TSL1_YEAST - dbPTM
TSL1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TSL1_YEAST
UniProt AC P38427
Protein Name Trehalose synthase complex regulatory subunit TSL1
Gene Name TSL1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1098
Subcellular Localization Cytoplasm .
Protein Description Regulatory subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-glucose in a two step process. May stabilize the trehalose synthase complex, and confer sensitivity to physiological concentrations of phosphate and to fructose 6-phosphate..
Protein Sequence MALIVASLFLPYQPQFELDTSLPENSQVDSSLVNIQAMANDQQQQRALSNNISQESLVAPAPEQGVPPAISRSATRSPSAFNRASSTTNTATLDDLVSSDIFMENLTANATTSHTPTSKTMLKPRKNGSVERFFSPSSNIPTDRIASPIQHEHDSGSRIASPIQQQQQDPTTNLLKNVNKSLLVHSLLNNTSQTSLEGPNNHIVTPKSRAGNRPTSAATSLVNRTKQGSASSGSSGSSAPPSIKRITPHLTASAAKQRPLLAKQPSNLKYSELADISSSETSSQHNESDPDDLTTAPDEEYVSDLEMDDAKQDYKVPKFGGYSNKSKLKKYALLRSSQELFSRLPWSIVPSIKGNGAMKNAINTAVLENIIPHRHVKWVGTVGIPTDEIPENILANISDSLKDKYDSYPVLTDDDTFKAAYKNYCKQILWPTLHYQIPDNPNSKAFEDHSWKFYRNLNQRFADAIVKIYKKGDTIWIHDYHLMLVPQMVRDVLPFAKIGFTLHVSFPSSEVFRCLAQREKILEGLTGADFVGFQTREYARHFLQTSNRLLMADVVHDEELKYNGRVVSVRFTPVGIDAFDLQSQLKDGSVMQWRQLIRERWQGKKLIVCRDQFDRIRGIHKKLLAYEKFLVENPEYVEKSTLIQICIGSSKDVELERQIMIVVDRINSLSTNISISQPVVFLHQDLDFSQYLALSSEADLFVVSSLREGMNLTCHEFIVCSEDKNAPLLLSEFTGSASLLNDGAIIINPWDTKNFSQAILKGLEMPFDKRRPQWKKLMKDIINNDSTNWIKTSLQDIHISWQFNQEGSKIFKLNTKTLMEDYQSSKKRMFVFNIAEPPSSRMISILNDMTSKGNIVYIMNSFPKPILENLYSRVQNIGLIAENGAYVSLNGVWYNIVDQVDWRNDVAKILEDKVERLPGSYYKINESMIKFHTENAEDQDRVASVIGDAITHINTVFDHRGIHAYVYKNVVSVQQVGLSLSAAQFLFRFYNSASDPLDTSSGQITNIQTPSQQNPSDQEQQPPASPTVSMNHIDFACVSGSSSPVLEPLFKLVNDEASEGQVKAGHAIVYGDATSTYAKEHVNGLNELFTIISRIIED
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
49PhosphorylationQQQQRALSNNISQES
HHHHHHHHCCCCHHH		27.1822369663
53PhosphorylationRALSNNISQESLVAP
HHHHCCCCHHHHCCC		29.9822369663
56PhosphorylationSNNISQESLVAPAPE
HCCCCHHHHCCCCCC		22.1022369663
71PhosphorylationQGVPPAISRSATRSP
CCCCCCCCCCCCCCH		23.4522369663
73PhosphorylationVPPAISRSATRSPSA
CCCCCCCCCCCCHHH		27.4822369663
75PhosphorylationPAISRSATRSPSAFN
CCCCCCCCCCHHHHH		32.6922369663
77PhosphorylationISRSATRSPSAFNRA
CCCCCCCCHHHHHHC		20.8922369663
79PhosphorylationRSATRSPSAFNRASS
CCCCCCHHHHHHCCC		46.9022369663
85PhosphorylationPSAFNRASSTTNTAT
HHHHHHCCCCCCCCC		25.6122369663
86PhosphorylationSAFNRASSTTNTATL
HHHHHCCCCCCCCCH		37.9622369663
87PhosphorylationAFNRASSTTNTATLD
HHHHCCCCCCCCCHH		22.9022369663
88PhosphorylationFNRASSTTNTATLDD
HHHCCCCCCCCCHHH		32.3022369663
90PhosphorylationRASSTTNTATLDDLV
HCCCCCCCCCHHHHH		20.9422369663
92PhosphorylationSSTTNTATLDDLVSS
CCCCCCCCHHHHHCC		28.7821440633
98PhosphorylationATLDDLVSSDIFMEN
CCHHHHHCCCHHHHC		29.5922369663
99PhosphorylationTLDDLVSSDIFMENL
