ID CD11B_RAT Reviewed; 436 AA. AC P46892; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 08-NOV-2023, entry version 153. DE RecName: Full=Cyclin-dependent kinase 11B; 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 EC=2.7.11.22; 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 Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Salivary gland; RX PubMed=8049264; DOI=10.1016/0167-4781(94)90191-0; RA Kerr M., Fischer J.E., Purushotham K.R., Gao D., Nakagawa Y., Maeda N., RA Ghanta V., Hiramoto R., Chegini N., Humphreys-Beher M.G.; RT "Characterization of the synthesis and expression of the GTA-kinase from RT transformed and normal rodent cells."; RL Biochim. Biophys. Acta 1218:375-387(1994). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-236, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: Plays multiple roles in cell cycle progression, cytokinesis CC and apoptosis. Involved in pre-mRNA splicing in a kinase activity- CC dependent manner. May act as a negative regulator of normal cell cycle CC progression. {ECO:0000250|UniProtKB:P21127}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; 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 -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.22; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SUBUNIT: May interact PAK1 and RANBP9. p110C interacts with RNPS1. CC Interacts with CCND3. Interacts with CCNL1 and CCNL2. Forms complexes CC with pre-mRNA-splicing factors, including at least SRSF1, SRSF2 AND CC SRSF7/SLU7. {ECO:0000250|UniProtKB:P21127}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus membrane; Peripheral membrane CC protein. Endomembrane system; Peripheral membrane protein. Cytoplasm, CC perinuclear region. 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=AAA88509.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L24388; AAA88509.1; ALT_INIT; mRNA. DR PIR; S47628; S47628. DR AlphaFoldDB; P46892; -. DR SMR; P46892; -. DR STRING; 10116.ENSRNOP00000023274; -. DR iPTMnet; P46892; -. DR PhosphoSitePlus; P46892; -. DR jPOST; P46892; -. DR PaxDb; 10116-ENSRNOP00000039105; -. DR AGR; RGD:628604; -. DR RGD; 628604; Cdk11b. DR eggNOG; KOG0663; Eukaryota. DR InParanoid; P46892; -. DR PhylomeDB; P46892; -. DR BRENDA; 2.7.11.22; 5301. DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes. DR PRO; PR:P46892; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; ISO:RGD. DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD. DR GO; GO:0001824; P:blastocyst development; ISO:RGD. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:RGD. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0001558; P:regulation of cell growth; ISO:RGD. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central. DR GO; GO:0007088; P:regulation of mitotic nuclear division; ISO:RGD. DR GO; GO:0050684; P:regulation of mRNA processing; ISO:RGD. DR CDD; cd07843; STKc_CDC2L1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 ATP-binding; Cell cycle; Cytoplasm; Isopeptide bond; Kinase; Membrane; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase; Ubl conjugation. FT CHAIN 1..436 FT /note="Cyclin-dependent kinase 11B" FT /id="PRO_0000085710" FT DOMAIN 79..364 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 30..44 FT /note="Calmodulin-binding" FT /evidence="ECO:0000255" FT REGION 383..406 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 25..30 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT ACT_SITE 203 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 85..93 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 108 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 123 FT /note="Phosphoserine; by CDK7" FT /evidence="ECO:0000250|UniProtKB:P21127" FT MOD_RES 129 FT /note="Phosphothreonine; by CDK7" FT /evidence="ECO:0000250|UniProtKB:P21127" FT MOD_RES 230 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P21127" FT MOD_RES 235 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P21127" FT MOD_RES 236 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 392 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P24788" FT MOD_RES 393 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P24788" FT CROSSLNK 282 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P21127" SQ SEQUENCE 436 AA; 49547 MW; D2BA9BC73EAD3D27 CRC64; MKSEKSRTTS WLFQSHEVTE ILGRVKKNRK KLVKGLHRAG PPPEKNYLPD SPALSPIELK QELPKYLPAL QGCRSVEEFQ CLNRIEEGTY GVVYRAKDKK TDEIVALKRL KMEKEKEGFP LTSIREINTI LKAQHPNIVT VREIVVGSNM DKIYIVMNYV EHDLKSLMET MKQPFLPGEV KTLMIQLLSG VKHLHDNWIL HRDLKTSNLL LTHAGILKVG DFGLAREYGS PLKAYTPVVV TLWYRAPELL LGAKEYSTAC DMWSVGCIFG ELLTQKPLFP GKSDIDQINK IFKDIGTPSE KIWPGYSELP AVKKMTFSEL PYNNLRKRFG ALLSDQGFDL MNKFLTYYPG RRINAEDGLK HEYFRETPLP IDPSMFPTWP AKSEQQCVKR GTSPKPPEGG LGYSQLGDDD LKETGFHLTT TNDGAVSCRP WCSLLF //