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Cyclin-dependent kinase 11B (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 1) (CLK-1) (Cell division protein kinase 11B) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1) (p58 CLK-1)

 CD11B_HUMAN             Reviewed;         795 AA.
P21127; B7ZVY7; J3KTL7; J3QR29; J3QR44; O95265; Q12817; Q12818; Q12819;
Q12820; Q12822; Q8N530; Q9NZS5; Q9UBJ0; Q9UBQ1; Q9UBR0; Q9UNY2; Q9UP57;
Q9UP58; Q9UP59;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 4.
12-AUG-2020, entry version 219.
RecName: Full=Cyclin-dependent kinase 11B;
EC=2.7.11.22;
AltName: Full=Cell division cycle 2-like protein kinase 1;
Short=CLK-1;
AltName: Full=Cell division protein kinase 11B;
AltName: Full=Galactosyltransferase-associated protein kinase p58/GTA;
AltName: Full=PITSLRE serine/threonine-protein kinase CDC2L1;
AltName: Full=p58 CLK-1;
Name=CDK11B; Synonyms=CDC2L1, CDK11, PITSLREA, PK58;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), AND FUNCTION.
TISSUE=Liver;
PubMed=2217177; DOI=10.1073/pnas.87.19.7467;
Bunnell B.A., Heath L.S., Adams D.E., Lahti J.M., Kidd V.J.;
"Increased expression of a 58-kDa protein kinase leads to changes in the
CHO cell cycle.";
Proc. Natl. Acad. Sci. U.S.A. 87:7467-7471(1990).
[2]
ERRATUM OF PUBMED:2217177, AND SEQUENCE REVISION.
PubMed=2006197; DOI=10.1073/pnas.88.6.2612d;
Bunnell B.A., Heath L.S., Adams D.E., Lahti J.M., Kidd V.J.;
Proc. Natl. Acad. Sci. U.S.A. 88:2612-2612(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 7), AND VARIANT GLN-601.
TISSUE=Hematopoietic;
PubMed=1639388; DOI=10.1016/0888-7543(92)90132-c;
Eipers P.G., Lahti J.M., Kidd V.J.;
"Structure and expression of the human p58clk-1 protein kinase chromosomal
gene.";
Genomics 13:613-621(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SV1; 2; 3; 8 AND SV11), VARIANT
CYS-57, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
TISSUE=Cervix carcinoma;
PubMed=8195233;
Xiang J., Lahti J.M., Grenet J.A., Easton J.B., Kidd V.J.;
"Molecular cloning and expression of alternatively spliced PITSLRE protein
kinase isoforms.";
J. Biol. Chem. 269:15786-15794(1994).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS SV1; SV4; SV5; SV9; SV10
AND SV11), AND TISSUE SPECIFICITY.
TISSUE=Cervix carcinoma;
PubMed=9750192; DOI=10.1101/gr.8.9.929;
Gururajan R., Lahti J.M., Grenet J.A., Easton J., Gruber I., Ambros P.F.,
Kidd V.J.;
"Duplication of a genomic region containing the Cdc2L1-2 and MMP21-22 genes
on human chromosome 1p36.3 and their linkage to D1Z2.";
Genome Res. 8:929-939(1998).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SV11).
TISSUE=Placenta;
Govindan M.V., Warriar N.;
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SV1).
TISSUE=Brain;
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).
[9]
INTERACTION WITH RNPS1.
PubMed=9580558;
Loyer P., Trembley J.H., Lahti J.M., Kidd V.J.;
"The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-
related PITSLRE protein kinases in vivo.";
J. Cell Sci. 111:1495-1506(1998).
[10]
ALTERNATIVE INITIATION (ISOFORM 7), AND INDUCTION.
PubMed=10882096; DOI=10.1016/s1097-2765(00)80239-7;
Cornelis S., Bruynooghe Y., Denecker G., Van Huffel S., Tinton S.,
Beyaert R.;
"Identification and characterization of a novel cell cycle-regulated
internal ribosome entry site.";
Mol. Cell 5:597-605(2000).
[11]
INTERACTION WITH RANBP9, AUTOPHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=14511641; DOI=10.1016/j.bbrc.2003.08.116;
Mikolajczyk M., Shi J., Vaillancourt R.R., Sachs N.A., Nelson M.;
"The cyclin-dependent kinase 11(p46) isoform interacts with RanBPM.";
Biochem. Biophys. Res. Commun. 310:14-18(2003).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CCNL1 AND SFRS7.
PubMed=12501247; DOI=10.1074/jbc.m210057200;
Hu D., Mayeda A., Trembley J.H., Lahti J.M., Kidd V.J.;
"CDK11 complexes promote pre-mRNA splicing.";
J. Biol. Chem. 278:8623-8629(2003).
[13]
FUNCTION, AND INTERACTION WITH PAK1.
