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BORA_DROME
ID   BORA_DROME              Reviewed;         539 AA.
AC   Q9VVR2;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Protein aurora borealis;
GN   Name=bora; ORFNames=CG6897;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH AUR.
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Required for the activation of Aurora-A (aur) at the onset of
CC       mitosis. {ECO:0000269|PubMed:16890155}.
CC   -!- SUBUNIT: Interacts with aur. {ECO:0000269|PubMed:16890155}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16890155}. Nucleus
CC       {ECO:0000269|PubMed:16890155}. Note=Shuttles between the cytoplasm and
CC       the nucleus. In interphase cells, it is nuclear. Upon entry into
CC       mitosis, it is excluded from the nucleus and translocates into the
CC       cytoplasm in a Cdk1-dependent manner.
CC   -!- PTM: Phosphorylated by aur. {ECO:0000269|PubMed:16890155,
CC       ECO:0000269|PubMed:18327897}.
CC   -!- SIMILARITY: Belongs to the BORA family. {ECO:0000305}.
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DR   EMBL; AE014296; AAF49248.1; -; Genomic_DNA.
DR   EMBL; AY070548; AAL48019.1; -; mRNA.
DR   RefSeq; NP_649048.1; NM_140791.3.
DR   AlphaFoldDB; Q9VVR2; -.
DR   BioGRID; 65312; 5.
DR   IntAct; Q9VVR2; 3.
DR   STRING; 7227.FBpp0074874; -.
DR   iPTMnet; Q9VVR2; -.
DR   PaxDb; Q9VVR2; -.
DR   DNASU; 40031; -.
DR   EnsemblMetazoa; FBtr0075108; FBpp0074874; FBgn0259791.
DR   GeneID; 40031; -.
DR   KEGG; dme:Dmel_CG6897; -.
DR   CTD; 79866; -.
DR   FlyBase; FBgn0259791; bora.
DR   VEuPathDB; VectorBase:FBgn0259791; -.
DR   eggNOG; ENOG502S85H; Eukaryota.
DR   GeneTree; ENSGT00390000013790; -.
DR   HOGENOM; CLU_464825_0_0_1; -.
DR   InParanoid; Q9VVR2; -.
DR   OMA; TQFEWNI; -.
DR   OrthoDB; 1273292at2759; -.
DR   PhylomeDB; Q9VVR2; -.
DR   Reactome; R-DME-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   BioGRID-ORCS; 40031; 1 hit in 1 CRISPR screen.
DR   GenomeRNAi; 40031; -.
DR   PRO; PR:Q9VVR2; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0259791; Expressed in head epidermis primordium (Drosophila) and 39 other tissues.
DR   Genevisible; Q9VVR2; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0032147; P:activation of protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:FlyBase.
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; IBA:GO_Central.
DR   GO; GO:0060236; P:regulation of mitotic spindle organization; IBA:GO_Central.
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   Cell cycle; Cell division; Cytoplasm; Mitosis; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..539
FT                   /note="Protein aurora borealis"
FT                   /id="PRO_0000273210"
FT   REGION          23..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..429
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         383
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
SQ   SEQUENCE   539 AA;  59142 MW;  B5503F51B225CA02 CRC64;
     MYNDEVRTPQ ALKNRYITNV NGLKCRARRN SHSNSSNSSA ASATPTNGGK ENGKYSPQMS
     GNVCTPPPKR LHKVRNPFEG AMADRLHLPL IASPSLFRSR TPQLSSTQFE WNIDEVSQLK
     PADVEPHETQ FHDSPDPEQE SKAQLAISAF FKESLIVPSP VDCPLRKQRI ILNCSEDNTP
     ISNKSRRMRD CEVQTELTLP PILPKALEDA LRPYFQPHLA GRLSGRSKSS GGPDIFNSSM
     RRKLFDLHNV IVLGEQDTAE PSRSMVGSSP QGKQTMFAGR LSDSASGESS FGCLSPIRNL
     CGLPPGTPDN GTCSGKRKLL MHELELPSPI APSEHLSRRL VHSKVEISVT EQHDTLSERT
     ALKFTPDRSS SPMGGGLEHS DCSINQRVRR LRVNSTRQVV IETGDQPLFE ETEGEEEEAE
     SEDDEEADAM QLSTVSFNCS SSNSDTPRGH KRHRSAQRKN LSQSFSANLE EEADQTQGGA
     GSIQPAEPPS VAMPQQGARI PLYRADSGFN ETSSTTFAFS QDLPLDVSMA CCSTPSTRS
 
 
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