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Homo sapiens


Part of: Cancer Cell Line Encyclopedia (CCLE) project. Part of: COSMIC cell lines project. Part of: MD Anderson Cell Lines Project. Part of: Naval Biosciences Laboratory (NBL) collection (transferred to ATCC in 1982). Part of: NCI Pediatric Preclinical Testing Program (PPTP) cell line panel. Doubling time: 23 hours (PubMed=20922763). Microsatellite instability: Stable (MSS) (Sanger). Sequence variation: Homozygous for NRAS p.Gln61His (c.183A>T) (PubMed=3158613; PubMed=12068308; PubMed=22142829; ATCC). Sequence variation: Homozygous for TP53 p.Arg248Trp (c.742C>T) (PubMed=2216456; ATCC). Omics: Cell surface proteome. Omics: Deep exome analysis. Omics: Deep RNAseq analysis. Omics: DNA methylation analysis. Omics: Protein expression by reverse-phase protein arrays. Omics: SNP array analysis. Omics: Transcriptome analysis. Genome ancestry: African=3.96%; Native American=0%; East Asian, North=4.77%; East Asian, South=0%; South Asian=0%; European, North=53.65%; European, South=37.61% (PubMed=30894373). Discontinued: ATCC; CRL-7713. Discontinued: ATCC; CRL-7731. Discontinued: ATCC; HTB-97. DT Created: 04-04-12; Last updated: 05-07-19; Version: 29

Proper Citation

ATCC Cat# HTB-97, RRID:CVCL_1649


Cancer cell line DT Created: 04-04-12; Last updated: 05-07-19; Version: 29


DT Created: 04-04-12; Last updated: 05-07-19; Version: 29


R D, RD-2, RD 2, 130T, 130-T, 130 T, TE-32, TE 32, TE32, TE 32.T, Te 32.T DT Created: 04-04-12, Last updated: 05-07-19, Version: 29



Cat Num


Cross References

BTO; BTO:0005377 CLO; CLO_0008693 CLO; CLO_0008770 EFO; EFO_0002315 CLDB; cl4119 CLDB; cl4120 CLDB; cl4121 CLDB; cl4122 CLDB; cl4123 CLDB; cl4124 CLDB; cl4125 CLDB; cl4126 CLDB; cl4127 AddexBio; C0035001/4950 ArrayExpress; E-MTAB-2770 ArrayExpress; E-MTAB-3610 ATCC; CCL-136 ATCC; CRL-7713 ATCC; CRL-7731 ATCC; HTB-97 BCRC; 60113 BCRJ; 0260 BioSample; SAMN01821591 BioSample; SAMN01821716 BioSample; SAMN03472710 BioSample; SAMN10988441 CCLE; RD_SOFT_TISSUE CCRID; 3111C0001CCC000293 CCRID; 3111C0002000000079 CCRID; 3131C0001000700045 CCTCC; GDC0295 Cell_Model_Passport; SIDM00847 ChEMBL-Cells; CHEMBL3307547 ChEMBL-Targets; CHEMBL614144 CLS; 300401/p527_RD Cosmic; 724833 Cosmic; 801358 Cosmic; 801760 Cosmic; 802045 Cosmic; 909264 Cosmic; 1037298 Cosmic; 1048111 Cosmic; 1097753 Cosmic; 1309330 Cosmic; 1509195 Cosmic; 1620036 Cosmic; 1718099 Cosmic; 2296987 Cosmic; 2301590 Cosmic; 2355912 Cosmic-CLP; 909264 DepMap; ACH-000169 ECACC; 85111502 GDSC; 909264 GEO; GSM185149 GEO; GSM186446 GEO; GSM219726 GEO; GSM887528 GEO; GSM888610 GEO; GSM1670368 GEO; GSM1676309 GEO; GSM1701643 IARC_TP53; 767 IGRhCellID; RD IZSLER; BS TCL 57 JCRB; JCRB9072 KCLB; 10136 LiGeA; CCLE_882 LINCS_LDP; LCL-1411 Lonza; 1536 PRIDE; PXD000589 TOKU-E; 2986 Wikidata; Q54949532 DT Created: 04-04-12; Last updated: 05-07-19; Version: 29


DT Created: 04-04-12; Last updated: 05-07-19; Version: 29

Originate from Same Individual

DT Created: 04-04-12; Last updated: 05-07-19; Version: 29

KREMEN1 Is a Host Entry Receptor for a Major Group of Enteroviruses.

  • Staring J
  • Cell Host Microbe
  • 2018 May 9

Literature context:


Human type A Enteroviruses (EV-As) cause diseases ranging from hand-foot-and-mouth disease to poliomyelitis-like disease. Although cellular receptors are identified for some EV-As, they remain elusive for the majority of EV-As. We identify the cell surface molecule KREMEN1 as an entry receptor for coxsackievirus A10 (CV-A10). Whereas loss of KREMEN1 renders cells resistant to CV-A10 infection, KREMEN1 overexpression enhances CV-A10 binding to the cell surface and increases susceptibility to infection, indicating that KREMEN1 is a rate-limiting factor for CV-A10 infection. Furthermore, the extracellular domain of KREMEN1 binds CV-A10 and functions as a neutralizing agent during infection. Kremen-deficient mice are resistant to CV-A10-induced lethal paralysis, emphasizing the relevance of Kremen for infection in vivo. KREMEN1 is also essential for infection by a phylogenetic and pathogenic related group of EV-As. Collectively these findings highlight the importance of KREMEN1 for these emerging pathogens and its potential as an antiviral therapeutic target.

