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Mitotic spindle assembly checkpoint protein MAD2A (HsMAD2) (Mitotic arrest deficient 2-like protein 1) (MAD2-like protein 1)

 MD2L1_HUMAN             Reviewed;         205 AA.
Q13257; Q53F56; Q548X9; Q6IRW7; Q8IZX3;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 185.
RecName: Full=Mitotic spindle assembly checkpoint protein MAD2A;
Short=HsMAD2;
AltName: Full=Mitotic arrest deficient 2-like protein 1;
Short=MAD2-like protein 1;
Name=MAD2L1; Synonyms=MAD2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8824189; DOI=10.1126/science.274.5285.246;
Li Y., Benezra R.;
"Identification of a human mitotic checkpoint gene: hsMAD2.";
Science 274:246-248(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11390010; DOI=10.1016/S0169-5002(00)00223-3;
Gemma A., Hosoya Y., Seike M., Uematsu K., Kurimoto F., Hibino S.,
Yoshimura A., Shibuya M., Kudoh S., Emi M.;
"Genomic structure of the human MAD2 gene and mutation analysis in
human lung and breast cancers.";
Lung Cancer 32:289-295(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Jin D.-Y., Jeang K.-T.;
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Klebert S., Barnikol-Watanabe S., Kratzin H.D., Hilschmann N.;
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Nobori T.;
"Complete human MAD2 gene.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Yin F., Fan D.M.;
"Identifying a new variant of MAD2L1.";
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lung;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
PROTEIN SEQUENCE OF 2-7; 36-45; 123-129 AND 193-205, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Hepatoma;
Bienvenut W.V., Dhillon A.S., Kolch W.;
Submitted (FEB-2008) to UniProtKB.
[13]
INTERACTION WITH CDC20.
PubMed=9637688; DOI=10.1101/gad.12.12.1871;
Fang G., Yu H., Kirschner M.W.;
"The checkpoint protein MAD2 and the mitotic regulator CDC20 form a
ternary complex with the anaphase-promoting complex to control
anaphase initiation.";
Genes Dev. 12:1871-1883(1998).
[14]
INTERACTION WITH ADAM17.
PubMed=10527948; DOI=10.1042/bj3430673;
Nelson K.K., Schlondorff J., Blobel C.P.;
"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, MAD2-beta.";
Biochem. J. 343:673-680(1999).
[15]
INTERACTION WITH MAD2L1BP.
PubMed=12456649; DOI=10.1093/emboj/cdf659;
Habu T., Kim S.H., Weinstein J., Matsumoto T.;
"Identification of a MAD2-binding protein, CMT2, and its role in
mitosis.";
EMBO J. 21:6419-6428(2002).
[16]
PHOSPHORYLATION AT SER-170; SER-178 AND SER-195, INTERACTION WITH
MAD1L1 AND CDC20, AND MUTAGENESIS OF SER-170; SER-178 AND SER-195.
PubMed=12574116; DOI=10.1093/emboj/cdg071;
Wassmann K., Liberal V., Benezra R.;
"Mad2 phosphorylation regulates its association with Mad1 and the
APC/C.";
EMBO J. 22:797-806(2003).
[17]
SUBCELLULAR LOCATION.
PubMed=14978040; DOI=10.1074/jbc.M314205200;
Lou Y., Yao J., Zereshki A., Dou Z., Ahmed K., Wang H., Hu J.,
Wang Y., Yao X.;
"NEK2A interacts with MAD1 and possibly functions as a novel
integrator of the spindle checkpoint signaling.";
J. Biol. Chem. 279:20049-20057(2004).
[18]
SUBCELLULAR LOCATION.
PubMed=15020684; DOI=10.1242/jcs.01006;
Johnson V.L., Scott M.I., Holt S.V., Hussein D., Taylor S.S.;
"Bub1 is required for kinetochore localization of BubR1, Cenp-E, Cenp-
F and Mad2, and chromosome congression.";
J. Cell Sci. 117:1577-1589(2004).
[19]
SUBCELLULAR LOCATION, AND INTERACTION WITH UBD.
