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YK42_SCHPO
ID   YK42_SCHPO              Reviewed;         566 AA.
AC   Q9P7G6;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Transcription factor P14E8.02 {ECO:0000312|EMBL:CAB77003.1};
GN   ORFNames=SPAP14E8.02;
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] {ECO:0000312|EMBL:CAB77003.1}
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] {ECO:0000305}
RP   FUNCTION, AND INDUCTION.
RX   PubMed=15195092; DOI=10.1038/ng1377;
RA   Rustici G., Mata J., Kivinen K., Lio P., Penkett C.J., Burns G., Hayles J.,
RA   Brazma A., Nurse P., Baehler J.;
RT   "Periodic gene expression program of the fission yeast cell cycle.";
RL   Nat. Genet. 36:809-817(2004).
RN   [3] {ECO:0000305}
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] {ECO:0000305}
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-379 AND SER-382, 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: Probable transcriptional regulatory protein Required for G1/S
CC       progression. {ECO:0000269|PubMed:15195092}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- INDUCTION: Transcriptionally regulated in a cell cycle-dependent manner
CC       by the mlu1 cell-cycle box binding factor (MBF) complex independently
CC       of sep1 and ace2. Strongly up-regulated in cells arrested in S phase by
CC       hydroxyurea. {ECO:0000269|PubMed:15195092}.
CC   -!- SIMILARITY: Belongs to the PLM2/TOS4 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB77003.1; -; Genomic_DNA.
DR   RefSeq; NP_593538.1; NM_001018972.2.
DR   AlphaFoldDB; Q9P7G6; -.
DR   BioGRID; 278504; 105.
DR   STRING; 4896.SPAP14E8.02.1; -.
DR   iPTMnet; Q9P7G6; -.
DR   MaxQB; Q9P7G6; -.
DR   PaxDb; Q9P7G6; -.
DR   PRIDE; Q9P7G6; -.
DR   EnsemblFungi; SPAP14E8.02.1; SPAP14E8.02.1:pep; SPAP14E8.02.
DR   GeneID; 2542021; -.
DR   KEGG; spo:SPAP14E8.02; -.
DR   PomBase; SPAP14E8.02; -.
DR   VEuPathDB; FungiDB:SPAP14E8.02; -.
DR   eggNOG; ENOG502RZJP; Eukaryota.
DR   HOGENOM; CLU_027207_0_0_1; -.
DR   InParanoid; Q9P7G6; -.
DR   OMA; KQHKQYF; -.
DR   PhylomeDB; Q9P7G6; -.
DR   PRO; PR:Q9P7G6; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0003682; F:chromatin binding; ISO:PomBase.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:PomBase.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:PomBase.
DR   CDD; cd00060; FHA; 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   Pfam; PF00498; FHA; 1.
DR   SUPFAM; SSF49879; SSF49879; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..566
FT                   /note="Transcription factor P14E8.02"
FT                   /id="PRO_0000353195"
FT   DOMAIN          86..137
FT                   /note="FHA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          312..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         379
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         382
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   566 AA;  64103 MW;  2BA96729AFA8A556 CRC64;
     MNISSQNVLL PSPIPSSSPM ASHKKSWLSK HPNQSMTFEK PQLGQFVLTP EPSSNTFYAP
     SSPASAVRRE PLSPMSFVRM RSHRVNKIGR SSQQCDHVLS TVDKAISRVH AIVTCTQDRM
     IIECVGWNGM IVSDKMRKSV FHMKKNDRIV LVRPNSDACP VLDVFGYRVL LGWPSDSEDE
     WEGNLNAKNY EENREPMSPS PQEALPLMPS SPPSQDYQND QNHLILYTNS ESIPKLNLRS
     NELVYPPPSK DLLQKLLALE KDGQVEKSDC SKNTQLKPSF LPKNTDDLLN GTDDNNIVLR
     EVKVSFENEK IESDDLDKNE EISEGEEYTP IEESKEPITV RRDSVIQIDE SSAGLTDVIS
     ELNFTNHNDD SKNSNITTSN DSPVNEVEPM APELSSAVVE KKEPEDYESI SAVDENTNDS
     NESLPSSHDY SESTKENSAP DSLLLGLVLD ELVFSTTSTT PLPALSHLFP SNMPLQLIQD
     KLRDLAAKHP YFEEVKRYGT DANGDPLWSE WFYNPDVDDD LERRMRYAPL MRPVRSSRRV
     HKQYYWKKPR ARPRSSGHSS RRRRLS
 
 
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