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Mitotic spindle assembly checkpoint protein MAD1 (Mitotic arrest deficient 1-like protein 1) (MAD1-like protein 1) (Mitotic checkpoint MAD1 protein homolog) (HsMAD1) (hMAD1) (Tax-binding protein 181)

 MD1L1_HUMAN             Reviewed;         718 AA.
Q9Y6D9; B3KR41; Q13312; Q75MI0; Q86UM4; Q9UNH0;
27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
27-SEP-2004, sequence version 2.
18-JUL-2018, entry version 163.
RecName: Full=Mitotic spindle assembly checkpoint protein MAD1;
AltName: Full=Mitotic arrest deficient 1-like protein 1;
Short=MAD1-like protein 1;
AltName: Full=Mitotic checkpoint MAD1 protein homolog;
Short=HsMAD1;
Short=hMAD1;
AltName: Full=Tax-binding protein 181;
Name=MAD1L1; Synonyms=MAD1, TXBP181;
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), HOMODIMERIZATION,
HETEROTETRAMERIZATION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
INTERACTION WITH MAD2L1 AND VIRAL TAX.
PubMed=9546394; DOI=10.1016/S0092-8674(00)81148-4;
Jin D.-Y., Spencer F., Jeang K.-T.;
"Human T cell leukemia virus type 1 oncoprotein Tax targets the human
mitotic checkpoint protein MAD1.";
Cell 93:81-91(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION BY BUB1, AND
INTERACTION WITH BUB1/BUB3 COMPLEX.
TISSUE=Testis;
PubMed=10198256; DOI=10.1006/bbrc.1999.0514;
Seeley T.W., Wang L., Zhen J.Y.;
"Phosphorylation of human MAD1 by the BUB1 kinase in vitro.";
Biochem. Biophys. Res. Commun. 257:589-595(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, AND FUNCTION.
PubMed=10049595; DOI=10.1006/geno.1998.5654;
Jin D.-Y., Kozak C.A., Pangilinan F., Spencer F., Green E.D.,
Jeang K.-T.;
"Mitotic checkpoint locus MAD1L1 maps to human chromosome 7p22 and
mouse chromosome 5.";
Genomics 55:363-364(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Amygdala;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
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).
[7]
FUNCTION.
PubMed=12837246; DOI=10.1016/S0092-8674(03)00430-6;
Lin S.Y., Elledge S.J.;
"Multiple tumor suppressor pathways negatively regulate telomerase.";
Cell 113:881-889(2003).
[8]
SUBCELLULAR LOCATION, AND INTERACTION WITH NEK2.
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
INTERACTION WITH TPR AND MAD2L1, IDENTIFICATION BY MASS SPECTROMETRY,
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).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-428, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
INTERACTION WITH TPR.
PubMed=19273613; DOI=10.1083/jcb.200811012;
Lince-Faria M., Maffini S., Orr B., Ding Y., Florindo C., Sunkel C.E.,
Tavares A., Johansen J., Johansen K.M., Maiato H.;
"Spatiotemporal control of mitosis by the conserved spindle matrix
protein Megator.";
J. Cell Biol. 184:647-657(2009).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[17]
FUNCTION, INTERACTION WITH TPR, AND SUBCELLULAR LOCATION.
PubMed=20133940; DOI=10.1074/jbc.M110.105890;
Nakano H., Funasaka T., Hashizume C., Wong R.W.;
"Nucleoporin translocated promoter region (Tpr) associates with dynein
complex, preventing chromosome lagging formation during mitosis.";
J. Biol. Chem. 285:10841-10849(2010).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
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).
[20]
SUBCELLULAR LOCATION, AND INTERACTION WITH IK AND MAD2L1.
PubMed=22351768; DOI=10.1074/jbc.M111.299131;
Yeh P.C., Yeh C.C., Chen Y.C., Juang Y.L.;
"RED, a spindle pole-associated protein, is required for kinetochore
localization of MAD1, mitotic progression, and activation of the
spindle assembly checkpoint.";
J. Biol. Chem. 287:11704-11716(2012).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-428, 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).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-61, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-61, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[26]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 493-579 IN COMPLEX WITH
MAD2L1, AND COMPETITIVE INHIBITOR OF MAD2L1-CDC20 INTERACTION.
