BOREA_PONAB
ID BOREA_PONAB Reviewed; 280 AA.
AC Q5RBS5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Borealin;
DE AltName: Full=Cell division cycle-associated protein 8;
GN Name=CDCA8;
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=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the chromosomal passenger complex (CPC), a
CC complex that acts as a key regulator of mitosis. The CPC complex has
CC essential functions at the centromere in ensuring correct chromosome
CC alignment and segregation and is required for chromatin-induced
CC microtubule stabilization and spindle assembly. In the complex, it may
CC be required to direct the CPC to centromeric DNA (By similarity).
CC {ECO:0000250|UniProtKB:Q53HL2}.
CC -!- SUBUNIT: May form homooligomers and homodimers. Component of the
CC chromosomal passenger complex (CPC) composed of at least
CC BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; in the complex
CC forms a triple-helix bundle-based subcomplex with INCENP and BIRC5.
CC Interacts with SENP3, UBE2I and RANBP2. Interacts (phosphorylated) with
CC SGO1 and SGO2; the association is dependent on CDK1 (By similarity).
CC {ECO:0000250|UniProtKB:Q53HL2}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q53HL2}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q53HL2}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:Q53HL2}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q53HL2}. Note=Localizes on chromosome arms and
CC inner centromeres from prophase through metaphase and then transferring
CC to the spindle midzone and midbody from anaphase through cytokinesis.
CC {ECO:0000250|UniProtKB:Q53HL2}.
CC -!- DOMAIN: The C-terminal region (aa 207-280) represents the dimerization
CC motif.
CC -!- PTM: Phosphorylated by TTK, essentially at Thr-88, Thr94, Thr-169 and
CC Thr-230. Phosphorylation (probably by CDK1) promotes targeting of the
CC CPC to centromeric DNA. {ECO:0000250|UniProtKB:Q53HL2}.
CC -!- PTM: Sumoylated by UBE2I and RANBP2. Desumoylated by SENP3 through the
CC removal of SUMO2 and SUMO3. {ECO:0000250|UniProtKB:Q53HL2}.
CC -!- SIMILARITY: Belongs to the borealin family. {ECO:0000305}.
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DR EMBL; CR858559; CAH90785.1; -; mRNA.
DR RefSeq; NP_001127334.1; NM_001133862.1.
DR AlphaFoldDB; Q5RBS5; -.
DR BMRB; Q5RBS5; -.
DR SMR; Q5RBS5; -.
DR GeneID; 100174395; -.
DR KEGG; pon:100174395; -.
DR CTD; 55143; -.
DR InParanoid; Q5RBS5; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0032133; C:chromosome passenger complex; ISS:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR InterPro; IPR018851; Borealin_N.
DR InterPro; IPR018867; Cell_div_borealin.
DR Pfam; PF10512; Borealin; 1.
DR Pfam; PF10444; Nbl1_Borealin_N; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..280
FT /note="Borealin"
FT /id="PRO_0000247077"
FT REGION 1..140
FT /note="Required for interaction with SENP3"
FT /evidence="ECO:0000250"
FT REGION 1..88
FT /note="Required for centromere localization"
FT /evidence="ECO:0000250"
FT REGION 1..58
FT /note="Required for interaction with INCENP"
FT /evidence="ECO:0000250"
FT REGION 10..109
FT /note="Required to form a minimal CPC core complex that
FT localizes to the central spindle and midbody and properly
FT executes the role of the CPC during cytokinesis"
FT /evidence="ECO:0000250"
FT REGION 20..78
FT /note="Required for interaction with INCENP and BIRC5"
FT /evidence="ECO:0000250"
FT REGION 130..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 88
FT /note="Phosphothreonine; by TTK"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 94
FT /note="Phosphothreonine; by TTK"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 165
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 169
FT /note="Phosphothreonine; by TTK"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 189
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 204
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 230
FT /note="Phosphothreonine; by TTK"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
SQ SEQUENCE 280 AA; 31323 MW; 519978A7C295C571 CRC64;
MAPRKGSSRV AKTNSLRRRK LASFLKDFDR EVEIRIKQIE SDRQNLLKEV DNLYNIEILR
LPKALREMNW LDYFALGGNK QALEEAATAD LDITEINKLT AEAIQTPLKS AKTRKVIQVD
EMIVEEEEEE ENERKNLQTA RVKRCPPSKK RTQSIQGKGK GKRSSRANTV TPAVGRLEVS
MVKPTPGLTP RFDSRVFKTP GLRTPAAGER IYNISGNGSP LADSKEIFLT VPVGGGESLR
LLASDLQRHS IAQLDPEALG NIKKLSNRLA QICSSIRTHK
