Q8BRH4 (MLL3_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 108.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Histone-lysine N-methyltransferase MLL3 EC=2.1.1.43 Alternative name(s): Myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog | ||
| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 4903 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Central component of the MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation. MLL3 may be a catalytic subunit of this complex By similarity. |
| Catalytic activity | S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. |
| Subunit structure | Component of the MLL2/3 complex (also named ASCOM complex), at least composed of MLL2/ALR or MLL3, ASH2L, RBBP5, WDR5, NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin By similarity. Interacts with histone H3 By similarity. |
| Subcellular location | Nucleus Probable. |
| Tissue specificity | In adult, detected in testis, kidney, spleen and lung, weakly expressed in brain and absent in heart and liver. First detected throughout the embryo at 8 dpc when expression is strong in forebrain neuroepithelium and absent in heart. Expressed in the eye lens between 10 and 14.5 dpc. By 13 dpc, expressed strongly in spinal cord, hand/foot plates and gonads. Ref.1 |
| Domain | The SET domain interacts with histone H3 but not H2A, H2B and H4, and may have a H3 lysine specific methylation activity By similarity. |
| Sequence similarities | Belongs to the histone-lysine methyltransferase family. TRX/MLL subfamily. Contains 1 A.T hook DNA-binding domain. Contains 1 DHHC-type zinc finger. Contains 1 FYR C-terminal domain. Contains 1 FYR N-terminal domain. Contains 6 PHD-type zinc fingers. Contains 1 post-SET domain. Contains 1 RING-type zinc finger. Contains 1 SET domain. |
| Sequence caution | The sequence AAN11291.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q8BRH4-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q8BRH4-2) The sequence of this isoform differs from the canonical sequence as follows: 839-878: Missing. 1414-1448: Missing. 1791-3080: Missing. 3814-3884: Missing. 4714-4717: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 4903 | 4903 | Histone-lysine N-methyltransferase MLL3 | PRO_0000124880 | |||||
Regions | |||||||||
| Domain | 4537 – 4597 | 61 | FYR N-terminal | ||||||
| Domain | 4598 – 4683 | 86 | FYR C-terminal | ||||||
| Domain | 4762 – 4883 | 122 | SET | ||||||
| Domain | 4887 – 4903 | 17 | Post-SET | ||||||
| DNA binding | 34 – 46 | 13 | A.T hook | ||||||
| Zinc finger | 340 – 390 | 51 | PHD-type 1 | ||||||
| Zinc finger | 343 – 388 | 46 | RING-type | ||||||
| Zinc finger | 387 – 437 | 51 | PHD-type 2 | ||||||
| Zinc finger | 435 – 488 | 54 | DHHC-type | ||||||
| Zinc finger | 463 – 519 | 57 | PHD-type 3 | ||||||
| Zinc finger | 950 – 1003 | 54 | PHD-type 4 | ||||||
| Zinc finger | 1000 – 1050 | 51 | PHD-type 5 | ||||||
| Zinc finger | 1077 – 1132 | 56 | PHD-type 6 | ||||||
| Region | 4840 – 4841 | 2 | S-adenosyl-L-methionine binding By similarity | ||||||
| Coiled coil | 1330 – 1352 | 23 | Potential | ||||||
| Coiled coil | 1743 – 1790 | 48 | Potential | ||||||
| Coiled coil | 3047 – 3074 | 28 | Potential | ||||||
| Coiled coil | 3166 – 3193 | 28 | Potential | ||||||
| Coiled coil | 3224 – 3270 | 47 | Potential | ||||||
| Coiled coil | 3387 – 3432 | 46 | Potential | ||||||
