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Serine/threonine-protein kinase S6KL (EC 2.7.11.-) (Protein kinase-like 17E) (S6 kinase-like protein)

 S6KL_DROME              Reviewed;         483 AA.
Q9VWQ2; B9EQU9; M9NEP2; M9NFD4; O96630;
14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
27-SEP-2017, entry version 153.
RecName: Full=Serine/threonine-protein kinase S6KL {ECO:0000305};
EC=2.7.11.- {ECO:0000305};
AltName: Full=Protein kinase-like 17E {ECO:0000312|EMBL:AAF48886.1};
AltName: Full=S6 kinase-like protein {ECO:0000303|PubMed:25748449};
Name=S6KL {ECO:0000312|FlyBase:FBgn0283473};
Synonyms=Bin4 {ECO:0000303|PubMed:10717484},
Pk17E {ECO:0000312|FlyBase:FBgn0283473};
ORFNames=CG7001 {ECO:0000312|FlyBase:FBgn0283473};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
[1] {ECO:0000312|EMBL:AAC72971.1}
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10717484; DOI=10.1016/S0378-1119(00)00048-2;
Zhu W., Hanes S.D.;
"Identification of Drosophila bicoid-interacting proteins using a
custom two-hybrid selection.";
Gene 245:329-339(2000).
[2] {ECO:0000312|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3] {ECO:0000312|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4] {ECO:0000312|EMBL:AAL39636.1, ECO:0000312|EMBL:ACM16741.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
STRAIN=Berkeley {ECO:0000312|EMBL:AAL39636.1};
TISSUE=Embryo {ECO:0000312|EMBL:AAL39636.1};
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G.,
Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S.,
Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M.,
Celniker S.;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000305}
FUNCTION, COFACTOR, INTERACTION WITH TKV, SUBCELLULAR LOCATION,
DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-193.
PubMed=25748449; DOI=10.1371/journal.pgen.1004984;
Zhao G., Wu Y., Du L., Li W., Xiong Y., Yao A., Wang Q., Zhang Y.Q.;
"Drosophila S6 Kinase like inhibits neuromuscular junction growth by
downregulating the BMP receptor thickveins.";
PLoS Genet. 11:E1004984-E1004984(2015).
-!- FUNCTION: Displays kinase activity. Inhibits neuromuscular
junction (NMJ) growth by interacting with and promoting the
proteasome-mediated degradation of the receptor tkv which inhibits
bone morphogenetic protein (BMP) signaling.
{ECO:0000269|PubMed:25748449}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:25748449};
-!- SUBUNIT: Interacts with tkv. {ECO:0000269|PubMed:25748449}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25748449}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=A {ECO:0000312|FlyBase:FBgn0283473};
IsoId=Q9VWQ2-1; Sequence=Displayed;
Name=B {ECO:0000312|FlyBase:FBgn0283473};
IsoId=Q9VWQ2-3; Sequence=VSP_057952;
Name=C {ECO:0000312|FlyBase:FBgn0283473};
IsoId=Q9VWQ2-2; Sequence=VSP_057953;
Note=Gene prediction based on EST data. {ECO:0000305};
-!- DISRUPTION PHENOTYPE: Mutants are viable and fertile but display
NMJ overgrowth with excess satellite boutons, fewer and larger
synaptic vesicles, defective synaptic endocytosis and increased
levels of tkv. {ECO:0000269|PubMed:25748449}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF096866; AAC72971.1; -; mRNA.
EMBL; AE014298; AAF48886.1; -; Genomic_DNA.
EMBL; AE014298; AFH07455.1; -; Genomic_DNA.
EMBL; AE014298; AFH07456.1; -; Genomic_DNA.
EMBL; AY069491; AAL39636.1; -; mRNA.
EMBL; BT058024; ACM16741.1; -; mRNA.
RefSeq; NP_001245742.1; NM_001258813.1. [Q9VWQ2-3]
RefSeq; NP_001245743.1; NM_001258814.2. [Q9VWQ2-2]
RefSeq; NP_524861.2; NM_080122.4. [Q9VWQ2-1]
UniGene; Dm.211; -.
