MXI1

From Wikipedia, the free encyclopedia

MAX interactor 1

Identifiers

MXI1; MAD2; MGC43220; MXD2; MXI

External IDs

OMIM: 600020 MGI: 97245 HomoloGene: 4351

Gene ontology
Molecular Function:	• DNA binding • transcription corepressor activity • transcription regulator activity
Cellular Component:	• nucleus
Biological Process:	• regulation of transcription, DNA-dependent • negative regulation of cell proliferation • cytoplasmic sequestering of transcription factor • regulation of transcription

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001008541 (mRNA)
NP_001008541 (protein)

NM_001008542 (mRNA)
NP_001008542 (protein)

Location

Chr 10: 111.96 - 112.04 Mb

Chr 19: 53.36 - 53.43 Mb

Pubmed search

[1]

[2]

MAX interactor 1, also known as MXI1, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: MXI1 MAX interactor 1.

[edit] Further reading

Eagle LR, Yin X, Brothman AR, et al. (1995). "Mutation of the MXI1 gene in prostate cancer.". Nat. Genet. 9 (3): 249–55. doi:10.1038/ng0395-249. PMID 7773287.
Albarosa R, DiDonato S, Finocchiaro G (1995). "Redefinition of the coding sequence of the MXI1 gene and identification of a polymorphic repeat in the 3' non-coding region that allows the detection of loss of heterozygosity of chromosome 10q25 in glioblastomas.". Hum. Genet. 95 (6): 709–11. PMID 7789959.
Schreiber-Agus N, Chin L, Chen K, et al. (1995). "An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3.". Cell 80 (5): 777–86. PMID 7889571.
Zervos AS, Gyuris J, Brent R (1994). "Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites.". Cell 79 (2): following 388. PMID 7954804.
Wechsler DS, Hawkins AL, Li X, et al. (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.
Edelhoff S, Ayer DE, Zervos AS, et al. (1994). "Mapping of two genes encoding members of a distinct subfamily of MAX interacting proteins: MAD to human chromosome 2 and mouse chromosome 6, and MXI1 to human chromosome 10 and mouse chromosome 19.". Oncogene 9 (2): 665–8. PMID 8290278.
Zervos AS, Gyuris J, Brent R (1993). "Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites.". Cell 72 (2): 223–32. PMID 8425219.
Wechsler DS, Shelly CA, Dang CV (1997). "Genomic organization of human MXI1, a putative tumor suppressor gene.". Genomics 32 (3): 466–70. doi:10.1006/geno.1996.0144. PMID 8838813.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
Shimizu E, Shirasawa H, Kodama K, et al. (1997). "Expression, regulation and polymorphism of the mxi1 genes.". Gene 176 (1-2): 45–8. PMID 8918230.
Gupta K, Anand G, Yin X, et al. (1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc.". Oncogene 16 (9): 1149–59. doi:10.1038/sj.onc.1201634. PMID 9528857.
Schreiber-Agus N, Meng Y, Hoang T, et al. (1998). "Role of Mxi1 in ageing organ systems and the regulation of normal and neoplastic growth.". Nature 393 (6684): 483–7. doi:10.1038/31008. PMID 9624006.
Prochownik EV, Eagle Grove L, Deubler D, et al. (1999). "Commonly occurring loss and mutation of the MXI1 gene in prostate cancer.". Genes Chromosomes Cancer 22 (4): 295–304. PMID 9669667.
Li XJ, Wang DY, Zhu Y, et al. (1999). "Mxi1 mutations in human neurofibrosarcomas.". Jpn. J. Cancer Res. 90 (7): 740–6. PMID 10470286.
Benson LQ, Coon MR, Krueger LM, et al. (1999). "Expression of MXI1, a Myc antagonist, is regulated by Sp1 and AP2.". J. Biol. Chem. 274 (40): 28794–802. PMID 10497252.
Taj MM, Tawil RJ, Engstrom LD, et al. (2001). "Mxi1, a Myc antagonist, suppresses proliferation of DU145 human prostate cells.". Prostate 47 (3): 194–204. doi:10.1002/pros.1063. PMID 11351349.
Yin X, Landay MF, Han W, et al. (2001). "Dynamic in vivo interactions among Myc network members.". Oncogene 20 (34): 4650–64. doi:10.1038/sj.onc.1204606. PMID 11498788.
Manni I, Tunici P, Cirenei N, et al. (2002). "Mxi1 inhibits the proliferation of U87 glioma cells through down-regulation of cyclin B1 gene expression.". Br. J. Cancer 86 (3): 477–84. doi:10.1038/sj.bjc.6600065. PMID 11875718.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Ariyanayagam-Baksh SM, Baksh FK, Swalsky PA, Finkelstein SD (2004). "Loss of heterozygosity in the MXI1 gene is a frequent occurrence in melanoma.". Mod. Pathol. 16 (10): 992–5. doi:10.1097/01.MP.0000087421.44975.1C. PMID 14559981.

[edit] External links

MeSH MXI1+protein,+human

This article on a gene on chromosome 10 is a stub. You can help Wikipedia by expanding it.

