THTR_HUMAN - dbPTM
THTR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THTR_HUMAN
UniProt AC Q16762
Protein Name Thiosulfate sulfurtransferase
Gene Name TST
Organism Homo sapiens (Human).
Sequence Length 297
Subcellular Localization Mitochondrion matrix.
Protein Description Formation of iron-sulfur complexes, cyanide detoxification or modification of sulfur-containing enzymes. Other thiol compounds, besides cyanide, can act as sulfur ion acceptors. Also has weak mercaptopyruvate sulfurtransferase (MST) activity (By similarity). Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA..
Protein Sequence MVHQVLYRALVSTKWLAESIRTGKLGPGLRVLDASWYSPGTREARKEYLERHVPGASFFDIEECRDTASPYEMMLPSEAGFAEYVGRLGISNHTHVVVYDGEHLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAVFKATLDRSLLKTYEQVLENLESKRFQLVDSRSQGRFLGTEPEPDAVGLDSGHIRGAVNMPFMDFLTEDGFEKGPEELRALFQTKKVDLSQPLIATCRKGVTACHVALAAYLCGKPDVAVYDGSWSEWFRRAPPESRVSQGKSEKA
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
7Phosphorylation-MVHQVLYRALVSTK
-CHHHHHHHHHHCHH		8.5921253578
14AcetylationYRALVSTKWLAESIR
HHHHHCHHHHHHHHH		32.4819608861
14MalonylationYRALVSTKWLAESIR
HHHHHCHHHHHHHHH		32.4826320211
14SuccinylationYRALVSTKWLAESIR
HHHHHCHHHHHHHHH		32.48-
14SuccinylationYRALVSTKWLAESIR
HHHHHCHHHHHHHHH		32.48-
14UbiquitinationYRALVSTKWLAESIR
HHHHHCHHHHHHHHH		32.4819608861
24SuccinylationAESIRTGKLGPGLRV
HHHHHHCCCCCCEEE		50.0523954790
24MalonylationAESIRTGKLGPGLRV
HHHHHHCCCCCCEEE		50.0526320211
24AcetylationAESIRTGKLGPGLRV
HHHHHHCCCCCCEEE		50.0525953088
35O-linked_GlycosylationGLRVLDASWYSPGTR
CEEEEECCCCCCCCH		26.64UniProtKB CARBOHYD
35PhosphorylationGLRVLDASWYSPGTR
CEEEEECCCCCCCCH		26.6423186163
37PhosphorylationRVLDASWYSPGTREA
EEEECCCCCCCCHHH		11.5128857561
38PhosphorylationVLDASWYSPGTREAR
EEECCCCCCCCHHHH		15.5928555341
41PhosphorylationASWYSPGTREARKEY
CCCCCCCCHHHHHHH		28.8128857561
136SuccinylationGGFRNWLKEGHPVTS
CCHHHHHHCCCCCCC		53.95-
136MalonylationGGFRNWLKEGHPVTS
CCHHHHHHCCCCCCC		53.9526320211
136AcetylationGGFRNWLKEGHPVTS
CCHHHHHHCCCCCCC		53.95-
136SuccinylationGGFRNWLKEGHPVTS
CCHHHHHHCCCCCCC		53.95-
154AcetylationRPEPAVFKATLDRSL
CCCCCHHHHHHCHHH		33.5920167786
154MalonylationRPEPAVFKATLDRSL
CCCCCHHHHHHCHHH		33.5926320211
160PhosphorylationFKATLDRSLLKTYEQ
HHHHHCHHHHHHHHH		37.4124719451
163AcetylationTLDRSLLKTYEQVLE
HHCHHHHHHHHHHHH		55.12-
163UbiquitinationTLDRSLLKTYEQVLE
HHCHHHHHHHHHHHH		55.12-
164PhosphorylationLDRSLLKTYEQVLEN
HCHHHHHHHHHHHHH		32.0621082442
165PhosphorylationDRSLLKTYEQVLENL
CHHHHHHHHHHHHHH		11.6321082442
175SuccinylationVLENLESKRFQLVDS
HHHHHHHCCEEEECC		48.10-
175UbiquitinationVLENLESKRFQLVDS
HHHHHHHCCEEEECC		48.10-
175AcetylationVLENLESKRFQLVDS
HHHHHHHCCEEEECC		48.102380437
175SuccinylationVLENLESKRFQLVDS
HHHHHHHCCEEEECC		48.10-
191PhosphorylationSQGRFLGTEPEPDAV
CCCCCCCCCCCCCCC		50.98-
202PhosphorylationPDAVGLDSGHIRGAV
CCCCCCCCCCCCCCC		37.0022817900
218PhosphorylationMPFMDFLTEDGFEKG
CCHHHHHCCCCCHHC		31.83-
224SuccinylationLTEDGFEKGPEELRA
HCCCCCHHCHHHHHH		76.99-
224SuccinylationLTEDGFEKGPEELRA
HCCCCCHHCHHHHHH		76.99-
224AcetylationLTEDGFEKGPEELRA
HCCCCCHHCHHHHHH		76.99-
236AcetylationLRALFQTKKVDLSQP
HHHHHCCCCCCCCCC		39.76-
237SuccinylationRALFQTKKVDLSQPL
HHHHCCCCCCCCCCH		44.35-
237SuccinylationRALFQTKKVDLSQPL
HHHHCCCCCCCCCCH		44.35-
237AcetylationRALFQTKKVDLSQPL
HHHHCCCCCCCCCCH		44.35-
241PhosphorylationQTKKVDLSQPLIATC
CCCCCCCCCCHHHHH		25.86-
248S-nitrosocysteineSQPLIATCRKGVTAC
CCCHHHHHHCCHHHH		2.90-
248S-nitrosylationSQPLIATCRKGVTAC
CCCHHHHHHCCHHHH		2.9024105792
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 THTR_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THTR_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 THTR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NU1M_HUMANND1physical
6402020
UBC12_HUMANUBE2Mphysical
22939629
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 THTR_HUMAN

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Related Literatures of Post-Translational Modification

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