CDKL3_MOUSE
ID CDKL3_MOUSE Reviewed; 595 AA.
AC Q8BLF2; A2ACR7; A2ACR8; A2ACR9; A2ACS0; A2ACS1; Q5M6W2; Q8BKR2; Q8BL49;
AC Q8BLN9; Q8BVE0; Q8K134;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Cyclin-dependent kinase-like 3 {ECO:0000305};
DE EC=2.7.11.22;
GN Name=Cdkl3 {ECO:0000312|MGI:MGI:2388268};
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] (ISOFORMS 1; 2; 5 AND 6), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 368-595 (ISOFORM 7).
RC STRAIN=C57BL/6J;
RC TISSUE=Brain cortex, Corpora quadrigemina, Embryo, and Embryonic lung;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=FVB/N; TISSUE=Kidney;
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).
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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q8BLF2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BLF2-2; Sequence=VSP_016154, VSP_016157;
CC Name=3;
CC IsoId=Q8BLF2-7; Sequence=VSP_016155, VSP_016156;
CC Name=4;
CC IsoId=Q8BLF2-4; Sequence=VSP_016150, VSP_016151;
CC Name=5;
CC IsoId=Q8BLF2-5; Sequence=VSP_016149, VSP_016155, VSP_016156;
CC Name=6;
CC IsoId=Q8BLF2-6; Sequence=VSP_016152;
CC Name=7;
CC IsoId=Q8BLF2-8; Sequence=VSP_030154;
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}.
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DR EMBL; AK043995; BAC31729.2; -; mRNA.
DR EMBL; AK045356; BAC32324.1; -; mRNA.
DR EMBL; AK046394; BAC32701.1; -; mRNA.
DR EMBL; AK050990; BAC34488.1; -; mRNA.
DR EMBL; AK078804; BAC37400.1; -; mRNA.
DR EMBL; AL669920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028871; AAH28871.1; -; mRNA.
DR CCDS; CCDS24665.1; -. [Q8BLF2-1]
DR CCDS; CCDS48788.1; -. [Q8BLF2-7]
DR CCDS; CCDS48790.1; -. [Q8BLF2-2]
DR CCDS; CCDS48791.1; -. [Q8BLF2-6]
DR CCDS; CCDS48792.1; -. [Q8BLF2-4]
DR RefSeq; NP_001160125.1; NM_001166653.1.
DR RefSeq; NP_001160126.1; NM_001166654.1. [Q8BLF2-2]
DR RefSeq; NP_001160127.1; NM_001166655.1. [Q8BLF2-6]
DR RefSeq; NP_001160128.1; NM_001166656.1. [Q8BLF2-7]
DR RefSeq; NP_001160129.1; NM_001166657.1. [Q8BLF2-4]
DR RefSeq; NP_722480.3; NM_153785.4. [Q8BLF2-1]
DR RefSeq; XP_011247178.1; XM_011248876.1.
DR RefSeq; XP_011247179.1; XM_011248877.2. [Q8BLF2-2]
DR RefSeq; XP_011247180.1; XM_011248878.1. [Q8BLF2-2]
DR RefSeq; XP_011247181.1; XM_011248879.1.
DR RefSeq; XP_011247182.1; XM_011248880.2. [Q8BLF2-2]
DR RefSeq; XP_017169911.1; XM_017314422.1.
DR AlphaFoldDB; Q8BLF2; -.
DR SMR; Q8BLF2; -.
DR STRING; 10090.ENSMUSP00000064315; -.
DR iPTMnet; Q8BLF2; -.
DR PhosphoSitePlus; Q8BLF2; -.
DR MaxQB; Q8BLF2; -.
DR PaxDb; Q8BLF2; -.
DR PRIDE; Q8BLF2; -.
DR ProteomicsDB; 281562; -. [Q8BLF2-1]
DR ProteomicsDB; 281563; -. [Q8BLF2-2]
DR ProteomicsDB; 281564; -. [Q8BLF2-7]
DR ProteomicsDB; 281565; -. [Q8BLF2-4]
DR ProteomicsDB; 281566; -. [Q8BLF2-5]
DR ProteomicsDB; 281567; -. [Q8BLF2-6]
DR ProteomicsDB; 281568; -. [Q8BLF2-8]
DR Antibodypedia; 2061; 204 antibodies from 29 providers.
DR DNASU; 213084; -.
DR Ensembl; ENSMUST00000063303; ENSMUSP00000064315; ENSMUSG00000020389. [Q8BLF2-1]
DR Ensembl; ENSMUST00000063321; ENSMUSP00000065128; ENSMUSG00000020389. [Q8BLF2-7]
DR Ensembl; ENSMUST00000109076; ENSMUSP00000104704; ENSMUSG00000020389. [Q8BLF2-4]
DR Ensembl; ENSMUST00000109077; ENSMUSP00000104705; ENSMUSG00000020389. [Q8BLF2-4]
DR Ensembl; ENSMUST00000109078; ENSMUSP00000104706; ENSMUSG00000020389. [Q8BLF2-6]
DR Ensembl; ENSMUST00000109079; ENSMUSP00000104707; ENSMUSG00000020389. [Q8BLF2-7]
DR Ensembl; ENSMUST00000109081; ENSMUSP00000104709; ENSMUSG00000020389. [Q8BLF2-2]
DR Ensembl; ENSMUST00000121591; ENSMUSP00000112477; ENSMUSG00000020389. [Q8BLF2-2]
DR GeneID; 213084; -.
