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BUB33_ARATH
ID   BUB33_ARATH             Reviewed;         314 AA.
AC   F4I241; F4I242; Q8LA29; Q9C795; Q9C986;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Mitotic checkpoint protein BUB3.3;
DE   AltName: Full=Protein BUDDING UNINHIBITED BY BENZYMIDAZOL 3.3;
GN   Name=BUB3.3; OrderedLocusNames=At1g69400; ORFNames=F10D13.23, F23O10.3;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has a dual function in spindle-assembly checkpoint signaling
CC       and in promoting the establishment of correct kinetochore-microtubule
CC       (K-MT) attachments. Promotes the formation of stable end-on bipolar
CC       attachments. Necessary for kinetochore localization of BUB1. The
CC       BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting
CC       complex or cyclosome (APC/C) when spindle-assembly checkpoint is
CC       activated and inhibits the ubiquitin ligase activity of APC/C by
CC       phosphorylating its activator CDC20 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of the mitotic checkpoint complex (MCC). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere,
CC       kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, phragmoplast
CC       {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC       Note=Accumulates onto both kinetochores and the spindle microtubules in
CC       cell arrested in metaphase. Starts to localize at kinetochores in
CC       prometaphase I (Pro-MI) stage and maintains the localization until the
CC       metaphase I-anaphase I (MI-AI) transition. Associates with unattached
CC       kinetochores upon spindle assembly checkpoint (SAC) activation. Present
CC       in the phragmoplast midline during the final step of cell division (By
CC       similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=F4I241-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=F4I241-2; Sequence=VSP_047766;
CC   -!- SIMILARITY: Belongs to the WD repeat BUB3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG52491.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG60107.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BX814360; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AC018364; AAG52491.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC073178; AAG60107.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE34919.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34920.1; -; Genomic_DNA.
DR   EMBL; BX814360; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AY088063; AAM65609.1; -; mRNA.
DR   RefSeq; NP_564965.1; NM_105607.3. [F4I241-1]
DR   RefSeq; NP_974113.1; NM_202384.2. [F4I241-2]
DR   AlphaFoldDB; F4I241; -.
DR   SMR; F4I241; -.
DR   BioGRID; 28493; 15.
DR   IntAct; F4I241; 18.
DR   STRING; 3702.AT1G69400.1; -.
DR   PaxDb; F4I241; -.
DR   PRIDE; F4I241; -.
DR   ProteomicsDB; 240483; -. [F4I241-1]
DR   EnsemblPlants; AT1G69400.1; AT1G69400.1; AT1G69400. [F4I241-1]
DR   EnsemblPlants; AT1G69400.2; AT1G69400.2; AT1G69400. [F4I241-2]
DR   GeneID; 843272; -.
DR   Gramene; AT1G69400.1; AT1G69400.1; AT1G69400. [F4I241-1]
DR   Gramene; AT1G69400.2; AT1G69400.2; AT1G69400. [F4I241-2]
DR   KEGG; ath:AT1G69400; -.
DR   Araport; AT1G69400; -.
DR   TAIR; locus:2026446; AT1G69400.
DR   eggNOG; KOG1036; Eukaryota.
DR   HOGENOM; CLU_038526_3_0_1; -.
DR   InParanoid; F4I241; -.
DR   OMA; ENECKPK; -.
DR   PRO; PR:F4I241; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4I241; baseline and differential.
DR   Genevisible; F4I241; AT.
DR   GO; GO:1990298; C:bub1-bub3 complex; IBA:GO_Central.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR   GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR   GO; GO:0033597; C:mitotic checkpoint complex; IBA:GO_Central.
DR   GO; GO:0009524; C:phragmoplast; IBA:GO_Central.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW   Chromosome partition; Cytoplasm; Cytoskeleton; Kinetochore; Meiosis;
KW   Mitosis; Nucleus; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..314
FT                   /note="Mitotic checkpoint protein BUB3.3"
FT                   /id="PRO_0000423382"
FT   REPEAT          11..50
FT                   /note="WD 1"
FT   REPEAT          52..90
FT                   /note="WD 2"
FT   REPEAT          92..131
FT                   /note="WD 3"
FT   REPEAT          134..173
FT                   /note="WD 4"
FT   REPEAT          176..215
FT                   /note="WD 5"
FT   REPEAT          229..269
FT                   /note="WD 6"
FT   REPEAT          272..311
FT                   /note="WD 7"
FT   VAR_SEQ         242..313
FT                   /note="CGSGTFVTGDNEGYVISWNAKSRRRLNELPRYSNSIASLAFDHTGELLAIAS
FT                   SHTYQDAKEKEEAPQVFIHR -> WYMSLIHHLMVHMIDHQTNSFLVATVGQGL (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14993207"
FT                   /id="VSP_047766"
FT   CONFLICT        41
FT                   /note="D -> N (in Ref. 4; AAM65609)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69..70
FT                   /note="FT -> YA (in Ref. 4; AAM65609)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="V -> F (in Ref. 4; AAM65609)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="S -> A (in Ref. 4; AAM65609)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154
FT                   /note="D -> N (in Ref. 4; AAM65609)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   314 AA;  34763 MW;  3AE94B8B3086D8F9 CRC64;
     MSGDRLEFEN PIEDAVSRLR FSPQSNNLLV ASWDSYLRLY DVESSSLSLE LNSQAALLDC
     CFENESTSFT SGSDGFIRRY DLNAGTVDTI GRHDDISTSI VYSYEKGEVI STGFDEKIKF
     WDTRQRESLV FSTDAGGAVG CVTVSGNNLV VCVDASMHIY DLRNLDEAFQ SYASQVEVPI
     RCITSVPYSR GYAVGSVDGR VAVDFPNTSC SSEIKYSFRC HPKSRNGRLD GVCINAIEFS
     PCGSGTFVTG DNEGYVISWN AKSRRRLNEL PRYSNSIASL AFDHTGELLA IASSHTYQDA
     KEKEEAPQVF IHRL
 
 
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