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Cyclin-dependent kinase 2 (EC 2.7.11.22) (Cell division protein kinase 2)

 CDK2_MOUSE              Reviewed;         346 AA.
P97377; O55105;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
18-JUL-2018, entry version 176.
RecName: Full=Cyclin-dependent kinase 2;
EC=2.7.11.22 {ECO:0000269|PubMed:23853094};
AltName: Full=Cell division protein kinase 2;
Name=Cdk2; Synonyms=Cdkn2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CDK2-ALPHA).
STRAIN=C57BL/6J;
Jun D., Lee Y.H., Park H.K., Kim Y.H.;
"Exon-intron organization of the murine cyclin-dependent kinase-2
genes Cdk2-alpha and Cdk2-beta.";
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
Ellenrieder C., Bartosch B., Lee G.Y., Murphy M., Sweeney C.,
Hergersberg M., Hunt T., Carrington M., Jaussi R.;
"The 39 kDa form of CDK2 arises through alternative splicing, is
expressed in many but not all mammals, and is an active kinase.";
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CDK2-BETA).
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION AT TYR-15, MUTAGENESIS OF TYR-15, IDENTIFICATION IN A
COMPLEX WITH CABLES1; CCNA1 AND CCNE1, AND INTERACTION WITH CABLES1.
PubMed=11585773;
Wu C.-L., Kirley S.D., Xiao H., Chuang Y., Chung D.C., Zukerberg L.R.;
"Cables enhances cdk2 tyrosine 15 phosphorylation by Wee1, inhibits
cell growth, and is lost in many human colon and squamous cancers.";
Cancer Res. 61:7325-7332(2001).
[5]
FUNCTION AS CABLES1 KINASE.
PubMed=11733001; DOI=10.1046/j.0014-2956.2001.02555.x;
Yamochi T., Semba K., Tsuji K., Mizumoto K., Sato H., Matsuura Y.,
Nishimoto I., Matsuoka M.;
"ik3-1/Cables is a substrate for cyclin-dependent kinase 3 (cdk 3).";
Eur. J. Biochem. 268:6076-6082(2001).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=14561402; DOI=10.1016/j.cub.2003.09.024;
Berthet C., Aleem E., Coppola V., Tessarollo L., Kaldis P.;
"Cdk2 knockout mice are viable.";
Curr. Biol. 13:1775-1785(2003).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12923533; DOI=10.1038/ng1232;
Ortega S., Prieto I., Odajima J., Martin A., Dubus P., Sotillo R.,
Barbero J.L., Malumbres M., Barbacid M.;
"Cyclin-dependent kinase 2 is essential for meiosis but not for
mitotic cell division in mice.";
Nat. Genet. 35:25-31(2003).
[8]
INTERACTION WITH CEBPA.
PubMed=15107404; DOI=10.1101/gad.1183304;
Wang G.L., Iakova P., Wilde M., Awad S., Timchenko N.A.;
"Liver tumors escape negative control of proliferation via PI3K/Akt-
mediated block of C/EBP alpha growth inhibitory activity.";
Genes Dev. 18:912-925(2004).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17942597; DOI=10.1091/mbc.E07-06-0525;
Satyanarayana A., Hilton M.B., Kaldis P.;
"p21 Inhibits Cdk1 in the absence of Cdk2 to maintain the G1/S phase
DNA damage checkpoint.";
Mol. Biol. Cell 19:65-77(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=23853094; DOI=10.1074/jbc.M113.467704;
Morawski P.A., Mehra P., Chen C., Bhatti T., Wells A.D.;
"Foxp3 protein stability is regulated by cyclin-dependent kinase 2.";
J. Biol. Chem. 288:24494-24502(2013).
-!- FUNCTION: Serine/threonine-protein kinase involved in the control
of the cell cycle; essential for meiosis, but dispensable for
mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1,
BRCA2, MYC, NPAT, EZH2. 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. Phosphorylates
FOXP3 and negatively regulates its transcriptional activity and
protein stability (PubMed:23853094). Phosphorylates CDK2AP2 (By
similarity). {ECO:0000250|UniProtKB:P24941,
ECO:0000269|PubMed:11733001, ECO:0000269|PubMed:12923533,
ECO:0000269|PubMed:14561402, ECO:0000269|PubMed:17942597,
ECO:0000269|PubMed:23853094}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:23853094}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P24941};
Note=Binds 2 Mg(2+) ions. {ECO:0000250|UniProtKB:P24941};
-!- ENZYME REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
the enzyme, while phosphorylation at Thr-160 activates it.
Stimulated by MYC. Inactivated by CDKN1A (p21) (By similarity).
{ECO:0000250|UniProtKB:P24941}.
