| UniProt ID | SLX4_YEAST | |
|---|---|---|
| UniProt AC | Q12098 | |
| Protein Name | Structure-specific endonuclease subunit SLX4 {ECO:0000255|HAMAP-Rule:MF_03110} | |
| Gene Name | SLX4 {ECO:0000255|HAMAP-Rule:MF_03110} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 748 | |
| Subcellular Localization | Nucleus. Cytoplasm. | |
| Protein Description | Regulatory subunit that interacts with and increases the activity of different structure-specific endonucleases. Has several distinct roles in protecting genome stability by resolving diverse forms of deleterious DNA structures. Component of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for simple Y, 5'-flap and replication fork-like structures. It cleaves the strand bearing the 5'-non-homologous arm at the branch site junction and generates ligatable, nicked products from the 5'-flap or replication fork substrates. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. Has Holliday junction resolvase activity in vitro. Interacts with the structure-specific RAD1-RAD10 endonuclease and promotes RAD1-RAD10-dependent 3'-non-homologous tail removal (NHTR) during repair of double-strand breaks by single-strand annealing. SLX4 also promotes recovery from DNA-alkylation-induced replisome stalling during DNA replication by facilitating the error-free mode of lesion bypass. This does not require SLX1 or RAD1-RAD10, but probably RTT107.. | |
| Protein Sequence | MELQRAQRNLKFLQNEDYVNVTDQTNLNGESQNAYSLGMETQVPEMQFSLSSDDDSIGTQVKSVTAQKSPMTQETTKNDTERNKDVDKSCNPVSTSHPDLGGSNIEENIFINTQIQSRLDDAEEETNLKLKLEKFKYSFKSSNADDTHSNANVTAKRRPAIRKANSKLKTKPKTKRDPKIIKNITDFNINNYERSRTASLLKQLSGKHKKVLDIIKTQNEGNSDKPPRARNNKGEKATFDTYSEQEWKDIMKLLLQKFPQSEETDLNEVQKFLYGSEKSSNSLDNQESSQQRLWTASQLPPELPDEAIQPEQEERIRDTQSAVNFLSLSQVMDDKSEIMKDEESIIISRGDSTSSQEYGNGLEPQQPVGNVVGEDIELAVGTRINAFSLTDYKACKPMSVEVSRRCENSTDNDYDNISIVSDTTDETSTLFPLDQYRYVFIENDERPPLATDTIGSTQFFTPNTSPLDGIIDLTQESFKAVRSLISPLKVENNKTGVTSQASNQVQVPATRTPTIIPQKNLTTTLKTEEEKNNIGSSIRVKLLQESVVKLNPKLVKHNFYRVEANDSEEEETEFDDQFCIADIQLVDSSKISTKDSTQNPTTSNDIIDTSAASSIASPEKFCEIMMSQSMKELRQSLKTVGLKPMRTKVEIIQSLQTASQILSTANPDNKGEHGGVANFSKIEIFDHLTELIEAFPDFLERIYTFEPIPLNELIEKLFSAEPFVSQIDEMTIREWADVQGICLRNDKK | |
| 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 |
|---|---|---|---|---|---|
| 69 | Phosphorylation | KSVTAQKSPMTQETT EEEEECCCCCCCCCC | 14.07 | 28889911 | |
| 72 | Phosphorylation | TAQKSPMTQETTKND EECCCCCCCCCCCCC | 27.00 | 17636031 | |
| 75 | Phosphorylation | KSPMTQETTKNDTER CCCCCCCCCCCCCHH | 33.00 | 27017623 | |
| 113 | Phosphorylation | EENIFINTQIQSRLD HHCEEEEHHHHHCCC | 23.41 | 20382573 | |
| 138 | Phosphorylation | KLEKFKYSFKSSNAD HHHHHHHEECCCCCC | 27.13 | 21440633 | |
| 149 | Phosphorylation | SNADDTHSNANVTAK CCCCCCCCCCCHHHH | 39.47 | 28889911 | |
| 276 | Phosphorylation | VQKFLYGSEKSSNSL HHHHHHCCCCCCCCC | 28.44 | 30377154 | |
| 288 | Phosphorylation | NSLDNQESSQQRLWT CCCCCHHHHHHHHHH | 24.55 | 28889911 | |
| 289 | Phosphorylation | SLDNQESSQQRLWTA CCCCHHHHHHHHHHH | 29.58 | 25752575 | |
| 319 | Phosphorylation | QEERIRDTQSAVNFL HHHHHHHHHHHHHHH | 17.99 | - | |
