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BUB3_BOVIN
ID   BUB3_BOVIN              Reviewed;         326 AA.
AC   Q1JQB2; A5D9G0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Mitotic checkpoint protein BUB3;
GN   Name=BUB3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) 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. Regulates
CC       chromosome segregation during oocyte meiosis. The BUB1/BUB3 complex
CC       plays a role in the inhibition of anaphase-promoting complex or
CC       cyclosome (APC/C) when spindle-assembly checkpoint is activated and
CC       inhibits the ubiquitin ligase activity of APC/C by phosphorylating its
CC       activator CDC20. This complex can also phosphorylate MAD1L1 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with BUB1 and BUBR1. The BUB1/BUB3 complex interacts
CC       with MAD1L1. Interacts with ZNF207/BuGZ; leading to promote stability
CC       and kinetochore loading of BUB3 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere,
CC       kinetochore {ECO:0000250}. Note=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. {ECO:0000250}.
CC   -!- PTM: Poly-ADP-ribosylated by PARP1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat BUB3 family. {ECO:0000305}.
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DR   EMBL; BT030579; ABQ13019.1; -; mRNA.
DR   EMBL; BC116090; AAI16091.1; -; mRNA.
DR   RefSeq; NP_001069645.1; NM_001076177.1.
DR   AlphaFoldDB; Q1JQB2; -.
DR   SMR; Q1JQB2; -.
DR   STRING; 9913.ENSBTAP00000051164; -.
DR   PaxDb; Q1JQB2; -.
DR   PeptideAtlas; Q1JQB2; -.
DR   PRIDE; Q1JQB2; -.
DR   Ensembl; ENSBTAT00000057027; ENSBTAP00000051164; ENSBTAG00000017913.
DR   GeneID; 539594; -.
DR   KEGG; bta:539594; -.
DR   CTD; 9184; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017913; -.
DR   VGNC; VGNC:26606; BUB3.
DR   eggNOG; KOG1036; Eukaryota.
DR   GeneTree; ENSGT00950000183091; -.
DR   HOGENOM; CLU_038526_0_0_1; -.
DR   InParanoid; Q1JQB2; -.
DR   OMA; WDPFNRK; -.
DR   OrthoDB; 1048963at2759; -.
DR   TreeFam; TF105454; -.
DR   Reactome; R-BTA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR   Proteomes; UP000009136; Chromosome 26.
DR   Bgee; ENSBTAG00000017913; Expressed in oocyte and 107 other tissues.
DR   GO; GO:1990298; C:bub1-bub3 complex; IBA:GO_Central.
DR   GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR   GO; GO:0033597; C:mitotic checkpoint complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IEA:Ensembl.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IEA:Ensembl.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IEA:Ensembl.
DR   GO; GO:0034501; P:protein localization to kinetochore; IEA:Ensembl.
DR   GO; GO:0051983; P:regulation of chromosome segregation; ISS:UniProtKB.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00400; WD40; 3.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ADP-ribosylation; Cell cycle; Cell division; Centromere;
KW   Chromosome; Chromosome partition; Isopeptide bond; Kinetochore; Meiosis;
KW   Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Ubl conjugation; WD repeat.
FT   CHAIN           1..326
FT                   /note="Mitotic checkpoint protein BUB3"
FT                   /id="PRO_0000254025"
FT   REPEAT          5..43
FT                   /note="WD 1"
FT   REPEAT          46..83
FT                   /note="WD 2"
FT   REPEAT          86..124
FT                   /note="WD 3"
FT   REPEAT          128..163
FT                   /note="WD 4"
FT   REPEAT          223..262
FT                   /note="WD 5"
FT   MOD_RES         179
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O43684"
FT   MOD_RES         211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43684"
FT   CROSSLNK        216
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:O43684"
SQ   SEQUENCE   326 AA;  36955 MW;  F1EA57368E5A6345 CRC64;
     MTGSNEFKLN QPPEDGISSV KFSPNTSQFL LVSSWDTSVR LYDVPANSMR LKYQHTGAVL
     DCAFYDPTHA WSGGLDHQLK MHDLNTDQEN LVGTHDAPIR CVEYCPEVNV MVTGSWDQTV
     KLWDPRTPCN AGTFSQPEKV YTLSVSGDRL IVGTAGRRVL VWDLRNMGYV QQRRESSLKY
     QTRCIRAFPN KQGYVLSSIE GRVAVEYLDP SPEVQKKKYA FKCHRLKENN IEQIYPVNAI
     SFHNIHNTFA TGGSDGFVNI WDPFNKKRLC QFHRYPTSIA SLAFSNDGTT LAIASSYMYE
     MDDTEHPEDG IFIRQVTDAE TKPKST
 
 
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