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IEC1_SCHPO
ID   IEC1_SCHPO              Reviewed;         249 AA.
AC   Q9UTM0;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=INO80 complex subunit 1;
GN   Name=iec1; ORFNames=SPAC144.02;
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]
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   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   [3]
RP   IDENTIFICATION IN THE INO80 COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=19040720; DOI=10.1186/gb-2008-9-11-r167;
RA   Shevchenko A., Roguev A., Schaft D., Buchanan L., Habermann B., Sakalar C.,
RA   Thomas H., Krogan N.J., Shevchenko A., Stewart A.F.;
RT   "Chromatin Central: towards the comparative proteome by accurate mapping of
RT   the yeast proteomic environment.";
RL   Genome Biol. 9:R167.1-R167.22(2008).
CC   -!- FUNCTION: Component of the INO80 complex which remodels chromatin by
CC       shifting nucleosomes and is involved in DNA repair.
CC   -!- SUBUNIT: Component of the INO80 chromatin remodeling complex.
CC       {ECO:0000269|PubMed:19040720}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm
CC       {ECO:0000269|PubMed:16823372}.
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DR   EMBL; CU329670; CAB59682.1; -; Genomic_DNA.
DR   PIR; T37669; T37669.
DR   RefSeq; NP_594663.1; NM_001020092.2.
DR   AlphaFoldDB; Q9UTM0; -.
DR   SMR; Q9UTM0; -.
DR   BioGRID; 279300; 12.
DR   STRING; 4896.SPAC144.02.1; -.
DR   MaxQB; Q9UTM0; -.
DR   PaxDb; Q9UTM0; -.
DR   EnsemblFungi; SPAC144.02.1; SPAC144.02.1:pep; SPAC144.02.
DR   GeneID; 2542854; -.
DR   KEGG; spo:SPAC144.02; -.
DR   PomBase; SPAC144.02; iec1.
DR   VEuPathDB; FungiDB:SPAC144.02; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_046889_0_1_1; -.
DR   InParanoid; Q9UTM0; -.
DR   OMA; GMAHASG; -.
DR   PhylomeDB; Q9UTM0; -.
DR   PRO; PR:Q9UTM0; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0031011; C:Ino80 complex; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0003677; F:DNA binding; ISM:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0034080; P:CENP-A containing chromatin assembly; IMP:PomBase.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:PomBase.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:PomBase.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Cytoplasm; DNA damage; DNA repair; DNA-binding;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..249
FT                   /note="INO80 complex subunit 1"
FT                   /id="PRO_0000046868"
FT   ZN_FING         73..100
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         106..131
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
SQ   SEQUENCE   249 AA;  28348 MW;  4228FA9704DBA19F CRC64;
     MSISSDTSGS VPGSPIDLEP ESETICHWQS CEQDLLTLDN LVHHIHNGTT SNLRLISNIN
     SILDHIGNRR PKYTCEWDDC PRKGMVQTSR FALVAHLRSH TGEKPFICSV PECDRSFTRS
     DALAKHMRTV HEADTLRPSD PIPKAHPMHP QNVANAMVQS AREARAQQQM HGVGNTNEDV
     ENWLDAASMP KTSHDMYRLQ KRKLQWVKEE RTMLANHLEA LERKLIDARN RKEKILNEIV
     KQVDPSISR
 
 
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