CHHHHHCCCHHHHCC		27.5222369663
107PhosphorylationDIFMENLTANATTSH
CHHHHCCCCCCCCCC		29.4622369663
111PhosphorylationENLTANATTSHTPTS
HCCCCCCCCCCCCCC		28.7423749301
112PhosphorylationNLTANATTSHTPTSK
CCCCCCCCCCCCCCC		18.9922369663
113PhosphorylationLTANATTSHTPTSKT
CCCCCCCCCCCCCCC		22.4722369663
115PhosphorylationANATTSHTPTSKTML
CCCCCCCCCCCCCCC		28.2022369663
117PhosphorylationATTSHTPTSKTMLKP
CCCCCCCCCCCCCCC		43.9722369663
118PhosphorylationTTSHTPTSKTMLKPR
CCCCCCCCCCCCCCC		27.6022369663
129PhosphorylationLKPRKNGSVERFFSP
CCCCCCCCCCCCCCC		30.1422369663
135PhosphorylationGSVERFFSPSSNIPT
CCCCCCCCCCCCCCC		22.5922369663
137PhosphorylationVERFFSPSSNIPTDR
CCCCCCCCCCCCCCC		34.5122369663
138PhosphorylationERFFSPSSNIPTDRI
CCCCCCCCCCCCCCC		42.0122369663
142PhosphorylationSPSSNIPTDRIASPI
CCCCCCCCCCCCCCC		33.8322369663
147PhosphorylationIPTDRIASPIQHEHD
CCCCCCCCCCCCCCC		21.8422369663
155PhosphorylationPIQHEHDSGSRIASP
CCCCCCCCCCCCCCH		40.3422369663
157PhosphorylationQHEHDSGSRIASPIQ
CCCCCCCCCCCCHHH		25.1922369663
161PhosphorylationDSGSRIASPIQQQQQ
CCCCCCCCHHHHHHC		21.8422369663
171PhosphorylationQQQQQDPTTNLLKNV
HHHHCCCCCHHHHHH		36.2822890988
172PhosphorylationQQQQDPTTNLLKNVN
HHHCCCCCHHHHHHC		29.2922890988
181PhosphorylationLLKNVNKSLLVHSLL
HHHHHCHHHHHHHHH		23.0222369663
186PhosphorylationNKSLLVHSLLNNTSQ
CHHHHHHHHHCCCCC		27.3722369663
191PhosphorylationVHSLLNNTSQTSLEG
HHHHHCCCCCCCCCC		22.5722369663
192PhosphorylationHSLLNNTSQTSLEGP
HHHHCCCCCCCCCCC		33.3222369663
194PhosphorylationLLNNTSQTSLEGPNN
HHCCCCCCCCCCCCC		34.7422369663
195PhosphorylationLNNTSQTSLEGPNNH
HCCCCCCCCCCCCCC		19.4522369663
205PhosphorylationGPNNHIVTPKSRAGN
CCCCCCCCCCCCCCC		25.1322369663
208PhosphorylationNHIVTPKSRAGNRPT
CCCCCCCCCCCCCCC		28.6822369663
215PhosphorylationSRAGNRPTSAATSLV
CCCCCCCCHHHHHHH		27.9722369663
216PhosphorylationRAGNRPTSAATSLVN
CCCCCCCHHHHHHHC		20.7022369663
219PhosphorylationNRPTSAATSLVNRTK
CCCCHHHHHHHCCCC		23.4722369663
220PhosphorylationRPTSAATSLVNRTKQ
CCCHHHHHHHCCCCC		26.1222369663
229PhosphorylationVNRTKQGSASSGSSG
HCCCCCCCCCCCCCC		23.6022369663
231PhosphorylationRTKQGSASSGSSGSS
CCCCCCCCCCCCCCC		36.6122369663
232PhosphorylationTKQGSASSGSSGSSA
CCCCCCCCCCCCCCC		42.2722369663
234PhosphorylationQGSASSGSSGSSAPP
CCCCCCCCCCCCCCC		33.2122369663
235PhosphorylationGSASSGSSGSSAPPS
CCCCCCCCCCCCCCC		46.3422369663
237PhosphorylationASSGSSGSSAPPSIK
CCCCCCCCCCCCCHH		25.8522369663
238PhosphorylationSSGSSGSSAPPSIKR
CCCCCCCCCCCCHHH		48.6022369663
242PhosphorylationSGSSAPPSIKRITPH
CCCCCCCCHHHCCCC		39.4222369663
247PhosphorylationPPSIKRITPHLTASA
CCCHHHCCCCCCHHH		14.5322369663
251PhosphorylationKRITPHLTASAAKQR
HHCCCCCCHHHHHHC		18.6122369663
253PhosphorylationITPHLTASAAKQRPL
CCCCCCHHHHHHCCC		24.4322369663