-!- SUBUNIT: Found in a complex with CABLES1, CCNA1 and CCNE1.
Interacts with CABLES1 (PubMed:11585773). Interacts with UHRF2.
Part of a complex consisting of UHRF2, CDK2 and CCNE1. Interacts
with the Speedy/Ringo proteins SPDYA and SPDYC. Interaction with
SPDYA promotes kinase activation via a conformation change that
alleviates obstruction of the substrate-binding cleft by the T-
loop. Found in a complex with both SPDYA and CDKN1B/KIP1. Binds to
RB1 and CDK7. Binding to CDKN1A (p21) leads to CDK2/cyclin E
inactivation at the G1-S phase DNA damage checkpoint, thereby
arresting cells at the G1-S transition during DNA repair.
Associated with PTPN6 and beta-catenin/CTNNB1. Interacts with
CACUL1. May interact with CEP63. Interacts with ANKRD17 (By
similarity). Interacts with CEBPA (when phosphorylated)
(PubMed:15107404). Forms a ternary complex with CCNA2 and CDKN1B;
CDKN1B inhibits the kinase activity of CDK2 through conformational
rearrangements. Interacts with cyclins A, B1, B3, D, or E.
Interacts with CDK2AP2 (By similarity).
{ECO:0000250|UniProtKB:P24941, ECO:0000250|UniProtKB:Q63699,
ECO:0000269|PubMed:11585773, ECO:0000269|PubMed:15107404}.
-!- INTERACTION:
P51943:Ccna2; NbExp=3; IntAct=EBI-847048, EBI-846980;
Q61457:Ccne1; NbExp=3; IntAct=EBI-847048, EBI-643090;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000250}. Nucleus, Cajal body
{ECO:0000250}. Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}.
Note=Localized at the centrosomes in late G2 phase after
separation of the centrosomes but before the start of prophase.
Nuclear-cytoplasmic trafficking is mediated during the inhibition
by 1,25-(OH)(2)D(3) (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=CDK2-beta;
IsoId=P97377-1; Sequence=Displayed;
Name=CDK2-alpha;
IsoId=P97377-2; Sequence=VSP_004800;
-!- PTM: Phosphorylated at Thr-160 by CDK7 in a CAK complex.
Phosphorylation at Thr-160 promotes kinase activity, whereas
phosphorylation at Tyr-15 by WEE1 reduces slightly kinase
activity. Phosphorylated on Thr-14 and Tyr-15 during S and G2
phases before being dephosphorylated by CDC25A.
{ECO:0000250|UniProtKB:P24941}.
-!- PTM: Nitrosylated after treatment with nitric oxide (DETA-NO).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Reduced body size and impaired neural
progenitor cell proliferation. Sterility due to defective meiosis;
no effect on mitotic cells. Premature translocation of CDK1 from
the cytoplasm to the nucleus compensating CDK2 loss. Prolonged and
impaired DNA repair activity upon DNA damage by gamma-irradiation.
{ECO:0000269|PubMed:12923533, ECO:0000269|PubMed:14561402,
ECO:0000269|PubMed:17942597}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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EMBL; U63337; AAB37128.1; -; mRNA.
EMBL; AJ223732; CAA11533.1; -; mRNA.
EMBL; AJ223733; CAA11534.1; -; Genomic_DNA.
EMBL; AJ223733; CAA11535.1; -; Genomic_DNA.
EMBL; BC005654; AAH05654.1; -; mRNA.
CCDS; CCDS24288.1; -. [P97377-2]
CCDS; CCDS24289.1; -. [P97377-1]
RefSeq; NP_058036.1; NM_016756.4. [P97377-2]
RefSeq; NP_904326.1; NM_183417.3. [P97377-1]
UniGene; Mm.111326; -.
ProteinModelPortal; P97377; -.
SMR; P97377; -.
BioGrid; 198644; 30.
ComplexPortal; CPX-2065; Cyclin A1-CDK2 complex.
ComplexPortal; CPX-2066; Cyclin A2-CDK2 complex.
ComplexPortal; CPX-2071; Cyclin B3-CDK2 complex.
ComplexPortal; CPX-2081; Cyclin E1-CDK2 complex.
ComplexPortal; CPX-2082; Cyclin E2-CDK2 complex.
CORUM; P97377; -.
DIP; DIP-24176N; -.
ELM; P97377; -.
IntAct; P97377; 7.
MINT; P97377; -.
STRING; 10090.ENSMUSP00000026416; -.
iPTMnet; P97377; -.
PhosphoSitePlus; P97377; -.
SwissPalm; P97377; -.
PaxDb; P97377; -.
PeptideAtlas; P97377; -.
PRIDE; P97377; -.
