ID   EBP2_HUMAN              Reviewed;         306 AA.
AC   Q99848; Q96A66;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   27-MAR-2024, entry version 198.
DE   RecName: Full=Probable rRNA-processing protein EBP2;
DE   AltName: Full=EBNA1-binding protein 2;
DE   AltName: Full=Nucleolar protein p40;
GN   Name=EBNA1BP2; Synonyms=EBP2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH EBNA1.
RX   PubMed=10074103; DOI=10.1128/jvi.73.4.2587-2595.1999;
RA   Shire K., Ceccarelli D.F.J., Avolio-Hunter T.M., Frappier L.;
RT   "EBP2, a human protein that interacts with sequences of the Epstein-Barr
RT   virus nuclear antigen 1 important for plasmid maintenance.";
RL   J. Virol. 73:2587-2595(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=11327720; DOI=10.1006/bbrc.2001.4780;
RA   Henning D., Valdez B.C.;
RT   "Expression of p40/Epstein-Barr virus nuclear antigen 1 binding protein
RT   2.";
RL   Biochem. Biophys. Res. Commun. 283:430-436(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=2879624;
RA   Chatterjee A., Freeman J.W., Busch H.;
RT   "Identification and partial characterization of a Mr 40,000 nucleolar
RT   antigen associated with cell proliferation.";
RL   Cancer Res. 47:1123-1129(1987).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19170763; DOI=10.1111/j.1365-2443.2008.01262.x;
RA   Hirano Y., Ishii K., Kumeta M., Furukawa K., Takeyasu K., Horigome T.;
RT   "Proteomic and targeted analytical identification of BXDC1 and EBNA1BP2 as
RT   dynamic scaffold proteins in the nucleolus.";
RL   Genes Cells 14:155-166(2009).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT THR-3; SER-7; SER-9; SER-11; SER-13 AND SER-16, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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).
RN   [11]
RP   INTERACTION WITH WDR46.
RX   PubMed=23848194; DOI=10.1111/gtc.12077;
RA   Hirai Y., Louvet E., Oda T., Kumeta M., Watanabe Y., Horigome T.,
RA   Takeyasu K.;
RT   "Nucleolar scaffold protein, WDR46, determines the granular compartmental
RT   localization of nucleolin and DDX21.";
RL   Genes Cells 18:780-797(2013).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-270, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [14]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-94; LYS-179 AND LYS-218, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- FUNCTION: Required for the processing of the 27S pre-rRNA.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Specifically interacts with EBV EBNA1. The EBNA1-EBP2
CC       interaction is important for the stable segregation of EBV episomes
CC       during cell division (PubMed:10074103). Interacts with WDR46.
CC       {ECO:0000269|PubMed:10074103, ECO:0000269|PubMed:23848194}.
CC   -!- INTERACTION:
CC       Q99848; Q8TDN6: BRIX1; NbExp=4; IntAct=EBI-1048111, EBI-1052326;
CC       Q99848; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-1048111, EBI-739624;
CC       Q99848; Q8IZU0: FAM9B; NbExp=5; IntAct=EBI-1048111, EBI-10175124;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19170763,
CC       ECO:0000269|PubMed:2879624}. Note=Associated with the nucleolus in an
CC       RNA-dependent manner.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11327720}.
CC   -!- SIMILARITY: Belongs to the EBP2 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U86602; AAB46731.1; -; mRNA.
DR   EMBL; BC009175; AAH09175.1; -; mRNA.
DR   CCDS; CCDS478.1; -.
DR   PIR; JC7687; JC7687.
DR   RefSeq; NP_001153408.1; NM_001159936.1.
DR   RefSeq; NP_006815.2; NM_006824.2.
DR   PDB; 8FKP; EM; 2.85 A; SN=1-306.
DR   PDB; 8FKQ; EM; 2.76 A; SN=1-306.
DR   PDB; 8FKR; EM; 2.89 A; SN=1-306.
DR   PDB; 8FKS; EM; 2.88 A; SN=1-306.
DR   PDB; 8FKT; EM; 2.81 A; SN=1-306.
DR   PDB; 8FKU; EM; 2.82 A; SN=1-306.
DR   PDB; 8FKV; EM; 2.47 A; SN=1-306.
DR   PDB; 8FKW; EM; 2.50 A; SN=1-306.
DR   PDB; 8FKX; EM; 2.59 A; SN=1-306.
DR   PDB; 8FKY; EM; 2.67 A; SN=1-306.
DR   PDBsum; 8FKP; -.
DR   PDBsum; 8FKQ; -.
DR   PDBsum; 8FKR; -.
DR   PDBsum; 8FKS; -.
DR   PDBsum; 8FKT; -.
DR   PDBsum; 8FKU; -.
DR   PDBsum; 8FKV; -.
DR   PDBsum; 8FKW; -.
DR   PDBsum; 8FKX; -.
DR   PDBsum; 8FKY; -.
DR   AlphaFoldDB; Q99848; -.
DR   EMDB; EMD-29252; -.
DR   EMDB; EMD-29253; -.
DR   EMDB; EMD-29254; -.
