Domains within Homo sapiens protein NU153_HUMAN (P49790)
Nuclear pore complex protein Nup153
Alternative representations: 1 /
| Protein length | 1475 aa |
|---|---|
| Source database | UniProt |
| Identifiers | NU153_HUMAN, P49790, ENSP00000262077.2, ENSP00000262077, B4DIK2, E7EPX5, F6QR24, Q4LE47, Q5T9I7, Q7Z743 |
| Source gene | ENSG00000124789 |
| Alternative splicing | NU153_HUMAN, P49790-2, P49790-3 |
Domain architecture analysis
Display all proteins with similar:
| Domain organisation | Proteins having all the domains as the query in the same order. Additional domains are allowed. |
|---|---|
| Domain composition | Proteins with the same domain composition have at least one copy of each of the domains of the query. |
This domain architecture was probably invented with the emergence of Eukaryota
Post-translational modifications
PTM annotation is taken from PTMcode, a resource of known and predicted functional associations between protein post-translational modifications (PTMs). There are 160 PTMs annotated in this protein:
| PTM | Count | |
|---|---|---|
 | Phosphorylation | 104 |
 | Ubiquitination | 26 |
 | Acetylation | 14 |
 | O-linked glycosylation | 8 |
 | O-GlcNAc glycosylation | 8 |
To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein NUP153.
The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.