EBP2_YEAST
ID EBP2_YEAST Reviewed; 427 AA.
AC P36049; D6VX28;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=rRNA-processing protein EBP2;
DE AltName: Full=EBNA1-binding protein homolog;
GN Name=EBP2; OrderedLocusNames=YKL172W; ORFNames=YKL636;
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=8091858; DOI=10.1002/yea.320100004;
RA Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT "Sequencing and analysis of a 20.5 kb DNA segment located on the left arm
RT of yeast chromosome XI.";
RL Yeast 10:S25-S33(1994).
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, AND SUBCELLULAR LOCATION.
RX PubMed=10947841; DOI=10.1046/j.1365-2443.2000.00346.x;
RA Tsujii R., Miyoshi K., Tsuno A., Matsui Y., Toh-e A., Miyakawa T.,
RA Mizuta K.;
RT "Ebp2p, yeast homologue of a human protein that interacts with Epstein-Barr
RT virus nuclear antigen 1, is required for pre-rRNA processing and ribosomal
RT subunit assembly.";
RL Genes Cells 5:543-553(2000).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10849420; DOI=10.1074/jbc.m000594200;
RA Huber M.D., Dworet J.H., Shire K., Frappier L., McAlear M.A.;
RT "The budding yeast homolog of the human EBNA1-binding protein 2 (Ebp2p) is
RT an essential nucleolar protein required for pre-rRNA processing.";
RL J. Biol. Chem. 275:28764-28773(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-177 AND SER-183, 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 [7]
RP INTERACTION WITH LOC1; NOP12; SIZ2; ULS1 AND WSS1, SUMOYLATION, AND
RP MUTAGENESIS OF 36-LYS-LYS-37 AND 61-LYS-LYS-62.
RX PubMed=18603780; DOI=10.1271/bbb.80131;
RA Shirai C., Mizuta K.;
RT "SUMO mediates interaction of Ebp2p, the yeast homolog of Epstein-Barr
RT virus nuclear antigen 1-binding protein 2, with a RING finger protein
RT Ris1p.";
RL Biosci. Biotechnol. Biochem. 72:1881-1886(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-177 AND SER-183, 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 the processing of the 27S pre-rRNA. Probably
CC involved in the step of the processing of the 27 SA precursor into the
CC 27 SB intermediate. {ECO:0000269|PubMed:10849420,
CC ECO:0000269|PubMed:10947841}.
CC -!- SUBUNIT: Interacts with LOC1, NOP12, SIZ2, ULS1 and WSS1.
CC {ECO:0000269|PubMed:18603780}.
CC -!- INTERACTION:
CC P36049; Q08235: BRX1; NbExp=5; IntAct=EBI-6289, EBI-3775;
CC P36049; P53188: CGR1; NbExp=3; IntAct=EBI-6289, EBI-23731;
CC P36049; Q12389: DBP10; NbExp=3; IntAct=EBI-6289, EBI-5644;
CC P36049; P36049: EBP2; NbExp=3; IntAct=EBI-6289, EBI-6289;
CC P36049; P43586: LOC1; NbExp=6; IntAct=EBI-6289, EBI-22906;
CC P36049; P47069: MPS3; NbExp=4; IntAct=EBI-6289, EBI-25811;
CC P36049; P39744: NOC2; NbExp=3; IntAct=EBI-6289, EBI-29259;
CC P36049; P37838: NOP4; NbExp=5; IntAct=EBI-6289, EBI-12122;
CC P36049; P40078: NSA2; NbExp=3; IntAct=EBI-6289, EBI-22681;
CC P36049; P53131: PRP43; NbExp=3; IntAct=EBI-6289, EBI-505;
CC P36049; Q12754: RRP12; NbExp=3; IntAct=EBI-6289, EBI-30678;
CC P36049; P38789: SSF1; NbExp=3; IntAct=EBI-6289, EBI-18160;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10849420,
CC ECO:0000269|PubMed:10947841}.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:18603780}.
CC -!- SIMILARITY: Belongs to the EBP2 family. {ECO:0000305}.
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DR EMBL; Z26878; CAA81515.1; -; Genomic_DNA.
DR EMBL; Z28172; CAA82014.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08994.1; -; Genomic_DNA.
DR PIR; S38002; S38002.
DR RefSeq; NP_012749.1; NM_001179738.1.
DR PDB; 5Z1G; X-ray; 2.29 A; A/C=186-295.
