DPP1_YEAST - dbPTM
DPP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPP1_YEAST
UniProt AC Q05521
Protein Name Diacylglycerol pyrophosphate phosphatase 1
Gene Name DPP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 289
Subcellular Localization Vacuole membrane
Multi-pass membrane protein .
Protein Description Catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Together with LPP1, regulates intracellular DGPP and PA levels, which are phospholipid molecules believed to play a signaling role in stress response. Can also use lysophosphatidic acid (LPA) and phosphatidylglycerophosphate as substrates. Substrate preference is DGPP > LPA > PA. Activity is independent of a divalent cation ion and insensitive to inhibition by N-ethylmaleimide..
Protein Sequence MNRVSFIKTPFNIGAKWRLEDVFLLIIMILLNYPVYYQQPFERQFYINDLTISHPYATTERVNNNMLFVYSFVVPSLTILIIGSILADRRHLIFILYTSLLGLSLAWFSTSFFTNFIKNWIGRLRPDFLDRCQPVEGLPLDTLFTAKDVCTTKNHERLLDGFRTTPSGHSSESFAGLGYLYFWLCGQLLTESPLMPLWRKMVAFLPLLGAALIALSRTQDYRHHFVDVILGSMLGYIMAHFFYRRIFPPIDDPLPFKPLMDDSDVTLEEAVTHQRIPDEELHPLSDEGM
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
8UbiquitinationMNRVSFIKTPFNIGA
CCCCCCCCCCCCCCC		48.4024961812
285PhosphorylationDEELHPLSDEGM---
HHHHCCCCCCCC---		37.7622369663
289OxidationHPLSDEGM-------
CCCCCCCC-------		4.7015665377
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 DPP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPP1_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 DPP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DPP1_YEASTDPP1physical
18467557
KEX1_YEASTKEX1physical
18467557
VATH_YEASTVMA13physical
18467557
VAC8_YEASTVAC8physical
18467557
ATC2_YEASTPMC1physical
18467557
DPP1_YEASTDPP1physical
18719252
SEC62_YEASTSEC62physical
18719252
GST1_YEASTGTT1physical
18719252
CYB5_YEASTCYB5physical
18719252
YPR71_YEASTYPR071Wphysical
18719252
PEX29_YEASTPEX29physical
18719252
SNF1_YEASTSNF1genetic
19269370
CAK1_YEASTCAK1genetic
19269370
BUB1_YEASTBUB1genetic
19269370
DPP1_YEASTDPP1physical
22615397
KPYK1_YEASTCDC19physical
22940862
ENO2_YEASTENO2physical
22940862
HSC82_YEASTHSC82physical
22940862
HSP7F_YEASTSSE1physical
22940862
HSP72_YEASTSSA2physical
22940862
HSP82_YEASTHSP82physical
22940862
SYEC_YEASTGUS1physical
22940862
SSB1_YEASTSSB1physical
22940862
HSP71_YEASTSSA1physical
22940862
RV161_YEASTRVS161genetic
23891562
YPS6_YEASTYPS6genetic
23891562
PAH1_YEASTPAH1genetic
24196957
SAC3_YEASTSAC3genetic
27708008
RL8B_YEASTRPL8Bgenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DPP1_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 SER-285, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND MASSSPECTROMETRY.

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