UniProt ID | QCR7_HUMAN | |
---|---|---|
UniProt AC | P14927 | |
Protein Name | Cytochrome b-c1 complex subunit 7 | |
Gene Name | UQCRB | |
Organism | Homo sapiens (Human). | |
Sequence Length | 111 | |
Subcellular Localization | Mitochondrion inner membrane. | |
Protein Description | This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This component is involved in redox-linked proton pumping.. | |
Protein Sequence | MAGKQAVSASGKWLDGIRKWYYNAAGFNKLGLMRDDTIYEDEDVKEAIRRLPENLYNDRMFRIKRALDLNLKHQILPKEQWTKYEEENFYLEPYLKEVIRERKEREEWAKK | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MAGKQAVSA ------CCCCHHHCC | 33.61 | - | |
4 | Acetylation | ----MAGKQAVSASG ----CCCCHHHCCCC | 26.08 | 20167786 | |
4 | Ubiquitination | ----MAGKQAVSASG ----CCCCHHHCCCC | 26.08 | 33845483 | |
8 | Phosphorylation | MAGKQAVSASGKWLD CCCCHHHCCCCCHHH | 21.52 | 21712546 | |
10 | Phosphorylation | GKQAVSASGKWLDGI CCHHHCCCCCHHHHH | 33.14 | 21712546 | |
12 | Acetylation | QAVSASGKWLDGIRK HHHCCCCCHHHHHHH | 41.93 | 23236377 | |
12 | Succinylation | QAVSASGKWLDGIRK HHHCCCCCHHHHHHH | 41.93 | - | |
12 | Ubiquitination | QAVSASGKWLDGIRK HHHCCCCCHHHHHHH | 41.93 | 21890473 | |
12 | Ubiquitination | QAVSASGKWLDGIRK HHHCCCCCHHHHHHH | 41.93 | 21890473 | |
12 | Succinylation | QAVSASGKWLDGIRK HHHCCCCCHHHHHHH | 41.93 | 21890473 | |
13 | Ubiquitination | AVSASGKWLDGIRKW HHCCCCCHHHHHHHH | 11.83 | 22817900 | |
19 | Acetylation | KWLDGIRKWYYNAAG CHHHHHHHHHHCCCC | 37.31 | 25825284 | |
19 | Succinylation | KWLDGIRKWYYNAAG CHHHHHHHHHHCCCC | 37.31 | 23954790 | |
19 | Malonylation | KWLDGIRKWYYNAAG CHHHHHHHHHHCCCC | 37.31 | 26320211 | |
21 | Phosphorylation | LDGIRKWYYNAAGFN HHHHHHHHHCCCCCH | 7.00 | - | |
29 | Ubiquitination | YNAAGFNKLGLMRDD HCCCCCHHCCCCCCC | 41.49 | 21890473 | |
29 | Ubiquitination | YNAAGFNKLGLMRDD HCCCCCHHCCCCCCC | 41.49 | 21906983 | |
37 | Phosphorylation | LGLMRDDTIYEDEDV CCCCCCCCCCCCHHH | 29.73 | - | |
39 | Phosphorylation | LMRDDTIYEDEDVKE CCCCCCCCCCHHHHH | 21.30 | 27642862 | |
40 | Ubiquitination | MRDDTIYEDEDVKEA CCCCCCCCCHHHHHH | 51.58 | 23503661 | |
45 | Acetylation | IYEDEDVKEAIRRLP CCCCHHHHHHHHHCC | 54.47 | 26822725 | |
45 | Ubiquitination | IYEDEDVKEAIRRLP CCCCHHHHHHHHHCC | 54.47 | 21906983 | |
45 | 2-Hydroxyisobutyrylation | IYEDEDVKEAIRRLP CCCCHHHHHHHHHCC | 54.47 | - | |
46 | Acetylation | YEDEDVKEAIRRLPE CCCHHHHHHHHHCCH | 49.53 | 19608861 | |
46 | Ubiquitination | YEDEDVKEAIRRLPE CCCHHHHHHHHHCCH | 49.53 | 23503661 | |
51 | Ubiquitination | VKEAIRRLPENLYND HHHHHHHCCHHHHCC | 4.48 | 23503661 | |
56 | Phosphorylation | RRLPENLYNDRMFRI HHCCHHHHCCHHHHH | 26.97 | - | |
59 | Methylation | PENLYNDRMFRIKRA CHHHHCCHHHHHHHH | 23.62 | 115919541 | |
64 | Ubiquitination | NDRMFRIKRALDLNL CCHHHHHHHHHCCCC | 27.62 | 23503661 | |
72 | Ubiquitination | RALDLNLKHQILPKE HHHCCCCCCCCCCHH | 32.18 | 23503661 | |
72 | Acetylation | RALDLNLKHQILPKE HHHCCCCCCCCCCHH | 32.18 | 25825284 | |
78 | Acetylation | LKHQILPKEQWTKYE CCCCCCCHHHHCCHH | 60.12 | 23954790 | |
78 | Succinylation | LKHQILPKEQWTKYE CCCCCCCHHHHCCHH | 60.12 | - | |
78 | Succinylation | LKHQILPKEQWTKYE CCCCCCCHHHHCCHH | 60.12 | 23954790 | |
78 | Ubiquitination | LKHQILPKEQWTKYE CCCCCCCHHHHCCHH | 60.12 | 19608861 | |
83 | Ubiquitination | LPKEQWTKYEEENFY CCHHHHCCHHHHCCC | 47.94 | 23503661 | |
83 | Acetylation | LPKEQWTKYEEENFY CCHHHHCCHHHHCCC | 47.94 | 25038526 | |
90 | Phosphorylation | KYEEENFYLEPYLKE CHHHHCCCHHHHHHH | 23.03 | 27642862 | |
94 | Phosphorylation | ENFYLEPYLKEVIRE HCCCHHHHHHHHHHH | 22.49 | - | |
96 | Ubiquitination | FYLEPYLKEVIRERK CCHHHHHHHHHHHHH | 44.05 | 23503661 | |
96 | Acetylation | FYLEPYLKEVIRERK CCHHHHHHHHHHHHH | 44.05 | 23236377 | |
96 | Succinylation | FYLEPYLKEVIRERK CCHHHHHHHHHHHHH | 44.05 | 23954790 | |
110 | Acetylation | KEREEWAKK------ HHHHHHHHC------ | 61.15 | 6572095 | |
110 | Succinylation | KEREEWAKK------ HHHHHHHHC------ | 61.15 | 23954790 | |
111 | Acetylation | EREEWAKK------- HHHHHHHC------- | 58.80 | 5643605 |
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 QCR7_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of QCR7_HUMAN !! |
* 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 QCR7_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
H00473 | Mitochondrial respiratory chain deficiencies (MRCD), including: Mitochondrial complex I deficiency ( | |||||
OMIM Disease | ||||||
615158 | Mitochondrial complex III deficiency, nuclear 3 (MC3DN3) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78, AND MASS SPECTROMETRY. |