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PPC89_SCHPO
ID   PPC89_SCHPO             Reviewed;         783 AA.
AC   Q10218;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Spindle pole body protein ppc89;
DE   AltName: Full=Meiotically up-regulated gene 127 protein;
GN   Name=ppc89; Synonyms=mug127; ORFNames=SPAC4H3.11c;
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   FUNCTION IN MEIOSIS.
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   [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-157, 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: Has a role in meiosis. {ECO:0000269|PubMed:16303567}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole
CC       body {ECO:0000269|PubMed:16823372}.
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DR   EMBL; CU329670; CAA93350.1; -; Genomic_DNA.
DR   PIR; T38891; T38891.
DR   RefSeq; NP_594347.1; NM_001019768.2.
DR   AlphaFoldDB; Q10218; -.
DR   SMR; Q10218; -.
DR   BioGRID; 279971; 11.
DR   IntAct; Q10218; 2.
DR   STRING; 4896.SPAC4H3.11c.1; -.
DR   iPTMnet; Q10218; -.
DR   MaxQB; Q10218; -.
DR   PaxDb; Q10218; -.
DR   PRIDE; Q10218; -.
DR   EnsemblFungi; SPAC4H3.11c.1; SPAC4H3.11c.1:pep; SPAC4H3.11c.
DR   GeneID; 2543554; -.
DR   KEGG; spo:SPAC4H3.11c; -.
DR   PomBase; SPAC4H3.11c; ppc89.
DR   VEuPathDB; FungiDB:SPAC4H3.11c; -.
DR   eggNOG; ENOG502S7ZB; Eukaryota.
DR   HOGENOM; CLU_334364_0_0_1; -.
DR   InParanoid; Q10218; -.
DR   OMA; INCNAVH; -.
DR   PRO; PR:Q10218; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0061493; C:central plaque of mitotic spindle pole body; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0140475; F:spindle pole body anchor activity; EXP:PomBase.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0007052; P:mitotic spindle organization; EXP:PomBase.
DR   InterPro; IPR024957; Cep57_MT-bd_dom.
DR   InterPro; IPR025925; PPC89_CLD.
DR   Pfam; PF14197; Cep57_CLD_2; 1.
DR   Pfam; PF06657; Cep57_MT_bd; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Meiosis; Phosphoprotein; Reference proteome.
FT   CHAIN           1..783
FT                   /note="Spindle pole body protein ppc89"
FT                   /id="PRO_0000116485"
FT   REGION          180..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          471..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..549
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..584
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..599
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         157
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   783 AA;  89188 MW;  FA2FA539AE5682FE CRC64;
     MPSQFNDNFV ATDDDVGTMA RVGMALDREL NGDSFQDNLN FQPRSGKRED FEPFFQDTPN
     TKSLSKHFHD FTMNASLETL PSVEKPRGRN MNAFEETSWN RFRKNGSLFP LSSPPISEPD
     LRPQALNETP DYRNRFLGAF KKQGVLDDHG NLKLDASPSF LKKPAEYTPL ANRQNQNLAF
     DSPTEALPPK PTTPWRRNGF RSKTTPNLNS GKETPSSYKA SARLMEQLGL NHSEPSVDFN
     NQTSYRLPNL TNLSSLIRDD TIDENGNAKE HDRLPELNTI PVASTDEQLF NAHQLLEKKF
     EILKRERNEC NAKIDELQDK LELLTDAYNR EKRRARSLEE RMSKEMLTKL GESNVDDGMA
     ASRYDTVKRE KERLSEHLKS LQEQYEHIQS VYKNVLLDRE SYIMRLGNKI SENNELLNEN
     RVLKEKLQTY LDKKESNVTS KIKSTAENSS KPLSMNEADE RKDGLNNLLF ENKSGANTKE
     MSNGTETAKE NCSPQQDSTS PTSGYQDLVK ELAKEIEMRK SLELKLKLSQ SNKAGPVKHR
     KRRPKSKRRI TGKVVFDSPN VASGVESDEG SEEISLDSEY SDILSDDGDF EKEKQATLPR
     RRSSSSMKGN KLAEDSYLNE AGFDWNQGTF HNGSEFGTTG VPDEPNEEEL PKHVLKQVEH
     IINESAAHGV GKCNACHARQ EDLIRGEQKV SHSNCLYADQ TLRPSQPPSE ALKTVVNQLT
     NELMELKKRY EKLSDRYNSL TPGYHKHKRQ EIKNKLIKLI ECMESKSDQI YLLYDVNVGK
     DFS
 
 
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