DR KEGG; mmu:213084; -.
DR UCSC; uc007iuv.2; mouse. [Q8BLF2-1]
DR UCSC; uc007iux.2; mouse. [Q8BLF2-4]
DR UCSC; uc007iuz.2; mouse. [Q8BLF2-2]
DR UCSC; uc011xul.1; mouse. [Q8BLF2-7]
DR CTD; 51265; -.
DR MGI; MGI:2388268; Cdkl3.
DR VEuPathDB; HostDB:ENSMUSG00000020389; -.
DR eggNOG; KOG0593; Eukaryota.
DR GeneTree; ENSGT00940000161317; -.
DR HOGENOM; CLU_000288_136_1_1; -.
DR InParanoid; Q8BLF2; -.
DR OMA; GMEVKQV; -.
DR OrthoDB; 398098at2759; -.
DR TreeFam; TF101031; -.
DR BioGRID-ORCS; 213084; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Cdkl3; mouse.
DR PRO; PR:Q8BLF2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BLF2; protein.
DR Bgee; ENSMUSG00000020389; Expressed in spermatid and 113 other tissues.
DR ExpressionAtlas; Q8BLF2; baseline and differential.
DR Genevisible; Q8BLF2; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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:0097484; P:dendrite extension; IMP:MGI.
DR GO; GO:0030517; P:negative regulation of axon extension; IMP:MGI.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:MGI.
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 Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..595
FT /note="Cyclin-dependent kinase-like 3"
FT /id="PRO_0000085822"
FT DOMAIN 4..286
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 362..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 45..51
FT /note="[NKR]KIAxRE"
FT COMPBIAS 362..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
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 MOD_RES 158
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM01"
FT MOD_RES 160
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM01"
FT VAR_SEQ 1..17
FT /note="MEMYETLGKVGEGSYGT -> MKPLEKWEREVMEP (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016149"
FT VAR_SEQ 295..353
FT /note="FIPELRAKLLQEAKVNSFIKPKENFKENEPVRDEKKSVFTNTLLYGNPSLYG
FT KEVDRDK -> KWTETKGPRSSKSESLRPKGAKEMSQTRRSQSMKATTASRAQLMTHSP
FT HHWTRSLLSWN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016150"
FT VAR_SEQ 354..595
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016151"
FT VAR_SEQ 458..595
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016152"
FT VAR_SEQ 576..595
FT /note="GGDGDCEGKNLKRNRFFFSR -> QPVKQVNSNQ (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030154"
FT VAR_SEQ 576..585
FT /note="GGDGDCEGKN -> QSARHLPGQC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016154"
FT VAR_SEQ 576..581
FT /note="GGDGDC -> SLTMYL (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016155"
FT VAR_SEQ 582..595
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016156"
FT VAR_SEQ 586..595
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016157"
FT CONFLICT 12
FT /note="E -> Q (in Ref. 1; BAC32701)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="H -> Y (in Ref. 1; BAC37400)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="P -> H (in Ref. 1; BAC32324)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="D -> E (in Ref. 1; BAC37400)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 67739 MW; 3DB415A3EEBC7C4B CRC64;
MEMYETLGKV GEGSYGTVMK CKHKDTGRIV AIKIFYEKPE KSVNKIATRE IKFLKQFRHE
NLVNLIEVFR QKKKIHLVFE FIDHTVLDEL QHYCHGLESK RLRKYLFQIL RAIEYLHNNN
IIHRDIKPEN ILVSQSGITK LCDFGFARTL AAPGDVYTDY VATRWYRAPE LVLKDTSYGK
PVDIWALGCM IIEMATGHPF LPSSSDLDLL HKIVLKVGNL TPHLHNIFSK SPIFAGVVLP
QVQHPKTARK KYPKLNGLLA DIVHACLQID PAERTSSTDL LRHDYFTRDG FIEKFIPELR
AKLLQEAKVN SFIKPKENFK ENEPVRDEKK SVFTNTLLYG NPSLYGKEVD RDKRAKELKV
RVIKAKGGKG DVPDQKKPEY EGDHRQQGTA DDTQPSSLDK KPSVLELTNP LNPSENSDGV
KEDPHAGGCM IMPPINLTSS NLLAANLSSN LSHPNSRLTE RTKKRRTSSQ TIGQTLSNSR
QEDTGPTQVQ TEKGAFNERT GQNDQISSGN KRKLNFPKCD RKEFHFPELP FTVQAKEMKG
MEVKQIKVLK RESKKTDSSK IPTLLSMDPN QEKQEGGDGD CEGKNLKRNR FFFSR