263UbiquitinationKQRPLLAKQPSNLKY
HHCCCCCCCCCCCCH		63.8123749301
266PhosphorylationPLLAKQPSNLKYSEL
CCCCCCCCCCCHHHH		52.9122369663
270PhosphorylationKQPSNLKYSELADIS
CCCCCCCHHHHHCCC		15.5623607784
271PhosphorylationQPSNLKYSELADISS
CCCCCCHHHHHCCCC		25.2523607784
277PhosphorylationYSELADISSSETSSQ
HHHHHCCCCCCCCCC		28.4923607784
278PhosphorylationSELADISSSETSSQH
HHHHCCCCCCCCCCC		32.3121551504
279PhosphorylationELADISSSETSSQHN
HHHCCCCCCCCCCCC		37.8023607784
281PhosphorylationADISSSETSSQHNES
HCCCCCCCCCCCCCC		35.3123607784
282PhosphorylationDISSSETSSQHNESD
CCCCCCCCCCCCCCC		24.7723607784
283PhosphorylationISSSETSSQHNESDP
CCCCCCCCCCCCCCC		42.7619795423
288PhosphorylationTSSQHNESDPDDLTT
CCCCCCCCCCCCCCC		60.8121440633
294PhosphorylationESDPDDLTTAPDEEY
CCCCCCCCCCCCHHH		28.1021440633
295PhosphorylationSDPDDLTTAPDEEYV
CCCCCCCCCCCHHHC		43.4119779198
301PhosphorylationTTAPDEEYVSDLEMD
CCCCCHHHCCCCCCC		11.8221551504
303PhosphorylationAPDEEYVSDLEMDDA
CCCHHHCCCCCCCCH		35.2621440633
318AcetylationKQDYKVPKFGGYSNK
HCCCCCCCCCCCCCH		60.6825381059
323PhosphorylationVPKFGGYSNKSKLKK
CCCCCCCCCHHHHHH		40.8519779198
336PhosphorylationKKYALLRSSQELFSR
HHHHHHHCHHHHHHC		36.0222369663
337PhosphorylationKYALLRSSQELFSRL
HHHHHHCHHHHHHCC		22.6522369663
404AcetylationISDSLKDKYDSYPVL
CCHHHHHHCCCCCCC		49.7424489116
418AcetylationLTDDDTFKAAYKNYC
CCCCHHHHHHHHHHH		33.9124489116
426AcetylationAAYKNYCKQILWPTL
HHHHHHHHHHHHCCC		29.9724489116
452AcetylationAFEDHSWKFYRNLNQ
CCCCCHHHHHHHHHH		35.2224489116
467AcetylationRFADAIVKIYKKGDT
HHHHHHHHHHHCCCE		33.9224489116
561AcetylationVVHDEELKYNGRVVS
EECCHHHEECCEEEE		39.6924489116
628AcetylationKKLLAYEKFLVENPE
HHHHHHHHHHCCCHH		31.1824489116
640PhosphorylationNPEYVEKSTLIQICI
CHHHHCCCEEEEHHH		18.2319795423
641PhosphorylationPEYVEKSTLIQICIG
HHHHCCCEEEEHHHC		38.6619823750
649PhosphorylationLIQICIGSSKDVELE
EEEHHHCCCCCHHHH		17.8219823750
650PhosphorylationIQICIGSSKDVELER
EEHHHCCCCCHHHHH		27.8819823750
761AcetylationNFSQAILKGLEMPFD
CHHHHHHHCCCCCCC		56.1724489116
761UbiquitinationNFSQAILKGLEMPFD
CHHHHHHHCCCCCCC		56.1724961812
769AcetylationGLEMPFDKRRPQWKK
CCCCCCCCCCHHHHH		51.1624489116
815PhosphorylationSKIFKLNTKTLMEDY
CEEEEEEHHHHHHHH		35.5225752575
817PhosphorylationIFKLNTKTLMEDYQS
EEEEEHHHHHHHHHH		29.3327017623
822PhosphorylationTKTLMEDYQSSKKRM
HHHHHHHHHHCCCEE		9.2927017623
824PhosphorylationTLMEDYQSSKKRMFV
HHHHHHHHCCCEEEE		37.5927017623
844PhosphorylationPPSSRMISILNDMTS
CCCHHHHHHHHHCCC		16.2222369663
850PhosphorylationISILNDMTSKGNIVY
HHHHHHCCCCCCEEE		30.1022369663
851PhosphorylationSILNDMTSKGNIVYI
HHHHHCCCCCCEEEE		31.7422369663
857PhosphorylationTSKGNIVYIMNSFPK
CCCCCEEEEECCCCH		7.2319779198
861PhosphorylationNIVYIMNSFPKPILE
CEEEEECCCCHHHHH		26.0828889911
