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RRB1_SCHPO
ID   RRB1_SCHPO              Reviewed;         480 AA.
AC   Q9P783;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Ribosome assembly protein rrb1;
GN   Name=rrb1; ORFNames=SPBC1711.07;
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   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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-166, AND
RP   IDENTIFICATION BY 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: Involved in regulation of L3 expression and stability and
CC       plays a role in early 60S ribosomal subunit assembly. May be required
CC       for proper assembly of pre-ribosomal particles during early ribosome
CC       biogenesis, presumably by targeting L3 onto the 35S precursor rRNA (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Associates with ribosomal protein L3. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:16823372}.
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DR   EMBL; CU329671; CAB88237.1; -; Genomic_DNA.
DR   RefSeq; NP_595880.1; NM_001021786.2.
DR   AlphaFoldDB; Q9P783; -.
DR   SMR; Q9P783; -.
DR   BioGRID; 276247; 3.
DR   STRING; 4896.SPBC1711.07.1; -.
DR   iPTMnet; Q9P783; -.
DR   MaxQB; Q9P783; -.
DR   PaxDb; Q9P783; -.
DR   PRIDE; Q9P783; -.
DR   EnsemblFungi; SPBC1711.07.1; SPBC1711.07.1:pep; SPBC1711.07.
DR   GeneID; 2539693; -.
DR   KEGG; spo:SPBC1711.07; -.
DR   PomBase; SPBC1711.07; rrb1.
DR   VEuPathDB; FungiDB:SPBC1711.07; -.
DR   eggNOG; KOG0302; Eukaryota.
DR   HOGENOM; CLU_025272_1_1_1; -.
DR   InParanoid; Q9P783; -.
DR   OMA; DWSPLQP; -.
DR   PhylomeDB; Q9P783; -.
DR   PRO; PR:Q9P783; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005730; C:nucleolus; ISS:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0042254; P:ribosome biogenesis; ISS:PomBase.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR022052; Histone-bd_RBBP4_N.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF12265; CAF1C_H4-bd; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 5.
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; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Ribosome biogenesis; rRNA processing; WD repeat.
FT   CHAIN           1..480
FT                   /note="Ribosome assembly protein rrb1"
FT                   /id="PRO_0000316544"
FT   REPEAT          183..225
FT                   /note="WD 1"
FT   REPEAT          289..329
FT                   /note="WD 2"
FT   REPEAT          334..375
FT                   /note="WD 3"
FT   REPEAT          385..425
FT                   /note="WD 4"
FT   REPEAT          446..480
FT                   /note="WD 5"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..62
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         163
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   480 AA;  53834 MW;  FDC4DF882C831BA6 CRC64;
     MSKRAAEETV EFNSKNGPGQ RGTVADNVDT EMGEFEDAYE DEIESEEEYI EADGEKDNGM
     DEEEQNDAQP SKIPWLPGGK INADEKLVAD PSVYEMLHNI QVKWPFLSFD ILQDSLGEER
     RAWPHQMYLV GGSQALDSND NELTVMKLSQ LYKTQHDEND DASDNSDVEE DPILEHKSIS
     TKGACNRVRS ARRPANSSKE SLLASFHETG KVHIWDIAPH LRSLDSPGVM VSRKENSPLY
     TVNRHKTEGY ALDWSPFEYS LLSGDNANEI FLTKYSNGGW QTDSSPFLSH TAAVEDLQWS
     PSEKNVFSSC SCDGTFRIWD VRNKQKTSAL TVNAHPGVDV NVLSWNTRVP NLLATGADNG
     VWSVWDLRSL KSSSSVATPV ASFKWHRAPI YSIEWHPNED SVIGVVGADN QISLWDLSVE
     LDEEEQDSRA AEGLQDVPPQ LMFIHMGQQE IKEMHWHRQI PGTIVSTAMT GINVFKTITF
 
 
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