dbPTM

YN87_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	YN87_YEAST
UniProt AC	P53719
Protein Name	Uncharacterized protein YNR014W
Gene Name	YNR014W
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	212
Subcellular Localization
Protein Description
Protein Sequence	MSSTDIKPCAVNIPVSAHITFHYKSIADRSSSRSSSSSSCSSATSKACSPRGSSVGLPPALSTDNEIVETVLNVSAPVVADPTRPSLFKSNYTAASCLTSDPTSPSLLPSSRRNSVLPASDFHQCAHHKNFQRRASEPQLPSFDNRSSSEMKRSVSYAQHSMMFPISDQQEPQTSASPNDHSDPSCPCNRHHHRRNSVAVKFDKPLYERLET

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
25	Phosphorylation	HITFHYKSIADRSSS EEEEEECCHHCCCCC	18.82	28889911
30	Phosphorylation	YKSIADRSSSRSSSS ECCHHCCCCCCCCCC	32.96	26447709
31	Phosphorylation	KSIADRSSSRSSSSS CCHHCCCCCCCCCCC	30.57	26447709
32	Phosphorylation	SIADRSSSRSSSSSS CHHCCCCCCCCCCCC	37.11	28889911
41	Phosphorylation	SSSSSSCSSATSKAC CCCCCCCCHHCCCCC	25.59	28889911
49	Phosphorylation	SATSKACSPRGSSVG HHCCCCCCCCCCCCC	23.61	20377248
53	Phosphorylation	KACSPRGSSVGLPPA CCCCCCCCCCCCCCC	24.11	21440633
54	Phosphorylation	ACSPRGSSVGLPPAL CCCCCCCCCCCCCCC	24.03	20377248
62	Phosphorylation	VGLPPALSTDNEIVE CCCCCCCCCCCHHHH	35.50	22369663
63	Phosphorylation	GLPPALSTDNEIVET CCCCCCCCCCHHHHH	43.63	22369663
70	Phosphorylation	TDNEIVETVLNVSAP CCCHHHHHHHHCCCC	21.28	22369663
75	Phosphorylation	VETVLNVSAPVVADP HHHHHHCCCCEECCC	26.28	22369663
83	Phosphorylation	APVVADPTRPSLFKS CCEECCCCCHHHCCC	56.62	22369663
86	Phosphorylation	VADPTRPSLFKSNYT ECCCCCHHHCCCCCC	43.05	22369663
96	Phosphorylation	KSNYTAASCLTSDPT CCCCCCHHHHCCCCC	13.75	22369663
99	Phosphorylation	YTAASCLTSDPTSPS CCCHHHHCCCCCCHH	35.10	21440633
100	Phosphorylation	TAASCLTSDPTSPSL CCHHHHCCCCCCHHH	28.75	22369663
103	Phosphorylation	SCLTSDPTSPSLLPS HHHCCCCCCHHHCCC	59.25	22369663
104	Phosphorylation	CLTSDPTSPSLLPSS HHCCCCCCHHHCCCC	20.20	22369663
106	Phosphorylation	TSDPTSPSLLPSSRR CCCCCCHHHCCCCCC	42.16	21440633
110	Phosphorylation	TSPSLLPSSRRNSVL CCHHHCCCCCCCCCC	36.12	22369663
111	Phosphorylation	SPSLLPSSRRNSVLP CHHHCCCCCCCCCCC	33.06	22369663
115	Phosphorylation	LPSSRRNSVLPASDF CCCCCCCCCCCHHHH	24.18	22890988
136	Phosphorylation	KNFQRRASEPQLPSF HHHHHHCCCCCCCCC	48.26	22369663
142	Phosphorylation	ASEPQLPSFDNRSSS CCCCCCCCCCCCCCH	54.55	28132839
147	Phosphorylation	LPSFDNRSSSEMKRS CCCCCCCCCHHHHHH	44.46	19823750
148	Phosphorylation	PSFDNRSSSEMKRSV CCCCCCCCHHHHHHH	27.38	19823750
149	Phosphorylation	SFDNRSSSEMKRSVS CCCCCCCHHHHHHHH	42.85	19823750
154	Phosphorylation	SSSEMKRSVSYAQHS CCHHHHHHHHHHHHH	15.19	28889911
156	Phosphorylation	SEMKRSVSYAQHSMM HHHHHHHHHHHHHCE	18.92	21440633
157	Phosphorylation	EMKRSVSYAQHSMMF HHHHHHHHHHHHCEE	14.23	28889911
161	Phosphorylation	SVSYAQHSMMFPISD HHHHHHHHCEEECCC	10.40	30377154
185	Phosphorylation	PNDHSDPSCPCNRHH CCCCCCCCCCCCCCC	35.36	28889911
197	Phosphorylation	RHHHRRNSVAVKFDK CCCCCCCEEEEEECH	15.05	25752575

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 YN87_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of YN87_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 YN87_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
BMH2_YEAST	BMH2	physical	16554755
PBP1_YEAST	PBP1	physical	18719252

Drug and Disease Associations

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

Regulatory Network of YN87_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-75; SER-100; SER-104;SER-111; SER-136; SER-156 AND SER-197, AND MASS SPECTROMETRY.	18407956 [Abstract]
"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-136, AND MASSSPECTROMETRY.	17563356 [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-136, AND MASSSPECTROMETRY.	17287358 [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 SER-136, AND MASSSPECTROMETRY.	15665377 [Abstract]