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Gene Review

HOXA11  -  homeobox A11

Homo sapiens

Synonyms: HOX1, HOX1I, Homeobox protein Hox-1I, Homeobox protein Hox-A11
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Disease relevance of HOXA11


High impact information on HOXA11

  • In contrast, Hoxa10 and Hoxa11 induced morphogenesis of endometrioid-like and mucinous-like EOCs, respectively [5].
  • The microRNA miR-181 targets the homeobox protein Hox-A11 during mammalian myoblast differentiation [6].
  • Moreover, our results suggest that miR-181 downregulates the homeobox protein Hox-A11 (a repressor of the differentiation process), thus establishing a functional link between miR-181 and the complex process of mammalian skeletal-muscle differentiation [6].
  • The chromosomal breakpoints on 7p15 were located within introns of HOXA11 or HOXA13 genes [7].
  • We now report that six different genes of the cluster HOX 1 are sequentially induced by RA in a similar temporal pattern, beginning with genes at the 3' end of the cluster [8].

Biological context of HOXA11


Anatomical context of HOXA11

  • The spatial and temporal pattern of HOXA11 expression in the human endometrium suggests a role in endometrial development, implantation, and maintenance of pregnancy [12].
  • In primary stromal cell culture, progesterone down-regulated HOXA11 antisense transcription, and this was followed by up-regulation of HOXA11 mRNA, suggesting a possible role for the antisense transcript in regulating mRNA expression [13].
  • We found that HOXA-11 protein was expressed in the premyoblasts in the limb bud, but not in the somitic cells or migrating premyogenic cells in the trunk at stage 18 [14].
  • These results suggest that Hoxa-11 and Hoxa-13 expression in the migrating premyoblasts is under the control of the limb mesenchyme and the polarizing signal(s) [14].
  • As nephrons form, they express critical transcription factors such as WT-1, Pax-2, and Hoxa11 and d11, condense, and secrete Wnt-4 [15].

Associations of HOXA11 with chemical compounds

  • In vitro, HOXA11 expression is increased in response to estrogen or progesterone [12].
  • HOX-1 mRNA levels were found to be maximally induced after 6h of treatment with 200muM H(2)O(2) and remained elevated for at least 24h [16].
  • Moreover, the uterine expression of Hoxa 10 in mice with neonatal genistein and E(3) treatments, and that of Hoxa 11 in mice with all treatments, was significantly lower when compared with vehicle alone [17].

Physical interactions of HOXA11


Regulatory relationships of HOXA11

  • Taken together, our findings show that YY1 represses Hoxa11-dependent transcription via interactions with the Hox proteins and HDAC recruitment, providing a link between an Abd-type Hox protein and a Polycomb group protein at the level of direct protein-protein interactions [18].

Other interactions of HOXA11

  • The expression and regulation of HOXC and HOXD genes varies from that of HOXA10 and HOXA11 [19].
  • None of the 24 case-matched bloods had HOXA11 methylation, whereas three blood DNAs showed THBS2 methylation [1].
  • Among the interactors, we isolated the BMP-signaling effector Smad5, which interacted with the paralogous HOXD13 but not with HOXA11 or HOXA9, revealing unique interaction capabilities of the AbdB-like HOX proteins [20].
  • Real time quantitative PCR analysis for all HOXA genes revealed high levels of HOXA10 and HOXA11 expression in all inv(7) positive cases [2].
  • Taken together, neonatal estrogenic exposure induced stromal atrophy and/or hyalinization accompanied by repressed expression of Hoxa 10 and Hoxa 11, and exerted an inhibitory effect on PTEN-related tumorigenesis [17].

