| UniProt ID | MMS4_YEAST | |
|---|---|---|
| UniProt AC | P38257 | |
| Protein Name | Crossover junction endonuclease MMS4 | |
| Gene Name | MMS4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 691 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Interacts with MUS81 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 | MSQIVDFVEDKDSRNDASIQIIDGPSNVEIIALSESMDQDECKRAHVSSAEMIPSSPQRKSVSNDVENVDLNKSIELSAPFFQDISISKLDDFSTTVNSIIDSSLRNENNAKGNAKKLLDDLISDEWSADLESSGKKHNKSQYNLRDIAEKWGVQSLKNPEPIAVDCEYKTQGIGKTNSDISDSPKSQIGAADILFDFPLSPVKHENPTEEKHNSIANENSSPDNSLKPAGKQNHGEDGTSMAKRVYNKGEDEQEHLPKGKKRTIALSRTLINSTKLPDTVELNLSKFLDSSDSITTDVLSTPAKGSNIVRTGSQPIFSNANCFQEAKRSKTLTAEDPKCTKNTAREVSQLENYIAYGQYYTREDSKNKIRHLLKENKNAFKRVNQIYRDNIKARSQMIIEFSPSLLQLFKKGDSDLQQQLAPAVVQSSYNDSMPLLRFLRKCDSIYDFSNDFYYPCDPKIVEENVLILYYDAQEFFEQYTSQKKELYRKIRFFSKNGKHVILILSDINKLKRAIFQLENEKYKARVEQRLSGTEEALRPRSKKSSQVGKLGIKKFDLEQRLRFIDREWHVKIHTVNSHMEFINSLPNLVSLIGKQRMDPAIRYMKYAHLNVKSAQDSTETLKKTFHQIGRMPEMKANNVVSLYPSFQSLLEDIEKGRLQSDNEGKYLMTEAVEKRLYKLFTCTDPNDTIE | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSQIVDFVE ------CCCCCHHCC | 28.72 | 22814378 | |
| 2 | Phosphorylation | ------MSQIVDFVE ------CCCCCHHCC | 28.72 | 30377154 | |
| 48 | Phosphorylation | ECKRAHVSSAEMIPS HHHHHCCCHHHHCCC | 17.60 | 21440633 | |
| 49 | Phosphorylation | CKRAHVSSAEMIPSS HHHHCCCHHHHCCCC | 27.45 | 21440633 | |
| 55 | Phosphorylation | SSAEMIPSSPQRKSV CHHHHCCCCCCCCCC | 43.66 | 21440633 | |
| 56 | Phosphorylation | SAEMIPSSPQRKSVS HHHHCCCCCCCCCCC | 21.50 | 25752575 | |
| 61 | Phosphorylation | PSSPQRKSVSNDVEN CCCCCCCCCCCCCCC | 32.73 | 22369663 | |
| 63 | Phosphorylation | SPQRKSVSNDVENVD CCCCCCCCCCCCCCC | 34.11 | 22369663 | |
| 74 | Phosphorylation | ENVDLNKSIELSAPF CCCCCCCCEEECCCC | 21.88 | 21551504 | |
| 86 | Phosphorylation | APFFQDISISKLDDF CCCCCCCCHHHCCCC | 29.15 | 29688323 | |
| 88 | Phosphorylation | FFQDISISKLDDFST CCCCCCHHHCCCCHH | 22.00 | 29688323 | |
| 141 | Phosphorylation | SGKKHNKSQYNLRDI CCCCCCCCHHCHHHH | 43.12 | 19823750 | |
| 143 | Phosphorylation | KKHNKSQYNLRDIAE CCCCCCHHCHHHHHH | 24.21 | 21440633 | |
| 179 | Phosphorylation | QGIGKTNSDISDSPK CCCCCCCCCCCCCCH | 41.37 | 21551504 | |
| 182 | Phosphorylation | GKTNSDISDSPKSQI CCCCCCCCCCCHHHC | 36.71 | 21551504 | |
| 184 | Phosphorylation | TNSDISDSPKSQIGA CCCCCCCCCHHHCCC | 27.69 | 21551504 | |
