MSB1_YEAST
ID MSB1_YEAST Reviewed; 1137 AA.
AC P21339; D6W2P4;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Morphogenesis-related protein MSB1;
DE AltName: Full=Multicopy suppressor of bud emergence 1;
GN Name=MSB1; OrderedLocusNames=YOR188W;
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].
RX PubMed=1996092; DOI=10.1128/mcb.11.3.1295-1305.1991;
RA Bender A., Pringle J.R.;
RT "Use of a screen for synthetic lethal and multicopy suppressee mutants to
RT identify two new genes involved in morphogenesis in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 11:1295-1305(1991).
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 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538 AND SER-816, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538 AND SER-776, AND
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: May play a role in polarity establishment and bud formation.
CC The MSB1 gene may be functionally redundant.
CC -!- INTERACTION:
CC P21339; P40073: SHO1; NbExp=2; IntAct=EBI-11322, EBI-18140;
CC -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M37767; AAA34797.1; -; Genomic_DNA.
DR EMBL; Z75096; CAA99397.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10960.1; -; Genomic_DNA.
DR PIR; S13759; S13759.
DR RefSeq; NP_014831.3; NM_001183607.3.
DR AlphaFoldDB; P21339; -.
DR BioGRID; 34583; 78.
DR DIP; DIP-2687N; -.
DR IntAct; P21339; 5.
DR MINT; P21339; -.
DR STRING; 4932.YOR188W; -.
DR iPTMnet; P21339; -.
DR MaxQB; P21339; -.
DR PaxDb; P21339; -.
DR PRIDE; P21339; -.
DR EnsemblFungi; YOR188W_mRNA; YOR188W; YOR188W.
DR GeneID; 854360; -.
DR KEGG; sce:YOR188W; -.
DR SGD; S000005714; MSB1.
DR VEuPathDB; FungiDB:YOR188W; -.
DR eggNOG; ENOG502QUEY; Eukaryota.
DR HOGENOM; CLU_004952_0_0_1; -.
DR InParanoid; P21339; -.
DR OMA; LETHLEM; -.
DR BioCyc; YEAST:G3O-33698-MON; -.
DR PRO; PR:P21339; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P21339; protein.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; IGI:SGD.
DR InterPro; IPR037508; Msb1/Mug8.
DR InterPro; IPR012965; Msb1/Mug8_dom.
DR PANTHER; PTHR28093; PTHR28093; 1.
DR Pfam; PF08101; DUF1708; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1137
FT /note="Morphogenesis-related protein MSB1"
FT /id="PRO_0000096588"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
SQ SEQUENCE 1137 AA; 129971 MW; 59CDD6E0F1E43F8A CRC64;
MNDMAKPLPT PPTAEIRKSR SNSPKKAQKT NLSPNKNQNN EKNVPRSNGR TKNEHNSMDD
EEFEFFHQFS REKVKGVIHV ITAELKEKGP DVEFLMIPFR PEQTNDKLLT LLNQLFPLGN
GQPVNEKKQL RIVSKADVWT LFQCLKYIWC RLPNSEIIGW KSYLEFKFRE EDKKFPRKSF
LEIMPQCLAS PNHASIVYDF FDLIISISSN SRVNKMSARK ISKMCAIWAF SKQIPNSDIQ
DYDFESAAMK SFAPNNSIQD GLDQWIPASD AMFHLLLAFL RSFVPQDLES AKLPRTLKSL
LFNNQYPPRK STAYTSETIL TIPLVTLKTD VFSRKPWQLL ERCNDLLDFS DHDAFEARED
YALLKSLFRK KNTVEGISRK MSQESRRLMK AMSTKHSTFQ PGWAPRECIE NISHLKECIE
VKRLDIDDYF IWTWLSSLSF EQTSEKKKIF GRSIILEFEF DGFKKWVVFQ ECDITLDYNK
KGQLKKKTSA QSPTTEKELP PDDFELEDPP LSKSPTLSQT YKKFQAEVPQ QSTVRRDSAP
DNQGIYHTVI SKNALTKNKH NVNLHSFEHK ISKWNPLNNL RKKSGSNSSS SSFEEKSKDA
PIREEYHTNK NHKSKKEERV LSQFSTLNPD EYQLPVIETG SSNFKIEIPE LMYEHDDDDS
DKLKNSQKRA TDSAIEELNG MVEEMMINEP DDVKISITEA ETFESLTKFD QYKPSNITDD
DLQSSHSSAV HSLKLSTNTN DSCADSSKYT ADRKLAEPRK ISEESKVNDD SSSYYSPNIN
NLPASRMPSQ PTYSNSDSKK AFTNESRLNV LQGAVSPSQQ VTPKPYKNAP GDCVSPVQQK
YYQNDRRNEM SPASAPVPPS AYSPARSPQF STNSAGFKQN TINVPVGYND PAHVLANQPH
MTYRDQHNYP SHQQKQRPFQ NNIVPPELKS RNQRADASPI PQHMVPVKQG VPNLPSNVPL
YQQMERMNPN HQHPVNTYKV TQPPYHNNTT NAYGNSRAGN AHMLDGKWSN NPPQMVPKGV
RPNQYPQQHV NRYSPQAQPV VPAEYYNGPP PMRAPPMMSH MVPAQEPIRY TAGANRRSFP
QGMQQNAYSV PAQPMGAVNS EFYLPEAPQG NKLHGNINKR QERKKLYDNI RSGNFGI
