EBP2_SCHPO
ID EBP2_SCHPO Reviewed; 333 AA.
AC O13802;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Probable rRNA-processing protein ebp2;
GN Name=ebp2; ORFNames=SPAC17H9.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP INTERACTION WITH SAD1, AND SUBCELLULAR LOCATION.
RX PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
RA Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
RT "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
RT membrane-bound components of the spindle pole body in fission yeast.";
RL Mol. Genet. Genomics 270:449-461(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Required for the processing of the 27S pre-rRNA.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with sad1. {ECO:0000269|PubMed:14655046}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14655046}.
CC -!- SIMILARITY: Belongs to the EBP2 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11214.1; -; Genomic_DNA.
DR PIR; T37871; T37871.
DR RefSeq; NP_593575.1; NM_001019007.2.
DR AlphaFoldDB; O13802; -.
DR SMR; O13802; -.
DR BioGRID; 278597; 16.
DR IntAct; O13802; 4.
DR MINT; O13802; -.
DR STRING; 4896.SPAC17H9.05.1; -.
DR iPTMnet; O13802; -.
DR MaxQB; O13802; -.
DR PaxDb; O13802; -.
DR PRIDE; O13802; -.
DR EnsemblFungi; SPAC17H9.05.1; SPAC17H9.05.1:pep; SPAC17H9.05.
DR GeneID; 2542121; -.
DR KEGG; spo:SPAC17H9.05; -.
DR PomBase; SPAC17H9.05; ebp2.
DR VEuPathDB; FungiDB:SPAC17H9.05; -.
DR eggNOG; KOG3080; Eukaryota.
DR HOGENOM; CLU_036007_2_0_1; -.
DR InParanoid; O13802; -.
DR OMA; AFYKVCQ; -.
DR PhylomeDB; O13802; -.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:O13802; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0034399; C:nuclear periphery; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IPI:PomBase.
DR GO; GO:0006364; P:rRNA processing; ISO:PomBase.
DR InterPro; IPR008610; Ebp2.
DR PANTHER; PTHR13028; PTHR13028; 1.
DR Pfam; PF05890; Ebp2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis.
FT CHAIN 1..333
FT /note="Probable rRNA-processing protein ebp2"
FT /id="PRO_0000119999"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 212..240
FT /evidence="ECO:0000255"
FT COMPBIAS 58..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..333
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 333 AA; 37819 MW; 8EDF4BB55B30711F CRC64;
MAGIESKQRR AQKKAAKAAM KEKKNKESNE SSTSVEALNE KEMINTIKSP IIETADTADQ
ENESEGSDEV ELSDLEGIEL EEDADLIRKR KLAINNTVAL ENIYERIKYP DDISFVENQA
VTTKEPIIIE NVEDDLAREL AFYKQGVSSV KAAFAKLREA NVLISRPHDY FAEMLKSDDH
MEKVRQELIK EATAKKLSQQ AKKQRELKKF GKQVQLAKQE ERQREKKETL EKINLLKRKH
TGGDLTTEDD FDIALSSASA DTFKKGSRST KSRPQPNPKR QKKNEKYGFG GPKHRSKSND
LDSLAATEFG RKGLKNIKSK KRPGKARREK ARK