MAD2L2

MAD2L2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3ABD, 3ABE, 3VU7, 4EXT, 4GK0, 4GK5
Identifiers
Aliases	MAD2L2, MAD2B, POLZ2, REV7, MAD2 mitotic arrest deficient-like 2 (yeast)
External IDs	MGI: 1919140 HomoloGene: 4624 GeneCards: MAD2L2
Gene ontology Molecular function • JUN kinase binding • RNA polymerase II activating transcription factor binding • protein binding Cellular component • cytoplasm • spindle • nucleoplasm • zeta DNA polymerase complex • anaphase-promoting complex • cytoskeleton • nucleus Biological process • DNA damage response, signal transduction resulting in transcription • mitotic nuclear division • regulation of transcription, DNA-templated • negative regulation of protein catabolic process • actin filament organization • negative regulation of cell-cell adhesion mediated by cadherin • negative regulation of transcription by competitive promoter binding • negative regulation of transcription from RNA polymerase II promoter • negative regulation of sequence-specific DNA binding transcription factor activity • transcription, DNA-templated • mitotic spindle assembly checkpoint • positive regulation of peptidyl-serine phosphorylation • error-prone translesion synthesis • cellular response to DNA damage stimulus • cell division • positive regulation of transcription, DNA-templated • negative regulation of transcription regulatory region DNA binding • double-strand break repair • regulation of cell growth • cell cycle • negative regulation of canonical Wnt signaling pathway • negative regulation of epithelial to mesenchymal transition • negative regulation of ubiquitin protein ligase activity Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10459	71890
Ensembl	ENSG00000116670	ENSMUSG00000029003
UniProt	Q9UI95	Q9D752
RefSeq (mRNA)	NM_001127325 NM_006341	NM_027985 NM_001305420
RefSeq (protein)	NP_001120797.1 NP_006332.3	NP_001292349.1 NP_082261.2
Location (UCSC)	Chr 1: 11.67 – 11.69 Mb	Chr 4: 148.13 – 148.15 Mb
PubMed search	[1]	[2]
Wikidata

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Mitotic spindle assembly checkpoint protein MAD2B is a protein that in humans is encoded by the MAD2L2 gene.^[3][4]

Function

MAD2L2 is a component of the mitotic spindle assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. MAD2L2 is a homolog of MAD2L1.^[4]

Interactions

MAD2L2 has been shown to interact with:

• ADAM9,^[5]
• MAD2L1,^[6]
• REV1,^[7] and
• REV3L.^[6][7]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Cahill DP, da Costa LT, Carson-Walter EB, Kinzler KW, Vogelstein B, Lengauer C (Aug 1999). "Characterization of MAD2B and other mitotic spindle checkpoint genes". Genomics. 58 (2): 181–7. doi:10.1006/geno.1999.5831. PMID 10366450.
4. "Entrez Gene: MAD2L2 MAD2 mitotic arrest deficient-like 2 (yeast)".
5. Nelson KK, Schlöndorff J, Blobel CP (Nov 1999). "Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2beta". Biochem. J. 343. 343 (3): 673–80. doi:10.1042/0264-6021:3430673. PMC 1220601. PMID 10527948.
6. Murakumo Y, Roth T, Ishii H, Rasio D, Numata S, Croce CM, 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. 275 (6): 4391–7. doi:10.1074/jbc.275.6.4391. PMID 10660610.
7. Murakumo Y, Ogura Y, Ishii H, Numata S, Ichihara M, Croce CM, Fishel R, Takahashi M (Sep 2001). "Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7". J. Biol. Chem. 276 (38): 35644–51. doi:10.1074/jbc.M102051200. PMID 11485998.

Further reading

• Nelson KK, Schlöndorff J, Blobel CP (1999). "Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2beta". Biochem. J. 343. 343 (3): 673–80. doi:10.1042/0264-6021:3430673. PMC 1220601. PMID 10527948.
• Murakumo Y, Roth T, Ishii H, Rasio D, Numata S, Croce CM, Fishel R (2000). "A human REV7 homolog that interacts with the polymerase zeta catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD2". J. Biol. Chem. 275 (6): 4391–7. doi:10.1074/jbc.275.6.4391. PMID 10660610.
• Chan SH, Hung FS, Chan DS, Shaw PC (2001). "Trichosanthin interacts with acidic ribosomal proteins P0 and P1 and mitotic checkpoint protein MAD2B". Eur. J. Biochem. 268 (7): 2107–12. doi:10.1046/j.1432-1327.2001.02091.x. PMID 11277934.
• Chen J, Fang G (2001). "MAD2B is an inhibitor of the anaphase-promoting complex". Genes Dev. 15 (14): 1765–70. doi:10.1101/gad.898701. PMC 312737. PMID 11459826.
• Murakumo Y, Ogura Y, Ishii H, Numata S, Ichihara M, Croce CM, Fishel R, Takahashi M (2001). "Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7". J. Biol. Chem. 276 (38): 35644–51. doi:10.1074/jbc.M102051200. PMID 11485998.
• Weterman MA, van Groningen JJ, Tertoolen L, van Kessel AG (2001). "Impairment of MAD2B-PRCC interaction in mitotic checkpoint defective t(X;1)-positive renal cell carcinomas". Proc. Natl. Acad. Sci. U.S.A. 98 (24): 13808–13. doi:10.1073/pnas.241304198. PMC 61123. PMID 11717438.
• Masuda Y, Ohmae M, Masuda K, Kamiya K (2003). "Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins". J. Biol. Chem. 278 (14): 12356–60. doi:10.1074/jbc.M211765200. PMID 12529368.
• Ying B, Wold WS (2003). "Adenovirus ADP protein (E3-11.6K), which is required for efficient cell lysis and virus release, interacts with human MAD2B". Virology. 313 (1): 224–34. doi:10.1016/S0042-6822(03)00287-3. PMID 12951035.
• Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics. 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819.
• Ohashi E, Murakumo Y, Kanjo N, Akagi J, Masutani C, Hanaoka F, Ohmori H (2004). "Interaction of hREV1 with three human Y-family DNA polymerases". Genes Cells. 9 (6): 523–31. doi:10.1111/j.1356-9597.2004.00747.x. PMID 15189446.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Rimkus C, Friederichs J, Rosenberg R, Holzmann B, Siewert JR, Janssen KP (2007). "Expression of the mitotic checkpoint gene MAD2L2 has prognostic significance in colon cancer". Int. J. Cancer. 120 (1): 207–11. doi:10.1002/ijc.22155. PMID 17044027.
• Zhang L, Yang SH, Sharrocks AD (2007). "Rev7/MAD2B links c-Jun N-terminal protein kinase pathway signaling to activation of the transcription factor Elk-1". Mol. Cell. Biol. 27 (8): 2861–9. doi:10.1128/MCB.02276-06. PMC 1899940. PMID 17296730.
• Pinto M, Soares MJ, Cerveira N, Henrique R, Ribeiro FR, Oliveira J, Jerónimo C, Teixeira MR (2007). "Expression changes of the MAD mitotic checkpoint gene family in renal cell carcinomas characterized by numerical chromosome changes". Virchows Arch. 450 (4): 379–85. doi:10.1007/s00428-007-0386-7. PMID 17333263.