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).
[27]
VARIANTS HIS-558 AND HIS-572.
PubMed=10366450; DOI=10.1006/geno.1999.5831;
Cahill D.P., da Costa L.T., Carson-Walter E.B., Kinzler K.W.,
Vogelstein B., Lengauer C.;
"Characterization of MAD2B and other mitotic spindle checkpoint
genes.";
Genomics 58:181-187(1999).
[28]
VARIANT LUNG CANCER ALA-299, AND VARIANTS SER-160; MET-500; LYS-511;
HIS-556 AND HIS-558.
PubMed=10597320; DOI=10.1038/sj.onc.1203141;
Nomoto S., Haruki N., Takahashi T., Masuda A., Koshikawa T.,
Takahashi T., Fujii Y., Osada H., Takahashi T.;
"Search for in vivo somatic mutations in the mitotic checkpoint gene,
hMAD1, in human lung cancers.";
Oncogene 18:7180-7183(1999).
[29]
VARIANTS CANCER LEU-29; CYS-59; GLN-360; LYS-516; CYS-556 AND LYS-569,
AND VARIANTS MET-500 AND HIS-558.
PubMed=11423979; DOI=10.1038/sj.onc.1204421;
Tsukasaki K., Miller C.W., Greenspun E., Eshaghian S., Kawabata H.,
Fujimoto T., Tomonaga M., Sawyers C., Said J.W., Koeffler H.P.;
"Mutations in the mitotic check point gene, MAD1L1, in human
cancers.";
Oncogene 20:3301-3305(2001).
-!- FUNCTION: Component of the spindle-assembly checkpoint that
prevents the onset of anaphase until all chromosomes are properly
aligned at the metaphase plate. May recruit MAD2L1 to unattached
kinetochores. Has a role in the correct positioning of the septum.
Required for anchoring MAD2L1 to the nuclear periphery. Binds to
the TERT promoter and represses telomerase expression, possibly by
interfering with MYC binding. {ECO:0000269|PubMed:10049595,
ECO:0000269|PubMed:12837246, ECO:0000269|PubMed:20133940}.
-!- SUBUNIT: Homodimer. Heterodimerizes with MAD2L1 in order to form a
tetrameric MAD1L1-MAD2L1 core complex (PubMed:9546394,
PubMed:18981471, PubMed:22351768, PubMed:12006501). Perturbation
of the original MAD1L1-MAD2L1 structure by the spindle checkpoint
may decrease MAD2L1 affinity for MAD1L1. CDC20 can compete with
MAD1L1 for MAD2L1 binding, until the attachment and/or tension
dampen the checkpoint signal, preventing further release of MAD2L1
on to CDC20. Also able to interact with the BUB1/BUB3 complex
(PubMed:10198256). Interacts with NEK2 (PubMed:14978040).
Interacts with TPR; the interactions occurs in a microtubule-
independent manner (PubMed:18981471, PubMed:19273613,
PubMed:20133940). Interacts with IK (PubMed:22351768). Interacts
with the viral Tax protein (PubMed:9546394).
{ECO:0000269|PubMed:10198256, ECO:0000269|PubMed:12006501,
ECO:0000269|PubMed:14978040, ECO:0000269|PubMed:18981471,
ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:20133940,
ECO:0000269|PubMed:22351768, ECO:0000269|PubMed:9546394}.
