UniProt ID | PFKAL_RAT | |
---|---|---|
UniProt AC | P30835 | |
Protein Name | ATP-dependent 6-phosphofructokinase, liver type {ECO:0000255|HAMAP-Rule:MF_03184} | |
Gene Name | Pfkl | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 780 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (By similarity). Negatively regulates the phagocyte oxidative burst in response to bacterial infection by controlling cellular NADPH biosynthesis and NADPH oxidase-derived reactive oxygen species. Upon macrophage activation, drives the metabolic switch toward glycolysis, thus preventing glucose turnover that produces NADPH via pentose phosphate pathway (By similarity).. | |
Protein Sequence | MATVDLEKLRMSGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVEGGENIKPANWLSVSNIIQLGGTIIGSARCKAFTTREGRLAAAYNLLQHGITNLCVIGGDGSLTGANIFRNEWGSLLEELVKEGKISESTAQNYAHLSIAGLVGSIDNDFCGTDMTIGTDSALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWENFMCERLGETRSRGSRLNIIIIAEGAIDRHGKPISSSYVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRVLSSKMGMEAVMALLEATPDTPACVVSLSGNQSVRLPLMECVQVTKDVQKAMDEKRFDEAIQLRGRSFENNWKIYKLLAHQKVSKEKSNFSLAILNVGAPAAGMNAAVRSAVRTGISEGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPKPHLEAIVENLRTYNIHALLVIGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLGSDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIHDLKANVEHMTEKMKTDIQRGLVLRNEKCHEHYTTEFLYNLYSSEGRGVFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAMLWMSEKLRDVYRKGRVFANAPDSACVIGLRKKVVAFSSVTELKKETDFEHRMPREQWWLNLRLMLKMLAHYRISMADYVSGELEHVTRRTLSIDKGF | |
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 | ------MATVDLEKL ------CCCCCHHHH | - | ||
8 | Ubiquitination | MATVDLEKLRMSGAG CCCCCHHHHHHCCCC | - | ||
12 | Phosphorylation | DLEKLRMSGAGKAIG CHHHHHHCCCCCEEE | 26022182 | ||
22 | Phosphorylation | GKAIGVLTSGGDAQG CCEEEEEECCCCHHH | 26022182 | ||
23 | Phosphorylation | KAIGVLTSGGDAQGM CEEEEEECCCCHHHH | 26022182 | ||
304 | Phosphorylation | GHVQRGGTPSAFDRV ECHHHCCCCHHHHHH | 25403869 | ||
306 | Phosphorylation | VQRGGTPSAFDRVLS HHHCCCCHHHHHHHH | 22673903 | ||
360 | Acetylation | QVTKDVQKAMDEKRF HHHHHHHHHHHHCCH | 22902405 | ||
365 | Acetylation | VQKAMDEKRFDEAIQ HHHHHHHCCHHHHHH | 22902405 | ||
377 | Phosphorylation | AIQLRGRSFENNWKI HHHHCCCCCCCCHHH | 23984901 | ||
383 | Acetylation | RSFENNWKIYKLLAH CCCCCCHHHHHHHHC | 22902405 | ||
386 | Acetylation | ENNWKIYKLLAHQKV CCCHHHHHHHHCCCC | 22902405 | ||
474 | Acetylation | GTKRTLPKPHLEAIV CCCCCCCCHHHHHHH | 22902405 | ||
529 | O-linked_Glycosylation | CVIPATISNNVPGTD EEEECHHCCCCCCCC | - | ||
640 | Phosphorylation | HYTTEFLYNLYSSEG CCCHHHHHHHHCCCC | - | ||
677 | Acetylation | FDRNYGTKLGVKAML CCCCHHHHHHHHHHH | 22902405 | ||
726 | Acetylation | FSSVTELKKETDFEH EECHHHHHHHCCCCC | 22902405 | ||
773 | Phosphorylation | LEHVTRRTLSIDKGF CEECEEEEEECCCCC | 2539199 | ||
775 | Phosphorylation | HVTRRTLSIDKGF-- ECEEEEEECCCCC-- | 23712012 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
773 | T | Phosphorylation | Kinase | PRKACA | P17612 | GPS |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
529 | S | Oxidation |
| - |
* 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 PFKAL_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of PFKAL_RAT !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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