PubMed=16495226; DOI=10.1074/jbc.M507218200;
Ren J., Kan A., Leong S.H., Ooi L.L.P.J., Jeang K.-T., Chong S.S.,
Kon O.L., Lee C.G.L.;
"FAT10 plays a role in the regulation of chromosomal stability.";
J. Biol. Chem. 281:11413-11421(2006).
[20]
INTERACTION WITH HSF1.
PubMed=18794143; DOI=10.1158/0008-5472.CAN-08-0129;
Lee Y.J., Kim E.H., Lee J.S., Jeoung D., Bae S., Kwon S.H., Lee Y.S.;
"HSF1 as a mitotic regulator: phosphorylation of HSF1 by Plk1 is
essential for mitotic progression.";
Cancer Res. 68:7550-7560(2008).
[21]
INTERACTION WITH TPR; MAD1L1 AND CDC20, AND SUBCELLULAR LOCATION.
PubMed=18981471; DOI=10.1101/gad.1677208;
Lee S.H., Sterling H., Burlingame A., McCormick F.;
"Tpr directly binds to Mad1 and Mad2 and is important for the Mad1-
Mad2-mediated mitotic spindle checkpoint.";
Genes Dev. 22:2926-2931(2008).
[22]
SUBCELLULAR LOCATION.
PubMed=18712773; DOI=10.1002/jcb.21879;
Ho C.-Y., Wong C.-H., Li H.-Y.;
"Perturbation of the chromosomal binding of RCC1, Mad2 and survivin
causes spindle assembly defects and mitotic catastrophe.";
J. Cell. Biochem. 105:835-846(2008).
[23]
REVIEW.
PubMed=19029339; DOI=10.1083/jcb.200808122;
Skinner J.J., Wood S., Shorter J., Englander S.W., Black B.E.;
"The Mad2 partial unfolding model: regulating mitosis through Mad2
conformational switching.";
J. Cell Biol. 183:761-768(2008).
[24]
SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH NEK2.
PubMed=20034488; DOI=10.1016/j.yexmp.2009.12.004;
Liu Q., Hirohashi Y., Du X., Greene M.I., Wang Q.;
"Nek2 targets the mitotic checkpoint proteins Mad2 and Cdc20: a
mechanism for aneuploidy in cancer.";
Exp. Mol. Pathol. 88:225-233(2010).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-130; SER-185 AND
SER-195, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[27]
INTERACTION WITH UBD.
PubMed=25422469; DOI=10.1073/pnas.1403383111;
Theng S.S., Wang W., Mah W.C., Chan C., Zhuo J., Gao Y., Qin H.,
Lim L., Chong S.S., Song J., Lee C.G.;
"Disruption of FAT10-MAD2 binding inhibits tumor progression.";
Proc. Natl. Acad. Sci. U.S.A. 111:E5282-E5291(2014).
[28]
STRUCTURE BY NMR OF 11-195, FUNCTION, DOMAIN, AND INTERACTION WITH
CDC20.
PubMed=10700282; DOI=10.1038/73338;
Luo X., Fang G., Coldiron M., Lin Y., Yu H., Kirschner M.W.,
Wagner G.;
"Structure of the Mad2 spindle assembly checkpoint protein and its
interaction with Cdc20.";
Nat. Struct. Biol. 7:224-229(2000).
[29]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF MUTANT ALA-133 IN COMPLEX
WITH MAD1L1, SUBUNIT, DOMAIN, MUTAGENESIS OF ARG-133, AND INTERACTION
WITH MAD1L1.
PubMed=12006501; DOI=10.1093/emboj/21.10.2496;
Sironi L., Mapelli M., Knapp S., De Antoni A., Jeang K.-T.,
Musacchio A.;
"Crystal structure of the tetrameric Mad1-Mad2 core complex:
implications of a 'safety belt' binding mechanism for the spindle
checkpoint.";
EMBO J. 21:2496-2506(2002).