| 329 | Phosphorylation | AVNFLSLSQVMDDKS HHHHHHHHHHCCCHH | 19.83 | 17636031 | |
| 355 | Phosphorylation | SRGDSTSSQEYGNGL ECCCCCCCCCCCCCC | 27.41 | - | |
| 388 | Phosphorylation | GTRINAFSLTDYKAC ECCEECEECCCCCCC | 28.13 | 28889911 | |
| 390 | Phosphorylation | RINAFSLTDYKACKP CEECEECCCCCCCCC | 35.76 | 30377154 | |
| 457 | Phosphorylation | ATDTIGSTQFFTPNT CCCCCCCCCCCCCCC | 24.96 | 28889911 | |
| 474 | Phosphorylation | LDGIIDLTQESFKAV CCCHHCCCHHHHHHH | 26.92 | 28889911 | |
| 483 | Phosphorylation | ESFKAVRSLISPLKV HHHHHHHHHHCCEEE | 24.37 | 21440633 | |
| 486 | Phosphorylation | KAVRSLISPLKVENN HHHHHHHCCEEEECC | 29.49 | 17563356 | |
| 499 | Phosphorylation | NNKTGVTSQASNQVQ CCCCCCCCCCCCCEE | 22.73 | 25752575 | |
| 502 | Phosphorylation | TGVTSQASNQVQVPA CCCCCCCCCCEECCC | 21.84 | 30377154 | |
| 514 | Phosphorylation | VPATRTPTIIPQKNL CCCCCCCCCCCCCCC | 30.81 | 27017623 | |
| 597 | Phosphorylation | KISTKDSTQNPTTSN CCCCCCCCCCCCCCC | 42.36 | 28889911 | |
| 617 | Phosphorylation | SAASSIASPEKFCEI CHHHHCCCHHHHHHH | 31.74 | 29734811 | |
| 627 | Phosphorylation | KFCEIMMSQSMKELR HHHHHHHCHHHHHHH | 11.17 | 28889911 | |
| 659 | Phosphorylation | IQSLQTASQILSTAN HHHHHHHHHHHHHCC | 22.57 | 28889911 | |
| 725 | Phosphorylation | FSAEPFVSQIDEMTI HCCCCHHHHCHHHHH | 23.07 | 20190278 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 72 | T | Phosphorylation | Kinase | ATM | P38110 | Uniprot |
| 72 | T | Phosphorylation | Kinase | ATR | - | GPS |
| 72 | T | Phosphorylation | Kinase | ATM | - | GPS |
| 72 | T | Phosphorylation | Kinase | ATR | P38111 | Uniprot |
| 113 | T | Phosphorylation | Kinase | ATM | P38110 | Uniprot |
| 113 | T | Phosphorylation | Kinase | ATR | P38111 | Uniprot |
| 289 | S | Phosphorylation | Kinase | ATR | P38111 | Uniprot |
| 289 | S | Phosphorylation | Kinase | ATM | - | GPS |
| 289 | S | Phosphorylation | Kinase | ATR | - | GPS |
| 289 | S | Phosphorylation | Kinase | ATM | P38110 | Uniprot |
| 319 | T | Phosphorylation | Kinase | ATR | P38111 | Uniprot |
| 319 | T | Phosphorylation | Kinase | ATM | P38110 | Uniprot |
| 329 | S | Phosphorylation | Kinase | ATM | P38110 | Uniprot |
| 329 | S | Phosphorylation | Kinase | ATR | P38111 | Uniprot |
| 329 | S | Phosphorylation | Kinase | ATM | - | GPS |
| 329 | S | Phosphorylation | Kinase | ATR | - | GPS |
| 355 | S | Phosphorylation | Kinase | ATM | P38110 | Uniprot |
| 355 | S | Phosphorylation | Kinase | ATR | P38111 | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SLX4_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 SLX4_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-388 AND SER-499, 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 SER-486, AND MASSSPECTROMETRY. | |
| "Phosphorylation of Slx4 by Mec1 and Tel1 regulates the single-strandannealing mode of DNA repair in budding yeast."; Flott S., Alabert C., Toh G.W., Toth R., Sugawara N., Campbell D.G.,Haber J.E., Pasero P., Rouse J.; Mol. Cell. Biol. 27:6433-6445(2007). Cited for: FUNCTION, INTERACTION WITH RAD1 AND SLX1, AND PHOSPHORYLATION ATTHR-72; SER-289 AND SER-329 BY MEC1 AND TEL1. | |
