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CUTL1

April 18, 2024

Cux1 (CUTL1, CDP, CDP/Cux) is a homeodomain protein that in humans is encoded by the CUX1 gene.[3][4][5][6]

CUX1
Identifiers
AliasesCUX1, CASP, CDP, CDP/Cut, CDP1, COY1, CUTL1, CUX, Clox, Cux/CDP, GOLIM6, Nbla10317, p100, p110, p200, p75, cut like homeobox 1, GDDI
External IDsOMIM: 116896 HomoloGene: 22551 GeneCards: CUX1
Orthologs
SpeciesHumanMouse
Entrez

1523

n/a

Ensembl

ENSG00000257923

n/a

UniProt

P39880
Q13948

n/a

RefSeq (mRNA)

n/a

RefSeq (protein)

n/a

Location (UCSC)Chr 7: 101.82 – 102.28 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

Function edit

The protein encoded by this gene is a member of the homeodomain family of DNA binding proteins. It regulates gene expression, morphogenesis, and differentiation and it also plays a role in cell cycle progression, particularly at S-phase. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined, and the p200 isoform of Cux1 is processed proteolytically to smaller active isoforms, such as p110.[6] Cux1 DNA binding is stimulated by activation of the PAR2/F2RL1 cell-surface G-protein-coupled receptor in fibroblasts and breast-cancer epithelial cells to regulate Matrix metalloproteinase 10, Interleukin1-alpha, and Cyclo-oxygenase 2 (COX2) genes.[7]

Role in tumor growth edit

Genetic data from over 7,600 cancer patients shows that over 1% has the deactivated CUX1 which links to progression of tumor growth. Researchers from the Wellcome Trust Sanger Institute reported that the mutation of CUX1 reduces the inhibitory effects of a biological inhibitor, PIK3IP1 (phosphoinositide-3-kinase interacting protein 1), resulted in higher activity of the growth promoting enzyme, phosphoinositide 3-kinase (PI3K) which leads to tumor progression. Although CUX1 is mutated at a lower rate compared to other known gene mutations that cause cancer, this deactivated gene is found across many cancer types in this study to be the underlying cause of the disease.[8][9]

CASP edit

 
Model of tethering involving CASP.[10]

The CUX1 gene Alternatively Spliced Product was first reported in 1997.[11][a] The CUX1 gene has up to 33 exons. CASP mRNA includes exons 1 through 14 and 25 through 33.[13] The human CASP protein is predicted to contain 678 amino acids, of which 400 are shared with CUTL1.[11] CASP protein is approximately 80 kD.[11] It lacks the DNA binding region of CUTL1,[11][14] but instead contains a trans-membrane domain that allows it to insert into lipid bilayers.[14] It has been localized to the Golgi apparatus.[14]

CASP has been reported to be part of a complex with Golgin 84 that tethers COPI vesicles and is important for retrograde transport in the Golgi and between the Golgi and endoplasmic reticulum.[15] The targeting of vesicles involves tethers and SNAREs.[15]

Interactions edit

 
The CUX1 network identified in the BioPlex searchable website.

Cux1 (CUTL1, CDP, CDP/Cux) has been shown to interact with:

These physical interactions are reported in BioPlex 2.0

Notes edit

  1. ^ This CASP is not the same as the scaffolding protein called CASP[12] for Cytohesin/ARNO ... Scaffolding Protein

