Q06164 · MMS22_YEAST
- ProteinE3 ubiquitin-protein ligase substrate receptor MMS22
- GeneMMS22
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1454 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-MMS22). 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.
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 | DNA damage response | |
Biological Process | double-strand break repair | |
Biological Process | double-strand break repair via homologous recombination | |
Biological Process | meiotic sister chromatid segregation | |
Biological Process | nucleosome assembly | |
Biological Process | recombinational repair | |
Biological Process | replication fork processing |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase substrate receptor MMS22
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ06164
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Nuclear punctate foci structures.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000257821 | 1-1454 | E3 ubiquitin-protein ligase substrate receptor MMS22 | |||
Sequence: MDVDEPNPIVISDSEATDEEISIIYEPEFNENYLWAEENVQEASRSQKIVTERLSLDSTAGESCTPSVVTDTQVTTGLRWSLRKRKAIQKMPYSLERIKHRQLLEGYDISSFDSISNQLTLPKNASTVIHSNDILLTKRTGKPLDEQKDVTIDSIKPENSSVQSQRYDSDEEIPKKRHRTFKDLDQDIVFQSGDSTEDEQDLASTNLQNTQNDEVIFRGRVLNVRTGYRGVLPRVAWEKSLQKQQSSKVTKRKTQLLNHKGVAKRKMNRSAHIEDEEQNLLNDLIAPDDELDIEENAPPDIYLGNLPEDREANEKELKELQEYYESKYSEDAQSAGTSGFNLNEEYRNEPVYELEYDGPGSCISHVSYKDQPIIYLNSRHSDSGFSEQYNISAEDNQSVISLDAAEEHNDGIIDKMLVKPKRIKATNDANFLNTKSKRVRRYKYKYRNSCLAPSTKAIKVGKRSAHKSHLAANNPVSFVSKKNHVIDDYFFEELESQSLEQDDSSSLKPQKKRRKKKAPIYSSFSADLESRRKPVFNTVVEVPTNRYAFTKPNVRNRDSINHDMEFEEEDSNQELGPIMVVLDSILLKKPFEPPNFFKIQLSDKSFLLSKLNPADIATSLQKIFRVIIDKGITDTELVHFNESLIAFLVHLDMPELFDLIGEFHREFRSKVNSLRKKAKPIHFFQIAACQLMFLEISRYNKISAAAKFDMDVKLLDHIVSFFKLLSVCYDSVMKNPMQYLYTSYYILSAVVDVIHKKEALWDLFQKHPFSPHISLLLVNIFPTKVCRWQVLRLDSEFQPLSSAFRFINYCIETCNWNVTNSLILSLDRIFKRRRFSDFEEESDLSQNNKIIYPPTNQLTSRLMFNRYLHLLTLCELSSSDTQRVIPMGDISMNDSLSVLKNRLNLLIVLATRFDLNLEKRFQELTRPLYSKEYLNLHTQNTVRTITTLIMQASLSFLEISRIKNHPFSGKFIASLFDKLVLQQPSISGVTENFLKEFTNLVSKMKRKSVSMLKFLYPSLVAMSQENIFESSFFLLLQVYLKSLDVLGPTWVQNYLFQFIKSKAQENERWIECYCQIGKFLVDSGIFTWWTFFTYNGLDAALHFQLAFHSLIIDFCDTDSFELLKKPLYSIASDLLLISKDDAFYHFLSNLLKRAHIIVADLKPVSDENELLRLAYIFSKALKKNAYQDLLAVFLSLAKKHYDEGDISRNFLAKYLEFLNKNCLTELRNNQLFISLRRELGISSDEDEKCAFWDSFNEAGDILSKAAFVETGIVQACCTGNEIDGYLDNLSTLFTSTMLESPFAFFSDLVIAHIFENRPFFDVNIKNFLLSHFIDLFNKVLKMKFEQVSPDEFAELCKVYRALCIECATDDTFNSNSDLIAAKDAFLVSVLRIADGFWEHDKLLQLRMLDSNMNIPNQIPHTTLQSSLSAIVIKIIESNIGKIEASEPFKTFKNT |
Proteomic databases
PTM databases
Interaction
Subunit
Component of a cullin-RING ligase (CRL) composed of 4 subunits: the RING protein HRT1, the cullin RTT101, a linker protein MMS1, and 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. Interacts (via C-ter) with MMS1 (via N-ter). Interacts with RTT107.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q06164 | CTF4 Q01454 | 4 | EBI-31156, EBI-5209 | |
BINARY | Q06164 | MMS1 Q06211 | 9 | EBI-31156, EBI-38894 | |
BINARY | Q06164 | RTT101 P47050 | 11 | EBI-31156, EBI-25861 | |
BINARY | Q06164 | RTT107 P38850 | 9 | EBI-31156, EBI-24788 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 159-178 | Disordered | ||||
Sequence: NSSVQSQRYDSDEEIPKKRH | ||||||
Region | 1201-1454 | Required for interaction with MMS1 | ||||
Sequence: YDEGDISRNFLAKYLEFLNKNCLTELRNNQLFISLRRELGISSDEDEKCAFWDSFNEAGDILSKAAFVETGIVQACCTGNEIDGYLDNLSTLFTSTMLESPFAFFSDLVIAHIFENRPFFDVNIKNFLLSHFIDLFNKVLKMKFEQVSPDEFAELCKVYRALCIECATDDTFNSNSDLIAAKDAFLVSVLRIADGFWEHDKLLQLRMLDSNMNIPNQIPHTTLQSSLSAIVIKIIESNIGKIEASEPFKTFKNT |
Sequence similarities
Belongs to the MMS22 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,454
- Mass (Da)167,683
- Last updated1996-11-01 v1
- ChecksumEE9797D4A12A7488
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U20618 EMBL· GenBank· DDBJ | AAB64521.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006945 EMBL· GenBank· DDBJ | DAA09629.1 EMBL· GenBank· DDBJ | Genomic DNA |