KP58_DROME
ID KP58_DROME Reviewed; 952 AA.
AC Q9VPC0; Q5U100; Q8MQR7; Q94889; Q9TXB3;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Serine/threonine-protein kinase PITSLRE;
DE EC=2.7.11.22;
DE AltName: Full=Cell division cycle 2-like;
GN Name=Pitslre; ORFNames=CG4268;
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 [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8930898; DOI=10.1091/mbc.7.11.1759;
RA Sauer K., Weigmann K., Sigrist S., Lehner C.F.;
RT "Novel members of the cdc2-related kinase family in Drosophila: cdk4/6,
RT cdk5, PFTAIRE, and PITSLRE kinase.";
RL Mol. Biol. Cell 7:1759-1769(1996).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-952.
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 571-722.
RC TISSUE=Imaginal disk;
RX PubMed=1378625; DOI=10.1073/pnas.89.14.6295;
RA Biggs W.H. III, Zipursky S.L.;
RT "Primary structure, expression, and signal-dependent tyrosine
RT phosphorylation of a Drosophila homolog of extracellular signal-regulated
RT kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6295-6299(1992).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439; SER-442; TYR-447;
RP SER-449; SER-881 AND SER-886, AND IDENTIFICATION BY 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: Acts as a negative regulator of the normal cell cycle
CC progression. May function in regulating proliferation by the
CC phosphorylation and subsequent plasma membrane targeting of
CC galactosyltransferase (By similarity). {ECO:0000250}.
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=2.7.11.22;
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=2.7.11.22;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Present throughout the early embryo. In late
CC embryos levels are highest in the CNS. {ECO:0000269|PubMed:8930898}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Highest
CC levels in early embryogenesis (0-6 hours), low levels during later
CC embryogenesis, moderate levels in pupae and adults.
CC {ECO:0000269|PubMed:8930898}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM75018.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; X99513; CAA67863.1; -; mRNA.
DR EMBL; AE014296; AAF51635.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN12141.1; -; Genomic_DNA.
DR EMBL; BT016092; AAV36977.1; -; mRNA.
DR EMBL; AY128425; AAM75018.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001246851.1; NM_001259922.2.
DR RefSeq; NP_001246852.1; NM_001259923.2.
DR RefSeq; NP_001262122.1; NM_001275193.1.
DR RefSeq; NP_649251.2; NM_140994.4.
DR RefSeq; NP_730563.1; NM_168869.3.
DR AlphaFoldDB; Q9VPC0; -.
DR SMR; Q9VPC0; -.
DR BioGRID; 65549; 7.
DR IntAct; Q9VPC0; 9.
DR STRING; 7227.FBpp0077905; -.
DR iPTMnet; Q9VPC0; -.
DR PaxDb; Q9VPC0; -.
DR PRIDE; Q9VPC0; -.
DR DNASU; 40292; -.
DR EnsemblMetazoa; FBtr0078247; FBpp0077905; FBgn0016696.
DR EnsemblMetazoa; FBtr0078250; FBpp0077908; FBgn0016696.
DR GeneID; 40292; -.
DR KEGG; dme:Dmel_CG4268; -.
DR UCSC; CG4268-RC; d. melanogaster.
DR CTD; 40292; -.
DR FlyBase; FBgn0016696; Pitslre.
DR VEuPathDB; VectorBase:FBgn0016696; -.
DR eggNOG; KOG0663; Eukaryota.
DR GeneTree; ENSGT00940000158459; -.
DR InParanoid; Q9VPC0; -.
DR PhylomeDB; Q9VPC0; -.
DR BRENDA; 2.7.11.22; 1994.
DR BioGRID-ORCS; 40292; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 40292; -.
DR PRO; PR:Q9VPC0; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0016696; Expressed in egg cell and 62 other tissues.
DR ExpressionAtlas; Q9VPC0; baseline and differential.
DR Genevisible; Q9VPC0; DM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; ISS:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:FlyBase.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0002225; P:positive regulation of antimicrobial peptide production; IMP:FlyBase.
DR GO; GO:0045752; P:positive regulation of Toll signaling pathway; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:FlyBase.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR CDD; cd07843; STKc_CDC2L1; 1.
DR InterPro; IPR045267; CDK11/PITSLRE_STKc.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..952
FT /note="Serine/threonine-protein kinase PITSLRE"
FT /id="PRO_0000086160"
FT DOMAIN 558..851
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 51..56
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 14..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..400
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 685
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 564..572
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 587
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 447
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 69
FT /note="D -> E (in Ref. 1; CAA67863)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="V -> A (in Ref. 1; CAA67863)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="I -> S (in Ref. 1; CAA67863)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="V -> A (in Ref. 1; CAA67863)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="V -> E (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="L -> R (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="G -> GG (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="Missing (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="Missing (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="Missing (in Ref. 6)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 952 AA; 108838 MW; 9CBDE8D459D0713D CRC64;
MVNSSGSEDG QLRSPNDVHY HSRGEEDEHE GDADALYIQP PQASRESGSG PRREKKKHSR
ERRRHKERDD VGGAALALER DHRYDYRSRE EHYHHHQRER SSNAAAAYAK HHLGHAYHYP
QPPQQQQQPL PPAPSYAAHH YHHHQHLSGA RAAPREYHSY PSGYHSGSRH GDYPMEEPTR
RSSKYAESKD AESLEQDLRS RLLKKRHNYV KDYETEENYE HRVERSDRRE GGRKERERTV
RSTHKQNRHD RVIELLDSPE QEHHHQHQHK SHRSKWREEV EVIRRKVPED LELLARREKL
LAAERESRQR KQTAREELEA RRELLRERNE HSDALSPTTV AASVTAGLNI HVKRKSKPDN
YEKEIKLKKR REDDIEVIRD DDDEESEESD SNEEVPEQDS EGSATESGSE DSYASKKKSK
IKSKSQLEDD DEDLPLPDSP LSVGELYKSP KQRQRSRSVS SKSSSQSSRS SRSRSRSRSQ
SSLEDEVDRQ DVGADASPSS STRSEERGMT QEQPEEKPEE KLKEKQKSLE EQIPCDDKGI
PLPNYYPGVQ GCRSVEEFQC LNRIEEGTYG VVYRAKDKRT NEIVALKRLK MEKEKEGFPI
TSLREINTLL KGQHPNIVTV REIVVGSNMD KIFIVMDYVE HDLKSLMETM KNRKQSFFPG
EVKCLTQQLL RAVAHLHDNW ILHRDLKTSN LLLSHKGILK VGDFGLAREY GSPIKKYTSL
VVTLWYRAPE LLLCSPVYST PIDVWSVGCI FAEFLQMLPL FPGKSEIDEL NRIFKELGTP
NEKIWPGYTE LPAVKNMLSQ NSQFTEYPVS QLRKHFQEKT SEMGLSLLQG LLTYDPKQRL
SADAALKHGF FKELPLPIDP SMFPTWPAKS ELGARKAQAS SPKPPSGGSQ FKQLGRDEPI
IVGPGNKLSS GIITGNKKSH GAGGSSASTG FVLNAGITQR QLAMGPGFSL KF
