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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; O95265; Q12817; Q12818; Q12819; Q12820; Q12822; Q8N530;
Q9NZS5; Q9UBJ0; Q9UBQ1; Q9UBR0; Q9UNY2; Q9UP57; Q9UP58; Q9UP59;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
19-SEP-2003, sequence version 3.
30-AUG-2017, entry version 191.
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, 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;
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]
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).
[8]
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).
[9]
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).
[10]
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).
[11]
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).
[12]
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).
[13]
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).
[14]
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).
[15]
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).
[16]
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).
[17]
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).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME 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:
O00303:EIF3F; NbExp=3; IntAct=EBI-1298, EBI-711990;
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;
Note=Produced by alternative initiation at Met-357 of isoform
SV9 via an internal ribosomal entry site (IRES).;
-!- 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.
-!- 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=AAC83664.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAF36538.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; M37712; AAA36406.1; ALT_SEQ; 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.
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_277022.1; NM_033487.2. [P21127-5]
RefSeq; NP_277025.1; NM_033490.2. [P21127-10]
UniGene; Hs.651228; -.
UniGene; Hs.709182; -.
ProteinModelPortal; P21127; -.
SMR; P21127; -.
BioGrid; 107421; 47.
IntAct; P21127; 16.
MINT; MINT-1400900; -.
STRING; 9606.ENSP00000384442; -.
BindingDB; P21127; -.
ChEMBL; CHEMBL5808; -.
GuidetoPHARMACOLOGY; 1964; -.
iPTMnet; P21127; -.
PhosphoSitePlus; P21127; -.
BioMuta; CDK11B; -.
DMDM; 34978359; -.
EPD; P21127; -.
MaxQB; P21127; -.
PaxDb; P21127; -.
PeptideAtlas; P21127; -.
PRIDE; P21127; -.
DNASU; 984; -.
GeneID; 984; -.
KEGG; hsa:984; -.
CTD; 984; -.
DisGeNET; 984; -.
GeneCards; CDK11B; -.
HGNC; HGNC:1729; CDK11B.
HPA; HPA025061; -.
HPA; HPA073626; -.
MIM; 176873; gene.
neXtProt; NX_P21127; -.
PharmGKB; PA26262; -.
eggNOG; KOG0663; Eukaryota.
eggNOG; ENOG410XQ50; LUCA.
HOVERGEN; HBG014652; -.
InParanoid; P21127; -.
KO; K08818; -.
PhylomeDB; P21127; -.
BRENDA; 2.7.11.22; 2681.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
SignaLink; P21127; -.
SIGNOR; P21127; -.
ChiTaRS; CDK11B; human.
GeneWiki; CDC2L1; -.
GenomeRNAi; 984; -.
PMAP-CutDB; P21127; -.
PRO; PR:P21127; -.
Proteomes; UP000005640; Unplaced.
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; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
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: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.
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; Complete proteome; Cytoplasm; Isopeptide bond; Kinase;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Ubl conjugation.
CHAIN 1 795 Cyclin-dependent kinase 11B.
/FTId=PRO_0000024311.
DOMAIN 438 723 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 444 452 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 126 393 Glu-rich.
ACT_SITE 562 562 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 467 467 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000250|UniProtKB:P24788}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000250|UniProtKB:P24788}.
MOD_RES 115 115 Phosphoserine.
{ECO:0000269|PubMed:15883043}.
MOD_RES 283 283 Phosphoserine.
{ECO:0000250|UniProtKB:P24788}.
MOD_RES 482 482 Phosphoserine; by CDK7.
{ECO:0000269|PubMed:16327805}.
MOD_RES 488 488 Phosphothreonine; by CDK7.
{ECO:0000269|PubMed:16327805}.
MOD_RES 589 589 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 594 594 Phosphotyrosine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 595 595 Phosphothreonine.
{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 751 751 Phosphothreonine.
{ECO:0000250|UniProtKB:P24788}.
MOD_RES 752 752 Phosphoserine.
{ECO:0000250|UniProtKB:P24788}.
CROSSLNK 641 641 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 356 Missing (in isoform 7).
{ECO:0000303|PubMed:2217177}.
/FTId=VSP_018834.
VAR_SEQ 1 269 Missing (in isoform SV4).
{ECO:0000303|PubMed:9750192}.
/FTId=VSP_008275.
VAR_SEQ 1 217 Missing (in isoform SV11).
{ECO:0000303|PubMed:8195233,
ECO:0000303|PubMed:9750192,
ECO:0000303|Ref.6}.
/FTId=VSP_008274.
VAR_SEQ 1 34 Missing (in isoform SV5 and isoform
SV10). {ECO:0000303|PubMed:9750192}.
/FTId=VSP_008273.
VAR_SEQ 2 335 Missing (in isoform 3).
{ECO:0000303|PubMed:8195233}.
/FTId=VSP_008276.
VAR_SEQ 35 37 LKN -> MSQ (in isoform SV5 and isoform
SV10). {ECO:0000303|PubMed:9750192}.
/FTId=VSP_008277.
VAR_SEQ 110 119 Missing (in isoform 2, isoform SV5 and
isoform 8). {ECO:0000303|PubMed:8195233,
ECO:0000303|PubMed:9750192}.
/FTId=VSP_008278.
VAR_SEQ 165 165 R -> RGNDGVCLFR (in isoform 2).
{ECO:0000303|PubMed:8195233}.
/FTId=VSP_008279.
VAR_SEQ 252 265 GEARPARAQKPAQL -> V (in isoform SV1,
isoform 2, isoform SV5, isoform 8,
isoform SV10 and isoform SV11).
{ECO:0000303|PubMed:8195233,
ECO:0000303|PubMed:9750192,
ECO:0000303|Ref.6}.
/FTId=VSP_008280.
VARIANT 57 57 R -> C (in dbSNP:rs17424353).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:8195233}.
/FTId=VAR_041958.
VARIANT 93 93 R -> W (in dbSNP:rs1059831).
/FTId=VAR_057775.
VARIANT 109 109 R -> C (in dbSNP:rs1059830).
/FTId=VAR_062199.
VARIANT 201 201 R -> W. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041959.
VARIANT 414 414 S -> L. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041960.
VARIANT 452 452 V -> A. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_045577.
VARIANT 463 463 I -> V. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041961.
VARIANT 506 506 G -> S. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_045578.
VARIANT 601 601 L -> Q. {ECO:0000269|PubMed:1639388,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_041962.
VARIANT 641 641 K -> N. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041963.
VARIANT 670 670 A -> V (in dbSNP:rs1059811).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041964.
CONFLICT 109 109 Missing (in Ref. 4; AAA19582/AAA19583 and
5; AAC72079). {ECO:0000305}.
CONFLICT 126 126 E -> K (in Ref. 4; AAA19582/AAA19583/
AAA19586). {ECO:0000305}.
CONFLICT 320 320 S -> T (in Ref. 6). {ECO:0000305}.
CONFLICT 324 326 Missing (in Ref. 4; AAA19582/AAA19583/
AAA19584/AAA19586). {ECO:0000305}.
CONFLICT 436 436 E -> D (in Ref. 3). {ECO:0000305}.
CONFLICT 560 560 H -> Q (in Ref. 6). {ECO:0000305}.
CONFLICT 567 567 N -> T (in Ref. 6). {ECO:0000305}.
CONFLICT 678 678 E -> R (in Ref. 4 and 6). {ECO:0000305}.
CONFLICT 694 694 D -> E (in Ref. 3). {ECO:0000305}.
CONFLICT 697 697 F -> C (in Ref. 6). {ECO:0000305}.
CONFLICT 712 712 I -> L (in Ref. 3). {ECO:0000305}.
CONFLICT 715 715 E -> Q (in Ref. 3). {ECO:0000305}.
CONFLICT 792 792 S -> R (in Ref. 6). {ECO:0000305}.
SEQUENCE 795 AA; 92707 MW; C07CEE9A4F7A6804 CRC64;
MGDEKDSWKV KTLDEILQEK KRRKEQEEKA EIKRLKNSDD RDSKRDSLEE GELRDHRMEI
TIRNSPYRRE DSMEDRGEED DSLAIKPPQQ MSRKEKVHHR KDEKRKEKRR HRSHSAEGGK
HARVKEKERE HERRKRHREE QDKARREWER QKRREMAREH SRRERDRLEQ LERKRERERK
MREQQKEQRE QKERERRAEE RRKEREARRE VSAHHRTMRE DYSDKVKASH WSRSPPRPPR
ERFELGDGRK PGEARPARAQ 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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