CD11A_HUMAN
ID CD11A_HUMAN Reviewed; 783 AA.
AC Q9UQ88; O95227; O95228; O96012; Q12821; Q12853; Q12854; Q2TAJ0; Q5QPR0;
AC Q5QPR1; Q5QPR2; Q9UBC4; Q9UBI3; Q9UEI1; Q9UEI2; Q9UP53; Q9UP54; Q9UP55;
AC Q9UP56; Q9UQ86; Q9UQ87; Q9UQ89;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Cyclin-dependent kinase 11A;
DE EC=2.7.11.22;
DE AltName: Full=Cell division cycle 2-like protein kinase 2;
DE AltName: Full=Cell division protein kinase 11A;
DE AltName: Full=Galactosyltransferase-associated protein kinase p58/GTA;
DE AltName: Full=PITSLRE serine/threonine-protein kinase CDC2L2;
GN Name=CDK11A; Synonyms=CDC2L2, CDC2L3, PITSLREB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SV1; SV2 AND 4), TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND VARIANT SER-402.
RC TISSUE=Cervix carcinoma;
RX PubMed=8195233; DOI=10.1016/s0021-9258(17)40749-6;
RA Xiang J., Lahti J.M., Grenet J.A., Easton J.B., Kidd V.J.;
RT "Molecular cloning and expression of alternatively spliced PITSLRE protein
RT kinase isoforms.";
RL J. Biol. Chem. 269:15786-15794(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SV1; SV2; SV3; SV6; SV7; SV12 AND
RP SV13), TISSUE SPECIFICITY, AND VARIANT TRP-93.
RC TISSUE=Cervix carcinoma;
RX PubMed=9750192; DOI=10.1101/gr.8.9.929;
RA Gururajan R., Lahti J.M., Grenet J.A., Easton J., Gruber I., Ambros P.F.,
RA Kidd V.J.;
RT "Duplication of a genomic region containing the Cdc2L1-2 and MMP21-22 genes
RT on human chromosome 1p36.3 and their linkage to D1Z2.";
RL Genome Res. 8:929-939(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TRP-93.
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SV7).
RC TISSUE=Skin;
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CCNL1 AND SFRS7.
RX PubMed=12501247; DOI=10.1074/jbc.m210057200;
RA Hu D., Mayeda A., Trembley J.H., Lahti J.M., Kidd V.J.;
RT "CDK11 complexes promote pre-mRNA splicing.";
RL J. Biol. Chem. 278:8623-8629(2003).
RN [6]
RP ALTERNATIVE INITIATION (ISOFORM 4), AND INDUCTION.
RX PubMed=10882096; DOI=10.1016/s1097-2765(00)80239-7;
RA Cornelis S., Bruynooghe Y., Denecker G., Van Huffel S., Tinton S.,
RA Beyaert R.;
RT "Identification and characterization of a novel cell cycle-regulated
RT internal ribosome entry site.";
RL Mol. Cell 5:597-605(2000).
RN [7]
RP FUNCTION, AND INTERACTION WITH PAK1.
RX PubMed=12624090; DOI=10.1074/jbc.m300818200;
RA Chen S., Yin X., Zhu X., Yan J., Ji S., Chen C., Cai M., Zhang S., Zong H.,
RA Hu Y., Yuan Z., Shen Z., Gu J.;
RT "The C-terminal kinase domain of the p34cdc2-related PITSLRE protein kinase
RT (p110C) associates with p21-activated kinase 1 and inhibits its activity
RT during anoikis.";
RL J. Biol. Chem. 278:20029-20036(2003).
CC -!- FUNCTION: Appears to play multiple roles in cell cycle progression,
CC cytokinesis and apoptosis. The p110 isoforms have been suggested to be
CC involved in pre-mRNA splicing, potentially by phosphorylating the
CC splicing protein SFRS7. The p58 isoform may act as a negative regulator
CC of normal cell cycle progression. {ECO:0000269|PubMed:12501247,
CC ECO:0000269|PubMed:12624090}.
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-436 or Tyr-437 inactivates
CC the enzyme, while phosphorylation at Thr-583 activates it.
CC {ECO:0000250}.
CC -!- SUBUNIT: The cleaved p110 isoform, p110C, binds to the serine/threonine
CC kinase PAK1. The p58 isoform but not the p110 isoform or p110C
CC interacts with CCND3. The p110 isoforms are found in large molecular
CC weight complexes containing CCNL1 and SFRS7.
CC {ECO:0000269|PubMed:12501247, ECO:0000269|PubMed:12624090}.
