ID   CD11B_MOUSE             Reviewed;         784 AA.
AC   P24788; Q3UI03; Q61399; Q7TST4; Q8BP53;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   02-SEP-2026, entry version 209.
DE   RecName: Full=Cyclin-dependent kinase 11B;
DE            EC=2.7.11.22 {ECO:0000250|UniProtKB:P21127};
DE            EC=2.7.11.23 {ECO:0000250|UniProtKB:P21127};
DE   AltName: Full=Cell division cycle 2-like protein kinase 1;
DE   AltName: Full=Cell division protein kinase 11;
DE   AltName: Full=Cyclin-dependent kinase 11;
DE   AltName: Full=Galactosyltransferase-associated protein kinase p58/GTA;
DE   AltName: Full=PITSLRE serine/threonine-protein kinase CDC2L1;
GN   Name=Cdk11b; Synonyms=Cdc2l1, Cdk11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=2069872;
RA   Kidd V.J., Luo W., Xiang J.L., Tu F., Easton J., McCune S., Snead M.L.;
RT   "Regulated expression of a cell division control-related protein kinase
RT   during development.";
RL   Cell Growth Differ. 2:85-93(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=7528743; DOI=10.1016/s0021-9258(20)30091-0;
RA   Malek S.N., Desiderio S.;
RT   "A cyclin-dependent kinase homologue, p130PITSLRE is a phosphotyrosine-
RT   independent SH2 ligand.";
RL   J. Biol. Chem. 269:33009-33020(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-784 (ISOFORM 1).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15060143; DOI=10.1128/mcb.24.8.3188-3197.2004;
RA   Li T., Inoue A., Lahti J.M., Kidd V.J.;
RT   "Failure to proliferate and mitotic arrest of CDK11(p110/p58)-null mutant
RT   mice at the blastocyst stage of embryonic cell development.";
RL   Mol. Cell. Biol. 24:3188-3197(2004).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-72; SER-270; SER-578;
RP   THR-584; THR-740 AND SER-741, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Cyclin-dependent protein kinase that acts as a regulator of
CC       transcription and pre-mRNA splicing (By similarity). Acts as a key
CC       regulator of pre-mRNA splicing by mediating phosphorylation of SF3B1,
CC       enabling the association between SF3B1 and U5 and U6 snRNAs in the
CC       activated spliceosome, thereby promoting spliceosome assembly (By
CC       similarity). Also acts as a regulator of transcription by
CC       phosphorylating 'Ser-2' of the CTD (C-terminal domain) of the large
CC       subunit of RNA polymerase II (RNAP II) POLR2A (By similarity). Involved
CC       in replication-dependent transcription of histone genes: binds to
CC       histone genes and phosphorylates POLR2A at 'Ser-2' of the CTD to
CC       specifically control transcriptional elongation of histones and
CC       recruitment of 3'-end processing factors (By similarity). Part of a
CC       transcription checkpoint upstream of CDK9, which regulates promoter-
CC       proximal pausing by RNA polymerase II, a transcription halt following
CC       transcription initiation, but prior to elongation (By similarity).
CC       Probably regulates promoter-proximal pausing by mediating
CC       phosphorylation of POLR2A at 'Ser-2' of the CTD (By similarity).
CC       Activated by the CDK-activating kinase (CAK) complex consisting of
CC       CDK7, cyclin-H/CCNH and MAT1, which is a master regulator of CDK
CC       activity (By similarity). {ECO:0000250|UniProtKB:P21127}.
CC   -!- FUNCTION: [Isoform 1]: Isoform expressed in a non-cell cycle-dependent
CC       manner. {ECO:0000250|UniProtKB:P21127}.
CC   -!- FUNCTION: [Isoform 2]: Isoform specifically expressed during the G2-M
CC       phases of the cell cycle. Phosphorylates 'Ser-2' of the CTD (C-terminal
CC       domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A.
