TPS3_YEAST - dbPTM
TPS3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPS3_YEAST
UniProt AC P38426
Protein Name Trehalose synthase complex regulatory subunit TPS3
Gene Name TPS3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1054
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..
Protein Sequence MTIIVASLFLPYTPQFEADVTNSDTAKLVESSMIKVDCNNQELSNNKQERSSSVTSASSHYIGLPQEAQINGEPLQRANVGSPATGVNYHNEMEMLSSEQFLEELTANATHAANSGIPPANNPVSSGSTAQRPSVEEFFSAPSARVCSPSQEASASSISASRSSAHHNDLSSSLMKNPNLSFDSHPPRVRSSSKSAVITPVSKSVPDVDPAVVDVAKVREEFQQQASLPSMKRVSGSTAGDSSIASSSSNLRYSQQFQDNFIEDTDSEDDIDSDLETDATKKYNVPKFGGYSNNAKLRASLMRNSYELFKHLPWTIVDSDKGNGSLKNAVNIAVAEKTVKEPVSWVGTMGIPTDELPHEVCHKISKKLEQDFSSFPVVTDDITFKGAYKNYAKQILWPTLHYQIPDNPNSKAFEDHSWDYYQKVNQKFSDRIVSVYKPGDTIWIHDYHLMLVPQMVREKLPKAKIGFFLHVSFPSSEVFRCLANRERILEGIIGANFVGFQTKEYKRHFLQTCNRLLAADVSNDEVKYHCNIVSVMYAPIGIDYYHLTSQLRNGSVLEWRQLIKERWRNKKLIVCRDQFDRIRGLQKKMLAYERFLIENPEYIEKVVLIQICIGKSSDPEYERQIMVVVDRINSLSSNISISQPVVFLHQDLDFAQYLALNCEADVFLVDALREGMNLTCHEFIVSSFEKNAPLLLSEFTGSSSVLKEGAILINPWDINHVAQSIKRSLEMSPEEKRRRWKKLFKSVIEHDSDNWITKCFEYINNAWESNQETSTVFNLAPEKFCADYKASKKHLFIFKISEPPTSRMLSLLSELSSNNIVYVLSSFTKNTFESLYNGVLNIGLIAENGAYVRVNGSWYNIVEELDWMKEVAKIFDEKVERLPGSYYKIADSMIRFHTENADDQDRVPTVIGEAITHINTLFDDRDIHAYVHKDIVFVQQTGLALAAAEFLMKFYNSGVSPTDNSRISLSRTSSSMSVGNNKKHFQNQVDFVCVSGSTSPIIEPLFKLVKQEVEKNNLKFGYTILYGSSRSTYAKEHINGVNELFTILHDLTAA
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------MTIIVASLF
------CEEEEEEEC
30.6230377154
7Phosphorylation-MTIIVASLFLPYTP
-CEEEEEEECCCCCC
14.5730377154
12PhosphorylationVASLFLPYTPQFEAD
EEEECCCCCCCCEEC
32.9528889911
13PhosphorylationASLFLPYTPQFEADV
EEECCCCCCCCEECC
14.5228889911
21PhosphorylationPQFEADVTNSDTAKL
CCCEECCCCHHHHHH
29.5628889911
25PhosphorylationADVTNSDTAKLVESS
ECCCCHHHHHHHHHH
26.0528889911
44PhosphorylationDCNNQELSNNKQERS
ECCCHHHHCCHHHHH
37.2923749301
51PhosphorylationSNNKQERSSSVTSAS
HCCHHHHHHCCCHHH
26.6422369663
52PhosphorylationNNKQERSSSVTSASS
CCHHHHHHCCCHHHH
34.7422369663
53PhosphorylationNKQERSSSVTSASSH
CHHHHHHCCCHHHHC
30.5722369663
55PhosphorylationQERSSSVTSASSHYI
HHHHHCCCHHHHCCC
22.1122369663
56PhosphorylationERSSSVTSASSHYIG
HHHHCCCHHHHCCCC
24.8122369663
58PhosphorylationSSSVTSASSHYIGLP
HHCCCHHHHCCCCCC
19.8822369663
59PhosphorylationSSVTSASSHYIGLPQ
HCCCHHHHCCCCCCH
21.7422369663
61PhosphorylationVTSASSHYIGLPQEA
CCHHHHCCCCCCHHC
9.9122369663
82PhosphorylationLQRANVGSPATGVNY
CCCCCCCCCCCCCCH
13.6928889911
148PhosphorylationAPSARVCSPSQEASA
CCCCEECCCCCCHHH
25.4022369663
