PEP5_YEAST - dbPTM
PEP5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PEP5_YEAST
UniProt AC P12868
Protein Name E3 ubiquitin-protein ligase PEP5 {ECO:0000305|PubMed:22570702}
Gene Name PEP5 {ECO:0000303|PubMed:3062374}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1029
Subcellular Localization Vacuole membrane
Peripheral membrane protein
Cytoplasmic side .
Protein Description Required for vacuolar biogenesis and for trafficking of hydrolase precursors to the vacuole. Mediates transport at the vacuolar membrane where it may be responsible for tethering transport vesicles on the target membranes. It is required for gluconeogenic growth of yeast. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion. [PubMed: 3062374]
Protein Sequence MSLSSWRQFQLFENIPIRDPNFGGDSLLYSDPTLCAATIVDPQTLIIAVNSNIIKVVKLNQSQVIHEFQSFPHDFQITFLKVINGEFLVALAESIGKPSLIRVYKLEKLPNREQLYHSQVELKNGNNTYPISVVSISNDLSCIVVGFINGKIILIRGDISRDRGSQQRIIYEDPSKEPITALFLNNDATACFAATTSRILLFNTTGRNRGRPSLVLNSKNGLDLNCGSFNPATNEFICCLSNFIEFFSSSGKKHQFAFDLSLRKRIFCVDKDHILIVTEETGVPTTSISVNELSPTIINRIFIIDAKNKIISLNFVVSSAIIDIFSTSQSGKNITYLLTSEGVMHRITPKSLENQINIIIQKELYPFALQLAKQHSLSPLDVQEIHKKYGDYLFKKGLRKEATDQYIQCLDVVETSEIISKFGVKEVPDPESMRNLADYLWSLIKNSISQRDHVTLLLIVLIKLKDVEGIDTFIQHFDRKGIWNEGVVMDDMDDVTFFYSDNDFFDLDLILELMKESDFKRLSYRLAKKYSKDSLIIVDILLNLLHNPVKAIKYIKSLPIDETLRCLVTYSKKLLEESPNETNALLIEVFTGKFKPSTFEVDLDRRDTTGDFSENIRTVFYSYKTFFNYMNSNGTSDAMSESSEASHEHEEPTYHPPKPSIVFSSFVTKPFEFVVFLEACLACYQQYEGFDEDRQVILTTLYDLYLNLAQNDVPERIDDWRSRATGVLRESNKLVYSAASNNTSKRVDNSIMLLISHMDQSSASAKDKTKIDIASFANDNPEMDLLSTFRAMTLNEEPSTCLKFLEKYGTEEPKLLQVALSYFVSNKLIFKEMGGNEVLKEKVLRPIIEGERMPLLDIIKALSRTNVAHFGLIQDIIIDHVKTEDTEIKRNEKLIESYDKELKEKNKKLKNTINSDQPLHVPLKNQTCFMCRLTLDIPVVFFKCGHIYHQHCLNEEEDTLESERKLFKCPKCLVDLETSNKLFEAQHEVVEKNDLLNFALNSEEGSRDRFKVITEFLGRGAISYSDITI
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
294PhosphorylationSISVNELSPTIINRI
CEEHHHCCHHHEEEE		17.5127214570
312PhosphorylationDAKNKIISLNFVVSS
ECCCCEEEEEEEEEE		22.2719823750
318PhosphorylationISLNFVVSSAIIDIF
EEEEEEEEEHHHHHH		14.5719823750
319PhosphorylationSLNFVVSSAIIDIFS
EEEEEEEEHHHHHHC		16.3319823750
326PhosphorylationSAIIDIFSTSQSGKN
EHHHHHHCCCCCCCC		27.7319823750
327PhosphorylationAIIDIFSTSQSGKNI
HHHHHHCCCCCCCCE		21.7519823750
328PhosphorylationIIDIFSTSQSGKNIT
HHHHHCCCCCCCCEE		22.5819823750
330PhosphorylationDIFSTSQSGKNITYL
HHHCCCCCCCCEEEE		52.0519823750
608PhosphorylationVDLDRRDTTGDFSEN
EECCCCCCCCCCCHH		30.7617330950
609PhosphorylationDLDRRDTTGDFSENI
ECCCCCCCCCCCHHH		38.7625752575
900AcetylationKLIESYDKELKEKNK
HHHHHHHHHHHHHHH		57.6324489116
1011UbiquitinationEGSRDRFKVITEFLG
CCCHHHHHHHHHHHC		33.3524961812
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 PEP5_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PEP5_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 PEP5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VPS41_YEASTVPS41physical
10944212
VAM6_YEASTVAM6physical
10944212
VPS16_YEASTVPS16physical
10944212
PEP3_YEASTPEP3physical
10944212
VPS33_YEASTVPS33physical
10944212
VPS16_YEASTVPS16physical
9362071
PEP3_YEASTPEP3physical
9362071
VPS33_YEASTVPS33physical
9362071
PEP3_YEASTPEP3physical
10978279
PEP5_YEASTPEP5physical
10978279
PEP7_YEASTPEP7physical
10978279
VAM6_YEASTVAM6physical
11062257
PEP7_YEASTPEP7genetic
11422941
VPS21_YEASTVPS21genetic
11422941
VPS45_YEASTVPS45genetic
11422941
VPS8_YEASTVPS8genetic
9475722
PEP3_YEASTPEP3physical
16429126
VAM6_YEASTVAM6physical
16429126
VPS16_YEASTVPS16physical
16429126
VPS33_YEASTVPS33physical
16429126
VPS16_YEASTVPS16physical
21325627
PEP3_YEASTPEP3physical
21325627
VPS33_YEASTVPS33physical
21325627
VPS41_YEASTVPS41physical
21325627
VPS3_YEASTVPS3physical
21325627
VPS8_YEASTVPS8physical
21325627
VAM6_YEASTVAM6physical
21325627
YPT7_YEASTYPT7physical
21325627
VPS21_YEASTVPS21physical
21325627
YPT11_YEASTYPT11physical
21325627
YPT52_YEASTYPT52physical
21325627
VAM6_YEASTVAM6physical
20604902
VPS3_YEASTVPS3physical
20604902
PEP3_YEASTPEP3physical
20604902
VPS8_YEASTVPS8physical
20604902
VPS16_YEASTVPS16physical
20604902
VPS33_YEASTVPS33physical
20604902
PEP5_YEASTPEP5physical
22754631
UBC4_YEASTUBC4physical
22570702
SCH9_YEASTSCH9genetic
24514902
TOR1_YEASTTOR1genetic
24514902
GTR1_YEASTGTR1genetic
24514902
GTR2_YEASTGTR2genetic
24514902
VATA_YEASTVMA1genetic
24514902
VPH2_YEASTVPH2genetic
24514902
NOP2_YEASTNOP2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PEP5_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-608 AND THR-609, ANDMASS SPECTROMETRY.
"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 THR-608, AND MASSSPECTROMETRY.

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