MSI1_YEAST
ID MSI1_YEAST Reviewed; 422 AA.
AC P13712; D6VQI9;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Chromatin assembly factor 1 subunit p50;
DE Short=CAF-1 p50 subunit;
DE AltName: Full=IRA1 multicopy suppressor;
DE AltName: Full=Protein MSI1;
GN Name=MSI1; Synonyms=CAC3; OrderedLocusNames=YBR195C; ORFNames=YBR1405;
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=2554329; DOI=10.1073/pnas.86.22.8778;
RA Ruggieri R., Tanaka K., Nakafuku M., Kaziro Y., Toh-e A., Matsumoto K.;
RT "MSI1, a negative regulator of the RAS-cAMP pathway in Saccharomyces
RT cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8778-8782(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8346681; DOI=10.1002/yea.320090611;
RA Demolis N., Mallet L., Bussereau F., Jacquet M.;
RT "RIM2, MSI1 and PGI1 are located within an 8 kb segment of Saccharomyces
RT cerevisiae chromosome II, which also contains the putative ribosomal gene
RT L21 and a new putative essential gene with a leucine zipper motif.";
RL Yeast 9:645-659(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 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 [6]
RP PROTEIN SEQUENCE OF 7-27; 32-43 AND 414-422, AND CHARACTERIZATION.
RX PubMed=9030687; DOI=10.1101/gad.11.3.345;
RA Kaufman P.D., Kobayashi R., Stillman B.;
RT "Ultraviolet radiation sensitivity and reduction of telomeric silencing in
RT Saccharomyces cerevisiae cells lacking chromatin assembly factor-I.";
RL Genes Dev. 11:345-357(1997).
RN [7]
RP FUNCTION, INTERACTION WITH NPR1, AND SUBCELLULAR LOCATION.
RX PubMed=11238915; DOI=10.1128/mcb.21.5.1784-1794.2001;
RA Johnston S.D., Enomoto S., Schneper L., McClellan M.C., Twu F.,
RA Montgomery N.D., Haney S.A., Broach J.R., Berman J.;
RT "CAC3(MSI1) suppression of RAS2(G19V) is independent of chromatin assembly
RT factor I and mediated by NPR1.";
RL Mol. Cell. Biol. 21:1784-1794(2001).
RN [8]
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 [9]
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 [10]
RP INTERACTION WITH RTT106.
RX PubMed=19683497; DOI=10.1016/j.molcel.2009.06.023;
RA Fillingham J., Kainth P., Lambert J.P., van Bakel H., Tsui K.,
RA Pena-Castillo L., Nislow C., Figeys D., Hughes T.R., Greenblatt J.,
RA Andrews B.J.;
RT "Two-color cell array screen reveals interdependent roles for histone
RT chaperones and a chromatin boundary regulator in histone gene repression.";
RL Mol. Cell 35:340-351(2009).
CC -!- FUNCTION: Acts as a component of chromatin assembly factor 1 (CAF-1),
CC which assembles histone octamers onto replicating DNA in vitro. It
CC performs the first step of the nucleosome assembly process, bringing
CC newly synthesized histones H3 and H4 to replicating DNA; histones
CC H2A/H2B can bind to this chromatin precursor subsequent to DNA
CC replication to complete the histone octamer. p50 and p60 form complexes
CC with newly synthesized histones H3 and acetylated H4 in cell extracts
CC (By similarity). Independently, MSI1 is involved in regulation of the
CC RAS/cAMP pathway via sequestration of NPR1. {ECO:0000250,
CC ECO:0000269|PubMed:11238915}.
CC -!- SUBUNIT: Interacts with protein kinase NPR1 (PubMed:11238915).
CC Component of chromatin assembly factor 1 (CAF-1), which is composed of
CC MSI1/p50, CAC2/p60 and CAC1/p90 (PubMed:11238915). Interacts with
CC RTT106 (PubMed:19683497). {ECO:0000269|PubMed:11238915,
CC ECO:0000269|PubMed:19683497}.
CC -!- INTERACTION:
CC P13712; Q04199: CAC2; NbExp=3; IntAct=EBI-11391, EBI-3920;
CC P13712; Q12495: RLF2; NbExp=5; IntAct=EBI-11391, EBI-3913;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11238915}. Nucleus
CC {ECO:0000269|PubMed:11238915}.
