RPKL1_MOUSE
ID RPKL1_MOUSE Reviewed; 544 AA.
AC Q8R2S1; Q8R1D4;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ribosomal protein S6 kinase-like 1;
DE EC=2.7.11.1;
GN Name=Rps6kl1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
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 [3]
RP PROTEIN SEQUENCE OF 361-374, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
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 -!- 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;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R2S1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R2S1-2; Sequence=VSP_017935, VSP_017936, VSP_017937,
CC VSP_017938;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. S6 kinase subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AK044050; BAC31753.1; -; mRNA.
DR EMBL; BC024798; AAH24798.1; -; mRNA.
DR EMBL; BC027298; AAH27298.1; -; mRNA.
DR CCDS; CCDS36496.1; -. [Q8R2S1-1]
DR RefSeq; NP_666356.2; NM_146244.4. [Q8R2S1-1]
DR AlphaFoldDB; Q8R2S1; -.
DR SMR; Q8R2S1; -.
DR STRING; 10090.ENSMUSP00000019379; -.
DR iPTMnet; Q8R2S1; -.
DR PhosphoSitePlus; Q8R2S1; -.
DR EPD; Q8R2S1; -.
DR PaxDb; Q8R2S1; -.
DR PRIDE; Q8R2S1; -.
DR ProteomicsDB; 300482; -. [Q8R2S1-1]
DR ProteomicsDB; 300483; -. [Q8R2S1-2]
DR Antibodypedia; 25730; 192 antibodies from 29 providers.
DR DNASU; 238323; -.
DR Ensembl; ENSMUST00000221972; ENSMUSP00000152336; ENSMUSG00000019235. [Q8R2S1-1]
DR GeneID; 238323; -.
DR KEGG; mmu:238323; -.
DR UCSC; uc007ogm.2; mouse. [Q8R2S1-1]
DR UCSC; uc007ogp.2; mouse. [Q8R2S1-2]
DR CTD; 83694; -.
DR MGI; MGI:2443413; Rps6kl1.
DR VEuPathDB; HostDB:ENSMUSG00000019235; -.
DR eggNOG; KOG0603; Eukaryota.
DR GeneTree; ENSGT00940000159815; -.
DR HOGENOM; CLU_014272_2_0_1; -.
DR InParanoid; Q8R2S1; -.
DR OMA; SLPRCHV; -.
DR OrthoDB; 255297at2759; -.
DR PhylomeDB; Q8R2S1; -.
DR TreeFam; TF323964; -.
DR BioGRID-ORCS; 238323; 1 hit in 75 CRISPR screens.
DR PRO; PR:Q8R2S1; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8R2S1; protein.
DR Bgee; ENSMUSG00000019235; Expressed in neural tube mantle layer and 83 other tissues.
DR ExpressionAtlas; Q8R2S1; baseline and differential.
DR Genevisible; Q8R2S1; MM.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd05576; STKc_RPK118_like; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR035050; RPS6KL1.
DR InterPro; IPR035053; STK_RPK118-like.
DR PANTHER; PTHR15508:SF4; PTHR15508:SF4; 1.
DR Pfam; PF04212; MIT; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00745; MIT; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF116846; SSF116846; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..544
FT /note="Ribosomal protein S6 kinase-like 1"
FT /id="PRO_0000232642"
FT DOMAIN 87..115
FT /note="MIT"
FT DOMAIN 145..534
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 262..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 407
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 151..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 79..88
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017935"
FT VAR_SEQ 162..177
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017936"
FT VAR_SEQ 449..467
FT /note="EVGGISELTEACDWWSYGS -> GTVPEPPFRIPGPHPTPAA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017937"
FT VAR_SEQ 468..544
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017938"
FT CONFLICT 418
FT /note="A -> AE (in Ref. 2; AAH24798)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 60193 MW; 05E16F8B4C33799B CRC64;
MSLVACECPP GPGLEPEPCS RARSQACMYL EQIRNRVATG TADVTKRDYL VDAATQIHLA
LERDVSEDYE AAFNHYQNGV DVLLRGVHVD PNKERREAVK LKITKYLRRA EEIFNCHLQR
TLGSGASPNT GFSSLRLRPI RTLSSALEQL KGCRVVGIIK KVQVVQDPAT GGTFIVKSLP
RCHMVSRERL TIIPHGVPYM TKLLRYFVSE DSIFLHLEHV QGGTLWSHLL SQDHFQYSGL
NSGSVQEKSQ AQLSTRLSLM TPAELTPGHT LRQNRIPMEP PRTSQSLPPA LQLQKEADAE
PSSRPSAVFS SDPTEAPCGH SHSQVRRAGQ SSNPAPTQRL HWVREGADRV LGAYGRGRGR
NPPSANRASL GSGRAAWSLR EGQVKQWAAE MLLALEALHQ QGVLCRDLNP QNLLLDQAGH
IQLTYFGQWS EVEPRCSQEA VDCLYSAPEV GGISELTEAC DWWSYGSLLY ELLTGMALSQ
SHPSGFQAHT QLQLPEWLSH PAASLLTELL QFEPQRRLGA GGGGTSRLKS HPFFSTIQWS
RLMG
