Domains within Mus musculus protein P55200-2
Isoform 2 of Histone-lysine N-methyltransferase 2A
Alternative representations: 1 /
| Protein length | 3963 aa |
|---|---|
| Source database | UniProt |
| Identifiers | P55200-2, ENSMUSP00000002095.3, ENSMUSP00000002095 |
| Source gene | ENSMUSG00000002028 |
| Alternative splicing | KMT2A_MOUSE, P55200-2, S4R199_MOUSE, S4R2S5_MOUSE, D3Z5H5_MOUSE, A0A1L1SQS9_MOUSE |
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 Eutheria
Predicted functional partners
P55200-2 is shown as 
Kmt2a 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.
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 10090.ENSMUSP00000002095 in eggNOG.
| OG | Taxonomic class | Description |
|---|---|---|
| LCOG2940 | All organisms (root) | uncharacterized protein,[histone H3]-lysine4/36 N-trimethyltransferase SMYD [EC:2.1.1.354 2.1.1.357],[histone H3]-lysine9 N-trimethyltransferase EHMT [EC:2.1.1.355] |
| KOG1084 | Eukaryota (superkingdom) | G2/M phase-specific E3 ubiquitin-protein ligase [EC:2.3.2.26],PHD finger protein 6,transcription factor 20 |
| HW4Y9 | Metazoa (kingdom) | [histone H3]-lysine4 N-trimethyltransferase MLL1 [EC:2.1.1.354],[histone H3]-lysine4 N-trimethyltransferase MLL4 [EC:2.1.1.354],[histone H3]-lysine4 N-trimethyltransferase SETD1 [EC:2.1.1.354] |
| 93XJ5 | Chordata (phylum) | [histone H3]-lysine4 N-trimethyltransferase MLL1 [EC:2.1.1.354],[histone H3]-lysine4 N-trimethyltransferase MLL4 [EC:2.1.1.354],[histone H3]-lysine4 N-trimethyltransferase SETD1 [EC:2.1.1.354] |
| 5R4TC | Sarcopterygii (superclass) | [histone H3]-lysine4 N-trimethyltransferase MLL1 [EC:2.1.1.354],[histone H3]-lysine4 N-trimethyltransferase MLL4 [EC:2.1.1.354] |
| 8Z6R3 | Mammalia (class) | [histone H3]-lysine4 N-trimethyltransferase MLL1 [EC:2.1.1.354],[histone H3]-lysine4 N-trimethyltransferase MLL4 [EC:2.1.1.354] |
| 4R80Z | Euarchontoglires (superorder) | [histone H3]-lysine4 N-trimethyltransferase MLL1 [EC:2.1.1.354] |
| AHYWM | Rodentia (order) | [histone H3]-lysine4 N-trimethyltransferase MLL1 [EC:2.1.1.354] |
| 8D3X2 | Myomorpha (suborder) | [histone H3]-lysine4 N-trimethyltransferase MLL1 [EC:2.1.1.354] |
| H48MM | Bilateria (clade) | [histone H3]-lysine4 N-trimethyltransferase MLL1 [EC:2.1.1.354],[histone H3]-lysine4 N-trimethyltransferase MLL4 [EC:2.1.1.354],[histone H3]-lysine4 N-trimethyltransferase SETD1 [EC:2.1.1.354] |
| 7I5VZ | Opisthokonta (clade) | [histone H3]-lysine4 N-trimethyltransferase MLL1 [EC:2.1.1.354],[histone H3]-lysine4 N-trimethyltransferase MLL4 [EC:2.1.1.354],[histone H3]-lysine4 N-trimethyltransferase SETD1 [EC:2.1.1.354] |
| 9FJY6 | Vertebrata (clade) | [histone H3]-lysine4 N-trimethyltransferase MLL1 [EC:2.1.1.354],[histone H3]-lysine4 N-trimethyltransferase MLL4 [EC:2.1.1.354] |
| CQ057 | Muridae (family) | [histone H3]-lysine4 N-trimethyltransferase MLL1 [EC:2.1.1.354] |
| AECG7 | Murinae (subfamily) | [histone H3]-lysine4 N-trimethyltransferase MLL1 [EC:2.1.1.354] |
| 5PTD5 | Mus (genus) | [histone H3]-lysine4 N-trimethyltransferase MLL1 [EC:2.1.1.354] |
| HDZA8 | Mus (subgenus) | [histone H3]-lysine4 N-trimethyltransferase MLL1 [EC:2.1.1.354] |
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.