MAK21_YEAST
ID MAK21_YEAST Reviewed; 1025 AA.
AC Q12176; D6VS46;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Ribosome biogenesis protein MAK21;
DE AltName: Full=Maintenance of killer protein 21;
DE AltName: Full=Nucleolar complex protein 1;
GN Name=MAK21; Synonyms=NOC1; OrderedLocusNames=YDR060W;
GN ORFNames=D4237, YD9609.14;
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 204508 / S288c;
RX PubMed=8789263;
RX DOI=10.1002/(sici)1097-0061(199601)12:1<85::aid-yea890>3.0.co;2-u;
RA Brandt P., Ramlow S., Otto B., Bloecker H.;
RT "Nucleotide sequence analysis of a 32,500 bp region of the right arm of
RT Saccharomyces cerevisiae chromosome IV.";
RL Yeast 12:85-90(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 CHARACTERIZATION.
RX PubMed=9786894; DOI=10.1074/jbc.273.44.28912;
RA Edskes H.K., Ohtake Y., Wickner R.B.;
RT "Mak21p of Saccharomyces cerevisiae, a homolog of human CAATT-binding
RT protein, is essential for 60 S ribosomal subunit biogenesis.";
RL J. Biol. Chem. 273:28912-28920(1998).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NOC2.
RX PubMed=11371346; DOI=10.1016/s0092-8674(01)00358-0;
RA Milkereit P., Gadal O., Podtelejnikov A., Trumtel S., Gas N., Petfalski E.,
RA Tollervey D., Mann M., Hurt E., Tschochner H.;
RT "Maturation and intranuclear transport of pre-ribosomes requires Noc
RT proteins.";
RL Cell 105:499-509(2001).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-73; SER-977 AND
RP SER-978, AND 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-73; SER-80; TYR-708;
RP SER-710 AND SER-878, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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-73; SER-275; SER-710;
RP SER-874; SER-878 AND SER-1024, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
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: Required for 60S ribosomal subunit synthesis.
CC {ECO:0000269|PubMed:11371346}.
CC -!- SUBUNIT: Interacts with NOC2. Forms a nucleolar complex with NOC2 that
CC binds to 90S and 66S pre-ribosomes. {ECO:0000269|PubMed:11371346}.
CC -!- INTERACTION:
CC Q12176; Q12389: DBP10; NbExp=3; IntAct=EBI-10944, EBI-5644;
CC Q12176; Q03532: HAS1; NbExp=3; IntAct=EBI-10944, EBI-8170;
CC Q12176; P43586: LOC1; NbExp=3; IntAct=EBI-10944, EBI-22906;
CC Q12176; Q12176: MAK21; NbExp=3; IntAct=EBI-10944, EBI-10944;
CC Q12176; P39744: NOC2; NbExp=8; IntAct=EBI-10944, EBI-29259;
CC Q12176; Q02892: NOG1; NbExp=3; IntAct=EBI-10944, EBI-12105;
CC Q12176; P53742: NOG2; NbExp=3; IntAct=EBI-10944, EBI-28532;
CC Q12176; P37838: NOP4; NbExp=6; IntAct=EBI-10944, EBI-12122;
CC Q12176; P40693: RLP7; NbExp=3; IntAct=EBI-10944, EBI-15415;
CC Q12176; P36160: RPF2; NbExp=5; IntAct=EBI-10944, EBI-15881;
CC Q12176; Q12754: RRP12; NbExp=3; IntAct=EBI-10944, EBI-30678;
CC Q12176; Q06511: RRP15; NbExp=4; IntAct=EBI-10944, EBI-34602;
CC Q12176; Q05022: RRP5; NbExp=7; IntAct=EBI-10944, EBI-16011;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11371346}.
CC -!- MISCELLANEOUS: Present with 15000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CBF/MAK21 family. {ECO:0000305}.
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DR EMBL; X84162; CAA58976.1; -; Genomic_DNA.
DR EMBL; Z74356; CAA98878.1; -; Genomic_DNA.
DR EMBL; Z49209; CAA89089.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11906.1; -; Genomic_DNA.
DR PIR; S54044; S54044.
DR RefSeq; NP_010345.3; NM_001180368.3.
DR AlphaFoldDB; Q12176; -.
