DDP1_YEAST - dbPTM
DDP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDP1_YEAST
UniProt AC Q99321
Protein Name Diphosphoinositol polyphosphate phosphohydrolase DDP1
Gene Name DDP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 188
Subcellular Localization Cytoplasm . Nucleus .
Protein Description May eliminate potentially toxic dinucleoside polyphosphates during sporulation. Most active against diadenosine 5',5'''-P1,P6-hexaphosphate (Ap6A). Can also hydrolyze diadenosine 5',5'''-P1,P5-pentaphosphate (Ap5A), adenosine 5'-pentaphosphate, and adenosine 5'-tetraphosphate are also substrates, but not diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) or other dinucleotides, mononucleotides, nucleotide sugars, or nucleotide alcohols. Also cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate)..
Protein Sequence MGKTADNHGPVRSETAREGRENQVYSPVTGARLVAGCICLTPDKKQVLMITSSAHKKRWIVPKGGVEKDEPNYETTAQRETWEEAGCIGKIVANLGTVEDMRPPKDWNKDIKQFENSRKDSEVAKHPPRTEFHFYELEIENLLDKFPECHKRHRKLYSYTEAKQNLIDAKRPELLEALNRSAIIKDDK
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
25PhosphorylationEGRENQVYSPVTGAR
CCCCCCCCCCCCCCC
9.4822369663
26PhosphorylationGRENQVYSPVTGARL
CCCCCCCCCCCCCCE
17.6522369663
29PhosphorylationNQVYSPVTGARLVAG
CCCCCCCCCCCEEEE
28.6222369663
105AcetylationVEDMRPPKDWNKDIK
CCCCCCCCCCCHHHH
77.4124489116
121PhosphorylationFENSRKDSEVAKHPP
HHHHHCCHHHHHCCC
36.6930377154
170AcetylationKQNLIDAKRPELLEA
HHHHHHCCCHHHHHH
65.8124489116

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 DDP1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDP1_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 DDP1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KCS1_YEASTKCS1genetic
21623372
DDP1_YEASTDDP1physical
22940862
SNF5_YEASTSNF5genetic
27708008
RPN4_YEASTRPN4genetic
27708008
VAM6_YEASTVAM6genetic
27708008
RSSA2_YEASTRPS0Bgenetic
27708008
ENV10_YEASTENV10genetic
27708008
ATP18_YEASTATP18genetic
27708008
MKT1_YEASTMKT1genetic
27708008
GEM1_YEASTGEM1genetic
27708008
SWD1_YEASTSWD1genetic
27708008
AIM4_YEASTAIM4genetic
27708008
ODPB_YEASTPDB1genetic
27708008
PAT1_YEASTPAT1genetic
27708008
SLX5_YEASTSLX5genetic
27708008
BRE1_YEASTBRE1genetic
27708008
MON1_YEASTMON1genetic
27708008
AIM21_YEASTAIM21genetic
27708008
F26_YEASTFBP26genetic
27708008
IXR1_YEASTIXR1genetic
27708008
FEN1_YEASTRAD27genetic
27708008
CTK1_YEASTCTK1genetic
27708008
RT109_YEASTRTT109genetic
27708008
PUF3_YEASTPUF3genetic
27708008
FPS1_YEASTFPS1genetic
27708008
ROM2_YEASTROM2genetic
27708008
RAD52_YEASTRAD52genetic
27708008
GAS1_YEASTGAS1genetic
27708008
EOS1_YEASTEOS1genetic
27708008
PHO23_YEASTPHO23genetic
27708008
MRN1_YEASTMRN1genetic
27708008
ATG41_YEASTICY2genetic
27708008
PHSG_YEASTGPH1genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DDP1_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-26, AND MASSSPECTROMETRY.

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