PubMed=12624090; DOI=10.1074/jbc.m300818200;
Chen S., Yin X., Zhu X., Yan J., Ji S., Chen C., Cai M., Zhang S., Zong H.,
Hu Y., Yuan Z., Shen Z., Gu J.;
"The C-terminal kinase domain of the p34cdc2-related PITSLRE protein kinase
(p110C) associates with p21-activated kinase 1 and inhibits its activity
during anoikis.";
J. Biol. Chem. 278:20029-20036(2003).
[14]
PHOSPHORYLATION AT SER-115.
PubMed=15883043; DOI=10.1016/j.bbrc.2005.04.078;
Feng Y., Qi W., Martinez J., Nelson M.A.;
"The cyclin-dependent kinase 11 interacts with 14-3-3 proteins.";
Biochem. Biophys. Res. Commun. 331:1503-1509(2005).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling
networks.";
Cell 127:635-648(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-595, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation
analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[17]
PHOSPHORYLATION AT SER-482 AND THR-488 BY CDK7.
PubMed=16327805; DOI=10.1038/nsmb1028;
Larochelle S., Batliner J., Gamble M.J., Barboza N.M., Kraybill B.C.,
Blethrow J.D., Shokat K.M., Fisher R.P.;
"Dichotomous but stringent substrate selection by the dual-function Cdk7
complex revealed by chemical genetics.";
Nat. Struct. Mol. Biol. 13:55-62(2006).
[18]
FUNCTION, AND INTERACTION WITH CCNL1 AND CCNL2.
PubMed=18216018; DOI=10.1074/jbc.m708188200;
Loyer P., Trembley J.H., Grenet J.A., Busson A., Corlu A., Zhao W.,
Kocak M., Kidd V.J., Lahti J.M.;
"Characterization of cyclin L1 and L2 interactions with CDK11 and splicing
factors: influence of cyclin L isoforms on splice site selection.";
J. Biol. Chem. 283:7721-7732(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-594 AND THR-595, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589 AND THR-595, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-595, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-595, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-595, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
INTERACTION WITH MYO18A.
PubMed=25965346; DOI=10.1371/journal.pone.0126576;
Yang L., Carrillo M., Wu Y.M., DiAngelo S.L., Silveyra P., Umstead T.M.,
Halstead E.S., Davies M.L., Hu S., Floros J., McCormack F.X.,
Christensen N.D., Chroneos Z.C.;
"SP-R210 (Myo18A) isoforms as intrinsic modulators of macrophage priming
and activation.";
PLoS ONE 10:E0126576-E0126576(2015).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-641, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[28]
VARIANTS [LARGE SCALE ANALYSIS] CYS-57; TRP-201; LEU-414; ALA-452; VAL-463;
SER-506; GLN-601; ASN-641 AND VAL-670.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Plays multiple roles in cell cycle progression, cytokinesis
and apoptosis. Involved in pre-mRNA splicing in a kinase activity-
dependent manner. Isoform 7 may act as a negative regulator of normal
cell cycle progression. {ECO:0000269|PubMed:12501247,
ECO:0000269|PubMed:12624090, ECO:0000269|PubMed:18216018,
ECO:0000269|PubMed:2217177}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.22;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ACTIVITY REGULATION: Phosphorylation at Thr-448 or Tyr-449 inactivates
the enzyme, while phosphorylation at Thr-595 activates it.
{ECO:0000250}.
-!- SUBUNIT: Cleaved isoform SV9 (p110C) binds to the serine/threonine
kinase PAK1 and RANBP9. p110C interacts with RNPS1. Isoform 7, but not
isoform SV9, nor its cleavage product p110C, interacts with CCND3.
Interacts with CCNL1 and CCNL2. Forms complexes with pre-mRNA-splicing
factors, including at least SRSF1, SRSF2 AND SRSF7/SLU7. Interacts with
isoform 5 of MYO18A (PubMed:25965346). {ECO:0000269|PubMed:12501247,
ECO:0000269|PubMed:12624090, ECO:0000269|PubMed:14511641,
ECO:0000269|PubMed:25965346, ECO:0000269|PubMed:9580558}.
