		22.90-
452UbiquitinationVGHLLRTKAIEHADG
HHHHHHHHHEECCCC		40.72-
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 GSHB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GSHB_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 GSHB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GSHB_HUMANGSSphysical
21988832
ABHEA_HUMANABHD14Aphysical
22863883
ASSY_HUMANASS1physical
22863883
ECHM_HUMANECHS1physical
22863883
PSF3_HUMANGINS3physical
22863883
KIME_HUMANMVKphysical
22863883
OLA1_HUMANOLA1physical
22863883
PA1B2_HUMANPAFAH1B2physical
22863883
PDIA4_HUMANPDIA4physical
22863883
GDS1_HUMANRAP1GDS1physical
22863883
TBCB_HUMANTBCBphysical
22863883
UBP14_HUMANUSP14physical
22863883
1433B_HUMANYWHABphysical
22863883
1433E_HUMANYWHAEphysical
22863883
1433G_HUMANYWHAGphysical
22863883
1433F_HUMANYWHAHphysical
22863883
GSHB_HUMANGSSphysical
25416956
GLGB_HUMANGBE1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
266130Glutathione synthetase deficiency (GSS deficiency)
231900Glutathione synthetase deficiency of erythrocytes (GLUSYNDE)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB06151Acetylcysteine
DB00143Glutathione
DB00145Glycine
DB00151L-Cysteine
Regulatory Network of GSHB_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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