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BIN4_ARATH
ID   BIN4_ARATH              Reviewed;         454 AA.
AC   Q9FLU1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=DNA-binding protein BIN4;
DE   AltName: Full=Protein BRASSINOSTEROID INSENSITIVE 4;
DE   AltName: Full=Protein MIDGET;
GN   Name=BIN4; Synonyms=MID; OrderedLocusNames=At5g24630; ORFNames=K18P6.17;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INTERACTION WITH RHL1.
RX   PubMed=17951446; DOI=10.1105/tpc.107.054361;
RA   Kirik V., Schrader A., Uhrig J.F., Hulskamp M.;
RT   "MIDGET unravels functions of the Arabidopsis topoisomerase VI complex in
RT   DNA endoreduplication, chromatin condensation, and transcriptional
RT   silencing.";
RL   Plant Cell 19:3100-3110(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   INTERACTION WITH TOP6A; TOP6B; BIN4 AND RHL1, AND DISRUPTION PHENOTYPE.
RX   PubMed=18055605; DOI=10.1105/tpc.107.054833;
RA   Breuer C., Stacey N.J., West C.E., Zhao Y., Chory J., Tsukaya H., Azumi Y.,
RA   Maxwell A., Roberts K., Sugimoto-Shirasu K.;
RT   "BIN4, a novel component of the plant DNA topoisomerase VI complex, is
RT   required for endoreduplication in Arabidopsis.";
RL   Plant Cell 19:3655-3668(2007).
CC   -!- FUNCTION: Component of the DNA topoisomerase VI complex. Binds to DNA.
CC       Required for chromatin organization and progression of
CC       endoreduplication cycles. The loss of BIN4 activates the ATM- and ATR-
CC       dependent DNA damage responses in postmitotic cells and induces the
CC       ectopic expression of the mitotic G2/M-specific cyclin B1;1 gene in
CC       non-dividing cells. {ECO:0000269|PubMed:17951446,
CC       ECO:0000269|PubMed:18055605}.
CC   -!- SUBUNIT: Interacts with TOP6A, RHL1 and itself, but not with TOP6B.
CC       {ECO:0000269|PubMed:17951446, ECO:0000269|PubMed:18055605}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17951446,
CC       ECO:0000269|PubMed:18055605}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9FLU1-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in expanding cotyledons, vascular cells,
CC       elongating root cells, developing leaf trichomes, root and apical
CC       meristems and lateral root primordia. {ECO:0000269|PubMed:17951446,
CC       ECO:0000269|PubMed:18055605}.
CC   -!- DEVELOPMENTAL STAGE: Ubiquitously expressed at low levels during the
CC       mitotic cell cycle. {ECO:0000269|PubMed:18055605}.
CC   -!- DISRUPTION PHENOTYPE: Plants show a severe dwarf phenotype. In bin4
CC       mutants, a specific DNA damage repair checkpoint is activated
CC       preventing further progression of endoreplication cycles.
CC       {ECO:0000269|PubMed:18055605}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB11215.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB010068; BAB11215.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED93342.1; -; Genomic_DNA.
DR   RefSeq; NP_001154739.1; NM_001161267.1. [Q9FLU1-1]
DR   AlphaFoldDB; Q9FLU1; -.
DR   BioGRID; 17809; 2.
DR   IntAct; Q9FLU1; 1.
DR   STRING; 3702.AT5G24630.6; -.
DR   iPTMnet; Q9FLU1; -.
DR   PaxDb; Q9FLU1; -.
DR   PRIDE; Q9FLU1; -.
DR   ProteomicsDB; 240841; -. [Q9FLU1-1]
DR   EnsemblPlants; AT5G24630.6; AT5G24630.6; AT5G24630. [Q9FLU1-1]
DR   GeneID; 832534; -.
DR   Gramene; AT5G24630.6; AT5G24630.6; AT5G24630. [Q9FLU1-1]
DR   KEGG; ath:AT5G24630; -.
DR   Araport; AT5G24630; -.
DR   TAIR; locus:2153939; AT5G24630.
DR   eggNOG; ENOG502QTVM; Eukaryota.
DR   InParanoid; Q9FLU1; -.
DR   OrthoDB; 1201463at2759; -.
DR   PhylomeDB; Q9FLU1; -.
DR   PRO; PR:Q9FLU1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FLU1; baseline and differential.
DR   Genevisible; Q9FLU1; AT.
DR   GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IPI:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:TAIR.
DR   GO; GO:0051276; P:chromosome organization; IMP:TAIR.
DR   GO; GO:0042023; P:DNA endoreduplication; IMP:TAIR.
DR   GO; GO:0009913; P:epidermal cell differentiation; IMP:TAIR.
DR   GO; GO:0030307; P:positive regulation of cell growth; IMP:TAIR.
DR   GO; GO:0048364; P:root development; IMP:TAIR.
DR   GO; GO:0048367; P:shoot system development; IMP:TAIR.
DR   GO; GO:0010090; P:trichome morphogenesis; IMP:TAIR.
DR   InterPro; IPR033246; BIN4.
DR   PANTHER; PTHR34810; PTHR34810; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Nucleus; Reference proteome.
FT   CHAIN           1..454
FT                   /note="DNA-binding protein BIN4"
FT                   /id="PRO_0000346107"
FT   REGION          24..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..441
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  49485 MW;  022EC68551BA5362 CRC64;
     MSSSSREGSP DWLRSYEAPM TTSLLSLSSS DDDSPYRESE VISSLPLPDD DGDDIVVLET
     ESVELLTRKN SETKVVTKQV SIEQVFSRKK KADASLNLED SCAGKENGNN VDCEKLSSKH
     KDAQGGADSV WLVSSDSEPS SPIKQEVTVS TEKDADFVLE ATEEEPAVKT VRKEKSPKTK
     SKSSRKTPKE GNSAQEILKT EDKDTDTTIA EQVTPEKSPK TKSKSSRKTP KEENCAQEIL
     KTEDKDKDTD TDTIIAEEVT TDQKIKPSSG SSSRLPLVLS EKVNRTKVLV ECEGDSIDLS
     GDMGAVGRVV VSDTTGDMYL DLKGTIYKST IIPSRTFCVV NVGQTEAKIE AIMNDFIQLI
     PQSNVYEAET MVEGTLEGFT FESDDESNKN AKTAVKPADQ SVGTEEETNT KAKPKAKAKG
     ETVIGKKRGR PSKEKQPPAK KARNSAPKKP KAKK
 
 
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