UniProt ID | NDUV1_MOUSE | |
---|---|---|
UniProt AC | Q91YT0 | |
Protein Name | NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial | |
Gene Name | Ndufv1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 464 | |
Subcellular Localization |
Mitochondrion inner membrane Peripheral membrane protein Matrix side. |
|
Protein Description | Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for 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 (By similarity).. | |
Protein Sequence | MLAARHFLGGLVPVRVSVRFSSGTTAPKKTSFGSLKDEDRIFTNLYGRHDWRLKGALRRGDWYKTKEILLKGPDWILGEMKTSGLRGRGGAGFPTGLKWSFMNKPSDGRPKYLVVNADEGEPGTCKDREIMRHDPHKLVEGCLVGGRAMGARAAYIYIRGEFYNEASNLQVAIREAYEAGLIGKNACGSDYDFDVFVVRGAGAYICGEETALIESIEGKQGKPRLKPPFPADVGVFGCPTTVANVETVAVSPTICRRGGTWFAGFGRERNSGTKLFNISGHVNHPCTVEEEMSVPLKELIEKHAGGVTGGWDNLLAVIPGGSSTPLIPKSVCETVLMDFDALVQAQTGLGTAAVIVMDRSTDIVKAIARLIEFYKHESCGQCTPCREGVDWMNKVMARFVKGDARPAEIDSLWEISKQIEGHTICALGDGAAWPVQGLIRHFRPELEDRMQRFAQQHRAWQAAS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
30 | Phosphorylation | GTTAPKKTSFGSLKD CCCCCCCCCCCCCCC | 35.10 | 27742792 | |
31 | Phosphorylation | TTAPKKTSFGSLKDE CCCCCCCCCCCCCCC | 36.17 | 27742792 | |
34 | Phosphorylation | PKKTSFGSLKDEDRI CCCCCCCCCCCCCCE | 30.18 | 23737553 | |
36 | Acetylation | KTSFGSLKDEDRIFT CCCCCCCCCCCCEEH | 61.85 | 23864654 | |
36 | Succinylation | KTSFGSLKDEDRIFT CCCCCCCCCCCCEEH | 61.85 | 26388266 | |
54 | Acetylation | GRHDWRLKGALRRGD CCCCHHHCCHHHCCC | 33.30 | 24062335 | |
64 | Acetylation | LRRGDWYKTKEILLK HHCCCCCEEEEHHCC | 49.19 | 23864654 | |
66 | Succinylation | RGDWYKTKEILLKGP CCCCCEEEEHHCCCC | 38.31 | 26388266 | |
66 | Acetylation | RGDWYKTKEILLKGP CCCCCEEEEHHCCCC | 38.31 | 24062335 | |
81 | Succinylation | DWILGEMKTSGLRGR CEECCCCCCCCCCCC | 34.93 | 23806337 | |
81 | Acetylation | DWILGEMKTSGLRGR CEECCCCCCCCCCCC | 34.93 | 23576753 | |
81 | Succinylation | DWILGEMKTSGLRGR CEECCCCCCCCCCCC | 34.93 | - | |
104 | Succinylation | LKWSFMNKPSDGRPK CCEEECCCCCCCCCC | 33.83 | 24315375 | |
104 | Acetylation | LKWSFMNKPSDGRPK CCEEECCCCCCCCCC | 33.83 | 23576753 | |
125 | S-nitrosylation | DEGEPGTCKDREIMR CCCCCCCCCCHHHHH | 5.52 | 21278135 | |
125 | S-palmitoylation | DEGEPGTCKDREIMR CCCCCCCCCCHHHHH | 5.52 | 28526873 | |
125 | S-nitrosocysteine | DEGEPGTCKDREIMR CCCCCCCCCCHHHHH | 5.52 | - | |
137 | Acetylation | IMRHDPHKLVEGCLV HHHCCHHHHCCCCEE | 60.66 | 24062335 | |
142 | S-nitrosocysteine | PHKLVEGCLVGGRAM HHHHCCCCEECCHHH | 1.44 | - | |
142 | S-palmitoylation | PHKLVEGCLVGGRAM HHHHCCCCEECCHHH | 1.44 | 28526873 | |
142 | S-nitrosylation | PHKLVEGCLVGGRAM HHHHCCCCEECCHHH | 1.44 | 22588120 | |