CC       Promotes centromeric transcription to maintain centromeric cohesion
CC       during mitosis. {ECO:0000250|UniProtKB:P21127}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC         Evidence={ECO:0000250|UniProtKB:P21127};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC         Evidence={ECO:0000250|UniProtKB:P21127};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC         Evidence={ECO:0000250|UniProtKB:P21127};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC         Evidence={ECO:0000250|UniProtKB:P21127};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[DNA-directed RNA polymerase] + ATP = phospho-[DNA-directed
CC         RNA polymerase] + ADP + H(+); Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC         COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC         ChEBI:CHEBI:456216; EC=2.7.11.23;
CC         Evidence={ECO:0000250|UniProtKB:P21127};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10217;
CC         Evidence={ECO:0000250|UniProtKB:P21127};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P21127};
CC   -!- ACTIVITY REGULATION: Phosphorylated and activated by CDK7 in the CDK-
CC       activating kinase (CAK) complex, and reciprocally phosphorylating its
CC       activating kinase CDK7 (By similarity). CDK11 is specifically inhibited
CC       by the anticancer agent OTS964 (By similarity).
CC       {ECO:0000250|UniProtKB:P06493, ECO:0000250|UniProtKB:P21127}.
CC   -!- SUBUNIT: Associates with cyclin-L1 (CCNL1) or cyclin-L2 (CCNL2) to form
CC       an active cyclin-L-CDK11 cyclin-dependent protein kinase complex.
CC       Interacts with SAP30BP; promoting assembly of the cyclin-L-CDK11
CC       cyclin-dependent protein kinase complex. Interacts with CASP8AP2/FLASH;
CC       promoting 3' end cleavage of histone pre-mRNAs.
CC       {ECO:0000250|UniProtKB:P21127}.
CC   -!- SUBUNIT: [Isoform 1]: Associates with cyclin-L1 (CCNL1) or cyclin-L2
CC       (CCNL2) to form an active cyclin-L-CDK11 cyclin-dependent protein
CC       kinase complex. Interacts with SFRS7. Forms complexes with pre-mRNA-
CC       splicing factors, including at least SRSF1, SRSF2 and SRSF7/SLU7.
CC       Interacts with isoform 5 of MYO18A. The cleaved p110 isoform, p110C,
CC       binds to the serine/threonine kinase PAK1 and RANBP9. p110C interacts
CC       with RNPS1. {ECO:0000250|UniProtKB:P21127}.
CC   -!- SUBUNIT: [Isoform 2]: Associates with cyclin-D3 (CCND3) to form an
CC       active cyclin-dependent protein kinase complex.
CC       {ECO:0000250|UniProtKB:P21127}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15060143}. Chromosome
CC       {ECO:0000250|UniProtKB:P21127}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P21127}. Note=Localizes to transcription start
CC       site (TSS) proximal regions. {ECO:0000250|UniProtKB:P21127}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC       {ECO:0000250|UniProtKB:P21127}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC       {ECO:0000250|UniProtKB:P21127}. Chromosome, centromere
CC       {ECO:0000250|UniProtKB:P21127}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1; Synonyms=p130PITSLRE;
CC         IsoId=P24788-1; Sequence=Displayed;
CC       Name=2; Synonyms=p58clk-1;
CC         IsoId=P24788-2; Sequence=VSP_018835;
CC   -!- PTM: [Isoform 1]: During FAS- or TNF-induced apoptosis, isoform SV9 is
CC       cleaved by caspases to produce p110C, a fragment that contains the C-
CC       terminal kinase domain. {ECO:0000250|UniProtKB:P21127}.
CC   -!- PTM: Phosphorylation at Ser-115 creates a binding site for 14-3-3
CC       proteins. p110C can be autophosphorylated.
CC       {ECO:0000250|UniProtKB:P21127}.
CC   -!- DISRUPTION PHENOTYPE: Early embryonic lethality due to apoptosis at the
CC       blastocyst stage between 3.5 and 4 days post coitum (dpc).
CC       {ECO:0000269|PubMed:15060143}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA03518.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M58633; AAA03518.1; ALT_FRAME; mRNA.
DR   EMBL; L37092; AAA66169.1; -; mRNA.
DR   EMBL; AK077668; BAC36942.1; -; mRNA.
DR   EMBL; AK147133; BAE27703.1; -; mRNA.
DR   EMBL; BC052920; AAH52920.1; -; mRNA.
DR   CCDS; CCDS19033.1; -. [P24788-1]
DR   PIR; A55817; A55817.
DR   RefSeq; NP_001334237.1; NM_001347308.2.
