BOREA_RAT
ID BOREA_RAT Reviewed; 288 AA.
AC Q6AXW0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Borealin;
DE AltName: Full=Cell division cycle-associated protein 8;
GN Name=Cdca8;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 215-288) represents the dimerization
CC motif. {ECO:0000250}.
CC -!- PTM: Phosphorylated by TTK, essentially at Thr-88 and Thr-94.
CC Phosphorylation (probably by CDK1) promotes targeting of the CPC to
CC centromeric DNA. {ECO:0000250|UniProtKB:Q53HL2}.
CC -!- PTM: Sumoylated by UBE2I and RANBP2. Desumoylated by SENP3 through the
CC removal of SUMO2 and SUMO3 (By similarity).
CC {ECO:0000250|UniProtKB:Q53HL2}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q8BHX3}.
CC -!- SIMILARITY: Belongs to the borealin family. {ECO:0000305}.
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DR EMBL; BC079293; AAH79293.1; -; mRNA.
DR EMBL; BC079274; AAH79274.1; -; mRNA.
DR RefSeq; NP_001020221.1; NM_001025050.1.
DR RefSeq; XP_008762286.1; XM_008764064.1.
DR AlphaFoldDB; Q6AXW0; -.
DR SMR; Q6AXW0; -.
DR STRING; 10116.ENSRNOP00000043633; -.
DR iPTMnet; Q6AXW0; -.
DR PhosphoSitePlus; Q6AXW0; -.
DR jPOST; Q6AXW0; -.
DR PaxDb; Q6AXW0; -.
DR PRIDE; Q6AXW0; -.
DR Ensembl; ENSRNOT00000048293; ENSRNOP00000043633; ENSRNOG00000031431.
DR GeneID; 500545; -.
DR KEGG; rno:500545; -.
DR UCSC; RGD:1566306; rat.
DR CTD; 55143; -.
DR RGD; 1566306; Cdca8.
DR eggNOG; ENOG502QS4S; Eukaryota.
DR GeneTree; ENSGT00390000011115; -.
DR HOGENOM; CLU_074128_0_0_1; -.
DR InParanoid; Q6AXW0; -.
DR OMA; NWLEHWK; -.
DR OrthoDB; 1587028at2759; -.
DR PhylomeDB; Q6AXW0; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q6AXW0; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000031431; Expressed in testis and 18 other tissues.
DR Genevisible; Q6AXW0; RN.
DR GO; GO:0010369; C:chromocenter; ISO:RGD.
DR GO; GO:0032133; C:chromosome passenger complex; ISS:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
DR GO; GO:0030496; C:midbody; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; ISO:RGD.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:RGD.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR InterPro; IPR018851; Borealin_N.
DR InterPro; IPR018867; Cell_div_borealin.
DR Pfam; PF10512; Borealin; 1.
DR Pfam; PF10444; Nbl1_Borealin_N; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Citrullination;
KW Cytoplasm; Cytoskeleton; Isopeptide bond; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..288
FT /note="Borealin"
FT /id="PRO_0000247078"
FT REGION 1..149
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 124..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..157
FT /note="Basic 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 91
FT /note="Citrulline"
FT /evidence="ECO:0000250"
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 174
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 197
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 212
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
SQ SEQUENCE 288 AA; 32099 MW; 1CF10957DF7635CF CRC64;
MAPKKRSSRG TRTNTLRSRK LASFLKDFDR EVQVRTKQIE SDRQTLLKEV ENLYNIEVLR
LPKALQVMKW LDYFALGGNR QALEEAATAD RDITEINNLT AEAIQTPLKS VKKRKVIEVD
EAIKEEEEDE EEEGGGGGGR KSHKNLRSAR VKRCPPSKKR TQSIQGRSRS KRLSHDFVTP
AMSRLEPSLV KPTPGMTPRF DSRVFKTPGL RTPAAKEQVY NISINGSPLA DSKEISLSVP
IGGGASLRLL ASDLQRVDIA QLNPEALGNI KKLSSRLAQI CSSIRTGR
