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HAP3_SCHPO
ID   HAP3_SCHPO              Reviewed;         116 AA.
AC   P36611;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 153.
DE   RecName: Full=Transcriptional activator hap3;
GN   Name=hap3; Synonyms=php3; ORFNames=SPAC23C11.08;
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].
RC   STRAIN=401;
RX   PubMed=8223474; DOI=10.1002/j.1460-2075.1993.tb06153.x;
RA   Xing Y., Fikes J.D., Guarente L.;
RT   "Mutations in yeast HAP2/HAP3 define a hybrid CCAAT box binding domain.";
RL   EMBO J. 12:4647-4655(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: Belongs to a complex that binds to the sequence CCAAT located
CC       upstream of genes involved in mitochondrial electron transport.
CC   -!- SUBUNIT: Belongs to a heterotrimeric CCAAT-binding complex.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the NFYB/HAP3 subunit family. {ECO:0000305}.
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DR   EMBL; X75072; CAA52966.1; -; mRNA.
DR   EMBL; CU329670; CAB11161.1; -; Genomic_DNA.
DR   PIR; S42744; S42744.
DR   RefSeq; NP_593639.1; NM_001019070.1.
DR   AlphaFoldDB; P36611; -.
DR   SMR; P36611; -.
DR   BioGRID; 278509; 126.
DR   STRING; 4896.SPAC23C11.08.1; -.
DR   MaxQB; P36611; -.
DR   PaxDb; P36611; -.
DR   EnsemblFungi; SPAC23C11.08.1; SPAC23C11.08.1:pep; SPAC23C11.08.
DR   GeneID; 2542027; -.
DR   KEGG; spo:SPAC23C11.08; -.
DR   PomBase; SPAC23C11.08; -.
DR   VEuPathDB; FungiDB:SPAC23C11.08; -.
DR   eggNOG; KOG0869; Eukaryota.
DR   HOGENOM; CLU_066247_12_2_1; -.
DR   InParanoid; P36611; -.
DR   OMA; KQNHRTI; -.
DR   PhylomeDB; P36611; -.
DR   PRO; PR:P36611; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0016602; C:CCAAT-binding factor complex; ISO:PomBase.
DR   GO; GO:0000785; C:chromatin; NAS:PomBase.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0000429; P:carbon catabolite regulation of transcription from RNA polymerase II promoter; ISO:PomBase.
DR   GO; GO:0010723; P:positive regulation of transcription from RNA polymerase II promoter in response to iron; IMP:PomBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR003958; CBFA_NFYB_domain.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR027113; Transc_fact_NFYB/HAP3.
DR   InterPro; IPR003956; Transcrpt_fac_NFYB/HAP3_CS.
DR   PANTHER; PTHR11064; PTHR11064; 1.
DR   Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00685; NFYB_HAP3; 1.
PE   3: Inferred from homology;
KW   Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..116
FT                   /note="Transcriptional activator hap3"
FT                   /id="PRO_0000204632"
FT   DNA_BIND        12..18
FT                   /evidence="ECO:0000250"
FT   REGION          39..50
FT                   /note="Subunit association domain (SAD)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   116 AA;  12910 MW;  930DFCA773099CB5 CRC64;
     MSADGLDYTN LLPIANVARI MKSALPENAK ISKEAKDCVQ DCVSEFISFV TGEASEQCTQ
     EKRKTITGED VLLALNTLGF ENYAEVLKIS LTKYREQQAR SASMKETKQS RSEEPQ
 
 
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