BOREA_MOUSE
ID BOREA_MOUSE Reviewed; 289 AA.
AC Q8BHX3; B1ARX0; B1ARX1; Q6NVD3; Q8BHB1; Q8BHQ5; Q8BHQ9; Q9CRN4; Q9CS02;
AC Q9CTF4;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Borealin;
DE AltName: Full=Cell division cycle-associated protein 8;
DE AltName: Full=MESrg;
GN Name=Cdca8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Nie Z., Du J., Lu G.;
RT "The cloning and functional analysis of MESrg.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Head, Liver, Testis, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; SER-175 AND SER-228, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP CITRULLINATION AT ARG-91.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
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. Major effector of the
CC TTK kinase in the control of attachment-error-correction and chromosome
CC alignment (By similarity). {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 (By
CC similarity). Interacts with SENP3, UBE2I and RANBP2. Interacts
CC (phosphorylated) with SGO1 and SGO2; the association is dependent on
CC CDK1 (By similarity). {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 Colocalizes with SENP3 in the nucleolus in interphase cells.
CC {ECO:0000250|UniProtKB:Q53HL2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BHX3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BHX3-2; Sequence=VSP_019924;
CC Name=3;
CC IsoId=Q8BHX3-3; Sequence=VSP_019922, VSP_019923;
CC -!- DOMAIN: The C-terminal region (aa 216-289) represents the dimerization
CC motif. {ECO:0000250}.
CC -!- PTM: Phosphorylated by TTK, essentially at Thr-94. Phosphorylation
CC (probably by CDK1) promotes targeting of the CPC to centromeric DNA.
CC {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:0000269|PubMed:24463520}.
CC -!- SIMILARITY: Belongs to the borealin family. {ECO:0000305}.
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DR EMBL; AY550907; AAT34966.1; -; mRNA.
DR EMBL; AK003755; BAB22980.1; -; mRNA.
DR EMBL; AK010905; BAB27258.1; -; mRNA.
DR EMBL; AK020070; BAB31983.3; -; mRNA.
DR EMBL; AK076065; BAC36158.1; -; mRNA.
DR EMBL; AK076422; BAC36334.1; -; mRNA.
DR EMBL; AK077717; BAC36977.1; -; mRNA.
DR EMBL; AK077920; BAC37063.1; -; mRNA.
DR EMBL; AK078404; BAC37258.1; -; mRNA.
DR EMBL; AK082800; BAC38627.1; -; mRNA.
DR EMBL; AL606933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC068181; AAH68181.1; -; mRNA.
DR CCDS; CCDS18631.1; -. [Q8BHX3-1]
DR RefSeq; NP_080836.3; NM_026560.4. [Q8BHX3-1]
DR AlphaFoldDB; Q8BHX3; -.
DR SMR; Q8BHX3; -.
DR BioGRID; 206490; 22.
DR ComplexPortal; CPX-119; Chromosomal passenger complex.
DR IntAct; Q8BHX3; 23.
DR STRING; 10090.ENSMUSP00000081319; -.
DR iPTMnet; Q8BHX3; -.
DR PhosphoSitePlus; Q8BHX3; -.
DR EPD; Q8BHX3; -.
DR jPOST; Q8BHX3; -.
DR MaxQB; Q8BHX3; -.
DR PaxDb; Q8BHX3; -.
DR PeptideAtlas; Q8BHX3; -.
DR PRIDE; Q8BHX3; -.
DR ProteomicsDB; 265222; -. [Q8BHX3-1]
DR ProteomicsDB; 265223; -. [Q8BHX3-2]
DR ProteomicsDB; 265224; -. [Q8BHX3-3]
DR Antibodypedia; 31756; 486 antibodies from 34 providers.
DR DNASU; 52276; -.
DR Ensembl; ENSMUST00000030690; ENSMUSP00000030690; ENSMUSG00000028873. [Q8BHX3-2]
DR Ensembl; ENSMUST00000084296; ENSMUSP00000081319; ENSMUSG00000028873. [Q8BHX3-1]
DR GeneID; 52276; -.
DR KEGG; mmu:52276; -.
DR UCSC; uc008urj.2; mouse. [Q8BHX3-1]
DR UCSC; uc008urk.2; mouse. [Q8BHX3-3]
DR CTD; 55143; -.
DR MGI; MGI:1196274; Cdca8.
DR VEuPathDB; HostDB:ENSMUSG00000028873; -.
DR eggNOG; ENOG502QS4S; Eukaryota.
DR GeneTree; ENSGT00390000011115; -.
DR HOGENOM; CLU_074128_0_0_1; -.
DR InParanoid; Q8BHX3; -.
DR OMA; NWLEHWK; -.
DR OrthoDB; 1587028at2759; -.
DR PhylomeDB; Q8BHX3; -.
DR TreeFam; TF101077; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 52276; 25 hits in 75 CRISPR screens.
DR PRO; PR:Q8BHX3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BHX3; protein.
DR Bgee; ENSMUSG00000028873; Expressed in metanephric renal vesicle and 192 other tissues.
DR ExpressionAtlas; Q8BHX3; baseline and differential.
DR Genevisible; Q8BHX3; MM.
DR GO; GO:0010369; C:chromocenter; IDA:MGI.
DR GO; GO:0032133; C:chromosome passenger complex; ISS:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0051276; P:chromosome organization; ISO:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:MGI.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IC:ComplexPortal.
DR GO; GO:0007052; P:mitotic spindle organization; IC:ComplexPortal.
DR GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IC:ComplexPortal.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IC:ComplexPortal.
DR GO; GO:1903490; P:positive regulation of mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:1901970; P:positive regulation of mitotic sister chromatid separation; IC:ComplexPortal.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IC:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IC:ComplexPortal.
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 Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Citrullination; Cytoplasm; Cytoskeleton; Isopeptide bond; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..289
FT /note="Borealin"
FT /id="PRO_0000247076"
FT REGION 1..150
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 122..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..158
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 91
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
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:0007744|PubMed:21183079"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 198
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 213
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q53HL2"
FT VAR_SEQ 129..162
FT /note="EEEEGGGGGGRTKKSHKNLRSAKVKRCLPSKKRT -> QKRAIRIFDLQKSK
FT DAFHPRREPSPYKEEAEVKG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019922"
FT VAR_SEQ 163..289
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019923"
FT VAR_SEQ 276..289
FT /note="SRLAQICSSIRTGR -> GRVILQHLCASLPRLRNESPLRSRLGKLERQEHL
FT RLQRTQVWLSANMAVHL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019924"
FT CONFLICT 25
FT /note="L -> P (in Ref. 2; BAB27258)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="G -> E (in Ref. 1; AAT34966 and 2; BAC36334)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="K -> E (in Ref. 2; BAC37258)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 32214 MW; 3971F9666DA8EEF5 CRC64;
MAPKKRSSRG TRTNTLRSRK LASFLKDFDR EVQVRTKQIE SDRQTLLKEV ENLYNIEILR
LPKALQGMKW LDYFALGGNK QALEEAAKAD RDITEINNLT AEAIQTPLKS VKKRKVIEVE
ESIKEEEEEE EEGGGGGGRT KKSHKNLRSA KVKRCLPSKK RTQSIQGRGR SKRLSHDFVT
PAMSRLEPSL VKPTPGMTPR FDSRVFKTPG LRTPAAKEQV YNISINGSPL ADSKEISLSV
PIGGGASLRL LASDLQRIDI AQLNPEALGN IRKLSSRLAQ ICSSIRTGR
