CD11B_MOUSE
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 03-AUG-2022, entry version 192.
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 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 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 [6]
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 [7]
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, Pancreas,
RC 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: 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 -!- ACTIVITY REGULATION: Phosphorylation at Thr-437 or Tyr-438 inactivates
CC the enzyme, while phosphorylation at Thr-584 activates it.
CC {ECO:0000250|UniProtKB:P06493}.
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 -!- 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: Phosphorylation at Ser-115 creates a binding site for 14-3-3
CC proteins. {ECO:0000250}.
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};
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; 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_001347308.1.
DR RefSeq; NP_031687.2; NM_007661.3. [P24788-1]
DR RefSeq; XP_006538571.1; XM_006538508.2.
DR RefSeq; XP_006538574.1; XM_006538511.2.
DR RefSeq; XP_011248481.1; XM_011250179.2.
DR RefSeq; XP_017175418.1; XM_017319929.1.
DR RefSeq; XP_017175419.1; XM_017319930.1.
DR RefSeq; XP_017175422.1; XM_017319933.1.
DR RefSeq; XP_017175423.1; XM_017319934.1.
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 IntAct; P24788; 4.
DR MINT; P24788; -.
DR STRING; 10090.ENSMUSP00000070527; -.
DR iPTMnet; P24788; -.
DR PhosphoSitePlus; P24788; -.
DR EPD; P24788; -.
DR jPOST; P24788; -.
DR MaxQB; P24788; -.
DR PaxDb; P24788; -.
DR PeptideAtlas; P24788; -.
DR PRIDE; P24788; -.
DR ProteomicsDB; 281432; -. [P24788-1]
DR ProteomicsDB; 281433; -. [P24788-2]
DR DNASU; 12537; -.
DR Ensembl; ENSMUST00000067081; ENSMUSP00000070527; ENSMUSG00000029062. [P24788-1]
DR Ensembl; ENSMUST00000105600; ENSMUSP00000101225; ENSMUSG00000029062. [P24788-1]
DR GeneID; 12537; -.
DR KEGG; mmu:12537; -.
DR UCSC; uc008wea.1; mouse. [P24788-1]
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; MLDNWDD; -.
DR OrthoDB; 925637at2759; -.
DR PhylomeDB; P24788; -.
DR TreeFam; TF101035; -.
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 75 CRISPR screens.
DR ChiTaRS; Cdk11b; mouse.
DR PRO; PR:P24788; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P24788; protein.
DR Bgee; ENSMUSG00000029062; Expressed in granulocyte and 275 other tissues.
DR ExpressionAtlas; P24788; baseline and differential.
DR Genevisible; P24788; MM.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
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:MGI.
DR GO; GO:0001824; P:blastocyst development; IMP:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IC:ComplexPortal.
DR GO; GO:0046605; P:regulation of centrosome cycle; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:MGI.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
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 Alternative initiation; ATP-binding; Cell cycle; Isopeptide bond; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; 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..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..118
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..351
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..371
FT /note="Basic and 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 433..441
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 456
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
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 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
