FOL1_YEAST - dbPTM
FOL1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOL1_YEAST
UniProt AC P53848
Protein Name Folic acid synthesis protein FOL1
Gene Name FOL1 {ECO:0000303|PubMed:15169867}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 824
Subcellular Localization Mitochondrion membrane .
Protein Description Catalyzes three sequential steps of tetrahydrofolate biosynthesis..
Protein Sequence MSKLFSTVNSARHSVPLGGMRDYVHIKKLEMNTVLGPDSWNQLMPQKCLLSLDMGTDFSKSAATDDLKYSLNYAVISRDLTNFVSKKKNWGSVSNLAKSVSQFVMDKYSGVECLNLEVQADTTHIRSDHISCIIQQERGNPESQEFDVVRISELKMLTLIGVFTFERLKKQYVTLDIKLPWPKKAELPPPVQSIIDNVVKFVEESNFKTVEALVESVSAVIAHNEYFQKFPDSPLVVKVLKLNAITATEGVGVSCIREPREIAMVNIPYLSSIHESSDIKFQLSSSQNTPIEGKNTWKRAFLAFGSNIGDRFKHIQMALQLLSREKTVKLRNISSIFESEPMYFKDQTPFMNGCVEVETLLTPSELLKLCKKIEYEELQRVKHFDNGPRTIDLDIVMFLNSAGEDIIVNEPDLNIPHPRMLERTFVLEPLCELISPVHLHPVTAEPIVDHLKQLYDKQHDEDTLWKLVPLPYRSGVEPRFLKFKTATKLDEFTGETNRITVSPTYIMAIFNATPDSFSDGGEHFADIESQLNDIIKLCKDALYLHESVIIDVGGCSTRPNSIQASEEEEIRRSIPLIKAIRESTELPQDKVILSIDTYRSNVAKEAIKVGVDIINDISGGLFDSNMFAVIAENPEICYILSHTRGDISTMNRLAHYENFALGDSIQQEFVHNTDIQQLDDLKDKTVLIRNVGQEIGERYIKAIDNGVKRWQILIDPGLGFAKTWKQNLQIIRHIPILKNYSFTMNSNNSQVYVNLRNMPVLLGPSRKKFIGHITKDVDAKQRDFATGAVVASCIGFGSDMVRVHDVKNCSKSIKLADAIYKGLE
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
2Acetylation------MSKLFSTVN
------CCCHHHHHH		37.7622814378
2Phosphorylation------MSKLFSTVN
------CCCHHHHHH		37.7630377154
3Acetylation-----MSKLFSTVNS
-----CCCHHHHHHC		52.8624489116
6Phosphorylation--MSKLFSTVNSARH
--CCCHHHHHHCCCC		41.7122369663
7Phosphorylation-MSKLFSTVNSARHS
-CCCHHHHHHCCCCC		19.1722369663
10PhosphorylationKLFSTVNSARHSVPL
CHHHHHHCCCCCCCC		23.4922369663
14PhosphorylationTVNSARHSVPLGGMR
HHHCCCCCCCCCCCC		21.6328889911
33PhosphorylationIKKLEMNTVLGPDSW
EEEEEECEECCCCCH		18.7919684113
56PhosphorylationLLSLDMGTDFSKSAA
EEEECCCCCCCCCCC		27.5119779198
69PhosphorylationAATDDLKYSLNYAVI
CCCCCHHHHCCEEHH		26.2028889911
77PhosphorylationSLNYAVISRDLTNFV
HCCEEHHCCCHHHHH		17.0928889911
238AcetylationPDSPLVVKVLKLNAI
CCCCCCEEEEECCEE		34.0824489116
269PhosphorylationIAMVNIPYLSSIHES
EEEEECCCHHHCCCC		18.5422369663
271PhosphorylationMVNIPYLSSIHESSD
EEECCCHHHCCCCCC		22.7722369663
272PhosphorylationVNIPYLSSIHESSDI
EECCCHHHCCCCCCC		25.9322369663
276PhosphorylationYLSSIHESSDIKFQL
CHHHCCCCCCCEEEE		21.1022369663
277PhosphorylationLSSIHESSDIKFQLS
HHHCCCCCCCEEEEC		40.1322369663
284PhosphorylationSDIKFQLSSSQNTPI
CCCEEEECCCCCCCC		19.7022369663
285PhosphorylationDIKFQLSSSQNTPIE
CCEEEECCCCCCCCC		44.5322369663
286PhosphorylationIKFQLSSSQNTPIEG
CEEEECCCCCCCCCC		24.8722369663
289PhosphorylationQLSSSQNTPIEGKNT
EECCCCCCCCCCCCH		20.2922369663
600PhosphorylationLSIDTYRSNVAKEAI
EEECCCCHHHHHHHH		25.8328889911
775AcetylationKFIGHITKDVDAKQR
HHCEEECCCCCHHHC		55.9724489116
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 FOL1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FOL1_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 FOL1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YMW4_YEASTYMR074Cphysical
16554755
FOL1_YEASTFOL1physical
22940862
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FOL1_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-286, AND MASSSPECTROMETRY.

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