Ensembl; ENSMUST00000026415; ENSMUSP00000026415; ENSMUSG00000025358. [P97377-2]
Ensembl; ENSMUST00000026416; ENSMUSP00000026416; ENSMUSG00000025358. [P97377-1]
GeneID; 12566; -.
KEGG; mmu:12566; -.
UCSC; uc007hny.2; mouse. [P97377-1]
CTD; 1017; -.
MGI; MGI:104772; Cdk2.
eggNOG; KOG0594; Eukaryota.
eggNOG; ENOG410XPP3; LUCA.
GeneTree; ENSGT00910000144030; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P97377; -.
KO; K02206; -.
OMA; RHTNETI; -.
OrthoDB; EOG091G0CH0; -.
PhylomeDB; P97377; -.
TreeFam; TF101021; -.
BRENDA; 2.7.11.22; 3474.
Reactome; R-MMU-1538133; G0 and Early G1.
Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
Reactome; R-MMU-176408; Regulation of APC/C activators between G1/S and early anaphase.
Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
Reactome; R-MMU-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
Reactome; R-MMU-68911; G2 Phase.
Reactome; R-MMU-68949; Orc1 removal from chromatin.
Reactome; R-MMU-68962; Activation of the pre-replicative complex.
Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-MMU-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
Reactome; R-MMU-69202; Cyclin E associated events during G1/S transition.
Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-MMU-69563; p53-Dependent G1 DNA Damage Response.
Reactome; R-MMU-69656; Cyclin A:Cdk2-associated events at S phase entry.
Reactome; R-MMU-8849470; PTK6 Regulates Cell Cycle.
ChiTaRS; Cdk2; mouse.
PRO; PR:P97377; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000025358; -.
CleanEx; MM_CDK2; -.
ExpressionAtlas; P97377; baseline and differential.
Genevisible; P97377; MM.
GO; GO:0015030; C:Cajal body; ISO:MGI.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0000781; C:chromosome, telomeric region; IDA:MGI.
GO; GO:0000793; C:condensed chromosome; IDA:MGI.
GO; GO:0097123; C:cyclin A1-CDK2 complex; IDA:MGI.
GO; GO:0097124; C:cyclin A2-CDK2 complex; IDA:MGI.
GO; GO:0097134; C:cyclin E1-CDK2 complex; IDA:MGI.
GO; GO:0097135; C:cyclin E2-CDK2 complex; IDA:MGI.
GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0000805; C:X chromosome; IDA:MGI.
GO; GO:0000806; C:Y chromosome; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0030332; F:cyclin binding; ISO:MGI.
GO; GO:0097472; F:cyclin-dependent protein kinase activity; ISO:MGI.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0035173; F:histone kinase activity; IEA:Ensembl.
GO; GO:0016301; F:kinase activity; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
GO; GO:0007099; P:centriole replication; ISO:MGI.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:MGI.
GO; GO:0016572; P:histone phosphorylation; ISO:MGI.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0032298; P:positive regulation of DNA-dependent DNA replication initiation; IGI:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:MGI.
GO; GO:0006813; P:potassium ion transport; IGI:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
GO; GO:0060968; P:regulation of gene silencing; ISO:MGI.
GO; GO:0051591; P:response to cAMP; ISO:MGI.
GO; GO:0051602; P:response to electrical stimulus; ISO:MGI.
GO; GO:0010033; P:response to organic substance; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 2.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Cell cycle;
Cell division; Complete proteome; Cytoplasm; Cytoskeleton; DNA damage;
DNA repair; Endosome; Kinase; Magnesium; Meiosis; Metal-binding;
Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 346 Cyclin-dependent kinase 2.
/FTId=PRO_0000085771.
DOMAIN 4 334 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 10 18 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 81 83 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 129 132 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 127 127 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
METAL 132 132 Magnesium.
{ECO:0000250|UniProtKB:P24941}.
METAL 145 145 Magnesium.
{ECO:0000250|UniProtKB:P24941}.
BINDING 33 33 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 86 86 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 145 145 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 9 9 CDK7 binding. {ECO:0000250}.
SITE 88 89 CDK7 binding. {ECO:0000250}.
SITE 166 166 CDK7 binding. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P24941}.
MOD_RES 6 6 N6-acetyllysine.
{ECO:0000250|UniProtKB:P24941}.
MOD_RES 14 14 Phosphothreonine.
{ECO:0000250|UniProtKB:P24941}.
MOD_RES 15 15 Phosphotyrosine; by WEE1.
{ECO:0000269|PubMed:11585773}.
MOD_RES 19 19 Phosphotyrosine.
{ECO:0000250|UniProtKB:P24941}.
