NDUBA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NDUBA_HUMAN
• UniProt AC: O96000
• Protein Name: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10
• Gene Name: NDUFB10
• Organism: Homo sapiens (Human).
• Sequence Length: 172
• 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: MPDSWDKDVYPEPPRRTPVQPNPIVYMMKAFDLIVDRPVTLVREFIERQHAKNRYYYYHRQYRRVPDITECKEEDIMCMYEAEMQWKRDYKVDQEIINIMQDRLKACQQREGQNYQQNCIKEVEQFTQVAKAYQDRYQDLGAYSSARKCLAKQRQRMLQERKAAKEAAAATS

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
4	Phosphorylation	----MPDSWDKDVYP ----CCCCCCCCCCC	31.16	20873877
7	Ubiquitination	-MPDSWDKDVYPEPP -CCCCCCCCCCCCCC	42.72	-
17	Phosphorylation	YPEPPRRTPVQPNPI CCCCCCCCCCCCCCH	29.14	25159151
26	Phosphorylation	VQPNPIVYMMKAFDL CCCCCHHHEHHHHHH	7.69	20068231
55	Phosphorylation	RQHAKNRYYYYHRQY HHHHHHHHHHHHCCC	12.76	28152594
56	Phosphorylation	QHAKNRYYYYHRQYR HHHHHHHHHHHCCCC	8.36	28152594
57	Phosphorylation	HAKNRYYYYHRQYRR HHHHHHHHHHCCCCC	5.49	28152594
58	Phosphorylation	AKNRYYYYHRQYRRV HHHHHHHHHCCCCCC	3.71	28152594
80	Phosphorylation	EEDIMCMYEAEMQWK HHHCHHHHHHHHHHH	13.68	26503514
91	Ubiquitination	MQWKRDYKVDQEIIN HHHHCCCCCCHHHHH	43.56	21890473
91	Ubiquitination	MQWKRDYKVDQEIIN HHHHCCCCCCHHHHH	43.56	21906983
105	Ubiquitination	NIMQDRLKACQQREG HHHHHHHHHHHHHCC	48.27	-
115	Phosphorylation	QQREGQNYQQNCIKE HHHCCCCHHHHHHHH	12.00	28152594
119	Glutathionylation	GQNYQQNCIKEVEQF CCCHHHHHHHHHHHH	4.01	22555962
121	Acetylation	NYQQNCIKEVEQFTQ CHHHHHHHHHHHHHH	58.89	26051181
121	Ubiquitination	NYQQNCIKEVEQFTQ CHHHHHHHHHHHHHH	58.89	21906983
121	Ubiquitination	NYQQNCIKEVEQFTQ CHHHHHHHHHHHHHH	58.89	21890473
131	Ubiquitination	EQFTQVAKAYQDRYQ HHHHHHHHHHHHHHH	49.09	21906983
131	Ubiquitination	EQFTQVAKAYQDRYQ HHHHHHHHHHHHHHH	49.09	21890473
136	Methylation	VAKAYQDRYQDLGAY HHHHHHHHHHHHHHH	18.58	115484717
137	Phosphorylation	AKAYQDRYQDLGAYS HHHHHHHHHHHHHHH	18.05	26074081
143	Phosphorylation	RYQDLGAYSSARKCL HHHHHHHHHHHHHHH	11.02	21082442
144	Phosphorylation	YQDLGAYSSARKCLA HHHHHHHHHHHHHHH	19.58	25159151
145	Phosphorylation	QDLGAYSSARKCLAK HHHHHHHHHHHHHHH	21.29	25159151
148	Ubiquitination	GAYSSARKCLAKQRQ HHHHHHHHHHHHHHH	33.06	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of NDUBA_HUMAN !!

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NDUBA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NDUBB_HUMAN	NDUFB11	physical	22939629
NDUV1_HUMAN	NDUFV1	physical	22939629
NDUS7_HUMAN	NDUFS7	physical	22939629
NDUS1_HUMAN	NDUFS1	physical	22939629
RM13_HUMAN	MRPL13	physical	22939629
FAM9B_HUMAN	FAM9B	physical	25416956
ATPO_HUMAN	ATP5O	physical	26344197
BAP31_HUMAN	BCAP31	physical	26344197
RT07_HUMAN	MRPS7	physical	26344197
NDUS1_HUMAN	NDUFS1	physical	26344197
NDUV2_HUMAN	NDUFV2	physical	26344197
TPM1_HUMAN	TPM1	physical	26344197
TPM2_HUMAN	TPM2	physical	26344197
TPM3_HUMAN	TPM3	physical	26344197
TPM4_HUMAN	TPM4	physical	26344197

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-56 AND TYR-143, AND MASSSPECTROMETRY.
PubMed: 18083107