BUB3_PONAB
ID BUB3_PONAB Reviewed; 328 AA.
AC Q5RB58;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Mitotic checkpoint protein BUB3;
GN Name=BUB3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR858797; CAH91002.1; -; mRNA.
DR RefSeq; NP_001125579.1; NM_001132107.1.
DR AlphaFoldDB; Q5RB58; -.
DR SMR; Q5RB58; -.
DR STRING; 9601.ENSPPYP00000003192; -.
DR GeneID; 100172494; -.
DR KEGG; pon:100172494; -.
DR CTD; 9184; -.
DR eggNOG; KOG1036; Eukaryota.
DR InParanoid; Q5RB58; -.
DR OrthoDB; 1048963at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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; 2.
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..328
FT /note="Mitotic checkpoint protein BUB3"
FT /id="PRO_0000050893"
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 328 AA; 37143 MW; 6168B69D5B140A3B CRC64;
MTGSNEFKLN QPPEDGISSV KFSPNTSQFL LVSSWDTSVR LYDVPANSMR LKYQHTGAVL
DCAFYDPTHA WSGGLDHQLK MHDLNTDQEN LVGTHDAPIR CVEYCPEVNV MATGSWDQTV
KLWDPRTPCN AGTFSQPEKV YTLSVSGDRL IVGTAGRRVL VWDLRNMGYV QQRRESSLKY
QTRCIRAFLN KQGYVLSSIE GRVAVEYLDP SPEVQKKKYA FKCHRLKENN IEQIYPVNAI
SFHNIHNTFA TGGSDGFVNI WDPFNKKRLC QFHRYPTSIA SLAFSNDGTT LAIASSYMYE
MDDTEHPEDG IFIRQVTDAE TKPKSPCT