GSHR_HUMAN - dbPTM
GSHR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GSHR_HUMAN
UniProt AC P00390
Protein Name Glutathione reductase, mitochondrial
Gene Name GSR
Organism Homo sapiens (Human).
Sequence Length 522
Subcellular Localization Isoform Mitochondrial: Mitochondrion.
Isoform Cytoplasmic: Cytoplasm.
Protein Description Maintains high levels of reduced glutathione in the cytosol..
Protein Sequence MALLPRALSAGAGPSWRRAARAFRGFLLLLPEPAALTRALSRAMACRQEPQPQGPPPAAGAVASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDPKPTIEVSGKKYTAPHILIATGGMPSTPHESQIPGASLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTLSGLEVSMVTAVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR
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
15PhosphorylationLSAGAGPSWRRAARA
HHCCCCHHHHHHHHH		32.0926091039
65PhosphorylationAAGAVASYDYLVIGG
CCCEEEECEEEEECC		10.0022817900
97AcetylationAAVVESHKLGGTCVN
EEEEEHHHCCCEEEE		59.0923749302
97UbiquitinationAAVVESHKLGGTCVN
EEEEEHHHCCCEEEE		59.09-
101PhosphorylationESHKLGGTCVNVGCV
EHHHCCCEEEECCCE		16.1029970186
107GlutathionylationGTCVNVGCVPKKVMW
CEEEECCCEECEEEC		4.0522555962
107S-nitrosylationGTCVNVGCVPKKVMW
CEEEECCCEECEEEC		4.0525040305
110AcetylationVNVGCVPKKVMWNTA
EECCCEECEEECCCC		37.29129591
1102-HydroxyisobutyrylationVNVGCVPKKVMWNTA
EECCCEECEEECCCC		37.29-
111UbiquitinationNVGCVPKKVMWNTAV
ECCCEECEEECCCCC		31.11-
137AcetylationGFPSCEGKFNWRVIK
CCCCCCCCEEEEEEH		17.1525953088
138 (in isoform 2)Ubiquitination-18.2321890473
146 (in isoform 2)Ubiquitination-51.0521890473
150NitrationIKEKRDAYVSRLNAI
EHHHHHHHHHHHHHH		11.84-
158PhosphorylationVSRLNAIYQNNLTKS
HHHHHHHHHCCCCHH		11.6328152594
158NitrationVSRLNAIYQNNLTKS
HHHHHHHHHCCCCHH		11.63-
163PhosphorylationAIYQNNLTKSHIEII
HHHHCCCCHHHEEEE		32.4028152594
164AcetylationIYQNNLTKSHIEIIR
HHHCCCCHHHEEEEE		43.1123749302
164UbiquitinationIYQNNLTKSHIEIIR
HHHCCCCHHHEEEEE		43.11-
1642-HydroxyisobutyrylationIYQNNLTKSHIEIIR
HHHCCCCHHHEEEEE		43.11-
165PhosphorylationYQNNLTKSHIEIIRG
HHCCCCHHHEEEEEC		25.1824247654
177PhosphorylationIRGHAAFTSDPKPTI
EECCCCCCCCCCCEE		27.7426657352
178PhosphorylationRGHAAFTSDPKPTIE
ECCCCCCCCCCCEEE		45.5220873877
181UbiquitinationAAFTSDPKPTIEVSG
CCCCCCCCCEEEECC		60.8421890473
1812-HydroxyisobutyrylationAAFTSDPKPTIEVSG
CCCCCCCCCEEEECC		60.84-
181UbiquitinationAAFTSDPKPTIEVSG
CCCCCCCCCEEEECC		60.8421890473
181UbiquitinationAAFTSDPKPTIEVSG
CCCCCCCCCEEEECC		60.8421890473
181UbiquitinationAAFTSDPKPTIEVSG
CCCCCCCCCEEEECC		60.8421890473
181 (in isoform 1)Ubiquitination-60.8421890473
183PhosphorylationFTSDPKPTIEVSGKK
CCCCCCCEEEECCEE		35.5820873877
187PhosphorylationPKPTIEVSGKKYTAP
CCCEEEECCEEEECC		31.9120873877
189AcetylationPTIEVSGKKYTAPHI
CEEEECCEEEECCEE		34.797669677
189UbiquitinationPTIEVSGKKYTAPHI
CEEEECCEEEECCEE		34.791890473
1892-HydroxyisobutyrylationPTIEVSGKKYTAPHI
CEEEECCEEEECCEE		34.79-
