CD11B_RAT
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 03-AUG-2022, entry version 149.
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};
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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 PRIDE; P46892; -.
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; IBA:GO_Central.
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:0006468; P:protein phosphorylation; ISO:RGD.
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 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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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
