TCM62_YEAST - dbPTM
TCM62_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TCM62_YEAST
UniProt AC P38228
Protein Name Mitochondrial chaperone TCM62
Gene Name TCM62
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 572
Subcellular Localization Mitochondrion inner membrane
Single-pass membrane protein
Matrix side .
Protein Description Chaperone. Required for the assembly of succinate dehydrogenase subunits. Ensures mitochondrial gene expression at elevated temperatures and prevents heat-aggregation of the ribosomal subunit VAR1..
Protein Sequence MLRNCLRKLGNHQTKCSVKTLHTPIYRTKNLQVLRDTLSGIKLLEKIITSSSYNKTLIYEPKYKSKPQVVSSHDTMRLHNVMRELLDSLQVDEATNTRLQSNRPRKLGRVGLQLFMDCIQDNLTATSTSLTCSLLEHYFKYPEKEVTNGIKAGLRYIRDFLAKNKIIVKSQNDVDALVEQLTMSSSDSQSIKRVLKAINYELFSDDIVRVINGNKTYDEVDVSKGWKYPAGILDSNEAYLRSLELPTKKLVSIDKDMLVLMYDGTLRDANKILPTITYARKLRKSVLLIVNGDCTGDALTSVTINNNRNKRENNESRIVVLKYSKKANNDLAPQENLDFIKFLRLPCGYDSIYSPEYSPLVPSKMCADKYYGSIESIKATTGEAFLYNSIDAEAIPNKVPKSFLQNTVTLSIGGHNEIEIDRRRNAIDNCLNNVLCHGLAKGFIPGYGISLLKAIPGLNELKANEPNFMTKVGINAVLSAVILPSEVAFKNAYGYNYYEINSLIAGAINEKSFPMAKFSPNSEPVNTVKDGNLEPWSKMDSCLAGVETFIELLTSCNTIITCVYKKPERHKA
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
88PhosphorylationVMRELLDSLQVDEAT
HHHHHHHHCCCCHHH
22.2230377154
151AcetylationKEVTNGIKAGLRYIR
HHHCCHHHHHHHHHH
37.4924489116
228PhosphorylationDVSKGWKYPAGILDS
CCCCCCCCCCEECCC
7.5727017623
235PhosphorylationYPAGILDSNEAYLRS
CCCEECCCCHHHHHH
32.8827017623
239PhosphorylationILDSNEAYLRSLELP
ECCCCHHHHHHCCCC
9.1127017623
275PhosphorylationDANKILPTITYARKL
CHHHHHHHHHHHHHH
23.6228889911
285PhosphorylationYARKLRKSVLLIVNG
HHHHHCCEEEEEECC
16.1527214570
300PhosphorylationDCTGDALTSVTINNN
CCCCCCCCEEEEECC
23.9129688323
301PhosphorylationCTGDALTSVTINNNR
CCCCCCCEEEEECCC
20.3627214570
303PhosphorylationGDALTSVTINNNRNK
CCCCCEEEEECCCCC
20.1129688323
519PhosphorylationSFPMAKFSPNSEPVN
CCCCCCCCCCCCCCC
23.5928889911
522PhosphorylationMAKFSPNSEPVNTVK
CCCCCCCCCCCCCCC
46.8130377154
527PhosphorylationPNSEPVNTVKDGNLE
CCCCCCCCCCCCCCC
29.2130377154

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 TCM62_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TCM62_YEAST !!

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 TCM62_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SDH3_YEASTSDH3physical
9822678
SDHA_YEASTSDH1physical
9822678
SDHB_YEASTSDH2physical
9822678
DCOR_YEASTSPE1genetic
27708008
SNF11_YEASTSNF11genetic
27708008
GNTK_YEASTYDR248Cgenetic
27708008
SGF73_YEASTSGF73genetic
27708008
STB5_YEASTSTB5genetic
27708008
HPM1_YEASTHPM1genetic
27708008
SIN3_YEASTSIN3genetic
27708008
KPC1_YEASTPKC1genetic
29674565
TPS2_YEASTTPS2genetic
29674565
RRP8_YEASTRRP8genetic
29674565
DHAS_YEASTHOM2genetic
29674565
AK_YEASTHOM3genetic
29674565
COG3_YEASTCOG3genetic
29674565
TFS2_YEASTDST1genetic
29674565
LRP1_YEASTLRP1genetic
29674565
SDHB_YEASTSDH2genetic
29674565
VRP1_YEASTVRP1genetic
29674565
ERG6_YEASTERG6genetic
29674565
IDH1_YEASTIDH1genetic
29674565
GGPPS_YEASTBTS1genetic
29674565
NCBP2_YEASTCBC2genetic
29674565
FUMH_YEASTFUM1genetic
29674565

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TCM62_YEAST

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Related Literatures of Post-Translational Modification

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