-!- INTERACTION:
P21127; O00303: EIF3F; NbExp=3; IntAct=EBI-1298, EBI-711990;
P21127; Q13153: PAK1; NbExp=4; IntAct=EBI-1298, EBI-1307;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=10;
Name=SV9; Synonyms=CDK11-p110;
IsoId=P21127-1; Sequence=Displayed;
Name=SV1; Synonyms=Alpha 2-1;
IsoId=P21127-2; Sequence=VSP_008280;
Name=2; Synonyms=Alpha 2-2;
IsoId=P21127-3; Sequence=VSP_008278, VSP_008279, VSP_008280;
Name=3; Synonyms=Alpha 1;
IsoId=P21127-4; Sequence=VSP_008276;
Name=SV4;
IsoId=P21127-5; Sequence=VSP_008275;
Name=SV5;
IsoId=P21127-6; Sequence=VSP_008273, VSP_008277, VSP_008278,
VSP_008280;
Name=8; Synonyms=Alpha 2-3;
IsoId=P21127-8; Sequence=VSP_008278, VSP_008280;
Name=SV10;
IsoId=P21127-9; Sequence=VSP_008273, VSP_008277, VSP_008280;
Name=SV11; Synonyms=Alpha 2-4;
IsoId=P21127-10; Sequence=VSP_008274, VSP_008280;
Name=7; Synonyms=CDK11-p58;
IsoId=P21127-12; Sequence=VSP_018834;
-!- TISSUE SPECIFICITY: Expressed ubiquitously. Some evidence of isoform-
specific tissue distribution. {ECO:0000269|PubMed:8195233,
ECO:0000269|PubMed:9750192}.
-!- INDUCTION: Isoform 7 is induced in G2/M phase of the cell cycle.
{ECO:0000269|PubMed:10882096}.
-!- PTM: During FAS- or TNF-induced apoptosis, isoform SV9 is cleaved by
caspases to produce p110C, a fragment that contains the C-terminal
kinase domain.
-!- PTM: Phosphorylation at Ser-115 creates a binding site for 14-3-3
proteins. p110C can be autophosphorylated.
{ECO:0000269|PubMed:15883043, ECO:0000269|PubMed:16327805}.
-!- MISCELLANEOUS: Duplicated gene. CDK11A and CDK11B encode almost
identical protein kinases of 110 kDa that contain at their C-termini
the open reading frame of a smaller 58 kDa isoform which is expressed
following IRES-mediated alternative initiation of translation.
-!- MISCELLANEOUS: [Isoform 7]: Produced by alternative initiation at Met-
357 of isoform SV9 via an internal ribosomal entry site (IRES).
{ECO:0000305}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
-!- CAUTION: Many references talk about 'p110 isoforms' but it is not yet
known if this refers to CDK11A and/or CDK11B or one/some of the
isoforms of each. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB59449.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAC83664.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAF36538.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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EMBL; M37712; AAA36406.1; -; mRNA.
EMBL; M88563; AAB59449.1; ALT_SEQ; Genomic_DNA.
EMBL; M88553; AAB59449.1; JOINED; Genomic_DNA.
EMBL; M88554; AAB59449.1; JOINED; Genomic_DNA.
EMBL; M88555; AAB59449.1; JOINED; Genomic_DNA.
EMBL; M88558; AAB59449.1; JOINED; Genomic_DNA.
EMBL; M88559; AAB59449.1; JOINED; Genomic_DNA.
EMBL; M88560; AAB59449.1; JOINED; Genomic_DNA.
EMBL; M88561; AAB59449.1; JOINED; Genomic_DNA.
EMBL; M88562; AAB59449.1; JOINED; Genomic_DNA.
EMBL; U04815; AAA19581.1; -; mRNA.
EMBL; U04816; AAA19582.1; -; mRNA.
EMBL; U04817; AAA19583.1; -; mRNA.
EMBL; U04818; AAA19584.1; -; mRNA.
EMBL; U04824; AAA19586.1; -; mRNA.
EMBL; AF067512; AAC72077.1; -; mRNA.
EMBL; AF067513; AAC72078.1; -; mRNA.
EMBL; AF067514; AAC72079.1; -; mRNA.
EMBL; AF067515; AAC72080.1; -; mRNA.
EMBL; AF067516; AAC72081.1; -; mRNA.
EMBL; AF067517; AAC72082.1; -; mRNA.
EMBL; AF080683; AAC83662.1; -; Genomic_DNA.
EMBL; AF080685; AAC83662.1; JOINED; Genomic_DNA.
EMBL; AF080686; AAC83662.1; JOINED; Genomic_DNA.
EMBL; AF080687; AAC83662.1; JOINED; Genomic_DNA.
EMBL; AF080688; AAC83662.1; JOINED; Genomic_DNA.
EMBL; AF092429; AAC83662.1; JOINED; Genomic_DNA.
EMBL; AF092430; AAC83662.1; JOINED; Genomic_DNA.
EMBL; AF080678; AAC83662.1; JOINED; Genomic_DNA.
EMBL; AF080679; AAC83662.1; JOINED; Genomic_DNA.
