dbPTM

YL177_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	YL177_YEAST
UniProt AC	Q06251
Protein Name	Uncharacterized protein YLR177W
Gene Name	YLR177W
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	628
Subcellular Localization	Cytoplasm .
Protein Description
Protein Sequence	MELPSINSTTSISDNQELRNYYDKLLFKNNSGKSLADLPGKMADFNDNSAAAHPRSRVDFINGYIGFREDKQSLLGQKNTKRASFSAFADEGRKQSEMSINGKSPNLSLFSFEFNGTPTQDRKPYKQDYLNVMNTSPNNILSPLNNSSQKYYPQKQQQQQQQQQQQQQQSIFDPGRRSSYISDALIHGNAATQQPQYSQPVYINNNPSLQVPYTAPSEYTQQQQYSSPFNARRNTQPVLNLHPAAAPTNDAGLAVVDGKNLTSSKELHDLYLDCGSNYFASDKVYKFIDSIKGTLRGDNVSASSSRIIEFLDFLKNCNLNYNPQSDAFISTAVSNASSTGAAKSKNSTSMHLHYKPLVLVSLKNGKLELLSKPQTATLILKRGDLVIIDGDRGKDLVLVVEPVVDINLALFINFLKKKIHFDSLITNSQQHFPNDQFIKTLVDTTNGKPVAHELNPKLYDIIELTQLIIPSKQVLRFATPWESSTNLHNKFQDELKALHIAQLKLRSLNNNNSGGGLNIKILNAEFQFDRKKLTFYYICQERNDFRDLIKELFKFYKTRIWLCAIPNNLSIDSKFYDSNKFEWEMYQDMMSHYSMDNTGIVVAPELNRLKLDDFQIGVYMELVKVLFG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MELPSINS -------CCCCCCCC	12.31	22814378
5	Phosphorylation	---MELPSINSTTSI ---CCCCCCCCCCCC	47.21	30377154
8	Phosphorylation	MELPSINSTTSISDN CCCCCCCCCCCCCCC	31.24	24961812
9	Phosphorylation	ELPSINSTTSISDNQ CCCCCCCCCCCCCCH	21.78	21551504
10	Phosphorylation	LPSINSTTSISDNQE CCCCCCCCCCCCCHH	24.71	21551504
11	Phosphorylation	PSINSTTSISDNQEL CCCCCCCCCCCCHHH	21.86	28889911
13	Phosphorylation	INSTTSISDNQELRN CCCCCCCCCCHHHHH	30.21	24961812
21	Phosphorylation	DNQELRNYYDKLLFK CCHHHHHHHHHHHEE	13.45	21551504
31	Phosphorylation	KLLFKNNSGKSLADL HHHEECCCCCCHHHC	57.92	21082442
34	Phosphorylation	FKNNSGKSLADLPGK EECCCCCCHHHCCCC	32.11	22369663
84	Phosphorylation	QKNTKRASFSAFADE CCCCCCCCHHHHCCC	24.62	22369663
86	Phosphorylation	NTKRASFSAFADEGR CCCCCCHHHHCCCCC	21.71	22369663
129	Phosphorylation	RKPYKQDYLNVMNTS CCCCCCCHHHHCCCC	9.55	27017623
135	Phosphorylation	DYLNVMNTSPNNILS CHHHHCCCCCCCCCC	27.71	22369663
136	Phosphorylation	YLNVMNTSPNNILSP HHHHCCCCCCCCCCC	22.18	22369663
235	Phosphorylation	PFNARRNTQPVLNLH CCCCCCCCCCCEEEC	32.22	22369663
248	Phosphorylation	LHPAAAPTNDAGLAV ECCCCCCCCCCCEEE	40.79	22890988

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 YL177_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of YL177_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 YL177_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BMH2_YEAST	BMH2	physical	18719252
BMH1_YEAST	BMH1	physical	18719252
NAB2_YEAST	NAB2	physical	18719252
NHP10_YEAST	NHP10	genetic	27708008
TPS2_YEAST	TPS2	genetic	27708008
ACL4_YEAST	YDR161W	genetic	27708008
GNTK_YEAST	YDR248C	genetic	27708008
RLA4_YEAST	RPP2B	genetic	27708008
FYV10_YEAST	FYV10	genetic	27708008
ALN_YEAST	DAL1	genetic	27708008
MNN11_YEAST	MNN11	genetic	27708008
1433E_HUMAN	YWHAE	physical	27107014
RBMX_HUMAN	RBMX	physical	27107014

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of YL177_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-11; SER-31; SER-34;SER-84; SER-136 AND THR-235, AND MASS SPECTROMETRY.	18407956 [Abstract]
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-34, AND MASSSPECTROMETRY.	17287358 [Abstract]
"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 THR-235, AND MASSSPECTROMETRY.	17330950 [Abstract]
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-235, AND MASSSPECTROMETRY.	15665377 [Abstract]