TGL1_YEAST - dbPTM
TGL1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TGL1_YEAST
UniProt AC P34163
Protein Name Sterol esterase TGL1
Gene Name TGL1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 548
Subcellular Localization Membrane
Single-pass type III membrane protein. Lipid droplet.
Protein Description Mediates the hydrolysis of steryl esters. Required for mobilization of steryl ester, thereby playing a central role in lipid metabolism. May have weak lipase activity toward triglycerides upon some conditions, however, the relevance of such activity is unclear in vivo..
Protein Sequence MYFPFLGRLSITDYIIVVLVYIESIISSVLKLIPQPMINLFEWLINFSTSSDDNTIEEKLRSAPTIHEMCAIFDISVEDHLVRTEDNYILTLHRIPPISKNRFNNKVVYLHHGLLMCSDVWCCNIERHKNLPFVLHDLGYDVWMGNNRGNKYSTAHLNKPPKSNKFWDFSIDEFAFFDIPNSIEFILDITKVDKVICIGFSQGSAQMFAAFSLSEKLNRKVSHFIAIAPAMTPKGLHNRIVDTLAKSSPGFMYLFFGRKIVLPSAVIWQRTLHPTLFNLCIDIANKILFNWKSFNILPRQKIASYAKLYSTTSVKSIVHWFQILRSQKFQMFEESDNMLNSLTRPYQIANFPTRTNIKIPILLIYGGIDSLVDIDVMKKNLPFNSVFDVKVDNYEHLDLIWGKDADTLVIAKVLRFIEFFNPGNVSVKTNQLLPSASLVEELPSTTWKTTHPTHGLSYRTHSADRSPLSVQADEADEVHNADNSRFLRRVFSTSAIDEDNENEHQDDTEDQIHKEQQRRLSAYLESSKDLRQLDANSSTTALDALNKE
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
1Acetylation-------MYFPFLGR
-------CCCCCCCC		7.5923613772
2Phosphorylation------MYFPFLGRL
------CCCCCCCCC		21.6928889911
21PhosphorylationYIIVVLVYIESIISS
HHHHHHHHHHHHHHH		8.5323749301
24PhosphorylationVVLVYIESIISSVLK
HHHHHHHHHHHHHHH		18.7023749301
28PhosphorylationYIESIISSVLKLIPQ
HHHHHHHHHHHHCCH		22.5123749301
100UbiquitinationHRIPPISKNRFNNKV
EECCCCCCCCCCCCE		53.5123749301
246UbiquitinationRIVDTLAKSSPGFMY
HHHHHHHHCCCCCEE		55.3622106047
248PhosphorylationVDTLAKSSPGFMYLF
HHHHHHCCCCCEEEE		28.4719779198
253PhosphorylationKSSPGFMYLFFGRKI
HCCCCCEEEEECCEE		9.7119779198
259UbiquitinationMYLFFGRKIVLPSAV
EEEEECCEEEECCHH		37.2323749301
379UbiquitinationVDIDVMKKNLPFNSV
CCHHHHHCCCCCCCE		45.6924961812
412UbiquitinationADTLVIAKVLRFIEF
HHHHHHHHHHHHHHH		30.5824961812
426PhosphorylationFFNPGNVSVKTNQLL
HCCCCCCEEECCCCC		23.1527214570
428UbiquitinationNPGNVSVKTNQLLPS
CCCCCEEECCCCCCC		33.9617644757
435PhosphorylationKTNQLLPSASLVEEL
ECCCCCCCCHHHHCC		30.3821440633
437PhosphorylationNQLLPSASLVEELPS
CCCCCCCHHHHCCCC		36.9730377154
448UbiquitinationELPSTTWKTTHPTHG
CCCCCCCCCCCCCCC		41.2617644757
460PhosphorylationTHGLSYRTHSADRSP
CCCCEEECCCCCCCC		16.3722369663
462PhosphorylationGLSYRTHSADRSPLS
CCEEECCCCCCCCCC		31.1122369663
466PhosphorylationRTHSADRSPLSVQAD
ECCCCCCCCCCCCCC		30.6422369663
469PhosphorylationSADRSPLSVQADEAD
CCCCCCCCCCCCCHH		18.6322369663
492PhosphorylationRFLRRVFSTSAIDED
