MAD2L1
entrez
4085
canonical
uniprot
Q13257
canonical
ensembl
ENSG00000164109
resolver
ensp
ENSP00000296509
resolver
genesymbol
MAD2L1
resolver
genesymbol_syn
MAD2
resolver
hgnc
HGNC:6763
resolver
uniprot
Q53F56
resolver
uniprot
Q548X9
resolver
uniprot
Q6IRW7
resolver
uniprot
Q8IZX3
resolver
uniprot_entry
MD2L1_HUMAN
resolver
uniprot_sec
Q53F56
resolver
uniprot_sec
Q548X9
resolver
uniprot_sec
Q6IRW7
resolver
uniprot_sec
Q8IZX3
resolver
amino_acid_sequence
MALQLSREQGITLRGSAEIVAEFFSFGINSILYQRGIYPSETFTRVQKYGLTLLVTTDLELIKYLNNVVEQLKDWLYKCSVQKLVVVISNIESGEVLERWQFDIECDKTAKDDSAPREKSQKAIQDEIRSVIRQITATVTFLPLLEVSCSFDLLIYTDKDLVVPEKWEESGPQFITNSEEVRLRSFTTTIHKVNSMVAYKIPVND
uniprot
proteins
function
FUNCTION: Component of the mitotic checkpoint complex (MCC), which inhibits APC/C and delays chromosome segregation until all chromosomes are properly attached to the mitotic spindle (PubMed:10700282, PubMed:11804586, PubMed:15024386, PubMed:29162720, PubMed:27509861). The MCC, which consists of CDC20, MAD2L1/MAD2, BUB1B/BUBR1 and BUB3, is a key player of the spindle assembly checkpoint (PubMed:15020684, PubMed:27509861). The MCC-bound APC/C complex is inactive and this delays the metaphase/anaphase transition (PubMed:27509861). When the spindle assembly checkpoint is silenced, the MCC-APC/C complex recruits the E2 enzyme UBCH10 and triggers the auto-ubiquitination of CDC20 in the MCC, thereby reactivating APC/C for transition into anaphase (PubMed:27509861). In the closed conformation (C-MAD2) forms a heterotetrameric complex with MAD1L1 at unattached kinetochores during prometaphase, the complex recruits open conformation molecules of MAD2L1 (O-MAD2) and then promotes the conversion of O-MAD2 to C-MAD2 (PubMed:29162720). {ECO:0000269|PubMed:10700282, ECO:0000269|PubMed:11804586, ECO:0000269|PubMed:15024386, ECO:0000269|PubMed:27509861, ECO:0000269|PubMed:29162720}.
uniprot
proteins
mass_dalton
23510
uniprot
proteins
mutagenesis
MUTAGEN 13; /note="L->A: Leads to formation the closed conformation and homodimerization. Reduces binding to MAD1L1."; /evidence="ECO:0000269|PubMed:18318601, ECO:0000269|PubMed:29162720"; MUTAGEN 75; /note="W->A: Prevents interaction with CDC20 and leads to formation of the closed conformation; when associated with A-133."; /evidence="ECO:0000269|PubMed:18318601"; MUTAGEN 133; /note="R->A: Prevents aggregation and promotes formation of monomeric protein that slowly interconverts between the open and closed conformation."; /evidence="ECO:0000269|PubMed:12006501"; MUTAGEN 153; /note="L->A: Leads to formation of the closed conformation; when associated with A-133."; /evidence="ECO:0000269|PubMed:18318601"; MUTAGEN 156; /note="Y->A: Leads to formation of the closed conformation; when associated with A-133."; /evidence="ECO:0000269|PubMed:18318601"; MUTAGEN 170; /note="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."; /evidence="ECO:0000269|PubMed:12574116"; MUTAGEN 170; /note="S->D: Abolishes interaction with MAD1L1 and reduces interaction with CDC20; when associated with D-178 and D-195."; /evidence="ECO:0000269|PubMed:12574116"; MUTAGEN 178; /note="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."; /evidence="ECO:0000269|PubMed:12574116"; MUTAGEN 178; /note="S->D: Abolishes interaction with MAD1L1 and reduces interaction with CDC20; when associated with D-170 and D-195."; /evidence="ECO:0000269|PubMed:12574116"; MUTAGEN 186; /note="F->A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133."; /evidence="ECO:0000269|PubMed:18318601"; MUTAGEN 188; /note="T->A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133."; /evidence="ECO:0000269|PubMed:18318601"; MUTAGEN 191; /note="H->A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133."; /evidence="ECO:0000269|PubMed:18318601"; MUTAGEN 195; /note="S->A: Abolishes phosphorylation on serine residues; when associated with A-170 and A-178."; /evidence="ECO:0000269|PubMed:12574116"; MUTAGEN 195; /note="S->D: Binds to the N and C-terminus of MAD1L1. Abolishes interaction with MAD1L1 and reduces interaction with CDC20; when associated with D-170 and D-178."; /evidence="ECO:0000269|PubMed:12574116, ECO:0000269|PubMed:29162720"; MUTAGEN 197; /note="V->A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133."; /evidence="ECO:0000269|PubMed:18318601"; MUTAGEN 199; /note="Y->A: Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133."; /evidence="ECO:0000269|PubMed:18318601
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on multiple serine residues (PubMed:12574116). The level of phosphorylation varies during the cell cycle and is highest during mitosis (PubMed:12574116). Phosphorylation abolishes interaction with MAD1L1 and reduces interaction with CDC20 (PubMed:12574116). Phosphorylated by NEK2 (PubMed:20034488). {ECO:0000269|PubMed:12574116, ECO:0000269|PubMed:20034488}.
uniprot
proteins
protein_family
MAD2 family
uniprot
proteins
pubmed
10527948
uniprot
proteins
pubmed
10700282
uniprot
proteins
pubmed
11390010
uniprot
proteins
pubmed
11804586
uniprot
proteins
pubmed
12006501
uniprot
proteins
pubmed
12456649
uniprot
proteins
pubmed
12574116
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14978040
uniprot
proteins
pubmed
15020684
uniprot
proteins
pubmed
15024386
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16495226
uniprot
proteins
pubmed
18022367
uniprot
proteins
pubmed
18022368
uniprot
proteins
pubmed
18318601
uniprot
proteins
pubmed
18712773
uniprot
proteins
pubmed
18794143
uniprot
proteins
pubmed
18981471
uniprot
proteins
pubmed
19010891
uniprot
proteins
pubmed
19029339
uniprot
proteins
pubmed
20034488
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25422469
uniprot
proteins
pubmed
27509861
uniprot
proteins
pubmed
29162720
uniprot
proteins
pubmed
8824189
uniprot
proteins
pubmed
9637688
uniprot
proteins
sequence_length
205
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19010891}. Chromosome, centromere, kinetochore. Cytoplasm {ECO:0000269|PubMed:19010891}. 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. Sequestered to the cytoplasm upon interaction with isoform 3 of MAD1L1 (PubMed:19010891). {ECO:0000269|PubMed:19010891, ECO:0000305}.
uniprot
proteins