Q8WUM0 · NU133_HUMAN
- ProteinNuclear pore complex protein Nup133
- GeneNUP133
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1156 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in poly(A)+ RNA transport. Involved in nephrogenesis (PubMed:30179222).
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 | cytosol | |
Cellular Component | kinetochore | |
Cellular Component | membrane | |
Cellular Component | nuclear envelope | |
Cellular Component | nuclear membrane | |
Cellular Component | nuclear pore | |
Cellular Component | nuclear pore outer ring | |
Molecular Function | structural constituent of nuclear pore | |
Biological Process | mRNA export from nucleus | |
Biological Process | nephron development | |
Biological Process | neural tube development | |
Biological Process | neurogenesis | |
Biological Process | nuclear pore organization | |
Biological Process | nucleocytoplasmic transport | |
Biological Process | paraxial mesoderm development | |
Biological Process | poly(A)+ mRNA export from nucleus | |
Biological Process | protein import into nucleus | |
Biological Process | somite development | |
Biological Process | transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameNuclear pore complex protein Nup133
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8WUM0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Nephrotic syndrome 18 (NPHS18)
- Note
- DescriptionA form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form that progresses to end-stage renal failure. NPHS18 is an autosomal recessive, steroid-resistant progressive form with onset in the first decade of life.
- See alsoMIM:618177
Natural variants in NPHS18
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_081359 | 231 | R>G | in NPHS18; decreased function in nephrogenesis; unable to fully rescue morpholino-induced nephrogenesis defects in Xenopus; dbSNP:rs1558108130 | |
VAR_081360 | 974 | S>R | in NPHS18; loss of function in nephrogenesis; unable to rescue morpholino-induced nephrogenesis defects in Xenopus; decreased interaction with NUP107; dbSNP:rs1558091788 | |
VAR_081361 | 1055 | L>S | in NPHS18; loss of function in nephrogenesis; unable to rescue morpholino-induced nephrogenesis defects in Xenopus; dbSNP:rs376476266 |
Galloway-Mowat syndrome 8 (GAMOS8)
- Note
- DescriptionA form of Galloway-Mowat syndrome, a severe renal-neurological disease characterized by early-onset nephrotic syndrome associated with microcephaly, central nervous system abnormalities, developmental delays, and a propensity for seizures. Brain anomalies include gyration defects ranging from lissencephaly to pachygyria and polymicrogyria, and cerebellar hypoplasia. Most patients show facial dysmorphism characterized by a small, narrow forehead, large/floppy ears, deep-set eyes, hypertelorism and micrognathia. Additional variable features are visual impairment and arachnodactyly. Most patients die in early childhood. GAMOS8 inheritance is autosomal recessive.
- See alsoMIM:618349
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_030829 | 106 | in dbSNP:rs428231 | |||
Sequence: T → P | ||||||
Natural variant | VAR_081359 | 231 | in NPHS18; decreased function in nephrogenesis; unable to fully rescue morpholino-induced nephrogenesis defects in Xenopus; dbSNP:rs1558108130 | |||
Sequence: R → G | ||||||
Natural variant | VAR_030830 | 294 | in dbSNP:rs11805194 | |||
Sequence: I → V | ||||||
Natural variant | VAR_035854 | 326 | in a breast cancer sample; somatic mutation | |||
Sequence: G → V | ||||||
Natural variant | VAR_030831 | 406 | in dbSNP:rs1065674 | |||
Sequence: Q → R | ||||||
Natural variant | VAR_035855 | 448 | in a breast cancer sample; somatic mutation | |||
Sequence: G → R | ||||||
Natural variant | VAR_081360 | 974 | in NPHS18; loss of function in nephrogenesis; unable to rescue morpholino-induced nephrogenesis defects in Xenopus; decreased interaction with NUP107; dbSNP:rs1558091788 | |||
Sequence: S → R | ||||||
Natural variant | VAR_081361 | 1055 | in NPHS18; loss of function in nephrogenesis; unable to rescue morpholino-induced nephrogenesis defects in Xenopus; dbSNP:rs376476266 | |||
Sequence: L → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,183 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000204838 | 1-1156 | UniProt | Nuclear pore complex protein Nup133 | |||
Sequence: MFPAAPSPRTPGTGSRRGPLAGLGPGSTPRTASRKGLPLGSAVSSPVLFSPVGRRSSLSSRGTPTRMFPHHSITESVNYDVKTFGSSLPVKVMEALTLAEVDDQLTINIDEGGWACLVCKEKLIIWKIALSPITKLSVCKELQLPPSDFHWSADLVALSYSSPSGEAHSTQAVAVMVATREGSIRYWPSLAGEDTYTEAFVDSGGDKTYSFLTAVQGGSFILSSSGSQLIRLIPESSGKIHQHILPQGQGMLSGIGRKVSSLFGILSPSSDLTLSSVLWDRERSSFYSLTSSNISKWELDDSSEKHAYSWDINRALKENITDAIWGSESNYEAIKEGVNIRYLDLKQNCDGLVILAAAWHSADNPCLIYYSLITIEDNGCQMSDAVTVEVTQYNPPFQSEDLILCQLTVPNFSNQTAYLYNESAVYVCSTGTGKFSLPQEKIVFNAQGDSVLGAGACGGVPIIFSRNSGLVSITSRENVSILAEDLEGSLASSVAGPNSESMIFETTTKNETIAQEDKIKLLKAAFLQYCRKDLGHAQMVVDELFSSHSDLDSDSELDRAVTQISVDLMDDYPASDPRWAESVPEEAPGFSNTSLIILHQLEDKMKAHSFLMDFIHQVGLFGRLGSFPVRGTPMATRLLLCEHAEKLSAAIVLKNHHSRLSDLVNTAILIALNKREYEIPSNLTPADVFFREVSQVDTICECLLEHEEQVLRDAPMDSIEWAEVVINVNNILKDMLQAASHYRQNRNSLYRREESLEKEPEYVPWTATSGPGGIRTVIIRQHEIVLKVAYPQADSNLRNIVTEQLVALIDCFLDGYVSQLKSVDKSSNRERYDNLEMEYLQKRSDLLSPLLSLGQYLWAASLAEKYCDFDILVQMCEQTDNQSRLQRYMTQFADQNFSDFLFRWYLEKGKRGKLLSQPISQHGQLANFLQAHEHLSWLHEINSQELEKAHATLLGLANMETRYFAKKKTLLGLSKLAALASDFSEDMLQEKIEEMAEQERFLLHQETLPEQLLAEKQLNLSAMPVLTAPQLIGLYICEENRRANEYDFKKALDLLEYIDEEEDININDLKLEILCKALQRDNWSSSDGKDDPIEVSKDSIFVKILQKLLKDGIQLSEYLPEVKDLLQADQLGSLKSNPYFEFVLKANYEYYVQGQI | |||||||