Funding information:
  • NIGMS NIH HHS - GM083863(United States)

LKB1, Salt-Inducible Kinases, and MEF2C Are Linked Dependencies in Acute Myeloid Leukemia.

  • Tarumoto Y
  • Mol. Cell
  • 2018 Mar 15

Literature context:


The lineage-specific transcription factor (TF) MEF2C is often deregulated in leukemia. However, strategies to target this TF have yet to be identified. Here, we used a domain-focused CRISPR screen to reveal an essential role for LKB1 and its Salt-Inducible Kinase effectors (SIK3, in a partially redundant manner with SIK2) to maintain MEF2C function in acute myeloid leukemia (AML). A key phosphorylation substrate of SIK3 in this context is HDAC4, a repressive cofactor of MEF2C. Consequently, targeting of LKB1 or SIK3 diminishes histone acetylation at MEF2C-bound enhancers and deprives leukemia cells of the output of this essential TF. We also found that MEF2C-dependent leukemias are sensitive to on-target chemical inhibition of SIK activity. This study reveals a chemical strategy to block MEF2C function in AML, highlighting how an oncogenic TF can be disabled by targeting of upstream kinases.

Funding information:
  • NCI NIH HHS - P01 CA013106()
  • NCI NIH HHS - R01 CA174793()
  • NIDDK NIH HHS - DK64540(United States)

CpG and UpA dinucleotides in both coding and non-coding regions of echovirus 7 inhibit replication initiation post-entry.

  • Fros JJ
  • Elife
  • 2017 Sep 29

Literature context:


Most vertebrate and plant RNA and small DNA viruses suppress genomic CpG and UpA dinucleotide frequencies, apparently mimicking host mRNA composition. Artificially increasing CpG/UpA dinucleotides attenuates viruses through an entirely unknown mechanism. Using the echovirus 7 (E7) model in several cell types, we show that the restriction in E7 replication in mutants with increased CpG/UpA dinucleotides occurred immediately after viral entry, with incoming virions failing to form replication complexes. Sequences of CpG/UpA-high virus stocks showed no evidence of increased mutational errors that would render them replication defective, these viral RNAs were not differentially sequestered in cytoplasmic stress granules nor did they induce a systemic antiviral state. Importantly, restriction was not mediated through effects on translation efficiency since replicons with high CpG/UpA sequences inserted into a non-coding region were similarly replication defective. Host-cells thus possess intrinsic defence pathways that prevent replication of viruses with increased CpG/UpA frequencies independently of codon usage.

IGF2 mRNA binding protein-2 is a tumor promoter that drives cancer proliferation through its client mRNAs IGF2 and HMGA1.

  • Dai N
  • Elife
  • 2017 Jul 28

Literature context:


The gene encoding the Insulin-like Growth Factor 2 mRNA binding protein 2/IMP2 is amplified and overexpressed in many human cancers, accompanied by a poorer prognosis. Mice lacking IMP2 exhibit a longer lifespan and a reduced tumor burden at old age. Herein we show in a diverse array of human cancer cells that IMP2 overexpression stimulates and IMP2 elimination diminishes proliferation by 50-80%. In addition to its known ability to promote the abundance of Insulin-like Growth Factor 2/IGF2, we find that IMP2 strongly promotes IGF action, by binding and stabilizing the mRNA encoding the DNA binding protein HMGA1, a known oncogene. HMGA1 suppresses the abundance of IGF binding protein 2/IGFBP2 and Grb14, inhibitors of IGF action. IMP2 stabilization of HMGA1 mRNA plus IMP2 stimulated IGF2 production synergistically drive cancer cell proliferation and account for IMP2's tumor promoting action. IMP2's ability to promote proliferation and IGF action requires IMP2 phosphorylation by mTOR.

Funding information:
  • NHLBI NIH HHS - 01HL118386(United States)
  • NIDDK NIH HHS - P30 DK040561()
  • NIDDK NIH HHS - P30 DK043351()
  • NIDDK NIH HHS - P30 DK057521()
  • NIDDK NIH HHS - R37 DK017776()

Human Virus-Derived Small RNAs Can Confer Antiviral Immunity in Mammals.

  • Qiu Y
  • Immunity
  • 2017 Jun 20

Literature context:


RNA interference (RNAi) functions as a potent antiviral immunity in plants and invertebrates; however, whether RNAi plays antiviral roles in mammals remains unclear. Here, using human enterovirus 71 (HEV71) as a model, we showed HEV71 3A protein as an authentic viral suppressor of RNAi during viral infection. When the 3A-mediated RNAi suppression was impaired, the mutant HEV71 readily triggered the production of abundant HEV71-derived small RNAs with canonical siRNA properties in cells and mice. These virus-derived siRNAs were produced from viral dsRNA replicative intermediates in a Dicer-dependent manner and loaded into AGO, and they were fully active in degrading cognate viral RNAs. Recombinant HEV71 deficient in 3A-mediated RNAi suppression was significantly restricted in human somatic cells and mice, whereas Dicer deficiency rescued HEV71 infection independently of type I interferon response. Thus, RNAi can function as an antiviral immunity, which is induced and suppressed by a human virus, in mammals.

Funding information:
  • NICHD NIH HHS - R01 HD053855(United States)