Domains within Homo sapiens protein PA24B_HUMAN (P0C869)
Cytosolic phospholipase A2 beta
Alternative representations: 1 /
| Protein length | 781 aa |
|---|---|
| Source database | UniProt |
| Identifiers | PA24B_HUMAN, P0C869, ENSP00000396045.1, ENSP00000396045, ENSP00000416610.1, ENSP00000416610, B4DRT9, Q19KD5, Q19KD6 |
| Source gene | ENSG00000243708 |
| Alternative splicing | PA24B_HUMAN, H3BSX5_HUMAN |
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 Chordata
Predicted functional partners
PA24B_HUMAN is shown as 
PLA2G4B 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 PA24B_HUMAN is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:
KEGG pathways
| Pathway | Description | |
|---|---|---|
| map04921 | Oxytocin signaling pathway | |
| map00564 | Glycerophospholipid metabolism | iPath3 |
KEGG orthologous groups
| KO | Name | Description | |
|---|---|---|---|
| K16342 | PLA2G4, CPLA2 | cytosolic phospholipase A2 [EC:3.1.1.4] | iPath3 |
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.ENSP00000396045 in eggNOG.
| OG | Taxonomic class | Description |
|---|---|---|
| 7553F | All organisms (root) | cytosolic phospholipase A2 [EC:3.1.1.4],lysophospholipase [EC:3.1.1.5],peptidyl-lysine (3S)-dioxygenase / protease [EC:1.14.11.63 3.4.-.-] |
| KOG1325 | Eukaryota (superkingdom) | cytosolic phospholipase A2 [EC:3.1.1.4],lysophospholipase [EC:3.1.1.5],peptidyl-lysine (3S)-dioxygenase / protease [EC:1.14.11.63 3.4.-.-] |
| HV6CN | Metazoa (kingdom) | peptidyl-lysine (3S)-dioxygenase / protease [EC:1.14.11.63 3.4.-.-],cytosolic phospholipase A2 [EC:3.1.1.4],blocked early in transport 1 |
| 93HT3 | Chordata (phylum) | cytosolic phospholipase A2 [EC:3.1.1.4],peptidyl-lysine (3S)-dioxygenase / protease [EC:1.14.11.63 3.4.-.-] |
| 5QD85 | Sarcopterygii (superclass) | cytosolic phospholipase A2 [EC:3.1.1.4] |
| 8YV97 | Mammalia (class) | cytosolic phospholipase A2 [EC:3.1.1.4] |
| 4R5R6 | Euarchontoglires (superorder) | cytosolic phospholipase A2 [EC:3.1.1.4] |
| 4ZUME | Primates (order) | cytosolic phospholipase A2 [EC:3.1.1.4] |
| 98A77 | Haplorrhini (suborder) | cytosolic phospholipase A2 [EC:3.1.1.4] |
| BVIAA | Simiiformes (infraorder) | cytosolic phospholipase A2 [EC:3.1.1.4] |
| 9EH1S | Catarrhini (parvorder) | cytosolic phospholipase A2 [EC:3.1.1.4] |
| H5TRC | Bilateria (clade) | peptidyl-lysine (3S)-dioxygenase / protease [EC:1.14.11.63 3.4.-.-],cytosolic phospholipase A2 [EC:3.1.1.4],blocked early in transport 1 |
| 7NISI | Opisthokonta (clade) | cytosolic phospholipase A2 [EC:3.1.1.4],peptidyl-lysine (3S)-dioxygenase / protease [EC:1.14.11.63 3.4.-.-],holo-[acyl-carrier protein] synthase [EC:2.7.8.7] |
| 9G56C | Vertebrata (clade) | cytosolic phospholipase A2 [EC:3.1.1.4],peptidyl-lysine (3S)-dioxygenase / protease [EC:1.14.11.63 3.4.-.-] |
| FX5N3 | Hominoidea (superfamily) | cytosolic phospholipase A2 [EC:3.1.1.4] |
| 5MZG3 | Hominidae (family) | cytosolic phospholipase A2 [EC:3.1.1.4] |
| 5XZVU | Homininae (subfamily) | cytosolic phospholipase A2 [EC:3.1.1.4] |
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.