LMO2

LIM domain only 2 (rhombotin-like 1)

Rendering based on PDB 2XJY.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2XJY, 2XJZ, 2YPA, 4KFZ

Identifiers

Symbols

LMO2 ; RBTN2; RBTNL1; RHOM2; TTG2

External IDs

OMIM: 180385 MGI: 102811 HomoloGene: 4072 GeneCards: LMO2 Gene

Gene ontology
Molecular function	• RNA polymerase II regulatory region sequence-specific DNA binding • sequence-specific DNA binding RNA polymerase II transcription factor activity • RNA polymerase II activating transcription factor binding • RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription • RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription • chromatin binding • protein binding • zinc ion binding • bHLH transcription factor binding • cofactor binding • E-box binding
Cellular component	• nucleus • transcription factor complex
Biological process	• multicellular organismal development • embryonic hemopoiesis • mRNA transcription from RNA polymerase II promoter • negative regulation of erythrocyte differentiation • positive regulation of transcription from RNA polymerase II promoter • cellular response to thyroid hormone stimulus
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 11:
33.88 – 33.91 Mb

Chr 2:
103.96 – 103.98 Mb

PubMed search

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.^[1]

Function

LMO2 encodes a cysteine-rich, two LIM domain protein that is required for yolk sac erythropoiesis.^[2] The LMO2 protein has a central and crucial role in hematopoietic development and is highly conserved.

Clinical significance

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.^[3]

Interactions

LMO2 has been shown to interact with:

References

↑ Boehm T, Foroni L, Kaneko Y, Perutz MF, Rabbitts TH (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.
↑ Warren AJ, Colledge WH, Carlton MB, Evans MJ, Smith AJ, Rabbitts TH (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.
↑ EntrezGene 4005
↑ 4.0 4.1 4.2 Osada H, Grutz G, Axelson H, Forster A, Rabbitts TH. "Association of erythroid transcription factors: complexes involving the LIM protein RBTN2 and the zinc-finger protein GATA1". Proc. Natl. Acad. Sci. U.S.A. 92 (21): 9585–9. doi:10.1073/pnas.92.21.9585. PMC 40846. PMID 7568177.
↑ Mao S, Neale GA, Goorha RM. "T-cell oncogene rhombotin-2 interacts with retinoblastoma-binding protein 2". Oncogene 14 (13): 1531–9. doi:10.1038/sj.onc.1200988. PMID 9129143.
↑ Bégay-Müller V, Ansieau S, Leutz A. "The LIM domain protein Lmo2 binds to AF6, a translocation partner of the MLL oncogene". FEBS Lett. 521 (1-3): 36–8. doi:10.1016/s0014-5793(02)02814-4. PMID 12067721. Vancouver style error (help)
↑ Wadman I, Li J, Bash RO, Forster A, Osada H, Rabbitts TH et al. "Specific in vivo association between the bHLH and LIM proteins implicated in human T cell leukemia". EMBO J. 13 (20): 4831–9. PMC 395422. PMID 7957052.
↑ Valge-Archer VE, Osada H, Warren AJ, Forster A, Li J, Baer R et al. "The LIM protein RBTN2 and the basic helix-loop-helix protein TAL1 are present in a complex in erythroid cells". Proc. Natl. Acad. Sci. U.S.A. 91 (18): 8617–21. doi:10.1073/pnas.91.18.8617. PMC 44657. PMID 8078932.
↑ Goardon N, Lambert JA, Rodriguez P, Nissaire P, Herblot S, Thibault P et al. "ETO2 coordinates cellular proliferation and differentiation during erythropoiesis". EMBO J. 25 (2): 357–66. doi:10.1038/sj.emboj.7600934. PMC 1383517. PMID 16407974.