163 | Phosphorylation | IYIRGEFYNEASNLQ EEECCCCCCCCCCHH | 14.06 | - | |
167 | Phosphorylation | GEFYNEASNLQVAIR CCCCCCCCCHHHHHH | 31.71 | - | |
177 | Phosphorylation | QVAIREAYEAGLIGK HHHHHHHHHCCCCCC | 11.10 | - | |
187 | S-nitrosylation | GLIGKNACGSDYDFD CCCCCCCCCCCCCEE | 8.19 | 24895380 | |
187 | S-nitrosocysteine | GLIGKNACGSDYDFD CCCCCCCCCCCCCEE | 8.19 | - | |
187 | S-palmitoylation | GLIGKNACGSDYDFD CCCCCCCCCCCCCEE | 8.19 | 28526873 | |
206 | S-nitrosocysteine | RGAGAYICGEETALI ECCCEEECCCCEEEE | 3.50 | - | |
206 | S-palmitoylation | RGAGAYICGEETALI ECCCEEECCCCEEEE | 3.50 | 28526873 | |
206 | S-nitrosylation | RGAGAYICGEETALI ECCCEEECCCCEEEE | 3.50 | 24895380 | |
226 | Acetylation | KQGKPRLKPPFPADV CCCCCCCCCCCCCCE | 52.50 | 23864654 | |
238 | S-palmitoylation | ADVGVFGCPTTVANV CCEEEECCCCCEECC | 1.51 | 28526873 | |
238 | S-nitrosylation | ADVGVFGCPTTVANV CCEEEECCCCCEECC | 1.51 | 24895380 | |
255 | S-palmitoylation | VAVSPTICRRGGTWF EEECCEEECCCCCEE | 2.39 | 28526873 | |
255 | S-nitrosylation | VAVSPTICRRGGTWF EEECCEEECCCCCEE | 2.39 | 24895380 | |
257 | Methylation | VSPTICRRGGTWFAG ECCEEECCCCCEEEE | 43.40 | 24129315 | |
286 | S-nitrosylation | SGHVNHPCTVEEEMS ECCCCCCCCCCCHHC | 5.31 | 21278135 | |
286 | S-nitrosocysteine | SGHVNHPCTVEEEMS ECCCCCCCCCCCHHC | 5.31 | - | |
308 | Phosphorylation | EKHAGGVTGGWDNLL HHHCCCCCCCHHHEE | 33.00 | - | |
365 | Succinylation | DRSTDIVKAIARLIE ECCHHHHHHHHHHHH | 34.12 | 23954790 | |
365 | Acetylation | DRSTDIVKAIARLIE ECCHHHHHHHHHHHH | 34.12 | 23864654 | |
375 | Acetylation | ARLIEFYKHESCGQC HHHHHHHHHCCCCCC | 46.33 | 23576753 | |
394 | Acetylation | EGVDWMNKVMARFVK HCHHHHHHHHHHHHC | 19.79 | 23864654 | |
401 | Acetylation | KVMARFVKGDARPAE HHHHHHHCCCCCCHH | 48.65 | 24062335 | |
401 | Succinylation | KVMARFVKGDARPAE HHHHHHHCCCCCCHH | 48.65 | 26388266 | |
425 | Glutathionylation | QIEGHTICALGDGAA HHCCCEEEECCCCHH | 2.41 | 24333276 | |
425 | S-nitrosylation | QIEGHTICALGDGAA HHCCCEEEECCCCHH | 2.41 | 21278135 | |
425 | S-palmitoylation | QIEGHTICALGDGAA HHCCCEEEECCCCHH | 2.41 | 28526873 | |
425 | S-nitrosocysteine | QIEGHTICALGDGAA HHCCCEEEECCCCHH | 2.41 | - | |
464 | Phosphorylation | HRAWQAAS------- HHHHHHCC------- | 43.71 | 25521595 |
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 NDUV1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NDUV1_MOUSE !! |
* 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 NDUV1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of NDUV1_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"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-81; LYS-104 AND LYS-375, ANDMASS SPECTROMETRY. |