NDUA7_HUMAN - dbPTM
NDUA7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NDUA7_HUMAN
UniProt AC O95182
Protein Name NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7
Gene Name NDUFA7
Organism Homo sapiens (Human).
Sequence Length 113
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 MASATRLIQRLRNWASGHDLQGKLQLRYQEISKRTQPPPKLPVGPSHKLSNNYYCTRDGRRESVPPSIIMSSQKALVSGKPAESSAVAATEKKAVTPAPPIKRWELSSDQPYL
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------MASATRLIQ
------CCHHHHHHH
14.10-
3Phosphorylation-----MASATRLIQR
-----CCHHHHHHHH
28.9528270605
5Phosphorylation---MASATRLIQRLR
---CCHHHHHHHHHH
24.4228270605
12MethylationTRLIQRLRNWASGHD
HHHHHHHHHHHCCCC
38.54115484701
23UbiquitinationSGHDLQGKLQLRYQE
CCCCCHHHHHHHHHH
21.7922817900
32PhosphorylationQLRYQEISKRTQPPP
HHHHHHHHHHCCCCC
18.4823312004
332-HydroxyisobutyrylationLRYQEISKRTQPPPK
HHHHHHHHHCCCCCC
66.19-
40SuccinylationKRTQPPPKLPVGPSH
HHCCCCCCCCCCCCC
71.8027452117
40MalonylationKRTQPPPKLPVGPSH
HHCCCCCCCCCCCCC
71.8026320211
40AcetylationKRTQPPPKLPVGPSH
HHCCCCCCCCCCCCC
71.80-
53PhosphorylationSHKLSNNYYCTRDGR
CCCCCCCEEECCCCC
12.2721945579
54PhosphorylationHKLSNNYYCTRDGRR
CCCCCCEEECCCCCC
6.8921945579
56PhosphorylationLSNNYYCTRDGRRES
CCCCEEECCCCCCCC
18.7021945579
63PhosphorylationTRDGRRESVPPSIIM
CCCCCCCCCCHHHEE
37.8123312004
67PhosphorylationRRESVPPSIIMSSQK
CCCCCCHHHEEECCE
20.7618691976
78PhosphorylationSSQKALVSGKPAESS
ECCEEHHCCCCCCCC
41.7817081983
80MalonylationQKALVSGKPAESSAV
CEEHHCCCCCCCCCC
33.2826320211
80AcetylationQKALVSGKPAESSAV
CEEHHCCCCCCCCCC
33.2826051181
84PhosphorylationVSGKPAESSAVAATE
HCCCCCCCCCCCCCC
26.2126437602
85PhosphorylationSGKPAESSAVAATEK
CCCCCCCCCCCCCCC
20.47-
90PhosphorylationESSAVAATEKKAVTP
CCCCCCCCCCCCCCC
38.30-
922-HydroxyisobutyrylationSAVAATEKKAVTPAP
CCCCCCCCCCCCCCC
41.50-
92AcetylationSAVAATEKKAVTPAP
CCCCCCCCCCCCCCC
41.5026051181
96PhosphorylationATEKKAVTPAPPIKR
CCCCCCCCCCCCCCC
20.7023312004
1022-HydroxyisobutyrylationVTPAPPIKRWELSSD
CCCCCCCCCEECCCC
58.18-

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 NDUA7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NDUA7_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 NDUA7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AAKB1_HUMANPRKAB1physical
16169070
RL38_HUMANRPL38physical
22939629
TIM44_HUMANTIMM44physical
22939629
RRBP1_HUMANRRBP1physical
22939629
PIN1_HUMANPIN1physical
22939629
SBDS_HUMANSBDSphysical
22939629
RAB8A_HUMANRAB8Aphysical
22939629
PDLI5_HUMANPDLIM5physical
22939629
RBM27_HUMANRBM27physical
22939629
RRFM_HUMANMRRFphysical
22939629
TAGL_HUMANTAGLNphysical
22939629
PIN4_HUMANPIN4physical
22939629
RAGP1_HUMANRANGAP1physical
22939629
UBL4A_HUMANUBL4Aphysical
22939629
PDLI7_HUMANPDLIM7physical
22939629
TPX2_HUMANTPX2physical
22939629
UB2L3_HUMANUBE2L3physical
22939629
SNX3_HUMANSNX3physical
22939629
ECI2_HUMANECI2physical
22939629
RIDA_HUMANHRSP12physical
22939629
RBMS1_HUMANRBMS1physical
22939629
SUGP1_HUMANSUGP1physical
22939629
QKI_HUMANQKIphysical
22939629
PQBP1_HUMANPQBP1physical
22939629
PAF15_HUMANKIAA0101physical
22939629
TBL2_HUMANTBL2physical
22939629
RFX5_HUMANRFX5physical
22939629
STX7_HUMANSTX7physical
22939629
MPLKI_HUMANMPLKIPphysical
22939629
RU1C_HUMANSNRPCphysical
22939629
SCO2_HUMANSCO2physical
22939629
SOSB1_HUMANNABP2physical
22939629
RT28_HUMANMRPS28physical
22939629
ZC11A_HUMANZC3H11Aphysical
22939629
RM14_HUMANMRPL14physical
22939629
OLA1_HUMANOLA1physical
22939629
SRRM2_HUMANSRRM2physical
22939629
TOM40_HUMANTOMM40physical
22939629
RS28_HUMANRPS28physical
22939629
UBC9_HUMANUBE2Iphysical
22939629
P66B_HUMANGATAD2Bphysical
22939629
UBE4B_HUMANUBE4Bphysical
22939629
VDAC3_HUMANVDAC3physical
22939629
NLTP_HUMANSCP2physical
22939629
THIK_HUMANACAA1physical
22939629
NU214_HUMANNUP214physical
22939629
MDFI_HUMANMDFIphysical
19060904

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 NDUA7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASSSPECTROMETRY.

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