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000257923 - Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ Scherer SW, Neufeld EJ, Lievens PM, Orkin SH, Kim J, Tsui LC (May 1993). "Regional localization of the CCAAT displacement protein gene (CUTL1) to 7q22 by analysis of somatic cell hybrids". Genomics. 15 (3): 695–6. doi:10.1006/geno.1993.1130. PMID 8468066.
  4. ^ Glöckner G, Scherer S, Schattevoy R, Boright A, Weber J, Tsui LC, Rosenthal A (December 1998). "Large-Scale Sequencing of Two Regions in Human Chromosome 7q22: Analysis of 650 kb of Genomic Sequence around the EPO and CUTL1 Loci Reveals 17 Genes". Genome Res. 8 (10): 1060–73. doi:10.1101/gr.8.10.1060. PMC 310788. PMID 9799793.
  5. ^ Oka T, Ungar D, Hughson FM, Krieger M (April 2004). "The COG and COPI Complexes Interact to Control the Abundance of GEARs, a Subset of Golgi Integral Membrane Proteins". Mol. Biol. Cell. 15 (5): 2423–35. doi:10.1091/mbc.E03-09-0699. PMC 404034. PMID 15004235.
  6. ^ a b "Entrez Gene: CUTL1 cut-like 1, CCAAT displacement protein (Drosophila)".
  7. ^ Wilson BJ, Harada R, LeDuy L, Hollenberg MD, Nepveu A (January 2009). "CUX1 transcription factor is a downstream effector of the proteinase-activated receptor 2 (PAR2)". J. Biol. Chem. 284 (1): 36–45. doi:10.1074/jbc.M803808200. PMID 18952606.
  8. ^ Press Release (8 December 2013). "Gene promotes one in a hundred of tumours". Wellcome Trust Sanger Institute. Retrieved 17 December 2013.
  9. ^ Wong CC, Martincorena I, Rust AG, et al. (2013). "Inactivating CUX1 mutations promote tumorigenesis". Nature Genetics. 46 (1): 33–8. doi:10.1038/ng.2846. PMC 3874239. PMID 24316979.
  10. ^ Sohda M, Misumi Y, Yamamoto A, Nakamura N, Ogata S, Sakisaka S, Hirose S, Ikehara Y, Oda K (2010). "Interaction of Golgin-84 with the COG complex mediates the intra-Golgi retrograde transport". Traffic. 11 (12): 1552–66. doi:10.1111/j.1600-0854.2010.01123.x. PMID 20874812. S2CID 20424336.
  11. ^ a b c d Lievens PM, Tufarelli C, Donady JJ, Stagg A, Neufeld EJ (1997). "CASP, a novel, highly conserved alternative-splicing product of the CDP/cut/cux gene, lacks cut-repeat and homeo DNA-binding domains, and interacts with full-length CDP in vitro". Gene. 197 (1–2): 73–81. doi:10.1016/s0378-1119(97)00243-6. PMID 9332351.
  12. ^ Mansour M, Lee SY, Pohajdak B (2002). "The N-terminal coiled coil domain of the cytohesin/ARNO family of guanine nucleotide exchange factors interacts with the scaffolding protein CASP". The Journal of Biological Chemistry. 277 (35): 32302–9. doi:10.1074/jbc.M202898200. PMID 12052827.
  13. ^ Ramdzan ZM, Nepveu A (2014). "CUX1, a haploinsufficient tumour suppressor gene overexpressed in advanced cancers". Nature Reviews Cancer. 14 (10): 673–82. doi:10.1038/nrc3805. PMID 25190083. S2CID 20468440.
  14. ^ a b c Gillingham AK, Pfeifer AC, Munro S (2002). "CASP, the alternatively spliced product of the gene encoding the CCAAT-displacement protein transcription factor, is a Golgi membrane protein related to giantin". Molecular Biology of the Cell. 13 (11): 3761–74. doi:10.1091/mbc.E02-06-0349. PMC 133590. PMID 12429822.
  15. ^ a b Malsam J, Satoh A, Pelletier L, Warren G (2005). "Golgin tethers define subpopulations of COPI vesicles". Science. 307 (5712): 1095–8. Bibcode:2005Sci...307.1095M. doi:10.1126/science.1108061. PMID 15718469. S2CID 12601850.
  16. ^ Li S, Aufiero B, Schiltz RL, Walsh MJ (June 2000). "Regulation of the homeodomain CCAAT displacement/cut protein function by histone acetyltransferases p300/CREB-binding protein (CBP)-associated factor and CBP". Proc. Natl. Acad. Sci. U.S.A. 97 (13): 7166–71. Bibcode:2000PNAS...97.7166L. doi:10.1073/pnas.130028697. PMC 16517. PMID 10852958.
  17. ^ Gupta S, Luong MX, Bleuming SA, Miele A, Luong M, Young D, Knudsen ES, Van Wijnen AJ, Stein JL, Stein GS (September 2003). "Tumor suppressor pRB functions as a co-repressor of the CCAAT displacement protein (CDP/cut) to regulate cell cycle controlled histone H4 transcription". J. Cell. Physiol. 196 (3): 541–56. doi:10.1002/jcp.10335. PMID 12891711. S2CID 2287673.
  18. ^ Liu J, Barnett A, Neufeld EJ, Dudley JP (July 1999). "Homeoproteins CDP and SATB1 interact: potential for tissue-specific regulation". Mol. Cell. Biol. 19 (7): 4918–26. doi:10.1128/mcb.19.7.4918. PMC 84297. PMID 10373541.

