CDK3_MOUSE
ID CDK3_MOUSE Reviewed; 304 AA.
AC Q80YP0; Q3TLP6; Q9D6V6;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Cyclin-dependent kinase 3;
DE EC=2.7.11.22;
DE AltName: Full=Cell division protein kinase 3;
GN Name=Cdk3; Synonyms=Cdk3-ps, Cdkn3;
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], DEVELOPMENTAL STAGE, AND POLYMORPHISM.
RC STRAIN=129/Sv, and C57BL/6J; TISSUE=Tongue;
RX PubMed=11172011; DOI=10.1073/pnas.98.4.1682;
RA Ye X., Zhu C., Harper J.W.;
RT "A premature-termination mutation in the Mus musculus cyclin-dependent
RT kinase 3 gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1682-1686(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland;
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 [3]
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 [4]
RP FUNCTION AS CABLES1 KINASE.
RX PubMed=11733001; DOI=10.1046/j.0014-2956.2001.02555.x;
RA Yamochi T., Semba K., Tsuji K., Mizumoto K., Sato H., Matsuura Y.,
RA Nishimoto I., Matsuoka M.;
RT "ik3-1/Cables is a substrate for cyclin-dependent kinase 3 (cdk 3).";
RL Eur. J. Biochem. 268:6076-6082(2001).
RN [5]
RP INTERACTION WITH CABLES2.
RX PubMed=11955625; DOI=10.1016/s0167-4781(01)00367-0;
RA Sato H., Nishimoto I., Matsuoka M.;
RT "Ik3-2, a relative to ik3-1/cables, is associated with cdk3, cdk5, and c-
RT abl.";
RL Biochim. Biophys. Acta 1574:157-163(2002).
CC -!- FUNCTION: Serine/threonine-protein kinase that plays a critical role in
CC the control of the eukaryotic cell cycle; involved in G0-G1 and G1-S
CC cell cycle transitions. Interacts with CCNC/cyclin-C during interphase.
CC Phosphorylates histone H1, ATF1, RB1 and CABLES1. ATF1 phosphorylation
CC triggers ATF1 transactivation and transcriptional activities, and
CC promotes cell proliferation and transformation. CDK3/cyclin-C mediated
CC RB1 phosphorylation is required for G0-G1 transition. Promotes G1-S
CC transition probably by contributing to the activation of E2F1, E2F2 and
CC E2F3 in a RB1-independent manner. {ECO:0000269|PubMed:11733001}.
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 -!- SUBUNIT: Interacts with CABLES1 and ATF1. Binding to CCNC/cyclin-C
CC promotes RB1 phosphorylation (By similarity). Binds to CABLES2.
CC {ECO:0000250, ECO:0000269|PubMed:11955625}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80YP0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80YP0-2; Sequence=VSP_023572;
CC -!- DEVELOPMENTAL STAGE: Expressed in heart, lung, nasal cavity, roof-plate
CC of the fourth ventricle, skin, cartilage primordium of the basisphenoid
CC and basioccipital bone at 12.5 dpc. {ECO:0000269|PubMed:11172011}.
CC -!- POLYMORPHISM: A point mutation converts Trp-187 to a premature
CC termination codon, resulting in a truncated form that has no catalytic
CC activity. This truncation occurs near the T loop, which is involved in
CC activation by CDK-activating kinase and deletes motif XI known to be
CC required for kinase function. Consequently, the truncated protein
CC generates a null allele. This mutation is found in laboratory strains
CC but not in wild-mice species such as M.spretus and M.musculus
CC castaneus. {ECO:0000269|PubMed:11172011}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC -!- CAUTION: Defined as a polymorphic pseudogene by MGI. {ECO:0000305}.
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DR EMBL; AF327523; AAK51354.1; -; Genomic_DNA.
DR EMBL; AK009918; BAB26584.1; -; mRNA.
DR EMBL; AK166387; BAE38746.1; -; mRNA.
DR EMBL; AL669925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q80YP0; -.
DR SMR; Q80YP0; -.
DR ComplexPortal; CPX-331; Cyclin C-CDK3 complex.
DR iPTMnet; Q80YP0; -.
DR PhosphoSitePlus; Q80YP0; -.
DR SwissPalm; Q80YP0; -.
DR jPOST; Q80YP0; -.
DR MaxQB; Q80YP0; -.
DR PeptideAtlas; Q80YP0; -.
DR PRIDE; Q80YP0; -.
DR ProteomicsDB; 281439; -. [Q80YP0-1]
DR ProteomicsDB; 281440; -. [Q80YP0-2]
DR MGI; MGI:1916931; Cdk3.
DR InParanoid; Q80YP0; -.
DR PhylomeDB; Q80YP0; -.
DR ChiTaRS; Cdkn3; mouse.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80YP0; protein.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell cycle; Cell division; Kinase;
KW Mitosis; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..304
FT /note="Cyclin-dependent kinase 3"
FT /id="PRO_0000085777"
FT DOMAIN 4..286
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 127
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 1..195
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023572"
SQ SEQUENCE 304 AA; 34075 MW; 468B5E805F0CBE36 CRC64;
MDVFQKVEKI GEGTYGVVYK ARNKVTGQLV ALKKIRLDLE AEGVPSTAVR EISLLKELKH
PNIIKLLDVV HREKKLYMVF EFLTQDLKRH MDSSPTSELP LPVVKSYLAQ LLEGVSFCHS
HRVIHRDLKP QNLLLDGLGA IKLADFGLAR AFGVPLRTYT HEVVTLWYRA PEILLGSKFY
STAVDIWSIG CIFAEMVTGK ALFPGDSEID QLFRIFRTLG TPSEATWPGV SQMPDYQSSF
PKWSRKGLEE IVPSLGPEGK DLLLRLLQYD PSQRISAKTA LAHPYFSPGH SLAPQQCTAG
RSSR
