Domains within Homo sapiens protein PLPP_HUMAN (Q96GD0)
Pyridoxal phosphate phosphatase
Alternative representations: 1 /
| Protein length | 296 aa |
|---|---|
| Source database | UniProt |
| Identifiers | PLPP_HUMAN, Q96GD0, ENSP00000215904.6, ENSP00000215904, Q9UGY2, A0A024R1I3_HUMAN, A0A024R1I3 |
| Source gene | ENSG00000241360 |
| Alternative splicing | PLPP_HUMAN, B1AHD3_HUMAN |
Predicted functional partners
PLPP_HUMAN is shown as 
PDXP in the network
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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.
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 6 PTMs annotated in this protein:
| PTM | Count | |
|---|---|---|
 | Phosphorylation | 6 |
To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein PDXP.
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.ENSP00000215904 in eggNOG.
| OG | Taxonomic class | Description |
|---|---|---|
| LCOG0647 | All organisms (root) | 5'-nucleotidase [EC:3.1.3.5],phosphoglycolate phosphatase [EC:3.1.3.18 3.1.3.48],glycerol-1-phosphatase [EC:3.1.3.21] |
| KOG2882 | Eukaryota (superkingdom) | phosphoglycolate phosphatase [EC:3.1.3.18 3.1.3.48],4-nitrophenyl phosphatase [EC:3.1.3.41],pyridoxal phosphatase [EC:3.1.3.74] |
| HUNJ7 | Metazoa (kingdom) | phosphoglycolate phosphatase [EC:3.1.3.18 3.1.3.48],pyridoxal phosphatase [EC:3.1.3.74],farnesyl diphosphate phosphatase [EC:3.1.3.-] |
| 941T3 | Chordata (phylum) | pyridoxal phosphatase [EC:3.1.3.74],phosphoglycolate phosphatase [EC:3.1.3.18 3.1.3.48],SH3-domain binding protein 1 |
| 5QFDR | Sarcopterygii (superclass) | pyridoxal phosphatase [EC:3.1.3.74],phosphoglycolate phosphatase [EC:3.1.3.18 3.1.3.48],SH3-domain binding protein 1 |
| 8ZC76 | Mammalia (class) | pyridoxal phosphatase [EC:3.1.3.74],SH3-domain binding protein 1 |
| 4RCGE | Euarchontoglires (superorder) | pyridoxal phosphatase [EC:3.1.3.74],SH3-domain binding protein 1 |
| 4ZPK4 | Primates (order) | pyridoxal phosphatase [EC:3.1.3.74],SH3-domain binding protein 1 |
| 986TZ | Haplorrhini (suborder) | pyridoxal phosphatase [EC:3.1.3.74],SH3-domain binding protein 1 |
| BVGH2 | Simiiformes (infraorder) | pyridoxal phosphatase [EC:3.1.3.74],SH3-domain binding protein 1 |
| 9F05B | Catarrhini (parvorder) | pyridoxal phosphatase [EC:3.1.3.74],SH3-domain binding protein 1 |
| 7P0KB | Opisthokonta (clade) | phosphoglycolate phosphatase [EC:3.1.3.18 3.1.3.48],4-nitrophenyl phosphatase [EC:3.1.3.41],pyridoxal phosphatase [EC:3.1.3.74] |
| H6BKY | Bilateria (clade) | phosphoglycolate phosphatase [EC:3.1.3.18 3.1.3.48],pyridoxal phosphatase [EC:3.1.3.74],farnesyl diphosphate phosphatase [EC:3.1.3.-] |
| 9FPG2 | Vertebrata (clade) | pyridoxal phosphatase [EC:3.1.3.74],phosphoglycolate phosphatase [EC:3.1.3.18 3.1.3.48],SH3-domain binding protein 1 |
| FXE5A | Hominoidea (superfamily) | pyridoxal phosphatase [EC:3.1.3.74],SH3-domain binding protein 1 |
| 5N8GB | Hominidae (family) | pyridoxal phosphatase [EC:3.1.3.74],SH3-domain binding protein 1 |
| 5XVAS | Homininae (subfamily) | pyridoxal phosphatase [EC:3.1.3.74],SH3-domain binding protein 1 |
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.