Further reading edit

  • Ottolenghi S, Mantovani R, Nicolis S, Ronchi A, Giglioni B (1990). "DNA sequences regulating human globin gene transcription in nondeletional hereditary persistence of fetal hemoglobin". Hemoglobin. 13 (6): 523–41. doi:10.3109/03630268908993104. PMID 2481658.
  • Nepveu A (2001). "Role of the multifunctional CDP/Cut/Cux homeodomain transcription factor in regulating differentiation, cell growth and development". Gene. 270 (1–2): 1–15. doi:10.1016/S0378-1119(01)00485-1. PMID 11403998.
  • Neufeld EJ, Skalnik DG, Lievens PM, Orkin SH (1993). "Human CCAAT displacement protein is homologous to the Drosophila homeoprotein, cut". Nat. Genet. 1 (1): 50–5. doi:10.1038/ng0492-50. PMID 1301999. S2CID 37107643.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Chernousov MA, Stahl RC, Carey DJ (1996). "Schwann cells secrete a novel collagen-like adhesive protein that binds N-syndecan". J. Biol. Chem. 271 (23): 13844–53. doi:10.1074/jbc.271.23.13844. PMID 8662884.
  • Lievens PM, Tufarelli C, Donady JJ, Stagg A, Neufeld EJ (1997). "CASP, a novel, highly conserved alternative-splicing product of the CDP/cut/cux gene, lacks cut-repeat and homeo DNA-binding domains, and interacts with full-length CDP in vitro". Gene. 197 (1–2): 73–81. doi:10.1016/S0378-1119(97)00243-6. PMID 9332351.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Chattopadhyay S, Whitehurst CE, Chen J (1998). "A nuclear matrix attachment region upstream of the T cell receptor beta gene enhancer binds Cux/CDP and SATB1 and modulates enhancer-dependent reporter gene expression but not endogenous gene expression". J. Biol. Chem. 273 (45): 29838–46. doi:10.1074/jbc.273.45.29838. PMID 9792700.
  • Liu J, Barnett A, Neufeld EJ, Dudley JP (1999). "Homeoproteins CDP and SATB1 Interact: Potential for Tissue-Specific Regulation". Mol. Cell. Biol. 19 (7): 4918–26. doi:10.1128/mcb.19.7.4918. PMC 84297. PMID 10373541.
  • Rong Zeng W, Soucie E, Sung Moon N, Martin-Soudant N, Bérubé G, Leduy L, Nepveu A (2000). "Exon/intron structure and alternative transcripts of the CUTL1 gene". Gene. 241 (1): 75–85. doi:10.1016/S0378-1119(99)00465-5. PMID 10607901.
  • Martin-Soudant N, Drachman JG, Kaushansky K, Nepveu A (2000). "CDP/Cut DNA binding activity is down-modulated in granulocytes, macrophages and erythrocytes but remains elevated in differentiating megakaryocytes". Leukemia. 14 (5): 863–73. doi:10.1038/sj.leu.2401764. PMID 10803519. S2CID 19998783.
  • Li S, Aufiero B, Schiltz RL, Walsh MJ (2000). "Regulation of the homeodomain CCAAT displacement/cut protein function by histone acetyltransferases p300/CREB-binding protein (CBP)-associated factor and CBP". Proc. Natl. Acad. Sci. U.S.A. 97 (13): 7166–71. Bibcode:2000PNAS...97.7166L. doi:10.1073/pnas.130028697. PMC 16517. PMID 10852958.
  • Nirodi C, Hart J, Dhawan P, Moon NS, Nepveu A, Richmond A (2001). "The Role of CDP in the Negative Regulation of CXCL1 Gene Expression". J. Biol. Chem. 276 (28): 26122–31. doi:10.1074/jbc.M102872200. PMC 2665279. PMID 11371564.
  • Moon NS, Premdas P, Truscott M, Leduy L, Bérubé G, Nepveu A (2001). "S Phase-Specific Proteolytic Cleavage Is Required To Activate Stable DNA Binding by the CDP/Cut Homeodomain Protein". Mol. Cell. Biol. 21 (18): 6332–45. doi:10.1128/MCB.21.18.6332-6345.2001. PMC 87367. PMID 11509674.
  • Santaguida M, Ding Q, Bérubé G, Truscott M, Whyte P, Nepveu A (2002). "Phosphorylation of the CCAAT displacement protein (CDP)/Cux transcription factor by cyclin A-Cdk1 modulates its DNA binding activity in G(2)". J. Biol. Chem. 276 (49): 45780–90. doi:10.1074/jbc.M107978200. PMID 11584018.
  • Dintilhac A, Bernués J (2002). "HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences" (PDF). J. Biol. Chem. 277 (9): 7021–8. doi:10.1074/jbc.M108417200. PMID 11748221. S2CID 39560486.