-!- INTERACTION:
Self; NbExp=11; IntAct=EBI-742610, EBI-742610;
P09917:ALOX5; NbExp=8; IntAct=EBI-742610, EBI-79934;
P53933:APP1 (xeno); NbExp=3; IntAct=EBI-742610, EBI-28798;
Q9UL15:BAG5; NbExp=6; IntAct=EBI-742610, EBI-356517;
Q9BW85:CCDC94; NbExp=3; IntAct=EBI-742610, EBI-10300345;
Q8TD31-3:CCHCR1; NbExp=5; IntAct=EBI-742610, EBI-10175300;
Q02224-2:CENPE; NbExp=2; IntAct=EBI-742610, EBI-11108893;
Q2TBE0:CWF19L2; NbExp=5; IntAct=EBI-742610, EBI-5453285;
P39976:DLD3 (xeno); NbExp=3; IntAct=EBI-742610, EBI-5933;
P32571:DOA4 (xeno); NbExp=3; IntAct=EBI-742610, EBI-19840;
P32502:GCD7 (xeno); NbExp=3; IntAct=EBI-742610, EBI-6260;
Q96CS2:HAUS1; NbExp=3; IntAct=EBI-742610, EBI-2514791;
Q3ZCW2:LGALSL; NbExp=5; IntAct=EBI-742610, EBI-10241423;
Q13257:MAD2L1; NbExp=23; IntAct=EBI-742610, EBI-78203;
P55081:MFAP1; NbExp=5; IntAct=EBI-742610, EBI-1048159;
O76041:NEBL; NbExp=5; IntAct=EBI-742610, EBI-2880203;
Q03718:NSE5 (xeno); NbExp=3; IntAct=EBI-742610, EBI-27756;
P28004:PRP45 (xeno); NbExp=3; IntAct=EBI-742610, EBI-20640;
P25786:PSMA1; NbExp=3; IntAct=EBI-742610, EBI-359352;
O76064:RNF8; NbExp=5; IntAct=EBI-742610, EBI-373337;
Q9UM82:SPATA2; NbExp=3; IntAct=EBI-742610, EBI-744066;
P09493:TPM1; NbExp=6; IntAct=EBI-742610, EBI-351158;
P09493-10:TPM1; NbExp=5; IntAct=EBI-742610, EBI-12123928;
P06753:TPM3; NbExp=9; IntAct=EBI-742610, EBI-355607;
Q5VU62:TPM3; NbExp=3; IntAct=EBI-742610, EBI-10184033;
P12270:TPR; NbExp=2; IntAct=EBI-742610, EBI-1048528;
Q14134:TRIM29; NbExp=6; IntAct=EBI-742610, EBI-702370;
Q99576-3:TSC22D3; NbExp=3; IntAct=EBI-742610, EBI-10294415;
Q63HK5:TSHZ3; NbExp=3; IntAct=EBI-742610, EBI-9053916;
Q9Y4E8:USP15; NbExp=3; IntAct=EBI-742610, EBI-1043104;
I3L3J2:ZSCAN32; NbExp=3; IntAct=EBI-742610, EBI-10178206;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore
{ECO:0000269|PubMed:22351768}. Nucleus envelope
{ECO:0000269|PubMed:22351768}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome. Cytoplasm,
cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole
{ECO:0000269|PubMed:22351768}. Note=Detected at the nucleus
envelope during interphase (PubMed:22351768). From the beginning
to the end of mitosis, it is seen to move from a diffusely nuclear
distribution to the centrosome, to the spindle midzone and finally
to the midbody. Detected at kinetochores during prometaphase
(PubMed:22351768). Colocalizes with NEK2 at the kinetochore
(PubMed:14978040). Colocalizes with IK at spindle poles during
metaphase and anaphase (PubMed:22351768).
{ECO:0000269|PubMed:14978040, ECO:0000269|PubMed:22351768}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y6D9-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y6D9-3; Sequence=VSP_056160, VSP_056161;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed weakly at G0/G1 and highly at late S
and G2/M phase.
-!- INDUCTION: Increased by p53/TP53. {ECO:0000269|PubMed:10049595}.
-!- PTM: Phosphorylated; by BUB1. Become hyperphosphorylated in late S
through M phases or after mitotic spindle damage.
{ECO:0000269|PubMed:10198256, ECO:0000269|PubMed:9546394}.
-!- DISEASE: Note=Defects in MAD1L1 are involved in the development
and/or progression of various types of cancer.
