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GAR2_SCHPO
ID   GAR2_SCHPO              Reviewed;         500 AA.
AC   P41891; O13707;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Protein gar2;
GN   Name=gar2; ORFNames=SPAC140.02;
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=7596817; DOI=10.1093/nar/23.11.1912;
RA   Gulli M.-P., Girard J.-P., Zabetakis D., Lapeyre B., Melese T.,
RA   Caizergues-Ferrer M.;
RT   "gar2 is a nucleolar protein from Schizosaccharomyces pombe required for
RT   18S rRNA and 40S ribosomal subunit accumulation.";
RL   Nucleic Acids Res. 23:1912-1918(1995).
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-143; SER-144 AND SER-146, 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: Helps the assembly of pre-ribosomal particles containing 18S
CC       rRNA.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC   -!- SIMILARITY: Belongs to the RRM GAR family. {ECO:0000305}.
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DR   EMBL; Z48166; CAA88179.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB86413.1; -; Genomic_DNA.
DR   PIR; S55785; S55785.
DR   RefSeq; NP_593531.1; NM_001018965.2.
DR   AlphaFoldDB; P41891; -.
DR   SMR; P41891; -.
DR   BioGRID; 279314; 65.
DR   STRING; 4896.SPAC140.02.1; -.
DR   iPTMnet; P41891; -.
DR   MaxQB; P41891; -.
DR   PaxDb; P41891; -.
DR   PRIDE; P41891; -.
DR   EnsemblFungi; SPAC140.02.1; SPAC140.02.1:pep; SPAC140.02.
DR   GeneID; 2542869; -.
DR   KEGG; spo:SPAC140.02; -.
DR   PomBase; SPAC140.02; gar2.
DR   VEuPathDB; FungiDB:SPAC140.02; -.
DR   eggNOG; KOG4210; Eukaryota.
DR   HOGENOM; CLU_026791_1_1_1; -.
DR   InParanoid; P41891; -.
DR   OMA; GYVQYSS; -.
DR   PRO; PR:P41891; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0001651; C:dense fibrillar component; IDA:PomBase.
DR   GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; ISS:PomBase.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; IMP:PomBase.
DR   CDD; cd12447; RRM1_gar2; 1.
DR   CDD; cd12448; RRM2_gar2; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR034272; Gar2_RRM1.
DR   InterPro; IPR034276; Gar2_RRM2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; SSF54928; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN           1..500
FT                   /note="Protein gar2"
FT                   /id="PRO_0000081595"
FT   DOMAIN          263..341
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          366..443
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          441..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..141
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         144
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        339
FT                   /note="S -> P (in Ref. 1; CAA88179)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   500 AA;  52988 MW;  9D37FAD0C5161A0B CRC64;
     MAKKDKTSVK KSVKETASKK GAIEKPSKSK KITKEAAKEI AKQSSKTDVS PKKSKKEAKR
     ASSPEPSKKS VKKQKKSKKK EESSSESESE SSSSESESSS SESESSSSES ESSSSESSSS
     ESEEEVIVKT EEKKESSSES SSSSESEEEE EAVVKIEEKK ESSSDSSSES SSSESESESS
     SSESEEEEEV VEKTEEKKEG SSESSSDSES SSDSSSESGD SDSSSDSESE SSSEDEKKRK
     AEPASEERPA KITKPSQDSN ETCTVFVGRL SWNVDDQWLG QEFEEYGTIV GARVIMDGQS
     GRSKGYGYVD FETPEAAKAA VAANGTKEID GRMVNLDLSN PRPANPQPYA QQRAGNFGDQ
     LSEPSDTVFV GNLSFNATED DLSTAFGGCG DIQSIRLPTD PQSGRLKGFG YVTFSDIDSA
     KKCVEMNGHF IAGRPCRLDF STPRTGGGSR GGRGGFGGRG GFGGRGGFGG GRGRGRGGAR
     SGNPNRGSVA PFSGNKVTFD
 
 
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