External links edit

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

April 18, 2024
cutl1, cux1, homeodomain, protein, that, humans, encoded, cux1, gene, cux1identifiersaliasescux1, casp, cdp1, coy1, clox, golim6, nbla10317, p100, p110, p200, like, homeobox, gddiexternal, idsomim, 116896, homologene, 22551, genecards, cux1gene, location, huma. Cux1 CUTL1 CDP CDP Cux is a homeodomain protein that in humans is encoded by the CUX1 gene 3 4 5 6 CUX1IdentifiersAliasesCUX1 CASP CDP CDP Cut CDP1 COY1 CUTL1 CUX Clox Cux CDP GOLIM6 Nbla10317 p100 p110 p200 p75 cut like homeobox 1 GDDIExternal IDsOMIM 116896 HomoloGene 22551 GeneCards CUX1Gene location Human Chr Chromosome 7 human 1 Band7q22 1Start101 815 904 bp 1 End102 283 958 bp 1 RNA expression patternBgeeHumanMouse ortholog Top expressed insecondary oocytestromal cell of endometriumganglionic eminenceright coronary arterysural nervemyometriumsmooth muscle tissuegastric mucosavisceral pleuraascending aortan aMore reference expression dataBioGPSn aGene ontologyMolecular functionsequence specific DNA binding DNA binding protein tyrosine kinase activity RNA polymerase II transcription regulatory region sequence specific DNA binding protein macromolecule adaptor activity protein binding DNA binding transcription factor activity RNA polymerase II specificCellular componentcytosol Golgi apparatus nucleus nucleoplasm Golgi membrane integral component of membrane integral component of Golgi membrane membraneBiological processregulation of transcription by RNA polymerase II multicellular organism development retrograde transport vesicle recycling within Golgi positive regulation of dendrite morphogenesis regulation of transcription DNA templated negative regulation of transcription by RNA polymerase II transcription DNA templated peptidyl tyrosine phosphorylation Golgi vesicle transport intra Golgi vesicle mediated transportSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez1523n aEnsemblENSG00000257923n aUniProtP39880Q13948n aRefSeq mRNA NM 001202543NM 001202544NM 001202545NM 001202546NM 001913NM 181500NM 181552n aRefSeq protein NP 001189472NP 001189473NP 001189474NP 001189475NP 001904NP 852477NP 853530NP 001189473 1NP 001189474 1NP 001189475 1NP 001904 2NP 852477 1n aLocation UCSC Chr 7 101 82 102 28 Mbn aPubMed search 2 n aWikidataView Edit Human Contents 1 Function 2 Role in tumor growth 3 CASP 4 Interactions 5 Notes 6 References 7 Further reading 8 External linksFunction editThe protein encoded by this gene is a member of the homeodomain family of DNA binding proteins It regulates gene expression morphogenesis and differentiation and it also plays a role in cell cycle progression particularly at S phase Several alternatively spliced transcript variants of this gene have been described but the full length nature of some of these variants has not been determined and the p200 isoform of Cux1 is processed proteolytically to smaller active isoforms such as p110 6 Cux1 DNA binding is stimulated by activation of the PAR2 F2RL1 cell surface G protein coupled receptor in fibroblasts and breast cancer epithelial cells to regulate Matrix metalloproteinase 10 Interleukin1 alpha and Cyclo oxygenase 2 COX2 genes 7 Role in tumor growth editGenetic data from over 7 600 cancer patients shows that over 1 has the