Q63850 · NUP62_MOUSE
- ProteinNuclear pore glycoprotein p62
- GeneNup62
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids526 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Essential component of the nuclear pore complex. The N-terminal is probably involved in nucleocytoplasmic transport. The C-terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of p62 to the pore complex. Plays a role in mitotic cell cycle progression by regulating centrosome segregation, centriole maturation and spindle orientation. It might be involved in protein recruitment to the centrosome after nuclear breakdown.
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
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNuclear pore glycoprotein p62
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ63850
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Central region of the nuclear pore, within the transporter. During mitotic cell division, it associates with the poles of the mitotic spindle.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 479 | Loss of reduction of influx rate of NLS cargo upon oxidative stress; when associated with S-509. | ||||
Sequence: C → S | ||||||
Mutagenesis | 510 | Loss of reduction of influx rate of NLS cargo upon oxidative stress; when associated with S-478. | ||||
Sequence: C → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 18 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000204881 | 2-526 | Nuclear pore glycoprotein p62 | |||
Sequence: SGFNFGGTGAPAGGFTFGTAKTATTTPATGFSFSASGTGTGGFNFGTPSQPAATTPSTSLFSLTTQTPTTQTPGFNFGTTPASGGTGFSLGISTPKLSLSNAAATPATANTGSFGLGSSTLTNAISSGSTSNQGTAPTGFVFGSSTTSAPSTGSTGFSFTSGSASQPGASGFSLGSVGSSAQPTALSGSPFTPATLVTTTAGATQPAAAAPTAATTSAGSTLFASIAAAPASSSATGLSLPAPVTTAATPSAGTLGFSLKAPGAAPGASTTSTTTTTTTTTTTAAAAAASTTTTGFALSLKPLVSAGPSSVAATALPASSTAAGTATGPAMTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEESVKEQSGTIYLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHLNMAGGPADTSDPLQQICKILNAHMDSLQWVDQSSALLQRRVEEASRVCEGRRKEQERSLRIAFD | ||||||
Glycosylation | 377 | O-linked (GlcNAc) threonine | ||||
Sequence: T | ||||||
Modified residue | 412 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 422 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 472 | O-linked (GlcNAc) serine | ||||
Sequence: S | ||||||
Disulfide bond | 479 | Interchain (with NUP155) | ||||
Sequence: C | ||||||
Disulfide bond | 510 | Interchain (with NUP155) | ||||
Sequence: C |
Post-translational modification
O-glycosylated.
The inner channel of the NPC has a different redox environment from the cytoplasm and allows the formation of interchain disulfide bonds between some nucleoporins, the significant increase of these linkages upon oxidative stress reduces the permeability of the NPC.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Component of the p62 complex, a complex at least composed of NUP62, NUP54, and NUP58. Interacts with NUP88. Interacts with NUTF2. Interacts with HIKESHI. Interacts with OSBPL8. Interacts with CAPG. Interacts with SAS6 and TUBG1 at the centrosome. Interacts with MCM3AP (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 6-7 | 1 | ||||
Sequence: FG | ||||||
Region | 6-144 | 5 X 2 AA repeats of F-G | ||||
Sequence: FGGTGAPAGGFTFGTAKTATTTPATGFSFSASGTGTGGFNFGTPSQPAATTPSTSLFSLTTQTPTTQTPGFNFGTTPASGGTGFSLGISTPKLSLSNAAATPATANTGSFGLGSSTLTNAISSGSTSNQGTAPTGFVFG | ||||||
Region | 43-82 | Disordered | ||||
Sequence: GFNFGTPSQPAATTPSTSLFSLTTQTPTTQTPGFNFGTTP | ||||||
Repeat | 46-47 | 2 | ||||
Sequence: FG | ||||||
Repeat | 78-79 | 3 | ||||
Sequence: FG | ||||||
Repeat | 115-116 | 4 | ||||
Sequence: FG | ||||||
Region | 128-148 | Disordered | ||||
Sequence: SGSTSNQGTAPTGFVFGSSTT | ||||||
Repeat | 143-144 | 5 | ||||
Sequence: FG | ||||||
Region | 332-462 | Required for centrosome localization | ||||
Sequence: MTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEESVKEQSGTIYLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHL | ||||||
Coiled coil | 332-462 | |||||
Sequence: MTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEESVKEQSGTIYLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHL |
Domain
Contains FG repeats.
Sequence similarities
Belongs to the nucleoporin NSP1/NUP62 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length526
- Mass (Da)53,255
- Last updated2002-05-27 v2
- Checksum54AE74B211018FE4
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A140LJH5 | A0A140LJH5_MOUSE | Nup62 | 42 | ||
A0A140LJ77 | A0A140LJ77_MOUSE | Nup62 | 159 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 113 | in Ref. 1; AAB19953 | ||||
Sequence: G → V | ||||||
Sequence conflict | 319 | in Ref. 1; AAB19953 | ||||
Sequence: A → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
S59342 EMBL· GenBank· DDBJ | AAB19953.1 EMBL· GenBank· DDBJ | mRNA | ||
BC005784 EMBL· GenBank· DDBJ | AAH05784.1 EMBL· GenBank· DDBJ | mRNA |