DR PDB; 5Z3G; EM; 3.65 A; b=1-427.
DR PDB; 6ELZ; EM; 3.30 A; J=1-427.
DR PDB; 6EM1; EM; 3.60 A; J=1-427.
DR PDB; 6EM3; EM; 3.20 A; J=1-427.
DR PDB; 6EM4; EM; 4.10 A; J=1-427.
DR PDB; 6EM5; EM; 4.30 A; J=1-427.
DR PDB; 7OHR; EM; 4.72 A; J=1-427.
DR PDB; 7OHV; EM; 3.90 A; J=1-427.
DR PDB; 7OHW; EM; 3.50 A; J=1-427.
DR PDBsum; 5Z1G; -.
DR PDBsum; 5Z3G; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM3; -.
DR PDBsum; 6EM4; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR AlphaFoldDB; P36049; -.
DR SMR; P36049; -.
DR BioGRID; 33966; 240.
DR DIP; DIP-6507N; -.
DR IntAct; P36049; 51.
DR MINT; P36049; -.
DR STRING; 4932.YKL172W; -.
DR iPTMnet; P36049; -.
DR MaxQB; P36049; -.
DR PaxDb; P36049; -.
DR PRIDE; P36049; -.
DR EnsemblFungi; YKL172W_mRNA; YKL172W; YKL172W.
DR GeneID; 853682; -.
DR KEGG; sce:YKL172W; -.
DR SGD; S000001655; EBP2.
DR VEuPathDB; FungiDB:YKL172W; -.
DR eggNOG; KOG3080; Eukaryota.
DR GeneTree; ENSGT00390000014984; -.
DR HOGENOM; CLU_036007_3_1_1; -.
DR InParanoid; P36049; -.
DR OMA; AFYKVCQ; -.
DR BioCyc; YEAST:G3O-31939-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P36049; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36049; protein.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
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:0000280; P:nuclear division; IMP:SGD.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR InterPro; IPR008610; Ebp2.
DR PANTHER; PTHR13028; PTHR13028; 1.
DR Pfam; PF05890; Ebp2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; Ubl conjugation.
FT CHAIN 1..427
FT /note="rRNA-processing protein EBP2"
FT /id="PRO_0000120000"
FT REGION 29..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 45..174
FT /evidence="ECO:0000255"
FT COILED 234..265
FT /evidence="ECO:0000255"
FT COILED 291..348
FT /evidence="ECO:0000255"
FT COMPBIAS 48..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..127
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..427
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 36..37
FT /note="KK->RR: Reduces sumoylation and impairs interaction
FT with SIZ2, WSS1 and ULS1, when associated with R-61 and R-
FT 62."
FT /evidence="ECO:0000269|PubMed:18603780"
FT MUTAGEN 61..62
FT /note="KK->RR: Reduces sumoylation and impairs interaction
FT with SIZ2, WSS1 and ULS1, when associated with R-36 and R-
FT 37."
FT /evidence="ECO:0000269|PubMed:18603780"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:5Z1G"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:5Z1G"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:5Z1G"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:5Z1G"
FT HELIX 239..263
FT /evidence="ECO:0007829|PDB:5Z1G"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:5Z1G"
FT HELIX 282..288
FT /evidence="ECO:0007829|PDB:5Z1G"
SQ SEQUENCE 427 AA; 49734 MW; 4A11F6CDF779DB5A CRC64;
MAKGFKLKEL LSHQKEIEKA EKLENDLKKK KSQELKKEEP TIVTASNLKK LEKKEKKADV
KKEVAADTEE YQSQALSKKE KRKLKKELKK MQEQDATEAQ KHMSGDEDES GDDREEEEEE
EEEEEGRLDL EKLAKSDSES EDDSESENDS EEDEDVVAKE ESEEKEEQEE EQDVPLSDVE
FDSDADVVPH HKLTVNNTKA MKHALERVQL PWKKHSFQEH QSVTSETNTD EHIKDIYDDT
ERELAFYKQS LDAVLVARDE LKRLKVPFKR PLDYFAEMVK SDEHMDKIKG KLIEEASDKK
AREEARRQRQ LKKFGKQVQN ATLQKRQLEK RETLEKIKSL KNKRKHNEID HSEFNVGVEE
EVEGKRFDRG RPNGKRAAKN AKYGQGGMKR FKRKNDATSS ADVSGFSSRK MKGKTNRPGK
SRRARRF
