TEC1_YEAST - dbPTM
TEC1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TEC1_YEAST
UniProt AC P18412
Protein Name Ty transcription activator TEC1
Gene Name TEC1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 486
Subcellular Localization Nucleus.
Protein Description TEC1 is involved in the activation of TY1 and TY1-mediated gene expression. It is not involved in mating or sporulation processes..
Protein Sequence MSLKEDDFGKDNSRNIESYTGRIFDVYIQKDSYSQSALDDMFPEAVVSTAACVKNEAEDNINLIDTHPQFELVNTGLGAKSDDLKSPSAKATFTDKQRKNEVPNISVSNYFPGQSSETSSTTESWTIGCDKWSEKVEEAFLEALRLIMKNGTTKIKIRNANFGRNELISLYIKHKTNEFRTKKQISSHIQVWKKTIQNKIKDSLTLSSKEKELLHLIEHGAEQTTENSNLFYDIFEEIIDSLPSVSDSGSLTPKNLYVSNNSSGLSVHSKLLTPITASNEKKIENFIKTNAASQAKTPLIYAKHIYENIDGYKCVPSKRPLEQLSPTELHQGDRPNKASFSNKKAILESAKKIEIEQRKIINKYQRISRIQEHESNPEFSSNSNSGSEYESEEEVVPRSATVTQLQSRPVPYYKNNGMPYSLSKVRGRPMYPRPAEDAYNANYIQGLPQYQTSYFSQLLLSSPQHYEHSPHQRNFTPSNQSHGNFY
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
2Acetylation------MSLKEDDFG
------CCCCCCCCC		48.4222814378
54SumoylationVSTAACVKNEAEDNI
HHHHHHHCCCCCCCC		49.29-
86PhosphorylationAKSDDLKSPSAKATF
CCCCCCCCCCCCCCC		31.2417563356
88PhosphorylationSDDLKSPSAKATFTD
CCCCCCCCCCCCCCC		49.8730377154
257PhosphorylationSLTPKNLYVSNNSSG
CCCCCCEEEECCCCC		15.9522369663
259PhosphorylationTPKNLYVSNNSSGLS
CCCCEEEECCCCCCE		19.4122369663
262PhosphorylationNLYVSNNSSGLSVHS
CEEEECCCCCCEECC		29.9922369663
263PhosphorylationLYVSNNSSGLSVHSK
EEEECCCCCCEECCC		45.9722369663
266PhosphorylationSNNSSGLSVHSKLLT
ECCCCCCEECCCEEC		22.7022369663
269PhosphorylationSSGLSVHSKLLTPIT
CCCCEECCCEECCCC		23.8922369663
273PhosphorylationSVHSKLLTPITASNE
EECCCEECCCCCCCH		24.0715620356
276PhosphorylationSKLLTPITASNEKKI
CCEECCCCCCCHHHH		25.8228889911
278PhosphorylationLLTPITASNEKKIEN
EECCCCCCCHHHHHH		36.5521551504
297PhosphorylationNAASQAKTPLIYAKH
CHHHHCCCCEEEEEE		26.7528889911
306PhosphorylationLIYAKHIYENIDGYK
EEEEEEHHHCCCCCC		11.5727017623
317PhosphorylationDGYKCVPSKRPLEQL
CCCCCCCCCCCHHHC		22.3927017623
325PhosphorylationKRPLEQLSPTELHQG
CCCHHHCCCCCCCCC		29.4819823750
327PhosphorylationPLEQLSPTELHQGDR
CHHHCCCCCCCCCCC		48.0419823750
401PhosphorylationEVVPRSATVTQLQSR
CCCCCCCEEEEHHCC		25.9027017623
476PhosphorylationSPHQRNFTPSNQSHG
CCCCCCCCCCCCCCC		29.3822369663
478PhosphorylationHQRNFTPSNQSHGNF
CCCCCCCCCCCCCCC		44.4322369663
481PhosphorylationNFTPSNQSHGNFY--
CCCCCCCCCCCCC--		37.3022369663
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
-KUbiquitinationE3 ubiquitin ligaseCDC4P07834
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseDIA2Q08496