150PhosphorylationSARVCSPSQEASASS
CCEECCCCCCHHHHH
25.1022369663
154PhosphorylationCSPSQEASASSISAS
CCCCCCHHHHHHCCC
28.1222890988
156PhosphorylationPSQEASASSISASRS
CCCCHHHHHHCCCHH
26.2122890988
157PhosphorylationSQEASASSISASRSS
CCCHHHHHHCCCHHH
21.9322890988
159PhosphorylationEASASSISASRSSAH
CHHHHHHCCCHHHHC
23.3422890988
161PhosphorylationSASSISASRSSAHHN
HHHHHCCCHHHHCCC
26.3822890988
163PhosphorylationSSISASRSSAHHNDL
HHHCCCHHHHCCCCC
29.4030377154
164PhosphorylationSISASRSSAHHNDLS
HHCCCHHHHCCCCCC
30.4328889911
176UbiquitinationDLSSSLMKNPNLSFD
CCCHHHHHCCCCCCC
74.6417644757
181PhosphorylationLMKNPNLSFDSHPPR
HHHCCCCCCCCCCCC
33.3822369663
184PhosphorylationNPNLSFDSHPPRVRS
CCCCCCCCCCCCCCC
35.5622369663
191PhosphorylationSHPPRVRSSSKSAVI
CCCCCCCCCCCCEEE
35.7919823750
192PhosphorylationHPPRVRSSSKSAVIT
CCCCCCCCCCCEEEE
31.0819823750
193PhosphorylationPPRVRSSSKSAVITP
CCCCCCCCCCEEEEC
31.6917330950
195PhosphorylationRVRSSSKSAVITPVS
CCCCCCCCEEEECCC
29.7122369663
199PhosphorylationSSKSAVITPVSKSVP
CCCCEEEECCCCCCC
15.8423749301
202PhosphorylationSAVITPVSKSVPDVD
CEEEECCCCCCCCCC
22.0321440633
204PhosphorylationVITPVSKSVPDVDPA
EEECCCCCCCCCCHH
31.2322369663
217AcetylationPAVVDVAKVREEFQQ
HHHHHHHHHHHHHHH
41.4924489116
230PhosphorylationQQQASLPSMKRVSGS
HHHCCCCCCCCCCCC
42.0830377154
232UbiquitinationQASLPSMKRVSGSTA
HCCCCCCCCCCCCCC
54.7224961812
232AcetylationQASLPSMKRVSGSTA
HCCCCCCCCCCCCCC
54.7225381059
235PhosphorylationLPSMKRVSGSTAGDS
CCCCCCCCCCCCCCC
30.9322369663
237PhosphorylationSMKRVSGSTAGDSSI
CCCCCCCCCCCCCCC
13.9422369663
238PhosphorylationMKRVSGSTAGDSSIA
CCCCCCCCCCCCCCC
37.8823749301
242PhosphorylationSGSTAGDSSIASSSS
CCCCCCCCCCCCCCC
23.7922369663
243PhosphorylationGSTAGDSSIASSSSN
CCCCCCCCCCCCCCC
27.2422369663
246PhosphorylationAGDSSIASSSSNLRY
CCCCCCCCCCCCCCC
29.1422369663
247PhosphorylationGDSSIASSSSNLRYS
CCCCCCCCCCCCCCC
28.8522369663
248PhosphorylationDSSIASSSSNLRYSQ
CCCCCCCCCCCCCCH
22.2822369663
249PhosphorylationSSIASSSSNLRYSQQ
CCCCCCCCCCCCCHH
41.6622369663
253PhosphorylationSSSSNLRYSQQFQDN
CCCCCCCCCHHHHHC
17.6322369663
254PhosphorylationSSSNLRYSQQFQDNF
CCCCCCCCHHHHHCC
15.8622369663
265PhosphorylationQDNFIEDTDSEDDID
HHCCCCCCCCCCCCC
28.7422369663
267PhosphorylationNFIEDTDSEDDIDSD
CCCCCCCCCCCCCCC
45.0422369663
273PhosphorylationDSEDDIDSDLETDAT
CCCCCCCCCCCCCCH
44.4222369663
277PhosphorylationDIDSDLETDATKKYN
CCCCCCCCCCHHCCC
37.9322369663
280PhosphorylationSDLETDATKKYNVPK
CCCCCCCHHCCCCCC
30.7722369663
287AcetylationTKKYNVPKFGGYSNN
HHCCCCCCCCCCCCC
52.9724489116
