NOC3_YEAST
ID NOC3_YEAST Reviewed; 663 AA.
AC Q07896; D6VY04; Q92280;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Nucleolar complex-associated protein 3;
GN Name=NOC3; OrderedLocusNames=YLR002C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 443-663.
RC STRAIN=ATCC 90840 / EAY235 / FY23;
RX PubMed=8810043;
RX DOI=10.1002/(sici)1097-0061(19960615)12:7<693::aid-yea956>3.0.co;2-g;
RA Miosga T., Zimmermann F.K.;
RT "Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on a
RT 43.7 kb fragment of chromosome XII including an open reading frame
RT homologous to the human cystic fibrosis transmembrane conductance regulator
RT protein CFTR.";
RL Yeast 12:693-708(1996).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP INTERACTION WITH NOC2 AND 66S PRE-RIBOSOMAL PARTICLES.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN 60S
RP PRE-RIBOSOMAL PARTICLES.
RX PubMed=11583615; DOI=10.1016/s1097-2765(01)00342-2;
RA Bassler J., Grandi P., Gadal O., Lessmann T., Petfalski E., Tollervey D.,
RA Lechner J., Hurt E.;
RT "Identification of a 60S preribosomal particle that is closely linked to
RT nuclear export.";
RL Mol. Cell 8:517-529(2001).
RN [6]
RP FUNCTION, AND INTERACTION WITH MCM2; MCM5 AND ORC1.
RX PubMed=12110182; DOI=10.1016/s0092-8674(02)00805-x;
RA Zhang Y., Yu Z., Fu X., Liang C.;
RT "Noc3p, a bHLH protein, plays an integral role in the initiation of DNA
RT replication in budding yeast.";
RL Cell 109:849-860(2002).
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-395, AND IDENTIFICATION BY
RP 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 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: Required for synthesis of 60S ribosomal subunits and the
CC transport of pre-ribosomes from the nucleoplasm to the cytoplasm. Also
CC required for initiation of DNA replication. May function downstream of
CC the origin recognition complex (ORC complex) in the loading of CDC6 and
CC the minichromosome maintenance complex (MCM complex) onto chromatin
CC during the G1 phase of the cell cycle. Essential for growth.
CC {ECO:0000269|PubMed:11371346, ECO:0000269|PubMed:12110182}.
CC -!- SUBUNIT: Forms a heterodimer with NOC2. This complex may be associated
CC with pre-ribosomal particles. Also interacts with MCM2, MCM5 and ORC1.
CC {ECO:0000269|PubMed:11371346, ECO:0000269|PubMed:11583615,
CC ECO:0000269|PubMed:12110182}.
CC -!- INTERACTION:
CC Q07896; P39744: NOC2; NbExp=7; IntAct=EBI-36093, EBI-29259;
CC Q07896; P25582: SPB1; NbExp=3; IntAct=EBI-36093, EBI-17814;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11371346}.
CC -!- MISCELLANEOUS: Present with 11700 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; Z73174; CAA97524.1; -; Genomic_DNA.
DR EMBL; X91488; CAA62771.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09320.1; -; Genomic_DNA.
DR PIR; S64824; S64824.
DR RefSeq; NP_013102.1; NM_001181889.1.
DR PDB; 6ELZ; EM; 3.30 A; I=1-663.
DR PDB; 6EM5; EM; 4.30 A; I=1-663.
DR PDB; 7OHR; EM; 4.72 A; I=1-663.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 7OHR; -.
DR AlphaFoldDB; Q07896; -.
DR SMR; Q07896; -.
DR BioGRID; 31275; 275.
DR ComplexPortal; CPX-1734; NOC2-NOC3 pre-ribosome maturation complex.
DR DIP; DIP-4839N; -.
DR IntAct; Q07896; 28.
DR MINT; Q07896; -.
DR STRING; 4932.YLR002C; -.
DR iPTMnet; Q07896; -.
DR MaxQB; Q07896; -.
DR PaxDb; Q07896; -.
DR PRIDE; Q07896; -.
DR EnsemblFungi; YLR002C_mRNA; YLR002C; YLR002C.
DR GeneID; 850688; -.
DR KEGG; sce:YLR002C; -.
DR SGD; S000003992; NOC3.
DR VEuPathDB; FungiDB:YLR002C; -.
DR eggNOG; KOG2153; Eukaryota.
DR GeneTree; ENSGT00390000008540; -.
DR HOGENOM; CLU_012441_3_1_1; -.
DR InParanoid; Q07896; -.
DR OMA; FGNMANF; -.
DR BioCyc; YEAST:G3O-32163-MON; -.
DR PRO; PR:Q07896; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07896; protein.
DR GO; GO:0030691; C:Noc2p-Noc3p complex; IDA:SGD.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IDA:SGD.
DR GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IMP:SGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IDA:ComplexPortal.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IDA:SGD.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR005612; CCAAT-binding_factor.
DR InterPro; IPR011501; Noc3_N.
DR InterPro; IPR016903; Nucleolar_cplx-assoc_3.
DR PANTHER; PTHR14428; PTHR14428; 1.
DR Pfam; PF03914; CBF; 1.
DR Pfam; PF07540; NOC3p; 1.
DR PIRSF; PIRSF028977; Nucleolar_complex_p3; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Coiled coil; DNA replication;
KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..663
FT /note="Nucleolar complex-associated protein 3"
FT /id="PRO_0000173483"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 363..408
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..127
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 663 AA; 75582 MW; 4CA9461A4A1F1E9E CRC64;
MAKRNRSQFR IQERTAKKRK HEDSLLEGNV FQNAPEDMDE NTIYSAKGSS WDEEEQDYEM
VPRKNRSDTS NLVEGLPIKV NGKVERKLHK AQEKPKDDDE EDEDSNDSSE DDEGPNEEQE
AEAKEDEPDT EEKILQLKED IADLVTKVME EPEENTAALG RLCKMVESKN PNTCKFSMLA
LVPVFKSIIP GYRIRPLTET EKKEKVSKEV SKLRNFEQAL VYNYKNYVGR LQSLSKTPSN
AAPIQVSLGI LATQAAKELI STASHFNFRT DIFTLLLRRI CKPRISTDPT SIQIIQTFET
LLNEDEEGSI SFEILRIFNK ILKTRNFNIE ESVLNMLLSL DVLHDYDPNT KLKGNVSAPK
LKKKDRVHLS KKQRKARKEM QQIEEEMRNA EQAVSAEERE RNQSEILKIV FTIYLNILKN
NAKTLIGSVL EGLTKFGNMA NFDLLGDFLE VMKELISDTE FDNLSSAEVR KALLCIVSAF
SLISNTQYMK VNVDLSKFVD GLYALLPYIC LDADIELSYR SLRLADPLNN EIIKPSVNVS
TKAELLLKAL DHVFFRSKSG TKERATAFTK RLYMCISHTP EKTSIAILKF IDKLMNRYPE
ISGLYSSEDR IGNGHFIMEA DNPSRSNPEA ATLWDNALLE KHYCPVVTKG LRSLSSRSKE
CSK