CC -!- INTERACTION:
CC Q9UQ88-1; O96017: CHEK2; NbExp=2; IntAct=EBI-11579223, EBI-1180783;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=8;
CC Comment=Additional isoforms seem to exist.;
CC Name=SV6; Synonyms=p110;
CC IsoId=Q9UQ88-1; Sequence=Displayed;
CC Name=SV1; Synonyms=Pbeta21, Beta 2-1;
CC IsoId=Q9UQ88-2; Sequence=VSP_008286, VSP_008288;
CC Name=SV2; Synonyms=Pbeta22;
CC IsoId=Q9UQ88-3; Sequence=VSP_008287, VSP_008288;
CC Name=SV3;
CC IsoId=Q9UQ88-4; Sequence=VSP_008288;
CC Name=SV7; Synonyms=SV8;
CC IsoId=Q9UQ88-5; Sequence=VSP_008283, VSP_008289;
CC Name=SV12;
CC IsoId=Q9UQ88-8; Sequence=VSP_008284, VSP_008292;
CC Name=SV13;
CC IsoId=Q9UQ88-9; Sequence=VSP_008281, VSP_008287, VSP_008288,
CC VSP_008290, VSP_008291;
CC Name=4; Synonyms=Beta 1, p58;
CC IsoId=Q9UQ88-10; Sequence=VSP_018836;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. Some evidence of isoform-
CC specific tissue distribution. {ECO:0000269|PubMed:8195233,
CC ECO:0000269|PubMed:9750192}.
CC -!- INDUCTION: The p58 isoform is specifically induced in G2/M phase of the
CC cell cycle. {ECO:0000269|PubMed:10882096}.
CC -!- PTM: During apoptosis, induced by Fas or tumor necrosis factor,
CC specific CKD11 p110 isoforms are cleaved by caspases to produce a
CC protein (p110C) that contains the C-terminal kinase domain of the CDK11
CC proteins.
CC -!- MISCELLANEOUS: Duplicated gene. CDK11A and CDK11B encode almost
CC identical protein kinases of 110 kDa that contain at their C-termini
CC the open reading frame of a smaller 58 kDa isoform which is expressed
CC following IRES-mediated alternative initiation of translation.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative initiation at Met-
CC 345 of isoform SV6. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC -!- CAUTION: Many references talk about 'p110 isoforms' but it is not yet
CC known if this refers to CDK11A and/or CDK11B or one/some of the
CC isoforms of each. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC95297.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC95298.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC95299.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC95300.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC95302.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC95303.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U04819; AAA19585.1; -; mRNA.
DR EMBL; U07704; AAA19594.1; -; mRNA.
DR EMBL; U07705; AAA19595.1; -; mRNA.
DR EMBL; AF067518; AAC72083.1; -; mRNA.
DR EMBL; AF067519; AAC72084.1; -; mRNA.
DR EMBL; AF067520; AAC72085.1; -; mRNA.
DR EMBL; AF067521; AAC72086.1; -; mRNA.
DR EMBL; AF067522; AAC72087.1; -; mRNA.
DR EMBL; AF067523; AAC72088.1; -; mRNA.
DR EMBL; AF067524; AAC72089.1; -; mRNA.
DR EMBL; AF067525; AAC72090.1; -; mRNA.
DR EMBL; AF067526; AAC72091.1; -; mRNA.
DR EMBL; AF067527; AAC72092.1; -; mRNA.
DR EMBL; AF067528; AAC72093.1; -; mRNA.
DR EMBL; AF067529; AAC72094.1; -; mRNA.
DR EMBL; AF080694; AAC95297.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF080695; AAC95297.1; JOINED; Genomic_DNA.
DR EMBL; AF105714; AAC95297.1; JOINED; Genomic_DNA.
DR EMBL; AF080696; AAC95297.1; JOINED; Genomic_DNA.
DR EMBL; AF080697; AAC95297.1; JOINED; Genomic_DNA.
DR EMBL; AF092427; AAC95297.1; JOINED; Genomic_DNA.
DR EMBL; AF092428; AAC95297.1; JOINED; Genomic_DNA.
DR EMBL; AF080689; AAC95297.1; JOINED; Genomic_DNA.
DR EMBL; AF080690; AAC95297.1; JOINED; Genomic_DNA.
DR EMBL; AF080691; AAC95297.1; JOINED; Genomic_DNA.
DR EMBL; AF080692; AAC95297.1; JOINED; Genomic_DNA.
DR EMBL; AF080693; AAC95297.1; JOINED; Genomic_DNA.