CC -!- MISCELLANEOUS: Present with 149 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
CC {ECO:0000305}.
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DR EMBL; M27300; AAA34804.1; -; Genomic_DNA.
DR EMBL; Z21487; CAA79682.1; -; Genomic_DNA.
DR EMBL; Z36064; CAA85157.1; -; Genomic_DNA.
DR EMBL; AY692834; AAT92853.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07309.1; -; Genomic_DNA.
DR PIR; S07865; BVBYMS.
DR RefSeq; NP_009754.1; NM_001178543.1.
DR AlphaFoldDB; P13712; -.
DR SMR; P13712; -.
DR BioGRID; 32892; 160.
DR ComplexPortal; CPX-568; Chromatin assembly factor 1 complex.
DR DIP; DIP-338N; -.
DR IntAct; P13712; 16.
DR MINT; P13712; -.
DR STRING; 4932.YBR195C; -.
DR iPTMnet; P13712; -.
DR MaxQB; P13712; -.
DR PaxDb; P13712; -.
DR PRIDE; P13712; -.
DR EnsemblFungi; YBR195C_mRNA; YBR195C; YBR195C.
DR GeneID; 852494; -.
DR KEGG; sce:YBR195C; -.
DR SGD; S000000399; MSI1.
DR VEuPathDB; FungiDB:YBR195C; -.
DR eggNOG; KOG0264; Eukaryota.
DR GeneTree; ENSGT00940000168296; -.
DR HOGENOM; CLU_020445_3_1_1; -.
DR InParanoid; P13712; -.
DR OMA; DSYLCIW; -.
DR BioCyc; YEAST:G3O-29137-MON; -.
DR Reactome; R-SCE-3214815; HDACs deacetylate histones.
DR Reactome; R-SCE-3214847; HATs acetylate histones.
DR Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR PRO; PR:P13712; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P13712; protein.
DR GO; GO:0033186; C:CAF-1 complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0033698; C:Rpd3L complex; IBA:GO_Central.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; IBA:GO_Central.
DR GO; GO:0031497; P:chromatin assembly; IDA:ComplexPortal.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IC:ComplexPortal.
DR GO; GO:0006260; P:DNA replication; IC:ComplexPortal.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IDA:SGD.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR022052; Histone-bd_RBBP4_N.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12265; CAF1C_H4-bd; 1.
DR Pfam; PF08662; eIF2A; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW cAMP; Cytoplasm; Direct protein sequencing; Nucleus; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..422
FT /note="Chromatin assembly factor 1 subunit p50"
FT /id="PRO_0000051086"
FT REPEAT 127..158
FT /note="WD 1"
FT REPEAT 198..238
FT /note="WD 2"
FT REPEAT 249..289
FT /note="WD 3"
FT REPEAT 294..334
FT /note="WD 4"
FT REPEAT 338..379
FT /note="WD 5"
FT REPEAT 382..421
FT /note="WD 6"
SQ SEQUENCE 422 AA; 47365 MW; 0D3DB6CB2AC74166 CRC64;
MNQCAKDITH EASSIPIDLQ ERYSHWKKNT KLLYDYLNTN STKWPSLTCQ FFPDLDTTSD
EHRILLSSFT SSQKPEDETI YISKISTLGH IKWSSLNNFD MDEMEFKPEN STRFPSKHLV
NDISIFFPNG ECNRARYLPQ NPDIIAGASS DGAIYIFDRT KHGSTRIRQS KISHPFETKL
FGSHGVIQDV EAMDTSSADI NEATSLAWNL QQEALLLSSH SNGQVQVWDI KQYSHENPII
DLPLVSINSD GTAVNDVTWM PTHDSLFAAC TEGNAVSLLD LRTKKEKLQS NREKHDGGVN
SCRFNYKNSL ILASADSNGR LNLWDIRNMN KSPIATMEHG TSVSTLEWSP NFDTVLATAG
QEDGLVKLWD TSCEETIFTH GGHMLGVNDI SWDAHDPWLM CSVANDNSVH IWKPAGNLVG
HS
