EBP2_HUMAN
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 03-AUG-2022, entry version 189.
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}.
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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 AlphaFoldDB; Q99848; -.
DR SMR; Q99848; -.
DR BioGRID; 116166; 266.
DR CORUM; Q99848; -.
DR IntAct; Q99848; 109.
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 SWISS-2DPAGE; Q99848; -.
DR EPD; Q99848; -.
DR jPOST; Q99848; -.
DR MassIVE; Q99848; -.
DR MaxQB; Q99848; -.
DR PaxDb; Q99848; -.
DR PeptideAtlas; Q99848; -.
DR PRIDE; Q99848; -.
DR ProteomicsDB; 78504; -.
DR Antibodypedia; 18196; 137 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 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; 1154126at2759; -.
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; 620 hits in 1085 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 202 other tissues.
DR ExpressionAtlas; Q99848; baseline and differential.
DR Genevisible; Q99848; HS.
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; PTHR13028; 1.
DR Pfam; PF05890; Ebp2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein;
KW 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
