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MAX interactor 1, dimerization protein
Symbols MXI1 ; MAD2; MXD2; MXI; bHLHc11
External IDs OMIM600020 MGI97245 HomoloGene4351 GeneCards: MXI1 Gene
RNA expression pattern
PBB GE MXI1 202364 at tn.png
More reference expression data
Species Human Mouse
Entrez 4601 17859
Ensembl ENSG00000119950 ENSMUSG00000025025
UniProt P50539 P50540
RefSeq (mRNA) NM_001008541 NM_001008542
RefSeq (protein) NP_001008541 NP_001008542
Location (UCSC) Chr 10:
111.97 – 112.05 Mb
Chr 19:
53.31 – 53.38 Mb
PubMed search [1] [2]

MAX-interacting protein 1 is a protein that in humans is encoded by the MXI1 gene.[1][2]

Expression of the c-myc gene, which produces an oncogenic transcription factor, is tightly regulated in normal cells but is frequently deregulated in human cancers. The protein encoded by this gene is a transcriptional repressor thought to negatively regulate MYC function, and is therefore a potential tumor suppressor. This protein inhibits the transcriptional activity of MYC by competing for MAX, another basic helix-loop-helix protein that binds to MYC and is required for its function. Defects in this gene are frequently found in patients with prostate tumors. Three alternatively spliced transcripts encoding different isoforms have been described. Additional alternatively spliced transcripts may exist but the products of these transcripts have not been verified experimentally.[2]


MXI1 has been shown to interact with SMC3[3] and MAX.[3][4][5][6][7]


  1. ^ Wechsler DS, Hawkins AL, Li X, Jabs EW, Griffin CA, Dang CV (Nov 1994). "Localization of the human Mxi1 transcription factor gene (MXI1) to chromosome 10q24-q25". Genomics 21 (3): 669–72. doi:10.1006/geno.1994.1336. PMID 7959753. 
  2. ^ a b "Entrez Gene: MXI1 MAX interactor 1". 
  3. ^ a b Gupta, K; Anand G; Yin X; Grove L; Prochownik E V (Mar 1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene (ENGLAND) 16 (9): 1149–59. doi:10.1038/sj.onc.1201634. ISSN 0950-9232. PMID 9528857. 
  4. ^ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
  5. ^ Billin, A N; Eilers A L; Queva C; Ayer D E (Dec 1999). "Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors". J. Biol. Chem. (United States) 274 (51): 36344–50. doi:10.1074/jbc.274.51.36344. ISSN 0021-9258. PMID 10593926. 
  6. ^ Meroni, G; Reymond A, Alcalay M, Borsani G, Tanigami A, Tonlorenzi R, Lo Nigro C, Messali S, Zollo M, Ledbetter D H, Brent R, Ballabio A, Carrozzo R (May 1997). "Rox, a novel bHLHZip protein expressed in quiescent cells that heterodimerizes with Max, binds a non-canonical E box and acts as a transcriptional repressor". EMBO J. (ENGLAND) 16 (10): 2892–906. doi:10.1093/emboj/16.10.2892. ISSN 0261-4189. PMC 1169897. PMID 9184233. 
  7. ^ FitzGerald, M J; Arsura M; Bellas R E; Yang W; Wu M; Chin L; Mann K K; DePinho R A; Sonenshein G E (Apr 1999). "Differential effects of the widely expressed dMax splice variant of Max on E-box vs initiator element-mediated regulation by c-Myc". Oncogene (ENGLAND) 18 (15): 2489–98. doi:10.1038/sj.onc.1202611. ISSN 0950-9232. PMID 10229200. 

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