UniProt ID | HMGCL_MOUSE | |
---|---|---|
UniProt AC | P38060 | |
Protein Name | Hydroxymethylglutaryl-CoA lyase, mitochondrial | |
Gene Name | Hmgcl | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 325 | |
Subcellular Localization | Mitochondrion matrix . Peroxisome . Unprocessed form is peroxisomal. | |
Protein Description | Key enzyme in ketogenesis (ketone body formation). Terminal step in leucine catabolism. Ketone bodies (beta-hydroxybutyrate, acetoacetate and acetone) are essential as an alternative source of energy to glucose, as lipid precursors and as regulators of metabolism (By similarity).. | |
Protein Sequence | MASVRKAFPRRLVGLTSLRAVSTSSMGTLPKQVKIVEVGPRDGLQNEKSIVPTPVKIRLIDMLSEAGLPVIEATSFVSPKWVPQMADHSDVLKGIQKFPGINYPVLTPNMKGFEEAVAAGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRGYVSCALGCPYEGKVSPAKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGGCPYAKGASGNLATEDLVYMLNGLGIHTGVNLQKLLEAGDFICQALNRKTSSKVAQATCKL | |
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 |
---|---|---|---|---|---|
17 | Phosphorylation | RRLVGLTSLRAVSTS HHHHCHHHEEEEECC | 22.39 | 27600695 | |
31 | Ubiquitination | SSMGTLPKQVKIVEV CCCCCCCCEEEEEEE | 71.48 | 27667366 | |
48 | Succinylation | RDGLQNEKSIVPTPV CCCCCCCCCCCCCCC | 53.70 | - | |
48 | Glutarylation | RDGLQNEKSIVPTPV CCCCCCCCCCCCCCC | 53.70 | 24703693 | |
48 | Malonylation | RDGLQNEKSIVPTPV CCCCCCCCCCCCCCC | 53.70 | 26320211 | |
48 | Succinylation | RDGLQNEKSIVPTPV CCCCCCCCCCCCCCC | 53.70 | 23806337 | |
48 | Acetylation | RDGLQNEKSIVPTPV CCCCCCCCCCCCCCC | 53.70 | 23806337 | |
56 | Ubiquitination | SIVPTPVKIRLIDML CCCCCCCCHHHHHHH | 24.26 | 27667366 | |
80 | Acetylation | ATSFVSPKWVPQMAD ECCCCCCCCCCCCCC | 54.00 | 23576753 | |
93 | Acetylation | ADHSDVLKGIQKFPG CCHHHHHHHHHHCCC | 54.54 | 23864654 | |
97 | Ubiquitination | DVLKGIQKFPGINYP HHHHHHHHCCCCCCC | 52.16 | 22790023 | |
111 | Succinylation | PVLTPNMKGFEEAVA CCCCCCCCCHHHHHH | 68.06 | 24315375 | |
111 | Acetylation | PVLTPNMKGFEEAVA CCCCCCCCCHHHHHH | 68.06 | 23576753 | |
137 | Succinylation | VSELFTRKNANCSIE HHHHHHHCCCCCCHH | 58.30 | - | |
137 | Glutarylation | VSELFTRKNANCSIE HHHHHHHCCCCCCHH | 58.30 | 24703693 | |
137 | Malonylation | VSELFTRKNANCSIE HHHHHHHCCCCCCHH | 58.30 | 26320211 | |
137 | Succinylation | VSELFTRKNANCSIE HHHHHHHCCCCCCHH | 58.30 | 23806337 | |
137 | Acetylation | VSELFTRKNANCSIE HHHHHHHCCCCCCHH | 58.30 | 23576753 | |
137 | Ubiquitination | VSELFTRKNANCSIE HHHHHHHCCCCCCHH | 58.30 | - | |
141 | S-palmitoylation | FTRKNANCSIEESFQ HHHCCCCCCHHHHHH | 3.94 | 28526873 | |
141 | S-nitrosylation | FTRKNANCSIEESFQ HHHCCCCCCHHHHHH | 3.94 | 22178444 | |
141 | S-nitrosocysteine | FTRKNANCSIEESFQ HHHCCCCCCHHHHHH | 3.94 | - | |
170 | S-palmitoylation | SVRGYVSCALGCPYE CCCCCHHHHCCCCCC | 2.30 | 28526873 | |
174 | S-palmitoylation | YVSCALGCPYEGKVS CHHHHCCCCCCCCCC | 3.18 | 28526873 | |
179 | Succinylation | LGCPYEGKVSPAKVA CCCCCCCCCCHHHHH | 27.83 | - | |
179 | Malonylation | LGCPYEGKVSPAKVA CCCCCCCCCCHHHHH | 27.83 | 26320211 | |
179 | Acetylation | LGCPYEGKVSPAKVA CCCCCCCCCCHHHHH | 27.83 | 23576753 | |
179 | Succinylation | LGCPYEGKVSPAKVA CCCCCCCCCCHHHHH | 27.83 | 23806337 | |
190 | Acetylation | AKVAEVAKKLYSMGC HHHHHHHHHHHHCCC | 48.78 | 23864654 | |
190 | Succinylation | AKVAEVAKKLYSMGC HHHHHHHHHHHHCCC | 48.78 | 23954790 | |
191 | Acetylation | KVAEVAKKLYSMGCY HHHHHHHHHHHCCCE | 42.81 | 7625235 | |
307 | S-nitrosocysteine | LEAGDFICQALNRKT HHHHHHHHHHHCCCC | 1.63 | - | |
307 | S-nitrosylation | LEAGDFICQALNRKT HHHHHHHHHHHCCCC | 1.63 | 22178444 | |
307 | S-palmitoylation | LEAGDFICQALNRKT HHHHHHHHHHHCCCC | 1.63 | 28526873 | |
323 | Glutathionylation | SKVAQATCKL----- HHHHHHHHCC----- | 4.78 | 24333276 | |
324 | Malonylation | KVAQATCKL------ HHHHHHHCC------ | 53.53 | 26320211 | |
324 | Glutarylation | KVAQATCKL------ HHHHHHHCC------ | 53.53 | 24703693 | |
324 | Acetylation | KVAQATCKL------ HHHHHHHCC------ | 53.53 | 23576753 |
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 HMGCL_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HMGCL_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 HMGCL_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of HMGCL_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-48, AND MASS SPECTROMETRY. |