Domains within Homo sapiens protein IPSP_HUMAN (P05154)
Plasma serine protease inhibitor
Alternative representations: 1 /
| Protein length | 406 aa |
|---|---|
| Source database | UniProt |
| Identifiers | IPSP_HUMAN, P05154, ENSP00000450837.1, ENSP00000450837, ENSP00000451126.1, ENSP00000451126, ENSP00000451610.1, ENSP00000451610, ENSP00000333203.7, ENSP00000333203, Q07616, Q9UG30, A0A024R6N9_HUMAN, A0A024R6N9, G3V2M1_HUMAN, G3V2M1, G3V265_HUMAN, G3V265, G3V3F5_HUMAN, G3V3F5, G3V264_HUMAN, G3V264, G3V4B4_HUMAN, G3V4B4, G3V482_HUMAN, G3V482 |
| Source gene | ENSG00000188488 |
| Alternative splicing | ENSP00000450484.1, IPSP_HUMAN, G3V5Q9_HUMAN, ENSP00000450745.1, ENSP00000451215.1, ENSP00000451697.1, ENSP00000451650.1, ENSP00000450485.1, ENSP00000451487.1 |
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 cellular organisms
Predicted functional partners
IPSP_HUMAN is shown as 
SERPINA5 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 IPSP_HUMAN is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:
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 21 PTMs annotated in this protein:
| PTM | Count | |
|---|---|---|
 | Phosphorylation | 8 |
 | N-linked glycosylation | 5 |
 | Acetylation | 4 |
 | Proteolytic cleavage | 2 |
 | O-GalNAc glycosylation | 1 |
 | O-linked glycosylation | 1 |
To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein SERPINA5.
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.ENSP00000333203 in eggNOG.
| OG | Taxonomic class | Description |
|---|---|---|
| LCOG4826 | All organisms (root) | serpin A,serpin B,serpin peptidase inhibitor, clade H, member 1 |
| KOG2392 | Eukaryota (superkingdom) | serpin A,serpin B,serpin peptidase inhibitor, clade H, member 1 |
| HTCWE | Metazoa (kingdom) | serpin A,serpin B,leukocyte elastase inhibitor |
| 94TDG | Chordata (phylum) | serpin A,pigment epithelium-derived factor,alpha-1-antitrypsin |
| 5R9WQ | Sarcopterygii (superclass) | serpin A,alpha-1-antitrypsin,thyroxine-binding globulin |
| 8YX53 | Mammalia (class) | serpin A,thyroxine-binding globulin,protein C inhibitor |
| 4RBF4 | Euarchontoglires (superorder) | protein C inhibitor,serpin A |
| 4ZYWW | Primates (order) | protein C inhibitor |
| 98G0Q | Haplorrhini (suborder) | protein C inhibitor |
| BV6DB | Simiiformes (infraorder) | protein C inhibitor |
| 9ES8R | Catarrhini (parvorder) | protein C inhibitor |
| 9FS9C | Vertebrata (clade) | serpin A,pigment epithelium-derived factor,alpha-1-antitrypsin |
| H4UFA | Bilateria (clade) | serpin A,serpin B,leukocyte elastase inhibitor |
| 7HDH9 | Opisthokonta (clade) | serpin A,serpin B,leukocyte elastase inhibitor |
| FX5K7 | Hominoidea (superfamily) | protein C inhibitor |
| 5MZFT | Hominidae (family) | protein C inhibitor |
| 5Y36G | Homininae (subfamily) | protein C inhibitor |
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.