| UniProt ID | MUS81_YEAST | |
|---|---|---|
| UniProt AC | Q04149 | |
| Protein Name | Crossover junction endonuclease MUS81 | |
| Gene Name | MUS81 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 632 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Interacts with MMS4 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks with regressed leading strands and nicked Holliday junctions. Cleavage probably occurs approximately half a helical turn upstream of the free 5'-end in these structures. May be required in mitosis for the processing of stalled replication fork intermediates arising spontaneously or subsequent to treatment with DNA damaging agents such as methylmethane sulfonate (MMS), camptothecin (CPT) or UV. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI). This involves consecutive cleavage of D-loops and nicked Holliday junctions leading to sister chromatid crossover. In contrast to MSH4-MSH5 dependent crossover, double Holliday junctions do not seem to be involved. Spore formation and viability are severely impaired in deletion strains.. | |
| Protein Sequence | MELSSNLKDLYIEWLQELVDGLTPKQEQLKIAYEKAKRNLQNAEGSFYYPTDLKKVKGIGNTIIKRLDTKLRNYCKIHHISPVEAPSLTQTSSTRPPKRTTTALRSIVNSCENDKNEAPEEKGTKKRKTRKYIPKKRSGGYAILLSLLELNAIPRGVSKEQIIEVAGKYSDHCMTPNFSTKEFYGAWSSIAALKKHSLVLEEGRPKRYSLTEEGVELTKSLKTADGISFPKENEEPNEYSVTRNESSEFTANLTDLRGEYGKEEEPCDINNTSFMLDITFQDLSTPQRLQNNVFKNDRLNSQTNISSHKLEEVSDDQTVPDSALKAKSTIKRRRYNGVSYELWCSGDFEVFPIIDHREIKSQSDREFFSRAFERKGMKSEIRQLALGDIIWVAKNKNTGLQCVLNTIVERKRLDDLALSIRDNRFMEQKNRLEKSGCEHKYYLIEETMSGNIGNMNEALKTALWVILVYYKFSMIRTCNSDETVEKIHALHTVISHHYSQKDLIVIFPSDLKSKDDYKKVLLQFRREFERKGGIECCHNLECFQELMGKGDLKTVGELTIHVLMLVKGISLEKAVAIQEIFPTLNKILMAYKTCSSEEEAKLLMFNVLGDAPGAKKITKSLSEKIYDAFGKL | |
| 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 |
|---|---|---|---|---|---|
| 81 | Phosphorylation | YCKIHHISPVEAPSL HCEEEECCCCCCCCC | 20.66 | 27017623 | |
| 91 | Phosphorylation | EAPSLTQTSSTRPPK CCCCCCCCCCCCCCC | 21.29 | 27017623 | |
| 93 | Phosphorylation | PSLTQTSSTRPPKRT CCCCCCCCCCCCCCH | 31.65 | 27017623 | |
| 110 | Phosphorylation | ALRSIVNSCENDKNE HHHHHHHHCCCCCCC | 16.35 | 23749301 | |
| 169 | Phosphorylation | IIEVAGKYSDHCMTP HHHHHHHCCCCCCCC | 20.57 | 22890988 | |
| 170 | Phosphorylation | IEVAGKYSDHCMTPN HHHHHHCCCCCCCCC | 25.10 | 22890988 | |
| 175 | Phosphorylation | KYSDHCMTPNFSTKE HCCCCCCCCCCCHHH | 22.07 | 22890988 | |
| 179 | Phosphorylation | HCMTPNFSTKEFYGA CCCCCCCCHHHHHHC | 45.25 | 22890988 | |
| 180 | Phosphorylation | CMTPNFSTKEFYGAW CCCCCCCHHHHHHCH | 30.38 | 22890988 | |
| 240 | Phosphorylation | NEEPNEYSVTRNESS CCCCCCCCCCCCCCC | 15.72 | 28889911 | |
| 246 | Phosphorylation | YSVTRNESSEFTANL CCCCCCCCCCEEEEH | 38.42 | 27214570 | |
| 247 | Phosphorylation | SVTRNESSEFTANLT CCCCCCCCCEEEEHH | 30.47 | 27214570 | |
| 295 | Acetylation | RLQNNVFKNDRLNSQ HHHHCCCCCCCCCCC | 54.37 | 25381059 | |
| 301 | Phosphorylation | FKNDRLNSQTNISSH CCCCCCCCCCCCCCC | 42.87 | 23749301 | |
| 303 | Phosphorylation | NDRLNSQTNISSHKL CCCCCCCCCCCCCCC | 34.05 | 21440633 | |
| 306 | Phosphorylation | LNSQTNISSHKLEEV CCCCCCCCCCCCEEC | 28.58 | 24961812 | |
| 307 | Phosphorylation | NSQTNISSHKLEEVS CCCCCCCCCCCEECC | 22.35 | 24961812 | |
| 314 | Phosphorylation | SHKLEEVSDDQTVPD CCCCEECCCCCCCCH | 38.46 | 21440633 | |
| 318 | Phosphorylation | EEVSDDQTVPDSALK EECCCCCCCCHHHHH | 40.79 | 24961812 | |
| 509 | Phosphorylation | DLIVIFPSDLKSKDD CEEEEECHHCCCCHH | 44.84 | 21440633 |
| 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 MUS81_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MUS81_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 MUS81_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-246 AND SER-247, ANDMASS SPECTROMETRY. | |