| Compositional bias | 384 – 487 | 104 | Cys-rich | ||||||
| Compositional bias | 970 – 1099 | 130 | Cys-rich | ||||||
| Compositional bias | 1519 – 1568 | 50 | Pro-rich | ||||||
| Compositional bias | 1708 – 1787 | 80 | Gln-rich | ||||||
| Compositional bias | 1831 – 2622 | 792 | Pro-rich | ||||||
| Compositional bias | 2682 – 2780 | 99 | Asp-rich | ||||||
| Compositional bias | 3022 – 3504 | 483 | Gln-rich | ||||||
Sites | |||||||||
| Metal binding | 4843 | 1 | Zinc By similarity | ||||||
| Metal binding | 4891 | 1 | Zinc By similarity | ||||||
| Metal binding | 4893 | 1 | Zinc By similarity | ||||||
| Metal binding | 4898 | 1 | Zinc By similarity | ||||||
| Binding site | 4817 | 1 | S-adenosyl-L-methionine By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 46 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 89 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 751 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 1294 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1497 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 1761 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 2005 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 2796 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 2803 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 2826 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 3709 | 1 | N6-acetyllysine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 839 – 878 | 40 | Missing in isoform 2. | VSP_020568 | |||||
| Alternative sequence | 1414 – 1448 | 35 | Missing in isoform 2. | VSP_020569 | |||||
| Alternative sequence | 1791 – 3080 | 1290 | Missing in isoform 2. | VSP_020570 | |||||
| Alternative sequence | 3814 – 3884 | 71 | Missing in isoform 2. | VSP_020571 | |||||
| Alternative sequence | 4714 – 4717 | 4 | Missing in isoform 2. | VSP_020572 | |||||
Experimental info | |||||||||
| Sequence conflict | 28 – 36 | 9 | SPAAADKRP → RSFVCGCGA in AAN11291. Ref.1 | ||||||
| Sequence conflict | 276 | 1 | V → A in AAN11291. Ref.1 | ||||||
| Sequence conflict | 433 – 440 | 8 | NCRICIEC → VSDFLICF in BAC32109. Ref.3 | ||||||
| Sequence conflict | 533 | 1 | E → G in AAN11291. Ref.1 | ||||||
| Sequence conflict | 577 | 1 | D → DA in AAN11291. Ref.1 | ||||||
| Sequence conflict | 675 | 1 | S → C in BAC35712. Ref.3 | ||||||
| Sequence conflict | 720 | 1 | K → E in AAN11291. Ref.1 | ||||||
| Sequence conflict | 763 | 1 | F → L in AAN11291. Ref.1 | ||||||
| Sequence conflict | 791 | 1 | H → Y in AAN11291. Ref.1 | ||||||
| Sequence conflict | 1324 – 1325 | 2 | VD → LH in AAN11291. Ref.1 | ||||||
| Sequence conflict | 1737 | 1 | E → V in AAN11291. Ref.1 | ||||||
| Sequence conflict | 1776 | 1 | Q → R in AAN11291. Ref.1 | ||||||
| Sequence conflict | 3236 | 1 | M → MM in AAN11291. Ref.1 | ||||||
| Sequence conflict | 3423 – 3424 | 2 | QR → P in AAN11291. Ref.1 | ||||||
| Sequence conflict | 3657 | 1 | E → G in AAN11291. Ref.1 | ||||||
| Sequence conflict | 3668 | 1 | A → V in AAN11291. Ref.1 | ||||||
| Sequence conflict | 4283 | 1 | C → Y in AAN11291. Ref.1 | ||||||
| Sequence conflict | 4306 | 1 | E → D in AAN11291. Ref.1 | ||||||
| Sequence conflict | 4520 | 1 | Q → R in AAN11291. Ref.1 | ||||||
| Sequence conflict | 4531 | 1 | V → G in AAN11291. Ref.1 | ||||||
