EBP2_MOUSE
ID EBP2_MOUSE Reviewed; 306 AA.
AC Q9D903; A2ACZ0; Q3TKB5;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable rRNA-processing protein EBP2;
GN Name=Ebna1bp2; Synonyms=Ebp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
CC -!- FUNCTION: Required for the processing of the 27S pre-rRNA.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with WDR46. {ECO:0000250|UniProtKB:Q99848}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q99848}.
CC -!- SIMILARITY: Belongs to the EBP2 family. {ECO:0000305}.
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DR EMBL; AK007491; BAB25065.1; -; mRNA.
DR EMBL; AK134732; BAE22261.1; -; mRNA.
DR EMBL; AK167070; BAE39230.1; -; mRNA.
DR EMBL; AK168269; BAE40215.1; -; mRNA.
DR EMBL; AL669952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054723; AAH54723.1; -; mRNA.
DR EMBL; BC062876; AAH62876.1; -; mRNA.
DR CCDS; CCDS18555.1; -.
DR RefSeq; NP_081208.1; NM_026932.4.
DR AlphaFoldDB; Q9D903; -.
DR SMR; Q9D903; -.
DR BioGRID; 213211; 10.
DR CORUM; Q9D903; -.
DR DIP; DIP-48579N; -.
DR IntAct; Q9D903; 1.
DR STRING; 10090.ENSMUSP00000030501; -.
DR iPTMnet; Q9D903; -.
DR PhosphoSitePlus; Q9D903; -.
DR EPD; Q9D903; -.
DR MaxQB; Q9D903; -.
DR PaxDb; Q9D903; -.
DR PeptideAtlas; Q9D903; -.
DR PRIDE; Q9D903; -.
DR ProteomicsDB; 277666; -.
DR Antibodypedia; 18196; 137 antibodies from 27 providers.
DR DNASU; 69072; -.
DR Ensembl; ENSMUST00000030501; ENSMUSP00000030501; ENSMUSG00000028729.
DR GeneID; 69072; -.
DR KEGG; mmu:69072; -.
DR UCSC; uc008ukn.2; mouse.
DR CTD; 10969; -.
DR MGI; MGI:1916322; Ebna1bp2.
DR VEuPathDB; HostDB:ENSMUSG00000028729; -.
DR eggNOG; KOG3080; Eukaryota.
DR GeneTree; ENSGT00390000014984; -.
DR HOGENOM; CLU_036007_1_0_1; -.
DR InParanoid; Q9D903; -.
DR OMA; MFHRQAQ; -.
DR OrthoDB; 1154126at2759; -.
DR PhylomeDB; Q9D903; -.
DR TreeFam; TF314642; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 69072; 22 hits in 73 CRISPR screens.
DR ChiTaRS; Ebna1bp2; mouse.
DR PRO; PR:Q9D903; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D903; protein.
DR Bgee; ENSMUSG00000028729; Expressed in embryonic post-anal tail and 258 other tissues.
DR ExpressionAtlas; Q9D903; baseline and differential.
DR Genevisible; Q9D903; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0034399; C:nuclear periphery; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
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 2: Evidence at transcript 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_0000119994"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..169
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 135..171
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Polar 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:0000250|UniProtKB:Q99848"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99848"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99848"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99848"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99848"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99848"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99848"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99848"
FT CROSSLNK 93
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99848"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99848"
FT CROSSLNK 218
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99848"
SQ SEQUENCE 306 AA; 34703 MW; C612FB25A47084EA CRC64;
MDTPPLSESD SESDACLASD QELQDAFSRG LLKPGLNVVL EKPKKAVNDV SGLKQCLAEF
RRDLEWVERL DVTLGPVPEV SETQPTPQNQ DQKKGVNPED DFQREMSFYR QAQAAVLAVL
PRLHQLQVPT KRPTDYFAEM AKSDQQMQKI RQKLQTKQAA MEKSEKAKQL RALRKYGKKV
QTEVLQKRQR EKAHMMNAIK KYQKGFSDKL DFLEGDQKPV ERSAKAGGKG QQMSKGPNAK
RRYKNQKFGF GGKKKGSKWN TKESYDDVSS FRAKVAHGKG SRRPGKKGAN KRPGKRARQK
LKSKAR
