TREB_YEAST - dbPTM
TREB_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TREB_YEAST
UniProt AC P35172
Protein Name Probable trehalase
Gene Name NTH2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 780
Subcellular Localization
Protein Description
Protein Sequence MVDFLPKVTEINPPSEGNDGEDNIKPLSSGSEQRPLKEEGQQGGRRHHRRLSSMHEYFDPFSNAEVYYGPITDPRKQSKIHRLNRTRTMSVFNKVSDFKNGMKDYTLKRRGSEDDSFLSSQGNRRFYIDNVDLALDELLASEDTDKNHQITIEDTGPKVIKVGTANSNGFKHVNVRGTYMLSNLLQELTIAKSFGRHQIFLDEARINENPVDRLSRLITTQFWTSLTRRVDLYNIAEIARDSKIDTPGAKNPRIYVPYNCPEQYEFYIQASQMNPSLKLEVEYLPKDITAEYVKSLNDTPGLLALAMEEHVNPSTGERSLVGYPYAVPGGRFNELYGWDSYLMALGLIESNKVDVARGMVEHFIFEIDHYSKILNANRSYYLCRSQPPFLTDMALLVFEKIGGKNNPNAIQLLKRAFRAAIKEYKEVWMSSPRLDSLTGLSCYHSDGIGIPPETEPDHFDTILLPYAEKYNVTLEKLRYLYNEGMIKEPKLDAFFLHDRAVRESGHDTTYRFEGVCAYLATIDLNSLLYKYEKDIAFVIKEYFGNEYKDENDGTVTDSEHWEELAELRKTRINKYMWDEDSGFFFYYNTKLKCRTSYESATTFWSLWAGLATEEQAKITVEKALPQLEMLGGLVACTEKSRGPISIDRPIRQWDYPFGWAPHQILAWKGLSAYGYQQVATRLAYRWLYMITKSFVDYNGMVVEKYDVTRGTDPHRVDAEYGNQGADFKGVATEGFGWVNTSYLLGLKYMNNHARRALAACSPPLPFFNSLKPSEKKLYYL
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
52PhosphorylationRRHHRRLSSMHEYFD
HHHHHHHHHHHHHCC		24.6523749301
53PhosphorylationRHHRRLSSMHEYFDP
HHHHHHHHHHHHCCC		28.8421440633
57PhosphorylationRLSSMHEYFDPFSNA
HHHHHHHHCCCCCCC		9.9021440633
62PhosphorylationHEYFDPFSNAEVYYG
HHHCCCCCCCEEEEC		40.2819779198
67PhosphorylationPFSNAEVYYGPITDP
CCCCCEEEECCCCCH		8.3319779198
68PhosphorylationFSNAEVYYGPITDPR
CCCCEEEECCCCCHH		22.9219779198
86PhosphorylationKIHRLNRTRTMSVFN
HHHHCCCHHHHHHHH		29.4428152593
88PhosphorylationHRLNRTRTMSVFNKV
HHCCCHHHHHHHHHH		17.1217287358
90PhosphorylationLNRTRTMSVFNKVSD
CCCHHHHHHHHHHHH		23.9717287358
112PhosphorylationYTLKRRGSEDDSFLS
CCCCCCCCCCCCCCC		35.7225533186
116PhosphorylationRRGSEDDSFLSSQGN
CCCCCCCCCCCCCCC		40.1729136822
119PhosphorylationSEDDSFLSSQGNRRF
CCCCCCCCCCCCCCE		20.7124961812
120PhosphorylationEDDSFLSSQGNRRFY
CCCCCCCCCCCCCEE		44.2324961812
127PhosphorylationSQGNRRFYIDNVDLA
CCCCCCEEEECCHHH		12.9324961812
141PhosphorylationALDELLASEDTDKNH
HHHHHHHCCCCCCCC		35.6528889911
192UbiquitinationLQELTIAKSFGRHQI
HHHHHHHHHHCCCEE		42.3323749301
246PhosphorylationARDSKIDTPGAKNPR
HHHCCCCCCCCCCCE		27.3927214570
250UbiquitinationKIDTPGAKNPRIYVP
CCCCCCCCCCEEECC		73.6923749301
283PhosphorylationSLKLEVEYLPKDITA
CCEEEEEECCCCCCH		33.2219823750
509PhosphorylationRESGHDTTYRFEGVC
HHHCCCCCCCCCCCC		20.8227017623
637PhosphorylationLGGLVACTEKSRGPI
HCCEEEECCCCCCCC		36.3926447709
640PhosphorylationLVACTEKSRGPISID
EEEECCCCCCCCCCC		35.9226447709
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 TREB_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TREB_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 TREB_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CALM_YEASTCMD1physical
16554755
VATB_YEASTVMA2physical
16554755
HSP42_YEASTHSP42physical
16554755
MLC1_YEASTMLC1physical
16554755
BEM1_YEASTBEM1genetic
20093466
STE50_YEASTSTE50genetic
20093466
SNF11_YEASTSNF11genetic
20093466
ENT5_YEASTENT5genetic
20093466
RAD54_YEASTRAD54genetic
20093466
SNF6_YEASTSNF6genetic
20093466
SAC1_YEASTSAC1genetic
20093466
METW_YEASTYLL058Wgenetic
20093466
HMDH1_YEASTHMG1genetic
20093466
YSP3_YEASTYSP3genetic
20093466
GGPPS_YEASTBTS1genetic
20093466
TPS1_YEASTTPS1genetic
20159575
TPS2_YEASTTPS2genetic
20159575
TPS1_YEASTTPS1genetic
19180643
TPS2_YEASTTPS2genetic
19180643
MAL11_YEASTMAL11genetic
25918381
APC11_YEASTAPC11genetic
27708008
RPN5_YEASTRPN5genetic
27708008
CDC1_YEASTCDC1genetic
27708008
CDC12_YEASTCDC12genetic
27708008
YJ9I_YEASTYJR141Wgenetic
27708008
TAD3_YEASTTAD3genetic
27708008
DCP2_YEASTDCP2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TREB_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-90 AND SER-112, AND MASSSPECTROMETRY.
"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-112, 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-88 AND SER-90, AND MASSSPECTROMETRY.

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