DDI1_YEAST - dbPTM
DDI1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDI1_YEAST
UniProt AC P40087
Protein Name DNA damage-inducible protein 1
Gene Name DDI1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 428
Subcellular Localization Cytoplasm . Cell membrane
Peripheral membrane protein
Cytoplasmic side .
Protein Description Aspartic protease. [PubMed: 21266539 Appears to act as negative regulator of constitutive exocytosis]
Protein Sequence MDLTISNELTGEIYGPIEVSEDMALTDLIALLQADCGFDKTKHDLYYNMDILDSNRTQSLKELGLKTDDLLLIRGKISNSIQTDAATLSDEAFIEQFRQELLNNQMLRSQLILQIPGLNDLVNDPLLFRERLGPLILQRRYGGYNTAMNPFGIPQDEYTRLMANPDDPDNKKRIAELLDQQAIDEQLRNAIEYTPEMFTQVPMLYINIEINNYPVKAFVDTGAQTTIMSTRLAKKTGLSRMIDKRFIGEARGVGTGKIIGRIHQAQVKIETQYIPCSFTVLDTDIDVLIGLDMLKRHLACVDLKENVLRIAEVETSFLSEAEIPKSFQEGLPAPTSVTTSSDKPLTPTKTSSTLPPQPGAVPALAPRTGMGPTPTGRSTAGATTATGRTFPEQTIKQLMDLGFPRDAVVKALKQTNGNAEFAASLLFQ
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
42UbiquitinationDCGFDKTKHDLYYNM
CCCCCCCCCHHHHCC		40.6423749301
61UbiquitinationSNRTQSLKELGLKTD
CCCCHHHHHCCCCCC		57.0223749301
171UbiquitinationNPDDPDNKKRIAELL
CCCCCCHHHHHHHHH		51.3022817900
172UbiquitinationPDDPDNKKRIAELLD
CCCCCHHHHHHHHHH		56.1222817900
193PhosphorylationQLRNAIEYTPEMFTQ
HHHHHHHHCHHHHHC		22.8327017623
194PhosphorylationLRNAIEYTPEMFTQV
HHHHHHHCHHHHHCC		10.4527017623
205PhosphorylationFTQVPMLYINIEINN
HHCCCEEEEEEEECC		5.9127017623
213PhosphorylationINIEINNYPVKAFVD
EEEEECCEEEEEEEE		12.6227017623
234UbiquitinationIMSTRLAKKTGLSRM
HHHHHHHHHHCCHHH		56.3022817900
235UbiquitinationMSTRLAKKTGLSRMI
HHHHHHHHHCCHHHH		42.0722817900
257UbiquitinationARGVGTGKIIGRIHQ
CCCCCCCCCCEEEEE		30.8723749301
325UbiquitinationLSEAEIPKSFQEGLP
CCHHCCCHHHHCCCC		70.3523749301
335PhosphorylationQEGLPAPTSVTTSSD
HCCCCCCCCEECCCC		37.6322369663
336PhosphorylationEGLPAPTSVTTSSDK
CCCCCCCCEECCCCC		19.1922369663
338PhosphorylationLPAPTSVTTSSDKPL
CCCCCCEECCCCCCC		22.2622369663
339PhosphorylationPAPTSVTTSSDKPLT
CCCCCEECCCCCCCC		24.8725521595
340PhosphorylationAPTSVTTSSDKPLTP
CCCCEECCCCCCCCC		27.4622369663
341PhosphorylationPTSVTTSSDKPLTPT
CCCEECCCCCCCCCC		47.7822369663
343AcetylationSVTTSSDKPLTPTKT
CEECCCCCCCCCCCC		43.8224489116
343UbiquitinationSVTTSSDKPLTPTKT
CEECCCCCCCCCCCC		43.8223749301
346PhosphorylationTSSDKPLTPTKTSST
CCCCCCCCCCCCCCC		37.1225521595
348PhosphorylationSDKPLTPTKTSSTLP
CCCCCCCCCCCCCCC		41.5422369663
349UbiquitinationDKPLTPTKTSSTLPP
CCCCCCCCCCCCCCC		47.8423749301
373PhosphorylationPRTGMGPTPTGRSTA
CCCCCCCCCCCCCCC		27.9627214570
378PhosphorylationGPTPTGRSTAGATTA
CCCCCCCCCCCCCCC		24.7723749301
384PhosphorylationRSTAGATTATGRTFP
CCCCCCCCCCCCCCC		22.9919779198
410UbiquitinationFPRDAVVKALKQTNG
CCHHHHHHHHHHHCC		41.2123749301
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 DDI1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDI1_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 DDI1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBI4P_YEASTUBI4physical
11323716
SNC1_YEASTSNC1physical
12925750
SNC2_YEASTSNC2physical
12925750
TLG1_YEASTTLG1physical
12925750
TLG2_YEASTTLG2physical
12925750
HO_YEASTHOphysical
15964793
RPN1_YEASTRPN1physical
15964793
RPN12_YEASTRPN12physical
15964793
UFO1_YEASTUFO1physical
16478980
YJ9I_YEASTYJR141Wphysical
11283351
RAD23_YEASTRAD23genetic
18035052
DDI1_YEASTDDI1physical
17010377
POP7_YEASTPOP7genetic
19061648
NOP12_YEASTNOP12genetic
19061648
KA120_YEASTKAP120genetic
19061648
DBR1_YEASTDBR1genetic
19061648
DDI1_YEASTDDI1physical
18719252
DDI1_YEASTDDI1physical
18562697
DSK2_YEASTDSK2genetic
17144915
UFO1_YEASTUFO1genetic
21627799
UBI4P_YEASTUBI4physical
19620964
SSO1_YEASTSSO1genetic
12925750
CDC53_YEASTCDC53physical
22815701
UFO1_YEASTUFO1physical
22815701
RPN1_YEASTRPN1physical
22815701
HO_YEASTHOphysical
22815701
RS27A_YEASTRPS27Aphysical
22815701
UBI4P_YEASTUBI4physical
24709957
UBI4P_YEASTUBI4physical
17082762
PRS6A_YEASTRPT5physical
21627799
RPN9_YEASTRPN9physical
12051757
UBI4P_YEASTUBI4physical
25703377
UBI4P_YEASTUBI4physical
27646017
DDI1_YEASTDDI1physical
27646017
PRP9_YEASTPRP9genetic
27708008
DAD1_YEASTDAD1genetic
27708008
CDC37_YEASTCDC37genetic
27708008
RPN12_YEASTRPN12genetic
27708008
NUP57_YEASTNUP57genetic
27708008
MET30_YEASTMET30genetic
27708008
MCM1_YEASTMCM1genetic
27708008
YPQ3_YEASTRTC2genetic
27708008
WSS1_YEASTWSS1genetic
27708008
LSM7_YEASTLSM7genetic
27708008
TLG2_YEASTTLG2genetic
27708008
DDI1_HUMANDDI1physical
27107014
DVL2_HUMANDVL2physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DDI1_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-346 AND THR-348, 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-346, AND MASSSPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-346, UBIQUITINATION ATLYS-171, AND MASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery.";
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-257, AND MASSSPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-346, UBIQUITINATION ATLYS-171, AND MASS SPECTROMETRY.

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