MSA1_YEAST
ID MSA1_YEAST Reviewed; 629 AA.
AC Q08471; D6W2C9; O00026;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=G1-specific transcription factors activator MSA1;
DE AltName: Full=MBF and SBF-associated protein 1;
GN Name=MSA1; OrderedLocusNames=YOR066W; ORFNames=YOR29-17;
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 96604 / S288c / FY1679;
RX PubMed=9133743;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g;
RA Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.;
RT "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT presence of two tRNAs and 24 new open reading frames.";
RL Yeast 13:379-390(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
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 [5]
RP PHOSPHORYLATION BY CDC28.
RX PubMed=14574415; DOI=10.1038/nature02062;
RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA Shokat K.M., Morgan D.O.;
RT "Targets of the cyclin-dependent kinase Cdk1.";
RL Nature 425:859-864(2003).
RN [6]
RP FUNCTION.
RX PubMed=16464826; DOI=10.1093/nar/gkj493;
RA Titz B., Thomas S., Rajagopala S.V., Chiba T., Ito T., Uetz P.;
RT "Transcriptional activators in yeast.";
RL Nucleic Acids Res. 34:955-967(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH MBP1; SWI6;
RP SBF AND MBF COMPLEXES, AND DEVELOPMENTAL STAGE.
RX PubMed=18160399; DOI=10.1074/jbc.m708248200;
RA Ashe M., de Bruin R.A.M., Kalashnikova T., McDonald W.H., Yates J.R. III,
RA Wittenberg C.;
RT "The SBF- and MBF-associated protein Msa1 is required for proper timing of
RT G1-specific transcription in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 283:6040-6049(2008).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, 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: Activator of G1-specific transcription factors, MBF and SBF.
CC Promotes both the timing of G1-specific gene transcription and cell
CC cycle initiation. Associates with SBF- and MBF-regulated target
CC promoters and this binding is maximal during the G1 phase, prior to
CC maximum budding. Affects cell cycle initiation by advancing the timing
CC of transcription of G1-specific genes. Overexpression advances the
CC timing of SBF-dependent transcription and budding. Depletion delays
CC both indicators of cell cycle initiation. {ECO:0000269|PubMed:16464826,
CC ECO:0000269|PubMed:18160399}.
CC -!- SUBUNIT: Interacts with transcription complexes SCB-binding factor
CC (SBF) and MCB-binding factor (MBF) at their target promoters. Interacts
CC with MBP1 and SWI6. {ECO:0000269|PubMed:18160399}.
CC -!- DEVELOPMENTAL STAGE: Expressed periodically during the cell cycle with
CC peak mRNA levels occurring at the late M/early G1 phase, prior to
CC budding, and levels decrease rapidly as cells enter into the S phase.
CC In early G1 peak occurs (at protein level).
CC {ECO:0000269|PubMed:18160399}.
CC -!- PTM: Phosphorylated by CDC28. {ECO:0000269|PubMed:14574415}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z70678; CAA94551.1; -; Genomic_DNA.
DR EMBL; Z74974; CAA99259.1; -; Genomic_DNA.
DR EMBL; AY692621; AAT92640.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10845.1; -; Genomic_DNA.
DR PIR; S66949; S66949.
DR RefSeq; NP_014709.1; NM_001183485.1.
DR AlphaFoldDB; Q08471; -.
DR BioGRID; 34465; 93.
DR DIP; DIP-2714N; -.
DR IntAct; Q08471; 5.
DR MINT; Q08471; -.
DR STRING; 4932.YOR066W; -.
DR iPTMnet; Q08471; -.
DR MaxQB; Q08471; -.
DR PaxDb; Q08471; -.
DR PRIDE; Q08471; -.
DR EnsemblFungi; YOR066W_mRNA; YOR066W; YOR066W.
DR GeneID; 854232; -.
DR KEGG; sce:YOR066W; -.
DR SGD; S000005592; MSA1.
DR VEuPathDB; FungiDB:YOR066W; -.
DR eggNOG; ENOG502QUYM; Eukaryota.
DR HOGENOM; CLU_027374_0_0_1; -.
DR InParanoid; Q08471; -.
DR OMA; IQQTMNG; -.
DR BioCyc; YEAST:G3O-33606-MON; -.
DR PRO; PR:Q08471; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08471; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IMP:SGD.
PE 1: Evidence at protein level;
KW Activator; Cell cycle; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..629
FT /note="G1-specific transcription factors activator MSA1"
FT /id="PRO_0000237651"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 629 AA; 68691 MW; 302204DCC8ECFD0D CRC64;
MDKSMIKKRG RPPITKDYPN PLQSPMAHSS MQVQKQGPHS FAKPLMKVGQ SSPSPNKRRL
SIDHHHNLAA TTRKGRYRGV LLSTPTKKSS TNGSTPISTP SSNDSYNNTV FSETRKTFLQ
SSPPIMTSSP AFQKKNDYMF PSQEQFKLSL TITESGKAVI AGSLPFSPSS KSSHLMNNNN
KKIMQNEKIH KGSKKNAPKF EKRRILSLLK QMKNEKYCDT DTLPEAPPAK PSRSDIIDTE
LPTIIETSAS PIGSARNNNI LLSQPPQSPP SSAQLKPPST PKSSLQFRMG FTPNVALNSV
SLSDTISKST NAVGASNNNN QNGNSISNIA DANTLLTLTN SPGVFLSPRN KMLPKSTTAS
NEQQQEFVFK FSSGDPLLLT DDADGNWPEM LFNVSNTPRR QKCFNTPPSW INFGSPGLFS
PPRSSNVMVN GTTVATASDS GNVHRQLQAQ LEAQVQVQSQ SNSPTQRQQQ QRQFQIPPPH
INMNSSPPQI NIASPPHQSM SRVSSIYFNK EKTTTGVANM LGNTKSENLQ PPANLFTAAH
GPSTPRNQEF QLPTLIECTP LIQQTMNGSL GTKYIPGTSI SNSATPNLHG FPVGTGKAPS
SFDDSLKQNP YSNKQDDART ALKRLIDDQ
