O75694 · NU155_HUMAN

  • Protein
    Nuclear pore complex protein Nup155
  • Gene
    NUP155
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport.

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 Componentcytosol
Cellular Componentmembrane
Cellular Componentnuclear envelope
Cellular Componentnuclear membrane
Cellular Componentnuclear pore
Cellular Componentnuclear pore inner ring
Molecular Functionstructural constituent of nuclear pore
Biological Processatrial cardiac muscle cell action potential
Biological ProcessmiRNA processing
Biological ProcessmRNA export from nucleus
Biological Processnuclear envelope organization
Biological Processnucleocytoplasmic transport
Biological Processprotein import into nucleus
Biological Processprotein localization to nuclear inner membrane
Biological ProcessRNA export from nucleus
Biological Processtranscription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Nuclear pore complex protein Nup155
  • Alternative names
    • 155 kDa nucleoporin
    • Nucleoporin Nup155

Gene names

    • Name
      NUP155
    • Synonyms
      KIAA0791

Organism names

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

Accessions

  • Primary accession
    O75694
  • Secondary accessions
    • Q9UBE9
    • Q9UFL5

Proteomes

Organism-specific databases

Subcellular Location

Nucleus membrane
; Peripheral membrane protein
Nucleus membrane
; Peripheral membrane protein
Note: In mitosis, assumes a diffuse cytoplasmic distribution probably as a monomer, before reversing back into a punctate nuclear surface localization at the end of mitosis.

Keywords

Disease & Variants

Involvement in disease

Atrial fibrillation, familial, 15 (ATFB15)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure.
  • See also
    MIM:615770
Natural variants in ATFB15
Variant IDPosition(s)ChangeDescription
VAR_071762391R>Hin ATFB15; fails to accumulate at various foci of the nuclear envelope and is diffusely distributed in the cytoplasm; shows significantly reduced permeability of the nuclear envelope compared to wild-type; dbSNP:rs587777339

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_071762391in ATFB15; fails to accumulate at various foci of the nuclear envelope and is diffusely distributed in the cytoplasm; shows significantly reduced permeability of the nuclear envelope compared to wild-type; dbSNP:rs587777339

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1,417 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for initiator methionine, chain, modified residue (large scale data), glycosylation, cross-link, modified residue.

TypeIDPosition(s)SourceDescription
Initiator methionine1UniProtRemoved
ChainPRO_00002048442-1391UniProtNuclear pore complex protein Nup155
Modified residue (large scale data)3PRIDEPhosphoserine
Modified residue (large scale data)4PRIDEPhosphoserine
Modified residue (large scale data)486PRIDEPhosphoserine
Glycosylation526UniProtO-linked (GlcNAc) serine
Cross-link740UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)914PRIDEPhosphoserine
Modified residue (large scale data)992PRIDEPhosphoserine
Modified residue (large scale data)994PRIDEPhosphoserine
Modified residue (large scale data)1006PRIDEPhosphoserine
Modified residue1057UniProtPhosphoserine
Modified residue (large scale data)1057PRIDEPhosphoserine
Modified residue (large scale data)1133PRIDEPhosphoserine

Post-translational modification

Phosphorylated. Phosphorylation and dephosphorylation may be important for the function of NUP155 and may play a role in the reversible disassembly of the nuclear pore complex during mitosis (By similarity).
Disulfide-linked to NUP62. 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 (By similarity).

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in all tissues tested, including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with GLE1. Able to form a heterotrimer with GLE1 and NUP42 in vitro. Forms a complex with NUP35, NUP93, NUP205 and lamin B.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY O75694EFS O432813EBI-1050769, EBI-718488
BINARY O75694LMNA P025456EBI-1050769, EBI-351935

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region985-1012Disordered

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.

