Protein: E3 ubiquitin-protein ligase linker protein MMS1 (Methyl methanesulfonate-sensitivity protein 1) (Regulator of Ty1 transposition protein 108) (Synthetically lethal with MCM10 protein 6) (Q06211)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: 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.
Subcellular location: Nucleus {ECO:0000269|PubMed:21593207}. Note=Enriched on chromatin at sites where replication forks have stalled.
Interaction partners:
- E3 ubiquitin-protein ligase substrate receptor MMS22
- Cullin-8
- Regulator of Ty1 transposition protein 107
- RING-box protein HRT1
- ATP-dependent DNA helicase SRS2
- DNA polymerase alpha-binding protein
- ATP-dependent DNA helicase RRM3
- Histone acetyltransferase RTT109
- ATP-dependent helicase SGS1
- Mediator of replication checkpoint protein 1
Sequence:
MLGLRTHGLDRYEHYIRRPSDFGKLELQDWLNHKSFRVSPNLLIDSSTTREWNEPELFYQNTEDETWVRPCVGPKLEPSMMMLRYHDSNIGQMPQFCYPISSPINFKPVLKYILQERSELSDGFPQKYNTLIGSLFDIDKNPETLDDSDIEALDDIEMSSDSGNVKEPKIELQALEEIQQKHFSLIVSNNGIFQTGSTSITYIQSGISGSIAIKPNNVAILILLTQPSGHLLSILPLDDGKETYLLQYWNLGQKGQWNIIKHQNEKQFVLIHKELGICKFFEFHLPFTFQLVNNLTLTDSVIMNGSFFPTNYTDLDPYFIIFITAIRYERIVYFVIEWNNNEIKKKEVYQLTVFDGEKTNMTIPIGLNACLVETPLKFSLVSANQIMSGETEFHSFQLKALKGIKSFFPAPLLLLKLQELHPHTFKKFQYCTIISSSTGNICFCVTERSTIVNGNLKFYELTRFKGLKSISPLPSNPINLDSRSSSYVLVVISFSRTLELTLSLEDLRCLDKKDVIKPLKNITFKHTIDSSTEENSQILAFTSSKFYNTHTGSNINDTRNSQVWLTSPNAITQPCIDYKLRKTHQLIHLKQFQIFRHLRIWKCKNLDIALLQRLGINQSNTESSLIFATDAVSNNRIFLLDLTMTTTIDNDDPVQGLINIEDLLCDTENETILLNFTKNNLIQVTRDTIYIDPIGGDKELRKISPGWEFENVTYNDGILIVWNAGLGCVSYIENIDAVDESGALVSNLSSSKGMSKFFKQLGTVTSVNFQIKESTDDPTKYDIWILLPDCVIRTPFSDWISDSLDFSDVYILSVQQALINGPYFCSLDYESYFEVHTLQNNCFKKGSRCTSRVNFQGKDIKFRSFGVNQCLAFSAFEIFVINLTPIHDSRELDFYKLKLPHLGNNNSILEVCPDIENNQLFILYSDGLRILELSYLTSNNGNFLLKSTRSKNKKFLYLDKINRMLVLNQDLREWECIRLSDGKAVGLDSQLLKDDSEEILEIKELPIATEDNPLEKKTVLLISFTSSLKLVLLTAAKNKISNQIIDSYKLDNSRLLNHLVITPRGEIFFLDYKVMGTDNEMSFNKLKVTKHCIDQEERNNTTLRLTLETRFTFKSWSTVKTFTVVGDNIIATTNMGEKLYLIKDFSSSSDESRRVYPLEMYPDSKVQKIIPLNECCFVVAAYCGNRNDLDSRLIFYSLPTIKVGLNNETGSLPDEYGNGRVDDIFEVDFPEGFQFGTMALYDVLHGERHVNRYSEGIRSENDEAEVALRQRRNLLLFWRNHSSTPKPSLRRAATIVYEDHVSSRYFEDISSILGSTAMRTKRLSPYNAVALDKPIQDISYDPAVQTLYVLMADQTIHKFGKDRLPCQDEYEPRWNSGYLVSRRSIVKSDLICEVGLWNLSDNCKNTV