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

v • d • e

Transcription factors and intracellular receptors

(1) Basic domains

(1.1) Basic leucine zipper (bZIP)	Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) • AP-1 (c-Fos, FOSB, FOSL1, FOSL2, c-Jun, JUNB, JUND) • BACH (1, 2) • BATF • BLZF1 • C/EBP (α, β, γ, δ, ε, ζ) • CREB (1, 3, L1) • CREM • DBP • DDIT3 • GABPA • HLF • MAF (B, F, G, K) • NFE (2, L1, L2) • NRL • NRF1 • XBP1

(1.2) Basic helix-loop-helix (bHLH)	ATOH1 • AhR • AHRR • ARNT • ASCL1 • BHLHB2 • BMAL (ARNTL, ARNTL2) • CLOCK • EPAS1 • HAND (1, 2) • HES (5, 6) • HEY (1, 2, L) • HES1 • HIF (1A, 3A) • ID (1, 2, 3, 4) • LYL1 • MXD4 • MYCL1 • MYCN • Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) • Neurogenins • NeuroD (1, 2) • NPAS (1, 2, 3) • OLIG (1, 2) • Scleraxis • TAL1 • Twist • USF1

(1.3) bHLH-ZIP	MAX • MITF • MNT • MLX • MXI1 • Myc • SREBP (1, 2)

(1.6) Basic helix-span-helix (bHSH)	AP-2

(2) Zinc finger
DNA-binding domains

(2.1) Nuclear receptor (Cys₄)	subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) • subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) • subfamily 3 (Steroid hormone (Estrogen (α, β), Estrogen related (α, β, γ), Androgen, Glucocorticoid, Mineralocorticoid, Progesterone)) • subfamily 4 NUR (NGFIB, NOR1, NURR1) • subfamily 5 (LRH-1, SF1) • subfamily 6 (GCNF) • subfamily 0 (DAX1, SHP)

(2.2) Other Cys₄	GATA (1, 2, 3, 4, 5, 6) • MTA (1, 2, 3)

(2.3) Cys₂His₂	ATBF1 • BCL(6, 11A, 11B) • CTCF • E4F1 • EGR (2, 3) • ERV3 • General transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF: 1, 2, TFIIH: 1, 2, 4, 2I, 3A, 3C1, 3C2) • GFI1 • GLI-Krüppel family (1, 2, 3, YY1) • HIC (1, 2) • HIVEP (1, 2, 3) • IKZF (1, 2, 3) • ILF (2, 3) • KLF (2, 4, 5, 6, 9, 10, 11, 12, 13) • MTF1 • MYT1 • OSR1 • Sp1 • zinc finger ((3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 318, 330, 346, 350, 365, 366, 384, 451, 452, 471, 593, 638, 649, 655) • Zbtb7 (7A) • ZBT (16, 17, 33)

(2.4) Cys₆	HIVEP1

(2.5) Alternating composition	AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B

(3) Helix-turn-helix
domains

(3.1) Homeo domain	ARX • CDX (1, 2) • CRX • CUTL1 • DLX (3, 4, 5) • EMX2 • EN (1, 2) • FHL (1, 2, 3) • HESX1 • HHEX • HLX • Homeobox (A1, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) • HOPX • MEIS (1, 2) • MEOX2 • MNX1 • MSX (1, 2) • NANOG • NKX (2-1, 2-5, 3-1) • PHF (3, 6, 10, 17) • POU domain (PIT-1, BRN-3: 1, 2, Octamer transcription factor: 1, 2, 3/4, 6, 7) • OTX (1, 2) • PDX1

(3.2) Paired box	PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)

(3.3) Fork head / winged helix	E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)

(3.4) Heat Shock Factors	HSF (1, 2, 4)

(3.5) Tryptophan clusters	ELF (4, 5) • EGF • ELK (1, 3, 4) • ERF • ERG • ETS (1, 2) • ETV (1, 4, 5, 6) • FLI1 • Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) • MYB • MYBL2

(3.6) TEA domain	transcriptional enhancer factor 1, 2

(4) β-Scaffold factors with
minor groove contacts

(4.1) Rel homology region	NF-κB (NFKB1, NFKB2, REL, RELA, RELB) • NFAT (C1, C2, C3, C4, 5)

(4.2) STAT	STAT (1, 2, 3, 4, 5, 6)

(4.3) p53	p53

(4.4) MADS box	Mef2 (A, B, C, D) • SRF

(4.7) High mobility group	HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1

(4.10) Cold-shock domain	CSDA, YBX1

(4.11) Runt	CBF (CBFA2T2, CBFA2T3, RUNX1, RUNX2, RUNX3, RUNX1T1)

(0) Other
transcription factors

(0.2) HMGI(Y)	HMGA (1, 2) • HBP1

(0.3) Pocket domain	Rb • RBL1 • RBL2

(0.5) AP-2/EREBP-related factors	Apetala 2 • EREBP • B3

(0.6) Miscellaneous	ARID (1A, 1B, 2, 3A, 3B, 4A) • CAP • IFI (16, 35) • MLL (2, 3, T1) • MNDA • NFI (A, B, C, X) • NFY (A, B, C) • Rho/Sigma • R-SMAD