Q08226 · CRT10_YEAST
- ProteinProtein CRT10
- GeneCRT10
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids957 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-CRT10). RTT101(MMS1-CRT10) may regulate nucleotide synthesis through transcriptional regulation of RNR genes encoding ribonucleotide reductases.
Miscellaneous
Present with 125 molecules/cell in log phase SD medium.
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 | |
---|---|---|
Biological Process | nonfunctional rRNA decay |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein CRT10
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ08226
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000235920 | 1-957 | Protein CRT10 | |||
Sequence: MPPQIPNENDDLFTRWLKSRAIIQRAVSTRECFDSEVFLASGGWNITNEIITLKKYYQLKWPNSSCNSFHPKTVEFIKERLHNLEEHDSSWKIPNPAYSFKKAFLEDTKSAFSNLEPVWGPSRLLNPAELLLPQDEKLLVQEIPLEFAPFQYTNRFAYGGLQFKNNLFVTYGSYSFLAAGQCVEVHNFDILLNVSSLEICHALLPVIIPDDGDVRNFRNSSYVKFKDTQFNSIPELCSINFMKICNFMHQDFLLACGDNGIVYIWEINKVIKIFNKFTSDILGGKDNSRERYINVDPYMVLRVEESCWSVDVIDINGIIYIAVGHNKPGVTVFAFDKDVKKERRYIRPLDLPSSHNVPCVNFVPNSKDSVGYITLSYCSIFGNVVTVKLKEHDCTILTSFLDTQFFGDDLWTITPLTKKDFAKVDNFELLNLNYQDGFKESMLYSICRDDFLLGYYCDNAYLSGNFGIGTLLNQFQVPVTDLRLTSSAGIPDEVIPLRFTSFDRNYTTTGSIKYEYSREDFALILHAGDLDDMNDAVTKNTSCEQHLHQWTFWEDSGYKHYRATERGFSKYKDIINTFPQLITPSGRNKTSQYQNTSGRKICEPSTYKLTDLENDIEDISREFNRSIRNLKMDKQRQLRTSKEFKSLSSVNHIPNIESGNFLWYNTDAAADWRTLFGKDLNTVLKDPEICSLQLNSTEEDDVNSDPENEESGSSLTSFQRRYRDTEQRAHLKSESQKSWGFHNYVRNVKRLLESAVPGSEDSPLGYQLSEMHDEFFFLTTAHRLVLMKANPLIIISATHHEIFPLDGVVTCASKSLLQALNRINFVCHIKELNCIAVASQLGLISLLRLTEYRGIYSFRQEYILGWEVQDPVNPSPECRCNRNLFDAPMYGADGESSDTYCGVCDVYFPMGDICGLDYTYASDSEELKRKGYATLYVASRGSLRAFKITTEHGTTQQ | ||||||
Modified residue | 704 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
By DNA damage and hydroxyurea (HU).
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 CRT10. Interacts with MMS1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q08226 | RTT101 P47050 | 2 | EBI-30025, EBI-25861 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length957
- Mass (Da)109,715
- Last updated1996-11-01 v1
- ChecksumEBBB9627C335EFD3
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 604 | in Ref. 3; AAT92715 | ||||
Sequence: P → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z74804 EMBL· GenBank· DDBJ | CAA99072.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z74805 EMBL· GenBank· DDBJ | CAA99073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY692696 EMBL· GenBank· DDBJ | AAT92715.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006948 EMBL· GenBank· DDBJ | DAA10720.1 EMBL· GenBank· DDBJ | Genomic DNA |