LMO2

  • Official Full Name

    LIM domain only 2 (rhombotin-like 1)

  • Overview

    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.

  • Synonyms

    LMO2;LIM domain only 2 (rhombotin-like 1);RBTNL1;rhombotin-2;RBTN2;RHOM2;rhombotin like 1;T cell translocation gene 2;TTG2;LMO-2;rhombotin 2;rhombotin-like 1;LIM domain only protein 2;T-cell translocation gene 2;cysteine-rich protein TTG-2;T-cell translocation protein 2

Recombinant Proteins

  • Rhesus macaque
  • Chicken
  • Zebrafish
  • Human
  • Mouse
  • Mammalian Cells
  • HEK293
  • E.coli
  • His
  • Non
  • Myc&DDK
  • His&Fc&Avi

    Involved Pathway

    LMO2 involved in several pathways and played different roles in them. We selected most pathways LMO2 participated on our site, such as Transcriptional misregulation in cancer, which may be useful for your reference. Also, other proteins which involved in the same pathway with LMO2 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein
    Transcriptional misregulation in cancer KLF3,REL,FCGR1A,SPINT1,NTRK1,ASPSCR1,BIRC3,HIST1H3E,RXRB,RXRA

    Protein Function

    LMO2 has several biochemical functions, for example, E-box binding,RNA polymerase II activating transcription factor binding,RNA polymerase II regulatory region sequence-specific DNA binding. Some of the functions are cooperated with other proteins, some of the functions could acted by LMO2 itself. We selected most functions LMO2 had, and list some proteins which have the same functions with LMO2. You can find most of the proteins on our site.

    Function Related Protein
    transcriptional activator activity, RNA polymerase II transcription factor binding CREB1,KLF14,PPARA,MED12,JUN,KLF4,NFE2L1,NKX2,SOX10,CLOCK
    RNA polymerase II transcription factor activity, sequence-specific DNA binding TP73,ZNF446,SOX8,GCM1,ZNF434,FOXO1,PLAGL2,FEV,NFIXB,FOXP3A
    bHLH transcription factor binding EP300,PSMD9,IKZF4,FOXH1,USF1,TCF21,ISL1,TCF4,ASCL1,SOX9
    transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding BARX2,GABPA,ETV5,ELF5,SLAMF7,AIRE,MYOCD,RFX6,GATA5,MAFG
    E-box binding ASCL1,C1orf51,NEUROG2,ARNTL2,ARNTL,MYOD1,NEUROG1,TWIST1,AHR,BHLHE40
    chromatin binding MORF4L1,TWIST2,SIRT6,CITED2,MED1,CTBP2,NR5A1B,SMARCA2,ARID3C,SUV39H1
    RNA polymerase II activating transcription factor binding BHLHE40,TBX20,EP300,RB1,CREBBP,SMAD3,TBX3,JUN,ISL1,NHLH2
    RNA polymerase II regulatory region sequence-specific DNA binding PHF21A,CREB3L3,CSDA,ALX1,AASS,GATA2B,FOXD3,PRDM15,HMX1,ZFY1
    protein binding FAM162A,XCL2,PAEP,RAP2A,DEF6,TBX5A,SLC19A2,EXOC7,TRIM10,RAB22A

    Interacting Protein

    LMO2 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with LMO2 here. Most of them are supplied by our site. Hope this information will be useful for your research of LMO2.

    MAPRE3;HNRNPM;MAPRE2;LDB1;PHC2

    Resources

    Research Area

    Hemangioblast Markers
    Cancer Stem Cell Transcription Factors
    Hemangioblast Transcription Factors
    Hematopoietic Stem Cell Transcription Factors and Regulators
    Mesodermal Lineage Markers

    References

    • Zhang, J; Rabbitts, TH; et al. Intracellular antibody capture: A molecular biology approach to inhibitors of protein-protein interactions. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS 1844:1970-1976(2014).
    • Sewell, H; Tanaka, T; et al. Conformational flexibility of the oncogenic protein LMO2 primes the formation of the multi-protein transcription complex. SCIENTIFIC REPORTS 4:-(2014).

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