YP260_YEAST - dbPTM
YP260_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YP260_YEAST
UniProt AC Q08977
Protein Name UPF0662 protein YPL260W
Gene Name YPL260W
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 551
Subcellular Localization Cytoplasm . Nucleus .
Protein Description
Protein Sequence MFASAGQQHPQIVPKEEESILNYLLEVRSSLAKLKQNRTQYLNSKDVQTTYQHVLTKVRELDDIRKNSHETPAKSAATLIHSTELHNRVDSVLDDVFQLLSLCFLTVGLKNSAPATYASLSTVESLLEHLNESNVFTHHDLSPIKERLEEISKIVEQKNSSPAYDEDGNDDRLREIDNERKKNKIEEDLLLRAKLKHCKDEYDILEGKLEEIDPSLSTVMEKLFRIRRGLLSLVASAKKTMSKSDINTNSLLQEQNDLQTNNESLTDDKHLVSQEYVHEKLSVLKNELSELESNRDDSGKFKSLESHQVAEKGQSVLNGLLDDCHDLVNDLSHQKNGGLTLDPYLQPIYEQLIDIKTTLENLMITRRWTLRETDLFSYQKKLNEIDNKRINGKFPTKSQDSKGQSILLYLLRRCYAIIYKLLESSEPVSEALQPIHNQLSTVRRCLLELKRMGGVNNERELYPYQMKLASLDNLRTEGIFYDSDGNIPEGQGILNALLAECFDILHELKVEAEEKAQNSTSSDGSDDDDNGESGIDSNSNDSEPESEYQQE
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
45AcetylationRTQYLNSKDVQTTYQ
HHHHCCCHHHHHHHH		61.9324489116
57AcetylationTYQHVLTKVRELDDI
HHHHHHHHHHHHHHH		34.8224489116
74AcetylationNSHETPAKSAATLIH
CCCCCCCHHHHHHHH		41.6624489116
153AcetylationERLEEISKIVEQKNS
HHHHHHHHHHHHHCC		57.3324489116
184AcetylationDNERKKNKIEEDLLL
HHHHHHCHHHHHHHH		61.4424489116
280AcetylationSQEYVHEKLSVLKNE
CHHHHHHHHHHHHHH		31.0524489116
285AcetylationHEKLSVLKNELSELE
HHHHHHHHHHHHHHH		46.3424489116
300AcetylationSNRDDSGKFKSLESH
HCCCCCCCCCCHHHH		54.2824489116
380AcetylationTDLFSYQKKLNEIDN
HCHHHHHHHHHHHCC		51.5024489116
402AcetylationPTKSQDSKGQSILLY
CCCCCCCHHHHHHHH		70.0724489116
467AcetylationELYPYQMKLASLDNL
CHHCCHHHHHHHCCC		25.9424489116
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 YP260_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YP260_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 YP260_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NDC80_YEASTNDC80physical
10688190
RTK1_YEASTRTK1physical
18719252
GPR1_YEASTGPR1genetic
27708008
ILM1_YEASTILM1genetic
27708008
ENV10_YEASTENV10genetic
27708008
SIC1_YEASTSIC1genetic
27708008
BUD21_YEASTBUD21genetic
27708008
SIN3_YEASTSIN3genetic
29674565
RS16A_YEASTRPS16Bgenetic
29674565
RS16B_YEASTRPS16Bgenetic
29674565
YOR1_YEASTYOR1genetic
29674565
RPA34_YEASTRPA34genetic
29674565
YJ9I_YEASTYJR141Wgenetic
29674565
ERG6_YEASTERG6genetic
29674565
CTF18_YEASTCTF18genetic
29674565
UTP15_YEASTUTP15genetic
29674565
BUB3_YEASTBUB3genetic
29674565
CHL1_YEASTCHL1genetic
29674565
KAR3_YEASTKAR3genetic
29674565
DBF4_YEASTDBF4genetic
29674565
GUP1_YEASTGUP1genetic
29674565
FABG_YEASTOAR1genetic
29674565
NUF2_YEASTNUF2genetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YP260_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-273 AND SER-470, ANDMASS SPECTROMETRY.
"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-161, AND MASSSPECTROMETRY.

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