EMBL; AF080680; AAC83662.1; JOINED; Genomic_DNA.
EMBL; AF080681; AAC83662.1; JOINED; Genomic_DNA.
EMBL; AF080682; AAC83662.1; JOINED; Genomic_DNA.
EMBL; AF080683; AAC83663.1; -; Genomic_DNA.
EMBL; AF080685; AAC83663.1; JOINED; Genomic_DNA.
EMBL; AF080686; AAC83663.1; JOINED; Genomic_DNA.
EMBL; AF080687; AAC83663.1; JOINED; Genomic_DNA.
EMBL; AF080688; AAC83663.1; JOINED; Genomic_DNA.
EMBL; AF092429; AAC83663.1; JOINED; Genomic_DNA.
EMBL; AF092430; AAC83663.1; JOINED; Genomic_DNA.
EMBL; AF080678; AAC83663.1; JOINED; Genomic_DNA.
EMBL; AF080679; AAC83663.1; JOINED; Genomic_DNA.
EMBL; AF080680; AAC83663.1; JOINED; Genomic_DNA.
EMBL; AF080681; AAC83663.1; JOINED; Genomic_DNA.
EMBL; AF080682; AAC83663.1; JOINED; Genomic_DNA.
EMBL; AF080683; AAC83664.1; ALT_SEQ; Genomic_DNA.
EMBL; AF080685; AAC83664.1; JOINED; Genomic_DNA.
EMBL; AF080686; AAC83664.1; JOINED; Genomic_DNA.
EMBL; AF080687; AAC83664.1; JOINED; Genomic_DNA.
EMBL; AF080688; AAC83664.1; JOINED; Genomic_DNA.
EMBL; AF092429; AAC83664.1; JOINED; Genomic_DNA.
EMBL; AF092430; AAC83664.1; JOINED; Genomic_DNA.
EMBL; AF080678; AAC83664.1; JOINED; Genomic_DNA.
EMBL; AF080679; AAC83664.1; JOINED; Genomic_DNA.
EMBL; AF080680; AAC83664.1; JOINED; Genomic_DNA.
EMBL; AF080681; AAC83664.1; JOINED; Genomic_DNA.
EMBL; AF080682; AAC83664.1; JOINED; Genomic_DNA.
EMBL; AF080683; AAC83665.1; -; Genomic_DNA.
EMBL; AF080685; AAC83665.1; JOINED; Genomic_DNA.
EMBL; AF080686; AAC83665.1; JOINED; Genomic_DNA.
EMBL; AF080687; AAC83665.1; JOINED; Genomic_DNA.
EMBL; AF080688; AAC83665.1; JOINED; Genomic_DNA.
EMBL; AF092429; AAC83665.1; JOINED; Genomic_DNA.
EMBL; AF092430; AAC83665.1; JOINED; Genomic_DNA.
EMBL; AF080678; AAC83665.1; JOINED; Genomic_DNA.
EMBL; AF080679; AAC83665.1; JOINED; Genomic_DNA.
EMBL; AF080680; AAC83665.1; JOINED; Genomic_DNA.
EMBL; AF080681; AAC83665.1; JOINED; Genomic_DNA.
EMBL; AF080682; AAC83665.1; JOINED; Genomic_DNA.
EMBL; AF080683; AAC83666.1; -; Genomic_DNA.
EMBL; AF092430; AAC83666.1; JOINED; Genomic_DNA.
EMBL; AF080678; AAC83666.1; JOINED; Genomic_DNA.
EMBL; AF080679; AAC83666.1; JOINED; Genomic_DNA.
EMBL; AF080680; AAC83666.1; JOINED; Genomic_DNA.
EMBL; AF080681; AAC83666.1; JOINED; Genomic_DNA.
EMBL; AF080682; AAC83666.1; JOINED; Genomic_DNA.
EMBL; AF174497; AAF36538.1; ALT_INIT; mRNA.
EMBL; FO704657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC140714; AAI40715.1; -; mRNA.
EMBL; BC171773; AAI71773.1; -; mRNA.
CCDS; CCDS72682.1; -. [P21127-9]
CCDS; CCDS72683.1; -. [P21127-1]
CCDS; CCDS72684.1; -. [P21127-2]
PIR; A38282; A38282.
PIR; B54024; B54024.
PIR; E54024; E54024.
PIR; F54024; F54024.
PIR; H54024; H54024.
PIR; T09568; T09568.
RefSeq; NP_001278274.1; NM_001291345.1. [P21127-8]
RefSeq; NP_001778.2; NM_001787.2. [P21127-1]
RefSeq; NP_277021.2; NM_033486.2. [P21127-2]
RefSeq; NP_277022.1; NM_033487.2. [P21127-5]
RefSeq; NP_277024.2; NM_033489.2. [P21127-9]
RefSeq; NP_277025.1; NM_033490.2. [P21127-10]
RefSeq; XP_016858415.1; XM_017002926.1. [P21127-3]
SMR; P21127; -.
