ID MAD1_YEAST Reviewed; 749 AA.
AC P40957; D6VU58;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 195.
DE RecName: Full=Spindle assembly checkpoint component MAD1;
DE AltName: Full=Mitotic arrest deficient protein 1;
GN Name=MAD1; OrderedLocusNames=YGL086W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 200060 / W303;
RX PubMed=7593191; DOI=10.1083/jcb.131.3.709;
RA Hardwick K.G., Murray A.W.;
RT "Mad1p, a phosphoprotein component of the spindle assembly checkpoint in
RT budding yeast.";
RL J. Cell Biol. 131:709-720(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP PHOSPHORYLATION BY MPS1.
RX PubMed=8688079; DOI=10.1126/science.273.5277.953;
RA Hardwick K.G., Weiss E., Luca F.C., Winey M., Murray A.W.;
RT "Activation of the budding yeast spindle assembly checkpoint without
RT mitotic spindle disruption.";
RL Science 273:953-956(1996).
RN [6]
RP INTERACTION WITH MAD2.
RX PubMed=10436016; DOI=10.1091/mbc.10.8.2607;
RA Chen R.H., Brady D.M., Smith D., Murray A.W., Hardwick K.G.;
RT "The spindle checkpoint of budding yeast depends on a tight complex between
RT the Mad1 and Mad2 proteins.";
RL Mol. Biol. Cell 10:2607-2618(1999).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH BUB1 AND BUB3, AND MUTAGENESIS OF
RP 653-ARG--LYS-655.
RX PubMed=10837255; DOI=10.1016/s0960-9822(00)00515-7;
RA Brady D.M., Hardwick K.G.;
RT "Complex formation between Mad1p, Bub1p and Bub3p is crucial for spindle
RT checkpoint function.";
RL Curr. Biol. 10:675-678(2000).
RN [8]
RP INTERACTION WITH BUB3.
RX PubMed=11726501; DOI=10.1093/emboj/20.23.6648;
RA Fraschini R., Beretta A., Sironi L., Musacchio A., Lucchini G., Piatti S.;
RT "Bub3 interaction with Mad2, Mad3 and Cdc20 is mediated by WD40 repeats and
RT does not require intact kinetochores.";
RL EMBO J. 20:6648-6659(2001).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-502, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Central component of the spindle assembly checkpoint. Thought
CC to recruit MAD2 to unattached kinetochores. During checkpoint activity,
CC MAD2 is relayed from the MAD1-MAD2 complex to the mitotic checkpoint
CC complex (MCC). The formation of a MAD1-BUB1-BUB3 complex seems to be
CC required for the spindle checkpoint mechanism.
CC -!- SUBUNIT: Forms a stable heteromer with MAD2 throughout the cell cycle.
CC Part of complex consisting of MAD1, BUB1 and BUB3 after activation of
CC spindle checkpoint. {ECO:0000269|PubMed:10837255}.
CC -!- INTERACTION:
CC P40957; P41695: BUB1; NbExp=5; IntAct=EBI-10354, EBI-3816;
CC P40957; P26449: BUB3; NbExp=4; IntAct=EBI-10354, EBI-3830;
CC P40957; P40958: MAD2; NbExp=6; IntAct=EBI-10354, EBI-10362;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Becomes hyperphosphorylated when wild-type cells are arrested in
CC mitosis. Phosphorylated by MPS1. {ECO:0000269|PubMed:8688079}.
CC -!- MISCELLANEOUS: Present with 656 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MAD1 family. {ECO:0000305}.
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DR EMBL; U14632; AAA91620.1; -; Genomic_DNA.
DR EMBL; Z72608; CAA96791.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08019.1; -; Genomic_DNA.
DR PIR; A57276; A57276.
DR RefSeq; NP_011429.3; NM_001180951.3.
DR AlphaFoldDB; P40957; -.
DR SMR; P40957; -.
DR BioGRID; 33164; 453.
DR ComplexPortal; CPX-3212; Mitotic checkpoint complex, MAD1-MAD2-BUB1-BUB3 subcomplex.
DR ComplexPortal; CPX-961; Mitotic spindle assembly checkpoint, MAD1-MAD2 complex.
DR DIP; DIP-293N; -.
