YD444_YEAST - dbPTM
YD444_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YD444_YEAST
UniProt AC Q04093
Protein Name Putative lipase YDR444W
Gene Name YDR444W
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 687
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MPYKINRMKNSLEINETGGTLLVDERKRLRIGELYRYKFSVNKDVIKEQGLDVSHLFLRIKNEESALLRPLYLTGPYSFYIDVRPHNYNENRKFPGKEIIPFVENLKPDERFKVKILLNENSRVGDTSLYSWTIDIISQLAVTTIPKLEFSFRIGTTRKVVKKSNGLFKSIEGVSLEMWDTETLWDLPPKFPEKPVHLVIMTHGIFSNIGCDMLYMKDKIEEMTFPMDESINPNIIVRGFMGNVGKSGHGIHCLGVRVGKYVLETVDKLNKKYKVDRISFIGHSLGGPTQSMAVRYISIKRPDFFDAVKGVKPVNFITLASPFIGVIGDFPFYLSVPLDMGALGLTGRDLNLKYTPLTSKDGLYADDEVYPEHSKYILEILPQAPAKKVFESFKRRTIYANVMDDGIVPLRTAALLYLDWRSIHKVQKIRKKNKNSPTSSEFVSSDSPESSGASSPSNENGNNVGEIPAESPNKKATLQWTLPQAVIHGSKINKYKRGQTNEANSDSDNEQGVFLDGQKFEPPKEANTVLSALSVLTAAIPDQEYIKNPAVRKDEVIHDKLYHPEELPPPHYENRPIVKKLIYPNESVNRIQERIAREWQETMTWRKVLVQIQPDSHNNIVVRRRFVNLYGYVAVEHMVEHHFGSKVCSELAEDANEPKDEPNQSSQADRSNEYNEGEISKGAENAT
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
11PhosphorylationKINRMKNSLEINETG
CCCCCCCCEEECCCC		23.1228889911
20PhosphorylationEINETGGTLLVDERK
EECCCCCEEEECCCH		20.4728889911
122PhosphorylationKILLNENSRVGDTSL
EEEECCCCCCCCCCH		23.3630377154
151PhosphorylationTIPKLEFSFRIGTTR
CCCEEEEEEECCCCE		12.3030377154
157PhosphorylationFSFRIGTTRKVVKKS
EEEECCCCEEEEHHC		24.2330377154
261PhosphorylationLGVRVGKYVLETVDK
CCCCCCHHHHHHHHH		12.3527017623
450PhosphorylationVSSDSPESSGASSPS
CCCCCCCCCCCCCCC		37.1424961812
451PhosphorylationSSDSPESSGASSPSN
CCCCCCCCCCCCCCC		36.3924961812
454PhosphorylationSPESSGASSPSNENG
CCCCCCCCCCCCCCC		46.4324961812
455PhosphorylationPESSGASSPSNENGN
CCCCCCCCCCCCCCC		31.6423749301
457PhosphorylationSSGASSPSNENGNNV
CCCCCCCCCCCCCCC		59.7424961812
471PhosphorylationVGEIPAESPNKKATL
CCCCCCCCCCCCCEE		35.5621440633
477PhosphorylationESPNKKATLQWTLPQ
CCCCCCCEEEEECCC		28.5027017623
500PhosphorylationNKYKRGQTNEANSDS
CCCCCCCCCCCCCCC		37.5422369663
505PhosphorylationGQTNEANSDSDNEQG
CCCCCCCCCCCCCCC		45.6022369663
507PhosphorylationTNEANSDSDNEQGVF
CCCCCCCCCCCCCEE		42.0022369663
665PhosphorylationPKDEPNQSSQADRSN
CCCCCCCCCCCCCCC		30.9330377154
666PhosphorylationKDEPNQSSQADRSNE
CCCCCCCCCCCCCCC		21.4428889911
671PhosphorylationQSSQADRSNEYNEGE
CCCCCCCCCCCCCCC		34.2621551504
674PhosphorylationQADRSNEYNEGEISK
CCCCCCCCCCCCCCC		23.8221440633
681UbiquitinationYNEGEISKGAENAT-
CCCCCCCCCCCCCC-		68.7323749301
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 YD444_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YD444_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 YD444_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SWC4_YEASTSWC4genetic
27708008
CDK1_YEASTCDC28genetic
27708008
TAF12_YEASTTAF12genetic
27708008
ERF3_YEASTSUP35genetic
27708008
TFB1_YEASTTFB1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
SYMC_YEASTMES1genetic
27708008
CDC12_YEASTCDC12genetic
27708008
MET30_YEASTMET30genetic
27708008
KTHY_YEASTCDC8genetic
27708008
CDC11_YEASTCDC11genetic
27708008
FIP1_YEASTFIP1genetic
27708008
SEC22_YEASTSEC22genetic
27708008
APC5_YEASTAPC5genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YD444_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-666, AND MASSSPECTROMETRY.

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