TRI1_YEAST - dbPTM
TRI1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI1_YEAST
UniProt AC Q05024
Protein Name Protein TRI1
Gene Name TRI1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 226
Subcellular Localization Cytoplasm . Nucleus . Nucleus, nucleolus .
Protein Description May be involved in transcription regulation..
Protein Sequence MADINKYIPMVDAILSVSNPDEISPKRVRKALQILYSVNLDSQRKLINELILERFGDIQENPRVLIPKNDLISRDQELSLRLQKEEERPLRSTRKRKGKSESKSKRKKKKNDSPDSNSISVRKVLLSAPLQKFLGSEELPRTQVVKMIWQYIKEHDLQNPKDRREILCDEKMEPIFGKKMTMFSMNKLLTKHLFNPDEIVKHEEEQKQTPEKEIKLENESLPNLSG
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
24PhosphorylationVSNPDEISPKRVRKA
CCCCCCCCHHHHHHH
23.4821440633
68AcetylationNPRVLIPKNDLISRD
CCCEEEECCCCCCCC
56.9824489116
79PhosphorylationISRDQELSLRLQKEE
CCCCHHHHHHHHHHH
15.6427214570
100PhosphorylationTRKRKGKSESKSKRK
HHHHCCCCCCHHHHH
56.6328889911
113PhosphorylationRKKKKNDSPDSNSIS
HHCCCCCCCCCCCHH
39.7522369663
116PhosphorylationKKNDSPDSNSISVRK
CCCCCCCCCCHHHHH
35.5422369663
178AcetylationKMEPIFGKKMTMFSM
CCCCCCCCCCCHHHH
28.7325381059
179AcetylationMEPIFGKKMTMFSMN
CCCCCCCCCCHHHHH
39.7325381059
201SumoylationFNPDEIVKHEEEQKQ
CCHHHHHCCHHHHCC
51.46-
201SumoylationFNPDEIVKHEEEQKQ
CCHHHHHCCHHHHCC
51.46-
209PhosphorylationHEEEQKQTPEKEIKL
CHHHHCCCCHHHHHC
40.2124961812
215SumoylationQTPEKEIKLENESLP
CCCHHHHHCCCCCCC
51.33-
215SumoylationQTPEKEIKLENESLP
CCCHHHHHCCCCCCC
51.33-
220PhosphorylationEIKLENESLPNLSG-
HHHCCCCCCCCCCC-
61.7922369663
225PhosphorylationNESLPNLSG------
CCCCCCCCC------
49.4422369663

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 TRI1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI1_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 TRI1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMT3_YEASTSMT3physical
18719252
LRP1_YEASTLRP1genetic
20093466
MRT4_YEASTMRT4genetic
20093466
SYT1_YEASTSYT1genetic
20093466
MRT4_YEASTMRT4genetic
27708008
NNK1_YEASTNNK1genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRI1_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-113 AND SER-225, ANDMASS SPECTROMETRY.
Sumoylation
ReferencePubMed
"Topoisomerase I-dependent viability loss in saccharomyces cerevisiaemutants defective in both SUMO conjugation and DNA repair.";
Chen X.L., Silver H.R., Xiong L., Belichenko I., Adegite C.,Johnson E.S.;
Genetics 177:17-30(2007).
Cited for: SUMOYLATION AT LYS-201 AND LYS-215, AND MUTAGENESIS OF LYS-201 ANDLYS-215.

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