Mad1
Mitotic spindle assembly checkpoint protein MAD1 is a protein that in humans is encoded by the MAD1L1 gene.[1][2][3]
MAD1L1 is also known as Human Accelerated Region 3. It may therefore have played a key role in differentiating Humans from Apes.
MAD1L1 is a component of the mitotic spindle-assembly checkpoint that prevents the onset of anaphase until all chromosome are properly aligned at the metaphase plate. MAD1L1 functions as a homodimer and interacts with MAD2L1. MAD1L1 may play a role in cell cycle control and tumor suppression. Three transcript variants encoding the same protein have been found for this gene.[3]
Interactions
Mad1 has been shown to interact with HDAC1,[4] Histone deacetylase 2[4] and MAD2L1.[5][6][7]
See also
References
- ^ Jin DY, Kozak CA, Pangilinan F, Spencer F, Green ED, Jeang KT (May 1999). "Mitotic checkpoint locus MAD1L1 maps to human chromosome 7p22 and mouse chromosome 5". Genomics 55 (3): 363–4. doi:10.1006/geno.1998.5654. PMID 10049595.
- ^ Jin DY, Spencer F, Jeang KT (May 1998). "Human T cell leukemia virus type 1 oncoprotein Tax targets the human mitotic checkpoint protein MAD1". Cell 93 (1): 81–91. doi:10.1016/S0092-8674(00)81148-4. PMID 9546394.
- ^ a b "Entrez Gene: MAD1L1 MAD1 mitotic arrest deficient-like 1 (yeast)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8379.
- ^ a b Yoon, Young-Mee; Baek Kwan-Hyuck, Jeong Sook-Jung, Shin Hyun-Jin, Ha Geun-Hyoung, Jeon Ae-Hwa, Hwang Sang-Gu, Chun Jang-Soo, Lee Chang-Woo (Sep. 2004). "WD repeat-containing mitotic checkpoint proteins act as transcriptional repressors during interphase". FEBS Lett. (Netherlands) 575 (1-3): 23–9. doi:10.1016/j.febslet.2004.07.089. ISSN 0014-5793. PMID 15388328.
- ^ 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.
- ^ Sironi, L; Melixetian M, Faretta M, Prosperini E, Helin K, Musacchio A (Nov. 2001). "Mad2 binding to Mad1 and Cdc20, rather than oligomerization, is required for the spindle checkpoint". EMBO J. (England) 20 (22): 6371–82. doi:10.1093/emboj/20.22.6371. ISSN 0261-4189. PMC 125308. PMID 11707408. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125308.
- ^ Murakumo, Y; Roth T, Ishii H, Rasio D, Numata S, Croce C M, Fishel R (Feb. 2000). "A human REV7 homolog that interacts with the polymerase zeta catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD2". J. Biol. Chem. (UNITED STATES) 275 (6): 4391–7. doi:10.1074/jbc.275.6.4391. ISSN 0021-9258. PMID 10660610.
PDB gallery
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1go4: CRYSTAL STRUCTURE OF MAD1-MAD2 REVEALS A CONSERVED MAD2 BINDING MOTIF IN MAD1 AND CDC20.
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