| Tag | Content |
|---|
| EKPD ID | EKS-BOT-00056 |
| Classification | | Group/Family | Score | E-Value | Start | End | Domain Length |
|---|
| CMGC/CDK | 450.8 | 1.8E-135 | 4 | 286 | 283 |
|
| Status | Reviewed |
| Ensembl Protein | ENSBTAP00000005252 |
| UniProt Accession | Q5E9Y0; A6QQX1; |
| Protein Name | Cyclin-dependent kinase 2 |
| Protein Synonyms/Alias | Cell division protein kinase 2; |
| Gene Name | CDK2 |
| Gene Synonyms/Alias | CDK2; CDKN2; |
| Ensembl Information | |
| Organism | Bos taurus |
| Functional Description | Serine/threonine-protein kinase involved in the controlof the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Interacts with cyclins A, B1, B3, D, or E. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1 (By similarity). Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT- mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization (By similarity). |
| Protein Length | 298 |
Protein Sequence
(FASTA) | | MENFQKVEKI GEGTYGVVYK AKNKLTGEVV ALKKIRLDTE TEGVPSTAIR EISLLKELNH 60 | | PNIVKLLDVI HTENKLYLVF EFLHQDLKKF MDASALTGIP LPLIKSYLFQ LLQGLAFCHS 120 | | HRVLHRDLKP QNLLINADGS IKLADFGLAR AFGVPVRTYT HEVVTLWYRA PEILLGCKYY 180 | | STAVDIWSLG CIFAEMVTRR ALFPGDSEID QLFRIFRTLG TPDEVVWPGV TSMPDYKPSF 240 | | PKWARQDFSK VVPPLDEDGR SLLSQMLHYD PNKRISAKAA LAHPFFQDVT KPVPHLRL 298 |
|
Nucleotide Sequence
(FASTA) | | ATGGAGAACT TCCAAAAAGT GGAAAAGATC GGAGAGGGAA CGTACGGAGT TGTGTACAAA 60 | | GCCAAAAACA AGTTGACGGG AGAAGTGGTG GCGCTTAAAA AAATCCGCCT GGACACTGAG 120 | | ACAGAGGGTG TACCCAGTAC TGCCATACGA GAGATCTCTC TGCTTAAGGA GCTTAATCAC 180 | | CCTAATATTG TCAAGCTGCT GGATGTCATT CACACAGAAA ACAAACTCTA CCTGGTTTTT 240 | | GAGTTTCTGC ACCAGGATCT CAAGAAATTC ATGGATGCCT CTGCGCTCAC TGGCATTCCT 300 | | CTTCCGCTCA TAAAGAGCTA CTTGTTCCAG CTGCTCCAGG GCCTAGCTTT CTGCCACTCT 360 | | CATCGAGTCC TGCACCGAGA CCTTAAACCT CAGAACCTGC TTATCAACGC AGATGGGTCC 420 | | ATCAAGCTAG CAGACTTTGG ACTAGCCAGA GCTTTTGGGG TCCCTGTTCG TACTTATACC 480 | | CACGAGGTGG TGACTCTGTG GTACCGAGCA CCGGAAATCC TTCTGGGCTG CAAATACTAC 540 | | TCCACAGCAG TGGACATATG GAGCCTCGGT TGCATCTTTG CTGAGATGGT GACCCGCCGG 600 | | GCCCTATTCC CCGGAGATTC TGAGATCGAC CAACTCTTCC GGATCTTTCG GACCCTGGGA 660 | | ACCCCAGATG AGGTGGTTTG GCCAGGAGTT ACTTCTATGC CTGATTATAA GCCAAGTTTC 720 | | CCCAAGTGGG CCAGGCAGGA TTTTAGCAAA GTGGTGCCTC CCCTGGATGA AGATGGACGG 780 | | AGCTTGTTAT CGCAAATGCT GCACTACGAC CCTAACAAGC GGATTTCAGC CAAGGCAGCT 840 | | CTGGCTCACC CTTTCTTCCA AGATGTGACC AAGCCAGTAC CTCACCTTCG ACTCTGA 897 |
|
| Domain Profile | S: 1 yeklekigeGtygkvykakdketgevvAlKkirlekekegvpitalrEisllkelkhkni 60 | ++k+ekigeGtyg+vykak+k tgevvAlKkirl++e+egvp+ta+rEisllkel+h+ni | Q: 4 FQKVEKIGEGTYGVVYKAKNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNI 63 | 89********************************************************** |
| S: 61 vkLlevvakdkkklyLvfefleqdLkkllkkkkkkklsleevkslllqlleglaylHsnk 120 | vkLl+v++ +++klyLvfefl+qdLkk++++++ ++++l +ks+l+qll+gla++Hs++ | Q: 64 VKLLDVIH-TENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHR 122 | ********.99************************************************* |
| S: 121 ilHRDlKpqNlLiskegklklaDfGlarafssplktytkevvTlwYraPelLlgakeYst 180 | +lHRDlKpqNlLi+++g++klaDfGlaraf++p++tyt+evvTlwYraPe+Llg+k+Yst | Q: 123 VLHRDLKPQNLLINADGSIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYST 182 | ************************************************************ |
| S: 181 avDiWsvgcilaelltrkplfqgkseidqlerifkllgtpsekvwpevsklpeykksfpk 240 | avDiWs+gci+ae++tr++lf+g+seidql+rif++lgtp+e vwp+v+++p+yk sfpk | Q: 183 AVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPK 242 | ************************************************************ |
| S: 241 kkkkklkekvkklkekaldllekllaldpkkRisakealqhkyf 284 | +++++++++v+ l+e++++ll+++l++dp+kRisak+al+h++f | Q: 243 WARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFF 286 | ******************************************98 |
|
Domain Sequence
(FASTA) | | FQKVEKIGEG TYGVVYKAKN KLTGEVVALK KIRLDTETEG VPSTAIREIS LLKELNHPNI 60 | | VKLLDVIHTE NKLYLVFEFL HQDLKKFMDA SALTGIPLPL IKSYLFQLLQ GLAFCHSHRV 120 | | LHRDLKPQNL LINADGSIKL ADFGLARAFG VPVRTYTHEV VTLWYRAPEI LLGCKYYSTA 180 | | VDIWSLGCIF AEMVTRRALF PGDSEIDQLF RIFRTLGTPD EVVWPGVTSM PDYKPSFPKW 240 | | ARQDFSKVVP PLDEDGRSLL SQMLHYDPNK RISAKAALAH PFF 283 |
|
| Keyword | Acetylation; ATP-binding; Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Endosome; Kinase; Magnesium; Meiosis; Metal-binding; Mitosis; Nitration; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase. |
| Sequence Source | Ensembl |
| Orthology | |
| Gene Ontology | |
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| Created Date | 20-Feb-2013 |