dbPTM

YB75_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	YB75_YEAST
UniProt AC	P38321
Protein Name	Uncharacterized protein YBR225W
Gene Name	YBR225W
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	900
Subcellular Localization
Protein Description
Protein Sequence	MGSNKEAKNIDSKNDRGLTSITSNKISNLKAHDNHTSSMITEHKNADKEKGKQEKESRNGTTQSSSSVESHSPQVSHHSDKLSSFDSPLHLPNFRLADDLFSNSSRRSSDSAASSSVSKLKSAQLSKIGLHHHHTSNNKHSHRSGTPTSEVKANYSPDPSAPRFIVSNMVGNGRGGGGLHGATSNVVKKLHSRKKWDWNTLPASDSSLLIKTVSGNHNLINICIDGEFKQIMYDPNHNELFNRMDLFLSFNMDSSPEDSLIFAKKRLRSYIDFLTKYLESRKYAFECYPFNIENIINIETEVKCFPSFDPLKDYSEIESLIQLWLAQSQKFLLQSNSFFFSSEVVEELIKRKPTTRQHSNPTISTTSNKISDPTLYIQQLDIEANSPRPVISDPLDEIDILLIRPLHKTLGGWQLAYDEPSLNIADFALDLSPWMIDSSDNDAQNKNASEIAPEYLTNLQNYLPRKGSRAKIVSDEQEVIELNSSNASEYMYDCMNRKFFTDDAKERISRNNFNQGVEEDPLNDQFASSRSLSLPSSGADAVKRKKSPTKATKKSGFVNFFKRKHSQLASTSHTTSPSVSPSISSSSSPKIQPQSHISSPPRTEKAPHVKSANQAHQNEWLENFFCRTLNNYKEIDLPTQFILPKEVKRSSNAQLQPEDEPPLSSPISSNSDNSFPNEGLDRAKSAAIYGKEYLKLRLPFASDTIPAVICPWVWTSLSYYKWKALLREIYRSIIPGGYALAIVPDLRISNTYYTGILGNADAEKANNSSEEFLTTKERDKTFDAMAIDAINKGLHIHPTKHLTRTFKDVGFTGIKSSVLSLKTGDFKTDMGFLNEFNSLDMWDYMLRRQLPDSSCPPKDTDPTTLFKRYVEEHIGKIDDNAGCFRTLYVVAQKPKLPYTK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
20	Phosphorylation	KNDRGLTSITSNKIS CCCCCCCHHHCCCCC	28.98	28889911
22	Phosphorylation	DRGLTSITSNKISNL CCCCCHHHCCCCCCC	26.47	22369663
23	Phosphorylation	RGLTSITSNKISNLK CCCCHHHCCCCCCCC	34.16	22369663
27	Phosphorylation	SITSNKISNLKAHDN HHHCCCCCCCCCCCC	37.41	27017623
36	Phosphorylation	LKAHDNHTSSMITEH CCCCCCCCHHHHHHC	28.84	27017623
37	Phosphorylation	KAHDNHTSSMITEHK CCCCCCCHHHHHHCC	15.45	27017623
61	Phosphorylation	EKESRNGTTQSSSSV CHHHCCCCCCCCHHC	25.80	29136822
62	Phosphorylation	KESRNGTTQSSSSVE HHHCCCCCCCCHHCC	28.05	21440633
64	Phosphorylation	SRNGTTQSSSSVESH HCCCCCCCCHHCCCC	30.05	29136822
65	Phosphorylation	RNGTTQSSSSVESHS CCCCCCCCHHCCCCC	19.47	21440633
66	Phosphorylation	NGTTQSSSSVESHSP CCCCCCCHHCCCCCC	43.58	21440633
67	Phosphorylation	GTTQSSSSVESHSPQ CCCCCCHHCCCCCCC	31.67	29136822
70	Phosphorylation	QSSSSVESHSPQVSH CCCHHCCCCCCCCCC	27.40	21551504
72	Phosphorylation	SSSVESHSPQVSHHS CHHCCCCCCCCCCCC	26.72	20377248
76	Phosphorylation	ESHSPQVSHHSDKLS CCCCCCCCCCCCCCC	15.38	20377248
79	Phosphorylation	SPQVSHHSDKLSSFD CCCCCCCCCCCCCCC	30.89	21551504
83	Phosphorylation	SHHSDKLSSFDSPLH CCCCCCCCCCCCCCC	34.40	22369663
84	Phosphorylation	HHSDKLSSFDSPLHL CCCCCCCCCCCCCCC	43.43	22369663