[30]
STRUCTURE BY NMR OF 11-205 IN COMPLEX WITH PEPTIDE LIGAND, DOMAIN,
SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH CDC20 AND MAD1L1.
PubMed=11804586; DOI=10.1016/S1097-2765(01)00435-X;
Luo X., Tang Z., Rizo J., Yu H.;
"The Mad2 spindle checkpoint protein undergoes similar major
conformational changes upon binding to either Mad1 or Cdc20.";
Mol. Cell 9:59-71(2002).
[31]
STRUCTURE BY NMR, DOMAIN, SUBUNIT, FUNCTION, INTERACTION WITH MAD1L1,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15024386; DOI=10.1038/nsmb748;
Luo X., Tang Z., Xia G., Wassmann K., Matsumoto T., Rizo J., Yu H.;
"The Mad2 spindle checkpoint protein has two distinct natively folded
states.";
Nat. Struct. Mol. Biol. 11:338-345(2004).
[32]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF DIMER CONTAINING BOTH
CONFORMERS, AND INTERACTION OF THE TWO MAD2L1 CONFORMERS.
PubMed=18022367; DOI=10.1016/j.cell.2007.08.049;
Mapelli M., Massimiliano L., Santaguida S., Musacchio A.;
"The Mad2 conformational dimer: structure and implications for the
spindle assembly checkpoint.";
Cell 131:730-743(2007).
[33]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEXES WITH MAD2L1BP, AND
INTERACTION WITH MAD2L1BP.
PubMed=18022368; DOI=10.1016/j.cell.2007.08.048;
Yang M., Li B., Tomchick D.R., Machius M., Rizo J., Yu H., Luo X.;
"p31comet blocks Mad2 activation through structural mimicry.";
Cell 131:744-755(2007).
[34]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF HOMODIMER OF MUTANT ALA-13
IN THE CLOSED CONFORMATION, DOMAIN, SUBUNIT, AND MUTAGENESIS OF
LEU-13; TRP-75; LEU-153; TYR-156; PHE-186; THR-188; HIS-191; VAL-197
AND TYR-199.
PubMed=18318601; DOI=10.1371/journal.pbio.0060050;
Yang M., Li B., Liu C.-J., Tomchick D.R., Machius M., Rizo J., Yu H.,
Luo X.;
"Insights into Mad2 regulation in the spindle checkpoint revealed by
the crystal structure of the symmetric Mad2 dimer.";
PLoS Biol. 6:E50-E50(2008).
-!- FUNCTION: Component of the spindle-assembly checkpoint that
prevents the onset of anaphase until all chromosomes are properly
aligned at the metaphase plate. Required for the execution of the
mitotic checkpoint which monitors the process of kinetochore-
spindle attachment and inhibits the activity of the anaphase
promoting complex by sequestering CDC20 until all chromosomes are
aligned at the metaphase plate. {ECO:0000269|PubMed:10700282,
ECO:0000269|PubMed:11804586, ECO:0000269|PubMed:15024386}.
-!- SUBUNIT: Monomer and homodimer. Heterotetramer with MAD1L1.
Formation of a heterotetrameric core complex containing two
molecules each of MAD1L1 and of MAD2L1 promotes binding of another
molecule of MAD2L1 to each MAD2L1, resulting in a heterohexamer.
Interacts with CDC20, MAD2L1BP and with ADAM17/TACE. Dimeric
MAD2L1 in the closed conformation interacts with CDC20. Monomeric
MAD2L1 in the open conformation does not interact with CDC20.
CDC20 competes with MAD1L1 for MAD2L1 binding. Interacts with TPR.
Binds to UBD (via ubiquitin-like 1 domain) during mitosis.
Interacts with isoform 1 and isoform 2 of NEK2. Interacts with
HSF1; this interaction occurs in mitosis (PubMed:18794143).