DR EMBL; AF080694; AAC95298.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF080695; AAC95298.1; JOINED; Genomic_DNA.
DR EMBL; AF105714; AAC95298.1; JOINED; Genomic_DNA.
DR EMBL; AF080696; AAC95298.1; JOINED; Genomic_DNA.
DR EMBL; AF080697; AAC95298.1; JOINED; Genomic_DNA.
DR EMBL; AF092427; AAC95298.1; JOINED; Genomic_DNA.
DR EMBL; AF092428; AAC95298.1; JOINED; Genomic_DNA.
DR EMBL; AF080689; AAC95298.1; JOINED; Genomic_DNA.
DR EMBL; AF080690; AAC95298.1; JOINED; Genomic_DNA.
DR EMBL; AF080691; AAC95298.1; JOINED; Genomic_DNA.
DR EMBL; AF080692; AAC95298.1; JOINED; Genomic_DNA.
DR EMBL; AF080693; AAC95298.1; JOINED; Genomic_DNA.
DR EMBL; AF080694; AAC95299.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF080695; AAC95299.1; JOINED; Genomic_DNA.
DR EMBL; AF105714; AAC95299.1; JOINED; Genomic_DNA.
DR EMBL; AF080696; AAC95299.1; JOINED; Genomic_DNA.
DR EMBL; AF080697; AAC95299.1; JOINED; Genomic_DNA.
DR EMBL; AF092427; AAC95299.1; JOINED; Genomic_DNA.
DR EMBL; AF092428; AAC95299.1; JOINED; Genomic_DNA.
DR EMBL; AF080689; AAC95299.1; JOINED; Genomic_DNA.
DR EMBL; AF080690; AAC95299.1; JOINED; Genomic_DNA.
DR EMBL; AF080691; AAC95299.1; JOINED; Genomic_DNA.
DR EMBL; AF080692; AAC95299.1; JOINED; Genomic_DNA.
DR EMBL; AF080693; AAC95299.1; JOINED; Genomic_DNA.
DR EMBL; AF080694; AAC95300.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF080695; AAC95300.1; JOINED; Genomic_DNA.
DR EMBL; AF105714; AAC95300.1; JOINED; Genomic_DNA.
DR EMBL; AF080696; AAC95300.1; JOINED; Genomic_DNA.
DR EMBL; AF080697; AAC95300.1; JOINED; Genomic_DNA.
DR EMBL; AF092427; AAC95300.1; JOINED; Genomic_DNA.
DR EMBL; AF092428; AAC95300.1; JOINED; Genomic_DNA.
DR EMBL; AF080689; AAC95300.1; JOINED; Genomic_DNA.
DR EMBL; AF080690; AAC95300.1; JOINED; Genomic_DNA.
DR EMBL; AF080691; AAC95300.1; JOINED; Genomic_DNA.
DR EMBL; AF080692; AAC95300.1; JOINED; Genomic_DNA.
DR EMBL; AF080693; AAC95300.1; JOINED; Genomic_DNA.
DR EMBL; AF080697; AAC95302.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF080695; AAC95302.1; JOINED; Genomic_DNA.
DR EMBL; AF105714; AAC95302.1; JOINED; Genomic_DNA.
DR EMBL; AF080696; AAC95302.1; JOINED; Genomic_DNA.
DR EMBL; AF080697; AAC95303.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF080695; AAC95303.1; JOINED; Genomic_DNA.
DR EMBL; AF105714; AAC95303.1; JOINED; Genomic_DNA.
DR EMBL; AF080696; AAC95303.1; JOINED; Genomic_DNA.
DR EMBL; AL031282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC110905; AAI10906.1; -; mRNA.
DR CCDS; CCDS44042.1; -. [Q9UQ88-2]
DR CCDS; CCDS44043.1; -. [Q9UQ88-4]
DR CCDS; CCDS81253.1; -. [Q9UQ88-1]
DR CCDS; CCDS81254.1; -. [Q9UQ88-3]
DR PIR; B54024; B54024.
DR PIR; E54024; E54024.
DR PIR; F54024; F54024.
DR PIR; H54024; H54024.
DR RefSeq; NP_001300825.1; NM_001313896.1. [Q9UQ88-1]
DR RefSeq; NP_001300911.1; NM_001313982.1.
DR RefSeq; NP_076916.2; NM_024011.3. [Q9UQ88-2]
DR RefSeq; NP_277071.2; NM_033529.3. [Q9UQ88-4]
DR AlphaFoldDB; Q9UQ88; -.
DR SMR; Q9UQ88; -.