| Sequence conflict | 4649 | 1 | Y → H in AAN11291. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterization and expression analysis during embryo development of the mouse ortholog of MLL3." Brun M.-E., Gasca S., Girard C., Bouton K., De Massy B., De Sario A. Gene 371:25-33(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY. Strain: BALB/c. Tissue: Testis. |
| [2] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [3] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-814 AND 4803-4903. Strain: C57BL/6J. Tissue: Embryo. |
| [4] | "Novel human HALR (MLL3) gene encodes a protein homologous to ALR and to ALL-1 involved in leukemia, and maps to chromosome 7q36 associated with leukemia and developmental defects." Tan Y.C., Chow V.T. Cancer Detect. Prev. 25:454-469(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 957-1376 AND 4214-4894. Tissue: Myeloma. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY138582 mRNA. Translation: AAN11291.1. Different initiation. AC116469 Genomic DNA. No translation available. AC127319 Genomic DNA. No translation available. AC134910 Genomic DNA. No translation available. AK044828 mRNA. Translation: BAC32109.1. AK054270 mRNA. Translation: BAC35712.2. AK077567 mRNA. Translation: BAC36867.1. AY036886 mRNA. Translation: AAK70213.1. AY036887 mRNA. Translation: AAK70214.1. |
| IPI | IPI00620674. IPI00623069. |
| UniGene | Mm.332268. |
3D structure databases | |
| ProteinModelPortal | Q8BRH4. |
| SMR | Q8BRH4. Positions 281-438, 479-517, 953-1050, 1080-1130, 1613-1702, 4440-4503, 4753-4903. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q8BRH4. 2 interactions. |
PTM databases | |
| PhosphoSite | Q8BRH4. |
Proteomic databases | |
| PaxDb | Q8BRH4. |
| PRIDE | Q8BRH4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Organism-specific databases | |
| MGI | MGI:2444959. Mll3. |
Phylogenomic databases | |
| eggNOG | COG2940. |
| HOGENOM | HOG000113602. |
| HOVERGEN | HBG045586. |
| InParanoid | Q8BRH4. |
| OrthoDB | EOG4THVS4. |
Gene expression databases | |
| ArrayExpress | Q8BRH4. |
| Bgee | Q8BRH4. |
| CleanEx | MM_MLL3. |
| Genevestigator | Q8BRH4. |
| GermOnline | ENSMUSG00000038056. Mus musculus. |
Family and domain databases | |
| Gene3D | 3.30.40.10. 6 hits. |
| InterPro | IPR017956. AT_hook_DNA-bd_motif. IPR003889. FYrich_C. IPR003888. FYrich_N. IPR009071. HMG_box_dom. IPR000637. HMGI/Y_DNA-bd_CS. IPR003616. Post-SET_dom. IPR002219. Prot_Kinase_C-like_PE/DAG-bd. IPR001214. SET_dom. IPR001594. Znf_DHHC_palmitoyltrfase. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view] |
| Pfam | PF05965. FYRC. 1 hit. PF05964. FYRN. 1 hit. PF00628. PHD. 2 hits. PF00856. SET. 1 hit. [Graphical view] |
| SMART | SM00384. AT_hook. 2 hits. SM00109. C1. 2 hits. SM00542. FYRC. 1 hit. SM00541. FYRN. 1 hit. SM00398. HMG. 1 hit. SM00249. PHD. 8 hits. SM00508. PostSET. 1 hit. SM00184. RING. 4 hits. SM00317. SET. 1 hit. [Graphical view] |
| SUPFAM | SSF57903. FYVE_PHD_ZnF. 6 hits. |
| PROSITE | PS51543. FYRC. 1 hit. PS51542. FYRN. 1 hit. PS00354. HMGI_Y. 1 hit. PS50868. POST_SET. 1 hit. PS50280. SET. 1 hit. PS50216. ZF_DHHC. 1 hit. PS01359. ZF_PHD_1. 5 hits. PS50016. ZF_PHD_2. 6 hits. PS50089. ZF_RING_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | MLL3. mouse. |
| SOURCE | Search... |
Entry information
| Entry name | MLL3_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q8BRH4 Secondary accession number(s): Q5YLV9 Q923H6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
