Domains within Homo sapiens protein Q9UGL1-2
Isoform 2 of Lysine-specific demethylase 5B
Alternative representations: 1 /
| Protein length | 1580 aa |
|---|---|
| Source database | UniProt |
| Identifiers | Q9UGL1-2, ENSP00000356233.2, ENSP00000356233, Q9UIW7_HUMAN, Q9UIW7, B3KMS8_HUMAN, B3KMS8, Q9UFC7_HUMAN, Q9UFC7, B3KMS2_HUMAN, B3KMS2, Q9NSZ7_HUMAN, Q9NSZ7, Q6UGB8_HUMAN, Q6UGB8 |
| Source gene | ENSG00000117139 |
| Alternative splicing | KDM5B_HUMAN, Q9UGL1-2, ENSP00000235790.4, R4GN45_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. |
Predicted functional partners
Q9UGL1-2 is shown as 
KDM5B 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 Q9UGL1-2 is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:
KEGG pathways
| Pathway | Description | |
|---|---|---|
| map04550 | Signaling pathways regulating pluripotency of stem cells |
KEGG orthologous groups
| KO | Name | Description | |
|---|---|---|---|
| K11446 | KDM5, JARID1 | [histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67] | |
| K02112 | ATPF1B, atpD | F-type H+/Na+-transporting ATPase subunit beta [EC:7.1.2.2 7.2.2.1] | 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.ENSP00000356233 in eggNOG.
| OG | Taxonomic class | Description |
|---|---|---|
| LCOG0055 | All organisms (root) | F-type H+/Na+-transporting ATPase subunit beta [EC:7.1.2.2 7.2.2.1],[histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67],F-type H+-transporting ATPase subunit beta [EC:7.1.2.2] |
| KOG1246 | Eukaryota (superkingdom) | [histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67],protein Jumonji,lysine-specific demethylase 6A [EC:1.14.11.68] |
| HU39X | Metazoa (kingdom) | [histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67] |
| 94MHV | Chordata (phylum) | [histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67] |
| 5QS5C | Sarcopterygii (superclass) | [histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67] |
| 8ZKIC | Mammalia (class) | [histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67] |
| 4RS14 | Euarchontoglires (superorder) | [histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67] |
| 4ZV5C | Primates (order) | [histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67] |
| 98GFD | Haplorrhini (suborder) | [histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67] |
| BV2J5 | Simiiformes (infraorder) | [histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67] |
| 9F0HG | Catarrhini (parvorder) | [histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67] |
| H4NJT | Bilateria (clade) | [histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67] |
| 7M280 | Opisthokonta (clade) | [histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67] |
| 9G8N2 | Vertebrata (clade) | [histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67] |
| FX9DH | Hominoidea (superfamily) | [histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67] |
| 5N7DN | Hominidae (family) | [histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67] |
| 5XURW | Homininae (subfamily) | [histone H3]-trimethyl-L-lysine4 demethylase [EC:1.14.11.67] |
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.