BORA_HUMAN
ID BORA_HUMAN Reviewed; 559 AA.
AC Q6PGQ7; B4DQ30; Q5W0P3; Q5W0P4; Q86YC6; Q96IW9; Q9H640;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein aurora borealis;
DE Short=HsBora;
GN Name=BORA; Synonyms=C13orf34;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 135-559 (ISOFORM 1).
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow, Leiomyosarcoma, Rhabdomyosarcoma, and Testis carcinoma;
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 FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH AURKA.
RX PubMed=16890155; DOI=10.1016/j.devcel.2006.06.002;
RA Hutterer A., Berdnik D., Wirtz-Peitz F., Zigman M., Schleiffer A.,
RA Knoblich J.A.;
RT "Mitotic activation of the kinase Aurora-A requires its binding partner
RT Bora.";
RL Dev. Cell 11:147-157(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Required for the activation of AURKA at the onset of mitosis.
CC {ECO:0000269|PubMed:16890155}.
CC -!- SUBUNIT: Interacts with AURKA. {ECO:0000269|PubMed:16890155}.
CC -!- INTERACTION:
CC Q6PGQ7; P53350: PLK1; NbExp=5; IntAct=EBI-719836, EBI-476768;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PGQ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PGQ7-2; Sequence=VSP_055543;
CC -!- PTM: Phosphorylated by AURKA. {ECO:0000269|PubMed:16890155}.
CC -!- SIMILARITY: Belongs to the BORA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15426.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK026277; BAB15426.1; ALT_INIT; mRNA.
DR EMBL; AK298608; BAG60792.1; -; mRNA.
DR EMBL; AL138695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471093; EAW80515.1; -; Genomic_DNA.
DR EMBL; BC007119; AAH07119.1; -; mRNA.
DR EMBL; BC025367; AAH25367.2; -; mRNA.
DR EMBL; BC044213; AAH44213.1; -; mRNA.
DR EMBL; BC056876; AAH56876.2; -; mRNA.
DR CCDS; CCDS66560.1; -. [Q6PGQ7-2]
DR CCDS; CCDS73583.1; -. [Q6PGQ7-1]
DR CCDS; CCDS9446.2; -. [Q6PGQ7-1]
DR RefSeq; NP_001273675.1; NM_001286746.1. [Q6PGQ7-1]
DR RefSeq; NP_001273676.1; NM_001286747.1. [Q6PGQ7-2]
DR RefSeq; NP_079084.3; NM_024808.3. [Q6PGQ7-1]
DR AlphaFoldDB; Q6PGQ7; -.
DR BioGRID; 122954; 47.
DR DIP; DIP-53424N; -.
DR ELM; Q6PGQ7; -.
DR IntAct; Q6PGQ7; 23.
DR STRING; 9606.ENSP00000479266; -.
DR iPTMnet; Q6PGQ7; -.
DR PhosphoSitePlus; Q6PGQ7; -.
DR BioMuta; BORA; -.
DR DMDM; 74737659; -.
DR EPD; Q6PGQ7; -.
DR jPOST; Q6PGQ7; -.
DR MassIVE; Q6PGQ7; -.
DR MaxQB; Q6PGQ7; -.
DR PaxDb; Q6PGQ7; -.
DR PeptideAtlas; Q6PGQ7; -.
DR PRIDE; Q6PGQ7; -.
DR ProteomicsDB; 67120; -. [Q6PGQ7-1]
DR Antibodypedia; 24385; 186 antibodies from 33 providers.
DR DNASU; 79866; -.
DR Ensembl; ENST00000390667.11; ENSP00000375082.6; ENSG00000136122.18. [Q6PGQ7-1]
DR Ensembl; ENST00000651477.1; ENSP00000498664.1; ENSG00000136122.18. [Q6PGQ7-1]
DR Ensembl; ENST00000652266.1; ENSP00000498882.1; ENSG00000136122.18. [Q6PGQ7-2]
DR GeneID; 79866; -.
DR KEGG; hsa:79866; -.
DR MANE-Select; ENST00000390667.11; ENSP00000375082.6; NM_024808.5; NP_079084.4.
