GSTK1_HUMAN - dbPTM
GSTK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GSTK1_HUMAN
UniProt AC Q9Y2Q3
Protein Name Glutathione S-transferase kappa 1
Gene Name GSTK1
Organism Homo sapiens (Human).
Sequence Length 226
Subcellular Localization Peroxisome .
Protein Description Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB)..
Protein Sequence MGPLPRTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLPRKGLYMANDLKLLRHHLQIPIHFPKDFLSVMLEKGSLSAMRFLTAVNLEHPEMLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPKVKNQLKETTEAACRYGAFGLPITVAHVDGQTHMLFGSDRMELLAHLLGEKWMGPIPPAVNARL
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
49SuccinylationSLITGIMKDSGNKPP
HHHHHHHCCCCCCCC		46.99-
49SuccinylationSLITGIMKDSGNKPP
HHHHHHHCCCCCCCC		46.99-
54 (in isoform 2)Malonylation-56.9926320211
54SuccinylationIMKDSGNKPPGLLPR
HHCCCCCCCCCCCCC		56.9927452117
54AcetylationIMKDSGNKPPGLLPR
HHCCCCCCCCCCCCC		56.9926051181
54MalonylationIMKDSGNKPPGLLPR
HHCCCCCCCCCCCCC		56.9926320211
62 (in isoform 2)Malonylation-51.8626320211
62UbiquitinationPPGLLPRKGLYMAND
CCCCCCCCCEEECCH		51.86-
62MalonylationPPGLLPRKGLYMAND
CCCCCCCCCEEECCH		51.8626320211
65PhosphorylationLLPRKGLYMANDLKL
CCCCCCEEECCHHHH		11.6619835603
71UbiquitinationLYMANDLKLLRHHLQ
EEECCHHHHHHHHCC		48.6221890473
71 (in isoform 2)Malonylation-48.6226320211
71 (in isoform 2)Ubiquitination-48.62-
71UbiquitinationLYMANDLKLLRHHLQ
EEECCHHHHHHHHCC		48.62-
71UbiquitinationLYMANDLKLLRHHLQ
EEECCHHHHHHHHCC		48.6221890473
71MalonylationLYMANDLKLLRHHLQ
EEECCHHHHHHHHCC		48.6226320211
71AcetylationLYMANDLKLLRHHLQ
EEECCHHHHHHHHCC		48.6219608861
85AcetylationQIPIHFPKDFLSVML
CCCCCCCHHHHHHHH		61.23-
89PhosphorylationHFPKDFLSVMLEKGS
CCCHHHHHHHHHHCC		12.8922985185
94AcetylationFLSVMLEKGSLSAMR
HHHHHHHHCCHHHHH		50.2519413330
96PhosphorylationSVMLEKGSLSAMRFL
HHHHHHCCHHHHHHH		30.1620068230
98PhosphorylationMLEKGSLSAMRFLTA
HHHHCCHHHHHHHHH		23.0119413330
104PhosphorylationLSAMRFLTAVNLEHP
HHHHHHHHHHCCCCH		26.3319413330
116 (in isoform 2)Ubiquitination-47.93-
116AcetylationEHPEMLEKASRELWM
CCHHHHHHHHHHHHH		47.9325953088
116UbiquitinationEHPEMLEKASRELWM
CCHHHHHHHHHHHHH		47.93-
116SuccinylationEHPEMLEKASRELWM
CCHHHHHHHHHHHHH		47.93-
116SuccinylationEHPEMLEKASRELWM
CCHHHHHHHHHHHHH		47.93-
126AcetylationRELWMRVWSRNEDIT
HHHHHHHHHCCCCCC		4.9219608861
144SuccinylationSILAAAEKAGMSAEQ
HHHHHHHHHCCCHHH		45.58-
144SuccinylationSILAAAEKAGMSAEQ
HHHHHHHHHCCCHHH		45.58-
144AcetylationSILAAAEKAGMSAEQ
HHHHHHHHHCCCHHH		45.5823954790
147SulfoxidationAAAEKAGMSAEQAQG
HHHHHHCCCHHHHHH		4.0221406390
148PhosphorylationAAEKAGMSAEQAQGL
HHHHHCCCHHHHHHH		27.9521712546
