HIBCH_YEAST - dbPTM
HIBCH_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HIBCH_YEAST
UniProt AC P28817
Protein Name 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial
Gene Name EHD3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 500
Subcellular Localization Mitochondrion . Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner memb
Protein Description Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. [PubMed: 14566057]
Protein Sequence MLRNTLKCAQLSSKYGFKTTTRTFMTTQPQLNVTDAPPVLFTVQDTARVITLNRPKKLNALNAEMSESMFKTLNEYAKSDTTNLVILKSSNRPRSFCAGGDVATVAIFNFNKEFAKSIKFFTDEYSLNFQIATYLKPIVTFMDGITMGGGVGLSIHTPFRIATENTKWAMPEMDIGFFPDVGSTFALPRIVTLANSNSQMALYLCLTGEVVTGADAYMLGLASHYVSSENLDALQKRLGEISPPFNNDPQSAYFFGMVNESIDEFVSPLPKDYVFKYSNEKLNVIEACFNLSKNGTIEDIMNNLRQYEGSAEGKAFAQEIKTKLLTKSPSSLQIALRLVQENSRDHIESAIKRDLYTAANMCMNQDSLVEFSEATKHKLIDKQRVPYPWTKKEQLFVSQLTSITSPKPSLPMSLLRNTSNVTWTQYPYHSKYQLPTEQEIAAYIEKRTNDDTGAKVTEREVLNHFANVIPSRRGKLGIQSLCKIVCERKCEEVNDGLRWK
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
18AcetylationLSSKYGFKTTTRTFM
HHHHHCCEECCCEEE		40.3725381059
79PhosphorylationTLNEYAKSDTTNLVI
HHHHHHCCCCCCEEE		31.8322369663
81PhosphorylationNEYAKSDTTNLVILK
HHHHCCCCCCEEEEE		25.3622369663
82PhosphorylationEYAKSDTTNLVILKS
HHHCCCCCCEEEEEC		31.3922369663
276AcetylationLPKDYVFKYSNEKLN
CCCCCEEEECCCCCC		37.4124489116
326PhosphorylationEIKTKLLTKSPSSLQ
HHHHHHHCCCHHHHH		39.6528889911
328PhosphorylationKTKLLTKSPSSLQIA
HHHHHCCCHHHHHHH		25.4428889911
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 HIBCH_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HIBCH_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 HIBCH_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RT04_YEASTMRP4physical
11805826
RT01_YEASTMRP1physical
11805826
RT13_YEASTMRP13physical
11805826
RT51_YEASTMRP51physical
11805826
RT28_YEASTMRPS28physical
11805826
RT09_YEASTMRPS9physical
11805826
NAM9_YEASTNAM9physical
11805826
RT10_YEASTRSM10physical
11805826
RT22_YEASTRSM22physical
11805826
RT23_YEASTRSM23physical
11805826
RT24_YEASTRSM24physical
11805826
RT25_YEASTRSM25physical
11805826
RT07_YEASTRSM7physical
11805826
RT17_YEASTMRPS17physical
11805826
RT18_YEASTMRPS18physical
11805826
RT01_YEASTMRP1physical
16429126
RT13_YEASTMRP13physical
16429126
RT04_YEASTMRP4physical
16429126
RT51_YEASTMRP51physical
16429126
RT17_YEASTMRPS17physical
16429126
RT18_YEASTMRPS18physical
16429126
RT28_YEASTMRPS28physical
16429126
RT09_YEASTMRPS9physical
16429126
NAM9_YEASTNAM9physical
16429126
RT10_YEASTRSM10physical
16429126
RT22_YEASTRSM22physical
16429126
RT23_YEASTRSM23physical
16429126
RT24_YEASTRSM24physical
16429126
RT25_YEASTRSM25physical
16429126
RT07_YEASTRSM7physical
16429126
AFG2_YEASTAFG2physical
18719252
PEX14_YEASTPEX14physical
18719252
MRP8_YEASTMRP8physical
18719252
FMP10_YEASTFMP10genetic
19300474
INA22_YEASTINA22genetic
19300474
CND2_YEASTBRN1genetic
27708008
MED8_YEASTMED8genetic
27708008
MED6_YEASTMED6genetic
27708008
PRS7_YEASTRPT1genetic
27708008
ORC1_YEASTORC1genetic
27708008
OST2_YEASTOST2genetic
27708008
TF2B_YEASTSUA7genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HIBCH_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase.";
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
Mol. Cell. Proteomics 6:1896-1906(2007).
Cited for: PROTEIN SEQUENCE OF 324-337, SUBCELLULAR LOCATION, PHOSPHORYLATION ATTHR-326 AND SER-328, AND MASS SPECTROMETRY.

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