DR ELM; P40957; -.
DR IntAct; P40957; 12.
DR MINT; P40957; -.
DR STRING; 4932.YGL086W; -.
DR iPTMnet; P40957; -.
DR MaxQB; P40957; -.
DR PaxDb; 4932-YGL086W; -.
DR PeptideAtlas; P40957; -.
DR EnsemblFungi; YGL086W_mRNA; YGL086W; YGL086W.
DR GeneID; 852794; -.
DR KEGG; sce:YGL086W; -.
DR AGR; SGD:S000003054; -.
DR SGD; S000003054; MAD1.
DR VEuPathDB; FungiDB:YGL086W; -.
DR eggNOG; KOG4593; Eukaryota.
DR HOGENOM; CLU_026595_0_0_1; -.
DR InParanoid; P40957; -.
DR OMA; YKLDFMP; -.
DR OrthoDB; 2787310at2759; -.
DR BioCyc; YEAST:G3O-30587-MONOMER; -.
DR BioGRID-ORCS; 852794; 0 hits in 10 CRISPR screens.
DR PRO; PR:P40957; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P40957; Protein.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
DR GO; GO:0090268; P:activation of mitotic cell cycle spindle assembly checkpoint; IMP:SGD.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044774; P:mitotic DNA integrity checkpoint signaling; IGI:SGD.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IDA:ComplexPortal.
DR GO; GO:1901925; P:negative regulation of protein import into nucleus during spindle assembly checkpoint; IMP:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IGI:SGD.
DR Gene3D; 3.30.457.60; -; 1.
DR InterPro; IPR008672; Mad1.
DR PANTHER; PTHR23168:SF0; MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD1; 1.
DR PANTHER; PTHR23168; MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD1 MITOTIC ARREST DEFICIENT-LIKE PROTEIN 1; 1.
DR Pfam; PF05557; MAD; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..749
FT /note="Spindle assembly checkpoint component MAD1"
FT /id="PRO_0000213798"
FT REGION 39..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 57..324
FT /evidence="ECO:0000255"
FT COILED 390..656
FT /evidence="ECO:0000255"
FT COMPBIAS 333..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 502
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 653..655
FT /note="RLK->AAA: Abolishes interaction with BUB1 and BUB3
FT and spindle checkpoint function."
FT /evidence="ECO:0000269|PubMed:10837255"
SQ SEQUENCE 749 AA; 87651 MW; 312DDE1BE241610D CRC64;
MDVRAALQCF FSALSGRFTG KKLGLEIYSI QYKMSNSGGS SPFLESPGGS PDVGSTNGQS
NRQIQALQFK LNTLQNEYEI EKLQLQKQTN ILEKKYKATI DELEKALNDT KYLYESNDKL
EQELKSLKER SANSMNDKDK CIEELRTTLQ NKDLEMETLR QQYDSKLSKV TNQCDHFKLE
AESSHSLLMK YEKEIKRQSV DIKDLQHQVM EKDDELSSVK ASKMINSHPN YSTEEFNELT
EMNKMIQDQV QYTKELELAN MQQANELKKL KQSQDTSTFW KLENEKLQNK LSQLHVLESQ
YENLQLENID LKSKLTKWEI YNDSDDDDDN NVNNNDNNNN NKNDNNNDNN NDTSNNNNIN
NNNRTKNNIR NNPEEIIRDW KLTKKECLIL TDMNDKLRLD NNNLKLLNDE MALERNQILD
LNKNYENNIV NLKRLNHELE QQKSLSFEEC RLLREQLDGL YSAQNNALLE VENSETHASN
KNVNEDMNNL IDTYKNKTED LTNELKKLND QLLSNSNDVE TQRKKRKLTS DQIGLNYSQR
LNELQLENVS VSRELSKAQT TIQLLQEKLE KLTKLKEKKI RILQLRDGPF IKDQFIKKNK
LLLLEKENAD LLNELKKNNP AVETVPISVY DSLNFELKQF EQEVFKSNKR FSRLKQVFNN
KSLEFIDVVN SLLGFKLEFQ QDSRVKIFSC FKPEKYLIAD LNENTLKSNL DADIEGWDDL
MNLWVEDRGQ LPCFLATITL RLWEQRQAK
//