DR BioGRID; 609064; 113.
DR ComplexPortal; CPX-341; Cyclin L1-CDK11A(p110) complex. [Q9UQ88-1]
DR ComplexPortal; CPX-343; Cyclin L2-CDK11A(p110) complex. [Q9UQ88-1]
DR ComplexPortal; CPX-344; Cyclin L1-CDK11A(p58) complex. [Q9UQ88-10]
DR ComplexPortal; CPX-347; Cyclin L2-CDK11A(p58) complex. [Q9UQ88-10]
DR IntAct; Q9UQ88; 57.
DR MINT; Q9UQ88; -.
DR BindingDB; Q9UQ88; -.
DR ChEMBL; CHEMBL5416; -.
DR DrugCentral; Q9UQ88; -.
DR GlyGen; Q9UQ88; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UQ88; -.
DR PhosphoSitePlus; Q9UQ88; -.
DR BioMuta; CDK11A; -.
DR DMDM; 317373559; -.
DR EPD; Q9UQ88; -.
DR jPOST; Q9UQ88; -.
DR MassIVE; Q9UQ88; -.
DR MaxQB; Q9UQ88; -.
DR PeptideAtlas; Q9UQ88; -.
DR PRIDE; Q9UQ88; -.
DR ProteomicsDB; 85520; -. [Q9UQ88-1]
DR ProteomicsDB; 85521; -. [Q9UQ88-10]
DR ProteomicsDB; 85522; -. [Q9UQ88-2]
DR ProteomicsDB; 85523; -. [Q9UQ88-3]
DR ProteomicsDB; 85524; -. [Q9UQ88-4]
DR ProteomicsDB; 85525; -. [Q9UQ88-5]
DR ProteomicsDB; 85526; -. [Q9UQ88-8]
DR ProteomicsDB; 85527; -. [Q9UQ88-9]
DR Antibodypedia; 4184; 139 antibodies from 21 providers.
DR DNASU; 728642; -.
DR Ensembl; ENST00000358779.9; ENSP00000351629.5; ENSG00000008128.23. [Q9UQ88-4]
DR Ensembl; ENST00000378633.5; ENSP00000367900.1; ENSG00000008128.23. [Q9UQ88-1]
DR Ensembl; ENST00000404249.8; ENSP00000384442.3; ENSG00000008128.23. [Q9UQ88-2]
DR GeneID; 728642; -.
DR KEGG; hsa:728642; -.
DR MANE-Select; ENST00000404249.8; ENSP00000384442.3; NM_024011.4; NP_076916.2. [Q9UQ88-2]
DR UCSC; uc009vkr.4; human. [Q9UQ88-1]
DR CTD; 728642; -.
DR DisGeNET; 728642; -.
DR GeneCards; CDK11A; -.
DR HGNC; HGNC:1730; CDK11A.
DR HPA; ENSG00000008128; Low tissue specificity.
DR MIM; 116951; gene.
DR neXtProt; NX_Q9UQ88; -.
DR OpenTargets; ENSG00000008128; -.
DR PharmGKB; PA26263; -.
DR VEuPathDB; HostDB:ENSG00000008128; -.
DR GeneTree; ENSGT00940000158459; -.
DR HOGENOM; CLU_000288_91_3_1; -.
DR InParanoid; Q9UQ88; -.
DR OMA; DSWHVKS; -.
DR OrthoDB; 925637at2759; -.
DR PhylomeDB; Q9UQ88; -.
DR TreeFam; TF101035; -.
DR PathwayCommons; Q9UQ88; -.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR SignaLink; Q9UQ88; -.
DR SIGNOR; Q9UQ88; -.
DR BioGRID-ORCS; 728642; 726 hits in 1110 CRISPR screens.
DR ChiTaRS; CDK11A; human.
DR GeneWiki; CDC2L2; -.
DR GenomeRNAi; 728642; -.
DR Pharos; Q9UQ88; Tchem.
DR PRO; PR:Q9UQ88; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UQ88; protein.
DR Bgee; ENSG00000008128; Expressed in sural nerve and 94 other tissues.
DR ExpressionAtlas; Q9UQ88; baseline and differential.
DR Genevisible; Q9UQ88; HS.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; NAS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; NAS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
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:0001558; P:regulation of cell growth; IEP:UniProtKB.