HHHHHHHCCCCCCCC		20.7022369663
493PhosphorylationFLRRVFSTSAIDEDN
HHHHHHCCCCCCCCC		15.6522369663
494PhosphorylationLRRVFSTSAIDEDNE
HHHHHCCCCCCCCCC		23.2522369663
508PhosphorylationENEHQDDTEDQIHKE
CCCCCCCCHHHHHHH		50.1519779198
514UbiquitinationDTEDQIHKEQQRRLS
CCHHHHHHHHHHHHH		59.8724961812
521PhosphorylationKEQQRRLSAYLESSK
HHHHHHHHHHHHCCH		17.0422369663
523PhosphorylationQQRRLSAYLESSKDL
HHHHHHHHHHCCHHH		13.9722890988
526PhosphorylationRLSAYLESSKDLRQL
HHHHHHHCCHHHHHH		39.8422890988
527PhosphorylationLSAYLESSKDLRQLD
HHHHHHCCHHHHHHC		22.3322890988
537PhosphorylationLRQLDANSSTTALDA
HHHHCCCCCHHHHHH		30.6825521595
538PhosphorylationRQLDANSSTTALDAL
HHHCCCCCHHHHHHH		29.5922369663
539PhosphorylationQLDANSSTTALDALN
HHCCCCCHHHHHHHH		18.8622369663
540PhosphorylationLDANSSTTALDALNK
HCCCCCHHHHHHHHC		27.4625521595
547UbiquitinationTALDALNKE------
HHHHHHHCC------		66.7017644757
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 TGL1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TGL1_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 TGL1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YEH1_YEASTYEH1genetic
15713625
YEH2_YEASTYEH2genetic
15713625
PIL1_YEASTPIL1genetic
16269340
CASP_YEASTCOY1genetic
16269340
SCS7_YEASTSCS7genetic
16269340
SAC1_YEASTSAC1genetic
16269340
BFR1_YEASTBFR1genetic
16269340
CHO2_YEASTCHO2genetic
16269340
TGL1_YEASTTGL1physical
18467557
ENG2_YEASTACF2physical
18467557
YIM1_YEASTYIM1physical
18467557
6PGD1_YEASTGND1genetic
21623372
SUR1_YEASTSUR1genetic
21623372
LEU1_YEASTLEU4genetic
21623372
ADH3_YEASTADH3genetic
21623372
PDX3_YEASTPDX3genetic
21623372
GGPPS_YEASTBTS1genetic
21623372
PUR3_YEASTADE8genetic
21623372
ADK_YEASTADO1genetic
21623372
RPN10_YEASTRPN10genetic
23891562
TYSY_YEASTCDC21genetic
27708008
AAR2_YEASTAAR2genetic
27708008
MAK21_YEASTMAK21genetic
27708008
PRP19_YEASTPRP19genetic
27708008
TAD3_YEASTTAD3genetic
27708008
SEC39_YEASTSEC39genetic
27708008
TAF13_YEASTTAF13genetic
27708008
TAF8_YEASTTAF8genetic
27708008
PGA3_YEASTPGA3genetic
27708008
HMCS_YEASTERG13genetic
27708008
RSC9_YEASTRSC9genetic
27708008
ERO1_YEASTERO1genetic
27708008
NOP2_YEASTNOP2genetic
27708008
SEC62_YEASTSEC62genetic
27708008
ASA1_YEASTASA1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TGL1_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-469; SER-492; SER-521;SER-537; SER-538 AND THR-539, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492 AND SER-521, ANDMASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521 AND SER-537, ANDMASS SPECTROMETRY.

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