LMO2

LIM domain only 2 (rhombotin-like 1)

Rendering based on PDB 2XJY.
Identifiers
Symbols LMO2; RBTN2; RBTNL1; RHOM2; TTG2
External IDs OMIM180385 MGI102811 HomoloGene4072 GeneCards: LMO2 Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 4005 16909
Ensembl ENSG00000135363 ENSMUSG00000032698
UniProt P25791 Q544Z2
RefSeq (mRNA) NM_001142315.1 XM_001001351
RefSeq (protein) NP_001135787.1 XP_001001351
Location (UCSC) Chr 11:
33.88 – 33.91 Mb
Chr 2:
103.8 – 103.82 Mb
PubMed search [1] [2]

LIM domain only 2 (rhombotin-like 1), also known as LMO2, is a protein which in humans is encoded by the LMO2 gene.[1]

Contents

Function

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.[2]

Interactions

LMO2 has been shown to interact with JARID1A,[3] GATA1,[4] GATA2,[4] TAL1[4][5][6][7] and MLLT4.[8]

References

  1. ^ Boehm, T. (1991). "The Rhombotin Family of Cysteine-Rich LIM-Domain Oncogenes: Distinct Members are Involved in T-Cell Translocations to Human Chromosomes 11p15 and 11p13". Proceedings of the National Academy of Sciences 88 (10): 4367–71. doi:10.1073/pnas.88.10.4367. PMC 51660. PMID 2034676. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=51660. 
  2. ^ EntrezGene 4005
  3. ^ Mao, Shifeng; Neale, Geoffrey AM; Goorha, Rakesh M (1997). "T-cell oncogene rhombotin-2 interacts with retinoblastoma-binding protein 2". Oncogene 14 (13): 1531–9. doi:10.1038/sj.onc.1200988. PMID 9129143. 
  4. ^ a b c Osada, H. (1995). "Association of Erythroid Transcription Factors: Complexes Involving the LIM Protein RBTN2 and the Zinc-Finger Protein GATA1". Proceedings of the National Academy of Sciences 92 (21): 9585–9. doi:10.1073/pnas.92.21.9585. PMC 40846. PMID 7568177. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=40846. 
  5. ^ Wadman, I; Li, J; Bash, RO; Forster, A; Osada, H; Rabbitts, TH; Baer, R (1994). "Specific in vivo association between the bHLH and LIM proteins implicated in human T cell leukemia". The EMBO journal 13 (20): 4831–9. PMC 395422. PMID 7957052. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=395422. 
  6. ^ Valge-Archer, V. E. (1994). "The LIM Protein RBTN2 and the Basic Helix-Loop-Helix Protein TAL1 are Present in a Complex in Erythroid Cells". Proceedings of the National Academy of Sciences 91 (18): 8617–21. doi:10.1073/pnas.91.18.8617. PMC 44657. PMID 8078932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=44657. 
  7. ^ Goardon, Nicolas; Lambert, Julie A; Rodriguez, Patrick; Nissaire, Philippe; Herblot, Sabine; Thibault, Pierre; Dumenil, Dominique; Strouboulis, John et al. (2006). "ETO2 coordinates cellular proliferation and differentiation during erythropoiesis". The EMBO Journal 25 (2): 357–66. doi:10.1038/sj.emboj.7600934. PMC 1383517. PMID 16407974. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1383517. 
  8. ^ Begaymuller, V; Ansieau, S; Leutz, A (2002). "The LIM domain protein Lmo2 binds to AF6, a translocation partner of the MLL oncogene". FEBS Letters 521 (1–3): 36–8. doi:10.1016/S0014-5793(02)02814-4. PMID 12067721. 

Further reading