dbPTM

PTH2_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTH2_YEAST
UniProt AC	P34222
Protein Name	Peptidyl-tRNA hydrolase 2
Gene Name	PTH2
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	208
Subcellular Localization	Cytoplasm.
Protein Description	The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis..
Protein Sequence	MEKMTVSSNYTIALWATFTAISFAVGYQLGTSNASSTKKSSATLLRSKEMKEGKLHNDTDEEESESEDESDEDEDIESTSLNDIPGEVRMALVIRQDLGMTKGKIAAQCCHAALSCFRHIATNPARASYNPIMTQRWLNAGQAKITLKCPDKFTMDELYAKAISLGVNAAVIHDAGRTQIAAGSATVLGLGPAPKAVLDQITGDLKLY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
41	Phosphorylation	ASSTKKSSATLLRSK CCCCCCHHCHHHHCH	33.87	23749301
59	Phosphorylation	EGKLHNDTDEEESES CCCCCCCCCHHHHCC	51.10	19795423
64	Phosphorylation	NDTDEEESESEDESD CCCCHHHHCCCCCCC	50.10	19795423
66	Phosphorylation	TDEEESESEDESDED CCHHHHCCCCCCCCC	60.68	19795423
70	Phosphorylation	ESESEDESDEDEDIE HHCCCCCCCCCCCHH	59.63	19795423
78	Phosphorylation	DEDEDIESTSLNDIP CCCCCHHHCCCCCCC	24.51	19795423
80	Phosphorylation	DEDIESTSLNDIPGE CCCHHHCCCCCCCHH	34.16	27214570
148	Ubiquitination	GQAKITLKCPDKFTM CCCEEEEECCCCCCH	34.76	22817900
152	Ubiquitination	ITLKCPDKFTMDELY EEEECCCCCCHHHHH	28.07	23749301
161	Ubiquitination	TMDELYAKAISLGVN CHHHHHHHHHHHCCC	32.47	-
206	Ubiquitination	DQITGDLKLY----- HHHCCCCCCC-----	50.94	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 PTH2_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PTH2_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 PTH2_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DSK2_YEAST	DSK2	physical	17082762
EIF3J_YEAST	HCR1	genetic	19061648
RPB1_YEAST	RPO21	genetic	19061648
UAF30_YEAST	UAF30	genetic	19061648
DSK2_YEAST	DSK2	physical	18719252
HSP71_YEAST	SSA1	physical	19536198
DLD1_YEAST	DLD1	genetic	20093466
RV167_YEAST	RVS167	genetic	20093466
PUS3_YEAST	DEG1	genetic	20093466
YGY5_YEAST	YGL235W	genetic	20093466
MPC1_YEAST	MPC1	genetic	20093466
PUS2_YEAST	PUS2	genetic	20093466
YG34_YEAST	YGR122W	genetic	20093466
PAM17_YEAST	PAM17	genetic	20093466
NKP2_YEAST	NKP2	genetic	20093466
YO029_YEAST	YOL029C	genetic	20093466
MNE1_YEAST	MNE1	genetic	20093466
PUR3_YEAST	ADE8	physical	22940862
UBI4P_YEAST	UBI4	physical	24709957
UBI4P_YEAST	UBI4	physical	17082762
DSK2_YEAST	DSK2	genetic	17082762
RAD23_YEAST	RAD23	genetic	17082762
THRC_YEAST	THR4	genetic	27708008
HMI1_YEAST	HMI1	genetic	27708008
MBA1_YEAST	MBA1	genetic	27708008
IMG2_YEAST	IMG2	genetic	27708008
RV167_YEAST	RVS167	genetic	27708008
PALF_YEAST	RIM8	genetic	27708008
MPC1_YEAST	MPC1	genetic	27708008
ASK10_YEAST	ASK10	genetic	27708008
ELP2_YEAST	ELP2	genetic	27708008
FMC1_YEAST	FMC1	genetic	27708008
CYP7_YEAST	CPR7	genetic	27708008
DOA1_YEAST	DOA1	genetic	27708008
PAM17_YEAST	PAM17	genetic	27708008
FRA1_YEAST	FRA1	genetic	27708008
ARV1_YEAST	ARV1	genetic	27708008
NKP2_YEAST	NKP2	genetic	27708008
MSS1_YEAST	MSS1	genetic	27708008
JNM1_YEAST	JNM1	genetic	27708008
KC12_YEAST	YCK2	genetic	27708008
CY1_YEAST	CYT1	genetic	27708008
SFL1_YEAST	SFL1	genetic	27708008
PRPD_YEAST	PDH1	genetic	27708008
VPS4_YEAST	VPS4	genetic	27708008
SGTA_HUMAN	SGTA	physical	27107014

Drug and Disease Associations

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

Regulatory Network of PTH2_YEAST

Related Literatures of Post-Translational Modification

Ubiquitylation
Reference	PubMed
"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-152, AND MASSSPECTROMETRY.	14557538 [Abstract]