deactivated CUX1 which links to progression of tumor growth Researchers from the Wellcome Trust Sanger Institute reported that the mutation of CUX1 reduces the inhibitory effects of a biological inhibitor PIK3IP1 phosphoinositide 3 kinase interacting protein 1 resulted in higher activity of the growth promoting enzyme phosphoinositide 3 kinase PI3K which leads to tumor progression Although CUX1 is mutated at a lower rate compared to other known gene mutations that cause cancer this deactivated gene is found across many cancer types in this study to be the underlying cause of the disease 8 9 CASP edit nbsp Model of tethering involving CASP 10 The CUX1 gene Alternatively Spliced Product was first reported in 1997 11 a The CUX1 gene has up to 33 exons CASP mRNA includes exons 1 through 14 and 25 through 33 13 The human CASP protein is predicted to contain 678 amino acids of which 400 are shared with CUTL1 11 CASP protein is approximately 80 kD 11 It lacks the DNA binding region of CUTL1 11 14 but instead contains a trans membrane domain that allows it to insert into lipid bilayers 14 It has been localized to the Golgi apparatus 14 CASP has been reported to be part of a complex with Golgin 84 that tethers COPI vesicles and is important for retrograde transport in the Golgi and between the Golgi and endoplasmic reticulum 15 The targeting of vesicles involves tethers and SNAREs 15 Interactions edit nbsp The CUX1 network identified in the BioPlex searchable website Cux1 CUTL1 CDP CDP Cux has been shown to interact with CREB binding protein 16 Retinoblastoma protein 17 and SATB1 18 These physical interactions are reported in BioPlex 2 0 MAGEA10 EXT2 RAB30 HLA DQA1 STX6 WDR83 SLC39A4 LAMP1 POTEB SLC39A12Notes edit This CASP is not the same as the scaffolding protein called CASP 12 for Cytohesin ARNO Scaffolding ProteinReferences edit a b c GRCh38 Ensembl release 89 ENSG00000257923 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Scherer SW Neufeld EJ Lievens PM Orkin SH Kim J Tsui LC May 1993 Regional localization of the CCAAT displacement protein gene CUTL1 to 7q22 by analysis of somatic cell hybrids Genomics 15 3 695 6 doi 10 1006 geno 1993 1130 PMID 8468066 Glockner G Scherer S Schattevoy R Boright A Weber J Tsui LC Rosenthal A December 1998 Large Scale Sequencing of Two Regions in Human Chromosome 7q22 Analysis of 650 kb of Genomic Sequence around the EPO and CUTL1 Loci Reveals 17 Genes Genome Res 8 10 1060 73 doi 10 1101 gr 8 10 1060 PMC 310788 PMID 9799793 Oka T Ungar D Hughson FM Krieger M April 2004 The COG and COPI Complexes Interact to Control the Abundance of GEARs a Subset of Golgi Integral Membrane Proteins Mol Biol Cell 15 5 2423 35 doi 10 1091 mbc E03 09 0699 PMC 404034 PMID 15004235 a b Entrez Gene CUTL1 cut like 1 CCAAT displacement protein Drosophila Wilson BJ Harada R LeDuy L Hollenberg MD Nepveu A January 2009 CUX1 transcription factor is a downstream effector of the proteinase activated receptor 2 PAR2 J Biol Chem 284 1 36 45 doi 10 1074 jbc M803808200 PMID 18952606 Press Release 8 December 2013 Gene promotes one in a hundred of tumours Wellcome Trust Sanger Institute Retrieved 17 December 2013 Wong CC Martincorena I Rust AG et al 2013 Inactivating CUX1 mutations promote tumorigenesis Nature Genetics 46 1 33 8 doi 10 1038 ng 2846 PMC 3874239 