Summary: Non-repetitive/WGA-negative nucleoporin C-terminal
Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.
This is the Wikipedia entry entitled "Nucleoporin". More...
Nucleoporin Edit Wikipedia article
| Nucleoporin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| File:PDB 3cqg EBI.jpg | |||||||||
| Structure of nucleoporin Nup107/Nup133 interaction complex, delta finger mutant. | |||||||||
| Identifiers | |||||||||
| Symbol | Nucleoporin | ||||||||
| Pfam | PF03177 | ||||||||
| InterPro | IPR004870 | ||||||||
|
|||||||||
The nucleoporins are a family of proteins which are the constituent building blocks of the nuclear pore complex.[1] The nuclear pore complex is a massive structure that extends across the nuclear envelope, forming a gateway that regulates the flow of macromolecules between the cell nucleus and the cytoplasm. Nucleoporins, a family of 50 to 100 proteins, are the main components of the nuclear pore complex in eukaryotic cells. Nuclear pores in turn allow the transport of water-soluble molecules across the nuclear envelope.
The proteins involved are named for their molecular weight (in kilo Daltons), and include the following:
- NUP35, NUP37, NUP43, NUP50
- NUP54, NUP62, NUP85, NUP88, NUP93, NUP98
- NUP107, NUP133, NUP153, NUP155, NUP160, NUP188
- NUP205, NUP210, NUP214
[edit] References
- ^ Doye V, Hurt E (June 1997). "From nucleoporins to nuclear pore complexes". Curr. Opin. Cell Biol. 9 (3): 401â11. doi:10.1016/S0955-0674(97)80014-2. PMID 9159086.
[edit] External links
- Nucleoporin at the US National Library of Medicine Medical Subject Headings (MeSH)
|
||||||||||||||
| This biochemistry article is a stub. You can help Wikipedia by expanding it. |
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Non-repetitive/WGA-negative nucleoporin C-terminal Provide feedback
This is the C-termainl half of a family of nucleoporin proteins. Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells, and mediate bidirectional nucleocytoplasmic transport, especially of mRNA and proteins. Two nucleoporin classes are known: one is characterised by the FG repeat PF03093; the other is represented by this family, and lacks any repeats. RNA undergoing nuclear export first encounters the basket of the nuclear pore and many nucleoporins are accessible on the basket side of the pore [2].
Literature references
-
Zhang X, Yang H, Corydon MJ, Zhang X, Pedersen S, Korenberg JR, Chen XN, Laporte J, Gregersen N, Niebuhr E, Liu G, Bolund L; , Genomics 1999;57:144-151.: Localization of a human nucleoporin 155 gene (NUP155) to the 5p13 region and cloning of its cDNA. PUBMED:10191094 EPMC:10191094
-
Vasu S, Shah S, Orjalo A, Park M, Fischer WH, Forbes DJ; , J Cell Biol 2001;155:339-354.: Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export. PUBMED:11684705 EPMC:11684705
External database links
| PANDIT: | PF03177 |
| Pseudofam: | PF03177 |
| SYSTERS: | Nucleoporin_C |
This tab holds annotation information from the InterPro database.
InterPro entry IPR007187
This is the C-terminal half of a family of nucleoporin proteins. Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells, and mediate bidirectional nucleocytoplasmic transport, especially of mRNA and proteins. Two nucleoporin classes are known: one is characterised by the FG repeat and the other is represented by this family, which lacks any repeats. RNA undergoing nuclear export first encounters the basket of the nuclear pore and many nucleoporins are accessible on the basket side of the pore [PUBMED:10191094, PUBMED:11684705].
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
Loading domain graphics...
Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
View options
We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (63) |
Full (645) |
Representative proteomes | NCBI (629) |
Meta (4) |
||||
|---|---|---|---|---|---|---|---|---|
| RP15 (144) |
RP35 (236) |
RP55 (357) |
RP75 (432) |
|||||
| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
Download options
We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (63) |
Full (645) |
Representative proteomes | NCBI (629) |
Meta (4) |
||||
|---|---|---|---|---|---|---|---|---|
| RP15 (144) |
RP35 (236) |
RP55 (357) |
RP75 (432) |
|||||
| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_1212 (release 6.5) |
| Previous IDs: | Nucleoporin; |
| Type: | Domain |
| Author: | Mifsud W |
| Number in seed: | 63 |
| Number in full: | 645 |
| Average length of the domain: | 485.40 aa |
| Average identity of full alignment: | 17 % |
| Average coverage of the sequence by the domain: | 42.05 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|
||||||||||||
| Model details: |
|
||||||||||||
| Model length: | 587 | ||||||||||||
| Family (HMM) version: | 9 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Sunburst controls
ShowThis visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
Loading...
Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Nucleoporin_C domain has been found. There are 7 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
Loading structure mapping...

Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence