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RL3A_SCHPO
ID   RL3A_SCHPO              Reviewed;         388 AA.
AC   P40372;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=60S ribosomal protein L3-A;
GN   Name=rpl301; Synonyms=rpl3a; ORFNames=SPAC17A5.03;
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 [GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=8181745; DOI=10.1016/0378-1119(94)90365-4;
RA   Liebich I., Kohler G., Witt I., Gross T., Kaufer N.F.;
RT   "Two genes encoding ribosomal protein L3 of Schizosaccharomyces pombe and
RT   their proximal promoter regions.";
RL   Gene 142:119-122(1994).
RN   [2]
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-65; SER-140; SER-143;
RP   SER-207; SER-295; SER-355 AND THR-372, AND IDENTIFICATION BY MASS
RP   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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: There are two genes for L3 in S.pombe.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC       {ECO:0000305}.
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DR   EMBL; U00798; AAA19655.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB11503.1; -; Genomic_DNA.
DR   PIR; T37818; T37818.
DR   RefSeq; NP_593471.1; NM_001018904.2.
DR   AlphaFoldDB; P40372; -.
DR   SMR; P40372; -.
DR   BioGRID; 278734; 11.
DR   IntAct; P40372; 2.
DR   STRING; 4896.SPAC17A5.03.1; -.
DR   iPTMnet; P40372; -.
DR   MaxQB; P40372; -.
DR   PaxDb; P40372; -.
DR   PRIDE; P40372; -.
DR   EnsemblFungi; SPAC17A5.03.1; SPAC17A5.03.1:pep; SPAC17A5.03.
DR   GeneID; 2542265; -.
DR   KEGG; spo:SPAC17A5.03; -.
DR   PomBase; SPAC17A5.03; rpl301.
DR   VEuPathDB; FungiDB:SPAC17A5.03; -.
DR   eggNOG; KOG0746; Eukaryota.
DR   HOGENOM; CLU_033361_2_1_1; -.
DR   InParanoid; P40372; -.
DR   OMA; HQRTEYN; -.
DR   PhylomeDB; P40372; -.
DR   Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-SPO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-SPO-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-SPO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-SPO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-SPO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   PRO; PR:P40372; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; ISO:PomBase.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; ISO:PomBase.
DR   GO; GO:0002181; P:cytoplasmic translation; ISO:PomBase.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; ISO:PomBase.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   Gene3D; 4.10.960.10; -; 1.
DR   InterPro; IPR045077; L3_arc_euk.
DR   InterPro; IPR000597; Ribosomal_L3.
DR   InterPro; IPR019926; Ribosomal_L3_CS.
DR   InterPro; IPR044892; Ribosomal_L3_dom_3_arc_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR11363; PTHR11363; 1.
DR   Pfam; PF00297; Ribosomal_L3; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..388
FT                   /note="60S ribosomal protein L3-A"
FT                   /id="PRO_0000077249"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         207
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         372
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   388 AA;  43803 MW;  A4D8377470786D8A CRC64;
     MSHCKFEQPR HGSLGFLPRK RASRQRGKVK AFPKDDASKP VHLTAFLGYK AGMTHIVRDL
     DRPGSKMHKR EILEAVTVIE TPPMVVVGVV GYVETPRGLR SLTTVWAEHL SEEVKRRFYK
     NWFKSKKKAF TKYAKKYAES TQSINRELER IKKYCSVVRV LAHTQIRKTP LAQKKAHLME
     IQVNGGSVAD KVEWAREHFE KTVDIKSTFE QNEMIDVIGV TRGKGNEGTT ARWGTKRLPR
     KTHRGLRKVA CIGAWHPANV QWTVARAGNA GYMHRTQLNS KIYRIGAGDD AKNASTDFDA
     TEKRITPMGG FVRYGVVEND FVMLNGATPG PVKRVLTLRK SLLTHTSRKA LEPVSLKWID
     TASKFGHGRF QTPAEAKQFL GTLKKDVA
 
 
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