PMID 24316979 Sohda M Misumi Y Yamamoto A Nakamura N Ogata S Sakisaka S Hirose S Ikehara Y Oda K 2010 Interaction of Golgin 84 with the COG complex mediates the intra Golgi retrograde transport Traffic 11 12 1552 66 doi 10 1111 j 1600 0854 2010 01123 x PMID 20874812 S2CID 20424336 a b c d Lievens PM Tufarelli C Donady JJ Stagg A Neufeld EJ 1997 CASP a novel highly conserved alternative splicing product of the CDP cut cux gene lacks cut repeat and homeo DNA binding domains and interacts with full length CDP in vitro Gene 197 1 2 73 81 doi 10 1016 s0378 1119 97 00243 6 PMID 9332351 Mansour M Lee SY Pohajdak B 2002 The N terminal coiled coil domain of the cytohesin ARNO family of guanine nucleotide exchange factors interacts with the scaffolding protein CASP The Journal of Biological Chemistry 277 35 32302 9 doi 10 1074 jbc M202898200 PMID 12052827 Ramdzan ZM Nepveu A 2014 CUX1 a haploinsufficient tumour suppressor gene overexpressed in advanced cancers Nature Reviews Cancer 14 10 673 82 doi 10 1038 nrc3805 PMID 25190083 S2CID 20468440 a b c Gillingham AK Pfeifer AC Munro S 2002 CASP the alternatively spliced product of the gene encoding the CCAAT displacement protein transcription factor is a Golgi membrane protein related to giantin Molecular Biology of the Cell 13 11 3761 74 doi 10 1091 mbc E02 06 0349 PMC 133590 PMID 12429822 a b Malsam J Satoh A Pelletier L Warren G 2005 Golgin tethers define subpopulations of COPI vesicles Science 307 5712 1095 8 Bibcode 2005Sci 307 1095M doi 10 1126 science 1108061 PMID 15718469 S2CID 12601850 Li S Aufiero B Schiltz RL Walsh MJ June 2000 Regulation of the homeodomain CCAAT displacement cut protein function by histone acetyltransferases p300 CREB binding protein CBP associated factor and CBP Proc Natl Acad Sci U S A 97 13 7166 71 Bibcode 2000PNAS 97 7166L doi 10 1073 pnas 130028697 PMC 16517 PMID 10852958 Gupta S Luong MX Bleuming SA Miele A Luong M Young D Knudsen ES Van Wijnen AJ Stein JL Stein GS September 2003 Tumor suppressor pRB functions as a co repressor of the CCAAT displacement protein CDP cut to regulate cell cycle controlled histone H4 transcription J Cell Physiol 196 3 541 56 doi 10 1002 jcp 10335 PMID 12891711 S2CID 2287673 Liu J Barnett A Neufeld EJ Dudley JP July 1999 Homeoproteins CDP and SATB1 interact potential for tissue specific regulation Mol Cell Biol 19 7 4918 26 doi 10 1128 mcb 19 7 4918 PMC 84297 PMID 10373541 Further reading editOttolenghi S Mantovani R Nicolis S Ronchi A Giglioni B 1990 DNA sequences regulating human globin gene transcription in nondeletional hereditary persistence of fetal hemoglobin Hemoglobin 13 6 523 41 doi 10 3109 03630268908993104 PMID 2481658 Nepveu A 2001 Role of the multifunctional CDP Cut Cux homeodomain transcription factor in regulating differentiation cell growth and development Gene 270 1 2 1 15 doi 10 1016 S0378 1119 01 00485 1 PMID 11403998 Neufeld EJ Skalnik DG Lievens PM Orkin SH 1993 Human CCAAT displacement protein is homologous to the Drosophila homeoprotein cut Nat Genet 1 1 50 5 doi 10 1038 ng0492 50 PMID 1301999 S2CID 37107643 Maruyama K Sugano S 1994 Oligo capping a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides Gene 138 1 2 171 4 doi 10 1016 0378 1119 94 90802 8 PMID 8125298 Chernousov MA Stahl RC Carey DJ 1996 Schwann cells secrete a novel collagen like adhesive protein that binds N syndecan J Biol Chem 271 23 13844 53 doi 10 1074 jbc 271 23 13844 PMID 8662884 Lievens PM Tufarelli C Donady JJ Stagg A Neufeld EJ 1997 CASP a novel highly conserved alternative splicing product of the CDP cut cux gene lacks cut repeat and homeo DNA binding domains and interacts with full length CDP in vitro Gene 197 1 2 73 81 doi 10 1016 S0378 1119 97 00243 6 PMID 9332351 Suzuki Y Yoshitomo Nakagawa K Maruyama K Suyama A Sugano S 1997 Construction and characterization of a full length enriched and a 5 end enriched cDNA library Gene 200 1 2 149 56 doi 10 1016 S0378 1119 97 00411 3 PMID 9373149 Chattopadhyay S Whitehurst CE Chen J 1998 A nuclear matrix attachment region upstream of the T cell receptor beta gene enhancer binds Cux CDP and SATB1 and modulates enhancer dependent reporter gene expression but not endogenous gene expression J Biol Chem 273 45 29838 46 doi 10 1074 jbc 273 45 29838 PMID 9792700 Liu J Barnett A Neufeld EJ Dudley JP 1999 Homeoproteins CDP and SATB1 Interact Potential for Tissue Specific Regulation Mol Cell Biol 19 7 4918 26 doi 10 1128 mcb 19 7 4918 PMC 84297 PMID 10373541 Rong Zeng W Soucie E Sung Moon N Martin Soudant N Berube G Leduy L Nepveu A 2000 Exon intron structure and alternative transcripts of the CUTL1 gene Gene 241 1 75 85 doi 10 1016 S0378 1119 99 00465 5 PMID 10607901 Martin Soudant N Drachman JG Kaushansky K Nepveu A 2000 CDP Cut DNA binding activity is down modulated in granulocytes macrophages and erythrocytes but remains elevated in differentiating megakaryocytes Leukemia 14 5 863 73 doi 10 1038 sj leu 2401764 PMID 10803519 S2CID 19998783 Li S Aufiero B Schiltz RL Walsh MJ 2000 Regulation of the homeodomain CCAAT displacement cut protein function by histone acetyltransferases p300 CREB binding protein CBP associated factor and CBP Proc Natl Acad Sci U S A 97 13 7166 71 Bibcode 2000PNAS 97 7166L doi 10 1073 pnas 130028697 PMC 16517 PMID 10852958 Nirodi C Hart J Dhawan P Moon NS Nepveu A Richmond A 2001 The Role of CDP in the Negative Regulation of CXCL1 Gene Expression J Biol Chem 276 28 26122 31 doi 10 1074 jbc M102872200 PMC 2665279 PMID 11371564 Moon NS Premdas P Truscott M Leduy L Berube G Nepveu A 2001 S Phase Specific Proteolytic Cleavage Is Required To Activate Stable DNA Binding by the CDP Cut Homeodomain Protein Mol Cell Biol 21 18 6332 45 doi 10 1128 MCB 21 18 6332 6345 2001 PMC 87367 PMID 11509674 Santaguida M Ding Q Berube G Truscott M Whyte P Nepveu A 2002 Phosphorylation of the CCAAT displacement protein CDP Cux transcription factor by cyclin A Cdk1 modulates its DNA binding activity in G 2 J Biol Chem 276 49 45780 90 doi 10 1074 jbc M107978200 PMID 11584018 Dintilhac A Bernues J 2002 HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences PDF J Biol Chem 277 9 7021 8 doi 10 1074 jbc M108417200 PMID 11748221 S2CID 39560486 External links editCUTL1 protein human at the U S National Library of Medicine Medical Subject Headings MeSH Human CUX1 genome location and CUX1 gene details page in the UCSC Genome Browser This article incorporates text from the United States National Library of Medicine which is in the public domain Retrieved from https en wikipedia org w index php title CUTL1 amp oldid 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