P16554 · NUMB_DROME
- ProteinProtein numb
- Genenumb
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids556 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required in determination of cell fate during sensory organ formation in embryos (PubMed:2752427).
Restricts developmental potential and promote maturation of intermediary neuronal progenitor (INP) cells probably acting as an antagonist of Notch signaling (PubMed:18342578, PubMed:24550111, PubMed:28899667).
Restricts developmental potential and promote maturation of intermediary neuronal progenitor (INP) cells probably acting as an antagonist of Notch signaling (PubMed:18342578, PubMed:24550111, PubMed:28899667).
Features
Showing features for binding site.
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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Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProtein numb
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP16554
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In larval brain, shows asymmetric localization and asymmetrically sized divisions in type II secondary neuroblasts.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
In larval brain, leads to overgrowth and defective differentiation halting the development of secondary neuroblasts beyond the stage of immature type II intermediary neuronal progenitors (INP).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 24-56 | Reduced cortical localization and increased cytoplasmic localization. | ||||
Sequence: Missing | ||||||
Mutagenesis | 36-37 | Slight reduction in cortical localization. | ||||
Sequence: KK → DD | ||||||
Mutagenesis | 46-47 | In 4R-D; phosphomimetic mutant that displays decreased phospholipid binding and reduced cortical localization; when associated with D-54 and D-55. | ||||
Sequence: RR → DD | ||||||
Mutagenesis | 48 | In 2S-A; loss of phosphorylation. In the presence of aPKC remains localized to the cell cortex and does not display any decrease in phospholipid binding; when associated with A-52. | ||||
Sequence: S → A | ||||||
Mutagenesis | 48 | In 2S-D; phosphomimetic mutant that displays reduced cortical localization but no significant decrease in phospholipid binding; when associated with D-52. | ||||
Sequence: S → D | ||||||
Mutagenesis | 52 | In 2S-A; loss of phosphorylation. In the presence of aPKC remains localized to the cell cortex and does not display any decrease in phospholipid binding; when associated with A-48. | ||||
Sequence: S → A | ||||||
Mutagenesis | 52 | In 2S-D; phosphomimetic mutant that displays reduced cortical localization but no significant decrease in phospholipid binding; when associated with D-48. | ||||
Sequence: S → D | ||||||
Mutagenesis | 54-55 | In 4R-D; phosphomimetic mutant that displays decreased phospholipid binding and reduced cortical localization; when associated with D-46 and D-47. | ||||
Sequence: RR → DD | ||||||
Mutagenesis | 144 | Loss of binding affinity to Nak and drop in binding to single helical peptide. | ||||
Sequence: I → A | ||||||
Mutagenesis | 147 | Loss of binding affinity to Nak and drop in binding to single helical peptide. | ||||
Sequence: V → A | ||||||
Mutagenesis | 149 | Loss of binding affinity to Nak and single helical peptide. | ||||
Sequence: F → V | ||||||
Mutagenesis | 195 | Loss of binding affinity to Nak and single helical peptide. | ||||
Sequence: F → V |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000021869 | 1-556 | Protein numb | |||
Sequence: MGNSSSHTHEPLERGFTRGKFGDVKNGKSASFRFSKKSPKKMDRLRRSFRDSFRRRKDRVPESSKPHQWQADEEAVRSATCSFSVKYLGCVEVFESRGMQVCEEALKVLRQSRRRPVRGLLHVSGDGLRVVDDETKGLIVDQTIEKVSFCAPDRNHERGFSYICRDGTTRRWMCHGFLACKDSGERLSHAVGCAFAVCLERKQRRDKECGVTMTFDTKNSTFTRTGSFRQQTLTERLAMATVGTNERSVDGPGSAMPGPPAATVKPFNPFAIERPHATPNMLERQSSFRLSTIGSQSPFKRQMSLRINDLPSNADRQRAFLTAAAGNPMQTPLRSVSPIAEVSPAKSAGADPLSAAAVAADSVSQLCQELSQGLSLLTQTDALLAAGEDLNFNNNRSINQNIIAAEKQVQHVHSYAPPTAQVTPRVASTTPTYQTLHSQSPSRSEQSIETSTELPNAEQWLGHVVRSTSPAAPKRPTYLANVGRAQTLASGTGAAVGGGGPDDPFDAEWVANVAAAKQLSPDLPIPSTARSPLARHSTNPFISPPKAPAQSFQVQL | ||||||
