Q8N1F7 · NUP93_HUMAN
- ProteinNuclear pore complex protein Nup93
- GeneNUP93
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids819 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance (PubMed:9348540).
May anchor nucleoporins, but not NUP153 and TPR, to the NPC. During renal development, regulates podocyte migration and proliferation through SMAD4 signaling (PubMed:26878725).
May anchor nucleoporins, but not NUP153 and TPR, to the NPC. During renal development, regulates podocyte migration and proliferation through SMAD4 signaling (PubMed:26878725).
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | centrosome | |
Cellular Component | cytosol | |
Cellular Component | membrane | |
Cellular Component | nuclear envelope | |
Cellular Component | nuclear membrane | |
Cellular Component | nuclear periphery | |
Cellular Component | nuclear pore | |
Molecular Function | structural constituent of nuclear pore | |
Biological Process | nuclear envelope organization | |
Biological Process | nuclear pore complex assembly | |
Biological Process | nucleocytoplasmic transport | |
Biological Process | poly(A)+ mRNA export from nucleus | |
Biological Process | positive regulation of SMAD protein signal transduction | |
Biological Process | protein import into nucleus |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameNuclear pore complex protein Nup93
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8N1F7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Nucleus membrane ; Peripheral membrane protein
Note: Localizes at the nuclear basket and at or near the nuclear entry to the gated channel of the pore.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Nephrotic syndrome 12 (NPHS12)
- 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 and progress to end-stage renal failure. NPHS12 inheritance is autosomal recessive.
- See alsoMIM:616892
Natural variants in NPHS12
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_076473 | 388 | R>W | in NPHS12; doesnt affect nuclear envelope localization; impairs nuclear pore complex assembly; doesn't abrogate interaction with NUP205; doesn't affect SMAD4 interaction; doesn't affect IPO7 interaction; impairs SMAD4 protein import into nucleus; impairs SMAD4 protein signal transduction; dbSNP:rs145146218 | |
VAR_076474 | 591 | G>V | in NPHS12; doesnt affect nuclear envelope localization; doesn't affect nuclear pore complex assembly; doesn't abrogate interaction with NUP205; abrogates SMAD4 interaction; abrogates IPO7 interaction; impairs SMAD4 protein import into nucleus; impairs SMAD4 protein signal transduction; dbSNP:rs145473779 | |
VAR_076475 | 629 | Y>C | in NPHS12; doesnt affect nuclear envelope localization; doesn't affect nuclear pore complex assembly; doesn't abrogate interaction with NUP205; abrogates SMAD4 interaction; abrogates IPO7 interaction; impairs SMAD4 protein import; impairs SMAD4 protein signal transduction into nucleus;; dbSNP:rs757674160 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_076473 | 388 | in NPHS12; doesnt affect nuclear envelope localization; impairs nuclear pore complex assembly; doesn't abrogate interaction with NUP205; doesn't affect SMAD4 interaction; doesn't affect IPO7 interaction; impairs SMAD4 protein import into nucleus; impairs SMAD4 protein signal transduction; dbSNP:rs145146218 | |||
Sequence: R → W | ||||||
Natural variant | VAR_028160 | 509 | in dbSNP:rs17853288 | |||
Sequence: S → R | ||||||
Natural variant | VAR_076474 | 591 | in NPHS12; doesnt affect nuclear envelope localization; doesn't affect nuclear pore complex assembly; doesn't abrogate interaction with NUP205; abrogates SMAD4 interaction; abrogates IPO7 interaction; impairs SMAD4 protein import into nucleus; impairs SMAD4 protein signal transduction; dbSNP:rs145473779 | |||
Sequence: G → V | ||||||
Natural variant | VAR_076475 | 629 | in NPHS12; doesnt affect nuclear envelope localization; doesn't affect nuclear pore complex assembly; doesn't abrogate interaction with NUP205; abrogates SMAD4 interaction; abrogates IPO7 interaction; impairs SMAD4 protein import; impairs SMAD4 protein signal transduction into nucleus;; dbSNP:rs757674160 | |||
Sequence: Y → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 990 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 chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000124782 | 1-819 | UniProt | Nuclear pore complex protein Nup93 | |||
Sequence: MDTEGFGELLQQAEQLAAETEGISELPHVERNLQEIQQAGERLRSRTLTRTSQETADVKASVLLGSRGLDISHISQRLESLSAATTFEPLEPVKDTDIQGFLKNEKDNALLSAIEESRKRTFGMAEEYHRESMLVEWEQVKQRILHTLLASGEDALDFTQESEPSYISDVGPPGRSSLDNIEMAYARQIYIYNEKIVNGHLQPNLVDLCASVAELDDKSISDMWTMVKQMTDVLLTPATDALKNRSSVEVRMEFVRQALAYLEQSYKNYTLVTVFGNLHQAQLGGVPGTYQLVRSFLNIKLPAPLPGLQDGEVEGHPVWALIYYCMRCGDLLAASQVVNRAQHQLGEFKTWFQEYMNSKDRRLSPATENKLRLHYRRALRNNTDPYKRAVYCIIGRCDVTDNQSEVADKTEDYLWLKLNQVCFDDDGTSSPQDRLTLSQFQKQLLEDYGESHFTVNQQPFLYFQVLFLTAQFEAAVAFLFRMERLRCHAVHVALVLFELKLLLKSSGQSAQLLSHEPGDPPCLRRLNFVRLLMLYTRKFESTDPREALQYFYFLRDEKDSQGENMFLRCVSELVIESREFDMILGKLENDGSRKPGVIDKFTSDTKPIINKVASVAENKGLFEEAAKLYDLAKNADKVLELMNKLLSPVVPQISAPQSNKERLKNMALSIAERYRAQGISANKFVDSTFYLLLDLITFFDEYHSGHIDRAFDIIERLKLVPLNQESVEERVAAFRNFSDEIRHNLSEVLLATMNILFTQFKRLKGTSPSSSSRPQRVIEDRDSQLRSQARTLITFAGMIPYRTSGDTNARLVQMEVLMN | |||||||
Modified residue (large scale data) | 47 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 49 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 49 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 51 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 52 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 52 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 66 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 66 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 72 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 72 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 75 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 75 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 80 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 80 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 82 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 85 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 159 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 162 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 168 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 236 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 364 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 430 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 430 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 438 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 647 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 726 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 766 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 767 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 767 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 772 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Part of the nuclear pore complex (NPC) (PubMed:15229283, PubMed:15703211, PubMed:9348540).
