SUCB_YEAST - dbPTM
SUCB_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SUCB_YEAST
UniProt AC P53312
Protein Name Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03219, ECO:0000305|PubMed:9874242}
Gene Name LSC2 {ECO:0000303|PubMed:9874242}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 427
Subcellular Localization Mitochondrion .
Protein Description Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. [PubMed: 9874242 The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit (By similarity]
Protein Sequence MYSRKSLSLISKCGQLSRLNAQAALQARRHLSIHEYRSAQLLREYGIGTPEGFPAFTPEEAFEAAKKLNTNKLVIKAQALTGGRGKGHFDTGYKSGVHMIESPQQAEDVAKEMLNHNLITKQTGIAGKPVSAVYIVKRVDTKHEAYLSILMDRQTKKPMIIASSQGGMNIEEVAERTPDAIKKFSIETSKGLSPQMAKDVAKSLGFSPDAQDEAAKAVSNLYKIFMERDATQVEINPLSEIEHDPTHKIMCTDAKFGFDDNASFRQEKIYSWRDLSQEDPDEVKAKKYDLNFVKLKGNIGCLVNGAGLAMATMDVIKLNGGDPANFLDCGGGATPETIKQGFELILSNKNVDAIFVNIFGGIVRCDYVALGLVEAARELEVRVPIVARLQGTKVEEGRDIINKSGVKIYSFDELDPAAKKVVELTQN
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
8PhosphorylationMYSRKSLSLISKCGQ
CCCHHHHHHHHHHHH		30.6530377154
93PhosphorylationKGHFDTGYKSGVHMI
CCCCCCCCCCCEEEE		12.2219684113
94AcetylationGHFDTGYKSGVHMIE
CCCCCCCCCCEEEEC		41.9224489116
95PhosphorylationHFDTGYKSGVHMIES
CCCCCCCCCEEEECC		37.2522369663
102PhosphorylationSGVHMIESPQQAEDV
CCEEEECCHHHHHHH		19.6522369663
121AcetylationLNHNLITKQTGIAGK
HHCCCCCCCCCCCCC		38.5822865919
137AcetylationVSAVYIVKRVDTKHE
EEEEEEEEECCCCHH		36.8324489116
198AcetylationGLSPQMAKDVAKSLG
CCCHHHHHHHHHHCC		47.6024489116
202AcetylationQMAKDVAKSLGFSPD
HHHHHHHHHCCCCHH		46.1724489116
207PhosphorylationVAKSLGFSPDAQDEA
HHHHCCCCHHHHHHH		21.7728889911
216AcetylationDAQDEAAKAVSNLYK
HHHHHHHHHHHHHHH		57.2624489116
223AcetylationKAVSNLYKIFMERDA
HHHHHHHHHHHHCCC		32.4124489116
263PhosphorylationFGFDDNASFRQEKIY
CCCCCCCHHHHHHEE		27.5022369663
268AcetylationNASFRQEKIYSWRDL
CCHHHHHHEECHHCC		38.3122865919
276PhosphorylationIYSWRDLSQEDPDEV
EECHHCCCCCCHHHH		35.4925752575
284UbiquitinationQEDPDEVKAKKYDLN
CCCHHHHHHHCCCCC		53.0623749301
287AcetylationPDEVKAKKYDLNFVK
HHHHHHHCCCCCEEE		49.1822865919
294AcetylationKYDLNFVKLKGNIGC
CCCCCEEEECCCEEE		40.1024489116
347PhosphorylationQGFELILSNKNVDAI
HHHHHHHCCCCCCEE		38.4728889911
393AcetylationVARLQGTKVEEGRDI
EEECCCCCCCCCCCC		55.2424489116
403AcetylationEGRDIINKSGVKIYS
CCCCCCCCCCCEEEE		37.8724489116
407AcetylationIINKSGVKIYSFDEL
CCCCCCCEEEEHHHC		39.1824489116
410PhosphorylationKSGVKIYSFDELDPA
CCCCEEEEHHHCCHH		29.6927214570
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 SUCB_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SUCB_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 SUCB_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LYS12_YEASTLYS12genetic
16941010
HOSC_YEASTLYS20genetic
16941010
LYS4_YEASTLYS4genetic
16941010
MDM10_YEASTMDM10genetic
20093466
ACH1_YEASTACH1genetic
20093466
CSG2_YEASTCSG2genetic
20093466
C1TM_YEASTMIS1genetic
20093466
CCZ1_YEASTCCZ1genetic
20093466
CEM1_YEASTCEM1genetic
20093466
AIM11_YEASTAIM11genetic
20093466
MTC3_YEASTMTC3genetic
20093466
XRN1_YEASTXRN1genetic
20093466
GEP7_YEASTGEP7genetic
20093466
PALF_YEASTRIM8genetic
20093466
PACC_YEASTRIM101genetic
20093466
FYV4_YEASTFYV4genetic
20093466
HTD2_YEASTHTD2genetic
20093466
COX23_YEASTCOX23genetic
20093466
PTH_YEASTPTH1genetic
20093466
MRX5_YEASTYJL147Cgenetic
20093466
LPLA_YEASTAIM22genetic
20093466
AIM25_YEASTAIM25genetic
20093466
COXM1_YEASTCMC1genetic
20093466
HAP4_YEASTHAP4genetic
20093466