ProteinModelPortal; Q9VWQ2; -.
SMR; Q9VWQ2; -.
IntAct; Q9VWQ2; 58.
MINT; MINT-1025885; -.
STRING; 7227.FBpp0074405; -.
PaxDb; Q9VWQ2; -.
PRIDE; Q9VWQ2; -.
EnsemblMetazoa; FBtr0074634; FBpp0074405; FBgn0004462. [Q9VWQ2-1]
EnsemblMetazoa; FBtr0307198; FBpp0298027; FBgn0004462. [Q9VWQ2-3]
EnsemblMetazoa; FBtr0307199; FBpp0298028; FBgn0004462. [Q9VWQ2-2]
GeneID; 45970; -.
KEGG; dme:Dmel_CG7001; -.
UCSC; CG7001-RA; d. melanogaster. [Q9VWQ2-1]
CTD; 45970; -.
FlyBase; FBgn0283473; S6KL.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00890000139524; -.
KO; K17529; -.
OMA; HYHQEEL; -.
OrthoDB; EOG091G076X; -.
PhylomeDB; Q9VWQ2; -.
ChiTaRS; Pk17E; fly.
GenomeRNAi; 45970; -.
PRO; PR:Q9VWQ2; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0004462; -.
Genevisible; Q9VWQ2; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
Pfam; PF00069; Pkinase; 1.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
Kinase; Nucleotide-binding; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 483 Serine/threonine-protein kinase S6KL.
{ECO:0000305}.
/FTId=PRO_0000434556.
DOMAIN 159 435 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 165 173 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 36 88 Gln-rich. {ECO:0000255|PROSITE-
ProRule:PRU00006}.
ACT_SITE 281 281 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 189 189 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
VAR_SEQ 1 314 Missing (in isoform B). {ECO:0000305}.
/FTId=VSP_057952.
VAR_SEQ 85 86 Missing (in isoform C). {ECO:0000305}.
/FTId=VSP_057953.
MUTAGEN 193 193 K->A: Abolishes kinase activity.
{ECO:0000269|PubMed:25748449}.
CONFLICT 42 42 E -> EQQQQ (in Ref. 1; AAC72971).
{ECO:0000305}.
CONFLICT 182 182 I -> N (in Ref. 1; AAC72971).
{ECO:0000305}.
CONFLICT 362 362 R -> G (in Ref. 4; ACM16741).
{ECO:0000305}.
CONFLICT 467 467 H -> Q (in Ref. 1; AAC72971).
{ECO:0000305}.
SEQUENCE 483 AA; 55372 MW; 24629C417D601F0F CRC64;
MGNSQPRNAS RSRRTSQWPQ GAAELGASAS DHHYHQEELY QEQQQQQQQP QQEQPSSRRI
QFQAHTNQPT QSHPPGDEEQ PVQSQQQQLS TWSLGSLSGG RLNWSFSGAR NSFRHRNKAT
RKSLTSLHGS RRGKTQWHRP LTNSIFNSHF KETSKNDLYR IDHLVAKGAF GVVFKVSSKS
DISQCYALKV LKKSKLIEDN SVRQIKDEAD IQKVCGHHPF IVKQIDLWQN RHNLHILSEY
VPNGELFSKI THFSIDLVRL YIGEIALALD FLHNAGIIYR DAKPENILLT EQFHIKLTDF
GLSKWLKLGA NTRTMCGTFK YMAPEILCGE PYGHAVDWWA LGVIACQMLT QKSPNIKRHL
LRRRESVEPE DGLSNAPSIA QINGCLQDSD GDSEDFLPEE VQHLTHEGRD VLRKLLTIEP
RQRIRSVMAL QRIAIYKDYN LSSKQLLSLS PREIIARDGI RIYEDRHFDQ LTNQCAIDAF
LDF


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