O75694-1

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
    1,391
  • Mass (Da)
    155,199
  • Last updated
    1998-11-01 v1
  • Checksum
    7F07A103AFF7EE1D
MPSSLLGAAMPASTSAAALQEALENAGRLIDRQLQEDRMYPDLSELLMVSAPNNPTVSGMSDMDYPLQGPGLLSVPNLPEISSIRRVPLPPELVEQFGHMQCNCMMGVFPPISRAWLTIDSDIFMWNYEDGGDLAYFDGLSETILAVGLVKPKAGIFQPHVRHLLVLATPVDIVILGLSYANLQTGSGVLNDSLSGGMQLLPDPLYSLPTDNTYLLTITSTDNGRIFLAGKDGCLYEVAYQAEAGWFSQRCRKINHSKSSLSFLVPSLLQFTFSEDDPILQIAIDNSRNILYTRSEKGVIQVYDLGQDGQGMSRVASVSQNAIVSAAGNIARTIDRSVFKPIVQIAVIENSESLDCQLLAVTHAGVRLYFSTCPFRQPLARPNTLTLVHVRLPPGFSASSTVEKPSKVHRALYSKGILLMAASENEDNDILWCVNHDTFPFQKPMMETQMTAGVDGHSWALSAIDELKVDKIITPLNKDHIPITDSPVVVQQHMLPPKKFVLLSAQGSLMFHKLRPVDQLRHLLVSNVGGDGEEIERFFKLHQEDQACATCLILACSTAACDREVSAWATRAFFRYGGEAQMRFPTTLPPPSNVGPILGSPVYSSSPVPSGSPYPNPSFLGTPSHGIQPPAMSTPVCALGNPATQATNMSCVTGPEIVYSGKHNGICIYFSRIMGNIWDASLVVERIFKSGNREITAIESSVPCQLLESVLQELKGLQEFLDRNSQFAGGPLGNPNTTAKVQQRLIGFMRPENGNPQQMQQELQRKFHEAQLSEKISLQAIQQLVRKSYQALALWKLLCEHQFTIIVAELQKELQEQLKITTFKDLVIRDKELTGALIASLINCYIRDNAAVDGISLHLQDICPLLYSTDDAICSKANELLQRSRQVQNKTEKERMLRESLKEYQKISNQVDLSNVCAQYRQVRFYEGVVELSLTAAEKKDPQGLGLHFYKHGEPEEDIVGLQAFQERLNSYKCITDTLQELVNQSKAAPQSPSVPKKPGPPVLSSDPNMLSNEEAGHHFEQMLKLSQRSKDELFSIALYNWLIQVDLADKLLQVASPFLEPHLVRMAKVDQNRVRYMDLLWRYYEKNRSFSNAARVLSRLADMHSTEISLQQRLEYIARAILSAKSSTAISSIAADGEFLHELEEKMEVARIQLQIQETLQRQYSHHSSVQDAVSQLDSELMDITKLYGEFADPFKLAECKLAIIHCAGYSDPILVQTLWQDIIEKELSDSVTLSSSDRMHALSLKIVLLGKIYAGTPRFFPLDFIVQFLEQQVCTLNWDVGFVIQTMNEIGVPLPRLLEVYDQLFKSRDPFWNRMKKPLHLLDCIHVLLIRYVENPSQVLNCERRRFTNLCLDAVCGYLVELQSMSSSVAVQAITGNFKSLQAKLERLH

O75694-2

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

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
D6RA13D6RA13_HUMANNUP15554
E9PF10E9PF10_HUMANNUP1551327

Sequence caution

The sequence AAD52966.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence BAA34511.2 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0144371-59in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ007558
EMBL· GenBank· DDBJ
CAA07553.1
EMBL· GenBank· DDBJ
mRNA
AF165926
EMBL· GenBank· DDBJ
AAD52966.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
AB018334
EMBL· GenBank· DDBJ
BAA34511.2
EMBL· GenBank· DDBJ
mRNA Different initiation
BC039257
EMBL· GenBank· DDBJ
AAH39257.1
EMBL· GenBank· DDBJ
mRNA
AL117585
EMBL· GenBank· DDBJ
CAB56007.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp