UniProt ID | NDUS1_MOUSE | |
---|---|---|
UniProt AC | Q91VD9 | |
Protein Name | NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial | |
Gene Name | Ndufs1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 727 | |
Subcellular Localization | Mitochondrion inner membrane. Matrix and cytoplasmic side of the mitochondrial inner membrane.. | |
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). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized (By similarity).. | |
Protein Sequence | MLRIPIKRALIGLSNSPKGYVRTTGTAASNLIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGSDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELSGNVIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQRLTEPMVRNEKGLLTYTSWEDALSRVAGMLQNFEGNAVAAIAGGLVDAEALVALKDLLNKVDSDNLCTEEIFPTEGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALIGSPVDLTYRYDHLGDSPKILQDIASGRHSFCEVLKDAKKPMVVLGSSALQRDDGAAILVAVSNMVQKIRVTTGVAAEWKVMNILHRIASQVAALDLGYKPGVEAIRKNPPKMLFLLGADGGCITRQDLPKDCFIVYQGHHGDVGAPMADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIAGITLPYDTLDQVRNRLEEVSPNLVRYDDIEETNYFQQASELAKLVNQEVLADPLVPPQLTIKDFYMTDSISRASQTMAKCVKAVTEGAQAVEEPSIC | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
64 | S-nitrosylation | GMQIPRFCYHERLSV CCCCCCCCCCCCCCC | 3.41 | 21278135 | |
64 | S-nitrosocysteine | GMQIPRFCYHERLSV CCCCCCCCCCCCCCC | 3.41 | - | |
64 | S-palmitoylation | GMQIPRFCYHERLSV CCCCCCCCCCCCCCC | 3.41 | 26165157 | |
75 | S-nitrosocysteine | RLSVAGNCRMCLVEI CCCCCCCCEEEEEEH | 2.61 | - | |
75 | S-nitrosylation | RLSVAGNCRMCLVEI CCCCCCCCEEEEEEH | 2.61 | 21278135 | |
75 | S-palmitoylation | RLSVAGNCRMCLVEI CCCCCCCCEEEEEEH | 2.61 | 28526873 | |
75 | Glutathionylation | RLSVAGNCRMCLVEI CCCCCCCCEEEEEEH | 2.61 | 24333276 | |
78 | S-palmitoylation | VAGNCRMCLVEIEKA CCCCCEEEEEEHHHC | 1.67 | 28526873 | |
78 | Glutathionylation | VAGNCRMCLVEIEKA CCCCCEEEEEEHHHC | 1.67 | 24333276 | |
84 | Acetylation | MCLVEIEKAPKVVAA EEEEEHHHCCHHHHH | 75.54 | 23576753 | |
84 | Malonylation | MCLVEIEKAPKVVAA EEEEEHHHCCHHHHH | 75.54 | 26320211 | |
84 | Succinylation | MCLVEIEKAPKVVAA EEEEEHHHCCHHHHH | 75.54 | 23806337 | |
92 | S-nitrosylation | APKVVAACAMPVMKG CCHHHHHHHCCCCCC | 2.10 | 21278135 | |
92 | S-nitrosocysteine | APKVVAACAMPVMKG CCHHHHHHHCCCCCC | 2.10 | - | |
92 | S-palmitoylation | APKVVAACAMPVMKG CCHHHHHHHCCCCCC | 2.10 | 28526873 | |
98 | Acetylation | ACAMPVMKGWNILTN HHHCCCCCCCHHCCC | 62.09 | 23864654 | |
98 | Succinylation | ACAMPVMKGWNILTN HHHCCCCCCCHHCCC | 62.09 | 24315375 | |
108 | Acetylation | NILTNSEKSKKAREG HHCCCCHHHHHHHHH | 68.35 | 23864654 | |
170 | Ubiquitination | KNIGPLVKTIMTRCI CCHHHHHHHHHHHHH | 39.76 | - | |
170 | Acetylation | KNIGPLVKTIMTRCI CCHHHHHHHHHHHHH | 39.76 | 24062335 | |
236 | Phosphorylation | GALTSKPYAFTARPW CHHCCCCEEEECCCC | 20.34 | - | |
248 | Phosphorylation | RPWETRKTESIDVMD CCCCCCCCCCCEEEH | 31.51 | 30635358 | |
250 | Phosphorylation | WETRKTESIDVMDAV CCCCCCCCCEEEHHC | 29.35 | 20495213 | |
259 | Phosphorylation | DVMDAVGSNIVVSTR EEEHHCCCCEEEECC | 19.45 | 30635358 | |
264 | Phosphorylation | VGSNIVVSTRTGEVM CCCCEEEECCCHHHH | 10.98 | 30635358 | |
265 | Phosphorylation | GSNIVVSTRTGEVMR CCCEEEECCCHHHHH | 22.20 | 30635358 | |
267 | Phosphorylation | NIVVSTRTGEVMRIL CEEEECCCHHHHHHH | 37.47 | 30635358 | |
298 | Ubiquitination | RFAYDGLKRQRLTEP HHCCCCHHHCCCCCC | 52.60 | - | |
298 | Acetylation | RFAYDGLKRQRLTEP HHCCCCHHHCCCCCC | 52.60 | 24062335 | |
311 | Succinylation | EPMVRNEKGLLTYTS CCCCCCCCCCEEECC | 59.41 | 26388266 | |
311 | Ubiquitination | EPMVRNEKGLLTYTS CCCCCCCCCCEEECC | 59.41 | - | |
311 | Acetylation | EPMVRNEKGLLTYTS CCCCCCCCCCEEECC | 59.41 | 23864654 | |
367 | S-palmitoylation | KVDSDNLCTEEIFPT HCCCCCCCCCCCCCC | 5.88 | 28526873 | |
367 | S-nitrosocysteine | KVDSDNLCTEEIFPT HCCCCCCCCCCCCCC | 5.88 | - | |
367 | S-nitrosylation | KVDSDNLCTEEIFPT HCCCCCCCCCCCCCC | 5.88 | 21278135 | |
448 | Phosphorylation | RYDHLGDSPKILQDI ECCCCCCCHHHHHHH | 26.71 | 27841257 | |
450 | Acetylation | DHLGDSPKILQDIAS CCCCCCHHHHHHHHC | 61.06 | 23864654 | |
450 | Succinylation | DHLGDSPKILQDIAS CCCCCCHHHHHHHHC | 61.06 | 23806337 | |
457 | Phosphorylation | KILQDIASGRHSFCE HHHHHHHCCCCCHHH | 36.37 | 23140645 | |
461 | Phosphorylation | DIASGRHSFCEVLKD HHHCCCCCHHHHHHH | 30.17 | 26745281 | |
463 | S-nitrosylation | ASGRHSFCEVLKDAK HCCCCCHHHHHHHCC | 3.86 | 21278135 | |
463 | S-palmitoylation | ASGRHSFCEVLKDAK HCCCCCHHHHHHHCC | 3.86 | 28526873 | |
463 | S-nitrosocysteine | ASGRHSFCEVLKDAK HCCCCCHHHHHHHCC | 3.86 | - | |
467 | Acetylation | HSFCEVLKDAKKPMV CCHHHHHHHCCCCEE | 61.90 | 23576753 | |
470 | Acetylation | CEVLKDAKKPMVVLG HHHHHHCCCCEEEEC | 68.49 | 23201123 | |
499 | Acetylation | AVSNMVQKIRVTTGV EEHHHHHHCCCCCCC | 22.52 | 23576753 | |
531 | Ubiquitination | AALDLGYKPGVEAIR HHHHCCCCCCHHHHH | 33.23 | - | |
539 | Acetylation | PGVEAIRKNPPKMLF CCHHHHHHCCCCEEE | 68.63 | 24062335 | |
543 | Acetylation | AIRKNPPKMLFLLGA HHHHCCCCEEEEEEC | 49.87 | 23864654 | |
554 | S-nitrosylation | LLGADGGCITRQDLP EEECCCCEECCCCCC | 3.34 | 21278135 | |
554 | S-nitrosocysteine | LLGADGGCITRQDLP EEECCCCEECCCCCC | 3.34 | - | |
554 | S-palmitoylation | LLGADGGCITRQDLP EEECCCCEECCCCCC | 3.34 | 28526873 | |
562 | Acetylation | ITRQDLPKDCFIVYQ ECCCCCCCCEEEEEC | 74.54 | 23864654 | |
564 | S-nitrosylation | RQDLPKDCFIVYQGH CCCCCCCEEEEECCC | 2.90 | 21278135 | |
564 | S-nitrosocysteine | RQDLPKDCFIVYQGH CCCCCCCEEEEECCC | 2.90 | - | |
564 | S-palmitoylation | RQDLPKDCFIVYQGH CCCCCCCEEEEECCC | 2.90 | 28680068 | |
611 | Phosphorylation | QQTKVAVTPPGLARE EEEEEEECCCCHHHH | 17.64 | - | |
636 | Nitration | IAGITLPYDTLDQVR HHCCCCCCHHHHHHH | 25.36 | - | |
650 | Phosphorylation | RNRLEEVSPNLVRYD HHHHHHHCCCCCCCC | 16.02 | 25159016 | |
692 | Acetylation | VPPQLTIKDFYMTDS CCCCCEEHHEEECHH | 36.23 | 23954790 | |
692 | Succinylation | VPPQLTIKDFYMTDS CCCCCEEHHEEECHH | 36.23 | 23954790 | |
706 | Phosphorylation | SISRASQTMAKCVKA HHHHHHHHHHHHHHH | 19.32 | 28576409 | |
709 | Succinylation | RASQTMAKCVKAVTE HHHHHHHHHHHHHHH | 28.83 | 23806337 | |
709 | Acetylation | RASQTMAKCVKAVTE HHHHHHHHHHHHHHH | 28.83 | 23576753 | |
710 | S-nitrosocysteine | ASQTMAKCVKAVTEG HHHHHHHHHHHHHHH | 2.49 | - | |
710 | S-nitrosylation | ASQTMAKCVKAVTEG HHHHHHHHHHHHHHH | 2.49 | 21278135 | |
725 | Phosphorylation | AQAVEEPSIC----- HHHHCCCCCC----- | 39.61 | 23140645 | |
727 | S-palmitoylation | AVEEPSIC------- HHCCCCCC------- | 5.53 | 28526873 | |
727 | S-nitrosocysteine | AVEEPSIC------- HHCCCCCC------- | 5.53 | - | |
727 | S-nitrosylation | AVEEPSIC------- HHCCCCCC------- | 5.53 | 21278135 |
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 NDUS1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
84 | K | Acetylation |
| 23576753 |
* 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 NDUS1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of NDUS1_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
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-84, AND MASS SPECTROMETRY. |