{ECO:0000269|PubMed:10597320, ECO:0000269|PubMed:11423979}.
-!- SIMILARITY: Belongs to the MAD1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC52059.1; Type=Frameshift; Positions=663; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U33822; AAC52059.1; ALT_FRAME; mRNA.
EMBL; AF123318; AAD20359.1; -; mRNA.
EMBL; AF083811; AAD24498.1; -; mRNA.
EMBL; AK090959; BAG52253.1; -; mRNA.
EMBL; AC005282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC006433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC069288; AAS07503.1; -; Genomic_DNA.
EMBL; AC104129; AAP21876.1; -; Genomic_DNA.
EMBL; AC110781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC009964; AAH09964.1; -; mRNA.
CCDS; CCDS43539.1; -. [Q9Y6D9-1]
CCDS; CCDS78201.1; -. [Q9Y6D9-3]
RefSeq; NP_001013858.1; NM_001013836.1. [Q9Y6D9-1]
RefSeq; NP_001013859.1; NM_001013837.1. [Q9Y6D9-1]
RefSeq; NP_001291452.1; NM_001304523.1. [Q9Y6D9-1]
RefSeq; NP_001291453.1; NM_001304524.1. [Q9Y6D9-3]
RefSeq; NP_003541.2; NM_003550.2. [Q9Y6D9-1]
UniGene; Hs.654838; -.
PDB; 1GO4; X-ray; 2.05 A; E/F/G/H=485-584.
PDB; 4DZO; X-ray; 1.76 A; A/B=597-718.
PDBsum; 1GO4; -.
PDBsum; 4DZO; -.
ProteinModelPortal; Q9Y6D9; -.
SMR; Q9Y6D9; -.
BioGrid; 113971; 75.
ComplexPortal; CPX-82; Mitotic spindle assembly checkpoint Mad1 complex.
ComplexPortal; CPX-85; Mitotic spindle assembly checkpoint MAD1-MAD2 complex.
CORUM; Q9Y6D9; -.
DIP; DIP-29654N; -.
ELM; Q9Y6D9; -.
IntAct; Q9Y6D9; 75.
MINT; Q9Y6D9; -.
STRING; 9606.ENSP00000265854; -.
iPTMnet; Q9Y6D9; -.
PhosphoSitePlus; Q9Y6D9; -.
BioMuta; MAD1L1; -.
DMDM; 52783153; -.
EPD; Q9Y6D9; -.
PaxDb; Q9Y6D9; -.
PeptideAtlas; Q9Y6D9; -.
PRIDE; Q9Y6D9; -.
ProteomicsDB; 86656; -.
DNASU; 8379; -.
Ensembl; ENST00000265854; ENSP00000265854; ENSG00000002822. [Q9Y6D9-1]
Ensembl; ENST00000399654; ENSP00000382562; ENSG00000002822. [Q9Y6D9-1]
Ensembl; ENST00000402746; ENSP00000384155; ENSG00000002822. [Q9Y6D9-3]
Ensembl; ENST00000406869; ENSP00000385334; ENSG00000002822. [Q9Y6D9-1]
GeneID; 8379; -.
KEGG; hsa:8379; -.
UCSC; uc003slf.2; human. [Q9Y6D9-1]
CTD; 8379; -.
DisGeNET; 8379; -.
EuPathDB; HostDB:ENSG00000002822.15; -.
GeneCards; MAD1L1; -.
HGNC; HGNC:6762; MAD1L1.
HPA; CAB015338; -.
HPA; HPA003635; -.
MalaCards; MAD1L1; -.
MIM; 602686; gene.
neXtProt; NX_Q9Y6D9; -.
OpenTargets; ENSG00000002822; -.
PharmGKB; PA372; -.
eggNOG; KOG4593; Eukaryota.
eggNOG; ENOG410ZCEV; LUCA.
GeneTree; ENSGT00390000001316; -.
HOGENOM; HOG000004808; -.
HOVERGEN; HBG052441; -.
InParanoid; Q9Y6D9; -.
KO; K06638; -.
