ENP1_YEAST
ID ENP1_YEAST Reviewed; 483 AA.
AC P38333; D6VQP3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Essential nuclear protein 1;
GN Name=ENP1; Synonyms=MEG1; OrderedLocusNames=YBR247C; ORFNames=YBR1635;
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=9034325; DOI=10.1016/s0378-1119(96)00661-0;
RA Roos J., Luz J.M., Centoducati S., Sternglanz R., Lennarz W.J.;
RT "ENP1, an essential gene encoding a nuclear protein that is highly
RT conserved from yeast to humans.";
RL Gene 185:137-146(1997).
RN [2]
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 [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, AND SUBCELLULAR LOCATION.
RX PubMed=12628929; DOI=10.1093/emboj/cdg121;
RA Schaefer T., Strauss D., Petfalski E., Tollervey D., Hurt E.;
RT "The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes.";
RL EMBO J. 22:1370-1380(2003).
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16159874; DOI=10.1074/jbc.m506916200;
RA Leger-Silvestre I., Caffrey J.M., Dawaliby R., Alvarez-Arias D.A., Gas N.,
RA Bertolone S.J., Gleizes P.E., Ellis S.R.;
RT "Specific role for yeast homologs of the Diamond Blackfan anemia-associated
RT Rps19 protein in ribosome synthesis.";
RL J. Biol. Chem. 280:38177-38185(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172 AND SER-404, 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-172 AND SER-190, 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).
CC -!- FUNCTION: Required for normal export of the pre-40S particles from the
CC nucleus to the cytoplasm. Its subcellular location and association with
CC pre-40S subunit shifts from mixed cytoplasm/nucleus to all nuclear in
CC RPS19 disruptions, suggesting it acts after the ribosomal protein.
CC {ECO:0000269|PubMed:12628929, ECO:0000269|PubMed:16159874}.
CC -!- INTERACTION:
CC P38333; P36009: DHR2; NbExp=2; IntAct=EBI-6482, EBI-5844;
CC P38333; P32899: IMP3; NbExp=4; IntAct=EBI-6482, EBI-9237;
CC P38333; P53941: IMP4; NbExp=6; IntAct=EBI-6482, EBI-9243;
CC P38333; P38217: KAP104; NbExp=2; IntAct=EBI-6482, EBI-9152;
CC P38333; P25586: KRR1; NbExp=5; IntAct=EBI-6482, EBI-21773;
CC P38333; P15646: NOP1; NbExp=4; IntAct=EBI-6482, EBI-6838;
CC P38333; Q99207: NOP14; NbExp=10; IntAct=EBI-6482, EBI-35157;
CC P38333; Q12481: RRP36; NbExp=2; IntAct=EBI-6482, EBI-31770;
CC P38333; P53251: SLX9; NbExp=3; IntAct=EBI-6482, EBI-23221;
CC P38333; Q06078: UTP21; NbExp=3; IntAct=EBI-6482, EBI-359;
CC P38333; P53254: UTP22; NbExp=9; IntAct=EBI-6482, EBI-1878;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus.
CC -!- MISCELLANEOUS: Present with 21600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the bystin family. {ECO:0000305}.
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DR EMBL; U50779; AAC49647.1; -; Genomic_DNA.
DR EMBL; Z36116; CAA85210.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07363.1; -; Genomic_DNA.
DR PIR; S46124; S46124.
DR RefSeq; NP_009806.3; NM_001178595.3.
DR PDB; 5WLC; EM; 3.80 A; SZ=1-483.
DR PDB; 5WWO; X-ray; 2.40 A; A/B=121-483.
DR PDB; 5WYJ; EM; 8.70 A; E3=1-483.
DR PDB; 6EML; EM; 3.60 A; e=1-483.
DR PDB; 6FAI; EM; 3.40 A; i=1-483.
DR PDB; 6KE6; EM; 3.40 A; RS=1-483.
DR PDB; 6LQP; EM; 3.20 A; RS=1-483.
DR PDB; 6LQQ; EM; 4.10 A; RS=1-483.
DR PDB; 6LQR; EM; 8.60 A; RS=1-483.
DR PDB; 6LQS; EM; 3.80 A; RS=1-480.
DR PDB; 6LQU; EM; 3.70 A; RS=1-483.
DR PDB; 6LQV; EM; 4.80 A; RS=1-483.
DR PDB; 6RBD; EM; 3.47 A; i=1-483.