157AcetylationEQAQGLLEKIATPKV
HHHHHHHHHHCCHHH		47.6719608861
158SuccinylationQAQGLLEKIATPKVK
HHHHHHHHHCCHHHH		37.30-
158SuccinylationQAQGLLEKIATPKVK
HHHHHHHHHCCHHHH		37.30-
158AcetylationQAQGLLEKIATPKVK
HHHHHHHHHCCHHHH		37.3020167786
158UbiquitinationQAQGLLEKIATPKVK
HHHHHHHHHCCHHHH		37.30-
161PhosphorylationGLLEKIATPKVKNQL
HHHHHHCCHHHHHHH		27.41-
165AcetylationKIATPKVKNQLKETT
HHCCHHHHHHHHHHH		45.1425953088
169MalonylationPKVKNQLKETTEAAC
HHHHHHHHHHHHHHH		43.1626320211
169UbiquitinationPKVKNQLKETTEAAC
HHHHHHHHHHHHHHH		43.16-
169SuccinylationPKVKNQLKETTEAAC
HHHHHHHHHHHHHHH		43.1627452117
169AcetylationPKVKNQLKETTEAAC
HHHHHHHHHHHHHHH		43.1619608861
171PhosphorylationVKNQLKETTEAACRY
HHHHHHHHHHHHHHH		28.4828348404
172PhosphorylationKNQLKETTEAACRYG
HHHHHHHHHHHHHHH		25.3928348404
214 (in isoform 2)Ubiquitination-7.83-
225 (in isoform 2)Malonylation-35.4126320211
225AcetylationIPPAVNARL------
CCHHHCCCC------		35.4119608861
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 GSTK1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GSTK1_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 GSTK1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LPPRC_HUMANLRPPRCphysical
17353931
DAAF5_HUMANDNAAF5physical
17353931
XPO5_HUMANXPO5physical
17353931
IPO4_HUMANIPO4physical
17353931
PDC6I_HUMANPDCD6IPphysical
17353931
EPIPL_HUMANEPPK1physical
17353931
HNRPM_HUMANHNRNPMphysical
17353931
SEC63_HUMANSEC63physical
17353931
DCTN1_HUMANDCTN1physical
17353931
CYC_HUMANCYCSphysical
17353931
RPN2_HUMANRPN2physical
17353931
SYIC_HUMANIARSphysical
17353931
HORN_HUMANHRNRphysical
17353931
RPN1_HUMANRPN1physical
17353931
5HT1B_HUMANHTR1Bphysical
17353931
U5S1_HUMANEFTUD2physical
17353931
OST48_HUMANDDOSTphysical
17353931
KBP_HUMANKIAA1279physical
17353931
CCAR2_HUMANCCAR2physical
17353931
ZW10_HUMANZW10physical
17353931
FANCI_HUMANFANCIphysical
17353931
MCM7_HUMANMCM7physical
17353931
MATR3_HUMANMATR3physical
17353931
ATX10_HUMANATXN10physical
17353931
4F2_HUMANSLC3A2physical
17353931
PI42A_HUMANPIP4K2Aphysical
21988832
PRP19_HUMANPRPF19physical
21988832
GSTK1_HUMANGSTK1physical
25416956
CYC_HUMANCYCSphysical
26344197
KITM_HUMANTK2physical
28514442
2ABD_HUMANPPP2R2Dphysical
28514442
LIMA1_HUMANLIMA1physical
28514442
PHAG1_HUMANPAG1physical
28514442
CH60_HUMANHSPD1physical
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
There are no disease associations of PTM sites.
DrugBank
DB00143Glutathione
Regulatory Network of GSTK1_HUMAN

loading...

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-71 AND LYS-169, AND MASSSPECTROMETRY.

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