{ECO:0000269|PubMed:10527948, ECO:0000269|PubMed:10700282,
ECO:0000269|PubMed:11804586, ECO:0000269|PubMed:12006501,
ECO:0000269|PubMed:12456649, ECO:0000269|PubMed:12574116,
ECO:0000269|PubMed:15024386, ECO:0000269|PubMed:16495226,
ECO:0000269|PubMed:18022367, ECO:0000269|PubMed:18022368,
ECO:0000269|PubMed:18318601, ECO:0000269|PubMed:18794143,
ECO:0000269|PubMed:18981471, ECO:0000269|PubMed:20034488,
ECO:0000269|PubMed:25422469, ECO:0000269|PubMed:9637688}.
-!- INTERACTION:
Self; NbExp=9; IntAct=EBI-78203, EBI-78203;
P78536:ADAM17; NbExp=3; IntAct=EBI-78203, EBI-78188;
O60566:BUB1B; NbExp=14; IntAct=EBI-78203, EBI-1001438;
Q12834:CDC20; NbExp=33; IntAct=EBI-78203, EBI-367462;
P30260:CDC27; NbExp=8; IntAct=EBI-78203, EBI-994813;
Q14145:KEAP1; NbExp=6; IntAct=EBI-78203, EBI-751001;
Q9Y6D9:MAD1L1; NbExp=23; IntAct=EBI-78203, EBI-742610;
Q15013:MAD2L1BP; NbExp=13; IntAct=EBI-78203, EBI-712181;
O00560:SDCBP; NbExp=3; IntAct=EBI-78203, EBI-727004;
Q562F6:SGO2; NbExp=10; IntAct=EBI-78203, EBI-989213;
Q9Y3Q8:TSC22D4; NbExp=4; IntAct=EBI-78203, EBI-739485;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere,
kinetochore. Cytoplasm. Cytoplasm, cytoskeleton, spindle pole.
Note=Recruited by MAD1L1 to unattached kinetochores (Probable).
Recruited to the nuclear pore complex by TPR during interphase.
Recruited to kinetochores in late prometaphase after BUB1, CENPF,
BUB1B and CENPE. Kinetochore association requires the presence of
NEK2. Kinetochore association is repressed by UBD. {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13257-1; Sequence=Displayed;
Name=2;
IsoId=Q13257-2; Sequence=VSP_047644, VSP_047645;
-!- DOMAIN: The protein has two highly different native conformations,
an inactive open conformation that cannot bind CDC20 and that
predominates in cytosolic monomers, and an active closed
conformation. The protein in the closed conformation
preferentially dimerizes with another molecule in the open
conformation, but can also form a dimer with a molecule in the
closed conformation. Formation of a heterotetrameric core complex
containing two molecules of MAD1L1 and of MAD2L1 in the closed
conformation promotes binding of another molecule of MAD2L1 in the
open conformation and the conversion of the open to the closed
form, and thereby promotes interaction with CDC20.
{ECO:0000269|PubMed:10700282, ECO:0000269|PubMed:11804586,
ECO:0000269|PubMed:12006501, ECO:0000269|PubMed:15024386,
ECO:0000269|PubMed:18318601}.
-!- PTM: Phosphorylated on multiple serine residues. The level of
phosphorylation varies during the cell cycle and is highest during
mitosis. Phosphorylation abolishes interaction with MAD1L1 and
reduces interaction with CDC20. Phosphorylated by NEK2.
{ECO:0000269|PubMed:12574116, ECO:0000269|PubMed:20034488}.
-!- SIMILARITY: Belongs to the MAD2 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MAD2L1ID304.html";
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EMBL; U65410; AAC50781.1; -; mRNA.
EMBL; AF202273; AAK38174.1; -; Genomic_DNA.
EMBL; AF202269; AAK38174.1; JOINED; Genomic_DNA.
EMBL; AF202270; AAK38174.1; JOINED; Genomic_DNA.
EMBL; AF202271; AAK38174.1; JOINED; Genomic_DNA.
EMBL; AF202272; AAK38174.1; JOINED; Genomic_DNA.
EMBL; U31278; AAC52060.1; -; mRNA.
EMBL; AJ000186; CAA03943.1; -; mRNA.
