Q2LC84 · NUMB_RAT
- ProteinProtein numb homolog
- GeneNumb
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids652 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Regulates clathrin-mediated receptor endocytosis (By similarity).
Plays a role in the process of neurogenesis. Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate. Not required for the proliferation of neural progenitor cells before the onset of neurogenesis. Also involved postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity. May also mediate local repair of brain ventricular wall damage (By similarity).
Plays a role in the process of neurogenesis. Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate. Not required for the proliferation of neural progenitor cells before the onset of neurogenesis. Also involved postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity. May also mediate local repair of brain ventricular wall damage (By similarity).
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
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein numb homolog
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ2LC84
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Endosome membrane ; Peripheral membrane protein
Note: Localizes to perinuclear endosomes in an AAK1-dependent manner.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 275 | Loss of phosphorylation by CaMK1. | ||||
Sequence: S → A | ||||||
Mutagenesis | 294 | Loss of phosphorylation by CaMK1. | ||||
Sequence: S → A |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000412901 | 1-652 | Protein numb homolog | |||
Sequence: MNKLRQSFRRKKDVYVPEASRPHQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKAERKFFKGFFGKTGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLERKQKREKECGVTATFDASRTTFTREGSFRVTTATEQAEREEIMKQLQDAKKAETDKTVGPSVAPGNSAPSPSSPTSPTLDPTASLEMNNPHAIPRRHAPIEQLARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDFPIKNTVPEVEGEAESISSLCSQITSAFSTPCEDPFSSAPMTKPVTLVAPQSPVLQANGTDSALHVLTAKPASTALAPVAMPVRETNPWAHAPDAANKEIAAIHSGTEWGQSSGAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPAAIAPPAPPFQGHAFLTSQPVPVGVVPPLQPAFVSTQSYPVANGMPYPASNVPVVGITPSQMVANVFGTAGHPQATHPHQSPSLAKQQTFPQYETSSATTSPFFKPSAQHLNGSAAFNGVDNSGLVSGNRPAQVPPGTCPVDPFEAQWAALESKPKQRTNPSPTNPFSSDAQKAFEIEL | ||||||
Modified residue | 102 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 194 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 242 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 243 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 275 | Phosphoserine; by CaMK1 | ||||
Sequence: S | ||||||
Modified residue | 294 | Phosphoserine; by CaMK1 | ||||
Sequence: S | ||||||
Modified residue | 426 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 437 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 439 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 635 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated on Ser-275 and Ser-294 by CaMK1.
Isoform 1 and isoform 2 are ubiquitinated by LNX leading to their subsequent proteasomal degradation. Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with SIAH1 (By similarity).
Interacts with LNX (By similarity).
Interacts with CDH1 (By similarity).
Interacts with TFAP2A and TFAP2B (PubMed:17022975).
Interacts with RALBP1 in a complex also containing EPN1 and TFAP2A during interphase and mitosis (By similarity).
Interacts with AAK1 (By similarity).
May interact with DUOXA1 (By similarity).
Interacts with LNX (By similarity).
Interacts with CDH1 (By similarity).
Interacts with TFAP2A and TFAP2B (PubMed:17022975).
Interacts with RALBP1 in a complex also containing EPN1 and TFAP2A during interphase and mitosis (By similarity).
Interacts with AAK1 (By similarity).
May interact with DUOXA1 (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 37-173 | PID | ||||
Sequence: CSFPVKYLGHVEVDESRGMHICEDAVKRLKAERKFFKGFFGKTGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLERKQKRE | ||||||
Region | 213-256 | Disordered | ||||
Sequence: LQDAKKAETDKTVGPSVAPGNSAPSPSSPTSPTLDPTASLEMNN | ||||||
Region | 418-440 | Disordered | ||||
Sequence: WGQSSGAASPGLFQAGHRRTPSE | ||||||
Region | 543-580 | Disordered | ||||
Sequence: AGHPQATHPHQSPSLAKQQTFPQYETSSATTSPFFKPS | ||||||
Compositional bias | 547-580 | Polar residues | ||||
Sequence: QATHPHQSPSLAKQQTFPQYETSSATTSPFFKPS | ||||||
Region | 624-652 | Disordered | ||||
Sequence: LESKPKQRTNPSPTNPFSSDAQKAFEIEL | ||||||
Compositional bias | 626-644 | Polar residues | ||||
Sequence: SKPKQRTNPSPTNPFSSDA |
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q2LC84-1
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.
- Name1
- Synonymsi/i
- Length652
- Mass (Da)70,596
- Last updated2011-09-21 v2
- ChecksumB4AD582D3A0CA45A
Q2LC84-2
- Name2
- Differences from canonical
- 68-78: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_041811 | 68-78 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 459 | in Ref. 1; ABC69737 | ||||
Sequence: A → V | ||||||
Compositional bias | 547-580 | Polar residues | ||||
Sequence: QATHPHQSPSLAKQQTFPQYETSSATTSPFFKPS | ||||||
Compositional bias | 626-644 | Polar residues | ||||
Sequence: SKPKQRTNPSPTNPFSSDA |
Keywords
- Coding sequence diversity
- Technical term