| UniProt ID | RAD24_YEAST | |
|---|---|---|
| UniProt AC | P32641 | |
| Protein Name | Checkpoint protein RAD24 | |
| Gene Name | RAD24 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 659 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Participates in checkpoint pathways arrest of the cell cycle, a mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. Regulates the DNA damage checkpoint pathway throughout the cell cycle, when associated with RCF5. Component of the RFC-like RAD24-RFC complex which loads the checkpoint clamp DDC1:MEC3:RAD17 complex and is involved in DNA repair pathways. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA.. | |
| Protein Sequence | MDSTNLNKRPLLQYSLSSLGSQITKWSSSRPTSPVRKARSTENDFLSKQDTSSILPSINDDGGEQWYEKFKPNCLEQVAIHKRKLKDVQEALDAMFLPNAKHRILLLSGPSGCSKSTVIKELSKILVPKYRQNSNGTSFRSTPNEHKVTEFRGDCIVNDLPQMESFSEFLKGARYLVMSNLSLILIEDLPNVFHIDTRRRFQQLILQWLYSSEPLLPPLVICITECEIPENDNNYRKFGIDYTFSAETIMNKEILMHPRLKRIKFNPINSTLLKKHLKFICVQNMKMLKEKNKWNKRQEVIDYIAQETGDIRSAITTLQFWATSSGSLPISTRESTISYFHAIGKVIHGSHSTNNDNEMINNLFENSNNLLSKEDFKLGILENYNTFNKGEFSISDASSIVDCLSECDNMNGLPESNEYGLREVRKTFRNISKQGHNHGTVYFPREWKVRKLQNSFKVQAEDWLNVSLYKYNAVHSFRNITLEFGYYAPLIRKCQSYKKKYILYYLKNLPSGSSGPKQTMDKFSDIMKVENGIDVVDRIGGPIEALSVEDGLAPLMDNDSNNCDHLEDQKKERDRRLRMLIDQYERNVMMANDDLEDEETSFNDDPIVDSDSDNSNNIGNETFGRSDEDESLCEILSQRQPRKAPVISESLSDSDLEIL | |
| 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 |
|---|---|---|---|---|---|
| 4 | Phosphorylation | ----MDSTNLNKRPL ----CCCCCCCCCHH | 39.19 | 28889911 | |
| 8 | Acetylation | MDSTNLNKRPLLQYS CCCCCCCCCHHHHHH | 59.57 | 25381059 | |
| 17 | Phosphorylation | PLLQYSLSSLGSQIT HHHHHHHHHHHHHHH | 19.99 | 21440633 | |
| 18 | Phosphorylation | LLQYSLSSLGSQITK HHHHHHHHHHHHHHH | 41.88 | 21440633 | |
| 28 | Phosphorylation | SQITKWSSSRPTSPV HHHHHCCCCCCCCCC | 29.29 | 21440633 | |
| 29 | Phosphorylation | QITKWSSSRPTSPVR HHHHCCCCCCCCCCC | 36.44 | 21440633 | |
| 32 | Phosphorylation | KWSSSRPTSPVRKAR HCCCCCCCCCCCCCC | 44.55 | 21440633 | |
| 33 | Phosphorylation | WSSSRPTSPVRKARS CCCCCCCCCCCCCCC | 24.87 | 21440633 | |
| 40 | Phosphorylation | SPVRKARSTENDFLS CCCCCCCCCCCCCCC | 44.95 | 28889911 | |
| 130 | Phosphorylation | SKILVPKYRQNSNGT HHHHHCCCCCCCCCC | 16.03 | 19779198 | |
| 138 | Phosphorylation | RQNSNGTSFRSTPNE CCCCCCCEECCCCCC | 21.77 | 19779198 | |
| 271 | Phosphorylation | KFNPINSTLLKKHLK CCCCCCHHHHHHHHH | 31.46 | 27017623 | |
| 291 | Acetylation | NMKMLKEKNKWNKRQ CHHHHHHHCCCCHHH | 63.34 | 23572591 | |
| 648 | Phosphorylation | PRKAPVISESLSDSD CCCCCCCCCCCCHHH | 22.74 | 21440633 | |
| 650 | Phosphorylation | KAPVISESLSDSDLE CCCCCCCCCCHHHCC | 26.78 | 21440633 | |
| 652 | Phosphorylation | PVISESLSDSDLEIL CCCCCCCCHHHCCCC | 44.33 | 17330950 | |
| 654 | Phosphorylation | ISESLSDSDLEIL-- CCCCCCHHHCCCC-- | 40.49 | 17330950 |
| 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 RAD24_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAD24_YEAST !! | ||||||
* 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 RAD24_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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 SER-17, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652 AND SER-654, ANDMASS SPECTROMETRY. | |