BioGRID; 107421; 61.
ComplexPortal; CPX-345; Cyclin L2-CDK11B(p58) complex. [P21127-12]
ComplexPortal; CPX-346; Cyclin L1-CDK11B(p58) complex. [P21127-12]
ComplexPortal; CPX-348; Cyclin L1-CDK11B(p110) complex. [P21127-1]
ComplexPortal; CPX-349; Cyclin L2-CDK11B(p110) complex. [P21127-1]
CORUM; P21127; -.
IntAct; P21127; 28.
MINT; P21127; -.
STRING; 9606.ENSP00000464036; -.
BindingDB; P21127; -.
ChEMBL; CHEMBL5808; -.
DrugCentral; P21127; -.
iPTMnet; P21127; -.
PhosphoSitePlus; P21127; -.
BioMuta; CDK11B; -.
DMDM; 34978359; -.
EPD; P21127; -.
jPOST; P21127; -.
MassIVE; P21127; -.
PaxDb; P21127; -.
PeptideAtlas; P21127; -.
PRIDE; P21127; -.
ProteomicsDB; 53836; -. [P21127-1]
ProteomicsDB; 53837; -. [P21127-10]
ProteomicsDB; 53838; -. [P21127-12]
ProteomicsDB; 53839; -. [P21127-2]
ProteomicsDB; 53840; -. [P21127-3]
ProteomicsDB; 53841; -. [P21127-4]
ProteomicsDB; 53842; -. [P21127-5]
ProteomicsDB; 53843; -. [P21127-6]
ProteomicsDB; 53844; -. [P21127-8]
ProteomicsDB; 53845; -. [P21127-9]
Antibodypedia; 62301; 104 antibodies.
DNASU; 984; -.
Ensembl; ENST00000340677; ENSP00000464016; ENSG00000248333. [P21127-9]
Ensembl; ENST00000341832; ENSP00000463048; ENSG00000248333. [P21127-2]
Ensembl; ENST00000407249; ENSP00000464036; ENSG00000248333. [P21127-1]
GeneID; 984; -.
KEGG; hsa:984; -.
UCSC; uc031tmi.2; human.
CTD; 984; -.
DisGeNET; 984; -.
EuPathDB; HostDB:ENSG00000248333.8; -.
GeneCards; CDK11B; -.
HGNC; HGNC:1729; CDK11B.
MIM; 176873; gene.
neXtProt; NX_P21127; -.
OpenTargets; ENSG00000248333; -.
PharmGKB; PA26262; -.
eggNOG; KOG0663; Eukaryota.
GeneTree; ENSGT00940000158459; -.
InParanoid; P21127; -.
KO; K08818; -.
OMA; HMRKCSI; -.
OrthoDB; 925637at2759; -.
PhylomeDB; P21127; -.
TreeFam; TF101035; -.
BRENDA; 2.7.11.22; 2681.
PathwayCommons; P21127; -.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
SignaLink; P21127; -.
SIGNOR; P21127; -.
BioGRID-ORCS; 984; 35 hits in 131 CRISPR screens.
ChiTaRS; CDK11B; human.
GeneWiki; CDC2L1; -.
GenomeRNAi; 984; -.
Pharos; P21127; Tchem.
PRO; PR:P21127; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; P21127; protein.
Bgee; ENSG00000248333; Expressed in sural nerve and 113 other tissues.
