SUCA_YEAST - dbPTM
SUCA_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SUCA_YEAST
UniProt AC P53598
Protein Name Succinate--CoA ligase [ADP-forming] subunit alpha, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03222, ECO:0000305|PubMed:9874242}
Gene Name LSC1 {ECO:0000303|PubMed:9874242}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 329
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 alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit (By similarity]
Protein Sequence MLRSTVSKASLKICRHFHRESIPYDKTIKNLLLPKDTKVIFQGFTGKQGTFHASISQEYGTNVVGGTNPKKAGQTHLGQPVFASVKDAIKETGATASAIFVPPPIAAAAIKESIEAEIPLAVCITEGIPQHDMLYIAEMLQTQDKTRLVGPNCPGIINPATKVRIGIQPPKIFQAGKIGIISRSGTLTYEAVQQTTKTDLGQSLVIGMGGDAFPGTDFIDALKLFLEDETTEGIIMLGEIGGKAEIEAAQFLKEYNFSRSKPMPVASFIAGTVAGQMKGVRMGHSGAIVEGSGTDAESKKQALRDVGVAVVESPGYLGQALLDQFAKFK
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
26AcetylationRESIPYDKTIKNLLL
HCCCCCCCHHHHHCC		46.4324489116
27PhosphorylationESIPYDKTIKNLLLP
CCCCCCCHHHHHCCC		34.0028889911
29AcetylationIPYDKTIKNLLLPKD
CCCCCHHHHHCCCCC		46.9322865919
38AcetylationLLLPKDTKVIFQGFT
HCCCCCCEEEEECCC		43.3924489116
86AcetylationQPVFASVKDAIKETG
CCEEEHHHHHHHHHC		38.6624489116
171AcetylationRIGIQPPKIFQAGKI
EEECCCCCCEECCCE		63.9424489116
184PhosphorylationKIGIISRSGTLTYEA
CEEEEECCCEECHHH		29.3728889911
186PhosphorylationGIISRSGTLTYEAVQ
EEEECCCEECHHHHH		19.7128889911
188PhosphorylationISRSGTLTYEAVQQT
EECCCEECHHHHHHC		21.1028889911
198PhosphorylationAVQQTTKTDLGQSLV
HHHHCCCCCCCCCEE		34.0728889911
216PhosphorylationGGDAFPGTDFIDALK
CCCCCCCCCHHHHHH		28.1628889911
253AcetylationIEAAQFLKEYNFSRS
HHHHHHHHHCCCCCC		60.4824489116
258PhosphorylationFLKEYNFSRSKPMPV
HHHHCCCCCCCCCCH		31.8224909858
285PhosphorylationKGVRMGHSGAIVEGS
CCCCCCCCCEEEECC		24.9622369663
292PhosphorylationSGAIVEGSGTDAESK
CCEEEECCCCCHHHH		25.6423749301
294PhosphorylationAIVEGSGTDAESKKQ
EEEECCCCCHHHHHH		33.4623749301
298PhosphorylationGSGTDAESKKQALRD
CCCCCHHHHHHHHHH		47.0422369663
313PhosphorylationVGVAVVESPGYLGQA
HCEEEEECCCHHHHH		16.4122369663
316PhosphorylationAVVESPGYLGQALLD
EEEECCCHHHHHHHH		15.8422369663
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 SUCA_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SUCA_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 SUCA_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AAKG_YEASTSNF4physical
16554755
SUCB_YEASTLSC2physical
16554755
ACH1_YEASTACH1genetic
21623372
CEM1_YEASTCEM1genetic
21623372
GCSH_YEASTGCV3genetic
21623372
ODPA_YEASTPDA1genetic
21623372
ATP18_YEASTATP18genetic
21623372
ARO1_YEASTARO1genetic
21623372
ARGJ_YEASTARG7genetic
21623372
PPT2_YEASTPPT2genetic
21623372
HTD2_YEASTHTD2genetic
21623372
COX10_YEASTCOX10genetic
21623372
FABG_YEASTOAR1genetic
21623372
COX5A_YEASTCOX5Agenetic
21623372
ERG2_YEASTERG2genetic
21623372
SUCA_YEASTLSC1physical
22940862
SUCB_YEASTLSC2physical
22940862
HSP71_YEASTSSA1physical
22940862
STE50_YEASTSTE50genetic
27708008
YRA2_YEASTYRA2genetic
27708008
ACH1_YEASTACH1genetic
27708008
ODPB_YEASTPDB1genetic
27708008
ARO1_YEASTARO1genetic
27708008
CEM1_YEASTCEM1genetic
27708008
DLDH_YEASTLPD1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
HTD2_YEASTHTD2genetic
27708008
LPLA_YEASTAIM22genetic
27708008
FABG_YEASTOAR1genetic
27708008
DBP7_YEASTDBP7genetic
27708008
LIPB_YEASTLIP2genetic
27708008
YL413_YEASTINA1genetic
27708008
OCA2_YEASTOCA2genetic
27708008
ODP2_YEASTLAT1genetic
27708008
WDR6_YEASTRTT10genetic
27708008
PCL8_YEASTPCL8genetic
27708008
AGP1_YEASTAGP1genetic
29674565
WDR59_YEASTMTC5genetic
29674565
UBX5_YEASTUBX5genetic
29674565
PSP1_YEASTPSP1genetic
29674565
CEM1_YEASTCEM1genetic
29674565
SLX9_YEASTSLX9genetic
29674565
TBP7_YEASTYTA7genetic
29674565
HTD2_YEASTHTD2genetic
29674565
LPLA_YEASTAIM22genetic
29674565
MNN11_YEASTMNN11genetic
29674565
FABG_YEASTOAR1genetic
29674565
PRR1_YEASTPRR1genetic
29674565
ACE2_YEASTACE2genetic
29674565
ADH2_YEASTADH2genetic
29674565
ADE_YEASTAAH1genetic
29674565
FUMH_YEASTFUM1genetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SUCA_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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND THR-186, ANDMASS SPECTROMETRY.
"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 THR-186, AND MASSSPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27, AND MASSSPECTROMETRY.

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