Modified residue | 7 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 13 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 15 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 17 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 27 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 27 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 28 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 28 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 30 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 31 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 33 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 41 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 41 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 44 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 45 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 45 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 50 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 50 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 56 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 57 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 59 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 60 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 63 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 72 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 72 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 131 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 131 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 267 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 475 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 480 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 480 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 489 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 493 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 501 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 553 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 594 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 681 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 755 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 787 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1021 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1133 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1133 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Forms part of the Nup160 subcomplex in the nuclear pore which is composed of NUP160, NUP133, NUP107 and Nup96. This complex plays a role in RNA export and in tethering Nup98 and NUP153 to the nucleus.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8WUM0 | CENPF P49454 | 2 | EBI-295695, EBI-968343 | |
BINARY | Q8WUM0 | LRRK2 Q5S007 | 4 | EBI-295695, EBI-5323863 | |
BINARY | Q8WUM0 | NUP107 P57740 | 17 | EBI-295695, EBI-295687 | |
BINARY | Q8WUM0 | NUP85 Q9BW27 | 4 | EBI-295695, EBI-716392 | |
XENO | Q8WUM0 | NUP85 P46673 | 5 | EBI-295695, EBI-12345 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-39 | Disordered | ||||
Sequence: MFPAAPSPRTPGTGSRRGPLAGLGPGSTPRTASRKGLPL |
Sequence similarities
Belongs to the nucleoporin Nup133 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,156
- Mass (Da)128,979
- Last updated2007-04-03 v2
- Checksum78B733E353824577
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 61 | in Ref. 1; BAA91829 | ||||
Sequence: R → G | ||||||
Sequence conflict | 146 | in Ref. 1; BAA91829 | ||||
Sequence: P → S | ||||||
Sequence conflict | 345 | in Ref. 3; AAH20107 | ||||
Sequence: L → F | ||||||
Sequence conflict | 626 | in Ref. 1; BAA91829 | ||||
Sequence: S → N | ||||||
Sequence conflict | 928 | in Ref. 1; BAA91885 | ||||
Sequence: F → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK001676 EMBL· GenBank· DDBJ | BAA91829.1 EMBL· GenBank· DDBJ | mRNA | ||
AK001754 EMBL· GenBank· DDBJ | BAA91885.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK022572 EMBL· GenBank· DDBJ | BAB14106.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK314431 EMBL· GenBank· DDBJ | BAG37045.1 EMBL· GenBank· DDBJ | mRNA | ||
AL121990 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL139252 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL160004 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC020107 EMBL· GenBank· DDBJ | AAH20107.1 EMBL· GenBank· DDBJ | mRNA |