LMO2

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LMO2
Protein LDB1 PDB 2XJY.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases LMO2, RBTN2, RBTNL1, RHOM2, TTG2, LIM domain only 2
External IDs MGI: 102811 HomoloGene: 4072 GeneCards: LMO2
RNA expression pattern
PBB GE LMO2 204249 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001142315
NM_001142316
NM_005574

NM_001142335
NM_001142336
NM_001142337
NM_008505

RefSeq (protein)

NP_001135787
NP_001135788
NP_005565

Location (UCSC) Chr 11: 33.86 – 33.89 Mb Chr 2: 103.96 – 103.98 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

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. LMO2 is a protein which in humans is encoded by the LMO2 gene.[3]

Function[edit]

LMO2 encodes a cysteine-rich, two LIM domain protein that is required for yolk sac erythropoiesis.[4] The LMO2 protein has a central and crucial role in hematopoietic development and is highly conserved.

Clinical significance[edit]

The LMO2 transcription start site is located approximately 25 kb downstream from the 11p13 T-cell translocation cluster (11p13 ttc), where a number of T-cell acute lymphoblastic leukemia-specific translocations occur.[5]

Interactions[edit]

LMO2 has been shown to interact with:

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Boehm T, Foroni L, Kaneko Y, Perutz MF, Rabbitts TH (May 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 of the United States of America. 88 (10): 4367–71. doi:10.1073/pnas.88.10.4367. PMC 51660Freely accessible. PMID 2034676. 
  4. ^ Warren AJ, Colledge WH, Carlton MB, Evans MJ, Smith AJ, Rabbitts TH (Jul 1994). "The oncogenic cysteine-rich LIM domain protein rbtn2 is essential for erythroid development". Cell. 78 (1): 45–57. doi:10.1016/0092-8674(94)90571-1. PMID 8033210. 
  5. ^ EntrezGene 4005
  6. ^ a b c Osada H, Grutz G, Axelson H, Forster A, Rabbitts TH (Oct 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 of the United States of America. 92 (21): 9585–9. doi:10.1073/pnas.92.21.9585. PMC 40846Freely accessible. PMID 7568177. 
  7. ^ Mao S, Neale GA, Goorha RM (Apr 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. 
  8. ^ Bégay-Müller V, Ansieau S, Leutz A (Jun 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. 
  9. ^ Wadman I, Li J, Bash RO, Forster A, Osada H, Rabbitts TH, Baer R (Oct 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 395422Freely accessible. PMID 7957052. 
  10. ^ Valge-Archer VE, Osada H, Warren AJ, Forster A, Li J, Baer R, Rabbitts TH (Aug 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 of the United States of America. 91 (18): 8617–21. doi:10.1073/pnas.91.18.8617. PMC 44657Freely accessible. PMID 8078932. 
  11. ^ Goardon N, Lambert JA, Rodriguez P, Nissaire P, Herblot S, Thibault P, Dumenil D, Strouboulis J, Romeo PH, Hoang T (Jan 2006). "ETO2 coordinates cellular proliferation and differentiation during erythropoiesis". The EMBO Journal. 25 (2): 357–66. doi:10.1038/sj.emboj.7600934. PMC 1383517Freely accessible. PMID 16407974. 

Further reading[edit]