NDI1_YEAST - dbPTM
NDI1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NDI1_YEAST
UniProt AC P32340
Protein Name Rotenone-insensitive NADH-ubiquinone oxidoreductase, mitochondrial
Gene Name NDI1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 513
Subcellular Localization Mitochondrion inner membrane
Peripheral membrane protein
Matrix side . Bound to the mitochondrial inner membrane facing the matrix site.
Protein Description Catalyzes the oxidation of NADH generated inside the Mitochondrion..
Protein Sequence MLSKNLYSNKRLLTSTNTLVRFASTRSTGVENSGAGPTSFKTMKVIDPQHSDKPNVLILGSGWGAISFLKHIDTKKYNVSIISPRSYFLFTPLLPSAPVGTVDEKSIIEPIVNFALKKKGNVTYYEAEATSINPDRNTVTIKSLSAVSQLYQPENHLGLHQAEPAEIKYDYLISAVGAEPNTFGIPGVTDYGHFLKEIPNSLEIRRTFAANLEKANLLPKGDPERRRLLSIVVVGGGPTGVEAAGELQDYVHQDLRKFLPALAEEVQIHLVEALPIVLNMFEKKLSSYAQSHLENTSIKVHLRTAVAKVEEKQLLAKTKHEDGKITEETIPYGTLIWATGNKARPVITDLFKKIPEQNSSKRGLAVNDFLQVKGSNNIFAIGDNAFAGLPPTAQVAHQEAEYLAKNFDKMAQIPNFQKNLSSRKDKIDLLFEENNFKPFKYNDLGALAYLGSERAIATIRSGKRTFYTGGGLMTFYLWRILYLSMILSARSRLKVFFDWIKLAFFKRDFFKGL
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
27PhosphorylationVRFASTRSTGVENSG
HHHHHCCCCCCCCCC		29.6028889911
28PhosphorylationRFASTRSTGVENSGA
HHHHCCCCCCCCCCC		41.7927214570
214AcetylationTFAANLEKANLLPKG
HHHHHHHHCCCCCCC		45.8224489116
239PhosphorylationVVVGGGPTGVEAAGE
EEECCCCCHHHHHHH		58.0728889911
326PhosphorylationKHEDGKITEETIPYG
CCCCCCCCCEECCCC		31.1227017623
329PhosphorylationDGKITEETIPYGTLI
CCCCCCEECCCCEEE		22.4825533186
332PhosphorylationITEETIPYGTLIWAT
CCCEECCCCEEEECC		20.9225533186
334PhosphorylationEETIPYGTLIWATGN
CEECCCCEEEECCCC		14.8225533186
339PhosphorylationYGTLIWATGNKARPV
CCEEEECCCCCCCCH		26.7025533186
409AcetylationYLAKNFDKMAQIPNF
HHHHHHHHHHCCCCH		31.8124489116
418AcetylationAQIPNFQKNLSSRKD
HCCCCHHHHHHCCHH		56.5722865919
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 NDI1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NDI1_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 NDI1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OAC1_YEASTOAC1genetic
16941010
CSN5_YEASTRRI1genetic
20093466
YHR2_YEASTYHR112Cgenetic
20093466
ERG2_YEASTERG2genetic
20093466
ADH3_YEASTADH3genetic
21623372
PFKA1_YEASTPFK1genetic
21623372
GGPPS_YEASTBTS1genetic
21623372
6PGD1_YEASTGND1genetic
21623372
NDH1_YEASTNDE1genetic
21623372
HSP82_YEASTHSP82physical
22940862
PPT1_YEASTPPT1physical
22940862
HSC82_YEASTHSC82physical
22940862
HSP71_YEASTSSA1physical
22940862
NDI1_YEASTNDI1physical
22949654
NDI1_YEASTNDI1physical
23086143
NTC20_YEASTNTC20genetic
27708008
IME1_YEASTIME1genetic
29301906
PACC_YEASTRIM101genetic
29301906
SMP1_YEASTSMP1genetic
29301906
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NDI1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase.";
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
Mol. Cell. Proteomics 6:1896-1906(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND THR-28, AND MASSSPECTROMETRY.

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