NDUA9_MOUSE - dbPTM
NDUA9_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NDUA9_MOUSE
UniProt AC Q9DC69
Protein Name NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
Gene Name Ndufa9
Organism Mus musculus (Mouse).
Sequence Length 377
Subcellular Localization Mitochondrion matrix .
Protein Description Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone..
Protein Sequence MAAAVRFRVVRALPMSRPAITAAATSVFCGSSHRQLHHAVIPHGKGGRSSVSGVVATVFGATGFLGRYVVNHLGRMGSQVIIPYRCDVYDIMHLRLMGDLGQLTFLEWDARDKDSIRKAVQHSNVVINLIGREWETRNFDFEDVFVNIPRAIAQASKEAGVERFIHVSHLNASMKSSSKSLRSKAVGEKEVRSVFPEAIIIRPSDIFGREDRFLNHFANYRWFLAVPLVSLGFKTVKQPVYVADVSKGIVNATKDPDAVGKTFAFTGPNRYLLFHLVKYIFGMTHRTFIPYPLPLFVYSWIGKLFGLSPFEPWTTKDKVERIHISDVMPTDLPGLEDLGVQPTPLELKSIEVLRRHRTYRWLSSEIEETKPAKTVNY
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
16PhosphorylationVVRALPMSRPAITAA
EEECCCCCCHHHHHH
32.9222802335
21PhosphorylationPMSRPAITAAATSVF
CCCCHHHHHHHCEEC
16.6122802335
68PhosphorylationATGFLGRYVVNHLGR
CCCHHHHHHHHHHHC
13.6227180971
86S-palmitoylationQVIIPYRCDVYDIMH
EEEEEECCCHHHHHH
3.2426165157
86S-nitrosocysteineQVIIPYRCDVYDIMH
EEEEEECCCHHHHHH
3.24-
86S-nitrosylationQVIIPYRCDVYDIMH
EEEEEECCCHHHHHH
3.2421278135
113AcetylationLEWDARDKDSIRKAV
EEECCCCHHHHHHHH
48.0723201123
156O-linked_GlycosylationPRAIAQASKEAGVER
HHHHHHHHHHHCCCE
20.9615066235
157AcetylationRAIAQASKEAGVERF
HHHHHHHHHHCCCEE
55.3823806337
157SuccinylationRAIAQASKEAGVERF
HHHHHHHHHHCCCEE
55.3823806337
173PhosphorylationHVSHLNASMKSSSKS
EHHHHCHHHCCCCHH
26.18-
175SuccinylationSHLNASMKSSSKSLR
HHHCHHHCCCCHHHH
44.69-
175AcetylationSHLNASMKSSSKSLR
HHHCHHHCCCCHHHH
44.6923806337
175SuccinylationSHLNASMKSSSKSLR
HHHCHHHCCCCHHHH
44.6923806337
189AcetylationRSKAVGEKEVRSVFP
HHHHHCHHHHHHHCC
56.4323576753
189SuccinylationRSKAVGEKEVRSVFP
HHHHHCHHHHHHHCC
56.4326388266
193PhosphorylationVGEKEVRSVFPEAII
HCHHHHHHHCCCEEE
33.0324719451
237UbiquitinationSLGFKTVKQPVYVAD
HCCCCCCCCCEEEEE
54.8627667366
254UbiquitinationKGIVNATKDPDAVGK
CCCCCCCCCCCCCCC
65.9322790023
254AcetylationKGIVNATKDPDAVGK
CCCCCCCCCCCCCCC
65.9323201123
261SuccinylationKDPDAVGKTFAFTGP
CCCCCCCCEEEECCC
33.5923954790
316AcetylationPFEPWTTKDKVERIH
CCCCCCCCCCEEEEE
48.4523954790
370AcetylationSSEIEETKPAKTVNY
HHHHCCCCCCCCCCC
46.3823576753
373AcetylationIEETKPAKTVNY---
HCCCCCCCCCCC---
62.6324062335

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 NDUA9_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NDUA9_MOUSE !!

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 NDUA9_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of NDUA9_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NDUA9_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-370, AND MASS SPECTROMETRY.

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