DR BioGRID; 32115; 471.
DR ComplexPortal; CPX-1733; NOC1-NOC2 pre-ribosome maturation complex.
DR DIP; DIP-4040N; -.
DR IntAct; Q12176; 103.
DR MINT; Q12176; -.
DR STRING; 4932.YDR060W; -.
DR iPTMnet; Q12176; -.
DR MaxQB; Q12176; -.
DR PaxDb; Q12176; -.
DR PRIDE; Q12176; -.
DR EnsemblFungi; YDR060W_mRNA; YDR060W; YDR060W.
DR GeneID; 851632; -.
DR KEGG; sce:YDR060W; -.
DR SGD; S000002467; MAK21.
DR VEuPathDB; FungiDB:YDR060W; -.
DR eggNOG; KOG2038; Eukaryota.
DR GeneTree; ENSGT00390000006395; -.
DR HOGENOM; CLU_003417_0_0_1; -.
DR InParanoid; Q12176; -.
DR OMA; GNHIQYS; -.
DR BioCyc; YEAST:G3O-29668-MON; -.
DR PRO; PR:Q12176; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12176; protein.
DR GO; GO:0030690; C:Noc1p-Noc2p complex; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IDA:ComplexPortal.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR005612; CCAAT-binding_factor.
DR InterPro; IPR040155; CEBPZ/Mak21-like.
DR PANTHER; PTHR12048; PTHR12048; 1.
DR Pfam; PF03914; CBF; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1025
FT /note="Ribosome biogenesis protein MAK21"
FT /id="PRO_0000173472"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..1001
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 COMPBIAS 37..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..878
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..927
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..956
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 708
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 1024
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1025 AA; 116677 MW; FB80378727ED71D8 CRC64;
MSENNGNPLD LSSLRNKISS KLRDNNSKKA KKTHKGKDVK ASSNSKKVNE DIRREALALG
ASEEDLKLIQ GLSDDDDAKS EQEFDAVADE DADDKGFKND LQNFMKNVGF DQHKLEDVDD
DDIEEESTSS KESKIPAQEK EHAQSNIASS TIEKTSQESI DNGSEQEENT VEEANLSSDQ
EPESESAEKE KKEEKDGGLI TQTTIISSDK LIIPYDKPWY EIPLDPQVGQ NDDVEELSKE
QIEKLFERGK QTLEADNQTY YEEFTKDSSQ AKFMSQILSD GTLNDKISAV TLLIQDSPLH
NTKSLETLVS YCGKKSRNSA LQSLNALKDL FLNGLLPNRK LRYFKNQPGL SMMLNKKTLA
IFYFEDYLKK LFFRVLEVLE VLSHDPIIHV RLQILNHVFD LLTNQPEQEF NLLRLGVNKI
GDIDSKVSSK ASYLLLKLEQ AHPNMKSIVI DAIVDIALRP NADYHTTYYS VITLNQTILK
RSEDSVANKL VKTYFTLFEK FLINTDKDNT NGVVKSNSKS YEEKRKKNFK KGKHGGKSVK
IEKTENEVLD EKNSKLFSAL LTGINRAFPF AQIPASVYEV HMETLFKITH SSNFNTSIQA
LVLINQVTVK AKLNSDRYYR TLYESLFDPR LVNSSKQGIY LNLLYKSLKQ DALNVERVEA
FVKRILQVCS HWLNVGTITG FFFLLIQLAK TVPQIKNLLT NTPVDYEYES DAEEEQGDKD
IKRKEYDGRK RDPKFANAEK SSLWEINNFI NHFHPTVKTY ANAYVTGETE QIAKPDLGLF
TLSHFLDRFV YRSAKQTNTA RGTSIMQPLF SGSRVNDSVL VKASDIMHDQ GPVNTEDWLT
KKVEDIKPED KFFYQYFTTK KTADGKGKKS NKASNFDSDD EMDENEIWSA LVKSRPDVED
DSDDSELDFA EDDFSDSTSD DEPKLDAIDD EDAKSEGSQE SDQEEGLDED IFYSFDGEQD
NSDKKRSFAE SSEEDESSEE EKEEEENKEV SAKRAKKKQR KNMLKSLPVF ASADDYAQYL
DQDSD
