NDUA5_HUMAN - dbPTM
NDUA5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NDUA5_HUMAN
UniProt AC Q16718
Protein Name NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5
Gene Name NDUFA5
Organism Homo sapiens (Human).
Sequence Length 116
Subcellular Localization Mitochondrion inner membrane
Peripheral membrane protein
Matrix side .
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 MAGVLKKTTGLVGLAVCNTPHERLRILYTKILDVLEEIPKNAAYRKYTEQITNEKLAMVKAEPDVKKLEDQLQGGQLEEVILQAEHELNLARKMREWKLWEPLVEEPPADQWKWPI
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
2Acetylation------MAGVLKKTT
------CCCCCCCCC
19.46-
27AcetylationPHERLRILYTKILDV
HHHHHHHHHHHHHHH
3.4319608861
28PhosphorylationHERLRILYTKILDVL
HHHHHHHHHHHHHHH
12.01-
30AcetylationRLRILYTKILDVLEE
HHHHHHHHHHHHHHH
27.9319608861
40SuccinylationDVLEEIPKNAAYRKY
HHHHHCCCCHHHHHH
65.9523954790
40AcetylationDVLEEIPKNAAYRKY
HHHHHCCCCHHHHHH
65.9526822725
46AcetylationPKNAAYRKYTEQITN
CCCHHHHHHHHHHCH
43.7927452117
462-HydroxyisobutyrylationPKNAAYRKYTEQITN
CCCHHHHHHHHHHCH
43.79-
552-HydroxyisobutyrylationTEQITNEKLAMVKAE
HHHHCHHHHHHHCCC
43.55-
55AcetylationTEQITNEKLAMVKAE
HHHHCHHHHHHHCCC
43.5527452117
57AcetylationQITNEKLAMVKAEPD
HHCHHHHHHHCCCCC
16.2819608861
60SumoylationNEKLAMVKAEPDVKK
HHHHHHHCCCCCHHH
33.6719608861
60MalonylationNEKLAMVKAEPDVKK
HHHHHHHCCCCCHHH
33.6726320211
60SumoylationNEKLAMVKAEPDVKK
HHHHHHHCCCCCHHH
33.67-
60AcetylationNEKLAMVKAEPDVKK
HHHHHHHCCCCCHHH
33.6719608861
60SuccinylationNEKLAMVKAEPDVKK
HHHHHHHCCCCCHHH
33.6727452117
66AcetylationVKAEPDVKKLEDQLQ
HCCCCCHHHHHHHHC
60.0525038526
67AcetylationKAEPDVKKLEDQLQG
CCCCCHHHHHHHHCC
57.8925038526
98SuccinylationARKMREWKLWEPLVE
HHHHHHHCCCCCCCC
38.68-
98SuccinylationARKMREWKLWEPLVE
HHHHHHHCCCCCCCC
38.68-
98AcetylationARKMREWKLWEPLVE
HHHHHHHCCCCCCCC
38.6825038526

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 NDUA5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NDUA5_HUMAN !!

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 NDUA5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DAZP2_HUMANDAZAP2physical
16189514
NDUB1_HUMANNDUFB1physical
16189514
CC85B_HUMANCCDC85Bphysical
16189514
A4_HUMANAPPphysical
21832049
NDUS3_HUMANNDUFS3physical
22939629
NDUB9_HUMANNDUFB9physical
22939629
NDUBA_HUMANNDUFB10physical
22939629
RAB8A_HUMANRAB8Aphysical
27173435
WDR26_HUMANWDR26physical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NDUA5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30 AND LYS-60, AND MASSSPECTROMETRY.

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