CDKL2_MOUSE
ID CDKL2_MOUSE Reviewed; 568 AA.
AC Q9QUK0; Q3UL60; Q3V3X7; Q9QYI1; Q9QYI2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Cyclin-dependent kinase-like 2 {ECO:0000305};
DE EC=2.7.11.22;
DE AltName: Full=Serine/threonine-protein kinase KKIAMRE;
GN Name=Cdkl2 {ECO:0000312|MGI:MGI:1858227}; Synonyms=Kkiamre, Kkm;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/SvJ, and C57BL/6J; TISSUE=Brain;
RX PubMed=14605869; DOI=10.1007/s00441-003-0828-8;
RA Sassa T., Gomi H., Itohara S.;
RT "Postnatal expression of Cdkl2 in mouse brain revealed by LacZ inserted
RT into the Cdkl2 locus.";
RL Cell Tissue Res. 315:147-156(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Lung, and Pituitary;
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).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=KKIAMRE-beta;
CC IsoId=Q9QUK0-1; Sequence=Displayed;
CC Name=2; Synonyms=KKIAMRE-gamma;
CC IsoId=Q9QUK0-2; Sequence=VSP_016146, VSP_016147;
CC -!- TISSUE SPECIFICITY: Expressed in testis, kidney, lung and brain.
CC {ECO:0000269|PubMed:14605869}.
CC -!- DOMAIN: The [NKR]KIAxRE motif seems to be a cyclin-binding region.
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=BAE43274.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB029066; BAA88428.1; -; mRNA.
DR EMBL; AB029067; BAA88429.1; -; mRNA.
DR EMBL; AB029073; BAA88439.1; -; Genomic_DNA.
DR EMBL; AB029065; BAA88427.1; -; mRNA.
DR EMBL; AK030598; BAE43274.1; ALT_INIT; mRNA.
DR EMBL; AK144574; BAE25943.1; -; mRNA.
DR EMBL; AK145688; BAE26590.1; -; mRNA.
DR CCDS; CCDS19425.1; -. [Q9QUK0-2]
DR CCDS; CCDS19426.1; -. [Q9QUK0-1]
DR RefSeq; NP_001263244.1; NM_001276315.1. [Q9QUK0-2]
DR RefSeq; NP_058608.1; NM_016912.2. [Q9QUK0-1]
DR RefSeq; NP_796244.2; NM_177270.4. [Q9QUK0-2]
DR RefSeq; XP_011247839.1; XM_011249537.2. [Q9QUK0-1]
DR RefSeq; XP_017176476.1; XM_017320987.1. [Q9QUK0-1]
DR RefSeq; XP_017176477.1; XM_017320988.1. [Q9QUK0-1]
DR AlphaFoldDB; Q9QUK0; -.
DR SMR; Q9QUK0; -.
DR STRING; 10090.ENSMUSP00000084199; -.
DR iPTMnet; Q9QUK0; -.
DR PhosphoSitePlus; Q9QUK0; -.
DR MaxQB; Q9QUK0; -.
DR PaxDb; Q9QUK0; -.
DR PRIDE; Q9QUK0; -.
DR ProteomicsDB; 281560; -. [Q9QUK0-1]
DR ProteomicsDB; 281561; -. [Q9QUK0-2]
DR Antibodypedia; 24675; 250 antibodies from 28 providers.
DR DNASU; 53886; -.
DR Ensembl; ENSMUST00000069937; ENSMUSP00000063617; ENSMUSG00000029403. [Q9QUK0-2]
DR Ensembl; ENSMUST00000086978; ENSMUSP00000084199; ENSMUSG00000029403. [Q9QUK0-1]
DR Ensembl; ENSMUST00000113140; ENSMUSP00000108765; ENSMUSG00000029403. [Q9QUK0-1]
DR Ensembl; ENSMUST00000113143; ENSMUSP00000108768; ENSMUSG00000029403. [Q9QUK0-2]
DR GeneID; 53886; -.
DR KEGG; mmu:53886; -.
DR UCSC; uc008ycc.2; mouse. [Q9QUK0-1]
DR UCSC; uc008ycd.2; mouse. [Q9QUK0-2]
DR CTD; 8999; -.
DR MGI; MGI:1858227; Cdkl2.
DR VEuPathDB; HostDB:ENSMUSG00000029403; -.
DR eggNOG; KOG0593; Eukaryota.
DR GeneTree; ENSGT00940000160368; -.
DR HOGENOM; CLU_000288_136_0_1; -.
DR InParanoid; Q9QUK0; -.
DR OMA; KHSPAGH; -.
DR PhylomeDB; Q9QUK0; -.
DR TreeFam; TF101031; -.
DR BioGRID-ORCS; 53886; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q9QUK0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9QUK0; protein.
DR Bgee; ENSMUSG00000029403; Expressed in barrel cortex and 202 other tissues.
DR ExpressionAtlas; Q9QUK0; baseline and differential.
DR Genevisible; Q9QUK0; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Nucleus; Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..568
FT /note="Cyclin-dependent kinase-like 2"
FT /id="PRO_0000085816"
FT DOMAIN 4..289
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 309..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 45..51
FT /note="[NKR]KIAxRE"
FT ACT_SITE 126
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 548..564
FT /note="GAGSPLSDDSEADLPRM -> MLPALEMTSSCTRALIP (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14605869"
FT /id="VSP_016146"
FT VAR_SEQ 565..568
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14605869"
FT /id="VSP_016147"
FT CONFLICT 56
FT /note="K -> Q (in Ref. 2; BAE43274)"
FT /evidence="ECO:0000305"
FT CONFLICT 321..322
FT /note="NR -> KK (in Ref. 1; BAA88428)"
FT /evidence="ECO:0000305"
FT CONFLICT 325..329
FT /note="EKDDA -> KKKKK (in Ref. 1; BAA88428)"
FT /evidence="ECO:0000305"
FT CONFLICT 330..568
FT /note="Missing (in Ref. 1; BAA88428)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 568 AA; 64056 MW; A43B75E2E9EB86C4 CRC64;
MEKYENLGLV GEGSYGMVMK CRNKDSGRIV AIKKFLESDD DKMVKKIAMR EIKLLKQLRH
ENLVNLLEVC KKKKRWYLVF EFVDHTILDD LKLFPNGLDY QVVQKYLFQI INGIGFCHSH
NIIHRDIKPE NILVSQSGVV KLCDFGFART LAAPGEVYTD YVATRWYRAP ELLVGDVKYG
KAVDIWAIGC LVIEMLMGQP LFPGESDIDQ LHHIMTCLGN LIPRHQELFY KNPVFAGVRL
PEVKDAEAEP LESRYPKLPE AVISLAKKCL HIDPDKRPFC ADLLRHDFFQ MDGFAERFSQ
ELQLKIEKDA RNNSLPKKSQ NRKKEKDDAL GEERKTLVVQ DTNADPKIKD SKVFKVKGSK
IDVEKMEKGS RASNANCLHD NGTNHKGLAS TSLRDCSNVN IDHSRNPGTA IPPLTHNLSA
VAPGINAGMG TIPGVQNYRV DEKTKKYCNP FVKPNQPPPA GIYNMNVSTS VSGEKYLLQA
NKKRKEYPKA DVRLPELNYN HLPELRALEG IARNSRLIKK ENKCLSESRI PSLAAIDLHV
SSVASHQGAG SPLSDDSEAD LPRMEHQH
