| UniProt ID | KIN28_YEAST | |
|---|---|---|
| UniProt AC | P06242 | |
| Protein Name | Serine/threonine-protein kinase KIN28 | |
| Gene Name | KIN28 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 306 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Catalytic component of the TFIIK complex (KIN28-CCL1 dimer) which is the protein kinase component of transcription factor IIH (TFIIH) and phosphorylates the C-terminal domain of RNA polymerase II during transition from transcription to elongation after preinitiation complex (PIC) formation, thereby positively regulating transcription. TFIIH (or factor B) is essential for both basal and activated transcription, and is involved in nucleotide excision repair (NER) of damaged DNA. TFIIH has DNA-dependent ATPase activity and is essential for polymerase II transcription in vitro. Essential for cell proliferation.. | |
| Protein Sequence | MKVNMEYTKEKKVGEGTYAVVYLGCQHSTGRKIAIKEIKTSEFKDGLDMSAIREVKYLQEMQHPNVIELIDIFMAYDNLNLVLEFLPTDLEVVIKDKSILFTPADIKAWMLMTLRGVYHCHRNFILHRDLKPNNLLFSPDGQIKVADFGLARAIPAPHEILTSNVVTRWYRAPELLFGAKHYTSAIDIWSVGVIFAELMLRIPYLPGQNDVDQMEVTFRALGTPTDRDWPEVSSFMTYNKLQIYPPPSRDELRKRFIAASEYALDFMCGMLTMNPQKRWTAVQCLESDYFKELPPPSDPSSIKIRN | |
| 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 |
|---|---|---|---|---|---|
| 17 | Phosphorylation | EKKVGEGTYAVVYLG CEECCCCEEEEEEEE | 12.19 | 11839796 | |
| 162 | Phosphorylation | PAPHEILTSNVVTRW CCCHHHHCCCCCCEE | 24.74 | 22369663 | |
| 163 | Phosphorylation | APHEILTSNVVTRWY CCHHHHCCCCCCEEE | 24.96 | 22890988 | |
| 167 | Phosphorylation | ILTSNVVTRWYRAPE HHCCCCCCEEECCHH | 15.94 | 22890988 | |
| 260 | Phosphorylation | RKRFIAASEYALDFM HHHHHHHHHHHHHHH | 23.32 | 27017623 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 162 | T | Phosphorylation | Kinase | KIN28 | P06242 | GPS |
| 162 | T | Phosphorylation | Kinase | CDK7 | - | GPS |
| 162 | T | Phosphorylation | Kinase | CAK | - | Uniprot |
* 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 KIN28_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-162 AND THR-167, ANDMASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-162, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-162, AND MASSSPECTROMETRY. | |
| "Kin28 is found within TFIIH and a Kin28-Ccl1-Tfb3 trimer complex withdifferential sensitivities to T-loop phosphorylation."; Keogh M.-C., Cho E.-J., Podolny V., Buratowski S.; Mol. Cell. Biol. 22:1288-1297(2002). Cited for: IDENTIFICATION IN A COMPLEX WITH CCL1 AND TFB3, PHOSPHORYLATION ATTHR-162, AND MUTAGENESIS OF THR-17; LYS-36; GLU-54; ASP-147; THR-162AND SER-163. | |
| "Activating phosphorylation of the Kin28p subunit of yeast TFIIH byCak1p."; Kimmelman J., Kaldis P., Hengartner C.J., Laff G.M., Koh S.S.,Young R.A., Solomon M.J.; Mol. Cell. Biol. 19:4774-4787(1999). Cited for: PHOSPHORYLATION AT THR-162, AND MUTAGENESIS OF ASP-147; 17-THR-TYR-18AND THR-162. | |
| "Cak1 is required for Kin28 phosphorylation and activation in vivo."; Espinoza F.H., Farrell A., Nourse J.L., Chamberlin H.M., Gileadi O.,Morgan D.O.; Mol. Cell. Biol. 18:6365-6373(1998). Cited for: PHOSPHORYLATION AT THR-162, AND MUTAGENESIS OF THR-162. | |
