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IGO1_SCHPO
ID   IGO1_SCHPO              Reviewed;         139 AA.
AC   P79058;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 4.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=mRNA stability protein mug134;
DE   AltName: Full=Initiation of G zero protein 1;
GN   Name=mug134; Synonyms=igo1; ORFNames=SPAC10F6.16;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 20-139.
RA   Kawamukai M.;
RT   "S.pombe cDNA YNL157w homolog.";
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INDUCTION.
RX   PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA   Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA   Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA   Smith G.R., Moreno S.;
RT   "A large-scale screen in S. pombe identifies seven novel genes required for
RT   critical meiotic events.";
RL   Curr. Biol. 15:2056-2062(2005).
RN   [4]
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).
CC   -!- FUNCTION: Plays an essential role in initiation of the G0 program by
CC       preventing the degradation of specific nutrient-regulated mRNAs via the
CC       5'-3' mRNA decay pathway.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- INDUCTION: Expressed during meiosis. {ECO:0000269|PubMed:16303567}.
CC   -!- SIMILARITY: Belongs to the endosulfine family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA15729.1; -; Genomic_DNA.
DR   EMBL; AB001289; BAA19234.1; -; mRNA.
DR   PIR; T37510; T37510.
DR   RefSeq; NP_593267.1; NM_001018664.2.
DR   AlphaFoldDB; P79058; -.
DR   SMR; P79058; -.
DR   BioGRID; 279401; 14.
DR   STRING; 4896.SPAC10F6.16.1; -.
DR   iPTMnet; P79058; -.
DR   MaxQB; P79058; -.
DR   PaxDb; P79058; -.
DR   PRIDE; P79058; -.
DR   EnsemblFungi; SPAC10F6.16.1; SPAC10F6.16.1:pep; SPAC10F6.16.
DR   GeneID; 2542961; -.
DR   KEGG; spo:SPAC10F6.16; -.
DR   PomBase; SPAC10F6.16; mug134.
DR   VEuPathDB; FungiDB:SPAC10F6.16; -.
DR   eggNOG; KOG4076; Eukaryota.
DR   HOGENOM; CLU_101493_1_0_1; -.
DR   OMA; RPKSHEA; -.
DR   PhylomeDB; P79058; -.
DR   PRO; PR:P79058; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IDA:PomBase.
DR   GO; GO:0035556; P:intracellular signal transduction; IMP:PomBase.
DR   GO; GO:0035308; P:negative regulation of protein dephosphorylation; IBA:GO_Central.
DR   GO; GO:1905287; P:positive regulation of G2/M transition of mitotic cell cycle involved in cellular response to nitrogen starvation; IMP:PomBase.
DR   GO; GO:1900237; P:positive regulation of induction of conjugation with cellular fusion; IGI:PomBase.
DR   GO; GO:1902471; P:regulation of mitotic actomyosin contractile ring localization; IGI:PomBase.
DR   InterPro; IPR006760; Endosulphine.
DR   PANTHER; PTHR10358; PTHR10358; 1.
DR   Pfam; PF04667; Endosulfine; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Reference proteome.
FT   CHAIN           1..139
FT                   /note="mRNA stability protein mug134"
FT                   /id="PRO_0000116735"
FT   REGION          83..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..125
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   139 AA;  15441 MW;  D8D9D2A388ADA532 CRC64;
     MVRTRKWMLS TTIIAMSSSN SEQKVDVAKL SPEEQKLFRL YGRLPQRKDL LVQKLQQGRK
     YFDSGDYALN KAGKASDSGI TCIGKEIPSP DTIPHRVVSA GSPNKEPSLH TKRPSESSPS
     GASSRRESVT RHDLESNEN
 
 
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