MAK11_YEAST
ID MAK11_YEAST Reviewed; 414 AA.
AC P20484; D6VXR4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Protein MAK11;
DE AltName: Full=Maintenance of killer protein 11;
GN Name=MAK11; OrderedLocusNames=YKL021C;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2826479; DOI=10.1016/s0021-9258(19)57326-4;
RA Icho T., Wickner R.B.;
RT "The MAK11 protein is essential for cell growth and replication of M
RT double-stranded RNA and is apparently a membrane-associated protein.";
RL J. Biol. Chem. 263:1467-1475(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 FUNCTION.
RX PubMed=7739558; DOI=10.1128/mcb.15.5.2772;
RA Ohtake Y., Wickner R.B.;
RT "Yeast virus propagation depends critically on free 60S ribosomal subunit
RT concentration.";
RL Mol. Cell. Biol. 15:2772-2781(1995).
RN [5]
RP INTERACTION WITH 60S PRE-RIBOSOMAL PARTICLES, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12374754; DOI=10.1093/emboj/cdf547;
RA Nissan T.A., Bassler J., Petfalski E., Tollervey D., Hurt E.;
RT "60S pre-ribosome formation viewed from assembly in the nucleolus until
RT export to the cytoplasm.";
RL EMBO J. 21:5539-5547(2002).
RN [6]
RP FUNCTION, INTERACTION WITH 60S PRE-RIBOSOMAL PARTICLES, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=12808088; DOI=10.1128/mcb.23.13.4449-4460.2003;
RA Saveanu C., Namane A., Gleizes P.-E., Lebreton A., Rousselle J.-C.,
RA Noaillac-Depeyre J., Gas N., Jacquier A., Fromont-Racine M.;
RT "Sequential protein association with nascent 60S ribosomal particles.";
RL Mol. Cell. Biol. 23:4449-4460(2003).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376 AND SER-380, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376; SER-380 AND THR-382, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376 AND SER-380, 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).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Essential for cell growth. Plays a role in assembly of 60S
CC pre-ribosomal particles in the nucleolus. Also required for replication
CC of the M1 double-stranded RNA of the L-A virus. This latter function
CC may reflect an enhanced requirement for free 60S ribosomal particles
CC for the translation of viral mRNAs which lack poly-A tails.
CC {ECO:0000269|PubMed:12808088, ECO:0000269|PubMed:2826479,
CC ECO:0000269|PubMed:7739558}.
CC -!- SUBUNIT: Associates with 60S pre-ribosomal particles.
CC -!- INTERACTION:
CC P20484; Q06511: RRP15; NbExp=3; IntAct=EBI-10930, EBI-34602;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:2826479}.
CC Nucleus membrane {ECO:0000269|PubMed:2826479}; Peripheral membrane
CC protein {ECO:0000269|PubMed:2826479}. Note=Membrane associated.
CC -!- MISCELLANEOUS: Present with 3730 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34750.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA81856.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA09134.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J03506; AAA34750.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z28021; CAA81856.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006944; DAA09134.1; ALT_INIT; Genomic_DNA.
DR PIR; A29938; A29938.
DR RefSeq; NP_012904.3; NM_001179587.3.
DR AlphaFoldDB; P20484; -.
DR SMR; P20484; -.
DR BioGRID; 34110; 543.
DR DIP; DIP-6516N; -.
DR IntAct; P20484; 19.
DR STRING; 4932.YKL021C; -.
DR iPTMnet; P20484; -.
DR PaxDb; P20484; -.
DR PRIDE; P20484; -.
DR GeneID; 853847; -.
DR KEGG; sce:YKL021C; -.
DR SGD; S000001504; MAK11.
DR eggNOG; KOG0294; Eukaryota.
DR HOGENOM; CLU_031466_2_0_1; -.
DR InParanoid; P20484; -.
DR BioCyc; YEAST:G3O-31829-MON; -.
DR PRO; PR:P20484; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P20484; protein.
DR GO; GO:0016020; C:membrane; IDA:SGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
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; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribosome biogenesis; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..414
FT /note="Protein MAK11"
FT /id="PRO_0000051079"
FT REPEAT 50..78
FT /note="WD 1"
FT REPEAT 90..135
FT /note="WD 2"
FT REPEAT 147..177
FT /note="WD 3"
FT REPEAT 189..221
FT /note="WD 4"
FT REPEAT 238..267
FT /note="WD 5"
FT REPEAT 298..330
FT /note="WD 6"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 382
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 414 AA; 47291 MW; B3BD72C4E37ACF11 CRC64;
MSAIGDKNQF RIIVGSYEHN ILCLSLDIPN QKENDAAKTP HFMPIFHFQA HSLSIKCLAV
SRRYLVSGSN DEHIRIYDLQ KRKELGTLLS HQGSITALQF SHPASSSEDA AVSKGSKNSK
WLLSASEDHK IMVWRVKDWE TVGTLKGHTA RVNDVDIHPT NRIAISVSDD HSIRLWNLMT
LRNAAVLKLR KYNTNGTCVR WLGAKGDYFA VGLRDRVLIY ETGSAKVFKE IVFQRKTLMH
IETHILPFDN KEYLSVGISD GNVHFYPCEE LFEKVEENEK QEDDDDKEDI SPAFSLLGHT
NRIKDFKFYT NEFGTYLVTI GSDGKIVVWD MSTKEQVAVY DCGERLNCLT LCDESIEKYN
TMKKRDAETA DIGDQSEVES DTEELKKIMF GEKKKLNKKK RKQLKKSKVS VELE