OMA; YMLLGYR; -.
OrthoDB; EOG091G0IXP; -.
PhylomeDB; Q9Y6D9; -.
TreeFam; TF101083; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
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; Q9Y6D9; -.
ChiTaRS; MAD1L1; human.
EvolutionaryTrace; Q9Y6D9; -.
GeneWiki; Mad1; -.
GenomeRNAi; 8379; -.
PRO; PR:Q9Y6D9; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000002822; -.
CleanEx; HS_MAD1L1; -.
ExpressionAtlas; Q9Y6D9; baseline and differential.
Genevisible; Q9Y6D9; HS.
GO; GO:0005813; C:centrosome; NAS:UniProtKB.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
GO; GO:0005819; C:spindle; NAS:UniProtKB.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043515; F:kinetochore binding; IDA:UniProtKB.
GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IBA:GO_Central.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007093; P:mitotic cell cycle checkpoint; NAS:UniProtKB.
GO; GO:0007094; P:mitotic spindle assembly checkpoint; IBA:GO_Central.
GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0090235; P:regulation of metaphase plate congression; IDA:UniProtKB.
GO; GO:0048538; P:thymus development; IEA:Ensembl.
InterPro; IPR008672; Mad1.
PANTHER; PTHR23168; PTHR23168; 1.
Pfam; PF05557; MAD; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle;
Cell division; Centromere; Chromosome; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Disease mutation; Isopeptide bond;
Kinetochore; Mitosis; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1 718 Mitotic spindle assembly checkpoint
protein MAD1.
/FTId=PRO_0000213800.
REGION 301 340 Important for interaction with IK.
{ECO:0000269|PubMed:22351768}.
REGION 380 532 Necessary for interaction with NEK2.
{ECO:0000269|PubMed:14978040}.
REGION 439 480 Important for interaction with IK.
{ECO:0000269|PubMed:22351768}.
COILED 46 632 {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 61 61 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 428 428 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CROSSLNK 61 61 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 65 MEDLGENTMVLSTLRSLNNFISQRVEGGSGLDISTSAPGSL
QMQYQQSMQLEERAEQIRSKSHLI -> MLPARGCVRKRTV
WPRLARVLIVTLLTLELSYAPLPCQLSGVPYNTGDPVGRWA
RPCIWPCPWHT (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056160.
VAR_SEQ 66 157 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056161.
VARIANT 29 29 S -> L (in a lymphoid cancer cell line;
somatic mutation).
{ECO:0000269|PubMed:11423979}.
/FTId=VAR_019707.
VARIANT 59 59 R -> C (in a prostate cancer cell line;
somatic mutation; dbSNP:rs121908982).
{ECO:0000269|PubMed:11423979}.
/FTId=VAR_019708.
VARIANT 160 160 N -> S (in dbSNP:rs550573452).
{ECO:0000269|PubMed:10597320}.
/FTId=VAR_019709.
VARIANT 299 299 T -> A (in lung cancer cell line; somatic
mutation). {ECO:0000269|PubMed:10597320}.
/FTId=VAR_019710.
VARIANT 360 360 R -> Q (in a prostate cancer cell line;
somatic mutation; dbSNP:rs769418574).
{ECO:0000269|PubMed:11423979}.
/FTId=VAR_019711.
VARIANT 500 500 T -> M (in dbSNP:rs193231481).
{ECO:0000269|PubMed:10597320,
ECO:0000269|PubMed:11423979}.
/FTId=VAR_019712.
VARIANT 511 511 E -> K (in dbSNP:rs377555260).
{ECO:0000269|PubMed:10597320}.
/FTId=VAR_019713.
VARIANT 516 516 E -> K (in a breast cancer cell line;
somatic mutation).
{ECO:0000269|PubMed:11423979}.
/FTId=VAR_019714.
VARIANT 556 556 R -> C (in a prostate cancer cell line;
somatic mutation; dbSNP:rs371561369).
{ECO:0000269|PubMed:11423979}.
/FTId=VAR_019715.