EMBL; AB056160; BAB63410.1; -; Genomic_DNA.
EMBL; AF394735; AAN74648.1; -; mRNA.
EMBL; AK298228; BAG60497.1; -; mRNA.
EMBL; AK313827; BAG36562.1; -; mRNA.
EMBL; AK223433; BAD97153.1; -; mRNA.
EMBL; AC097173; AAY40945.1; -; Genomic_DNA.
EMBL; CH471056; EAX05271.1; -; Genomic_DNA.
EMBL; CH471056; EAX05273.1; -; Genomic_DNA.
EMBL; BC000356; AAH00356.1; -; mRNA.
EMBL; BC005945; AAH05945.1; -; mRNA.
EMBL; BC070283; AAH70283.1; -; mRNA.
CCDS; CCDS3715.1; -. [Q13257-1]
PIR; G01942; G01942.
RefSeq; NP_002349.1; NM_002358.3. [Q13257-1]
UniGene; Hs.591697; -.
PDB; 1DUJ; NMR; -; A=11-195.
PDB; 1GO4; X-ray; 2.05 A; A/B/C/D=1-205.
PDB; 1KLQ; NMR; -; A=11-205.
PDB; 1S2H; NMR; -; A=1-205.
PDB; 2QYF; X-ray; 2.30 A; A/C=1-205.
PDB; 2V64; X-ray; 2.90 A; A/C/D/E/F/H=2-205.
PDB; 2VFX; X-ray; 1.95 A; A/B/C/D/E/F/G/H/I/J/K/L=1-205.
PDB; 3GMH; X-ray; 3.95 A; A/B/C/D/E/F/G/H/I/J/K/L=11-205.
PDB; 5KHU; EM; 4.80 A; T=1-205.
PDB; 5LCW; EM; 4.00 A; Z=1-205.
PDB; 6F0X; EM; 4.60 A; Z=1-205.
PDBsum; 1DUJ; -.
PDBsum; 1GO4; -.
PDBsum; 1KLQ; -.
PDBsum; 1S2H; -.
PDBsum; 2QYF; -.
PDBsum; 2V64; -.
PDBsum; 2VFX; -.
PDBsum; 3GMH; -.
PDBsum; 5KHU; -.
PDBsum; 5LCW; -.
PDBsum; 6F0X; -.
ProteinModelPortal; Q13257; -.
SMR; Q13257; -.
BioGrid; 110260; 80.
ComplexPortal; CPX-85; Mitotic spindle assembly checkpoint MAD1-MAD2 complex.
ComplexPortal; CPX-88; Mitotic spindle assembly checkpoint complex MAD2.
CORUM; Q13257; -.
DIP; DIP-29653N; -.
IntAct; Q13257; 62.
MINT; Q13257; -.
STRING; 9606.ENSP00000296509; -.
iPTMnet; Q13257; -.
PhosphoSitePlus; Q13257; -.
SwissPalm; Q13257; -.
BioMuta; MAD2L1; -.
DMDM; 12230256; -.
EPD; Q13257; -.
MaxQB; Q13257; -.
PaxDb; Q13257; -.
PeptideAtlas; Q13257; -.
PRIDE; Q13257; -.
ProteomicsDB; 59256; -.
TopDownProteomics; Q13257-1; -. [Q13257-1]
DNASU; 4085; -.
Ensembl; ENST00000296509; ENSP00000296509; ENSG00000164109. [Q13257-1]
Ensembl; ENST00000333047; ENSP00000332295; ENSG00000164109. [Q13257-2]
GeneID; 4085; -.
KEGG; hsa:4085; -.
UCSC; uc003idl.3; human. [Q13257-1]
CTD; 4085; -.
DisGeNET; 4085; -.
EuPathDB; HostDB:ENSG00000164109.13; -.
GeneCards; MAD2L1; -.
HGNC; HGNC:6763; MAD2L1.
HPA; HPA003348; -.
MIM; 601467; gene.
neXtProt; NX_Q13257; -.