292PhosphorylationVPKFGGYSNNAKLRA
CCCCCCCCCCHHHHH
27.2128889911
300PhosphorylationNNAKLRASLMRNSYE
CCHHHHHHHHHCHHH
19.1021440633
305PhosphorylationRASLMRNSYELFKHL
HHHHHHCHHHHHHHC
15.0422369663
306PhosphorylationASLMRNSYELFKHLP
HHHHHCHHHHHHHCC
21.8722369663
321AcetylationWTIVDSDKGNGSLKN
CEEECCCCCCCCHHH
59.2224489116
373PhosphorylationKKLEQDFSSFPVVTD
HHHHHHHHCCCEECC
39.0828889911
374PhosphorylationKLEQDFSSFPVVTDD
HHHHHHHCCCEECCC
33.3028889911
379PhosphorylationFSSFPVVTDDITFKG
HHCCCEECCCCCCCC
28.3421551504
383PhosphorylationPVVTDDITFKGAYKN
CEECCCCCCCCHHHH
26.7021551504
389UbiquitinationITFKGAYKNYAKQIL
CCCCCHHHHHHHHHH
42.8423749301
393AcetylationGAYKNYAKQILWPTL
CHHHHHHHHHHHCEE
27.7524489116
423AcetylationHSWDYYQKVNQKFSD
CCCHHHHHHHHHHHH
27.3424489116
745AcetylationRRWKKLFKSVIEHDS
HHHHHHHHHHHHCCC
55.0024489116
752PhosphorylationKSVIEHDSDNWITKC
HHHHHCCCCCHHHHH
34.4519779198
810PhosphorylationPPTSRMLSLLSELSS
CCCHHHHHHHHHHCC
20.2328889911
813PhosphorylationSRMLSLLSELSSNNI
HHHHHHHHHHCCCCE
41.6119779198
817PhosphorylationSLLSELSSNNIVYVL
HHHHHHCCCCEEEEE
46.6619779198
822PhosphorylationLSSNNIVYVLSSFTK
HCCCCEEEEECCCCH
7.5919779198
878UbiquitinationVAKIFDEKVERLPGS
HHHHHHHHHHHCCCC
51.7623749301
885PhosphorylationKVERLPGSYYKIADS
HHHHCCCCHHHHHHH
24.2919779198
886PhosphorylationVERLPGSYYKIADSM
HHHCCCCHHHHHHHH
18.0719779198
888AcetylationRLPGSYYKIADSMIR
HCCCCHHHHHHHHHE
24.1624489116
955PhosphorylationAEFLMKFYNSGVSPT
HHHHHHHHHCCCCCC
11.6922369663
957PhosphorylationFLMKFYNSGVSPTDN
HHHHHHHCCCCCCCC
29.2322369663
960PhosphorylationKFYNSGVSPTDNSRI
HHHHCCCCCCCCCCE
26.1322369663
962PhosphorylationYNSGVSPTDNSRISL
HHCCCCCCCCCCEEE
40.0622369663
965PhosphorylationGVSPTDNSRISLSRT
CCCCCCCCCEEEEEC
33.5322369663
968PhosphorylationPTDNSRISLSRTSSS
CCCCCCEEEEECCCC
21.1222369663
970PhosphorylationDNSRISLSRTSSSMS
CCCCEEEEECCCCCC
27.0722369663
972PhosphorylationSRISLSRTSSSMSVG
CCEEEEECCCCCCCC
29.5922369663
973PhosphorylationRISLSRTSSSMSVGN
CEEEEECCCCCCCCC
21.2122369663
974PhosphorylationISLSRTSSSMSVGNN
EEEEECCCCCCCCCC
29.4622369663
975PhosphorylationSLSRTSSSMSVGNNK
EEEECCCCCCCCCCH
18.1622369663
977PhosphorylationSRTSSSMSVGNNKKH
EECCCCCCCCCCHHH
28.9022369663
1010AcetylationEPLFKLVKQEVEKNN
HHHHHHHHHHHHHCC
51.7022865919

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 TPS3_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPS3_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 TPS3_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TSL1_YEASTTSL1genetic
9837904
TPS1_YEASTTPS1physical