Component of the p62 complex, a complex composed of NUP62 and NUP54 (PubMed:9348540).
Forms a complex with NUP35, NUP155, NUP205 and lamin B; the interaction with NUP35 is direct (PubMed:15703211).
Does not interact with TPR (PubMed:12802065, PubMed:15229283).
Interacts with SMAD4 and IPO7; translocates SMAD4 to the nucleus through the NPC upon BMP7 stimulation resulting in activation of SMAD4 signaling (PubMed:26878725).
Component of the p62 complex, a complex composed of NUP62 and NUP54 (PubMed:9348540).
Forms a complex with NUP35, NUP155, NUP205 and lamin B; the interaction with NUP35 is direct (PubMed:15703211).
Does not interact with TPR (PubMed:12802065, PubMed:15229283).
Interacts with SMAD4 and IPO7; translocates SMAD4 to the nucleus through the NPC upon BMP7 stimulation resulting in activation of SMAD4 signaling (PubMed:26878725).
(Microbial infection) Interacts with SARS-CoV translation inhibitor nsp1; this interaction may disrupt nuclear pore function.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8N1F7 | AP5Z1 O43299 | 3 | EBI-1042703, EBI-740938 | |
BINARY | Q8N1F7 | MPPED2 Q15777 | 3 | EBI-1042703, EBI-2350461 | |
BINARY | Q8N1F7 | OPCML Q14982 | 3 | EBI-1042703, EBI-6447201 | |
BINARY | Q8N1F7 | PLA2G6 O60733 | 3 | EBI-1042703, EBI-12089905 | |
BINARY | Q8N1F7 | TMEM100 Q9NV29 | 3 | EBI-1042703, EBI-8644968 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8N1F7-1
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
- Length819
- Mass (Da)93,488
- Last updated2006-10-17 v2
- Checksum7A611FABE964FE98
Q8N1F7-2
- Name2
- Differences from canonical
- 1-123: Missing
Computationally mapped potential isoform sequences
There are 13 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H3BV11 | H3BV11_HUMAN | NUP93 | 136 | ||
H3BV15 | H3BV15_HUMAN | NUP93 | 84 | ||
H3BVG0 | H3BVG0_HUMAN | NUP93 | 880 | ||
H3BVE2 | H3BVE2_HUMAN | NUP93 | 117 | ||
H3BRI8 | H3BRI8_HUMAN | NUP93 | 151 | ||
H3BRD9 | H3BRD9_HUMAN | NUP93 | 140 | ||
H3BPA9 | H3BPA9_HUMAN | NUP93 | 229 | ||
H3BP95 | H3BP95_HUMAN | NUP93 | 156 | ||
H3BP72 | H3BP72_HUMAN | NUP93 | 16 | ||
H3BNG7 | H3BNG7_HUMAN | NUP93 | 40 | ||
H3BNN5 | H3BNN5_HUMAN | NUP93 | 132 | ||
H3BM93 | H3BM93_HUMAN | NUP93 | 178 | ||
H3BMX0 | H3BMX0_HUMAN | NUP93 | 125 |
Sequence caution
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_043117 | 1-123 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D42085 EMBL· GenBank· DDBJ | BAA07680.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK294176 EMBL· GenBank· DDBJ | BAH11689.1 EMBL· GenBank· DDBJ | mRNA | ||
BC034346 EMBL· GenBank· DDBJ | AAH34346.1 EMBL· GenBank· DDBJ | mRNA | ||
AC012181 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC106779 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC127456 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AK056637 EMBL· GenBank· DDBJ | BAG51770.1 EMBL· GenBank· DDBJ | mRNA |