Domains within Homo sapiens protein NANP_HUMAN (Q8TBE9)
N-acylneuraminate-9-phosphatase
Alternative representations: 1 /
| Protein length | 248 aa |
|---|---|
| Source database | UniProt |
| Identifiers | NANP_HUMAN, Q8TBE9, ENSP00000302441.3, ENSP00000302441, B3KP12, Q5JYN8, Q8TE97, Q9Y3N0, G3RAP1_GORGO, G3RAP1 |
| Source gene | ENSG00000170191 |
Predicted functional partners
NANP_HUMAN is shown as 
NANP in the network
Click and drag to pan the network, and zoom by using your mouse wheel. Click the protein nodes for additional options.
The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.
Protein NANP_HUMAN is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:
KEGG pathways
| Pathway | Description | |
|---|---|---|
| map00520 | Amino sugar and nucleotide sugar metabolism | iPath3 |
KEGG orthologous groups
| KO | Name | Description | |
|---|---|---|---|
| K08726 | EPHX2 | soluble epoxide hydrolase / lipid-phosphate phosphatase [EC:3.3.2.10 3.1.3.76] | iPath3 |
| K07025 | K07025 | putative hydrolase of the HAD superfamily | |
| K01097 | NANP | N-acylneuraminate-9-phosphatase [EC:3.1.3.29] | iPath3 |
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 3 PTMs annotated in this protein:
| PTM | Count | |
|---|---|---|
 | Phosphorylation | 3 |
To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein NANP.
Orthologous groups
Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 9606.ENSP00000302441 in eggNOG.
| OG | Taxonomic class | Description |
|---|---|---|
| LCOG1011 | All organisms (root) | putative hydrolase of the HAD superfamily,2-haloacid dehalogenase [EC:3.8.1.2],FMN hydrolase / 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase [EC:3.1.3.102 3.1.3.104] |
| KOG3085 | Eukaryota (superkingdom) | soluble epoxide hydrolase / lipid-phosphate phosphatase [EC:3.3.2.10 3.1.3.76],N-acylneuraminate-9-phosphatase [EC:3.1.3.29],FMN hydrolase / 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase [EC:3.1.3.102 3.1.3.104] |
| HWB8U | Metazoa (kingdom) | N-acylneuraminate-9-phosphatase [EC:3.1.3.29] |
| 93E7W | Chordata (phylum) | N-acylneuraminate-9-phosphatase [EC:3.1.3.29] |
| 5QJ5K | Sarcopterygii (superclass) | N-acylneuraminate-9-phosphatase [EC:3.1.3.29] |
| 8ZE9V | Mammalia (class) | N-acylneuraminate-9-phosphatase [EC:3.1.3.29] |
| 4RMCB | Euarchontoglires (superorder) | N-acylneuraminate-9-phosphatase [EC:3.1.3.29] |
| 4ZU1X | Primates (order) | N-acylneuraminate-9-phosphatase [EC:3.1.3.29] |
| 98B1B | Haplorrhini (suborder) | N-acylneuraminate-9-phosphatase [EC:3.1.3.29] |
| BV1HC | Simiiformes (infraorder) | N-acylneuraminate-9-phosphatase [EC:3.1.3.29] |
| 9EYZC | Catarrhini (parvorder) | N-acylneuraminate-9-phosphatase [EC:3.1.3.29] |
| 9GN64 | Vertebrata (clade) | N-acylneuraminate-9-phosphatase [EC:3.1.3.29] |
| 7GWC0 | Opisthokonta (clade) | N-acylneuraminate-9-phosphatase [EC:3.1.3.29],putative hydrolase of the HAD superfamily |
| H451Q | Bilateria (clade) | N-acylneuraminate-9-phosphatase [EC:3.1.3.29] |
| FX4ZE | Hominoidea (superfamily) | N-acylneuraminate-9-phosphatase [EC:3.1.3.29] |
| 5MX5I | Hominidae (family) | N-acylneuraminate-9-phosphatase [EC:3.1.3.29] |
| 5Y0CK | Homininae (subfamily) | N-acylneuraminate-9-phosphatase [EC:3.1.3.29] |
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.