189 (in isoform 1)Ubiquitination-34.7921890473
190AcetylationTIEVSGKKYTAPHIL
EEEECCEEEECCEEE		51.897672053
257 (in isoform 2)Ubiquitination-28.8821890473
278GlutathionylationDSMISTNCTEELENA
HHHHCCCCHHHHHHC		5.2622555962
278S-nitrosylationDSMISTNCTEELENA
HHHHCCCCHHHHHHC		5.2625040305
291UbiquitinationNAGVEVLKFSQVKEV
HCCCEEEEHHHHHHH		48.41-
296UbiquitinationVLKFSQVKEVKKTLS
EEEHHHHHHHHHHHC		49.50-
2962-HydroxyisobutyrylationVLKFSQVKEVKKTLS
EEEHHHHHHHHHHHC		49.50-
296AcetylationVLKFSQVKEVKKTLS
EEEHHHHHHHHHHHC		49.5025953088
297 (in isoform 2)Ubiquitination-61.7921890473
300UbiquitinationSQVKEVKKTLSGLEV
HHHHHHHHHHCCCEE		60.9321890473
300 (in isoform 1)Ubiquitination-60.9321890473
301PhosphorylationQVKEVKKTLSGLEVS
HHHHHHHHHCCCEEE		22.0528857561
303PhosphorylationKEVKKTLSGLEVSMV
HHHHHHHCCCEEEEE		46.7128857561
303 (in isoform 2)Ubiquitination-46.7121890473
308PhosphorylationTLSGLEVSMVTAVPG
HHCCCEEEEEEECCC		9.73-
319AcetylationAVPGRLPVMTMIPDV
ECCCCCCEEEEECCH		6.2119608861
340UbiquitinationIGRVPNTKDLSLNKL
HCCCCCCCCCCCHHC		64.4121906983
340 (in isoform 1)Ubiquitination-64.4121890473
346UbiquitinationTKDLSLNKLGIQTDD
CCCCCCHHCCEECCC		54.0821906983
346 (in isoform 1)Ubiquitination-54.0821890473
348AcetylationDLSLNKLGIQTDDKG
CCCCHHCCEECCCCC		16.1519608861
354UbiquitinationLGIQTDDKGHIIVDE
CCEECCCCCCEEEEC		56.02-
354AcetylationLGIQTDDKGHIIVDE
CCEECCCCCCEEEEC		56.0225038526
362 (in isoform 2)Ubiquitination-6.1721890473
368UbiquitinationEFQNTNVKGIYAVGD
CCCCCCCCCEEEEEC		41.48-
371PhosphorylationNTNVKGIYAVGDVCG
CCCCCCEEEEECCCC		12.1428152594
372AcetylationTNVKGIYAVGDVCGK
CCCCCEEEEECCCCH		9.2619608861
374UbiquitinationVKGIYAVGDVCGKAL
CCCEEEEECCCCHHH		17.2921890473
377GlutathionylationIYAVGDVCGKALLTP
EEEEECCCCHHHHHH		5.7222555962
377S-nitrosylationIYAVGDVCGKALLTP
EEEEECCCCHHHHHH		5.7225040305
379UbiquitinationAVGDVCGKALLTPVA
EEECCCCHHHHHHHH		30.63-
383PhosphorylationVCGKALLTPVAIAAG
CCCHHHHHHHHHHHH		19.3029255136
398 (in isoform 2)Ubiquitination-10.9921890473
401AcetylationAHRLFEYKEDSKLDY
HHHHHCCCCCCCCCC		48.0919608861
401UbiquitinationAHRLFEYKEDSKLDY
HHHHHCCCCCCCCCC		48.0919608861
4012-HydroxyisobutyrylationAHRLFEYKEDSKLDY
HHHHHCCCCCCCCCC		48.09-
403UbiquitinationRLFEYKEDSKLDYNN
HHHCCCCCCCCCCCC		47.0921890473
405UbiquitinationFEYKEDSKLDYNNIP
HCCCCCCCCCCCCCC		58.6721906983
4052-HydroxyisobutyrylationFEYKEDSKLDYNNIP
HCCCCCCCCCCCCCC		58.67-
405 (in isoform 1)Ubiquitination-58.6721890473
408PhosphorylationKEDSKLDYNNIPTVV
CCCCCCCCCCCCEEE		22.1222817900
413 (in isoform 2)Ubiquitination-26.0421890473
427PhosphorylationPIGTVGLTEDEAIHK
CCCCCCCCCCHHHHH		35.15-
427UbiquitinationPIGTVGLTEDEAIHK
CCCCCCCCCCHHHHH		35.1521890473
434UbiquitinationTEDEAIHKYGIENVK
CCCHHHHHHCCCCCE		38.77-
434AcetylationTEDEAIHKYGIENVK
CCCHHHHHHCCCCCE		38.7725038526
441UbiquitinationKYGIENVKTYSTSFT
HHCCCCCEEEECCCC		54.0121906983
441 (in isoform 1)Ubiquitination-54.0121890473
442PhosphorylationYGIENVKTYSTSFTP
HCCCCCEEEECCCCH		20.5821945579
443PhosphorylationGIENVKTYSTSFTPM
CCCCCEEEECCCCHH		12.3021945579
444PhosphorylationIENVKTYSTSFTPMY
CCCCEEEECCCCHHH		23.8621945579
445PhosphorylationENVKTYSTSFTPMYH
CCCEEEECCCCHHHH		19.9021945579
446PhosphorylationNVKTYSTSFTPMYHA
CCEEEECCCCHHHHH		22.6021945579
448PhosphorylationKTYSTSFTPMYHAVT
EEEECCCCHHHHHHC		13.6021945579
451PhosphorylationSTSFTPMYHAVTKRK
ECCCCHHHHHHCCCC		6.4521945579
455PhosphorylationTPMYHAVTKRKTKCV
CHHHHHHCCCCCHHH		26.3921945579
456AcetylationPMYHAVTKRKTKCVM
HHHHHHCCCCCHHHE		45.3525953088
456UbiquitinationPMYHAVTKRKTKCVM
HHHHHHCCCCCHHHE		45.3521890473
4562-HydroxyisobutyrylationPMYHAVTKRKTKCVM
HHHHHHCCCCCHHHE		45.35-
456MalonylationPMYHAVTKRKTKCVM
HHHHHHCCCCCHHHE		45.3526320211
456 (in isoform 1)Ubiquitination-45.3521890473
458 (in isoform 2)Ubiquitination-54.6221890473
464UbiquitinationRKTKCVMKMVCANKE
CCCHHHEEEEECCCC		14.05-
464AcetylationRKTKCVMKMVCANKE
CCCHHHEEEEECCCC		14.0526051181
470AcetylationMKMVCANKEEKVVGI
EEEEECCCCCEEEEE		49.0425953088
470UbiquitinationMKMVCANKEEKVVGI
EEEEECCCCCEEEEE		49.04-
4702-HydroxyisobutyrylationMKMVCANKEEKVVGI
EEEEECCCCCEEEEE		49.04-
484S-nitrosylationIHMQGLGCDEMLQGF
EEECCCCHHHHHHHH		4.8825040305
501UbiquitinationAVKMGATKADFDNTV
HHHHCCCHHCCCCCE		45.482190698
501 (in isoform 1)Ubiquitination-45.4821890473
507PhosphorylationTKADFDNTVAIHPTS
CHHCCCCCEEECCCC		17.1028450419
513PhosphorylationNTVAIHPTSSEELVT
CCEEECCCCCCHHEE		30.6228450419
514PhosphorylationTVAIHPTSSEELVTL
CEEECCCCCCHHEEC		39.9628450419
515PhosphorylationVAIHPTSSEELVTLR
EEECCCCCCHHEECC		37.2528450419
520PhosphorylationTSSEELVTLR-----
CCCCHHEECC-----		29.4628450419
522MethylationSEELVTLR-------
CCHHEECC-------		34.82-
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
507TPhosphorylationKinaseAMPKA1Q13131
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GSHR_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 GSHR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PJA1_HUMANPJA1physical
16169070
GSHR_HUMANGSRphysical
9151953
PURA2_HUMANADSSphysical
22863883
CNDP2_HUMANCNDP2physical
22863883
DX39A_HUMANDDX39Aphysical
22863883
EF2_HUMANEEF2physical
22863883
GBP2_HUMANGBP2physical
22863883
PSF2_HUMANGINS2physical
22863883
CH60_HUMANHSPD1physical
22863883
KYNU_HUMANKYNUphysical
22863883
MVD1_HUMANMVDphysical
22863883
NAMPT_HUMANNAMPTphysical
22863883
PEPD_HUMANPEPDphysical
22863883
KS6A1_HUMANRPS6KA1physical
22863883
AIFM1_HUMANAIFM1physical
26344197
ASSY_HUMANASS1physical
26344197
LSM12_HUMANLSM12physical
26344197
TOM40_HUMANTOMM40physical
26344197
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
There are no disease associations of PTM sites.
Regulatory Network of GSHR_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-65, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory