OYE2_YEAST - dbPTM
OYE2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OYE2_YEAST
UniProt AC Q03558
Protein Name NADPH dehydrogenase 2
Gene Name OYE2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 400
Subcellular Localization
Protein Description Oxidizes beta-NADH, beta-NADPH, and alpha-NADPH..
Protein Sequence MPFVKDFKPQALGDTNLFKPIKIGNNELLHRAVIPPLTRMRAQHPGNIPNRDWAVEYYAQRAQRPGTLIITEGTFPSPQSGGYDNAPGIWSEEQIKEWTKIFKAIHENKSFAWVQLWVLGWAAFPDTLARDGLRYDSASDNVYMNAEQEEKAKKANNPQHSITKDEIKQYVKEYVQAAKNSIAAGADGVEIHSANGYLLNQFLDPHSNNRTDEYGGSIENRARFTLEVVDAVVDAIGPEKVGLRLSPYGVFNSMSGGAETGIVAQYAYVLGELERRAKAGKRLAFVHLVEPRVTNPFLTEGEGEYNGGSNKFAYSIWKGPIIRAGNFALHPEVVREEVKDPRTLIGYGRFFISNPDLVDRLEKGLPLNKYDRDTFYKMSAEGYIDYPTYEEALKLGWDKN
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
8SuccinylationMPFVKDFKPQALGDT
CCCCCCCCCCCCCCC		46.4823954790
8AcetylationMPFVKDFKPQALGDT
CCCCCCCCCCCCCCC		46.4824489116
19SuccinylationLGDTNLFKPIKIGNN
CCCCCCCCCEEECCC		49.3423954790
19AcetylationLGDTNLFKPIKIGNN
CCCCCCCCCEEECCC		49.3424489116
22AcetylationTNLFKPIKIGNNELL
CCCCCCEEECCCHHH		53.7622865919
100AcetylationEQIKEWTKIFKAIHE
HHHHHHHHHHHHHHH		47.4124489116
103AcetylationKEWTKIFKAIHENKS
HHHHHHHHHHHHCCC		50.3222865919
137PhosphorylationRDGLRYDSASDNVYM
HCCCCCCCCCCCCCC		22.2728889911
139PhosphorylationGLRYDSASDNVYMNA
CCCCCCCCCCCCCCH		33.4027017623
151AcetylationMNAEQEEKAKKANNP
CCHHHHHHHHHCCCC		65.8324489116
164AcetylationNPQHSITKDEIKQYV
CCCCCCCHHHHHHHH		52.2522865919
168AcetylationSITKDEIKQYVKEYV
CCCHHHHHHHHHHHH		33.2624489116
172AcetylationDEIKQYVKEYVQAAK
HHHHHHHHHHHHHHH		38.0924489116
172SuccinylationDEIKQYVKEYVQAAK
HHHHHHHHHHHHHHH		38.0923954790
294PhosphorylationHLVEPRVTNPFLTEG
EEECCCCCCCCCCCC		38.1522369663
299PhosphorylationRVTNPFLTEGEGEYN
CCCCCCCCCCCCCCC		42.1822369663
305PhosphorylationLTEGEGEYNGGSNKF
CCCCCCCCCCCCCCE		29.9322369663
309PhosphorylationEGEYNGGSNKFAYSI
CCCCCCCCCCEEEEE		37.9422369663
311AcetylationEYNGGSNKFAYSIWK
CCCCCCCCEEEEECC		32.8224489116
314PhosphorylationGGSNKFAYSIWKGPI
CCCCCEEEEECCCCE		12.1122369663
315PhosphorylationGSNKFAYSIWKGPII
CCCCEEEEECCCCEE		20.6721440633
339AcetylationEVVREEVKDPRTLIG
HHHHHHCCCHHHEEE		66.3524489116
353PhosphorylationGYGRFFISNPDLVDR
ECCEEEECCHHHHHH		36.8322369663
363AcetylationDLVDRLEKGLPLNKY
HHHHHHHHCCCCCCC		71.0424489116
369UbiquitinationEKGLPLNKYDRDTFY
HHCCCCCCCCHHHCC		57.1023749301
369AcetylationEKGLPLNKYDRDTFY
HHCCCCCCCCHHHCC		57.1024489116
379PhosphorylationRDTFYKMSAEGYIDY
HHHCCCCCCCCCCCC		21.0128889911
388PhosphorylationEGYIDYPTYEEALKL
CCCCCCCCHHHHHHH		37.0228889911
389PhosphorylationGYIDYPTYEEALKLG
CCCCCCCHHHHHHHC		13.7825752575
