NOC2_YEAST
ID NOC2_YEAST Reviewed; 710 AA.
AC P39744; D6W2R2; Q08625;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Nucleolar complex protein 2;
GN Name=NOC2; OrderedLocusNames=YOR206W; ORFNames=YOX001;
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] OF 151-710.
RX PubMed=2263475; DOI=10.1093/nar/18.23.7137;
RA Choi I.S., Kim J.B., Park S.D.;
RT "Nucleotide sequence of RAD4 gene of Saccharomyces cerevisiae that can be
RT propagated in Escherichia coli without inactivation.";
RL Nucleic Acids Res. 18:7137-7137(1990).
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MAK21 AND NOC3.
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 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-149; SER-160;
RP SER-166; SER-698 AND SER-708, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-149, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-160; SER-698 AND
RP SER-708, AND 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: Involved in the intranuclear transport of ribosomal
CC precursors. {ECO:0000269|PubMed:11371346}.
CC -!- SUBUNIT: Interacts with MAK21/NOC1 and NOC3. Forms a nucleolar complex
CC with MAK21 that binds to 90S and 66S pre-ribosomes, as well as a
CC nuclear complex with NOC3 that binds to 66S pre-ribosomes.
CC {ECO:0000269|PubMed:11371346}.
CC -!- INTERACTION:
CC P39744; Q08235: BRX1; NbExp=4; IntAct=EBI-29259, EBI-3775;
CC P39744; Q12389: DBP10; NbExp=5; IntAct=EBI-29259, EBI-5644;
CC P39744; P36049: EBP2; NbExp=3; IntAct=EBI-29259, EBI-6289;
CC P39744; Q04660: ERB1; NbExp=8; IntAct=EBI-29259, EBI-28098;
CC P39744; Q03532: HAS1; NbExp=3; IntAct=EBI-29259, EBI-8170;
CC P39744; P43586: LOC1; NbExp=6; IntAct=EBI-29259, EBI-22906;
CC P39744; P10962: MAK16; NbExp=3; IntAct=EBI-29259, EBI-10937;
CC P39744; Q12176: MAK21; NbExp=8; IntAct=EBI-29259, EBI-10944;
CC P39744; Q07896: NOC3; NbExp=7; IntAct=EBI-29259, EBI-36093;
CC P39744; Q08208: NOP12; NbExp=3; IntAct=EBI-29259, EBI-35895;
CC P39744; P37838: NOP4; NbExp=4; IntAct=EBI-29259, EBI-12122;
CC P39744; P53261: NOP7; NbExp=3; IntAct=EBI-29259, EBI-13145;
CC P39744; P40078: NSA2; NbExp=3; IntAct=EBI-29259, EBI-22681;
CC P39744; P40693: RLP7; NbExp=3; IntAct=EBI-29259, EBI-15415;
CC P39744; P38805: RPF1; NbExp=3; IntAct=EBI-29259, EBI-24614;
CC P39744; P36160: RPF2; NbExp=6; IntAct=EBI-29259, EBI-15881;
CC P39744; P35178: RRP1; NbExp=3; IntAct=EBI-29259, EBI-16002;
CC P39744; Q05022: RRP5; NbExp=4; IntAct=EBI-29259, EBI-16011;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11371346}.
CC -!- MISCELLANEOUS: Present with 29000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NOC2 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be RAD4.
CC {ECO:0000305|PubMed:2263475}.
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DR EMBL; X55891; CAA39375.1; -; Genomic_DNA.
DR EMBL; Z75114; CAA99421.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10978.1; -; Genomic_DNA.
DR PIR; S67098; S67098.
DR RefSeq; NP_014849.3; NM_001183625.3.
DR AlphaFoldDB; P39744; -.
DR BioGRID; 34601; 172.
DR ComplexPortal; CPX-1733; NOC1-NOC2 pre-ribosome maturation complex.
DR ComplexPortal; CPX-1734; NOC2-NOC3 pre-ribosome maturation complex.
DR DIP; DIP-4559N; -.
DR IntAct; P39744; 69.
DR MINT; P39744; -.
DR STRING; 4932.YOR206W; -.