DR   EMDB; EMD-29255; -.
DR   EMDB; EMD-29256; -.
DR   EMDB; EMD-29257; -.
DR   EMDB; EMD-29258; -.
DR   EMDB; EMD-29259; -.
DR   EMDB; EMD-29260; -.
DR   EMDB; EMD-29261; -.
DR   SMR; Q99848; -.
DR   BioGRID; 116166; 304.
DR   CORUM; Q99848; -.
DR   IntAct; Q99848; 119.
DR   MINT; Q99848; -.
DR   STRING; 9606.ENSP00000407323; -.
DR   GlyGen; Q99848; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q99848; -.
DR   PhosphoSitePlus; Q99848; -.
DR   SwissPalm; Q99848; -.
DR   BioMuta; EBNA1BP2; -.
DR   DMDM; 116241344; -.
DR   EPD; Q99848; -.
DR   jPOST; Q99848; -.
DR   MassIVE; Q99848; -.
DR   MaxQB; Q99848; -.
DR   PaxDb; 9606-ENSP00000407323; -.
DR   PeptideAtlas; Q99848; -.
DR   ProteomicsDB; 78504; -.
DR   Pumba; Q99848; -.
DR   Antibodypedia; 18196; 162 antibodies from 27 providers.
DR   DNASU; 10969; -.
DR   Ensembl; ENST00000236051.3; ENSP00000236051.2; ENSG00000117395.13.
DR   GeneID; 10969; -.
DR   KEGG; hsa:10969; -.
DR   MANE-Select; ENST00000236051.3; ENSP00000236051.2; NM_006824.3; NP_006815.2.
DR   UCSC; uc001cin.4; human.
DR   AGR; HGNC:15531; -.
DR   CTD; 10969; -.
DR   DisGeNET; 10969; -.
DR   GeneCards; EBNA1BP2; -.
DR   HGNC; HGNC:15531; EBNA1BP2.
DR   HPA; ENSG00000117395; Low tissue specificity.
DR   MIM; 614443; gene.
DR   neXtProt; NX_Q99848; -.
DR   OpenTargets; ENSG00000117395; -.
DR   PharmGKB; PA27586; -.
DR   VEuPathDB; HostDB:ENSG00000117395; -.
DR   eggNOG; KOG3080; Eukaryota.
DR   GeneTree; ENSGT00390000014984; -.
DR   HOGENOM; CLU_036007_1_0_1; -.
DR   InParanoid; Q99848; -.
DR   OrthoDB; 11782at2759; -.
DR   PhylomeDB; Q99848; -.
DR   PathwayCommons; Q99848; -.
DR   Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   SignaLink; Q99848; -.
DR   BioGRID-ORCS; 10969; 633 hits in 1164 CRISPR screens.
DR   ChiTaRS; EBNA1BP2; human.
DR   GeneWiki; EBNA1BP2; -.
DR   GenomeRNAi; 10969; -.
DR   Pharos; Q99848; Tbio.
DR   PRO; PR:Q99848; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q99848; Protein.
DR   Bgee; ENSG00000117395; Expressed in right lobe of liver and 204 other cell types or tissues.
DR   ExpressionAtlas; Q99848; baseline and differential.
DR   GO; GO:0005694; C:chromosome; IDA:HPA.
DR   GO; GO:0034399; C:nuclear periphery; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR   InterPro; IPR008610; Ebp2.
DR   PANTHER; PTHR13028; RRNA PROCESSING PROTEIN EBNA1-BINDING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR13028:SF0; RRNA-PROCESSING PROTEIN EBP2-RELATED; 1.
DR   Pfam; PF05890; Ebp2; 1.
DR   SWISS-2DPAGE; Q99848; -.
DR   Genevisible; Q99848; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Coiled coil; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Ribosome biogenesis; Ubl conjugation.
FT   CHAIN           1..306
FT                   /note="Probable rRNA-processing protein EBP2"
FT                   /id="PRO_0000119993"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          138..169
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        235..251
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..306
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         3
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         264
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         270
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   CROSSLNK        94
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        179
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        218
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         223
FT                   /note="R -> H (in dbSNP:rs7163)"
FT                   /id="VAR_024437"
FT   CONFLICT        147
FT                   /note="M -> V (in Ref. 2; AAB46731)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   306 AA;  34852 MW;  1212FC2E9442FA2E CRC64;
     MDTPPLSDSE SESDESLVTD RELQDAFSRG LLKPGLNVVL EGPKKAVNDV NGLKQCLAEF
     KRDLEWVERL DVTLGPVPEI GGSEAPAPQN KDQKAVDPED DFQREMSFYR QAQAAVLAVL
     PRLHQLKVPT KRPTDYFAEM AKSDLQMQKI RQKLQTKQAA MERSEKAKQL RALRKYGKKV
     QTEVLQKRQQ EKAHMMNAIK KYQKGFSDKL DFLEGDQKPL AQRKKAGAKG QQMRKGPSAK
     RRYKNQKFGF GGKKKGSKWN TRESYDDVSS FRAKTAHGRG LKRPGKKGSN KRPGKRTREK
     MKNRTH
//