UniProt ID | LDHB_RAT | |
---|---|---|
UniProt AC | P42123 | |
Protein Name | L-lactate dehydrogenase B chain | |
Gene Name | Ldhb | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 334 | |
Subcellular Localization | Cytoplasm. | |
Protein Description | ||
Protein Sequence | MATLKEKLIAPVADDETAVPNNKITVVGVGQVGMACAISILGKSLADELALVDVLEDKLKGEMMDLQHGSLFLQTPKIVADKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKFIIPQIVKYSPDCTIIVVSNPVDILTYVTWKLSGLPKHRVIGSGCNLDSARFRYLMAEKLGIHPSSCHGWILGEHGDSSVAVWSGVNVAGVSLQELNPEMGTDNDSENWKEVHKMVVDSAYEVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVKGMYGIENEVFLSLPCILNARGLTSVINQKLKDDEVAQLRKSADTLWDIQKDLKDL | |
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 | ------MATLKEKLI ------CCCHHHHHC | 22.95 | - | |
5 | Acetylation | ---MATLKEKLIAPV ---CCCHHHHHCCCC | 48.74 | - | |
7 | Acetylation | -MATLKEKLIAPVAD -CCCHHHHHCCCCCC | 43.54 | 22902405 | |
7 | Ubiquitination | -MATLKEKLIAPVAD -CCCHHHHHCCCCCC | 43.54 | - | |
17 | Phosphorylation | APVADDETAVPNNKI CCCCCCCCCCCCCEE | 39.69 | 22673903 | |
44 | Phosphorylation | AISILGKSLADELAL HHHHHCHHHHHHHHH | 27.30 | 22673903 | |
58 | "N6,N6-dimethyllysine" | LVDVLEDKLKGEMMD HHHHHHHHHCCCCEE | 42.60 | - | |
58 | Acetylation | LVDVLEDKLKGEMMD HHHHHHHHHCCCCEE | 42.60 | 22902405 | |
58 | Methylation | LVDVLEDKLKGEMMD HHHHHHHHHCCCCEE | 42.60 | 12692561 | |
60 | "N6,N6-dimethyllysine" | DVLEDKLKGEMMDLQ HHHHHHHCCCCEECC | 59.57 | - | |
60 | Acetylation | DVLEDKLKGEMMDLQ HHHHHHHCCCCEECC | 59.57 | 22902405 | |
60 | Methylation | DVLEDKLKGEMMDLQ HHHHHHHCCCCEECC | 59.57 | 12692561 | |
82 | Acetylation | TPKIVADKDYSVTAN CCCEEECCCCEEECC | 49.15 | 22902405 | |
84 | Phosphorylation | KIVADKDYSVTANSK CEEECCCCEEECCCE | 15.69 | - | |
85 | Phosphorylation | IVADKDYSVTANSKI EEECCCCEEECCCEE | 24.11 | 29779826 | |
91 | Acetylation | YSVTANSKIVVVTAG CEEECCCEEEEEEEC | 39.05 | 26302492 | |
119 | Acetylation | QRNVNVFKFIIPQIV HHHHCCHHHHHHHHH | 31.22 | 22902405 | |
127 | Acetylation | FIIPQIVKYSPDCTI HHHHHHHHCCCCCEE | 41.46 | - | |
233 | Acetylation | ENWKEVHKMVVDSAY CCHHHHHHHHHHHHH | 38.27 | 22902405 | |
240 | Phosphorylation | KMVVDSAYEVIKLKG HHHHHHHHHHHHCCC | 18.06 | - | |
244 | Acetylation | DSAYEVIKLKGYTNW HHHHHHHHCCCCCCC | 49.69 | 22902405 | |
244 | Ubiquitination | DSAYEVIKLKGYTNW HHHHHHHHCCCCCCC | 49.69 | - | |
308 | Acetylation | LTSVINQKLKDDEVA HHHHHCHHCCCCHHH | 53.68 | 22902405 | |
308 | Ubiquitination | LTSVINQKLKDDEVA HHHHHCHHCCCCHHH | 53.68 | - | |
310 | Acetylation | SVINQKLKDDEVAQL HHHCHHCCCCHHHHH | 70.89 | 22902405 | |
310 | Ubiquitination | SVINQKLKDDEVAQL HHHCHHCCCCHHHHH | 70.89 | - | |
319 | Acetylation | DEVAQLRKSADTLWD CHHHHHHHHHHHHHH | 59.60 | 22902405 | |
329 | Acetylation | DTLWDIQKDLKDL-- HHHHHHHHHHHCC-- | 66.42 | 22902405 | |
329 | Ubiquitination | DTLWDIQKDLKDL-- HHHHHHHHHHHCC-- | 66.42 | - | |
332 | Acetylation | WDIQKDLKDL----- HHHHHHHHCC----- | 68.09 | 22902405 | |
332 | Ubiquitination | WDIQKDLKDL----- HHHHHHHHCC----- | 68.09 | - |
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 LDHB_RAT !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LDHB_RAT !! |
* 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 LDHB_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of LDHB_RAT !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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