ERB1_SCHPO
ID ERB1_SCHPO Reviewed; 740 AA.
AC O74399;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Ribosome biogenesis protein erb1 {ECO:0000255|HAMAP-Rule:MF_03027};
DE AltName: Full=Eukaryotic ribosome biogenesis protein 1 {ECO:0000255|HAMAP-Rule:MF_03027};
GN Name=erb1; ORFNames=SPBC4F6.13c;
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, 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: Component of the NOP7 complex, which is required for
CC maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S
CC ribosome. {ECO:0000255|HAMAP-Rule:MF_03027}.
CC -!- SUBUNIT: Component of the NOP7 complex, composed of erb1, ppp1/nop7 and
CC ytm1/SPAC890.04c. The complex is held together by erb1, which interacts
CC with ppp1/nop7 via its N-terminal domain and with ytm1/SPAC890.04c via
CC a high-affinity interaction between the seven-bladed beta-propeller
CC domains of the 2 proteins. The NOP7 complex associates with the 66S
CC pre-ribosome. {ECO:0000255|HAMAP-Rule:MF_03027}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03027, ECO:0000269|PubMed:16823372}. Nucleus, nucleoplasm
CC {ECO:0000255|HAMAP-Rule:MF_03027}.
CC -!- SIMILARITY: Belongs to the WD repeat BOP1/ERB1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03027}.
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DR EMBL; CU329671; CAA20733.2; -; Genomic_DNA.
DR PIR; T40510; T40510.
DR RefSeq; NP_596113.2; NM_001022030.2.
DR AlphaFoldDB; O74399; -.
DR SMR; O74399; -.
DR BioGRID; 277405; 5.
DR STRING; 4896.SPBC4F6.13c.1; -.
DR iPTMnet; O74399; -.
DR MaxQB; O74399; -.
DR PaxDb; O74399; -.
DR PRIDE; O74399; -.
DR EnsemblFungi; SPBC4F6.13c.1; SPBC4F6.13c.1:pep; SPBC4F6.13c.
DR GeneID; 2540888; -.
DR KEGG; spo:SPBC4F6.13c; -.
DR PomBase; SPBC4F6.13c; erb1.
DR VEuPathDB; FungiDB:SPBC4F6.13c; -.
DR eggNOG; KOG0650; Eukaryota.
DR HOGENOM; CLU_011390_0_1_1; -.
DR InParanoid; O74399; -.
DR OMA; MRPAKGE; -.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:O74399; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0070545; C:PeBoW complex; ISO:PomBase.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IBA:GO_Central.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:UniProtKB-UniRule.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03027; BOP1; 1.
DR InterPro; IPR028598; BOP1/Erb1.
DR InterPro; IPR012953; BOP1_N_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR17605; PTHR17605; 1.
DR Pfam; PF08145; BOP1NT; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM01035; BOP1NT; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribosome biogenesis;
KW rRNA processing; WD repeat.
FT CHAIN 1..740
FT /note="Ribosome biogenesis protein erb1"
FT /id="PRO_0000316569"
FT REPEAT 381..420
FT /note="WD 1"
FT REPEAT 526..568
FT /note="WD 2"
FT REPEAT 571..609
FT /note="WD 3"
FT REPEAT 612..651
FT /note="WD 4"
FT REPEAT 655..694
FT /note="WD 5"
FT REPEAT 710..740
FT /note="WD 6"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..104
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 740 AA; 82945 MW; D352AF12C7A1D0BE CRC64;
METGMNRKRS RSKRANSNVG VEKDKEKEKS KGVSNVPNEV ETESSSHEPS FKKDVDEEIP
SLTAELSEEE EGEYSSESGR STPELSPDDF EDADDEEEFE EIDAGYSSDS STEDVAPGLY
ESPYDENLYI NYDIDGKKIT RPATPAALDS LIASIDKDKG WTGIVDPMTG KPVNLTTEEL
GLLKRLAQSE IPDENFDPYP DYDDFFTNTV RETPLSSAPE PKRRFAPSKH EQKRILQLAY
AIRKGRILTS EQRAERERES QSNYADHDLW ADDDQATVNQ RKLDYAPAPK LPPPSHEESY
NPPEEYLKQS SDFPKKYKSL RVVPAYSNLI KEKFERCLDL YLAPRVRRTK LNIDPESLLP
KLPTPSELRP FPTRCTNVFI GHKGRVRCLS VHVSGNWLAS GGDDGVLRIW EVMTGRCVWK
CSLDSFGNAH NIDSDEDAVN ESLSHSTKSS IIQSLAWGPL SDSPVLAVAV DETVYFITPP
IFSDEQIEAS KELFTSAPYQ ESSAIWRRGA KQSLQLHGGI VHATVSTPSS IKSLSWHRRG
DYLATSSPTS SSQAVLIHQL SRGASQSPFS KSKGSVQAVT FHPTMPYLLV ATQRYVRIYN
LVKQELVKTL LTGVKWVSSL SVHSSGDHVI IGSYDKRLCW FDLDFSSKPY KNLRYHSRAL
RDVSYHPSLP LFCSGSDDGD VQVFHGRVYS DLLANPLIVP LKILRNHKVV DNVGVLSTCW
HPKEAWLFSA GAGGEIRMWT