DR UCSC; uc010thr.3; human. [Q6PGQ7-1]
DR CTD; 79866; -.
DR DisGeNET; 79866; -.
DR GeneCards; BORA; -.
DR HGNC; HGNC:24724; BORA.
DR HPA; ENSG00000136122; Low tissue specificity.
DR MIM; 610510; gene.
DR neXtProt; NX_Q6PGQ7; -.
DR OpenTargets; ENSG00000136122; -.
DR PharmGKB; PA162378045; -.
DR VEuPathDB; HostDB:ENSG00000136122; -.
DR eggNOG; ENOG502S85H; Eukaryota.
DR GeneTree; ENSGT00390000013790; -.
DR InParanoid; Q6PGQ7; -.
DR OMA; STWIKEP; -.
DR OrthoDB; 539473at2759; -.
DR PhylomeDB; Q6PGQ7; -.
DR TreeFam; TF329674; -.
DR PathwayCommons; Q6PGQ7; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR SignaLink; Q6PGQ7; -.
DR SIGNOR; Q6PGQ7; -.
DR BioGRID-ORCS; 79866; 564 hits in 1087 CRISPR screens.
DR ChiTaRS; BORA; human.
DR GenomeRNAi; 79866; -.
DR Pharos; Q6PGQ7; Tbio.
DR PRO; PR:Q6PGQ7; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q6PGQ7; protein.
DR Bgee; ENSG00000136122; Expressed in secondary oocyte and 130 other tissues.
DR ExpressionAtlas; Q6PGQ7; baseline and differential.
DR Genevisible; Q6PGQ7; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0072687; C:meiotic spindle; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
DR InterPro; IPR023252; Aurora_borealis_protein.
DR PANTHER; PTHR14728; PTHR14728; 1.
DR Pfam; PF15280; BORA_N; 1.
DR PRINTS; PR02038; AURORABORA.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Mitosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..559
FT /note="Protein aurora borealis"
FT /id="PRO_0000273205"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BS90"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BS90"
FT MOD_RES 354
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BS90"
FT VAR_SEQ 1..87
FT /note="MGDVKESKMQITPETPGRIPVLNPFESPSDYSNLHEQTLASPSVFKSTKLPT
FT PGKFRWSIDQLAVINPVEIDPEDIHRQALYLSHSR -> MNKLSPVLLFLNQQNYQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055543"
FT VARIANT 210
FT /note="S -> L (in dbSNP:rs9543107)"
FT /id="VAR_030110"
FT VARIANT 308
FT /note="S -> F (in dbSNP:rs1146858)"
FT /id="VAR_030111"
FT CONFLICT 545
FT /note="R -> K (in Ref. 4; AAH07119)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 61203 MW; F817E6DC2C7600DB CRC64;
MGDVKESKMQ ITPETPGRIP VLNPFESPSD YSNLHEQTLA SPSVFKSTKL PTPGKFRWSI
DQLAVINPVE IDPEDIHRQA LYLSHSRIDK DVEDKRQKAI EEFFTKDVIV PSPWTDHEGK
QLSQCHSSKC TNINSDSPVG KKLTIHSEKS DAACQTLLSL PVDFNLENIL GDYFRADEFA
DQSPGNLSSS SLRRKLFLDG NGSISDSLPS ASPGSPHSGV QTSLEMFYSI DLSPVKCRSP
LQTPSSGQFS SSPIQASAKK YSLGSITSPS PISSPTFSPI EFQIGETPLS EQRKFTVHSP
DASSGTNSNG ITNPCIRSPY IDGCSPIKNW SPMRLQMYSG GTQYRTSVIQ IPFTLETQGE
DEEDKENIPS TDVSSPAMDA AGIHLRQFSN EASTHGTHLV VTAMSVTQNQ SSASEKELAL
LQDVEREKDN NTVDMVDPIE IADETTWIKE PVDNGSLPMT DFVSGIAFSI ENSHMCMSPL
AESSVIPCES SNIQMDSGYN TQNCGSNIMD TVGAESYCKE SDAQTCEVES KSQAFNMKQD
HTTQRCWMKT ASPFQCSSP