871PhosphorylationKPILENLYSRVQNIG
HHHHHHHHHHHHHHE		13.1519779198
872PhosphorylationPILENLYSRVQNIGL
HHHHHHHHHHHHHEE		29.1919779198
908AcetylationDWRNDVAKILEDKVE
CCHHHHHHHHHHHHH		47.9024489116
913UbiquitinationVAKILEDKVERLPGS
HHHHHHHHHHHCCCC		36.3023749301
923AcetylationRLPGSYYKINESMIK
HCCCCEEECCHHHHH		30.7224489116
923UbiquitinationRLPGSYYKINESMIK
HCCCCEEECCHHHHH		30.7224961812
930AcetylationKINESMIKFHTENAE
ECCHHHHHEECCCCC		23.5824489116
1042PhosphorylationFACVSGSSSPVLEPL
EEEECCCCCCCHHHH		42.0328889911
1043PhosphorylationACVSGSSSPVLEPLF
EEECCCCCCCHHHHH		22.2628889911
1058PhosphorylationKLVNDEASEGQVKAG
HHHCCCCCCCCCCCC		39.9722369663
1075PhosphorylationIVYGDATSTYAKEHV
EEECCCCCHHHHHHH		22.5721551504
1093PhosphorylationNELFTIISRIIED--
HHHHHHHHHHHCC--		17.3622369663
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 TSL1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TSL1_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 TSL1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TSL1_YEASTTSL1physical
9194697
TPS1_YEASTTPS1physical
16554755
TPS3_YEASTTPS3physical
16554755
TPS1_YEASTTPS1physical
16429126
TPS2_YEASTTPS2physical
16429126
FAS1_YEASTFAS1physical
16429126
TPS1_YEASTTPS1physical
18719252
CAK1_YEASTCAK1genetic
19269370
2ABA_YEASTCDC55genetic
19269370
TPS2_YEASTTPS2genetic
21623372
COX9_YEASTCOX9genetic
21623372
APA2_YEASTAPA2genetic
21623372
PFKA1_YEASTPFK1genetic
21623372
NDH2_YEASTNDE2genetic
21623372
CSG2_YEASTCSG2genetic
21623372
ERG2_YEASTERG2genetic
21623372
POS5_YEASTPOS5genetic
21623372
YJ24_YEASTKCH1genetic
27708008
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
AP2A_YEASTAPL3genetic
27708008
YBQ6_YEASTYBR056Wgenetic
27708008
AGP1_YEASTAGP1genetic
27708008
MTU1_YEASTSLM3genetic
27708008
METE_YEASTMET6genetic
27708008
ILM1_YEASTILM1genetic
27708008
BPT1_YEASTBPT1genetic
27708008
RL8B_YEASTRPL8Bgenetic
27708008
SIC1_YEASTSIC1genetic
27708008
HAP5_YEASTHAP5genetic
27708008
AXL1_YEASTAXL1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TSL1_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-49; SER-53; SER-56;SER-71; SER-73; SER-77; SER-79; SER-113; THR-115; SER-118; SER-135;SER-147; SER-161; THR-191; SER-192; SER-303; SER-337; THR-815;SER-1042 AND SER-1043, 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 THR-75; SER-77; SER-79;SER-147 AND SER-192, AND MASS SPECTROMETRY.
"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-49; THR-75; SER-77 ANDSER-161, AND MASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75 AND SER-77, AND MASSSPECTROMETRY.
"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 THR-247 AND THR-251, ANDMASS SPECTROMETRY.

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