LMO2
Sign in to saveAlso known as RBTN2, RBTNL1, RHOM2, TTG2, LIM domain only 2, LMO-2
LIM domain only 2 (rhombotin-like 1), also known as LMO2, RBTNL1, RBTN2, RHOM2, LIM Domain Only Protein 2, TTG2, and T-Cell Translocation Protein 2, is a protein which in humans is encoded by the LMO2 gene.
Gene data
LMO2- Name
- LIM domain only 2
- Type
- protein-coding
- Aliases
- LMO-2, RBTN2, RBTNL1, RHOM2, TTG2
LMO2 encodes a cysteine-rich, two LIM-domain protein that is required for yolk sac erythropoiesis. The LMO2 protein has a central and crucial role in hematopoietic development and is highly conserved. The LMO2 transcription start site is located approximately 25 kb downstream from the 11p13 T-cell translocation cluster (11p13 ttc), where a number T-cell acute lymphoblastic leukemia-specific translocations occur. Alternative splicing results in multiple transcript variants encoding different isoforms.[provided by RefSeq, Nov 2008].
via MyGene.info
Gene · Ensembl
LIM domain only 2
- Symbol
- LMO2
- Biotype
- Protein coding
- Organism
- Homo sapiens
- Location
- 11:33,858,563-33,892,076
- Strand
- Reverse (−)
- Assembly
- GRCh38
via Ensembl · EMBL-EBI
Wikidata facts
- Image
- Protein LDB1 PDB 2XJY.png
Show 5 more facts
- HomoloGene ID
- 4072
- exact match
- identifiers.org/ncbigene/4005
- genomic end
- 33892076
- genomic start
- 33880122
- cytogenetic location
- 11p13
Sources (4)
via Wikidata · CC0
~3 min read
Article
7 sectionsContents
- Structure
- Function
- Clinical significance
- Interactions
- References
- Further reading
- External links
LIM domain only 2 (rhombotin-like 1), also known as LMO2, RBTNL1, RBTN2, RHOM2, LIM Domain Only Protein 2, TTG2, and T-Cell Translocation Protein 2, is a protein which in humans is encoded by the LMO2 gene.
== Structure == LMO2 is characterized as a small, cysteine-rich protein comprising two tandem LIM domains. Each LIM domain features a conserved double zinc finger motif, wherein zinc ions are coordinated by cysteine and histidine residues. These domains are critical for LMO2's primary function as a scaffolding protein facilitating protein-protein interactions within transcriptional regulatory complexes. Notably, LMO2 lacks an intrinsic DNA-binding domain; its influence on gene expression is mediated through its recruitment into multi-protein assemblies. The inter-domain linker region contributes to the protein's overall conformational dynamics, potentially modulating its interaction with diverse binding partners. The structural integrity conferred by the zinc fingers within the LIM domains is essential for maintaining the protein's functional architecture in the context of hematopoiesis and leukemogenesis.