LYS12_YEAST - dbPTM
LYS12_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LYS12_YEAST
UniProt AC P40495
Protein Name Homoisocitrate dehydrogenase, mitochondrial
Gene Name LYS12
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 371
Subcellular Localization Mitochondrion .
Protein Description Catalyzes the NAD(+)-dependent conversion of homoisocitrate to alpha-ketoadipate..
Protein Sequence MFRSVATRLSACRGLASNAARKSLTIGLIPGDGIGKEVIPAGKQVLENLNSKHGLSFNFIDLYAGFQTFQETGKALPDETVKVLKEQCQGALFGAVQSPTTKVEGYSSPIVALRREMGLFANVRPVKSVEGEKGKPIDMVIVRENTEDLYIKIEKTYIDKATGTRVADATKRISEIATRRIATIALDIALKRLQTRGQATLTVTHKSNVLSQSDGLFREICKEVYESNKDKYGQIKYNEQIVDSMVYRLFREPQCFDVIVAPNLYGDILSDGAAALVGSLGVVPSANVGPEIVIGEPCHGSAPDIAGKGIANPIATIRSTALMLEFLGHNEAAQDIYKAVDANLREGSIKTPDLGGKASTQQVVDDVLSRL
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
23PhosphorylationASNAARKSLTIGLIP
HHHHHHHCCEEEEEC		25.7828152593
25PhosphorylationNAARKSLTIGLIPGD
HHHHHCCEEEEECCC		21.7929734811
36AcetylationIPGDGIGKEVIPAGK
ECCCCCCCCCCCHHH		47.0624489116
82AcetylationALPDETVKVLKEQCQ
CCCHHHHHHHHHHHC		49.6324489116
85AcetylationDETVKVLKEQCQGAL
HHHHHHHHHHHCHHH		49.0425381059
98PhosphorylationALFGAVQSPTTKVEG
HHCCCCCCCCCCCCC		20.0219530703
102AcetylationAVQSPTTKVEGYSSP
CCCCCCCCCCCCCCH		40.5424489116
107PhosphorylationTTKVEGYSSPIVALR
CCCCCCCCCHHHHHH		40.2628889911
108PhosphorylationTKVEGYSSPIVALRR
CCCCCCCCHHHHHHH		15.3428889911
127AcetylationFANVRPVKSVEGEKG
CCCEEECEECCCCCC		52.0124489116
133SuccinylationVKSVEGEKGKPIDMV
CEECCCCCCCCCEEE		80.9923954790
133AcetylationVKSVEGEKGKPIDMV
CEECCCCCCCCCEEE		80.9924489116
135AcetylationSVEGEKGKPIDMVIV
ECCCCCCCCCEEEEE		50.2824489116
146PhosphorylationMVIVRENTEDLYIKI
EEEEECCCCEEEEEE		26.5619684113
152AcetylationNTEDLYIKIEKTYID
CCCEEEEEEEEEEEC		31.1224489116
155SuccinylationDLYIKIEKTYIDKAT
EEEEEEEEEEECCCC		50.5323954790
155AcetylationDLYIKIEKTYIDKAT
EEEEEEEEEEECCCC		50.5324489116
160AcetylationIEKTYIDKATGTRVA
EEEEEECCCCCCCHH		37.9924489116
1602-HydroxyisobutyrylationIEKTYIDKATGTRVA
EEEEEECCCCCCCHH		37.99-
191AcetylationIALDIALKRLQTRGQ
HHHHHHHHHHHHCCC		41.8825381059
207PhosphorylationTLTVTHKSNVLSQSD
EEEEEECCCHHCCCC		25.2722369663
211PhosphorylationTHKSNVLSQSDGLFR
EECCCHHCCCCCHHH		24.2922369663
213PhosphorylationKSNVLSQSDGLFREI
CCCHHCCCCCHHHHH		30.2122369663
222AcetylationGLFREICKEVYESNK
CHHHHHHHHHHHHCC		56.7425381059
229AcetylationKEVYESNKDKYGQIK
HHHHHHCCCCCCCCC		65.9524489116
229SuccinylationKEVYESNKDKYGQIK
HHHHHHCCCCCCCCC		65.9523954790
231AcetylationVYESNKDKYGQIKYN
HHHHCCCCCCCCCCC		53.5425381059
236AcetylationKDKYGQIKYNEQIVD
CCCCCCCCCCHHHHH		33.8522865919
338AcetylationEAAQDIYKAVDANLR
HHHHHHHHHHHHHCC		42.1225381059
348PhosphorylationDANLREGSIKTPDLG
HHHCCCCCCCCCCCC		19.0321440633
350AcetylationNLREGSIKTPDLGGK
HCCCCCCCCCCCCCC		56.5625381059
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 LYS12_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LYS12_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 LYS12_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCN1_YEASTGCN1physical
16429126
GFA1_YEASTGFA1physical
16429126
MET10_YEASTMET10physical
16429126
HSP82_YEASTHSP82physical
16429126
IDH2_YEASTIDH2physical
16429126
IMB4_YEASTKAP123physical
16429126
RSSA2_YEASTRPS0Bphysical
16429126
HSP74_YEASTSSA4physical
16429126
TBA1_YEASTTUB1physical
16429126
CLU_YEASTCLU1physical
16429126
RL10_YEASTRPL10physical
16429126
YHI0_YEASTYHR020Wphysical
16429126
RS5_YEASTRPS5physical
16429126
TBB_YEASTTUB2physical
16429126
PYR1_YEASTURA2physical
16429126
COPA_YEASTCOP1physical
16429126
COPB2_YEASTSEC27physical
16429126
MPG1_YEASTPSA1physical
16429126
KMO_YEASTBNA4genetic
16941010
I23O_YEASTBNA2genetic
16941010
KYNU_YEASTBNA5genetic
16941010
SDH3_YEASTSDH3genetic
16941010
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LYS12_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-107; SER-108;THR-146 AND SER-211, AND MASS SPECTROMETRY.

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