DR PDB; 6Y7C; EM; 3.80 A; i=1-483.
DR PDB; 6ZQA; EM; 4.40 A; JH=1-483.
DR PDB; 6ZQB; EM; 3.90 A; JH=1-483.
DR PDB; 6ZQC; EM; 3.80 A; JH=1-483.
DR PDB; 6ZQD; EM; 3.80 A; JH=1-483.
DR PDB; 6ZQE; EM; 7.10 A; JH=1-483.
DR PDB; 6ZQF; EM; 4.90 A; JH=1-483.
DR PDB; 6ZQG; EM; 3.50 A; JH=1-483.
DR PDB; 7AJT; EM; 4.60 A; JH=1-483.
DR PDB; 7AJU; EM; 3.80 A; JH=1-483.
DR PDB; 7D4I; EM; 4.00 A; RS=1-480.
DR PDB; 7D5S; EM; 4.60 A; RS=1-483.
DR PDB; 7D63; EM; 12.30 A; RS=1-480.
DR PDBsum; 5WLC; -.
DR PDBsum; 5WWO; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 6EML; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
DR PDBsum; 6RBD; -.
DR PDBsum; 6Y7C; -.
DR PDBsum; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 6ZQF; -.
DR PDBsum; 6ZQG; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; P38333; -.
DR SMR; P38333; -.
DR BioGRID; 32942; 361.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-6612N; -.
DR IntAct; P38333; 107.
DR MINT; P38333; -.
DR STRING; 4932.YBR247C; -.
DR iPTMnet; P38333; -.
DR MaxQB; P38333; -.
DR PaxDb; P38333; -.
DR PRIDE; P38333; -.
DR EnsemblFungi; YBR247C_mRNA; YBR247C; YBR247C.
DR GeneID; 852549; -.
DR KEGG; sce:YBR247C; -.
DR SGD; S000000451; ENP1.
DR VEuPathDB; FungiDB:YBR247C; -.
DR eggNOG; KOG3871; Eukaryota.
DR GeneTree; ENSGT00390000007241; -.
DR HOGENOM; CLU_029727_0_1_1; -.
DR InParanoid; P38333; -.
DR OMA; AGGQEKH; -.
DR BioCyc; YEAST:G3O-29175-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P38333; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38333; protein.
DR GO; GO:0030686; C:90S preribosome; IDA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IDA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0030515; F:snoRNA binding; IDA:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR InterPro; IPR007955; Bystin.
DR PANTHER; PTHR12821; PTHR12821; 1.
DR Pfam; PF05291; Bystin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis.
FT CHAIN 1..483
FT /note="Essential nuclear protein 1"
FT /id="PRO_0000186118"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..123
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Phosphoserine; by ATM or ATR"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 208..221
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 256..269
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 283..293
FT /evidence="ECO:0007829|PDB:5WWO"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:5WWO"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 314..320
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 322..326
FT /evidence="ECO:0007829|PDB:5WWO"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 349..360
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 366..377
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 384..395
FT /evidence="ECO:0007829|PDB:5WWO"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 415..428
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 434..447
FT /evidence="ECO:0007829|PDB:5WWO"
FT HELIX 452..461
FT /evidence="ECO:0007829|PDB:5WWO"
SQ SEQUENCE 483 AA; 55137 MW; 399A415131294637 CRC64;
MARASSTKAR KQRHDPLLKD LDAAQGTLKK INKKKLAQND AANHDAANEE DGYIDSKASR
KILQLAKEQQ DEIEGEELAE SERNKQFEAR FTTMSYDDED EDEDEDEEAF GEDISDFEPE
GDYKEEEEIV EIDEEDAAMF EQYFKKSDDF NSLSGSYNLA DKIMASIREK ESQVEDMQDD
EPLANEQNTS RGNISSGLKS GEGVALPEKV IKAYTTVGSI LKTWTHGKLP KLFKVIPSLR
NWQDVIYVTN PEEWSPHVVY EATKLFVSNL TAKESQKFIN LILLERFRDN IETSEDHSLN
YHIYRAVKKS LYKPSAFFKG FLFPLVETGC NVREATIAGS VLAKVSVPAL HSSAALSYLL
RLPFSPPTTV FIKILLDKKY ALPYQTVDDC VYYFMRFRIL DDGSNGEDAT RVLPVIWHKA
FLTFAQRYKN DITQDQRDFL LETVRQRGHK DIGPEIRREL LAGASREFVD PQEANDDLMI
DVN