87	Phosphorylation	DKLSSFDSPLHLPNF CCCCCCCCCCCCCCC	27.61	22369663
102	Phosphorylation	RLADDLFSNSSRRSS HHHHHHCCCCCCCCC	43.00	28889911
104	Phosphorylation	ADDLFSNSSRRSSDS HHHHCCCCCCCCCCC	24.83	20377248
105	Phosphorylation	DDLFSNSSRRSSDSA HHHCCCCCCCCCCCC	35.64	22369663
108	Phosphorylation	FSNSSRRSSDSAASS CCCCCCCCCCCCCCH	37.07	21440633
109	Phosphorylation	SNSSRRSSDSAASSS CCCCCCCCCCCCCHH	33.50	21082442
111	Phosphorylation	SSRRSSDSAASSSVS CCCCCCCCCCCHHHH	27.90	21440633
116	Phosphorylation	SDSAASSSVSKLKSA CCCCCCHHHHHHHHH	28.10	19779198
118	Phosphorylation	SAASSSVSKLKSAQL CCCCHHHHHHHHHHH	33.93	19779198
144	Phosphorylation	NNKHSHRSGTPTSEV CCCCCCCCCCCCHHH	41.41	21126336
146	Phosphorylation	KHSHRSGTPTSEVKA CCCCCCCCCCHHHCC	25.33	25752575
152	Ubiquitination	GTPTSEVKANYSPDP CCCCHHHCCCCCCCC	27.19	23749301
156	Phosphorylation	SEVKANYSPDPSAPR HHHCCCCCCCCCCCC	23.72	22369663
188	Ubiquitination	GATSNVVKKLHSRKK CHHHHHHHHHHCCCC	45.39	17644757
189	Ubiquitination	ATSNVVKKLHSRKKW HHHHHHHHHHCCCCC	39.56	17644757
211	Ubiquitination	SDSSLLIKTVSGNHN CCCEEEEEEECCCCC	42.73	17644757
229	Ubiquitination	ICIDGEFKQIMYDPN EEECCCCEEEEECCC	34.31	17644757
354	Phosphorylation	ELIKRKPTTRQHSNP HHHHCCCCCCCCCCC	37.33	17287358
359	Phosphorylation	KPTTRQHSNPTISTT CCCCCCCCCCCEECC	35.85	22369663
362	Phosphorylation	TRQHSNPTISTTSNK CCCCCCCCEECCCCC	31.63	22369663
364	Phosphorylation	QHSNPTISTTSNKIS CCCCCCEECCCCCCC	28.27	22369663
365	Phosphorylation	HSNPTISTTSNKISD CCCCCEECCCCCCCC	30.32	22369663
366	Phosphorylation	SNPTISTTSNKISDP CCCCEECCCCCCCCC	24.42	22369663
367	Phosphorylation	NPTISTTSNKISDPT CCCEECCCCCCCCCE	35.89	22369663
446	Ubiquitination	SDNDAQNKNASEIAP CCCHHHCCCHHHHCH	41.64	17644757
466	Ubiquitination	LQNYLPRKGSRAKIV HHHHCCCCCCCCEEC	60.34	17644757
531	Phosphorylation	DQFASSRSLSLPSSG CCCCCCCCCCCCCCC	25.02	22369663
533	Phosphorylation	FASSRSLSLPSSGAD CCCCCCCCCCCCCHH	39.21	22369663
536	Phosphorylation	SRSLSLPSSGADAVK CCCCCCCCCCHHHHH	46.85	27017623
537	Phosphorylation	RSLSLPSSGADAVKR CCCCCCCCCHHHHHC	35.74	19779198
564	Ubiquitination	FVNFFKRKHSQLAST CCHHHHHCHHHHHCC	48.47	17644757
566	Phosphorylation	NFFKRKHSQLASTSH HHHHHCHHHHHCCCC	29.89	28889911
574	Phosphorylation	QLASTSHTTSPSVSP HHHCCCCCCCCCCCC	28.83	24961812
575	Phosphorylation	LASTSHTTSPSVSPS HHCCCCCCCCCCCCC	32.96	19779198
576	Phosphorylation	ASTSHTTSPSVSPSI HCCCCCCCCCCCCCC	19.14	21440633
578	Phosphorylation	TSHTTSPSVSPSISS CCCCCCCCCCCCCCC	34.69	19779198
580	Phosphorylation	HTTSPSVSPSISSSS CCCCCCCCCCCCCCC	19.78	21440633
