PRTD_YEAST - dbPTM
PRTD_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRTD_YEAST
UniProt AC P25375
Protein Name Saccharolysin
Gene Name PRD1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 712
Subcellular Localization Cytoplasm.
Protein Description Could be involved in late stage of protein degradation..
Protein Sequence MRLLLCKNWFASPVISPLLYTRSLYSMANTTSFPIAPQAPPNWSFTPSDISGKTNEIINNSNNFYDSMSKVESPSVSNFVEPFMKFENELGPIINQLTFLQHVSSDKEIRDASVNSSMKLDELNIDLSLRHDIFLQFARVWQDVQSKADSVERETFKYVEKSYKDYIHSGLELDEGNRLKIKEIKKKISVNSINFSKNLGEQKEYITFTKEQLEGVPDSILTQFETIKSDKDSNETLYKVTFKYPDIFPVMKLASSAQTRKQAFLADQNKVPENEAILLDTLKLRDELASLLGYDTYANYNLYDKMAEDSTTVMNFLNDLKDKLIPLGRKELQVLQDMKAEDVKKLNQGADPNYYIWDHRYYDNKYLLENFNVDLEKISEYFPLEATITGMLEIYETLFNLKFIETKDSQNKSVWHDDVKQIAVWNMDDPKSPNFVGWIYFDLHPRDGKYGHAANFGLSSSFMIDDTTRSYPVTALVCNFSKSTKDKPSLLKHNEIVTFFHELGHGIHDLVGQNKESRFNGPGSVPWDFVEAPSQMLEFWTWNKNELINLSSHYKTGEKIPESLINSLIKTKHVNGALFTLRQLHFGLFDMKVHTCKDLQNLSICDTWNQLRQDISLISNGGTLSKGYDSFGHIMSDSYSAGYYGYLWAEVFATDMYHTKFAKDPLNAKNGIQYRDIVLARGGLYDINDNLKEFLGREPSKDAFLKELGLQN
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
73PhosphorylationDSMSKVESPSVSNFV
HHHHCCCCCCHHHHC		26.0122369663
75PhosphorylationMSKVESPSVSNFVEP
HHCCCCCCHHHHCHH		47.6719795423
77PhosphorylationKVESPSVSNFVEPFM
CCCCCCHHHHCHHHH		28.9629688323
189PhosphorylationKEIKKKISVNSINFS
HHHHHHEEECEEECC		24.9121126336
203AcetylationSKNLGEQKEYITFTK
CCCCCCCCEEEEEEH		48.4624489116
203SuccinylationSKNLGEQKEYITFTK
CCCCCCCCEEEEEEH		48.4623954790
219PhosphorylationQLEGVPDSILTQFET
HHCCCCHHHHHHHHE		17.2719823750
222PhosphorylationGVPDSILTQFETIKS
CCCHHHHHHHHEECC		29.5519795423
226PhosphorylationSILTQFETIKSDKDS
HHHHHHHEECCCCCC		34.6919823750
259PhosphorylationKLASSAQTRKQAFLA
HHHCCHHHHHHHHHC		39.2827017623
551PhosphorylationKNELINLSSHYKTGE
HHHHEECCCCCCCCC		15.5822369663
552PhosphorylationNELINLSSHYKTGEK
HHHEECCCCCCCCCC		33.7222369663
554PhosphorylationLINLSSHYKTGEKIP
HEECCCCCCCCCCCC		16.5222369663
570AcetylationSLINSLIKTKHVNGA
HHHHHHHHHCCCCCH		57.7324489116
616PhosphorylationNQLRQDISLISNGGT
HHHHHHHEEECCCCC		28.1322369663
619PhosphorylationRQDISLISNGGTLSK
HHHHEEECCCCCCCC		34.4122369663
623PhosphorylationSLISNGGTLSKGYDS
EEECCCCCCCCCCCC		29.2922369663
625PhosphorylationISNGGTLSKGYDSFG
ECCCCCCCCCCCCCC		24.7122369663
685PhosphorylationVLARGGLYDINDNLK
EEECCCEEECCCCHH		20.3227214570
700PhosphorylationEFLGREPSKDAFLKE
HHHCCCCCHHHHHHH		38.1121440633
706AcetylationPSKDAFLKELGLQN-
CCHHHHHHHHCCCC-		44.4324489116
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 PRTD_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRTD_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 PRTD_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAS5_YEASTYDJ1physical
19056735
CIP1_HUMANCCNB1IP1physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRTD_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-73 AND SER-75, AND MASSSPECTROMETRY.
"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-73, AND MASSSPECTROMETRY.

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