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 OYE2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OYE2_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 OYE2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP77_YEASTSSC1physical
16429126
OYE3_YEASTOYE3genetic
17897954
MCFS2_YEASTEHT1genetic
20093466
THRC_YEASTTHR4genetic
20093466
NDH2_YEASTNDE2genetic
20093466
BRE1_YEASTBRE1genetic
20093466
TRPE_YEASTTRP2genetic
20093466
RPOM_YEASTRPO41genetic
20093466
MTO1_YEASTMTO1genetic
20093466
CGR1_YEASTCGR1genetic
20093466
UPF3_YEASTUPF3genetic
20093466
MET28_YEASTMET28genetic
20093466
MTC1_YEASTMTC1genetic
20093466
YJY1_YEASTYJR011Cgenetic
20093466
RAD7_YEASTRAD7genetic
20093466
YJ24_YEASTKCH1genetic
20093466
YRA2_YEASTYRA2genetic
20093466
SAC1_YEASTSAC1genetic
20093466
DBP7_YEASTDBP7genetic
20093466
FMP46_YEASTFMP46genetic
20093466
SRL3_YEASTSRL3genetic
20093466
RL40A_YEASTRPL40Bgenetic
20093466
RL40B_YEASTRPL40Bgenetic
20093466
RL8B_YEASTRPL8Bgenetic
20093466
EMC6_YEASTEMC6genetic
20093466
PPR1_YEASTPPR1genetic
20093466
MDL1_YEASTMDL1genetic
20093466
TCB3_YEASTTCB3genetic
20093466
YMF3_YEASTYML053Cgenetic
20093466
AVO2_YEASTAVO2genetic
20093466
MKS1_YEASTMKS1genetic
20093466
SIN3_YEASTSIN3genetic
20093466
KIN4_YEASTKIN4genetic
20093466
PNT1_YEASTPNT1genetic
20093466
NCBP2_YEASTCBC2genetic
20093466
LGE1_YEASTLGE1genetic
20093466
KIN4_YEASTKIN4genetic
22282571
DEP1_YEASTDEP1genetic
27708008
MCFS2_YEASTEHT1genetic
27708008
BRE1_YEASTBRE1genetic
27708008
NDH2_YEASTNDE2genetic
27708008
UME6_YEASTUME6genetic
27708008
YGS6_YEASTYGL176Cgenetic
27708008
MTO1_YEASTMTO1genetic
27708008
UPF3_YEASTUPF3genetic
27708008
SNF6_YEASTSNF6genetic
27708008
MET28_YEASTMET28genetic
27708008
VPS53_YEASTVPS53genetic
27708008
MTC1_YEASTMTC1genetic
27708008
YJY1_YEASTYJR011Cgenetic
27708008
YJ24_YEASTKCH1genetic
27708008
ECM27_YEASTECM27genetic
27708008
PPR1_YEASTPPR1genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
PAU4_YEASTPAU4genetic
27708008
TCB3_YEASTTCB3genetic
27708008
SAP30_YEASTSAP30genetic
27708008
SCS7_YEASTSCS7genetic
27708008
SIW14_YEASTSIW14genetic
27708008
MKS1_YEASTMKS1genetic
27708008
SIN3_YEASTSIN3genetic
27708008
MSN1_YEASTMSN1genetic
27708008
ASE1_YEASTASE1genetic
27708008
KIN4_YEASTKIN4genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
AFT2_YEASTAFT2genetic
27708008
ATF1_YEASTATF1genetic
28137282
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OYE2_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-137; TYR-305; SER-353;SER-379 AND THR-388, AND MASS 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 SER-353, AND MASSSPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND MASSSPECTROMETRY.

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