LHS1_YEASTLHS1genetic
20093466
FABG_YEASTOAR1genetic
20093466
RL14A_YEASTRPL14Agenetic
20093466
LIPB_YEASTLIP2genetic
20093466
COX8_YEASTCOX8genetic
20093466
RCF1_YEASTRCF1genetic
20093466
MUB1_YEASTMUB1genetic
20093466
PFKA2_YEASTPFK2genetic
20093466
SWS2_YEASTSWS2genetic
20093466
ODP2_YEASTLAT1genetic
20093466
COX5A_YEASTCOX5Agenetic
20093466
ATP23_YEASTATP23genetic
20093466
SIN3_YEASTSIN3genetic
20093466
YO012_YEASTYOR012Wgenetic
20093466
DFG16_YEASTDFG16genetic
20093466
WHI2_YEASTWHI2genetic
20093466
YORA4_YEASTYOR114Wgenetic
20093466
LIPA_YEASTLIP5genetic
20093466
PALA_YEASTRIM20genetic
20093466
NIP80_YEASTNIP100genetic
20093466
KES1_YEASTKES1genetic
20093466
ACH1_YEASTACH1genetic
21623372
DCOR_YEASTSPE1genetic
21623372
CEM1_YEASTCEM1genetic
21623372
ODP2_YEASTLAT1genetic
21623372
GCSH_YEASTGCV3genetic
21623372
PHO84_YEASTPHO84genetic
21623372
ODPA_YEASTPDA1genetic
21623372
COX6_YEASTCOX6genetic
21623372
PDX3_YEASTPDX3genetic
21623372
MDM10_YEASTMDM10genetic
27708008
HAP3_YEASTHAP3genetic
27708008
REI1_YEASTREI1genetic
27708008
CBT1_YEASTCBT1genetic
27708008
FMT_YEASTFMT1genetic
27708008
ACH1_YEASTACH1genetic
27708008
VPS10_YEASTPEP1genetic
27708008
AVT5_YEASTAVT5genetic
27708008
OLA1_YEASTOLA1genetic
27708008
SIF2_YEASTSIF2genetic
27708008
ODPB_YEASTPDB1genetic
27708008
EFM2_YEASTEFM2genetic
27708008
CHK1_YEASTCHK1genetic
27708008
ATG22_YEASTATG22genetic
27708008
KAR4_YEASTKAR4genetic
27708008
PET18_YEASTPET18genetic
27708008
GPR1_YEASTGPR1genetic
27708008
STP4_YEASTSTP4genetic
27708008
RLA3_YEASTRPP1Bgenetic
27708008
PCL9_YEASTPCL9genetic
27708008
AIM11_YEASTAIM11genetic
27708008
ODPA_YEASTPDA1genetic
27708008
DLDH_YEASTLPD1genetic
27708008
RIM15_YEASTRIM15genetic
27708008
DCV1_YEASTDCV1genetic
27708008
PALF_YEASTRIM8genetic
27708008
GEP7_YEASTGEP7genetic
27708008
MON1_YEASTMON1genetic
27708008
MRM2_YEASTMRM2genetic
27708008
XRN1_YEASTXRN1genetic
27708008
MTC3_YEASTMTC3genetic
27708008
RTF1_YEASTRTF1genetic
27708008
HTD2_YEASTHTD2genetic
27708008
COX23_YEASTCOX23genetic
27708008
PTH_YEASTPTH1genetic
27708008
LPLA_YEASTAIM22genetic
27708008
MRX5_YEASTYJL147Cgenetic
27708008
SET2_YEASTSET2genetic
27708008
AIM25_YEASTAIM25genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
FABG_YEASTOAR1genetic
27708008
HAP4_YEASTHAP4genetic
27708008
COXM1_YEASTCMC1genetic
27708008
SAC1_YEASTSAC1genetic
27708008
COX12_YEASTCOX12genetic
27708008
EIF3J_YEASTHCR1genetic
27708008
LIPB_YEASTLIP2genetic
27708008
ATP10_YEASTATP10genetic
27708008
COX8_YEASTCOX8genetic
27708008
RCF1_YEASTRCF1genetic
27708008
ATP18_YEASTATP18genetic
27708008
RCO1_YEASTRCO1genetic
27708008
RIM13_YEASTRIM13genetic
27708008
AIM36_YEASTAIM36genetic
27708008
YM79_YEASTYMR244Wgenetic
27708008
AEP2_YEASTAEP2genetic
27708008
GAS1_YEASTGAS1genetic
27708008
COX5A_YEASTCOX5Agenetic
27708008
SWS2_YEASTSWS2genetic
27708008
NOP12_YEASTNOP12genetic
27708008
GLO4_YEASTGLO4genetic
27708008
CY1_YEASTCYT1genetic
27708008
YORA4_YEASTYOR114Wgenetic
27708008
COQ7_YEASTCAT5genetic
27708008
LIPA_YEASTLIP5genetic
27708008
PALA_YEASTRIM20genetic
27708008
MNE1_YEASTMNE1genetic
27708008
ALDH6_YEASTALD6genetic
27708008
KES1_YEASTKES1genetic
27708008
NIP80_YEASTNIP100genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SUCB_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-102; SER-207; SER-263AND SER-276, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND MASSSPECTROMETRY.

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