P39744 · NOC2_YEAST
- ProteinNucleolar complex protein 2
- GeneNOC2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids710 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the intranuclear transport of ribosomal precursors.
Miscellaneous
Present with 29000 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 | |
---|---|---|
Cellular Component | mitochondrion | |
Cellular Component | Noc1p-Noc2p complex | |
Cellular Component | Noc2p-Noc3p complex | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | preribosome, large subunit precursor | |
Molecular Function | mRNA binding | |
Biological Process | ribosomal large subunit biogenesis |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNucleolar complex protein 2
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP39744
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000121054 | 1-710 | Nucleolar complex protein 2 | |||
Sequence: MGKVSKSTKKFQSKHLKHTLDQRRKEKIQKKRIQGRRGNKTDQEKADAAGTREQQQLKKSAKEEVFKDMSVETFFEKGIEIPKENKKLKKKTTKEQSDEDSSSSEEEEDMGQSMAKLAEKDPEFYKYLEENDKDLLDFAGTNPLDGIDSQDEGEDAERNSNIEEKSEQMELEKEKIELSLKLVRKWKKQLHDSPSLKLLRNIISAFKVAVNLNKEENIEDYKYAITDEKAFHELMFMVLKDVPQAIQKMAPYKIVKGARTLPNGGNVSRVSSIVKSHAGSLLILLNDITNTETAALVLHSVNELMPYLLSYRRILKELIKSIVGVWSTTRELETQIASFAFLINTTKEFKKSMLETTLKTTYSTFIKSCRKTNMRSMPLINFQKNSAAELFGIDEVLGYQVGFEYIRQLAIHLRNTMNATTKKSSKINSAEAYKIVYNWQFCHSLDFWSRVLSFACQPEKENGSESPLRQLIYPLVQVTLGVIRLIPTPQFFPLRFYLIKSLIRLSQNSGVFIPIYPLLSEILTSTAFTKAPKKSPNLAAFDFEHNIKCTQAYLNTKIYQEGLSEQFVDLLGDYFALYCKNIAFPELVTPVIISLRRYIKTSTNVKLNKRLSTVVEKLNQNSTFIQEKRSDVEFGPTNKSEVSRFLNDVAWNKTPLGSYVAVQREVKEEKARLMRESMEEQDKERETEEAKLLNSLESDDDNEDVEMSDA | ||||||
Modified residue | 70 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 149 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 160 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 166 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 698 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 708 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with MAK21/NOC1 and NOC3. Forms a nucleolar complex with MAK21 that binds to 90S and 66S pre-ribosomes, as well as a nuclear complex with NOC3 that binds to 66S pre-ribosomes.
Binary interactions
Complex viewer
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-64 | Disordered | ||||
Sequence: MGKVSKSTKKFQSKHLKHTLDQRRKEKIQKKRIQGRRGNKTDQEKADAAGTREQQQLKKSAKEE | ||||||
Compositional bias | 35-64 | Basic and acidic residues | ||||
Sequence: GRRGNKTDQEKADAAGTREQQQLKKSAKEE | ||||||
Compositional bias | 76-99 | Basic and acidic residues | ||||
Sequence: EKGIEIPKENKKLKKKTTKEQSDE | ||||||
Region | 76-114 | Disordered | ||||
Sequence: EKGIEIPKENKKLKKKTTKEQSDEDSSSSEEEEDMGQSM | ||||||
Region | 138-169 | Disordered | ||||
Sequence: FAGTNPLDGIDSQDEGEDAERNSNIEEKSEQM | ||||||
Compositional bias | 153-169 | Basic and acidic residues | ||||
Sequence: GEDAERNSNIEEKSEQM | ||||||
Compositional bias | 672-698 | Basic and acidic residues | ||||
Sequence: RLMRESMEEQDKERETEEAKLLNSLES | ||||||
Region | 672-710 | Disordered | ||||
Sequence: RLMRESMEEQDKERETEEAKLLNSLESDDDNEDVEMSDA |
Sequence similarities
Belongs to the NOC2 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length710
- Mass (Da)81,601
- Last updated2000-05-30 v2
- Checksum48C3B9AE076B9B8F
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 35-64 | Basic and acidic residues | ||||
Sequence: GRRGNKTDQEKADAAGTREQQQLKKSAKEE | ||||||
Compositional bias | 76-99 | Basic and acidic residues | ||||
Sequence: EKGIEIPKENKKLKKKTTKEQSDE | ||||||
Sequence conflict | 151-179 | in Ref. 1 | ||||
Sequence: DEGEDAERNSNIEEKSEQMELEKEKIELS → MKVKMLKETVILKKNLNKWSWKRKKLSFL | ||||||
Compositional bias | 153-169 | Basic and acidic residues | ||||
Sequence: GEDAERNSNIEEKSEQM | ||||||
Sequence conflict | 231-232 | in Ref. 1; CAA39375 | ||||
Sequence: FH → LD | ||||||
Sequence conflict | 333 | in Ref. 1; CAA39375 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 360-362 | in Ref. 1; CAA39375 | ||||
Sequence: TTY → QRT | ||||||
Sequence conflict | 542 | in Ref. 1; CAA39375 | ||||
Sequence: D → H | ||||||
Compositional bias | 672-698 | Basic and acidic residues | ||||
Sequence: RLMRESMEEQDKERETEEAKLLNSLES | ||||||
Sequence conflict | 707-710 | in Ref. 1; CAA39375 | ||||
Sequence: MSDA → NVRRLTTQQDLIFCLEFNSIVYKCVNKRKVFFKAYISLCSHVLTCEHSKLSLVSWIFLYFGRFMDRKHVKRSMDLIKSNDVKQGTKMKEVRFTVIKFSKSFNSLKVPHEIDMIANITENFSTRYMISYCWKISSNLNLGAMFMDNNSWNNSFAAYGIVILIIFSALLQVVHQPL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X55891 EMBL· GenBank· DDBJ | CAA39375.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z75114 EMBL· GenBank· DDBJ | CAA99421.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006948 EMBL· GenBank· DDBJ | DAA10978.1 EMBL· GenBank· DDBJ | Genomic DNA |