MOD_RES 160 160 Phosphothreonine; by CAK and CCRK.
{ECO:0000250|UniProtKB:P24941}.
MOD_RES 218 218 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 197 244 Missing (in isoform CDK2-alpha).
{ECO:0000303|Ref.1}.
/FTId=VSP_004800.
MUTAGEN 15 15 Y->F: Loss of tyrosine phosphorylation by
WEE1 and CABLES1.
{ECO:0000269|PubMed:11585773}.
SEQUENCE 346 AA; 38978 MW; D806BC2F150AEDFC CRC64;
MENFQKVEKI GEGTYGVVYK AKNKLTGEVV ALKKIRLDTE TEGVPSTAIR EISLLKELNH
PNIVKLLDVI HTENKLYLVF EFLHQDLKKF MDASALTGIP LPLIKSYLFQ LLQGLAFCHS
HRVLHRDLKP QNLLINAEGS IKLADFGLAR AFGVPVRTYT HEVVTLWYRA PEILLGCKYY
STAVDIWSLG CIFAEMHLVC TQHHAKCCGE HRRNGRHSLC PLCSYLEVAA SQGGGMTAVS
APHPVTRRAL FPGDSEIDQL FRIFRTLGTP DEVVWPGVTS MPDYKPSFPK WARQDFSKVV
PPLDEDGRSL LSQMLHYDPN KRISAKAALA HPFFQDVTKP VPHLRL


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EIAAB06505 Cdc2l5,CDC2-related protein kinase 5,Cdk13,Cell division cycle 2-like protein kinase 5,Cell division protein kinase 13,Cyclin-dependent kinase 13,Kiaa1791,Mouse,Mus musculus
EIAAB06521 Cdc2l6,CDC2-related protein kinase 6,Cdk19,Cell division cycle 2-like protein kinase 6,Cell division protein kinase 19,Cyclin-dependent kinase 19,Kiaa1028,Mouse,Mus musculus
EIAAB06500 Cdc2l1,Cdk11,Cell division cycle 2-like protein kinase 1,Cell division protein kinase 11,Cyclin-dependent kinase 11,Galactosyltransferase-associated protein kinase p58_GTA,Mouse,Mus musculus,PITSLRE s
EIAAB06264 CDC2L1,CDK11,CDK11B,Cell division cycle 2-like protein kinase 1,Cell division protein kinase 11B,CLK-1,Cyclin-dependent kinase 11B,Galactosyltransferase-associated protein kinase p58_GTA,Homo sapiens,
EIAAB06499 Cdc2l1,Cdk11,Cell division cycle 2-like protein kinase 1,Cell division protein kinase 11,Cyclin-dependent kinase 11,Galactosyltransferase-associated protein kinase p58_GTA,PITSLRE serine_threonine-pro
EIAAB06507 CDC2L,CDC2L5,CDC2-related protein kinase 5,CDK13,Cell division cycle 2-like protein kinase 5,Cell division protein kinase 13,CHED,Cholinesterase-related cell division controller,Cyclin-dependent kinas
18-003-44328 Cell division protein kinase 9 - EC 2.7.11.22; EC 2.7.11.23; Cyclin-dependent kinase 9; Serine_threonine-protein kinase PITALRE; C-2K; Cell division cycle 2-like protein kinase 4 Polyclonal 0.1 mg Protein A
U1888h CLIA kit CDC2,CDC28A,CDK1,CDK1,CDKN1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Homo sapiens,Human,p34 protein kinase,P34CDC2 96T
U1888h CLIA CDC2,CDC28A,CDK1,CDK1,CDKN1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Homo sapiens,Human,p34 protein kinase,P34CDC2 96T
E1888h ELISA CDC2,CDC28A,CDK1,CDK1,CDKN1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Homo sapiens,Human,p34 protein kinase,P34CDC2 96T
E1888h ELISA kit CDC2,CDC28A,CDK1,CDK1,CDKN1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Homo sapiens,Human,p34 protein kinase,P34CDC2 96T
U1888m CLIA kit Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Mouse,Mus musculus,p34 protein kinase 96T
E1888m ELISA Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Mouse,Mus musculus,p34 protein kinase 96T
U1888m CLIA Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Mouse,Mus musculus,p34 protein kinase 96T
E1888r ELISA Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,p34 protein kinase,Rat,Rattus norvegicus 96T
U1888r CLIA Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,p34 protein kinase,Rat,Rattus norvegicus 96T
E1888r ELISA kit Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,p34 protein kinase,Rat,Rattus norvegicus 96T
U1888r CLIA kit Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,p34 protein kinase,Rat,Rattus norvegicus 96T
E1888m ELISA kit Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Mouse,Mus musculus,p34 protein kinase 96T


 

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