TREA_YEAST - dbPTM
TREA_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TREA_YEAST
UniProt AC P32356
Protein Name Neutral trehalase
Gene Name NTH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 751
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MSQVNTSQGPVAQGRQRRLSSLSEFNDPFSNAEVYYGPPTDPRKQKQAKPAKINRTRTMSVFDNVSPFKKTGFGKLQQTRRGSEDDTYSSSQGNRRFFIEDVDKTLNELLAAEDTDKNYQITIEDTGPKVLKVGTANSYGYKHINIRGTYMLSNLLQELTIAKSFGRHQIFLDEARINENPVNRLSRLINTQFWNSLTRRVDLNNVGEIAKDTKIDTPGAKNPRIYVPYDCPEQYEFYVQASQMHPSLKLEVEYLPKKITAEYVKSVNDTPGLLALAMEEHFNPSTGEKTLIGYPYAVPGGRFNELYGWDSYMMALGLLEANKTDVARGMVEHFIFEINHYGKILNANRSYYLCRSQPPFLTEMALVVFKKLGGRSNPDAVDLLKRAFQASIKEYKTVWTASPRLDPETGLSRYHPNGLGIPPETESDHFDTVLLPYASKHGVTLDEFKQLYNDGKIKEPKLDEFFLHDRGVRESGHDTTYRFEGVCAYLATIDLNSLLYKYEIDIADFIKEFCDDKYEDPLDHSITTSAMWKEMAKIRQEKITKYMWDDESGFFFDYNTKIKHRTSYESATTFWALWAGLATKEQAQKMVEKALPKLEMLGGLAACTERSRGPISISRPIRQWDYPFGWAPHQILAWEGLRSYGYLTVTNRLAYRWLFMMTKAFVDYNGIVVEKYDVTRGTDPHRVEAEYGNQGADFKGAATEGFGWVNASYILGLKYMNSHARRALGACIPPISFFSSLRPQERNLYGL
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
2Phosphorylation------MSQVNTSQG
------CCCCCCCCC		42.7222369663
2Acetylation------MSQVNTSQG
------CCCCCCCCC		42.7222814378
6Phosphorylation--MSQVNTSQGPVAQ
--CCCCCCCCCHHHH		24.4622369663
7Phosphorylation-MSQVNTSQGPVAQG
-CCCCCCCCCHHHHH		28.1222369663
20PhosphorylationQGRQRRLSSLSEFND
HHHHHHHHCHHHCCC		27.6717330950
21PhosphorylationGRQRRLSSLSEFNDP
HHHHHHHCHHHCCCC		40.2717330950
23PhosphorylationQRRLSSLSEFNDPFS
HHHHHCHHHCCCCCC		41.9317330950
30PhosphorylationSEFNDPFSNAEVYYG
HHCCCCCCCCEEEEC		40.2822890988
35PhosphorylationPFSNAEVYYGPPTDP
CCCCCEEEECCCCCH		8.3322890988
36PhosphorylationFSNAEVYYGPPTDPR
CCCCEEEECCCCCHH		28.4722890988
40PhosphorylationEVYYGPPTDPRKQKQ
EEEECCCCCHHHCCC		62.8722890988
56PhosphorylationKPAKINRTRTMSVFD
CCCCCCCCEEEECCC		26.4617330950
58PhosphorylationAKINRTRTMSVFDNV
CCCCCCEEEECCCCC		17.1222369663
59OxidationKINRTRTMSVFDNVS
CCCCCEEEECCCCCC		2.6415665377
60PhosphorylationINRTRTMSVFDNVSP
CCCCEEEECCCCCCC		21.0122369663
66PhosphorylationMSVFDNVSPFKKTGF
EECCCCCCCCCCCCC		30.7622369663
69AcetylationFDNVSPFKKTGFGKL
CCCCCCCCCCCCCCC		53.4624489116
75AcetylationFKKTGFGKLQQTRRG
CCCCCCCCCCCCCCC		40.6425381059
79PhosphorylationGFGKLQQTRRGSEDD
CCCCCCCCCCCCCCC		14.9019823750
83PhosphorylationLQQTRRGSEDDTYSS
CCCCCCCCCCCCCCC		35.7222369663
87PhosphorylationRRGSEDDTYSSSQGN
CCCCCCCCCCCCCCC		37.3119823750
88PhosphorylationRGSEDDTYSSSQGNR
CCCCCCCCCCCCCCC		17.3522890988
89PhosphorylationGSEDDTYSSSQGNRR
CCCCCCCCCCCCCCE		26.1322890988
90PhosphorylationSEDDTYSSSQGNRRF
CCCCCCCCCCCCCEE		19.1022890988
91PhosphorylationEDDTYSSSQGNRRFF
CCCCCCCCCCCCEEE		35.8522890988
142AcetylationTANSYGYKHINIRGT
EECCCCCCEEEECHH		33.3825381059
163UbiquitinationLQELTIAKSFGRHQI
HHHHHHHHHHCCCEE		42.3323749301
213PhosphorylationVGEIAKDTKIDTPGA
HHHHHHCCCCCCCCC		29.2327214570
217PhosphorylationAKDTKIDTPGAKNPR
HHCCCCCCCCCCCCC		27.3923749301
