TTL_YEAST - dbPTM
TTL_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TTL_YEAST
UniProt AC P38254
Protein Name Probable tubulin--tyrosine ligase PBY1
Gene Name PBY1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 753
Subcellular Localization Cytoplasm . Cytoplasm, P-body .
Protein Description Probable P-body-associated tubulin--tyrosine ligase..
Protein Sequence MRVLITNDDGPLSDQFSPYIRPFIQHIKRNYPEWKITVCVPHVQKSWVGKAHLAGKNLTAQFIYSKVDAEDNTFWGPFIQPQIRSENSKLPYVLNAEIPKDTIEWILIDGTPASCANIGLHLLSNEPFDLVLSGPNVGRNTSAAYITSSGTVGGAMESVITGNTKAIAISWAYFNGLKNVSPLLMEKASKRSLDVIKHLVKNWDPKTDLYSINIPLVESLSDDTKVYYAPIWENRWIPIFNGPHINLENSFAEIEDGNESSSISFNWAPKFGAHKDSIHYMDEYKDRTVLTDAEVIESEMISVTPMKATFKGVNHLLGELKLTEEENNLSKTNNLIVVSIDPMEYIYKPLTHALKKYLPQVEIVSNLPEFDNGGCEKEMKVFHYGDYEQLDMDKLMELPNNYFTNSYIYRKALIRKHFLSHTIQTYTAKNPESILKKAYLESFTIDLDYAEFLDDALDENWELRQELENESQDKWWIVKPSMSDKGQGIRVFKTIEDLQAIFDSFDDEDSEAEESGNDDDADDVNGEFMDNNKVNISQLRHFIIQEYLTNPLLLASMDNRKFHIRCYVVCRGDLQVFVYDRMLALFAAKPFVPLDPYAYSVTDLKDLECHLTNTCLQSKKKDKDSSVLEFDSIEEIPNERKSNIKEQIHSITNDVFLAAVNVNRLNFQPLPNAFETYGVDFLIDSNYEVKLLEINAFPDFKQTGKDLKNLIDELFDDTVKYCVTPIFNENRNKTDDETDPNFVKVIDYTSNGW
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
19PhosphorylationLSDQFSPYIRPFIQH
CCCCCCHHHHHHHHH		14.3628132839
187AcetylationVSPLLMEKASKRSLD
CHHHHHHHHHHCCHH		43.9524489116
197AcetylationKRSLDVIKHLVKNWD
HCCHHHHHHHHHCCC		30.6324489116
288PhosphorylationMDEYKDRTVLTDAEV
CHHCCCCEEEECHHH		29.9626447709
291PhosphorylationYKDRTVLTDAEVIES
CCCCEEEECHHHHHH		28.9128889911
298PhosphorylationTDAEVIESEMISVTP
ECHHHHHHHCCCCCC		22.7228889911
302PhosphorylationVIESEMISVTPMKAT
HHHHHCCCCCCCCEE		20.7327017623
304PhosphorylationESEMISVTPMKATFK
HHHCCCCCCCCEECC		15.7526447709
321AcetylationNHLLGELKLTEEENN
HHHHHHHCCCHHHCC		49.4024489116
365PhosphorylationLPQVEIVSNLPEFDN
CCCEEEECCCCCCCC		38.0128889911
481PhosphorylationKWWIVKPSMSDKGQG
CEEEECCCCCCCCCC		25.7919823750
483PhosphorylationWIVKPSMSDKGQGIR
EEECCCCCCCCCCEE		40.2719823750
485AcetylationVKPSMSDKGQGIRVF
ECCCCCCCCCCEEEE		45.9124489116
510PhosphorylationDSFDDEDSEAEESGN
HCCCCCCHHHHHHCC		36.3419795423
515PhosphorylationEDSEAEESGNDDDAD
CCHHHHHHCCCCCHH		34.1119795423
597PhosphorylationPFVPLDPYAYSVTDL
CCCCCCCCCCEECCH		20.1722369663
599PhosphorylationVPLDPYAYSVTDLKD
CCCCCCCCEECCHHH		9.6022369663
600PhosphorylationPLDPYAYSVTDLKDL
CCCCCCCEECCHHHC		15.4622369663
602PhosphorylationDPYAYSVTDLKDLEC
CCCCCEECCHHHCEE		29.6722369663
701AcetylationINAFPDFKQTGKDLK
EECCCCHHHHCHHHH		55.0924489116
734PhosphorylationFNENRNKTDDETDPN
CCCCCCCCCCCCCCC		52.8323749301
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 TTL_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TTL_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 TTL_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSK22_YEASTCKA2physical
11805837
EDC3_YEASTEDC3physical
16554755
DCP1_YEASTDCP1physical
11283351
DCP1_YEASTDCP1physical
18719252
TTL_YEASTPBY1physical
22940862
PRP9_YEASTPRP9genetic
27708008
PRS8_YEASTRPT6genetic
27708008
MED6_YEASTMED6genetic
27708008
SLN1_YEASTSLN1genetic
27708008
CDC11_YEASTCDC11genetic
27708008
PSB5_YEASTPRE2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TTL_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-600, AND MASSSPECTROMETRY.

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