OpenTargets; ENSG00000164109; -.
PharmGKB; PA30521; -.
eggNOG; KOG3285; Eukaryota.
eggNOG; ENOG410XSD7; LUCA.
GeneTree; ENSGT00390000007908; -.
HOGENOM; HOG000199586; -.
HOVERGEN; HBG105691; -.
InParanoid; Q13257; -.
KO; K02537; -.
OMA; SEVPVEW; -.
OrthoDB; EOG091G0JBM; -.
PhylomeDB; Q13257; -.
TreeFam; TF101084; -.
Reactome; R-HSA-141405; Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-68877; Mitotic Prometaphase.
SIGNOR; Q13257; -.
ChiTaRS; MAD2L1; human.
EvolutionaryTrace; Q13257; -.
GeneWiki; MAD2L1; -.
GenomeRNAi; 4085; -.
PRO; PR:Q13257; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000164109; Expressed in 200 organ(s), highest expression level in secondary oocyte.
CleanEx; HS_MAD2L1; -.
ExpressionAtlas; Q13257; baseline and differential.
Genevisible; Q13257; HS.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007093; P:mitotic cell cycle checkpoint; IDA:UniProtKB.
GO; GO:0000070; P:mitotic sister chromatid segregation; IEA:Ensembl.
GO; GO:0007094; P:mitotic spindle assembly checkpoint; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IMP:MGI.
GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB.
GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IDA:UniProtKB.
GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IMP:UniProtKB.
Gene3D; 3.30.900.10; -; 1.
InterPro; IPR003511; HORMA_dom.
InterPro; IPR036570; HORMA_dom_sf.
InterPro; IPR027097; Mad2.
PANTHER; PTHR11842:SF11; PTHR11842:SF11; 1.
Pfam; PF02301; HORMA; 1.
SUPFAM; SSF56019; SSF56019; 1.
PROSITE; PS50815; HORMA; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle;
Cell division; Centromere; Chromosome; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Kinetochore; Mitosis;
Nucleus; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.12}.
CHAIN 2 205 Mitotic spindle assembly checkpoint
protein MAD2A.
/FTId=PRO_0000126117.
DOMAIN 14 197 HORMA. {ECO:0000255|PROSITE-
ProRule:PRU00109}.
REGION 195 205 Required for assuming the closed
conformation and for interaction with
CDC20.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.12}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 130 130 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000269|PubMed:12574116}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000269|PubMed:12574116}.
MOD_RES 185 185 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 195 195 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:12574116}.
VAR_SEQ 74 90 DWLYKCSVQKLVVVISN -> VHPEKSLRKLSRMKSVQ
(in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.6}.
/FTId=VSP_047644.
VAR_SEQ 91 205 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.6}.
/FTId=VSP_047645.
MUTAGEN 13 13 L->A: Leads to formation the closed
conformation and homodimerization.
{ECO:0000269|PubMed:18318601}.
MUTAGEN 75 75 W->A: Prevents interaction with CDC20 and
leads to formation of the closed
conformation; when associated with A-133.
{ECO:0000269|PubMed:18318601}.
MUTAGEN 133 133 R->A: Prevents aggregation and promotes
formation of monomeric protein that
slowly interconverts between the open and
closed conformation.
{ECO:0000269|PubMed:12006501}.
MUTAGEN 153 153 L->A: Leads to formation of the closed
conformation; when associated with A-133.
{ECO:0000269|PubMed:18318601}.
MUTAGEN 156 156 Y->A: Leads to formation of the closed
conformation; when associated with A-133.
{ECO:0000269|PubMed:18318601}.
MUTAGEN 170 170 S->A: Reduces phosphorylation on serine
residues; when associated with A-178.
Abolishes phosphorylation on serine
residues; when associated with A-178 and
A-195. {ECO:0000269|PubMed:12574116}.
MUTAGEN 170 170 S->D: Abolishes interaction with MAD1L1
and reduces interaction with CDC20; when
associated with D-178 and D-195.
