Q8N1F7 · NUP93_HUMAN

  • Protein
    Nuclear pore complex protein Nup93
  • Gene
    NUP93
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcentrosome
Cellular Componentcytosol
Cellular Componentmembrane
Cellular Componentnuclear envelope
Cellular Componentnuclear membrane
Cellular Componentnuclear periphery
Cellular Componentnuclear pore
Molecular Functionstructural constituent of nuclear pore
Biological Processnuclear envelope organization
Biological Processnuclear pore complex assembly
Biological Processnucleocytoplasmic transport
Biological Processpoly(A)+ mRNA export from nucleus
Biological Processpositive regulation of SMAD protein signal transduction
Biological Processprotein import into nucleus

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Nuclear pore complex protein Nup93
  • Alternative names
    • 93 kDa nucleoporin
    • Nucleoporin Nup93

Gene names

    • Name
      NUP93
    • Synonyms
      KIAA0095

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q8N1F7
  • Secondary accessions
    • B3KPQ8
    • Q14705

Proteomes

Organism-specific databases

Subcellular Location

Nucleus membrane
; Peripheral membrane protein
Nucleus envelope
Note: Localizes at the nuclear basket and at or near the nuclear entry to the gated channel of the pore.

Keywords

Disease & Variants

Involvement in disease

Nephrotic syndrome 12 (NPHS12)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A 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 also
    MIM:616892
Natural variants in NPHS12
Variant IDPosition(s)ChangeDescription
VAR_076473388R>Win 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_076474591G>Vin 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_076475629Y>Cin 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.

TypeIDPosition(s)Description
Natural variantVAR_076473388in 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
Natural variantVAR_028160509in dbSNP:rs17853288
Natural variantVAR_076474591in 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
Natural variantVAR_076475629in 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

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.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_00001247821-819UniProtNuclear pore complex protein Nup93
Modified residue (large scale data)47PRIDEPhosphothreonine
Modified residue49UniProtPhosphothreonine
Modified residue (large scale data)49PRIDEPhosphothreonine
Modified residue (large scale data)51PRIDEPhosphothreonine
Modified residue52UniProtPhosphoserine
Modified residue (large scale data)52PRIDEPhosphoserine
Modified residue66UniProtPhosphoserine
Modified residue (large scale data)66PRIDEPhosphoserine
Modified residue72UniProtPhosphoserine
Modified residue (large scale data)72PRIDEPhosphoserine
Modified residue75UniProtPhosphoserine
Modified residue (large scale data)75PRIDEPhosphoserine
Modified residue80UniProtPhosphoserine
Modified residue (large scale data)80PRIDEPhosphoserine
Modified residue (large scale data)82PRIDEPhosphoserine
Modified residue (large scale data)85PRIDEPhosphothreonine
Modified residue (large scale data)159PRIDEPhosphothreonine
Modified residue (large scale data)162PRIDEPhosphoserine
Modified residue (large scale data)168PRIDEPhosphoserine
Modified residue (large scale data)236PRIDEPhosphothreonine
Modified residue (large scale data)364PRIDEPhosphoserine
Modified residue430UniProtPhosphoserine
Modified residue (large scale data)430PRIDEPhosphoserine
Modified residue (large scale data)438PRIDEPhosphoserine
Modified residue (large scale data)647PRIDEPhosphoserine
Modified residue (large scale data)726PRIDEPhosphoserine
Modified residue (large scale data)766PRIDEPhosphothreonine
Modified residue767UniProtPhosphoserine
Modified residue (large scale data)767PRIDEPhosphoserine
Modified residue (large scale data)772PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

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).
(Microbial infection) Interacts with SARS-CoV translation inhibitor nsp1; this interaction may disrupt nuclear pore function.

Binary interactions

Protein-protein interaction databases

Miscellaneous

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

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.

  • Length
    819
  • Mass (Da)
    93,488
  • Last updated
    2006-10-17 v2
  • Checksum
    7A611FABE964FE98
MDTEGFGELLQQAEQLAAETEGISELPHVERNLQEIQQAGERLRSRTLTRTSQETADVKASVLLGSRGLDISHISQRLESLSAATTFEPLEPVKDTDIQGFLKNEKDNALLSAIEESRKRTFGMAEEYHRESMLVEWEQVKQRILHTLLASGEDALDFTQESEPSYISDVGPPGRSSLDNIEMAYARQIYIYNEKIVNGHLQPNLVDLCASVAELDDKSISDMWTMVKQMTDVLLTPATDALKNRSSVEVRMEFVRQALAYLEQSYKNYTLVTVFGNLHQAQLGGVPGTYQLVRSFLNIKLPAPLPGLQDGEVEGHPVWALIYYCMRCGDLLAASQVVNRAQHQLGEFKTWFQEYMNSKDRRLSPATENKLRLHYRRALRNNTDPYKRAVYCIIGRCDVTDNQSEVADKTEDYLWLKLNQVCFDDDGTSSPQDRLTLSQFQKQLLEDYGESHFTVNQQPFLYFQVLFLTAQFEAAVAFLFRMERLRCHAVHVALVLFELKLLLKSSGQSAQLLSHEPGDPPCLRRLNFVRLLMLYTRKFESTDPREALQYFYFLRDEKDSQGENMFLRCVSELVIESREFDMILGKLENDGSRKPGVIDKFTSDTKPIINKVASVAENKGLFEEAAKLYDLAKNADKVLELMNKLLSPVVPQISAPQSNKERLKNMALSIAERYRAQGISANKFVDSTFYLLLDLITFFDEYHSGHIDRAFDIIERLKLVPLNQESVEERVAAFRNFSDEIRHNLSEVLLATMNILFTQFKRLKGTSPSSSSRPQRVIEDRDSQLRSQARTLITFAGMIPYRTSGDTNARLVQMEVLMN

Q8N1F7-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 13 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
H3BV11H3BV11_HUMANNUP93136
H3BV15H3BV15_HUMANNUP9384
H3BVG0H3BVG0_HUMANNUP93880
H3BVE2H3BVE2_HUMANNUP93117
H3BRI8H3BRI8_HUMANNUP93151
H3BRD9H3BRD9_HUMANNUP93140
H3BPA9H3BPA9_HUMANNUP93229
H3BP95H3BP95_HUMANNUP93156
H3BP72H3BP72_HUMANNUP9316
H3BNG7H3BNG7_HUMANNUP9340
H3BNN5H3BNN5_HUMANNUP93132
H3BM93H3BM93_HUMANNUP93178
H3BMX0H3BMX0_HUMANNUP93125

Sequence caution

The sequence BAA07680.2 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0431171-123in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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