ACM1_YEAST
ID ACM1_YEAST Reviewed; 209 AA.
AC Q08981; D6W3A3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=APC/C-CDH1 modulator 1;
GN Name=ACM1; OrderedLocusNames=YPL267W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
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 [5]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, AND INTERACTION
RP WITH CDH1; BMH1 AND BMH2.
RX PubMed=17030612; DOI=10.1128/mcb.00603-06;
RA Martinez J.S., Jeong D.-E., Choi E., Billings B.M., Hall M.C.;
RT "Acm1 is a negative regulator of the CDH1-dependent anaphase-promoting
RT complex/cyclosome in budding yeast.";
RL Mol. Cell. Biol. 26:9162-9176(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-161 AND SER-202, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161 AND SER-202, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP 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: Negative regulator of GDH1, the activator protein that
CC regulates the ubiquitin ligase activity and substrate specificity of
CC the anaphase promoting complex/cyclosome (APC/C), and which is required
CC for exit from mitosis, cytokinesis and formation of prereplicative
CC complexes in G1. {ECO:0000269|PubMed:17030612}.
CC -!- SUBUNIT: Interacts with CDH1, BMH1 and BMH2.
CC {ECO:0000269|PubMed:17030612}.
CC -!- INTERACTION:
CC Q08981; P53197: CDH1; NbExp=8; IntAct=EBI-2345174, EBI-23684;
CC -!- INDUCTION: Expressed very quickly after G1 release, just prior to
CC initiation of DNA replication. {ECO:0000269|PubMed:17030612}.
CC -!- MISCELLANEOUS: Present with 688 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z73623; CAA98002.1; -; Genomic_DNA.
DR EMBL; AY558139; AAS56465.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11169.1; -; Genomic_DNA.
DR PIR; S65300; S65300.
DR RefSeq; NP_015056.1; NM_001184081.1.
DR PDB; 4BH6; X-ray; 2.90 A; I/J/K/L/M/N/O/P=59-128.
DR PDBsum; 4BH6; -.
DR AlphaFoldDB; Q08981; -.
DR SMR; Q08981; -.
DR BioGRID; 35946; 78.
DR DIP; DIP-8871N; -.
DR ELM; Q08981; -.
DR IntAct; Q08981; 6.
DR MINT; Q08981; -.
DR STRING; 4932.YPL267W; -.
DR iPTMnet; Q08981; -.
DR PaxDb; Q08981; -.
DR PRIDE; Q08981; -.
DR EnsemblFungi; YPL267W_mRNA; YPL267W; YPL267W.
DR GeneID; 855861; -.
DR KEGG; sce:YPL267W; -.
DR SGD; S000006188; ACM1.
DR VEuPathDB; FungiDB:YPL267W; -.
DR eggNOG; ENOG502S399; Eukaryota.
DR HOGENOM; CLU_111692_0_0_1; -.
DR InParanoid; Q08981; -.
DR OMA; SPAKICP; -.
DR BioCyc; YEAST:G3O-34150-MON; -.
DR PRO; PR:Q08981; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08981; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0055105; F:ubiquitin-protein transferase inhibitor activity; IDA:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IDA:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Mitosis; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..209
FT /note="APC/C-CDH1 modulator 1"
FT /id="PRO_0000268174"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT HELIX 68..84
FT /evidence="ECO:0007829|PDB:4BH6"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:4BH6"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:4BH6"
SQ SEQUENCE 209 AA; 23870 MW; 0646D4E3AD41758C CRC64;
MISPSKKRTI LSSKNINQKP RAVVKGNELR SPSKRRSQID TDYALRRSPI KTIQISKAAQ
FMLYEETAEE RNIAVHRHNE IYNNNNSVSN ENNPSQVKEN LSPAKICPYE RAFLREGGRI
ALKDLSVDEF KGYIQDPLTD ETIPLTLPLG DKKISLPSFI TPPRNSKISI FFTSKHQGQN
PETKISRSTD DVSEKKVVRK LSFHVYEDE