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TEC1_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 TEC1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H2B1_YEASTHTB1physical
11805837
H4_YEASTHHF1physical
11805837
STE12_YEASTSTE12physical
11805837
FLO8_YEASTFLO8physical
15485921
CDC4_YEASTCDC4physical
15620356
UBI4P_YEASTUBI4physical
15620357
MSS11_YEASTMSS11physical
15485921
KAPR_YEASTBCY1genetic
10373537
RAS2_YEASTRAS2genetic
9055077
STE11_YEASTSTE11genetic
9055077
STE12_YEASTSTE12genetic
9055077
FUS3_YEASTFUS3genetic
15558284
GBB_YEASTSTE4genetic
15620357
STE12_YEASTSTE12physical
16782869
DIG1_YEASTDIG1physical
16782869
H4_YEASTHHF1genetic
17314980
FLO8_YEASTFLO8genetic
15466424
MSS11_YEASTMSS11genetic
15466424
PPZ2_YEASTPPZ2genetic
19269370
FAB1_YEASTFAB1genetic
19269370
YPT6_YEASTYPT6genetic
19269370
VAC14_YEASTVAC14genetic
19269370
RFA2_YEASTRFA2genetic
19269370
DIG1_YEASTDIG1physical
19218425
GBB_YEASTSTE4genetic
19897738
HAP3_YEASTHAP3genetic
20093466
STE50_YEASTSTE50genetic
20093466
CSM1_YEASTCSM1genetic
20093466
SWI5_YEASTSWI5genetic
20093466
SHE9_YEASTSHE9genetic
20093466
PT122_YEASTPET122genetic
20093466
HAP2_YEASTHAP2genetic
20093466
GSH1_YEASTGSH1genetic
20093466
YJ24_YEASTKCH1genetic
20093466
CBT1_YEASTCBT1genetic
20093466
SWS2_YEASTSWS2genetic
20093466
COQ7_YEASTCAT5genetic
20093466
AIM44_YEASTAIM44genetic
20093466
STE12_YEASTSTE12genetic
20118212
SFL1_YEASTSFL1genetic
20421603
KAPC_YEASTTPK3genetic
20421603
ZAP1_YEASTZAP1genetic
20959818
AFT1_YEASTAFT1genetic
20959818
AATC_YEASTAAT2genetic
20959818
CYC8_YEASTCYC8genetic
20959818
SWI5_YEASTSWI5genetic
20959818
CDC4_YEASTCDC4physical
19897738
FUS3_YEASTFUS3genetic
21127252
RSP5_YEASTRSP5physical
21840851
MSA1_YEASTMSA1physical
24732795
MSA2_YEASTMSA2physical
24732795
STE12_YEASTSTE12physical
24732795
MBP1_YEASTMBP1physical
24732795
SWI4_YEASTSWI4physical
24732795
HAP3_YEASTHAP3genetic
27708008
STE50_YEASTSTE50genetic
27708008
RV161_YEASTRVS161genetic
27708008
MTU1_YEASTSLM3genetic
27708008
GPR1_YEASTGPR1genetic
27708008
SWI5_YEASTSWI5genetic
27708008
RV167_YEASTRVS167genetic
27708008
SHE9_YEASTSHE9genetic
27708008
VMA21_YEASTVMA21genetic
27708008
YJ24_YEASTKCH1genetic
27708008
ILM1_YEASTILM1genetic
27708008
CBT1_YEASTCBT1genetic
27708008
LTHAD_YEASTSRY1genetic
27708008
AVL9_YEASTAVL9genetic
27708008
SWS2_YEASTSWS2genetic
27708008
HMI1_YEASTHMI1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
AIM44_YEASTAIM44genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TEC1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-86, 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 SER-325, AND MASSSPECTROMETRY.

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