Royer-Pokora B, Loos U, Ludwig WD (1991). "TTG-2, a new gene encoding a cysteine-rich protein with the LIM motif, is overexpressed in acute T-cell leukaemia with the t(11;14)(p13;q11)". Oncogene 6 (10): 1887–93. PMID 1923511.
Boehm T, Foroni L, Kaneko Y, Perutz MF, Rabbitts TH (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.
Boehm T, Spillantini MG, Sofroniew MV, Surani MA, Rabbitts TH (1991). "Developmentally regulated and tissue specific expression of mRNAs encoding the two alternative forms of the LIM domain oncogene rhombotin: Evidence for thymus expression". Oncogene 6 (5): 695–703. PMID 2052354.
Dong WF, Xu Y, Hu QL, Munroe D, Minowada J, Housman DE et al. (1995). "Molecular characterization of a chromosome translocation breakpoint t(11;14)(p13;q11) from the cell line KOPT-K1". Leukemia : official journal of the Leukemia Society of America, Leukemia Research Fund, U.K 9 (11): 1812–7. PMID 7475267.
Osada H, Grutz G, Axelson H, Forster A, Rabbitts TH (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.
Sánchez-García I, Axelson H, Rabbitts TH (1995). "Functional diversity of LIM proteins: Amino-terminal activation domains in the oncogenic proteins RBTN1 and RBTN2". Oncogene 10 (7): 1301–6. PMID 7731680. Vancouver style error (help)
Wadman I, Li J, Bash RO, Forster A, Osada H, Rabbitts TH et al. (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.
Valge-Archer VE, Osada H, Warren AJ, Forster A, Li J, Baer R et al. (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.
Wilkinson DA, Neale GA, Mao S, Naeve CW, Goorha RM (1997). "Elf-2, a rhombotin-2 binding ets transcription factor: Discovery and potential role in T cell leukemia". Leukemia 11 (1): 86–96. doi:10.1038/sj.leu.2400516. PMID 9001422.
Mao S, Neale GA, Goorha RM (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.
Osada H, Grutz GG, Axelson H, Forster A, Rabbitts TH (1997). "LIM-only protein Lmo2 forms a protein complex with erythroid transcription factor GATA-1". Leukemia : official journal of the Leukemia Society of America, Leukemia Research Fund, U.K. 11 Suppl 3: 307–12. PMID 9209374.
Wadman IA, Osada H, Grütz GG, Agulnick AD, Westphal H, Forster A et al. (1997). "The LIM-only protein Lmo2 is a bridging molecule assembling an erythroid, DNA-binding complex which includes the TAL1, E47, GATA-1 and Ldb1/NLI proteins". The EMBO Journal 16 (11): 3145–57. doi:10.1093/emboj/16.11.3145. PMC 1169933. PMID 9214632. Vancouver style error (help)
Visvader JE, Mao X, Fujiwara Y, Hahm K, Orkin SH (1997). "The LIM-domain binding protein Ldb1 and its partner LMO2 act as negative regulators of erythroid differentiation". Proceedings of the National Academy of Sciences 94 (25): 13707–12. doi:10.1073/pnas.94.25.13707. PMC 28370. PMID 9391090.
Jurata LW, Pfaff SL, Gill GN (1998). "The Nuclear LIM Domain Interactor NLI Mediates Homo- and Heterodimerization of LIM Domain Transcription Factors". Journal of Biological Chemistry 273 (6): 3152–7. doi:10.1074/jbc.273.6.3152. PMID 9452425.
Kenny DA, Jurata LW, Saga Y, Gill GN (1998). "Identification and characterization of LMO4, an LMO gene with a novel pattern of expression during embryogenesis". Proceedings of the National Academy of Sciences 95 (19): 11257–62. doi:10.1073/pnas.95.19.11257. PMC 21629. PMID 9736723.
Ono Y, Fukuhara N, Yoshie O (1998). "TAL1 and LIM-only proteins synergistically induce retinaldehyde dehydrogenase 2 expression in T-cell acute lymphoblastic leukemia by acting as cofactors for GATA3". Molecular and Cellular Biology 18 (12): 6939–50. PMC 109277. PMID 9819382.
Bach I, Rodriguez-Esteban C, Carrière C, Bhushan A, Krones A, Rose DW et al. (1999). "RLIM inhibits functional activity of LIM homeodomain transcription factors via recruitment of the histone deacetylase complex". Nature Genetics 22 (4): 394–9. doi:10.1038/11970. PMID 10431247. Vancouver style error (help)
Vitelli L, Condorelli G, Lulli V, Hoang T, Luchetti L, Croce CM et al. (2000). "A Pentamer Transcriptional Complex Including tal-1 and Retinoblastoma Protein Downmodulates c-kit Expression in Normal Erythroblasts". Molecular and Cellular Biology 20 (14): 5330–42. doi:10.1128/MCB.20.14.5330-5342.2000. PMC 85982. PMID 10866689.
Davenport J, Neale GA, Goorha R (2000). "Identification of genes potentially involved in LMO2-induced leukemogenesis". Leukemia 14 (11): 1986–96. doi:10.1038/sj.leu.2401913. PMID 11069036.
Sum EY, Peng B, Yu X, Chen J, Byrne J, Lindeman GJ et al. (2001). "The LIM Domain Protein LMO4 Interacts with the Cofactor CtIP and the Tumor Suppressor BRCA1 and Inhibits BRCA1 Activity". Journal of Biological Chemistry 277 (10): 7849–5. doi:10.1074/jbc.M110603200. PMID 11751867.

LMO2

Function

Clinical significance

Interactions

References

Further reading