DR   RefSeq; NP_001342498.1; NM_001355569.2. [P24788-2]
DR   RefSeq; NP_001406923.1; NM_001419994.1. [P24788-1]
DR   RefSeq; NP_001406929.1; NM_001420000.1. [P24788-2]
DR   RefSeq; NP_031687.2; NM_007661.5. [P24788-1]
DR   RefSeq; XP_036019509.1; XM_036163616.1. [P24788-2]
DR   AlphaFoldDB; P24788; -.
DR   SMR; P24788; -.
DR   BioGRID; 198625; 10.
DR   ComplexPortal; CPX-350; Cyclin L2-CDK11B(p110) complex. [P24788-1]
DR   ComplexPortal; CPX-351; Cyclin L1-CDK11B(p110) complex. [P24788-1]
DR   ComplexPortal; CPX-352; Cyclin L1-CDK11B(p58) complex. [P24788-2]
DR   ComplexPortal; CPX-353; Cyclin L2-CDK11B(p58) complex. [P24788-2]
DR   FunCoup; P24788; 2245.
DR   IntAct; P24788; 4.
DR   MINT; P24788; -.
DR   STRING; 10090.ENSMUSP00000101225; -.
DR   GlyGen; P24788; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P24788; -.
DR   PhosphoSitePlus; P24788; -.
DR   jPOST; P24788; -.
DR   PaxDb; 10090-ENSMUSP00000101225; -.
DR   PeptideAtlas; P24788; -.
DR   ProteomicsDB; 281432; -. [P24788-1]
DR   ProteomicsDB; 281433; -. [P24788-2]
DR   Pumba; P24788; -.
DR   DNASU; 12537; -.
DR   Ensembl; ENSMUST00000067081.10; ENSMUSP00000070527.4; ENSMUSG00000029062.15. [P24788-1]
DR   Ensembl; ENSMUST00000105600.8; ENSMUSP00000101225.2; ENSMUSG00000029062.15. [P24788-1]
DR   GeneID; 12537; -.
DR   KEGG; mmu:12537; -.
DR   UCSC; uc008wea.1; mouse. [P24788-1]
DR   AGR; MGI:88353; -.
DR   CTD; 984; -.
DR   MGI; MGI:88353; Cdk11b.
DR   VEuPathDB; HostDB:ENSMUSG00000029062; -.
DR   eggNOG; KOG0663; Eukaryota.
DR   GeneTree; ENSGT00940000158459; -.
DR   HOGENOM; CLU_000288_91_3_1; -.
DR   InParanoid; P24788; -.
DR   OMA; YYNVMLG; -.
DR   OrthoDB; 647at2759; -.
DR   PhylomeDB; P24788; -.
DR   BRENDA; 2.7.11.22; 3474.
DR   Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   BioGRID-ORCS; 12537; 15 hits in 80 CRISPR screens.
DR   PRO; PR:P24788; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; P24788; protein.
DR   Bgee; ENSMUSG00000029062; Expressed in granulocyte and 278 other cell types or tissues.
DR   ExpressionAtlas; P24788; baseline and differential.
DR   GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR   GO; GO:0000775; C:chromosome, centromeric region; ISO:GO_Central.
DR   GO; GO:0180038; C:cyclin L-CDK11 complex; ISS:UniProtKB.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISS:ComplexPortal.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; ISO:GO_Central.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:GO_Central.
DR   GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; ISS:UniProtKB.
DR   GO; GO:0140834; F:RNA polymerase II CTD heptapeptide repeat S2 kinase activity; ISS:UniProtKB.
DR   GO; GO:0140836; F:RNA polymerase II CTD heptapeptide repeat S5 kinase activity; ISS:UniProtKB.
DR   GO; GO:0001824; P:blastocyst development; IMP:MGI.
DR   GO; GO:0071962; P:mitotic sister chromatid cohesion, centromeric; ISO:MGI.
DR   GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:MGI.
DR   GO; GO:0042981; P:regulation of apoptotic process; NAS:ComplexPortal.
DR   GO; GO:0051726; P:regulation of cell cycle; NAS:ComplexPortal.
DR   GO; GO:0046605; P:regulation of centrosome cycle; NAS:ComplexPortal.
DR   GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:MGI.
DR   GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0043484; P:regulation of RNA splicing; ISS:ComplexPortal.
DR   GO; GO:0001111; P:RNA polymerase II promoter clearance; ISS:UniProtKB.