ExpressionAtlas; P21127; baseline and differential.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; NAS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; IEP:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0050684; P:regulation of mRNA processing; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative initiation; Alternative splicing; Apoptosis; ATP-binding;
Cell cycle; Cytoplasm; Isopeptide bond; Kinase; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
CHAIN 1..795
/note="Cyclin-dependent kinase 11B"
/id="PRO_0000024311"
DOMAIN 438..723
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 444..452
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
COMPBIAS 126..393
/note="Glu-rich"
ACT_SITE 562
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027"
BINDING 467
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 47
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P24788"
MOD_RES 72
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P24788"
MOD_RES 115
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:15883043"
MOD_RES 283
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P24788"
MOD_RES 482
/note="Phosphoserine; by CDK7"
/evidence="ECO:0000269|PubMed:16327805"
MOD_RES 488
/note="Phosphothreonine; by CDK7"
/evidence="ECO:0000269|PubMed:16327805"
MOD_RES 589
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332"
MOD_RES 594
/note="Phosphotyrosine"
/evidence="ECO:0000244|PubMed:18669648"
MOD_RES 595
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163"
MOD_RES 751
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P24788"
MOD_RES 752
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P24788"
CROSSLNK 641
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
VAR_SEQ 1..356
/note="Missing (in isoform 7)"
/evidence="ECO:0000303|PubMed:2217177"
/id="VSP_018834"
VAR_SEQ 1..269
/note="Missing (in isoform SV4)"
/evidence="ECO:0000303|PubMed:9750192"
/id="VSP_008275"
VAR_SEQ 1..217
/note="Missing (in isoform SV11)"
/evidence="ECO:0000303|PubMed:8195233,
ECO:0000303|PubMed:9750192, ECO:0000303|Ref.6"
/id="VSP_008274"
VAR_SEQ 1..34
/note="Missing (in isoform SV5 and isoform SV10)"
/evidence="ECO:0000303|PubMed:16710414,
ECO:0000303|PubMed:9750192"
/id="VSP_008273"
VAR_SEQ 2..335
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:8195233"
/id="VSP_008276"
VAR_SEQ 35..37
/note="LKN -> MSQ (in isoform SV5 and isoform SV10)"
/evidence="ECO:0000303|PubMed:9750192"
/id="VSP_008277"
VAR_SEQ 110..119
/note="Missing (in isoform 2, isoform SV5 and isoform 8)"
/evidence="ECO:0000303|PubMed:8195233,
ECO:0000303|PubMed:9750192"
/id="VSP_008278"
VAR_SEQ 165
/note="R -> RGNDGVCLFR (in isoform 2)"
/evidence="ECO:0000303|PubMed:8195233"
/id="VSP_008279"
VAR_SEQ 252..265
/note="GEARPAPAQKPAQL -> V (in isoform SV1, isoform 2,
isoform SV5, isoform 8, isoform SV10 and isoform SV11)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16710414, ECO:0000303|PubMed:8195233,
ECO:0000303|PubMed:9750192, ECO:0000303|Ref.6"
/id="VSP_008280"
VARIANT 57
/note="R -> C (in dbSNP:rs752740049)"
/evidence="ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:8195233"
/id="VAR_041958"
VARIANT 93
/note="R -> W (in dbSNP:rs1059831)"
/id="VAR_057775"
VARIANT 109
/note="R -> C (in dbSNP:rs1059830)"
/id="VAR_062199"
VARIANT 201
/note="R -> W"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041959"
VARIANT 414
/note="S -> L (in dbSNP:rs1241694892)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041960"
VARIANT 452
/note="V -> A"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_045577"
VARIANT 463
/note="I -> V"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041961"
VARIANT 506
/note="G -> S"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_045578"
VARIANT 601
/note="L -> Q (in dbSNP:rs200190129)"
/evidence="ECO:0000269|PubMed:1639388,
ECO:0000269|PubMed:17344846"
/id="VAR_041962"
VARIANT 641
/note="K -> N (in dbSNP:rs1059815)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041963"
VARIANT 670
/note="A -> V (in dbSNP:rs1059811)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041964"
CONFLICT 97
/note="A -> V (in Ref. 4; AAA19582/AAA19583/AAA19586 and 5;
AAC72077/AAC72079/AAC72080/AAC72081/AAC83662/AAC83664/
AAC83665)"
CONFLICT 109
/note="Missing (in Ref. 4; AAA19582/AAA19583 and 5;
AAC72079)"
/evidence="ECO:0000305"
CONFLICT 126
/note="E -> K (in Ref. 4; AAA19582/AAA19583/AAA19586)"
/evidence="ECO:0000305"
CONFLICT 258
/note="P -> R (in Ref. 5; AAC72080)"
CONFLICT 320
/note="S -> T (in Ref. 6; AAF36538)"
/evidence="ECO:0000305"
CONFLICT 324..326
/note="Missing (in Ref. 4; AAA19582/AAA19583/AAA19584/
AAA19586 and 6; AAF36538)"
/evidence="ECO:0000305"
CONFLICT 411..412
/note="PA -> LP (in Ref. 3; AAB59449)"
/evidence="ECO:0000305"
CONFLICT 436
/note="E -> D (in Ref. 3; AAB59449)"
/evidence="ECO:0000305"
CONFLICT 560
/note="H -> Q (in Ref. 6; AAF36538)"
/evidence="ECO:0000305"
CONFLICT 567
/note="N -> T (in Ref. 6; AAF36538)"
/evidence="ECO:0000305"
CONFLICT 678
/note="E -> R (in Ref. 4; AAA19582/AAA19581/AAA19583/
AAA19584 and 6; AAF36538)"
/evidence="ECO:0000305"
CONFLICT 694
/note="D -> E (in Ref. 3; AAB59449)"
/evidence="ECO:0000305"
CONFLICT 697
/note="F -> C (in Ref. 6; AAF36538)"
/evidence="ECO:0000305"
CONFLICT 712
/note="I -> L (in Ref. 3; AAB59449)"
/evidence="ECO:0000305"
CONFLICT 715
/note="E -> Q (in Ref. 3; AAB59449)"
/evidence="ECO:0000305"
CONFLICT 792
/note="S -> R (in Ref. 6; AAF36538)"
/evidence="ECO:0000305"
SEQUENCE 795 AA; 92620 MW; 8CCB0E688E66DF47 CRC64;
MGDEKDSWKV KTLDEILQEK KRRKEQEEKA EIKRLKNSDD RDSKRDSLEE GELRDHRMEI
TIRNSPYRRE DSMEDRGEED DSLAIKPPQQ MSRKEKAHHR KDEKRKEKRR HRSHSAEGGK
HARVKEKERE HERRKRHREE QDKARREWER QKRREMAREH SRRERDRLEQ LERKRERERK
MREQQKEQRE QKERERRAEE RRKEREARRE VSAHHRTMRE DYSDKVKASH WSRSPPRPPR
ERFELGDGRK PGEARPAPAQ KPAQLKEEKM EERDLLSDLQ DISDSERKTS SAESSSAESG
SGSEEEEEEE EEEEEEGSTS EESEEEEEEE EEEEEETGSN SEEASEQSAE EVSEEEMSED
EERENENHLL VVPESRFDRD SGESEEAEEE VGEGTPQSSA LTEGDYVPDS PALSPIELKQ
ELPKYLPALQ GCRSVEEFQC LNRIEEGTYG VVYRAKDKKT DEIVALKRLK MEKEKEGFPI
TSLREINTIL KAQHPNIVTV REIVVGSNMD KIYIVMNYVE HDLKSLMETM KQPFLPGEVK
TLMIQLLRGV KHLHDNWILH RDLKTSNLLL SHAGILKVGD FGLAREYGSP LKAYTPVVVT
LWYRAPELLL GAKEYSTAVD MWSVGCIFGE LLTQKPLFPG KSEIDQINKV FKDLGTPSEK
IWPGYSELPA VKKMTFSEHP YNNLRKRFGA LLSDQGFDLM NKFLTYFPGR RISAEDGLKH
EYFRETPLPI DPSMFPTWPA KSEQQRVKRG TSPRPPEGGL GYSQLGDDDL KETGFHLTTT
NQGASAAGPG FSLKF


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WP1659: Glycine, serine and threonine metabolism
WP1681: Pantothenate and CoA biosynthesis
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP2199: Seed Development
WP253: Glycolysis
WP1703: Streptomycin biosynthesis
WP414: Cell Cycle and Cell Division
WP1678: Nucleotide excision repair
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP1701: Starch and sucrose metabolism
WP1567: Glycolysis and Gluconeogenesis
WP1672: Mismatch repair
WP1676: Non-homologous end-joining
WP32: Translation Factors
WP1625: Base excision repair
WP1653: Galactose metabolism
WP1844: MAP kinase cascade
WP1566: Citrate cycle (TCA cycle)
WP1675: Nitrogen metabolism
WP2324: AGE/RAGE pathway
WP1613: 1,4-Dichlorobenzene degradation
WP1371: G Protein Signaling Pathways

Related Genes :
[CDK11B CDC2L1 CDK11 PITSLREA PK58] Cyclin-dependent kinase 11B (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 1) (CLK-1) (Cell division protein kinase 11B) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1) (p58 CLK-1)
[Cdk11b Cdc2l1 Cdk11] Cyclin-dependent kinase 11B (Cell division cycle 2-like protein kinase 1) (Cell division protein kinase 11) (Cyclin-dependent kinase 11) (EC 2.7.11.22) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1)
[CDK11A CDC2L2 CDC2L3 PITSLREB] Cyclin-dependent kinase 11A (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 2) (Cell division protein kinase 11A) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L2)
[cdc2 cdk1 swo2 pi002 SPBC11B10.09] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 2) (Cell division protein kinase 1) (p34 protein kinase)
[CDK7 CAK CAK1 CDKN7 MO15 STK1] Cyclin-dependent kinase 7 (EC 2.7.11.22) (EC 2.7.11.23) (39 kDa protein kinase) (p39 Mo15) (CDK-activating kinase 1) (Cell division protein kinase 7) (Serine/threonine-protein kinase 1) (TFIIH basal transcription factor complex kinase subunit)
[CDK9 CDC2L4 TAK] Cyclin-dependent kinase 9 (EC 2.7.11.22) (EC 2.7.11.23) (C-2K) (Cell division cycle 2-like protein kinase 4) (Cell division protein kinase 9) (Serine/threonine-protein kinase PITALRE) (Tat-associated kinase complex catalytic subunit)
[Cdk7 Cak Cak1 Mo15] Cyclin-dependent kinase 7 (EC 2.7.11.22) (EC 2.7.11.23) (39 protein kinase) (P39 Mo15) (CDK-activating kinase 1) (Cell division protein kinase 7) (TFIIH basal transcription factor complex kinase subunit) (Fragment)
[Cdk7 Cak Cdkn7 Crk4 Mo15 Mpk-7] Cyclin-dependent kinase 7 (EC 2.7.11.22) (EC 2.7.11.23) (39 kDa protein kinase) (P39 Mo15) (CDK-activating kinase) (CR4 protein kinase) (CRK4) (Cell division protein kinase 7) (Protein-tyrosine kinase MPK-7) (TFIIH basal transcription factor complex kinase subunit)
[PAK2] Serine/threonine-protein kinase PAK 2 (EC 2.7.11.1) (Gamma-PAK) (PAK65) (S6/H4 kinase) (p21-activated kinase 2) (PAK-2) (p58) [Cleaved into: PAK-2p27 (p27); PAK-2p34 (p34) (C-t-PAK2)]
[cdk1-b cdc2 cdc2x1.2] Cyclin-dependent kinase 1-B (CDK1-B) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog 2) (Cell division control protein 2-B) (Cell division protein kinase 1) (p34 protein kinase 2)
[CDK13 CDC2L CDC2L5 CHED KIAA1791] Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 2.7.11.23) (CDC2-related protein kinase 5) (Cell division cycle 2-like protein kinase 5) (Cell division protein kinase 13) (hCDK13) (Cholinesterase-related cell division controller)
[cdk1-a cdc2-a cdc2x1.1] Cyclin-dependent kinase 1-A (CDK1-A) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog 1) (Cell division control protein 2-A) (Cell division protein kinase 1-A) (p34 protein kinase 1)
[CDK1 CDC2 CDC28A CDKN1 P34CDC2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDK5 CDKN5] Cyclin-dependent-like kinase 5 (EC 2.7.11.1) (Cell division protein kinase 5) (Serine/threonine-protein kinase PSSALRE) (Tau protein kinase II catalytic subunit) (TPKII catalytic subunit)
[Cdk5 Cdkn5 Crk6] Cyclin-dependent-like kinase 5 (EC 2.7.11.1) (CR6 protein kinase) (CRK6) (Cell division protein kinase 5) (Serine/threonine-protein kinase PSSALRE) (Tau protein kinase II catalytic subunit) (TPKII catalytic subunit)
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[Cdk1 cdc2 CG5363] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDK1 CDC2 CDKN1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDK5 CDKN5] Cyclin-dependent-like kinase 5 (EC 2.7.11.1) (Cell division protein kinase 5) (Proline-directed protein kinase 33 kDa subunit) (PDPK) (Serine/threonine-protein kinase PSSALRE) (Tau protein kinase II catalytic subunit) (TPKII catalytic subunit)
[Cdk5 Cdkn5] Cyclin-dependent-like kinase 5 (EC 2.7.11.1) (Cell division protein kinase 5) (Serine/threonine-protein kinase PSSALRE) (Tau protein kinase II catalytic subunit) (TPKII catalytic subunit)
[cdk1 cdcB DDB_G0272813] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDK1 CDC2 CDKN1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDC28 CDK1 CAALFM_CR06050WA CaO19.11337 CaO19.3856] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 28) (Cell division protein kinase 2)
[CDC28 CDK1 HSL5 SRM5 YBR160W YBR1211] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 28) (Cell division protein kinase 1)
[nimX cdk1 AN4182] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 2) (Cell division protein kinase 1) (Never in mitosis protein X)
[Cdk5 CG8203] Cyclin-dependent kinase 5 homolog (EC 2.7.11.22) (Cell division protein kinase 5)
[CDKB1-1 CDC2B At3g54180 F24B22.140] Cyclin-dependent kinase B1-1 (CDKB1;1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog B)
[CDKA-1 CDC2 CDC2A At3g48750 T21J18.20] Cyclin-dependent kinase A-1 (CDKA;1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog A) (CDC2aAt)
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.22.-) (Papain-like proteinase) (PL-PRO) (p195); Non-structural protein 4 (nsp4) (Peptide HD2) (p41); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p33); Non-structural protein 6 (nsp6) (p34); Non-structural protein 7 (nsp7) (p9); Non-structural protein 8 (nsp8) (p24); Non-structural protein 9 (nsp9) (p10); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p68); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14) (p58); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p39); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16) (p35)]

Bibliography :
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