NDUAA_MOUSE - dbPTM
NDUAA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NDUAA_MOUSE
UniProt AC Q99LC3
Protein Name NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
Gene Name Ndufa10
Organism Mus musculus (Mouse).
Sequence Length 355
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 MALRLLRLVPASAPARGLAAGAQRVGRIHTSVHCKLRYGLLAAILGDKTTKKLHEYSRVITVDGNICSGKNKLAKEIAQQLGMKHYPEAGIQYSSTTTGDGRPLDIEFSGSCSLEKFYDDPKSNDGNSYRLQSWLYASRLLQYADALEHLLSTGQGVVLERSIYSDFVFLEAMYNQGYIRKQCVDHYNEIKRLTLPEYLPPHAVIYIDVPVPEVQSRIQKKGDPHEMKVTSAYLQDIENAYKKTFLPKMSEMCEVLVYDSWEAEDPTKVVEDIEYLKYNKGPWLKQDDWTFHYLRMLVQDKTEVLNYTTIPVYLPEITIGAHQGSRIYNSFRELPGRKYAPGYNAEVGDKWIWLK
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
67S-nitrosocysteineITVDGNICSGKNKLA
EEECCCCCCCCHHHH
5.21-
67S-palmitoylationITVDGNICSGKNKLA
EEECCCCCCCCHHHH
5.2128526873
67S-nitrosylationITVDGNICSGKNKLA
EEECCCCCCCCHHHH
5.2122588120
72AcetylationNICSGKNKLAKEIAQ
CCCCCCHHHHHHHHH
53.9924062335
75AcetylationSGKNKLAKEIAQQLG
CCCHHHHHHHHHHHC
61.1524062335
75SuccinylationSGKNKLAKEIAQQLG
CCCHHHHHHHHHHHC
61.1526388266
84AcetylationIAQQLGMKHYPEAGI
HHHHHCCCCCCCCCE
37.8824062335
112S-nitrosocysteineDIEFSGSCSLEKFYD
EEEEECCEEEEEECC
6.50-
112S-nitrosylationDIEFSGSCSLEKFYD
EEEEECCEEEEEECC
6.5021278135
122AcetylationEKFYDDPKSNDGNSY
EEECCCCCCCCCCCH
69.7323576753
122SuccinylationEKFYDDPKSNDGNSY
EEECCCCCCCCCCCH
69.73-
122UbiquitinationEKFYDDPKSNDGNSY
EEECCCCCCCCCCCH
69.73-
122SuccinylationEKFYDDPKSNDGNSY
EEECCCCCCCCCCCH
69.7323806337
181AcetylationYNQGYIRKQCVDHYN
HHCCCCHHHHHHCHH
38.1916916647
183S-nitrosocysteineQGYIRKQCVDHYNEI
CCCCHHHHHHCHHHH
4.33-
183S-nitrosylationQGYIRKQCVDHYNEI
CCCCHHHHHHCHHHH
4.3321278135
191AcetylationVDHYNEIKRLTLPEY
HHCHHHHHHCCCCCC
34.8723864654
228AcetylationKGDPHEMKVTSAYLQ
CCCHHHHHCCHHHHH
39.1024062335
230PhosphorylationDPHEMKVTSAYLQDI
CHHHHHCCHHHHHHH
11.3429899451
231PhosphorylationPHEMKVTSAYLQDIE
HHHHHCCHHHHHHHH
20.2220495213
233PhosphorylationEMKVTSAYLQDIENA
HHHCCHHHHHHHHHH
12.5029899451
242SuccinylationQDIENAYKKTFLPKM
HHHHHHHHHHCHHHH
42.8226388266
242AcetylationQDIENAYKKTFLPKM
HHHHHHHHHHCHHHH
42.8223864654
243SuccinylationDIENAYKKTFLPKMS
HHHHHHHHHCHHHHH
31.6526388266
243AcetylationDIENAYKKTFLPKMS
HHHHHHHHHCHHHHH
31.65130453
250PhosphorylationKTFLPKMSEMCEVLV
HHCHHHHHHCCEEEE
28.4524652937
277SuccinylationVEDIEYLKYNKGPWL
EEEHHHHEECCCCCC
45.9723954790
277AcetylationVEDIEYLKYNKGPWL
EEEHHHHEECCCCCC
45.9723864654
277UbiquitinationVEDIEYLKYNKGPWL
EEEHHHHEECCCCCC
45.97-
285SuccinylationYNKGPWLKQDDWTFH
ECCCCCCCCCCHHHH
48.05-
285SuccinylationYNKGPWLKQDDWTFH
ECCCCCCCCCCHHHH
48.0523806337
285AcetylationYNKGPWLKQDDWTFH
ECCCCCCCCCCHHHH
48.0523806337
318PhosphorylationPVYLPEITIGAHQGS
CEECCEEEEECCCCC
16.23-
325PhosphorylationTIGAHQGSRIYNSFR
EEECCCCCHHHHCHH
14.66-
338UbiquitinationFRELPGRKYAPGYNA
HHCCCCCCCCCCCCC
52.2427667366
350SuccinylationYNAEVGDKWIWLK--
CCCCCCCEEEEEC--
34.3523806337
350AcetylationYNAEVGDKWIWLK--
CCCCCCCEEEEEC--
34.3516916647

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
250SPhosphorylationKinasePINK1Q99MQ3
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
242KAcetylation

-
250SPhosphorylation

24652937

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 NDUAA_MOUSE !!

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

Oops, there are no PPI records of NDUAA_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NDUAA_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-122; LYS-181; LYS-242 ANDLYS-350, AND MASS SPECTROMETRY.

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