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Primary Information | |
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| BoMiProt ID | Bomi7941 |
| Protein Name | Phosphatidylinositol 4-kinase beta/PI4K-beta/PtdIns 4-kinase beta |
| Organism | Bos taurus |
| Uniprot ID | O02810 |
| Milk Fraction | Whey |
| Ref Sequence ID | NP_777208.1 |
| Aminoacid Length | 816 |
| Molecular Weight | 91375 |
| FASTA Sequence | Download |
| Gene Name | PI4KB/PIK4CB |
| Gene ID | 286846 |
| Protein Existence Status | reviewed |
Secondary Information | |
| Protein Function | A subunit of phosphatidylinositol 4-kinase (PI4K) which synthesize phosphatidylinositol 4-phosphate (PI4P).PI4P defines the membranes of Golgi and trans-Golgi network (TGN) and regulates trafficking to and from the Golgi. |
| Biochemical Properties | PI4K IIβ has an unstructured N-terminus but without the flexible helix. The hallmark of type II kinase domain is the CCPCC motif that is palmitoylated in vivo when the kinase is active. PI4K IIIβ has a helical domain in front of the kinase domain.contains three disordered regions; the very N-terminus that binds the ACBD3 protein, a disordered loop between the helical and kinase domain that has a binding site for the 14-3-3 proteins and a disordered loop within the N-lobe of the kinase domain. |
| PTMs | Acetylation and phosphorylation |
| Significance of PTMs | phosphorylation of Ser258 and Ser266 was shown to be important for Golgi recruitment of PI4KIIIβ.phosphorylation of PI4KIIIβ at Ser268 by protein kinase D (PKD) has shown to be essential for its kinase activity and its ability to support post-Golgi transport.Besides PKD, other kinases can phosphorylate PI4KIIIβ such as proline directed cyclin-dependent protein kinases (like cdc2), cyclic monophosphate-dependent protein kinases (protein kinase A/G), Ca2+/calmodulin-dependent protein kinase, casein kinase II or cyclin-dependent kinases. |
| PDB ID | 5EUQ, |
| Linking IDs | Bomi7941 |
| Bibliography | 1.Delang, L., Paeshuyse, J., & Neyts, J. (2012). The role of phosphatidylinositol 4-kinases and phosphatidylinositol 4-phosphate during viral replication. Biochemical pharmacology, 84(11), 1400–1408. https://doi.org/10.1016/j.bcp.2012.07.034 2.Boura E, Nencka R. Phosphatidylinositol 4-kinases: Function, structure, and inhibition. Exp Cell Res. 2015 Oct 1;337(2):136-45. doi: 10.1016/j.yexcr.2015.03.028. Epub 2015 Jul 14. Erratum in: Exp Cell Res. 2016 Feb 1;341(1):110. Erratum in: Exp Cell Res. 2016 Feb 1;341(1):110. PMID: 26183104. |
| Protein Function | A subunit of phosphatidylinositol 4-kinase (PI4K) which synthesize phosphatidylinositol 4-phosphate (PI4P).PI4P defines the membranes of Golgi and trans-Golgi network (TGN) and regulates trafficking to and from the Golgi. |
| Biochemical Properties | PI4K IIβ has an unstructured N-terminus but without the flexible helix. The hallmark of type II kinase domain is the CCPCC motif that is palmitoylated in vivo when the kinase is active. PI4K IIIβ has a helical domain in front of the kinase domain.contains three disordered regions; the very N-terminus that binds the ACBD3 protein, a disordered loop between the helical and kinase domain that has a binding site for the 14-3-3 proteins and a disordered loop within the N-lobe of the kinase domain. |
| PTMs | Acetylation and phosphorylation |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | >sp|O02810|PI4KB_BOVIN Phosphatidylinositol 4-kinase beta OS=Bos taurus OX=9913 GN=PI4KB PE=1 SV=2 MGDTIVEPAPLKPTSEPAPGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVK LLHGGVAISSRGTPLELVNGDGVDSEIRCLDDPPAQIREEEDEMGATVASGTAKGARRRR QNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLL NMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLI LSDELKPAHRKRELPSLS*258PAPDT*263GLS*266PSKRTHQRS*275KS*277DATASIS*284LSSNLKRTAS*294NPKVENEDEELSSSTESIDNSFSSPVRLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLN HKLPARVWLPTAGFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFDTTSVPARIPE NRIRSTRS*428VENLPECGIT*438HEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEVHTNSCD NISQFSVDSITSQESKEPVFIAAGDIRRRLS*511EQLAHT*517PT*519AFKRDPEDPSAVALKEPWQEK VRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKI LVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGY CLGCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGG LDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMSM TEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM |
| CATH | Matched CATH superfamily 3.40.50.300 |
| Predicted Disorder Regions | 1-29, 85-118, 228-312, 431-458 |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| Significance of PTMs | phosphorylation of Ser258 and Ser266 was shown to be important for Golgi recruitment of PI4KIIIβ.phosphorylation of PI4KIIIβ at Ser268 by protein kinase D (PKD) has shown to be essential for its kinase activity and its ability to support post-Golgi transport.Besides PKD, other kinases can phosphorylate PI4KIIIβ such as proline directed cyclin-dependent protein kinases (like cdc2), cyclic monophosphate-dependent protein kinases (protein kinase A/G), Ca2+/calmodulin-dependent protein kinase, casein kinase II or cyclin-dependent kinases. |
| PDB ID | 5EUQ, |
| Linking IDs | |
| Bibliography | 1.Delang, L., Paeshuyse, J., & Neyts, J. (2012). The role of phosphatidylinositol 4-kinases and phosphatidylinositol 4-phosphate during viral replication. Biochemical pharmacology, 84(11), 1400–1408. https://doi.org/10.1016/j.bcp.2012.07.034 2.Boura E, Nencka R. Phosphatidylinositol 4-kinases: Function, structure, and inhibition. Exp Cell Res. 2015 Oct 1;337(2):136-45. doi: 10.1016/j.yexcr.2015.03.028. Epub 2015 Jul 14. Erratum in: Exp Cell Res. 2016 Feb 1;341(1):110. Erratum in: Exp Cell Res. 2016 Feb 1;341(1):110. PMID: 26183104. |