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ESC1_SCHPO
ID   ESC1_SCHPO              Reviewed;         413 AA.
AC   Q04635;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 139.
DE   RecName: Full=Protein esc1;
GN   Name=esc1; ORFNames=SPAC56F8.16;
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 [MRNA].
RX   PubMed=8381348; DOI=10.1002/j.1460-2075.1993.tb05639.x;
RA   Benton B.K., Read M.S., Okayama H.;
RT   "A Schizosaccharomyces pombe gene that promotes sexual differentiation
RT   encodes a helix-loop-helix protein with homology to MyoD.";
RL   EMBO J. 12:135-143(1993).
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).
CC   -!- FUNCTION: Involved in the sexual differentiation process. Modulate the
CC       ability of the cell to differentiate in response to the nitrogen
CC       starvation signal; in particular in response to decreases in the level
CC       of cellular cAMP.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR   EMBL; X69389; CAA49186.1; -; mRNA.
DR   EMBL; CU329670; CAA93587.1; -; Genomic_DNA.
DR   PIR; S28066; S28066.
DR   RefSeq; NP_593230.1; NM_001018627.2.
DR   AlphaFoldDB; Q04635; -.
DR   SMR; Q04635; -.
DR   BioGRID; 279711; 5.
DR   STRING; 4896.SPAC56F8.16.1; -.
DR   PaxDb; Q04635; -.
DR   EnsemblFungi; SPAC56F8.16.1; SPAC56F8.16.1:pep; SPAC56F8.16.
DR   GeneID; 2543286; -.
DR   KEGG; spo:SPAC56F8.16; -.
DR   PomBase; SPAC56F8.16; esc1.
DR   VEuPathDB; FungiDB:SPAC56F8.16; -.
DR   eggNOG; KOG2483; Eukaryota.
DR   HOGENOM; CLU_750395_0_0_1; -.
DR   InParanoid; Q04635; -.
DR   OMA; PINCIAK; -.
DR   PRO; PR:Q04635; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; TAS:PomBase.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; TAS:PomBase.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0031141; P:induction of conjugation upon carbon starvation; IMP:PomBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:PomBase.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   2: Evidence at transcript level;
KW   Differentiation; DNA-binding; Nucleus; Reference proteome.
FT   CHAIN           1..413
FT                   /note="Protein esc1"
FT                   /id="PRO_0000127170"
FT   DOMAIN          334..385
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          1..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   413 AA;  44798 MW;  B8BF7DD11545A739 CRC64;
     MSSYALPSMQ PTPTSSIPLR QMSQPTTSAP SNSASSTPYS PQQVPLTHNS YPLSTPSSFQ
     HGQTRLPPIN CLAEPFNRPQ PWHSNSAAPA SSSPTSATLS TAAHPVHTNA AQVAGSSSSY
     VYSVPPTNST TSQASAKHSA VPHRSSQFQS TTLTPSTTDS SSTDVSSSDS VSTSASSSNA
     SNTVSVTSPA SSSATPLPNQ PSQQQFLVSK NDAFTTFVHS VHNTPMQQSM YVPQQQTSHS
     SGASYQNESA NPPVQSPMQY SYSQGQPFSY PQHKNQSFSA SPIDPSMSYV YRAPESFSSI
     NANVPYGRNE YLRRVTSLVP NQPEYTGPYT RNPELRTSHK LAERKRRKEI KELFDDLKDA
     LPLDKSTKSS KWGLLTRAIQ YIEQLKSEQV ALEAYVKSLE ENMQSNKEVT KGT
 
 
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