dbPTM

YP191_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	YP191_YEAST
UniProt AC	Q08930
Protein Name	Ubiquitin carboxyl-terminal hydrolase MIY1 {ECO:0000303\|PubMed:27292798}
Gene Name	YPL191C
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	360
Subcellular Localization	Cytoplasm .
Protein Description	Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins. Has endodeubiquitinase activity..
Protein Sequence	MDLSFTTKSVKINGQNHRILLQNENGPCALLALANILILSPDHTRFSNELIRLVNKGSQISLKELIEVLADIALQVTDKPSTDISELLSLLPRLHEGLNINPEFNGSFENTKEMSIFRLFNVDVVHGWVINSFINENIDEKLSHYSYESAQRILTQAADINCGISQDENSDEVLRDAMHLGLFLNESPTQLTAFGLLRLREKLLHNKFSILFRNDHFSTLFKYEDRLYTLVTDFGYKNCKDIVWQSLDSVDGSCDAFFAGNFSAAEVNGQQLSTDIERDFGTGNLLLEEIQQIENDKELAKQLQEQEQERVTKFEAKRKIHSHKKNSEIHAPVKKDKFKRRSSLLNAKASEKEKSECVVM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
56	Ubiquitination	ELIRLVNKGSQISLK HHHHHHHCCCCCCHH	53.08	23749301
313	Acetylation	QEQERVTKFEAKRKI HHHHHHHHHHHHHHH	38.05	25381059
313	Ubiquitination	QEQERVTKFEAKRKI HHHHHHHHHHHHHHH	38.05	23749301
327	Phosphorylation	IHSHKKNSEIHAPVK HHHCCCCCCCCCCCC	46.97	28889911
342	Phosphorylation	KDKFKRRSSLLNAKA CCHHHHHHHHHHCCC	29.39	28889911
343	Phosphorylation	DKFKRRSSLLNAKAS CHHHHHHHHHHCCCC	34.76	17563356
348	Ubiquitination	RSSLLNAKASEKEKS HHHHHHCCCCHHHHH	51.91	23749301

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 YP191_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of YP191_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 YP191_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PUS5_YEAST	PUS5	genetic	27708008
DEP1_YEAST	DEP1	genetic	27708008
YPQ3_YEAST	RTC2	genetic	27708008
CHK1_YEAST	CHK1	genetic	27708008
PEX19_YEAST	PEX19	genetic	27708008
VPS41_YEAST	VPS41	genetic	27708008
ARO1_YEAST	ARO1	genetic	27708008
PEX5_YEAST	PEX5	genetic	27708008
GNTK_YEAST	YDR248C	genetic	27708008
CP56_YEAST	DIT2	genetic	27708008
ODPA_YEAST	PDA1	genetic	27708008
YFF1_YEAST	YFL051C	genetic	27708008
YG036_YEAST	YGL036W	genetic	27708008
GTR2_YEAST	GTR2	genetic	27708008
HGH1_YEAST	HGH1	genetic	27708008
ELP2_YEAST	ELP2	genetic	27708008
OPI1_YEAST	OPI1	genetic	27708008
SDS3_YEAST	SDS3	genetic	27708008
FYV10_YEAST	FYV10	genetic	27708008
ASF1_YEAST	ASF1	genetic	27708008
LAC1_YEAST	LAC1	genetic	27708008
NU133_YEAST	NUP133	genetic	27708008
DPH6_YEAST	DPH6	genetic	27708008
PEX13_YEAST	PEX13	genetic	27708008
EIF3J_YEAST	HCR1	genetic	27708008
NEJ1_YEAST	NEJ1	genetic	27708008
TSR2_YEAST	TSR2	genetic	27708008
MSC1_YEAST	MSC1	genetic	27708008
IMP2_YEAST	IMP2	genetic	27708008
RCO1_YEAST	RCO1	genetic	27708008
SIW14_YEAST	SIW14	genetic	27708008
RRP6_YEAST	RRP6	genetic	27708008
AZF1_YEAST	AZF1	genetic	27708008

Drug and Disease Associations

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

Regulatory Network of YP191_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-343, AND MASSSPECTROMETRY.	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-343, AND MASSSPECTROMETRY.	17563356 [Abstract]