VARIANT 556 556 R -> H (in one individual with lung
cancer; dbSNP:rs755012008).
{ECO:0000269|PubMed:10597320}.
/FTId=VAR_019716.
VARIANT 558 558 R -> H (in a cancer cell line;
dbSNP:rs1801368).
{ECO:0000269|PubMed:10366450,
ECO:0000269|PubMed:10597320,
ECO:0000269|PubMed:11423979}.
/FTId=VAR_019717.
VARIANT 569 569 E -> K (in a breast cancer cell line;
somatic mutation; dbSNP:rs201951163).
{ECO:0000269|PubMed:11423979}.
/FTId=VAR_019718.
VARIANT 572 572 R -> H (in a cancer cell line;
dbSNP:rs1801500).
{ECO:0000269|PubMed:10366450}.
/FTId=VAR_019719.
CONFLICT 189 190 EL -> DV (in Ref. 1; AAC52059 and 3;
AAD24498). {ECO:0000305}.
CONFLICT 260 260 K -> E (in Ref. 1; AAC52059 and 3;
AAD24498). {ECO:0000305}.
CONFLICT 268 268 Missing (in Ref. 1; AAC52059).
{ECO:0000305}.
HELIX 487 492 {ECO:0000244|PDB:1GO4}.
HELIX 494 528 {ECO:0000244|PDB:1GO4}.
TURN 537 539 {ECO:0000244|PDB:1GO4}.
STRAND 540 547 {ECO:0000244|PDB:1GO4}.
HELIX 549 575 {ECO:0000244|PDB:1GO4}.
TURN 580 582 {ECO:0000244|PDB:1GO4}.
HELIX 599 637 {ECO:0000244|PDB:4DZO}.
STRAND 638 644 {ECO:0000244|PDB:4DZO}.
TURN 645 647 {ECO:0000244|PDB:4DZO}.
STRAND 648 653 {ECO:0000244|PDB:4DZO}.
STRAND 663 667 {ECO:0000244|PDB:4DZO}.
STRAND 675 678 {ECO:0000244|PDB:4DZO}.
HELIX 683 685 {ECO:0000244|PDB:4DZO}.
HELIX 687 693 {ECO:0000244|PDB:4DZO}.
HELIX 700 715 {ECO:0000244|PDB:4DZO}.
SEQUENCE 718 AA; 83067 MW; DA65529856A37EE3 CRC64;
MEDLGENTMV LSTLRSLNNF ISQRVEGGSG LDISTSAPGS LQMQYQQSMQ LEERAEQIRS
KSHLIQVERE KMQMELSHKR ARVELERAAS TSARNYEREV DRNQELLTRI RQLQEREAGA
EEKMQEQLER NRQCQQNLDA ASKRLREKED SLAQAGETIN ALKGRISELQ WSVMDQEMRV
KRLESEKQEL QEQLDLQHKK CQEANQKIQE LQASQEARAD HEQQIKDLEQ KLSLQEQDAA
IVKNMKSELV RLPRLERELK QLREESAHLR EMRETNGLLQ EELEGLQRKL GRQEKMQETL
VGLELENERL LAKLQSWERL DQTMGLSIRT PEDLSRFVVE LQQRELALKD KNSAVTSSAR
GLEKARQQLQ EELRQVSGQL LEERKKRETH EALARRLQKR VLLLTKERDG MRAILGSYDS
ELTPAEYSPQ LTRRMREAED MVQKVHSHSA EMEAQLSQAL EELGGQKQRA DMLEMELKML
KSQSSSAEQS FLFSREEADT LRLKVEELEG ERSRLEEEKR MLEAQLERRA LQGDYDQSRT
KVLHMSLNPT SVARQRLRED HSQLQAECER LRGLLRAMER GGTVPADLEA AAASLPSSKE
VAELKKQVES AELKNQRLKE VFQTKIQEFR KACYTLTGYQ IDITTENQYR LTSLYAEHPG
DCLIFKATSP SGSKMQLLET EFSHTVGELI EVHLRRQDSI PAFLSSLTLE LFSRQTVA


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