Q06211 · MMS1_YEAST
- ProteinE3 ubiquitin-protein ligase linker protein MMS1
- GeneMMS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1407 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | Cul8-RING ubiquitin ligase complex | |
Cellular Component | nucleus | |
Biological Process | cell division | |
Biological Process | heterochromatin formation | |
Biological Process | nonfunctional rRNA decay | |
Biological Process | nucleosome assembly | |
Biological Process | recombinational repair | |
Biological Process | regulation of DNA replication | |
Biological Process | replication fork processing | |
Biological Process | retrotransposon silencing |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase linker protein MMS1
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ06211
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Enriched on chromatin at sites where replication forks have stalled.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000257820 | 1-1407 | E3 ubiquitin-protein ligase linker protein MMS1 | |||
Sequence: MLGLRTHGLDRYEHYIRRPSDFGKLELQDWLNHKSFRVSPNLLIDSSTTREWNEPELFYQNTEDETWVRPCVGPKLEPSMMMLRYHDSNIGQMPQFCYPISSPINFKPVLKYILQERSELSDGFPQKYNTLIGSLFDIDKNPETLDDSDIEALDDIEMSSDSGNVKEPKIELQALEEIQQKHFSLIVSNNGIFQTGSTSITYIQSGISGSIAIKPNNVAILILLTQPSGHLLSILPLDDGKETYLLQYWNLGQKGQWNIIKHQNEKQFVLIHKELGICKFFEFHLPFTFQLVNNLTLTDSVIMNGSFFPTNYTDLDPYFIIFITAIRYERIVYFVIEWNNNEIKKKEVYQLTVFDGEKTNMTIPIGLNACLVETPLKFSLVSANQIMSGETEFHSFQLKALKGIKSFFPAPLLLLKLQELHPHTFKKFQYCTIISSSTGNICFCVTERSTIVNGNLKFYELTRFKGLKSISPLPSNPINLDSRSSSYVLVVISFSRTLELTLSLEDLRCLDKKDVIKPLKNITFKHTIDSSTEENSQILAFTSSKFYNTHTGSNINDTRNSQVWLTSPNAITQPCIDYKLRKTHQLIHLKQFQIFRHLRIWKCKNLDIALLQRLGINQSNTESSLIFATDAVSNNRIFLLDLTMTTTIDNDDPVQGLINIEDLLCDTENETILLNFTKNNLIQVTRDTIYIDPIGGDKELRKISPGWEFENVTYNDGILIVWNAGLGCVSYIENIDAVDESGALVSNLSSSKGMSKFFKQLGTVTSVNFQIKESTDDPTKYDIWILLPDCVIRTPFSDWISDSLDFSDVYILSVQQALINGPYFCSLDYESYFEVHTLQNNCFKKGSRCTSRVNFQGKDIKFRSFGVNQCLAFSAFEIFVINLTPIHDSRELDFYKLKLPHLGNNNSILEVCPDIENNQLFILYSDGLRILELSYLTSNNGNFLLKSTRSKNKKFLYLDKINRMLVLNQDLREWECIRLSDGKAVGLDSQLLKDDSEEILEIKELPIATEDNPLEKKTVLLISFTSSLKLVLLTAAKNKISNQIIDSYKLDNSRLLNHLVITPRGEIFFLDYKVMGTDNEMSFNKLKVTKHCIDQEERNNTTLRLTLETRFTFKSWSTVKTFTVVGDNIIATTNMGEKLYLIKDFSSSSDESRRVYPLEMYPDSKVQKIIPLNECCFVVAAYCGNRNDLDSRLIFYSLPTIKVGLNNETGSLPDEYGNGRVDDIFEVDFPEGFQFGTMALYDVLHGERHVNRYSEGIRSENDEAEVALRQRRNLLLFWRNHSSTPKPSLRRAATIVYEDHVSSRYFEDISSILGSTAMRTKRLSPYNAVALDKPIQDISYDPAVQTLYVLMADQTIHKFGKDRLPCQDEYEPRWNSGYLVSRRSIVKSDLICEVGLWNLSDNCKNTV | ||||||
Modified residue | 1294 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Component of multiple cullin-RING ligases (CRLs) composed of 4 subunits: the RING protein HRT1, the cullin RTT101, a linker protein MMS1, and one of many alternative substrate receptors belonging to a protein family described as DCAF (DDB1- and CUL4-associated factor). Component of a RTT101(MMS1-MMS22) complex with the substrate receptor MMS22. This complex further interacts with RTT107 and CTF4 to form RTT101-MMS1-MMS22-RTT107 and RTT101-MMS1-MMS22-CTF4 complexes respectively. Component of a RTT101(MSS1-CRT10) complex with the substrate receptor CRT10. Component of a RTT101(MSS1-ESC2) complex with the potential substrate receptor ESC2. Component of a RTT101(MSS1-ORC5) complex with the potential substrate receptor ORC5. Interacts with RTT101 (via N-ter). Interacts (via N-ter) with MMS22 (via C-ter). Interacts with CRT10.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q06211 | ESC2 Q06340 | 5 | EBI-38894, EBI-33799 | |
BINARY | Q06211 | HRT1 Q08273 | 3 | EBI-38894, EBI-31686 | |
BINARY | Q06211 | MMS22 Q06164 | 9 | EBI-38894, EBI-31156 | |
BINARY | Q06211 | ORC5 P50874 | 4 | EBI-38894, EBI-12584 | |
BINARY | Q06211 | RTT101 P47050 | 13 | EBI-38894, EBI-25861 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-600 | Required for interaction with MMS22 | ||||
Sequence: MLGLRTHGLDRYEHYIRRPSDFGKLELQDWLNHKSFRVSPNLLIDSSTTREWNEPELFYQNTEDETWVRPCVGPKLEPSMMMLRYHDSNIGQMPQFCYPISSPINFKPVLKYILQERSELSDGFPQKYNTLIGSLFDIDKNPETLDDSDIEALDDIEMSSDSGNVKEPKIELQALEEIQQKHFSLIVSNNGIFQTGSTSITYIQSGISGSIAIKPNNVAILILLTQPSGHLLSILPLDDGKETYLLQYWNLGQKGQWNIIKHQNEKQFVLIHKELGICKFFEFHLPFTFQLVNNLTLTDSVIMNGSFFPTNYTDLDPYFIIFITAIRYERIVYFVIEWNNNEIKKKEVYQLTVFDGEKTNMTIPIGLNACLVETPLKFSLVSANQIMSGETEFHSFQLKALKGIKSFFPAPLLLLKLQELHPHTFKKFQYCTIISSSTGNICFCVTERSTIVNGNLKFYELTRFKGLKSISPLPSNPINLDSRSSSYVLVVISFSRTLELTLSLEDLRCLDKKDVIKPLKNITFKHTIDSSTEENSQILAFTSSKFYNTHTGSNINDTRNSQVWLTSPNAITQPCIDYKLRKTHQLIHLKQFQIFRHLRI |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,407
- Mass (Da)161,238
- Last updated1996-11-01 v1
- ChecksumCC698C422631A7D7
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U25840 EMBL· GenBank· DDBJ | AAB68151.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U14001 EMBL· GenBank· DDBJ | AAG02022.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006949 EMBL· GenBank· DDBJ | DAA11581.1 EMBL· GenBank· DDBJ | Genomic DNA |