YG37_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: YG37_YEAST
• UniProt AC: P53275
• Protein Name: Uncharacterized protein YGR127W
• Gene Name: YGR127W
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 312
• Protein Sequence: MCILMATRAHPDYELILISNRDEFLARKTHATCWHNNDFILSPYDLAKTSAEKQIFGTWSGINKEGKLATILNLKLDNEQNNTKSRSRGLLPFIFLSIHKADFEDWDNYKKFEGHYDGLKSTGDFNFFYGDVIKKQYKVIDSLGRTFDVLSSTCRKDLDSYMVVSNGKFYDSSSIPGQAWEKVKVARDSLENLVLENIESDEEKIISSCFQLASKSSLPSTISNPDVLQMVDPNVTMNTIYVPPLRRPPRDDLGASIPDGDYYGTRSQIVLLVSKDSTRVTFIERVLYSSDEDVRKYSVTSPKEEKRFKFKL

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
85	Phosphorylation	NEQNNTKSRSRGLLP CCCCCCHHCCCCHHH	33.19	27017623
87	Phosphorylation	QNNTKSRSRGLLPFI CCCCHHCCCCHHHHH	37.48	28152593
298	Phosphorylation	DEDVRKYSVTSPKEE CCCHHHHCCCCCCHH	23.19	22369663
300	Phosphorylation	DVRKYSVTSPKEEKR CHHHHCCCCCCHHHC	33.11	22369663
301	Phosphorylation	VRKYSVTSPKEEKRF HHHHCCCCCCHHHCC	31.64	22369663

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of YG37_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of YG37_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of YG37_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NKP2_YEAST	NKP2	genetic	20093466
UME6_YEAST	UME6	genetic	27708008

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-301, AND MASSSPECTROMETRY.
PubMed: 18407956

"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-301, AND MASSSPECTROMETRY.
PubMed: 17563356

"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-301, AND MASSSPECTROMETRY.
PubMed: 17287358