COS3_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: COS3_YEAST
• UniProt AC: P0CX13
• Protein Name: Protein COS3
• Gene Name: COS3
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 379
• Subcellular Localization: Membrane; Multi-pass membrane protein.
• Protein Sequence: MKENELKNEKSVDVLSFKQLESQKIVLPQDLFRSSFTWFCYEIYKSLAFRIWMLLWLPLSVWWKLSNNCIYPLIVSLLVLFLGPIFVLVICGLSRKRSLSKQLIQFCKEITENTPSSDPHDWEVVAANLNSYLYENNVWNTKYFFFNAMVCQEAFRTTLLEPFSLKKDKAAKVKSFKDSVPYIEEALGVYFTEVEKQWKLFNTEKSWSPVGLEDAKLPKEAYRFKLTWFLKRISNIFMLIPFLNFLCCIYVSRGMCLLLRTLYLGWILFMLVQGFQNIRVLIMSMEHKMQFLSTIINEQESGANGWDEIARKMNRYLFEKKAWKNEEFFFDGIDCEWFFNHFFYRVLSAKKSMWPLPLNVELWPYIKEAQLSRSEVLLV

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
7	Ubiquitination	-MKENELKNEKSVDV -CCHHHCCCCCCCCE	57.81	24961812
10	Ubiquitination	ENELKNEKSVDVLSF HHHCCCCCCCCEEEH	66.24	23749301
11	Phosphorylation	NELKNEKSVDVLSFK HHCCCCCCCCEEEHH	19.85	22890988
16	Phosphorylation	EKSVDVLSFKQLESQ CCCCCEEEHHHHHHC	30.19	22369663
18	Ubiquitination	SVDVLSFKQLESQKI CCCEEEHHHHHHCCE	51.07	23749301
203	Phosphorylation	KQWKLFNTEKSWSPV HHHHCCCCCCCCCCC	37.14	28889911
205	Ubiquitination	WKLFNTEKSWSPVGL HHCCCCCCCCCCCCH	56.01	23749301
216	Ubiquitination	PVGLEDAKLPKEAYR CCCHHCCCCCHHHHH	77.10	23749301

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

Oops, there are no upstream regulatory protein records of COS3_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of COS3_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 COS3_YEAST !!

Protein-Protein Interaction

Oops, there are no PPI records of COS3_YEAST !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Ubiquitylation

"A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery.";
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-18 AND LYS-205, AND MASSSPECTROMETRY.
PubMed: 14557538