DR iPTMnet; P39744; -.
DR MaxQB; P39744; -.
DR PaxDb; P39744; -.
DR PRIDE; P39744; -.
DR EnsemblFungi; YOR206W_mRNA; YOR206W; YOR206W.
DR GeneID; 854381; -.
DR KEGG; sce:YOR206W; -.
DR SGD; S000005732; NOC2.
DR VEuPathDB; FungiDB:YOR206W; -.
DR eggNOG; KOG2256; Eukaryota.
DR GeneTree; ENSGT00390000010057; -.
DR HOGENOM; CLU_011272_0_0_1; -.
DR InParanoid; P39744; -.
DR OMA; FPLRFHC; -.
DR BioCyc; YEAST:G3O-33710-MON; -.
DR PRO; PR:P39744; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P39744; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0030690; C:Noc1p-Noc2p complex; IDA:SGD.
DR GO; GO:0030691; C:Noc2p-Noc3p complex; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
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; IPR005343; Noc2.
DR PANTHER; PTHR12687; PTHR12687; 1.
DR Pfam; PF03715; Noc2; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..710
FT /note="Nucleolar complex protein 2"
FT /id="PRO_0000121054"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 151..179
FT /note="DEGEDAERNSNIEEKSEQMELEKEKIELS -> MKVKMLKETVILKKNLNKW
FT SWKRKKLSFL (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 231..232
FT /note="FH -> LD (in Ref. 1; CAA39375)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="E -> Q (in Ref. 1; CAA39375)"
FT /evidence="ECO:0000305"
FT CONFLICT 360..362
FT /note="TTY -> QRT (in Ref. 1; CAA39375)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="D -> H (in Ref. 1; CAA39375)"
FT /evidence="ECO:0000305"
FT CONFLICT 707..710
FT /note="MSDA -> NVRRLTTQQDLIFCLEFNSIVYKCVNKRKVFFKAYISLCSHVLT
FT CEHSKLSLVSWIFLYFGRFMDRKHVKRSMDLIKSNDVKQGTKMKEVRFTVIKFSKSFNS
FT LKVPHEIDMIANITENFSTRYMISYCWKISSNLNLGAMFMDNNSWNNSFAAYGIVILII
FT FSALLQVVHQPL (in Ref. 1; CAA39375)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 710 AA; 81601 MW; 48C3B9AE076B9B8F CRC64;
MGKVSKSTKK FQSKHLKHTL DQRRKEKIQK KRIQGRRGNK TDQEKADAAG TREQQQLKKS
AKEEVFKDMS VETFFEKGIE IPKENKKLKK KTTKEQSDED SSSSEEEEDM GQSMAKLAEK
DPEFYKYLEE NDKDLLDFAG TNPLDGIDSQ DEGEDAERNS NIEEKSEQME LEKEKIELSL
KLVRKWKKQL HDSPSLKLLR NIISAFKVAV NLNKEENIED YKYAITDEKA FHELMFMVLK
DVPQAIQKMA PYKIVKGART LPNGGNVSRV SSIVKSHAGS LLILLNDITN TETAALVLHS
VNELMPYLLS YRRILKELIK SIVGVWSTTR ELETQIASFA FLINTTKEFK KSMLETTLKT
TYSTFIKSCR KTNMRSMPLI NFQKNSAAEL FGIDEVLGYQ VGFEYIRQLA IHLRNTMNAT
TKKSSKINSA EAYKIVYNWQ FCHSLDFWSR VLSFACQPEK ENGSESPLRQ LIYPLVQVTL
GVIRLIPTPQ FFPLRFYLIK SLIRLSQNSG VFIPIYPLLS EILTSTAFTK APKKSPNLAA
FDFEHNIKCT QAYLNTKIYQ EGLSEQFVDL LGDYFALYCK NIAFPELVTP VIISLRRYIK
TSTNVKLNKR LSTVVEKLNQ NSTFIQEKRS DVEFGPTNKS EVSRFLNDVA WNKTPLGSYV
AVQREVKEEK ARLMRESMEE QDKERETEEA KLLNSLESDD DNEDVEMSDA
