| UniProt ID | KPBA_DROME | |
|---|---|---|
| UniProt AC | Q9W391 | |
| Protein Name | Probable phosphorylase b kinase regulatory subunit alpha | |
| Gene Name | CG7766 | |
| Organism | Drosophila melanogaster (Fruit fly). | |
| Sequence Length | 1247 | |
| Subcellular Localization |
Cell membrane Lipid-anchor Cytoplasmic side . |
|
| Protein Description | Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin (By similarity).. | |
| Protein Sequence | MRSRSNSGVRLDYYQRIVHRLILAHQEPVTGLFPASNVNSHAWIRDNVYCILAVWGLSMAYKKIADQDEDRAKCYELEQSCVKLMRGLLMAMMNQKDKVEKFKMTQSPYDSLHAKYSSKNGLPVVDDNEWGHLQIDAVSLYLLILAQMTASGLQIVFSLDEVSFIQNLVFYIESAYSIPDYGIWERGDKTNHGEPELNASSIGMAKAALEAMNELDLFGARGGPASVIHVLADEAHKCQAVLQSMLPRESNSKELDSGLLCVIGFPAFAVDDAQLIHNTKDAILSRLQGKYGCKRFLRDGYRTPKEDPSRLYYERWELRMFENIECEWPLFYCYLILFHAFQSDKRAVEEYASRLEKIMVRSEDGILLVPESYAVPQDLVGFEYQKPGSQVREVVGRCPFLWGQSLFILGRLLQEGFLAVGELDPLNRRLGAQKKPDVVVQVVIIAEDNEIRDKLAEHDLHVQTIAEVAPIEVQPARVLSHLYTYLGRNRKLGLSGRKSRDVGILSTSKLYSLKDRIFAFTPQFADLSRFYIASDNELMIDILKGEINFLKSAWDLLGRPLVTLVLKRIHLDQDKIPLAMIQTMRKLKSGYINGTRVMLGSLKDFLNTSAITDLSFLGSTEDGYPDRLHPDVQTYLDEHLLRSFSNRSTMNLRGGQLRPRTLRRRMSCKGAIKKTRSINVDSDNLGMEGPSPLTERRLSSIVPPPWLQANKQSHVSVFATTPEEGPTSSPLSLGNDLIRENIYPVDPHHSRSAIDRRSEFVRQQEMPKILIQRHRAETNFADTEVEELIAMLRETENLEEQGDILQYLVDTQGLDFNTAGLGFKNKSEENATPNANNAGMLEEGRVVTVRDLLKGLYEKACQQKLWGLVRHTAGMLGKRVEDLAKAVTDLLVRQKQVTVGMPPNNEHTITAPLPEVELRQLIHDAYGDDESTAMLTQELMVYLAMFIRTEPQLFHEMLRLRVGLIIQVMAKELSRTLNCDGEAASEHLLNLSPFEMKNLLYHILSGKEFAVSSVARGNLSIVSCKSSRVSKKSQIGLGDPEGEDALIATIDDRQGQWLRRRRLDGALNRVPRDFYSRVWTVLEKCQGLAIEGRVLQQSLTQEMTPGELKFALEVETALNQIPQPEYRQLVVEALMVLTLVTEHNMVPSLGGVIYVEHLVHKANQLFLEDQRKVQGDATLCCAKIKDGKEQQQAASGMLLCGGAAYICQHLYDSAPSGSYGTMTYMSRAVALVLDCVPKHGEMECAIS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 677 | Phosphorylation | GAIKKTRSINVDSDN CHHCCCCCCCCCCCC | 24.60 | 23607784 | |
| 721 | Phosphorylation | HVSVFATTPEEGPTS CEEEEEECCCCCCCC | 25.85 | 21082442 | |
| 1012 | Phosphorylation | SGKEFAVSSVARGNL HCCCCEEHHHHCCCE | 18.70 | 23607784 | |
| 1013 | Phosphorylation | GKEFAVSSVARGNLS CCCCEEHHHHCCCEE | 17.13 | 28490779 | |
| 1020 | Phosphorylation | SVARGNLSIVSCKSS HHHCCCEEEEEECCC | 25.58 | 28490779 | |
| 1023 | Phosphorylation | RGNLSIVSCKSSRVS CCCEEEEEECCCCCC | 17.73 | 28490779 | |
| 1030 | Phosphorylation | SCKSSRVSKKSQIGL EECCCCCCCCHHCCC | 33.00 | 22817900 | |
| 1033 | Phosphorylation | SSRVSKKSQIGLGDP CCCCCCCHHCCCCCC | 30.66 | 19429919 | |
| 1244 | Farnesylation | PKHGEMECAIS---- CCCCCEEEECC---- | 3.83 | - |
| 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 KPBA_DROME !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KPBA_DROME !! | ||||||
* 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 KPBA_DROME !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| KPBB_DROME | CG8475 | physical | 22036573 | |
| RM23_DROME | mRpL23 | physical | 22036573 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Phosphoproteome analysis of Drosophila melanogaster embryos."; Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; J. Proteome Res. 7:1675-1682(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1030 AND SER-1033, ANDMASS SPECTROMETRY. | |