dbPTM

PPN1_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PPN1_YEAST
UniProt AC	Q04119
Protein Name	Endopolyphosphatase {ECO:0000303\|PubMed:11447286}
Gene Name	PPN1 {ECO:0000303\|PubMed:11447286}
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	674
Subcellular Localization	Vacuole membrane Single-pass type II membrane protein . Cytoplasm . The cytoplasmic form appears in the cytosol during the transition of cells from stationary growth phase to new budding on glucose addition and phosphate excess.
Protein Description	Catalyzes the hydrolysis of inorganic polyphosphate (polyP) chains of many hundreds of phosphate residues into shorter lengths both by cleaving phosphate from the chain end and by fragmenting long-chain polymers into shorter ones. The limited digestion products are 1 and 3 P(i) residues. [PubMed: 11102525]
Protein Sequence	MVVVGKSEVRNVSMSRPKKKSLIAILSTCVLFFLVFIIGAKFQYVSVFSKFLDDRGDNESLQLLNDIEFTRLGLTPREPVIIKDVKTGKERKLHGRFLHITDIHPDPYYVEGSSIDAVCHTGKPSKKKDVAPKFGKAMSGCDSPVILMEETLRWIKENLRDKIDFVIWTGDNIRHDNDRKHPRTEAQIFDMNNIVADKMTELFSAGNEEDPRDFDVSVIPSLGNNDVFPHNMFALGPTLQTREYYRIWKNFVPQQQQRTFDRSASFLTEVIPGKLAVLSINTLYLFKANPLVDNCNSKKEPGYQLLLWFGYVLEELRSRGMKVWLSGHVPPIAKNFDQSCYDKFTLWTHEYRDIIIGGLYGHMNIDHFIPTDGKKARKSLLKAMEQSTRVQQGEDSNEEDEETELNRILDHAMAAKEVFLMGAKPSNKEAYMNTVRDTYYRKVWNKLERVDEKNVENEKKKKEKKDKKKKKPITRKELIERYSIVNIGGSVIPTFNPSFRIWEYNITDIVNDSNFAVSEYKPWDEFFESLNKIMEDSLLEDEMDSSNIEVGINREKMGEKKNKKKKKNDKTMPIEMPDKYELGPAYVPQLFTPTRFVQFYADLEKINQELHNSFVESKDIFRYEIEYTSDEKPYSMDSLTVGSYLDLAGRLYENKPAWEKYVEWSFASSGYKDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Ubiquitination	--MVVVGKSEVRNVS --CEEECCHHCCCCC	31.65	23749301
44	Phosphorylation	IIGAKFQYVSVFSKF HHHHHHHHHHHHHHH	9.60	27717283
46	Phosphorylation	GAKFQYVSVFSKFLD HHHHHHHHHHHHHHC	16.71	27717283
49	Phosphorylation	FQYVSVFSKFLDDRG HHHHHHHHHHHCCCC	21.97	27717283
58	N-linked_Glycosylation	FLDDRGDNESLQLLN HHCCCCCCHHHHHHH	43.51	-
123	Ubiquitination	DAVCHTGKPSKKKDV CEEEECCCCCCCCCC	47.47	17644757
126	Ubiquitination	CHTGKPSKKKDVAPK EECCCCCCCCCCCHH	72.82	17644757
127	Ubiquitination	HTGKPSKKKDVAPKF ECCCCCCCCCCCHHC	59.55	17644757
139	Phosphorylation	PKFGKAMSGCDSPVI HHCHHHHCCCCCCCH	40.92	27017623
143	Phosphorylation	KAMSGCDSPVILMEE HHHCCCCCCCHHHHH	25.74	27017623
151	Phosphorylation	PVILMEETLRWIKEN CCHHHHHHHHHHHHH	14.33	24930733
282	Phosphorylation	LAVLSINTLYLFKAN EEEEEECCEEEEECC	18.34	28889911
416	Ubiquitination	LDHAMAAKEVFLMGA HHHHHHHHHHHHCCC	44.89	17644757
505	N-linked_Glycosylation	SFRIWEYNITDIVND CCCEEEEEEEEECCC	21.11	-
511	N-linked_Glycosylation	YNITDIVNDSNFAVS EEEEEECCCCCCCCC	47.53	-
571	Phosphorylation	KKKKNDKTMPIEMPD CCCCCCCCCCCCCCC	30.92	27017623

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
-	K	Ubiquitination	E3 ubiquitin ligase	RSP5	P39940	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	TUL1	P36096	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
6	K	ubiquitylation		11566881
Other cytoplasmic Lys residues than Lys-6 may also be ubiquitinated.

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 PPN1_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GPR1_YEAST	GPR1	genetic	27708008
UME6_YEAST	UME6	genetic	27708008
MRM2_YEAST	MRM2	genetic	27708008
YNV7_YEAST	YNL217W	genetic	28302909

Drug and Disease Associations

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

Regulatory Network of PPN1_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 THR-282, AND MASSSPECTROMETRY.	18407956 [Abstract]

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