{ECO:0000269|PubMed:12574116}.
MUTAGEN 178 178 S->A: Reduces phosphorylation on serine
residues; when associated with A-170.
Abolishes phosphorylation on serine
residues; when associated with A-170 and
A-195. {ECO:0000269|PubMed:12574116}.
MUTAGEN 178 178 S->D: Abolishes interaction with MAD1L1
and reduces interaction with CDC20; when
associated with D-170 and D-195.
{ECO:0000269|PubMed:12574116}.
MUTAGEN 186 186 F->A: Prevents formation of the closed
conformation and interaction with CDC20;
when associated with A-133.
{ECO:0000269|PubMed:18318601}.
MUTAGEN 188 188 T->A: Prevents formation of the closed
conformation and interaction with CDC20;
when associated with A-133.
{ECO:0000269|PubMed:18318601}.
MUTAGEN 191 191 H->A: Prevents formation of the closed
conformation and interaction with CDC20;
when associated with A-133.
{ECO:0000269|PubMed:18318601}.
MUTAGEN 195 195 S->A: Abolishes phosphorylation on serine
residues; when associated with A-170 and
A-178. {ECO:0000269|PubMed:12574116}.
MUTAGEN 195 195 S->D: Abolishes interaction with MAD1L1
and reduces interaction with CDC20; when
associated with D-170 and D-178.
{ECO:0000269|PubMed:12574116}.
MUTAGEN 197 197 V->A: Prevents formation of the closed
conformation and interaction with CDC20;
when associated with A-133.
{ECO:0000269|PubMed:18318601}.
MUTAGEN 199 199 Y->A: Prevents formation of the closed
conformation and interaction with CDC20;
when associated with A-133.
{ECO:0000269|PubMed:18318601}.
CONFLICT 16 16 S -> C (in Ref. 8; BAD97153).
{ECO:0000305}.
CONFLICT 190 190 I -> V (in Ref. 11; AAH70283).
{ECO:0000305}.
STRAND 2 5 {ECO:0000244|PDB:2VFX}.
STRAND 7 9 {ECO:0000244|PDB:1S2H}.
HELIX 13 34 {ECO:0000244|PDB:2VFX}.
HELIX 40 42 {ECO:0000244|PDB:2VFX}.
STRAND 43 48 {ECO:0000244|PDB:2VFX}.
STRAND 51 56 {ECO:0000244|PDB:2VFX}.
HELIX 59 77 {ECO:0000244|PDB:2VFX}.
STRAND 78 80 {ECO:0000244|PDB:1DUJ}.
STRAND 81 90 {ECO:0000244|PDB:2VFX}.
TURN 91 93 {ECO:0000244|PDB:2VFX}.
STRAND 96 106 {ECO:0000244|PDB:2VFX}.
HELIX 108 111 {ECO:0000244|PDB:1GO4}.
STRAND 116 118 {ECO:0000244|PDB:1S2H}.
HELIX 121 139 {ECO:0000244|PDB:2VFX}.
STRAND 149 157 {ECO:0000244|PDB:2VFX}.
HELIX 160 162 {ECO:0000244|PDB:2QYF}.
STRAND 167 169 {ECO:0000244|PDB:1GO4}.
STRAND 173 175 {ECO:0000244|PDB:2V64}.
STRAND 177 182 {ECO:0000244|PDB:2VFX}.
STRAND 189 200 {ECO:0000244|PDB:2VFX}.
SEQUENCE 205 AA; 23510 MW; B8DCBF0043836764 CRC64;
MALQLSREQG ITLRGSAEIV AEFFSFGINS ILYQRGIYPS ETFTRVQKYG LTLLVTTDLE
LIKYLNNVVE QLKDWLYKCS VQKLVVVISN IESGEVLERW QFDIECDKTA KDDSAPREKS
QKAIQDEIRS VIRQITATVT FLPLLEVSCS FDLLIYTDKD LVVPEKWEES GPQFITNSEE
VRLRSFTTTI HKVNSMVAYK IPVND


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