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SWC4_SCHPO
ID   SWC4_SCHPO              Reviewed;         437 AA.
AC   O14308;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=SWR1-complex protein 4;
GN   Name=swc4; ORFNames=SPAC9G1.13c;
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).
CC   -!- FUNCTION: Component of the SWR1 complex which mediates the ATP-
CC       dependent exchange of histone H2A for the H2A variant HZT1 leading to
CC       transcriptional regulation of selected genes by chromatin remodeling.
CC       Component of the NuA4 histone acetyltransferase complex which is
CC       involved in transcriptional activation of selected genes principally by
CC       acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also
CC       involved in DNA repair (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the SWR1 chromatin-remodeling complex and of the
CC       NuA4 histone acetyltransferase complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SWC4 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB11497.2; -; Genomic_DNA.
DR   PIR; T39236; T39236.
DR   RefSeq; NP_593568.2; NM_001019001.3.
DR   AlphaFoldDB; O14308; -.
DR   SMR; O14308; -.
DR   BioGRID; 278876; 5.
DR   IntAct; O14308; 1.
DR   MINT; O14308; -.
DR   STRING; 4896.SPAC9G1.13c.1; -.
DR   iPTMnet; O14308; -.
DR   MaxQB; O14308; -.
DR   PaxDb; O14308; -.
DR   EnsemblFungi; SPAC9G1.13c.1; SPAC9G1.13c.1:pep; SPAC9G1.13c.
DR   GeneID; 2542412; -.
DR   KEGG; spo:SPAC9G1.13c; -.
DR   PomBase; SPAC9G1.13c; swc4.
DR   VEuPathDB; FungiDB:SPAC9G1.13c; -.
DR   eggNOG; KOG2656; Eukaryota.
DR   HOGENOM; CLU_018539_4_1_1; -.
DR   InParanoid; O14308; -.
DR   OMA; MYQSSQG; -.
DR   PhylomeDB; O14308; -.
DR   PRO; PR:O14308; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000812; C:Swr1 complex; IDA:PomBase.
DR   GO; GO:0003677; F:DNA binding; ISO:PomBase.
DR   GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; ISO:PomBase.
DR   GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR   GO; GO:0043968; P:histone H2A acetylation; IBA:GO_Central.
DR   GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0034728; P:nucleosome organization; IC:PomBase.
DR   InterPro; IPR032563; DAMP1_SANT-like.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR027109; Swc4/Dmap1.
DR   PANTHER; PTHR12855; PTHR12855; 1.
DR   Pfam; PF16282; SANT_DAMP1_like; 1.
DR   SMART; SM00717; SANT; 1.
PE   3: Inferred from homology;
KW   Activator; Chromatin regulator; DNA damage; DNA repair; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..437
FT                   /note="SWR1-complex protein 4"
FT                   /id="PRO_0000076344"
FT   DOMAIN          125..176
FT                   /note="SANT"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   437 AA;  50384 MW;  88C1F0B4592D3CE1 CRC64;
     MTSADIRDVF ELPPPEIGNK QKSKTPTERR PEGISRELYS LLGENSAPLA IYQKKFKEKP
     KVSHKAKNWV RQPFSISSRK DDFTLHHWVL KSEVDSEASY KFEKFNVPLF IIDYTDEEYQ
     NYLKDEDWNK DETDYLFRLC KDYDLRFFVI ADRYDNEKYK KHRTLEDLKD RFYSVSRKIL
     LARNPINSMT AAQSSLLNTM EYNKEQEVIR KKYLIGLASR TPEEVAEEEA LFIELKRIET
     SQAKLLSDRD EVLRLLDEQK GDGGIHEYHT SAGMSSLIQD MINSQRTKNK VEEAIVSSSA
     PSSGVSSVLN TPTRPHALST PRIRYGPQPT DPQFGITWHE KLHPGTFVRS QKIPAIKASL
     SQRVSSVMTE LGVSSRLIMP TAKNFEKFVE LQNSIVSLLE LKRKVDRLSQ ETEIQDKLSR
     KRSASPDGSE SKKHISQ
 
 
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