221UbiquitinationKIDTPGAKNPRIYVP
CCCCCCCCCCCEECC		73.6923749301
254PhosphorylationSLKLEVEYLPKKITA
CCEEEEEECCHHCCH		33.2219795423
257AcetylationLEVEYLPKKITAEYV
EEEEECCHHCCHHHH		54.9624489116
260PhosphorylationEYLPKKITAEYVKSV
EECCHHCCHHHHHHC		23.4730377154
385AcetylationPDAVDLLKRAFQASI
HHHHHHHHHHHHHHH		49.3124489116
412PhosphorylationLDPETGLSRYHPNGL
CCCCCCCCCCCCCCC		31.9428889911
461AcetylationDGKIKEPKLDEFFLH
CCCCCCCCCCCCEEC		70.4424489116
480PhosphorylationRESGHDTTYRFEGVC
CCCCCCCCEEECCCE		20.8227017623
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 TREA_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TREA_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 TREA_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DCPS_YEASTDCS1physical
10688190
TREB_YEASTNTH2physical
16554755
BMH2_YEASTBMH2physical
16554755
YRA1_YEASTYRA1physical
16554755
BMH1_YEASTBMH1physical
16554755
YP216_YEASTYPL216Wphysical
16554755
BMH1_YEASTBMH1physical
16429126
BMH2_YEASTBMH2physical
16429126
TOP2_YEASTTOP2physical
16429126
DCPS_YEASTDCS1physical
18719252
SSB1_YEASTSSB1physical
19536198
TREB_YEASTNTH2genetic
19180643
TREB_YEASTNTH2genetic
18408719
BMH1_YEASTBMH1physical
17916074
BMH2_YEASTBMH2physical
17916074
BMH1_YEASTBMH1genetic
17916074
KAPA_YEASTTPK1genetic
17916074
KAPB_YEASTTPK2genetic
17916074
ATH1_YEASTATH1genetic
19016884
DEP1_YEASTDEP1genetic
20093466
RL14A_YEASTRPL14Agenetic
20093466
FPS1_YEASTFPS1genetic
20093466
TPS1_YEASTTPS1genetic
20159575
TPS2_YEASTTPS2genetic
20159575
TPS1_YEASTTPS1genetic
19180643
TPS2_YEASTTPS2genetic
19180643
PDX3_YEASTPDX3genetic
21623372
COX6_YEASTCOX6genetic
21623372
ARGJ_YEASTARG7genetic
21623372
FOLE_YEASTMET7genetic
21623372
PFKA1_YEASTPFK1genetic
21623372
CSG2_YEASTCSG2genetic
21623372
COX8_YEASTCOX8genetic
21623372
ATP18_YEASTATP18genetic
21623372
BMH1_YEASTBMH1physical
22320399
BMH2_YEASTBMH2physical
22320399
BMH1_YEASTBMH1physical
23155055
BMH2_YEASTBMH2physical
23155055
BMH1_YEASTBMH1physical
24713696
BMH1_YEASTBMH1physical
23726992
MAL11_YEASTMAL11genetic
25918381
PRS8_YEASTRPT6genetic
27708008
ARP4_YEASTARP4genetic
27708008
SEC22_YEASTSEC22genetic
27708008
MDM34_YEASTMDM34genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
FEN1_YEASTRAD27genetic
27708008
PFKA2_YEASTPFK2genetic
27708008
AEP2_YEASTAEP2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TREA_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-20; SER-21; SER-23;THR-56; THR-58; SER-60; SER-66; SER-83 AND THR-87, 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-20; SER-21; THR-58;SER-60; SER-66; SER-83; THR-87 AND SER-89, AND MASS 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 THR-58; SER-60; SER-66;SER-83 AND SER-91, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58 AND SER-60, 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-20 AND SER-60, AND MASSSPECTROMETRY.

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