| UniProt ID | MMS1_YEAST | |
|---|---|---|
| UniProt AC | Q06211 | |
| Protein Name | E3 ubiquitin-protein ligase linker protein MMS1 | |
| Gene Name | MMS1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1407 | |
| Subcellular Localization | Nucleus . Enriched on chromatin at sites where replication forks have stalled. | |
| Protein Description | Component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes (CRLs), which mediate the ubiquitination of target proteins. The CRL associates with CDC34 as the E2 ubiquitin-conjugating enzyme. The functional specificity of the CRL depends on the type of the associated substrate receptor protein. RTT101(MMS1-MMS22) promotes fork progression through damaged DNA or natural pause sites by stabilizing replication proteins like the replication fork-pausing complex (FPC) and leading-strand polymerase at stalled replication forks. RTT101(MMS1-MMS22) ubiquitinates the acetylated histones H3K56ac-H4 at lysine residues H3K121, H3K122 and H3K125. Ubiquitination is required for efficient histone deposition during replication-coupled nucleosome assembly, probably by facilitating the transfer of H3-H4 from ASF1 to other chaperones involved in histone deposition. RTT101(MMS1-CRT10) may regulate nucleotide synthesis through transcriptional regulation of ribonucleotide reductase. RTT101(MMS1) is also involved in the non-functional rRNA decay (NRD) of 25S rRNA through the selective, ubiquitination-dependent degradation of nonfunctional ribosomal particles. Involved in the regulation of TY1 transposition.. | |
| Protein Sequence | MLGLRTHGLDRYEHYIRRPSDFGKLELQDWLNHKSFRVSPNLLIDSSTTREWNEPELFYQNTEDETWVRPCVGPKLEPSMMMLRYHDSNIGQMPQFCYPISSPINFKPVLKYILQERSELSDGFPQKYNTLIGSLFDIDKNPETLDDSDIEALDDIEMSSDSGNVKEPKIELQALEEIQQKHFSLIVSNNGIFQTGSTSITYIQSGISGSIAIKPNNVAILILLTQPSGHLLSILPLDDGKETYLLQYWNLGQKGQWNIIKHQNEKQFVLIHKELGICKFFEFHLPFTFQLVNNLTLTDSVIMNGSFFPTNYTDLDPYFIIFITAIRYERIVYFVIEWNNNEIKKKEVYQLTVFDGEKTNMTIPIGLNACLVETPLKFSLVSANQIMSGETEFHSFQLKALKGIKSFFPAPLLLLKLQELHPHTFKKFQYCTIISSSTGNICFCVTERSTIVNGNLKFYELTRFKGLKSISPLPSNPINLDSRSSSYVLVVISFSRTLELTLSLEDLRCLDKKDVIKPLKNITFKHTIDSSTEENSQILAFTSSKFYNTHTGSNINDTRNSQVWLTSPNAITQPCIDYKLRKTHQLIHLKQFQIFRHLRIWKCKNLDIALLQRLGINQSNTESSLIFATDAVSNNRIFLLDLTMTTTIDNDDPVQGLINIEDLLCDTENETILLNFTKNNLIQVTRDTIYIDPIGGDKELRKISPGWEFENVTYNDGILIVWNAGLGCVSYIENIDAVDESGALVSNLSSSKGMSKFFKQLGTVTSVNFQIKESTDDPTKYDIWILLPDCVIRTPFSDWISDSLDFSDVYILSVQQALINGPYFCSLDYESYFEVHTLQNNCFKKGSRCTSRVNFQGKDIKFRSFGVNQCLAFSAFEIFVINLTPIHDSRELDFYKLKLPHLGNNNSILEVCPDIENNQLFILYSDGLRILELSYLTSNNGNFLLKSTRSKNKKFLYLDKINRMLVLNQDLREWECIRLSDGKAVGLDSQLLKDDSEEILEIKELPIATEDNPLEKKTVLLISFTSSLKLVLLTAAKNKISNQIIDSYKLDNSRLLNHLVITPRGEIFFLDYKVMGTDNEMSFNKLKVTKHCIDQEERNNTTLRLTLETRFTFKSWSTVKTFTVVGDNIIATTNMGEKLYLIKDFSSSSDESRRVYPLEMYPDSKVQKIIPLNECCFVVAAYCGNRNDLDSRLIFYSLPTIKVGLNNETGSLPDEYGNGRVDDIFEVDFPEGFQFGTMALYDVLHGERHVNRYSEGIRSENDEAEVALRQRRNLLLFWRNHSSTPKPSLRRAATIVYEDHVSSRYFEDISSILGSTAMRTKRLSPYNAVALDKPIQDISYDPAVQTLYVLMADQTIHKFGKDRLPCQDEYEPRWNSGYLVSRRSIVKSDLICEVGLWNLSDNCKNTV | |
| 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 |
|---|---|---|---|---|---|
| 20 | Phosphorylation | EHYIRRPSDFGKLEL HHHCCCHHHCCCCCH | 43.70 | 22369663 | |
| 144 | Phosphorylation | DIDKNPETLDDSDIE CCCCCCCCCCHHHCH | 36.42 | 21551504 | |
| 148 | Phosphorylation | NPETLDDSDIEALDD CCCCCCHHHCHHHHH | 39.91 | 21440633 | |
| 160 | Phosphorylation | LDDIEMSSDSGNVKE HHHEEECCCCCCCCC | 34.19 | 21551504 | |
| 688 | Phosphorylation | LIQVTRDTIYIDPIG EEEEECCEEEEECCC | 16.64 | 27017623 | |
| 690 | Phosphorylation | QVTRDTIYIDPIGGD EEECCEEEEECCCCC | 11.02 | 27017623 | |
| 1077 | Phosphorylation | LDYKVMGTDNEMSFN EEEEEECCCCCCCCC | 19.97 | 21551504 | |
| 1082 | Phosphorylation | MGTDNEMSFNKLKVT ECCCCCCCCCEEEEE | 21.35 | 21551504 | |
| 1089 | Phosphorylation | SFNKLKVTKHCIDQE CCCEEEEEEECCCHH | 17.30 | 21551504 | |
| 1121 | Phosphorylation | KSWSTVKTFTVVGDN CCCCEEEEEEEECCC | 21.87 | 21440633 | |
| 1132 | Phosphorylation | VGDNIIATTNMGEKL ECCCEEEECCCCCEE | 14.32 | 21440633 | |
| 1216 | Phosphorylation | TGSLPDEYGNGRVDD CCCCCCCCCCCCCCC | 24.22 | 27017623 | |
| 1294 | Phosphorylation | PSLRRAATIVYEDHV HHHHHHEEEEECCCC | 15.25 | 17330950 |
| 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 MMS1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MMS1_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 MMS1_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-20 AND THR-1294, ANDMASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1294, AND MASSSPECTROMETRY. | |
