UniProt ID | GCDH_MOUSE | |
---|---|---|
UniProt AC | Q60759 | |
Protein Name | Glutaryl-CoA dehydrogenase, mitochondrial | |
Gene Name | Gcdh | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 438 | |
Subcellular Localization | Mitochondrion matrix. | |
Protein Description | Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor.. | |
Protein Sequence | MSLRGVSARLLSRRSGLRFPRFPRTWSSAAAHTEKTQIRPAKSSRPVFDWKDPLILEEQLTADEKLIRDTFRNYCQERLMSRILLANRNEVFHRDIVYEMGELGVLGPTIKGYGCAGVSSVAYGLLTRELERVDSGYRSMMSVQSSLVMHPIYTYGSEEQRQKYLPGLAKGELLGCFGLTEPNHGSDPGGMETRARHNPSNQSYTLSGTKTWITNSPVADLFIVWARCEDNCIRGFILEKGMRGLSAPRIEGKFSLRASATGMIIMDSVEVPEENVLPNVSSLAGPFGCLNTARYGITWGVLGAAEFCLHTARQYALDRIQFGVPLARNQLVQKKLADMLTEITLGLHACLQLGRLKDQDKATPEMVSMLKRNNCGKALDIARQARDILGGNGISDEYHVIRHAMNLEAVNTYEGTHDIHALILGRAITGIQAFTVGK | |
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 |
---|---|---|---|---|---|
35 | Acetylation | SAAAHTEKTQIRPAK CCCCCCCCCCCCCCC | 47.05 | 23576753 | |
43 | Phosphorylation | TQIRPAKSSRPVFDW CCCCCCCCCCCCCCC | 33.41 | 23140645 | |
44 | Phosphorylation | QIRPAKSSRPVFDWK CCCCCCCCCCCCCCC | 39.64 | 23140645 | |
51 | Acetylation | SRPVFDWKDPLILEE CCCCCCCCCCCHHHH | 51.84 | 23576753 | |
51 | Succinylation | SRPVFDWKDPLILEE CCCCCCCCCCCHHHH | 51.84 | 23806337 | |
51 | Succinylation | SRPVFDWKDPLILEE CCCCCCCCCCCHHHH | 51.84 | - | |
65 | Acetylation | EQLTADEKLIRDTFR HHCCCCHHHHHHHHH | 50.16 | 23576753 | |
115 | S-palmitoylation | PTIKGYGCAGVSSVA CCCCCCCCCCHHHHH | 1.93 | 28526873 | |
163 | Acetylation | GSEEQRQKYLPGLAK CCHHHHHHHCCCCCC | 51.44 | 23576753 | |
170 | Acetylation | KYLPGLAKGELLGCF HHCCCCCCCCEEEEE | 58.94 | 23864654 | |
176 | S-nitrosocysteine | AKGELLGCFGLTEPN CCCCEEEEEECCCCC | 2.17 | - | |
176 | S-nitrosylation | AKGELLGCFGLTEPN CCCCEEEEEECCCCC | 2.17 | 21278135 | |
176 | S-palmitoylation | AKGELLGCFGLTEPN CCCCEEEEEECCCCC | 2.17 | 28526873 | |
200 | Phosphorylation | TRARHNPSNQSYTLS CCCCCCCCCCCEEEE | 53.47 | 29472430 | |
240 | Acetylation | IRGFILEKGMRGLSA EEHHHHHCCCCCCCC | 55.34 | 23576753 | |
240 | Succinylation | IRGFILEKGMRGLSA EEHHHHHCCCCCCCC | 55.34 | 23806337 | |
253 | Acetylation | SAPRIEGKFSLRASA CCCCEECCEEECCCC | 20.99 | 23576753 | |
289 | S-palmitoylation | SLAGPFGCLNTARYG HHCCCCCHHHHHHHC | 2.44 | 28526873 | |
334 | Acetylation | ARNQLVQKKLADMLT HHHHHHHHHHHHHHH | 42.13 | 23864654 | |
357 | Acetylation | CLQLGRLKDQDKATP HHHHCCCCCCCCCCH | 52.57 | 23864654 | |
361 | Acetylation | GRLKDQDKATPEMVS CCCCCCCCCCHHHHH | 48.83 | 23864654 | |
371 | Succinylation | PEMVSMLKRNNCGKA HHHHHHHHHCCHHHH | 44.42 | 23954790 | |
371 | Acetylation | PEMVSMLKRNNCGKA HHHHHHHHHCCHHHH | 44.42 | 23864654 | |
438 | Succinylation | IQAFTVGK------- EEEEECCC------- | 53.48 | 24315375 | |
438 | Acetylation | IQAFTVGK------- EEEEECCC------- | 53.48 | 23864654 |
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 GCDH_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GCDH_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 GCDH_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of GCDH_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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