Modified residue | 430 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 537 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 543 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by aPKC which lowers lipid affinity and promotes dissociation from the cell cortex.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with Nak.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P16554 | PRKCZ Q05513 | 2 | EBI-429581, EBI-295351 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-71 | Disordered | ||||
Sequence: MGNSSSHTHEPLERGFTRGKFGDVKNGKSASFRFSKKSPKKMDRLRRSFRDSFRRRKDRVPESSKPHQWQA | ||||||
Region | 15-86 | Phospho-regulated basic and hydrophobic (PRBH) motif | ||||
Sequence: GFTRGKFGDVKNGKSASFRFSKKSPKKMDRLRRSFRDSFRRRKDRVPESSKPHQWQADEEAVRSATCSFSVK | ||||||
Compositional bias | 44-71 | Basic and acidic residues | ||||
Sequence: RLRRSFRDSFRRRKDRVPESSKPHQWQA | ||||||
Domain | 81-208 | PID | ||||
Sequence: CSFSVKYLGCVEVFESRGMQVCEEALKVLRQSRRRPVRGLLHVSGDGLRVVDDETKGLIVDQTIEKVSFCAPDRNHERGFSYICRDGTTRRWMCHGFLACKDSGERLSHAVGCAFAVCLERKQRRDKE | ||||||
Region | 519-556 | Disordered | ||||
Sequence: LSPDLPIPSTARSPLARHSTNPFISPPKAPAQSFQVQL | ||||||
Compositional bias | 531-556 | Polar residues | ||||
Sequence: SPLARHSTNPFISPPKAPAQSFQVQL |
Domain
PTB domain recognizes multiple ligands by engaging different amounts of surface area dictated by tertiary contacts rather than primary sequence. This may allow interactions with a diverse set of proteins during asymmetric division and specification of cell fate.
The phospho-regulated basic and hydrophobic (PRBH) motif is necessary and sufficient for interaction with phospholipids permitting cortical localization (PubMed:26481050).
Phosphorylation of the PRBH motif by aPKC inhibits the association of the protein with the cortical membrane (PubMed:26481050).
Phosphorylation of the PRBH motif by aPKC inhibits the association of the protein with the cortical membrane (PubMed:26481050).
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative initiation.
P16554-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameZygotic
- SynonymsA
- Length556
- Mass (Da)60,614
- Last updated2004-08-31 v2
- Checksum91B26959B5DE8405
P16554-2
- NameMaternal
- SynonymsB
- Differences from canonical
- 1-41: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
M9PCN6 | M9PCN6_DROME | numb | 556 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_018787 | 1-41 | in isoform Maternal | |||
Sequence: Missing | ||||||
Compositional bias | 44-71 | Basic and acidic residues | ||||
Sequence: RLRRSFRDSFRRRKDRVPESSKPHQWQA | ||||||
Sequence conflict | 322 | in Ref. 1; AAA28730 | ||||
Sequence: T → A | ||||||
Sequence conflict | 326 | in Ref. 1; AAA28730 | ||||
Sequence: G → D | ||||||
Sequence conflict | 329 | in Ref. 1; AAA28730 | ||||
Sequence: M → L | ||||||
Sequence conflict | 353 | in Ref. 1; AAA28730 | ||||
Sequence: L → S | ||||||
Sequence conflict | 386 | in Ref. 1; AAA28730 | ||||
Sequence: A → T | ||||||
Compositional bias | 531-556 | Polar residues | ||||
Sequence: SPLARHSTNPFISPPKAPAQSFQVQL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M27815 EMBL· GenBank· DDBJ | AAA28730.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014134 EMBL· GenBank· DDBJ | AAF52776.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014134 EMBL· GenBank· DDBJ | AAN10693.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT056305 EMBL· GenBank· DDBJ | ACL68752.1 EMBL· GenBank· DDBJ | mRNA | ||
BT056311 EMBL· GenBank· DDBJ | ACL68758.1 EMBL· GenBank· DDBJ | mRNA | ||
AY051728 EMBL· GenBank· DDBJ | AAK93152.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |