NDUB9_HUMAN - dbPTM
NDUB9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NDUB9_HUMAN
UniProt AC Q9Y6M9
Protein Name NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
Gene Name NDUFB9
Organism Homo sapiens (Human).
Sequence Length 179
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 to be not 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 MAFLASGPYLTHQQKVLRLYKRALRHLESWCVQRDKYRYFACLMRARFEEHKNEKDMAKATQLLKEAEEEFWYRQHPQPYIFPDSPGGTSYERYDCYKVPEWCLDDWHPSEKAMYPDYFAKREQWKKLRRESWEREVKQLQEETPPGGPLTEALPPARKEGDLPPLWWYIVTRPRERPM
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------MAFLASGPY
------CCCCCCCCC
14.2525944712
6Phosphorylation--MAFLASGPYLTHQ
--CCCCCCCCCCHHH
42.3120068231
9PhosphorylationAFLASGPYLTHQQKV
CCCCCCCCCHHHHHH
27.9720068231
11PhosphorylationLASGPYLTHQQKVLR
CCCCCCCHHHHHHHH
16.2820068231
15UbiquitinationPYLTHQQKVLRLYKR
CCCHHHHHHHHHHHH
36.3421890473
55AcetylationFEEHKNEKDMAKATQ
HHHHCCHHHHHHHHH
63.3025825284
59UbiquitinationKNEKDMAKATQLLKE
CCHHHHHHHHHHHHH
45.3821906983
592-HydroxyisobutyrylationKNEKDMAKATQLLKE
CCHHHHHHHHHHHHH
45.38-
65UbiquitinationAKATQLLKEAEEEFW
HHHHHHHHHHHHHHH
64.5721890473
73PhosphorylationEAEEEFWYRQHPQPY
HHHHHHHHHCCCCCE
13.01-
80PhosphorylationYRQHPQPYIFPDSPG
HHCCCCCEECCCCCC
15.2225884760
85PhosphorylationQPYIFPDSPGGTSYE
CCEECCCCCCCCCCC
26.1925159151
89PhosphorylationFPDSPGGTSYERYDC
CCCCCCCCCCCCCCC
33.7720068231
90PhosphorylationPDSPGGTSYERYDCY
CCCCCCCCCCCCCCC
28.4223186163
91PhosphorylationDSPGGTSYERYDCYK
CCCCCCCCCCCCCCC
12.3120068231
98AcetylationYERYDCYKVPEWCLD
CCCCCCCCCCHHHCC
58.6125825284
98UbiquitinationYERYDCYKVPEWCLD
CCCCCCCCCCHHHCC
58.61-
112UbiquitinationDDWHPSEKAMYPDYF
CCCCHHHHHCCHHHH
42.67-
115PhosphorylationHPSEKAMYPDYFAKR
CHHHHHCCHHHHHHH
9.6025348954
118PhosphorylationEKAMYPDYFAKREQW
HHHCCHHHHHHHHHH
10.8425348954
121UbiquitinationMYPDYFAKREQWKKL
CCHHHHHHHHHHHHH
46.7121890473
121AcetylationMYPDYFAKREQWKKL
CCHHHHHHHHHHHHH
46.71133291
1212-HydroxyisobutyrylationMYPDYFAKREQWKKL
CCHHHHHHHHHHHHH
46.71-
132PhosphorylationWKKLRRESWEREVKQ
HHHHHHHHHHHHHHH
32.2123882029
138UbiquitinationESWEREVKQLQEETP
HHHHHHHHHHHHHCC
40.302190698
138MalonylationESWEREVKQLQEETP
HHHHHHHHHHHHHCC
40.3032601280
169PhosphorylationDLPPLWWYIVTRPRE
CCCCCEEEEECCCCC
3.64-

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 NDUB9_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NDUB9_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 NDUB9_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GDF9_HUMANGDF9physical
16169070
FEZ1_HUMANFEZ1physical
16169070
ELP1_HUMANIKBKAPphysical
16169070
SH3G3_HUMANSH3GL3physical
16169070
HAP1_HUMANHAP1physical
16169070
MIC60_HUMANIMMTphysical
16169070
NDUS1_HUMANNDUFS1physical
22939629
NDUBA_HUMANNDUFB10physical
22939629
SYNE2_HUMANSYNE2physical
22939629
STX4_HUMANSTX4physical
22939629
RT28_HUMANMRPS28physical
22939629
AT5F1_HUMANATP5F1physical
26344197
CLH1_HUMANCLTCphysical
26344197
ETFR1_HUMANLYRM5physical
26344197
NDUAC_HUMANNDUFA12physical
26344197
NDUA2_HUMANNDUFA2physical
26344197
NDUA6_HUMANNDUFA6physical
26344197
NDUA9_HUMANNDUFA9physical
26344197
NDUB8_HUMANNDUFB8physical
26344197
RPN1_HUMANRPN1physical
26344197
VDAC2_HUMANVDAC2physical
26344197

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NDUB9_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASSSPECTROMETRY.

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