DR   CDD; cd07843; STKc_CDC2L1; 1.
DR   FunFam; 3.30.200.20:FF:000054; Cyclin-dependent kinase 11B; 1.
DR   FunFam; 1.10.510.10:FF:000124; cyclin-dependent kinase 11B isoform X1; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR050108; CDK.
DR   InterPro; IPR045267; CDK11/PITSLRE_STKc.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR   PANTHER; PTHR24056:SF107; CYCLIN-DEPENDENT KINASE 11A-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative initiation; ATP-binding; Cell cycle; Centromere; Chromosome;
KW   Cytoplasm; Isopeptide bond; Kinase; Magnesium; Metal-binding;
KW   mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Ubl conjugation.
FT   CHAIN           1..784
FT                   /note="Cyclin-dependent kinase 11B"
FT                   /id="PRO_0000024313"
FT   DOMAIN          427..712
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          18..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          722..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..113
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..263
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..289
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..353
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..381
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        551
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         434
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   BINDING         434
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   BINDING         437
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   BINDING         437
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   BINDING         438
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   BINDING         438
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   BINDING         439
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   BINDING         439
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   BINDING         456
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   BINDING         456
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   BINDING         506
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   BINDING         508
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   BINDING         569
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   MOD_RES         47
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   MOD_RES         270
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         437
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P06493"
FT   MOD_RES         438
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P06493"
FT   MOD_RES         471
FT                   /note="Phosphoserine; by CDK7"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   MOD_RES         477
FT                   /note="Phosphothreonine; by CDK7"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   MOD_RES         578
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         583
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   MOD_RES         584
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         740
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         741
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        630
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P21127"
FT   VAR_SEQ         1..345
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:2069872"
FT                   /id="VSP_018835"
FT   CONFLICT        35..37
FT                   /note="LKN -> MSQ (in Ref. 4; AAH52920)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        284
FT                   /note="Missing (in Ref. 2; AAA66169)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        560
FT                   /note="S -> T (in Ref. 1; AAA03518)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        608
FT                   /note="V -> C (in Ref. 1; AAA03518)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        645
FT                   /note="T -> S (in Ref. 1; AAA03518)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        668
FT                   /note="Y -> I (in Ref. 1; AAA03518)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   784 AA;  91513 MW;  CDF03AC3957FA351 CRC64;
     MGDEKDSWKV KTLDEILQEK KRRKEQEEKA EIKRLKNSDD RDSKRDSLEE GELRDHRMEI
     TIRNSPYRRE DSMEDRGEED DSLAIKPPQQ MSRKEKAHHR KDEKRKEKRR HRSHSAEGGK
     HARVKEKERE HERRKRHREE QDKARREWER QKRREMAREH SRRERDRLEQ LERKRERERK
     LREQQKEQRE QKERERRAEE RRKEREARRE VSAHHRTMRE EYSDKGKVGH WSRSPLRPPR
     ERFEMGDNRK PVKEEKVEER DLLSDLQDIS DSERKTSSAE SSSAESGSGS EEEEEEEEEE
     EEEEGSTSEE SEEEEEEEEE EEEEETGSNS EEASEQSAEE VSDEEMSEDE DRENENHILV
     VPESRFDRDS GDSEEGEEEV GEGTPQSSAP TEGDYVPDSP ALSPIELKQE LPKYLPALQG
     CRSVEEFQCL NRIEEGTYGV VYRAKDKKTD EIVALKRLKM EKEKEGFPIT SLREINTILK
     AQHPNIVTVR EIVVGSNMDK IYIVMNYVEH DLKSLMETMK QPFLPGEVKT LMIQLLSGVK
     HLHDNWILHR DLKTSNLLLS HAGILKVGDF GLAREYGSPL KAYTPVVVTL WYRAPELLLG
     AKEYSTAVDM WSVGCIFGEL LTQKPLFPGK SDIDQINKIF KDLGTPSEKI WPGYNDLPAV
     KKMTFSEYPY NNLRKRFGAL LSDQGFDLMN KFLTYYPGRR INAEDGLKHE YFRETPLPID
     PSMFPTWPAK SEQQRVKRGT SPRPPEGGLG YSQLGDDDLK ETGFHLTTTN QGASAAGPGF
     SLKF
//