APTH1_YEAST - dbPTM
APTH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID APTH1_YEAST
UniProt AC Q12354
Protein Name Acyl-protein thioesterase 1
Gene Name YLR118C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 227
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Hydrolyzes fatty acids from S-acylated cysteine residues in proteins with a strong preference for palmitoylated G-alpha proteins over other acyl substrates. Mediates the deacylation of G-alpha proteins such as GPA1 in vivo, but has weak or no activity toward palmitoylated Ras proteins. Has weak lysophospholipase activity in vitro; however such activity may not exist in vivo..
Protein Sequence MNGLRVAAKIQPARQTIIFLHGLGDTGSGWGFLAQYLQQRDPAAFQHTNFVFPNAPELHVTANGGALMPAWFDILEWDPSFSKVDSDGFMNSLNSIEKTVKQEIDKGIKPEQIIIGGFSQGAALALATSVTLPWKIGGIVALSGFCSIPGILKQHKNGINVKTPIFHGHGDMDPVVPIGLGIKAKQFYQDSCEIQNYEFKVYKGMAHSTVPDELEDLASFIKKSLSS
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 Orthologous
Protein Cluster
208PhosphorylationVYKGMAHSTVPDELE
EEECCCCCCCCHHHH		22.8922369663
209PhosphorylationYKGMAHSTVPDELED
EECCCCCCCCHHHHH		26.6222369663
219PhosphorylationDELEDLASFIKKSLS
HHHHHHHHHHHHHHC		34.5021440633
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 APTH1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of APTH1_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 APTH1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RIM1_YEASTRIM1genetic
20093466
MRH1_YEASTMRH1genetic
20093466
EAF1_YEASTEAF1genetic
20093466
BCS1_YEASTBCS1genetic
20093466
BGL2_YEASTBGL2genetic
20093466
YJ24_YEASTKCH1genetic
20093466
SAC1_YEASTSAC1genetic
20093466
PET10_YEASTPET10genetic
20093466
BCH1_YEASTBCH1genetic
20093466
JNM1_YEASTJNM1genetic
20093466
COQ2_YEASTCOQ2genetic
20093466
CY1_YEASTCYT1genetic
20093466
SGF11_YEASTSGF11genetic
20093466
RIM1_YEASTRIM1genetic
27708008
GPR1_YEASTGPR1genetic
27708008
PALF_YEASTRIM8genetic
27708008
YJ24_YEASTKCH1genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
PET10_YEASTPET10genetic
27708008
MSC1_YEASTMSC1genetic
27708008
COQ2_YEASTCOQ2genetic
27708008
CY1_YEASTCYT1genetic
27708008
SGF11_YEASTSGF11genetic
27708008
RU2A_YEASTLEA1genetic
27708008
EFHC2_HUMANEFHC2physical
27107014
BACD1_HUMANKCTD13physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of APTH1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-208, AND MASSSPECTROMETRY.

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