| UniProt ID | RRM3_YEAST | |
|---|---|---|
| UniProt AC | P38766 | |
| Protein Name | ATP-dependent DNA helicase RRM3 {ECO:0000255|HAMAP-Rule:MF_03177} | |
| Gene Name | RRM3 {ECO:0000255|HAMAP-Rule:MF_03177} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 723 | |
| Subcellular Localization | Nucleus. Chromosome, telomere. | |
| Protein Description | 5' to 3' DNA replicative helicase recruited to paused replisomes to promote fork progression throughout nonhistone protein-DNA complexes, naturally occurring impediments that are encountered in each S phase where replication forks pauses. Needed for normal fork progression through over 1000 discrete sites scattered throughout the genome, like rDNA, tRNA genes, centromeres, active replication origins, or transcriptional silencers. Required for timely replication of the telomere and subtelomeric DNA and for wild-type levels of telomeric silencing. Involved in regulation of Ty1 transposition and protects the genome from instability at nascent sites of retrotransposition. Involved in DNA repair during stalled replication fork, regulation of fragile sites expression and essential for genome stability. Plays also a role in mtDNA replication. Has G-quadruplex (G4) unwinding activity and can suppress G4-induced genome instability when PIF1 levels are low.. | |
| Protein Sequence | MFRSHASGNKKQWSKRSSNGSTPAASASGSHAYRQQTLSSFFMGCGKKSAAASKNSTTIIDLESGDEGNRNITAPPRPRLIRNNSSSLFSQSQGSFGDDDPDAEFKKLVDVPRLNSYKKSSRSLSMTSSLHKTASASTTQKTYHFDEDETLREVTSVKSNSRQLSFTSTINIEDSSMKLSTDSERPAKRSKPSMEFQGLKLTVPKKIKPLLRKTVSNMDSMNHRSASSPVVLTMEQERVVNLIVKKRTNVFYTGSAGTGKSVILQTIIRQLSSLYGKESIAITASTGLAAVTIGGSTLHKWSGIGIGNKTIDQLVKKIQSQKDLLAAWRYTKVLIIDEISMVDGNLLDKLEQIARRIRKNDDPFGGIQLVLTGDFFQLPPVAKKDEHNVVKFCFESEMWKRCIQKTILLTKVFRQQDNKLIDILNAIRYGELTVDIAKTIRNLNRDIDYADGIAPTELYATRREVELSNVKKLQSLPGDLYEFKAVDNAPERYQAILDSSLMVEKVVALKEDAQVMMLKNKPDVELVNGSLGKVLFFVTESLVVKMKEIYKIVDDEVVMDMRLVSRVIGNPLLKESKEFRQDLNARPLARLERLKILINYAVKISPHKEKFPYVRWTVGKNKYIHELMVPERFPIDIPRENVGLERTQIPLMLCWALSIHKAQGQTIQRLKVDLRRIFEAGQVYVALSRAVTMDTLQVLNFDPGKIRTNERVKDFYKRLETLK | |
| 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 |
|---|---|---|---|---|---|
| 18 | Phosphorylation | KQWSKRSSNGSTPAA CCCCCCCCCCCCCCC | 49.60 | 30377154 | |
| 21 | Phosphorylation | SKRSSNGSTPAASAS CCCCCCCCCCCCHHC | 35.15 | 30377154 | |
| 22 | Phosphorylation | KRSSNGSTPAASASG CCCCCCCCCCCHHCC | 20.53 | 27017623 | |
| 26 | Phosphorylation | NGSTPAASASGSHAY CCCCCCCHHCCCHHH | 25.69 | 30377154 | |
| 28 | Phosphorylation | STPAASASGSHAYRQ CCCCCHHCCCHHHHH | 38.03 | 30377154 | |
| 30 | Phosphorylation | PAASASGSHAYRQQT CCCHHCCCHHHHHHH | 11.49 | 30377154 | |
| 33 | Phosphorylation | SASGSHAYRQQTLSS HHCCCHHHHHHHHHH | 11.97 | 30377154 | |
| 56 | Phosphorylation | SAAASKNSTTIIDLE HHHHCCCCCEEEECC | 30.57 | 30377154 | |
| 64 | Phosphorylation | TTIIDLESGDEGNRN CEEEECCCCCCCCCC | 59.86 | 21082442 | |
| 85 | Phosphorylation | PRLIRNNSSSLFSQS CCEECCCCCCHHCCC | 25.50 | 23749301 | |
| 86 | Phosphorylation | RLIRNNSSSLFSQSQ CEECCCCCCHHCCCC | 32.93 | 23749301 | |
| 87 | Phosphorylation | LIRNNSSSLFSQSQG EECCCCCCHHCCCCC | 33.00 | 23749301 | |
| 92 | Phosphorylation | SSSLFSQSQGSFGDD CCCHHCCCCCCCCCC | 35.00 | 28889911 | |
| 125 | Phosphorylation | KKSSRSLSMTSSLHK CCCCCCCCCCCCCHH | 22.66 | 23749301 | |
| 129 | Phosphorylation | RSLSMTSSLHKTASA CCCCCCCCCHHCCCC | 25.90 | 27017623 | |
| 161 | Phosphorylation | VTSVKSNSRQLSFTS EEECCCCCCEEEEEE | 28.61 | 27017623 | |
| 216 | Phosphorylation | PLLRKTVSNMDSMNH HHHHHHHCCHHHCCC | 31.50 | 28889911 | |
| 233 | Phosphorylation | ASSPVVLTMEQERVV CCCCEEEEECHHHHH | 13.67 | 27017623 | |
| 255 | Phosphorylation | TNVFYTGSAGTGKSV CCEEEECCCCCCHHH | 18.74 | 28889911 | |
| 493 | Phosphorylation | VDNAPERYQAILDSS CCCCHHHHHHHHCCC | 10.71 | 22890988 | |
| 499 | Phosphorylation | RYQAILDSSLMVEKV HHHHHHCCCCCCEEH | 23.17 | 22890988 | |
| 500 | Phosphorylation | YQAILDSSLMVEKVV HHHHHCCCCCCEEHH | 21.83 | 22890988 | |
| 565 | Phosphorylation | VMDMRLVSRVIGNPL HHCHHHHHHHHCCHH | 25.97 | 26447709 |
| 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 RRM3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RRM3_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 RRM3_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-64 AND SER-216, AND MASSSPECTROMETRY. | |
