CDKL4_MOUSE
ID CDKL4_MOUSE Reviewed; 342 AA.
AC Q3TZA2; B2RSS7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Cyclin-dependent kinase-like 4;
DE EC=2.7.11.22;
GN Name=Cdkl4; Synonyms=Gm942;
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].
RC STRAIN=C57BL/6J; TISSUE=Inner ear;
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].
RC TISSUE=Brain;
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:0000305}.
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; AK157995; BAE34307.1; -; mRNA.
DR EMBL; BC138986; AAI38987.1; -; mRNA.
DR EMBL; BC138988; AAI38989.1; -; mRNA.
DR CCDS; CCDS28992.1; -.
DR RefSeq; NP_001028615.1; NM_001033443.4.
DR RefSeq; XP_006524589.1; XM_006524526.1.
DR RefSeq; XP_006524590.1; XM_006524527.3.
DR RefSeq; XP_011244823.1; XM_011246521.2.
DR AlphaFoldDB; Q3TZA2; -.
DR SMR; Q3TZA2; -.
DR STRING; 10090.ENSMUSP00000083732; -.
DR iPTMnet; Q3TZA2; -.
DR PhosphoSitePlus; Q3TZA2; -.
DR MaxQB; Q3TZA2; -.
DR PaxDb; Q3TZA2; -.
DR PRIDE; Q3TZA2; -.
DR ProteomicsDB; 281355; -.
DR Antibodypedia; 29610; 194 antibodies from 25 providers.
DR DNASU; 381113; -.
DR Ensembl; ENSMUST00000086545; ENSMUSP00000083732; ENSMUSG00000033966.
DR Ensembl; ENSMUST00000234349; ENSMUSP00000157316; ENSMUSG00000033966.
DR Ensembl; ENSMUST00000234602; ENSMUSP00000157063; ENSMUSG00000033966.
DR GeneID; 381113; -.
DR KEGG; mmu:381113; -.
DR UCSC; uc008dri.2; mouse.
DR CTD; 344387; -.
DR MGI; MGI:3587025; Cdkl4.
DR VEuPathDB; HostDB:ENSMUSG00000033966; -.
DR eggNOG; KOG0593; Eukaryota.
DR GeneTree; ENSGT00940000161857; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q3TZA2; -.
DR OMA; LNFCHTH; -.
DR OrthoDB; 398098at2759; -.
DR PhylomeDB; Q3TZA2; -.
DR TreeFam; TF101031; -.
DR BioGRID-ORCS; 381113; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Cdkl4; mouse.
DR PRO; PR:Q3TZA2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q3TZA2; protein.
DR Bgee; ENSMUSG00000033966; Expressed in otolith organ and 95 other tissues.
DR Genevisible; Q3TZA2; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..342
FT /note="Cyclin-dependent kinase-like 4"
FT /id="PRO_0000085825"
FT DOMAIN 4..286
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 295..328
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"
SQ SEQUENCE 342 AA; 39446 MW; 384426A832F4D7C8 CRC64;
MEKYEKLAKI GEGSYGVVFK CRNKSSGQVV AIKKFVESED DRVVRKIALR EIRMLKQLKH
PNLVNLIEVF RRKRKMHLVF EYCDHTLLNE LERNPNGVSD GVIKSVLWQT LQALNFCHKH
NCIHRDVKPE NILITKQGMI KICDFGFARI LIPGDAYTDY VATRWYRAPE LLVGDTKYGS
SVDVWAVGCV FAELLTGQPL WPGKSDVDQL YLIIRTLGKL IPRHQSIFRS NQFFRGISIP
EPEDMETLEE KFSNVQPVAL SFMKGCLKMN PDERLTCAQL LDSAYFESFQ EDQMKRKARS
EGRSRRRQQN QLLPLIPGSH ISPTPDGRKQ VVQLKFDHLP NI
