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Protein

Cyclin-dependent kinase 3

Gene

Cdk3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331ATPPROSITE-ProRule annotation
Active sitei127 – 1271Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 189ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 3 (EC:2.7.11.22)
Alternative name(s):
Cell division protein kinase 3
Gene namesi
Name:Cdk3
Synonyms:Cdk3-ps, Cdkn3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1916931. Cdk3-ps.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303Cyclin-dependent kinase 3PRO_0000085777Add
BLAST

Proteomic databases

PaxDbiQ80YP0.
PRIDEiQ80YP0.

PTM databases

PhosphoSiteiQ80YP0.

Expressioni

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiQ80YP0.
CleanExiMM_CDK3.

Interactioni

Subunit structurei

Interacts with CABLES1 and ATF1. Binding to CCNC/cyclin-C promotes RB1 phosphorylation (By similarity). Binds to CABLES2.By similarity1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ80YP0.
SMRiQ80YP0. Positions 1-285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 285282Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG014652.
InParanoidiQ80YP0.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q80YP0-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDVFQKVEKI GEGTYGVVYK ARNKVTGQLV ALKKIRLDLE AEGVPSTAVR
60 70 80 90 100
EISLLKELKH PNIIKLLDVV HREKKLYMVF EFLTQDLKRH MDSSPTSELP
110 120 130 140 150
LPVVKSYLAQ LLEGVSFCHS HRVIHRDLKP QNLLLDGLGA IKLADFGLAR
160 170 180 190 200
AFGVPLRTYT HEVVTLWYRA PEILLGSKFY STAVDISIGC IFAEMVTGKA
210 220 230 240 250
LFPGDSEIDQ LFRIFRTLGT PSEATWPGVS QMPDYQSSFP KWSRKGLEEI
260 270 280 290 300
VPSLGPEGKD LLLRLLQYDP SQRISAKTAL AHPYFSPGHS LAPQQCTAGR

SSR
Length:303
Mass (Da):33,888
Last modified:March 20, 2007 - v2
Checksum:iD83EAAA8C133BC88
GO
Isoform 2 (identifier: Q80YP0-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:109
Mass (Da):12,034
Checksum:i5FCE672BA6403FE4
GO

Polymorphismi

A point mutation converts Trp-187 to a premature termination codon, resulting in a truncated form that has no catalytic activity. 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 M.spretus and M.musculus castaneus.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti187 – 303117Missing in truncated, inactive form.
Add
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 194194Missing in isoform 2. 1 PublicationVSP_023572Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF327523 Genomic DNA. Translation: AAK51354.1.
AK009918 mRNA. Translation: BAB26584.1.
AK166387 mRNA. Translation: BAE38746.1.
AL669925 Genomic DNA. No translation available.
UniGeneiMm.33677.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF327523 Genomic DNA. Translation: AAK51354.1.
AK009918 mRNA. Translation: BAB26584.1.
AK166387 mRNA. Translation: BAE38746.1.
AL669925 Genomic DNA. No translation available.
UniGeneiMm.33677.

3D structure databases

ProteinModelPortaliQ80YP0.
SMRiQ80YP0. Positions 1-285.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ80YP0.

Proteomic databases

PaxDbiQ80YP0.
PRIDEiQ80YP0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1916931. Cdk3-ps.

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG014652.
InParanoidiQ80YP0.

Miscellaneous databases

PROiQ80YP0.
SOURCEiSearch...

Gene expression databases

BgeeiQ80YP0.
CleanExiMM_CDK3.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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], DEVELOPMENTAL STAGE, POLYMORPHISM.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. 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.

Entry informationi

Entry nameiCDK3_MOUSE
AccessioniPrimary (citable) accession number: Q80YP0
Secondary accession number(s): Q3TLP6, Q9D6V6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: March 20, 2007
Last modified: June 24, 2015
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Defined as a polymorphic pseudogene by MGI.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.