582	Phosphorylation	TSPSVSPSISSSSSP CCCCCCCCCCCCCCC	27.83	21440633
584	Phosphorylation	PSVSPSISSSSSPKI CCCCCCCCCCCCCCC	28.62	21440633
585	Phosphorylation	SVSPSISSSSSPKIQ CCCCCCCCCCCCCCC	32.35	21440633
586	Phosphorylation	VSPSISSSSSPKIQP CCCCCCCCCCCCCCC	28.22	21440633
587	Phosphorylation	SPSISSSSSPKIQPQ CCCCCCCCCCCCCCC	53.24	21440633
588	Phosphorylation	PSISSSSSPKIQPQS CCCCCCCCCCCCCCC	31.96	21440633
590	Ubiquitination	ISSSSSPKIQPQSHI CCCCCCCCCCCCCCC	56.79	17644757
595	Phosphorylation	SPKIQPQSHISSPPR CCCCCCCCCCCCCCC	29.48	27717283
598	Phosphorylation	IQPQSHISSPPRTEK CCCCCCCCCCCCCCC	31.22	29136822
599	Phosphorylation	QPQSHISSPPRTEKA CCCCCCCCCCCCCCC	38.02	29136822
603	Phosphorylation	HISSPPRTEKAPHVK CCCCCCCCCCCCCCC	47.84	27717283
610	Ubiquitination	TEKAPHVKSANQAHQ CCCCCCCCCHHHHHH	40.59	17644757
651	Phosphorylation	PKEVKRSSNAQLQPE CHHHHCCCCCCCCCC	39.97	28889911
685	Phosphorylation	EGLDRAKSAAIYGKE CCHHHHHHHHHHCCC	23.19	23749301
751	Phosphorylation	PDLRISNTYYTGILG CCCEEECCEECCCCC	15.89	19779198
752	Phosphorylation	DLRISNTYYTGILGN CCEEECCEECCCCCC	11.86	19779198
753	Phosphorylation	LRISNTYYTGILGNA CEEECCEECCCCCCC	9.10	19779198
768	Phosphorylation	DAEKANNSSEEFLTT CHHHHCCCCHHHCCH	38.64	21126336
769	Phosphorylation	AEKANNSSEEFLTTK HHHHCCCCHHHCCHH	43.18	25752575
893	Ubiquitination	TLYVVAQKPKLPYTK EEEHEECCCCCCCCC	34.09	17644757
895	Ubiquitination	YVVAQKPKLPYTK-- EHEECCCCCCCCC--	69.95	17644757

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 YB75_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of YB75_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 YB75_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDC25_YEAST	CDC25	physical	11805826
MDS3_YEAST	MDS3	physical	11805826
MDS3_YEAST	MDS3	physical	16554755
CDC25_YEAST	CDC25	physical	16554755
THRC_YEAST	THR4	genetic	27708008
ELM1_YEAST	ELM1	genetic	27708008
SAC1_YEAST	SAC1	genetic	27708008
EIF3J_YEAST	HCR1	genetic	27708008
SEI1_YEAST	FLD1	genetic	27708008
NGL2_YEAST	NGL2	genetic	27708008
YND5_YEAST	YNL035C	genetic	27708008
MTQ1_YEAST	MTQ1	genetic	27708008
YO073_YEAST	DSC2	genetic	27708008
PP2B1_YEAST	CNA1	physical	24930733
PP2B2_YEAST	CMP2	physical	24930733

Drug and Disease Associations

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

Regulatory Network of YB75_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-109; SER-156; SER-651AND SER-769, 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-359, AND MASSSPECTROMETRY.	17287358 [Abstract]