Q80YP0 (CDK3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclin-dependent kinase 3
EC=2.7.11.22

Alternative name(s):
Cell division protein kinase 3

Gene names

Name:	Cdk3
Synonyms:	Cdkn3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine-protein kinase that plays a critical role in the control of the eukaryotic cell cycle; involved in G0-G1 and G1-S cell cycle transitions. Interacts with CCNC/cyclin-C during interphase. Phosphorylates histone H1, ATF1, RB1 and CABLES1. ATF1 phosphorylation triggers ATF1 transactivation and transcriptional activities, and promotes cell proliferation and transformation. CDK3/cyclin-C mediated RB1 phosphorylation is required for G0-G1 transition. Promotes G1-S transition probably by contributing to the activation of E2F1, E2F2 and E2F3 in a RB1-independent manner. Ref.4
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with CABLES1 and ATF1. Binding to CCNC/cyclin-C promotes RB1 phosphorylation By similarity. Binds to CABLES2. Ref.5
Developmental stage	Expressed in heart, lung, nasal cavity, roof-plate of the fourth ventricle, skin, cartilage primordium of the basisphenoid and basioccipital bone at 12.5 dpc. Ref.1
Miscellaneous	The truncated form has lost its catalytic activity due to a truncating mutation. This truncation occurs near the T loop, which is involved in activation by CDK-activating kinase and deletes motif XI known to be required for kinase function. Consequently, the truncated protein generates a null allele. This mutation is found in laboratory strains but not in wild-mice species such as Mus spretus and Mus mus castaneus.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cyclin-dependent protein serine/threonine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q80YP0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q80YP0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-194: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 303	303	Cyclin-dependent kinase 3		PRO_0000085777
Regions
	Domain	4 – 285	282	Protein kinase
	Nucleotide binding	10 – 18	9	ATP By similarity
Sites
	Active site	127	1	Proton acceptor By similarity
	Binding site	33	1	ATP By similarity
Amino acid modifications
	Modified residue	15	1	Phosphotyrosine Ref.6
Natural variations
	Alternative sequence	1 – 194	194	Missing in isoform 2.		VSP_023572
	Natural variant	187 – 303	117	Missing in truncated, inactive form.

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 20, 2007. Version 2. Checksum: D83EAAA8C133BC88	FASTA	303	33,888
	10 20 30 40 50 60 MDVFQKVEKI GEGTYGVVYK ARNKVTGQLV ALKKIRLDLE AEGVPSTAVR EISLLKELKH 70 80 90 100 110 120 PNIIKLLDVV HREKKLYMVF EFLTQDLKRH MDSSPTSELP LPVVKSYLAQ LLEGVSFCHS 130 140 150 160 170 180 HRVIHRDLKP QNLLLDGLGA IKLADFGLAR AFGVPLRTYT HEVVTLWYRA PEILLGSKFY 190 200 210 220 230 240 STAVDISIGC IFAEMVTGKA LFPGDSEIDQ LFRIFRTLGT PSEATWPGVS QMPDYQSSFP 250 260 270 280 290 300 KWSRKGLEEI VPSLGPEGKD LLLRLLQYDP SQRISAKTAL AHPYFSPGHS LAPQQCTAGR SSR
	Isoform 2 [UniParc]. Checksum: 5FCE672BA6403FE4	FASTA	109	12,034
	10 20 30 40 50 60 MVTGKALFPG DSEIDQLFRI FRTLGTPSEA TWPGVSQMPD YQSSFPKWSR KGLEEIVPSL 70 80 90 100 GPEGKDLLLR LLQYDPSQRI SAKTALAHPY FSPGHSLAPQ QCTAGRSSR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A premature-termination mutation in the Mus musculus cyclin-dependent kinase 3 gene." Ye X., Zhu C., Harper J.W. Proc. Natl. Acad. Sci. U.S.A. 98:1682-1686(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TRUNCATED ISOFORM), DEVELOPMENTAL STAGE. Strain: 129/Sv and C57BL/6J. Tissue: Tongue.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Mammary gland.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"ik3-1/Cables is a substrate for cyclin-dependent kinase 3 (cdk 3)." Yamochi T., Semba K., Tsuji K., Mizumoto K., Sato H., Matsuura Y., Nishimoto I., Matsuoka M. Eur. J. Biochem. 268:6076-6082(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS CABLES1 KINASE.
[5]	"Ik3-2, a relative to ik3-1/cables, is associated with cdk3, cdk5, and c-abl." Sato H., Nishimoto I., Matsuoka M. Biochim. Biophys. Acta 1574:157-163(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CABLES2.
[6]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF327523 Genomic DNA. Translation: AAK51354.1. AK009918 mRNA. Translation: BAB26584.1. AK166387 mRNA. Translation: BAE38746.1. AL669925 Genomic DNA. No translation available.
IPI	IPI00109650. IPI00830384.
UniGene	Mm.33677.
3D structure databases
ProteinModelPortal	Q80YP0.
SMR	Q80YP0. Positions 1-285.
ModBase	Search...
PTM databases
PhosphoSite	Q80YP0.
Proteomic databases
PaxDb	Q80YP0.
PRIDE	Q80YP0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
MGI	MGI:1916931. Cdk3.
Phylogenomic databases
eggNOG	COG0515.
HOVERGEN	HBG014652.
InParanoid	Q80YP0.
OrthoDB	EOG4C5CJV.
Gene expression databases
Bgee	Q80YP0.
CleanEx	MM_CDK3.
Genevestigator	Q80YP0.
GermOnline	ENSMUSG00000034288. Mus musculus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

CDK3_MOUSE

Accession

Primary (citable) accession number: Q80YP0
Secondary accession number(s): Q3TLP6, Q9D6V6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	March 20, 2007
Last modified:	May 1, 2013
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program