16429126
TPS2_YEASTTPS2physical
16429126
TPS3_YEASTTPS3physical
18467557
PP2C1_YEASTPTC1genetic
19269370
YPT6_YEASTYPT6genetic
19269370
TDA1_YEASTTDA1genetic
19269370
RAS1_YEASTRAS1genetic
19269370
HSP71_YEASTSSA1physical
19536198
TSL1_YEASTTSL1genetic
18408719
TSL1_YEASTTSL1genetic
16941010
ECM33_YEASTECM33genetic
20093466
RUD3_YEASTRUD3genetic
20093466
UBA3_YEASTUBA3genetic
20093466
MED1_YEASTMED1genetic
20093466
THI20_YEASTTHI20genetic
21623372
CISY3_YEASTCIT3genetic
21623372
GABAT_YEASTUGA1genetic
21623372
METE_YEASTMET6genetic
21623372
ETR1_YEASTETR1genetic
21623372
GPD1_YEASTGPD1genetic
21623372
HMDH2_YEASTHMG2genetic
21623372
LOT6_YEASTLOT6genetic
21623372
ADK_YEASTADO1genetic
21623372
DAK1_YEASTDAK1genetic
21623372
MALX3_YEASTIMA1genetic
21623372
QCR7_YEASTQCR7genetic
21623372
PUR4_YEASTADE6genetic
21623372
DUR1_YEASTDUR1,2genetic
21623372
ATPA_YEASTATP1genetic
21623372
AK_YEASTHOM3genetic
21623372
SPSY_YEASTSPE4genetic
21623372
PHO89_YEASTPHO89genetic
21623372
ODO2_YEASTKGD2genetic
21623372
PHO87_YEASTPHO87genetic
21623372
TREA_YEASTNTH1genetic
21623372
SPEE_YEASTSPE3genetic
21623372
UGA4_YEASTUGA4genetic
21623372
COX9_YEASTCOX9genetic
21623372
METK1_YEASTSAM1genetic
21623372
TPS3_YEASTTPS3physical
22615397
COQ2_YEASTCOQ2genetic
27708008
RIM15_YEASTRIM15genetic
27708008
SA155_YEASTSAP155genetic
27708008
CSK2B_YEASTCKB1genetic
27708008
MTC3_YEASTMTC3genetic
27708008
DBF2_YEASTDBF2genetic
27708008
PHB2_YEASTPHB2genetic
27708008
TVP38_YEASTTVP38genetic
27708008
MDM30_YEASTMDM30genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
UBA3_YEASTUBA3genetic
27708008
KAR3_YEASTKAR3genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPS3_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-51; SER-52; SER-53;THR-55; SER-56; SER-58; SER-59; SER-82; SER-148; SER-150; SER-181;SER-193; SER-195; SER-204; SER-237; SER-246; SER-249; SER-273;SER-960; SER-965; SER-974; SER-975 AND SER-977, 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-51; SER-52; SER-53;SER-181; SER-192; SER-193; SER-970; SER-973; SER-974; SER-975 ANDSER-977, 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 SER-181; SER-191; SER-192AND SER-193, 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 SER-148; SER-181 ANDSER-960, 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-53; THR-55; SER-148 ANDSER-181, 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 SER-974 AND SER-977, ANDMASS SPECTROMETRY.

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