| UniProt ID | SLX5_YEAST | |
|---|---|---|
| UniProt AC | P32828 | |
| Protein Name | E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX5 | |
| Gene Name | SLX5 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 619 | |
| Subcellular Localization | Nucleus, nucleolus . | |
| Protein Description | Mediates ubiquitination and subsequent desumoylation/degradation of sumoylated proteins and proteins containing SUMO-like domains. Promotes UBC4-dependent ubiquitination that mediates the proteolytic down-regulation of sumoylated proteins. Involved in the stimulation of ubiquitin conjugating enzymes, including UBC1, UBC4, UBC5 and UBC13-MMS2. Acts as a critical suppressor of gross chromosomal rearrangements (GCRs) during normal cell cycle progression. Has a role in localizing the DNA damage protein DCD2. Involved in stabilizing, restarting or resolving transiently stalled replication forks. Prevents accumulation of DNA damage during cell cycle progression. Along with SIR2, promotes silencing of genes at telomeric or ribosomal DNA (rDNA) loci.. | |
| Protein Sequence | MHSDTNGRTKSNNSPSDNNPNETVILIDSDKEEDASIREANLPVRLYPDRRVGRRRDALNRFVRSDSRSRNSQRTHITASSERPDFQANNDDITIIREVGRFFGDDGPIDPSAHYVDLDQEPGSETLETPRTIQVDNTNGYLNDNGNNNESDDGLTIVEERTTRPRVTLNLPGGERLEVTATTTDIPIRRSFEFQEDLGASRRQLLRRSATRARNLFVDRSDENDEDWTDDTHNLPEAIQRARRESRMRMSRRIAERQRRVQQQRVSSDENISTSIRLQSIRERIQSYTPDIRSAFHRAESLHEFRSILQNVAPITLQECEEELMALFTEFRNQLLQNWAIDRVRNTQEEALRLHREALERQERTAGRVFHRGTLRESITNYLNFNGEDGFLSRLWSGPALSDADEERHTQNIIDMIQEREERERDVVMKNLMNKTRAQQEEFEARAASLPEGYSASFDTTPKMKLDITKNGKEETIIVTDDDLAKTLEDIPVCCLCGAELGVGIPDDFTGISQKDRGVSFEGLVSKYKFHCPYQTLARPSMLDRDLSKRTFIASCGHAFCGRCFARIDNAKKKSKMPKKKLAQLKGSAHPDNYGPKLCPADSCKKLIRSRGRLKEVYF | |
| 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 |
|---|---|---|---|---|---|
| 11 | Phosphorylation | DTNGRTKSNNSPSDN CCCCCCCCCCCCCCC | 40.40 | 23749301 | |
| 14 | Phosphorylation | GRTKSNNSPSDNNPN CCCCCCCCCCCCCCC | 29.99 | 28889911 | |
| 16 | Phosphorylation | TKSNNSPSDNNPNET CCCCCCCCCCCCCCE | 53.44 | 28889911 | |
| 23 | Phosphorylation | SDNNPNETVILIDSD CCCCCCCEEEEEECC | 21.34 | 28889911 | |
| 29 | Phosphorylation | ETVILIDSDKEEDAS CEEEEEECCCCCCCC | 43.52 | 23749301 | |
| 36 | Phosphorylation | SDKEEDASIREANLP CCCCCCCCHHHCCCC | 34.20 | 28889911 | |
| 151 | Phosphorylation | DNGNNNESDDGLTIV CCCCCCCCCCCEEEE | 43.03 | 21440633 | |
| 209 | Phosphorylation | RRQLLRRSATRARNL HHHHHHHHHHHHHHC | 27.79 | 28747907 | |
| 221 | Phosphorylation | RNLFVDRSDENDEDW HHCCCCCCCCCCCCC | 44.83 | 25704821 | |
| 268 | Phosphorylation | VQQQRVSSDENISTS HHHHHHCCCCCHHHH | 46.19 | 23749301 | |
| 397 | Phosphorylation | GFLSRLWSGPALSDA CHHHHHHCCCCCCCC | 39.22 | 27017623 | |
| 402 | Phosphorylation | LWSGPALSDADEERH HHCCCCCCCCCHHHH | 32.62 | 27017623 | |
| 430 | Ubiquitination | RERDVVMKNLMNKTR HHHHHHHHHHHHHHH | 35.01 | 23749301 | |
| 436 | Phosphorylation | MKNLMNKTRAQQEEF HHHHHHHHHHHHHHH | 26.66 | 28889911 | |
| 449 | Phosphorylation | EFEARAASLPEGYSA HHHHHHHCCCCCCCC | 43.39 | 19779198 | |
| 528 | Phosphorylation | FEGLVSKYKFHCPYQ HHHHHHCCCCCCCHH | 16.04 | 19823750 | |
| 534 | Phosphorylation | KYKFHCPYQTLARPS CCCCCCCHHHCCCHH | 21.37 | 19823750 | |
| 536 | Phosphorylation | KFHCPYQTLARPSML CCCCCHHHCCCHHHC | 19.28 | 19823750 | |
| 541 | Phosphorylation | YQTLARPSMLDRDLS HHHCCCHHHCCCCHH | 26.82 | 19823750 | |
| 548 | Phosphorylation | SMLDRDLSKRTFIAS HHCCCCHHHCEEEHH | 25.12 | 19823750 |
| 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 SLX5_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SLX5_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 SLX5_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 SER-29, AND MASSSPECTROMETRY. | |
