ASATR_DROME
ID ASATR_DROME Reviewed; 1262 AA.
AC Q8IMC6; Q8IMC5;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Tau-tubulin kinase homolog Asator {ECO:0000303|PubMed:19890914};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q5TCY1};
GN Name=Asator {ECO:0000303|PubMed:19890914};
GN ORFNames=CG11533 {ECO:0000312|FlyBase:FBgn0039908};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AFA28428.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH MTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=19890914; DOI=10.1002/dvdy.22150;
RA Qi H., Yao C., Cai W., Girton J., Johansen K.M., Johansen J.;
RT "Asator, a tau-tubulin kinase homolog in Drosophila localizes to the
RT mitotic spindle.";
RL Dev. Dyn. 238:3248-3256(2009).
CC -!- FUNCTION: Probable serine/threonine protein kinase. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q5TCY1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q5TCY1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with Mtor. {ECO:0000269|PubMed:19890914}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:19890914}. Cytoplasm {ECO:0000269|PubMed:19890914}.
CC Note=Found in the cytoplasm during interphase. Localizes to the mitotic
CC spindle in dividing cells. {ECO:0000269|PubMed:19890914}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=E {ECO:0000312|FlyBase:FBgn0039908};
CC IsoId=Q8IMC6-1; Sequence=Displayed;
CC Name=F {ECO:0000312|FlyBase:FBgn0039908};
CC IsoId=Q8IMC6-2; Sequence=VSP_058795, VSP_058796, VSP_058797;
CC -!- TISSUE SPECIFICITY: Detected in larval brain.
CC {ECO:0000269|PubMed:19890914}.
CC -!- DEVELOPMENTAL STAGE: Detected at low levels throughout development.
CC Highest expression levels are seen in embryos.
CC {ECO:0000269|PubMed:19890914}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. {ECO:0000269|PubMed:19890914}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AE014135; AAN06495.2; -; Genomic_DNA.
DR EMBL; AE014135; AAN06496.2; -; Genomic_DNA.
DR EMBL; BT133187; AFA28428.1; -; mRNA.
DR RefSeq; NP_726576.2; NM_166765.3. [Q8IMC6-1]
DR RefSeq; NP_726577.2; NM_166766.3. [Q8IMC6-2]
DR AlphaFoldDB; Q8IMC6; -.
DR SMR; Q8IMC6; -.
DR STRING; 7227.FBpp0289571; -.
DR EnsemblMetazoa; FBtr0300343; FBpp0289572; FBgn0039908. [Q8IMC6-1]
DR EnsemblMetazoa; FBtr0300344; FBpp0289573; FBgn0039908. [Q8IMC6-2]
DR GeneID; 43794; -.
DR KEGG; dme:Dmel_CG11533; -.
DR CTD; 43794; -.
DR FlyBase; FBgn0039908; Asator.
DR VEuPathDB; VectorBase:FBgn0039908; -.
DR eggNOG; KOG1164; Eukaryota.
DR GeneTree; ENSGT00940000160367; -.
DR BioGRID-ORCS; 43794; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43794; -.
DR PRO; PR:Q8IMC6; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0039908; Expressed in brain and 18 other tissues.
DR ExpressionAtlas; Q8IMC6; baseline and differential.
DR Genevisible; Q8IMC5; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1262
FT /note="Tau-tubulin kinase homolog Asator"
FT /id="PRO_0000439147"
FT DOMAIN 173..436
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 13..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 293
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 179..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..156
FT /note="Missing (in isoform F)"
FT /id="VSP_058795"
FT VAR_SEQ 945..967
FT /note="YRMDIARNVCVRETYSEITHLAR -> SILNKSLPVIIYIYMHAVTFFCF
FT (in isoform F)"
FT /id="VSP_058796"
FT VAR_SEQ 968..1262
FT /note="Missing (in isoform F)"
FT /id="VSP_058797"
SQ SEQUENCE 1262 AA; 138828 MW; 48E1EEBAD9D51DE6 CRC64;
MFWHLLCVPN DENASAPDDG NQSCQPSSKQ DQYLSPNRNC QKNLLRLYPP PPSKPPPLVG
AILQTRLLHQ ISPSAIADAD ADLNAVGELL YPNVLQRSAT LPAKHNRLGV RSRVTFKVPS
SNLPAQDSYS HQPRNQVAVA AKDGILVDVK AKESVKMTSE DLLQPGHVVK ERWKVVRKIG
GGGFGEIYEG QDLITREQVA LKVESARQPK QVLKMEVAVL KKLQGKEHVC RFIGCGRNDR
FNYVVMQLQG KNLAELRRAQ PRGAFSLSTT LRLGLQILKA IESIHSVGFL HRDIKPSNFS
VGRLPYNCRR VYMLDFGLAR QYTTGTGEVR CPRAAAGFRG TVRYASINAH RNREMGRHDD
LWSLFYMLVE FVNGQLPWRK IKDKEQVGLT KEKYDHRILL KHLPSDLKQF LEHIQSLTYG
DRPDYAMLIG LFERCMKRRG VKESDPYDWE KVDSTAIGNI SATGNPSIPI KSDYMHGNIT
QMTVAASNAS GTEYIRKRAE IETAHITATD PLNIKEKVDK NCNATSLAQP AKGSGEPMVQ
HGNAANNQNI TSKGLQQQST LTNSQVAIAN IQSAPSMIER EDVQYTKLEE GAPTKFITMK
PNGECDNVDI AAKCIFEQKH VEANDDIVGR ASLSGVEQHY KSQIKKHNSP EIANKQIQRT
GTVTNDKTSE VNRSTEEQKS TFGRLRVLTA PPMSVHDLPS GGGHSHQVSD LSGKQDPYAA
TSNAAPIGIN SSSTKFGSQH GQIFGLAAMP PINRRSATST NLRPSSSASQ RINSGSTIGG
AVGNGSNTAR SSVAGDHSVT QFALIDDENV SALQQVTKGG ALTLASQWKS QFDDSEDTTD
NEWNREHQLQ PNLEQLIKLD ISLPLNEAKP FPQHGVAGTG KLINPPGEAK GRPKRYTLNI
TGIENYEALR ISIPNCWSEP AMGNVLRKGL EPPAVQQAAF DDTVYRMDIA RNVCVRETYS
EITHLARPST SSVLRNRLPS PFKKDSALQL NSTNDSLDKS RHRNSLPNVS VNDIFDDLQM
KLNLDLGSAI QENNCCISGR LEIRVIPKDT SHPDDSVYYD AMGAVKNTPT ANEGHDHSDQ
AVNNCDEMEA TSAVIAFPNK SISKIMSPPG RDATEERTGA SLCSLYSAGV NKLKLNGNTA
PRTQFKKGST DGFGENESEF DFPLLNPSKI PVRQSKCASW AGADFISASK PLESAEVPQE
IPYHPQSDTT YSVIDSIPVR KTTYSIALEC PPNISDLTPG LSYFYCNIVV PLRLFSILLT
ES