| 187 | Phosphorylation | DISDSPKSQIGAADI CCCCCCHHHCCCCCE | 30.34 | 21551504 | |
| 209 | Phosphorylation | PVKHENPTEEKHNSI CCCCCCCCHHHHHCC | 69.25 | 21440633 | |
| 215 | Phosphorylation | PTEEKHNSIANENSS CCHHHHHCCCCCCCC | 23.85 | 20377248 | |
| 221 | Phosphorylation | NSIANENSSPDNSLK HCCCCCCCCCCCCCC | 36.75 | 20377248 | |
| 222 | Phosphorylation | SIANENSSPDNSLKP CCCCCCCCCCCCCCC | 48.10 | 20377248 | |
| 226 | Phosphorylation | ENSSPDNSLKPAGKQ CCCCCCCCCCCCCCC | 45.19 | 21551504 | |
| 280 | Phosphorylation | NSTKLPDTVELNLSK CCCCCCCEEEEEHHH | 17.59 | 21440633 | |
| 286 | Phosphorylation | DTVELNLSKFLDSSD CEEEEEHHHHHCCCC | 21.93 | 21440633 | |
| 291 | Phosphorylation | NLSKFLDSSDSITTD EHHHHHCCCCCCCEE | 37.89 | 28889911 | |
| 292 | Phosphorylation | LSKFLDSSDSITTDV HHHHHCCCCCCCEEC | 34.74 | 19779198 | |
| 294 | Phosphorylation | KFLDSSDSITTDVLS HHHCCCCCCCEECCC | 24.63 | 21551504 | |
| 296 | Phosphorylation | LDSSDSITTDVLSTP HCCCCCCCEECCCCC | 22.39 | 19779198 | |
| 297 | Phosphorylation | DSSDSITTDVLSTPA CCCCCCCEECCCCCC | 23.57 | 19779198 | |
| 312 | Phosphorylation | KGSNIVRTGSQPIFS CCCCCEECCCCCCCC | 30.23 | 27214570 | |
| 314 | Phosphorylation | SNIVRTGSQPIFSNA CCCEECCCCCCCCCC | 31.97 | 21440633 | |
| 332 | Phosphorylation | QEAKRSKTLTAEDPK HHHHHHCCCCCCCCC | 30.50 | 30377154 | |
| 523 | Phosphorylation | FQLENEKYKARVEQR HHHCCHHHHHHHHHH | 12.05 | 27017623 | |
| 532 | Phosphorylation | ARVEQRLSGTEEALR HHHHHHHCCCHHHHC | 45.95 | 23749301 | |
| 534 | Phosphorylation | VEQRLSGTEEALRPR HHHHHCCCHHHHCCC | 27.55 | 24961812 | |
| 542 | Phosphorylation | EEALRPRSKKSSQVG HHHHCCCCCCCCCCC | 47.30 | 24961812 | |
| 607 | Phosphorylation | PAIRYMKYAHLNVKS HHHHHHHHEECCCCC | 5.24 | 27017623 | |
| 618 | Phosphorylation | NVKSAQDSTETLKKT CCCCCCCCHHHHHHH | 18.96 | 27017623 | |
| 619 | Phosphorylation | VKSAQDSTETLKKTF CCCCCCCHHHHHHHH | 41.08 | 27017623 | |
| 667 | Phosphorylation | QSDNEGKYLMTEAVE CCCCCCCCCCHHHHH | 16.74 | 30377154 | |
| 670 | Phosphorylation | NEGKYLMTEAVEKRL CCCCCCCHHHHHHHH | 20.42 | 30377154 |
| 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 MMS4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MMS4_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 MMS4_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-61; SER-291 AND SER-314,AND MASS SPECTROMETRY. | |