Analytical, diagnostic and therapeutic context of HOXA11


  1. Frequent HOXA11 and THBS2 promoter methylation, and a methylator phenotype in endometrial adenocarcinoma. Whitcomb, B.P., Mutch, D.G., Herzog, T.J., Rader, J.S., Gibb, R.K., Goodfellow, P.J. Clin. Cancer Res. (2003) [Pubmed]
  2. A new recurrent inversion, inv(7)(p15q34), leads to transcriptional activation of HOXA10 and HOXA11 in a subset of T-cell acute lymphoblastic leukemias. Speleman, F., Cauwelier, B., Dastugue, N., Cools, J., Verhasselt, B., Poppe, B., Van Roy, N., Vandesompele, J., Graux, C., Uyttebroeck, A., Boogaerts, M., De Moerloose, B., Benoit, Y., Selleslag, D., Billiet, J., Robert, A., Huguet, F., Vandenberghe, P., De Paepe, A., Marynen, P., Hagemeijer, A. Leukemia (2005) [Pubmed]
  3. Amegakaryocytic thrombocytopenia and radio-ulnar synostosis are associated with HOXA11 mutation. Thompson, A.A., Nguyen, L.T. Nat. Genet. (2000) [Pubmed]
  4. HOXA11 mutation in amegakaryocytic thrombocytopenia with radio-ulnar synostosis syndrome inhibits megakaryocytic differentiation in vitro. Horvat-Switzer, R.D., Thompson, A.A. Blood Cells Mol. Dis. (2006) [Pubmed]
  5. Lineage infidelity of epithelial ovarian cancers is controlled by HOX genes that specify regional identity in the reproductive tract. Cheng, W., Liu, J., Yoshida, H., Rosen, D., Naora, H. Nat. Med. (2005) [Pubmed]
  6. The microRNA miR-181 targets the homeobox protein Hox-A11 during mammalian myoblast differentiation. Naguibneva, I., Ameyar-Zazoua, M., Polesskaya, A., Ait-Si-Ali, S., Groisman, R., Souidi, M., Cuvellier, S., Harel-Bellan, A. Nat. Cell Biol. (2006) [Pubmed]
  7. Single-translocation and double-chimeric transcripts: detection of NUP98-HOXA9 in myeloid leukemias with HOXA11 or HOXA13 breaks of the chromosomal translocation t(7;11)(p15;p15). Fujino, T., Suzuki, A., Ito, Y., Ohyashiki, K., Hatano, Y., Miura, I., Nakamura, T. Blood (2002) [Pubmed]
  8. Alteration of homeobox gene expression by N-ras transformation of PA-1 human teratocarcinoma cells. Buettner, R., Yim, S.O., Hong, Y.S., Boncinelli, E., Tainsky, M.A. Mol. Cell. Biol. (1991) [Pubmed]
  9. HOX gene expression is altered in the endometrium of women with endometriosis. Taylor, H.S., Bagot, C., Kardana, A., Olive, D., Arici, A. Hum. Reprod. (1999) [Pubmed]
  10. The role of HOX genes in human implantation. Eun Kwon, H., Taylor, H.S. Ann. N. Y. Acad. Sci. (2004) [Pubmed]
  11. Complete mutation analysis panel of the 39 human HOX genes. Kosaki, K., Kosaki, R., Suzuki, T., Yoshihashi, H., Takahashi, T., Sasaki, K., Tomita, M., McGinnis, W., Matsuo, N. Teratology (2002) [Pubmed]
  12. Sex steroids mediate HOXA11 expression in the human peri-implantation endometrium. Taylor, H.S., Igarashi, P., Olive, D.L., Arici, A. J. Clin. Endocrinol. Metab. (1999) [Pubmed]
  13. HOXA11 silencing and endogenous HOXA11 antisense ribonucleic acid in the uterine endometrium. Chau, Y.M., Pando, S., Taylor, H.S. J. Clin. Endocrinol. Metab. (2002) [Pubmed]
  14. Coordinated expression of Hoxa-11 and Hoxa-13 during limb muscle patterning. Yamamoto, M., Gotoh, Y., Tamura, K., Tanaka, M., Kawakami, A., Ide, H., Kuroiwa, A. Development (1998) [Pubmed]
  15. Genes and proteins in renal development. Davies, J.A., Fisher, C.E. Exp. Nephrol. (2002) [Pubmed]
  16. Involvement of JNKs and p38-MAPK/MSK1 pathways in H(2)O(2)-induced upregulation of heme oxygenase-1 mRNA in H9c2 cells. Aggeli, I.K., Gaitanaki, C., Beis, I. Cell. Signal. (2006) [Pubmed]
  17. Neonatal estrogenic exposure suppresses PTEN-related endometrial carcinogenesis in recombinant mice. Begum, M., Tashiro, H., Katabuchi, H., Suzuki, A., Kurman, R.J., Okamura, H. Lab. Invest. (2006) [Pubmed]
  18. Yin Yang 1 Physically Interacts with Hoxa11 and Represses Hoxa11-dependent Transcription. Luke, M.P., Sui, G., Liu, H., Shi, Y. J. Biol. Chem. (2006) [Pubmed]
  19. HOXC and HOXD gene expression in human endometrium: lack of redundancy with HOXA paralogs. Akbas, G.E., Taylor, H.S. Biol. Reprod. (2004) [Pubmed]
  20. Group 13 HOX proteins interact with the MH2 domain of R-Smads and modulate Smad transcriptional activation functions independent of HOX DNA-binding capability. Williams, T.M., Williams, M.E., Heaton, J.H., Gelehrter, T.D., Innis, J.W. Nucleic Acids Res. (2005) [Pubmed]
  21. Expression of HOXA11 gene in human endometrium. Wang, L.F., Luo, H.Z., Zhu, Z.M., Wang, J.D. Am. J. Obstet. Gynecol. (2004) [Pubmed]
  22. Craniosynostosis and hemizygosity for D7S135 caused by a de novo and apparently balanced t(6;7) translocation. Tsuji, K., Narahara, K., Kikkawa, K., Murakami, M., Yokoyama, Y., Ninomiya, S., Seino, Y. Am. J. Med. Genet. (1994) [Pubmed]
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