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:0050684; P:regulation of mRNA processing; IDA:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
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; Alternative splicing; Apoptosis; ATP-binding;
KW Cell cycle; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..783
FT /note="Cyclin-dependent kinase 11A"
FT /id="PRO_0000024315"
FT DOMAIN 427..647
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 18..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..783
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..120
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..350
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 550
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 432..440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 455
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:0000250|UniProtKB:P24788"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24788"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24788"
FT MOD_RES 470
FT /note="Phosphoserine; by CDK7"
FT /evidence="ECO:0000250|UniProtKB:P21127"
FT MOD_RES 476
FT /note="Phosphothreonine; by CDK7"
FT /evidence="ECO:0000250|UniProtKB:P21127"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21127"
FT MOD_RES 582
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P21127"
FT MOD_RES 583
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P21127"
FT MOD_RES 739
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24788"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24788"
FT VAR_SEQ 1..616
FT /note="Missing (in isoform SV12)"
FT /evidence="ECO:0000303|PubMed:9750192"
FT /id="VSP_008284"
FT VAR_SEQ 1..386
FT /note="Missing (in isoform SV7)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9750192"
FT /id="VSP_008283"
FT VAR_SEQ 1..344
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8195233"
FT /id="VSP_018836"
FT VAR_SEQ 1..57
FT /note="Missing (in isoform SV13)"
FT /evidence="ECO:0000303|PubMed:9750192"
FT /id="VSP_008281"
FT VAR_SEQ 109
FT /note="W -> CRHHSHSAEGG (in isoform SV1)"
FT /evidence="ECO:0000303|PubMed:8195233,
FT ECO:0000303|PubMed:9750192"
FT /id="VSP_008286"
FT VAR_SEQ 153
FT /note="R -> RGNDGFCLFR (in isoform SV2 and isoform SV13)"
FT /evidence="ECO:0000303|PubMed:8195233,
FT ECO:0000303|PubMed:9750192"
FT /id="VSP_008287"
FT VAR_SEQ 240..253
FT /note="GEARPAPAQKPAQL -> V (in isoform SV1, isoform SV2,
FT isoform SV3 and isoform SV13)"
FT /evidence="ECO:0000303|PubMed:8195233,
FT ECO:0000303|PubMed:9750192"
FT /id="VSP_008288"
FT VAR_SEQ 387..418
FT /note="SALTEGDYVPDSPALLPIELKQELPKYLPALQ -> MKNEKMKTTSWLFQSH
FT GSTEIPGRVKKQRKKW (in isoform SV7)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9750192"
FT /id="VSP_008289"
FT VAR_SEQ 567..600
FT /note="GDFGLAREYGSPLKAYTPVVVTQWYRAPELLLGA -> SPPPSGPSQGDPPG
FT PTHSRPSVVAGG (in isoform SV13)"
FT /evidence="ECO:0000303|PubMed:9750192"
FT /id="VSP_008290"
FT VAR_SEQ 601..783
FT /note="Missing (in isoform SV13)"
FT /evidence="ECO:0000303|PubMed:9750192"
FT /id="VSP_008291"
FT VAR_SEQ 617..658
FT /note="GELLTQKPLFPGNSEIDQINKVFKELGTPSEKIWPGYSELPV -> MGKTEE
FT KGNGKGAFQERKGPLGAVRKEAGAGAQDAGAAEGAA (in isoform SV12)"
FT /evidence="ECO:0000303|PubMed:9750192"
FT /id="VSP_008292"
FT VARIANT 57
FT /note="C -> R (in dbSNP:rs1059832)"
FT /id="VAR_060152"
FT VARIANT 92
FT /note="S -> P (in dbSNP:rs7531938)"
FT /id="VAR_062200"
FT VARIANT 93
FT /note="R -> W (in dbSNP:rs1059831)"
FT /evidence="ECO:0000269|PubMed:16710414,
FT ECO:0000269|PubMed:9750192"
FT /id="VAR_031716"
FT VARIANT 402
FT /note="L -> S (in dbSNP:rs1059828)"
FT /evidence="ECO:0000269|PubMed:8195233"
FT /id="VAR_031717"
FT VARIANT 658
FT /note="V -> A (in dbSNP:rs866149312)"
FT /id="VAR_060153"
FT CONFLICT 109
FT /note="Missing (in Ref. 1; AAA19594/AAA19595)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="P -> R (in Ref. 2; AAC72087)"
FT /evidence="ECO:0000305"
FT CONFLICT 312..314
FT /note="Missing (in Ref. 1; AAA19594/AAA19595 and 2;
FT AAC72084/AAC72085/AAC72086/AAC72087/AAC72090)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="E -> D (in Ref. 1; AAA19585/AAA19594/AAA19595)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="K -> N (in Ref. 1; AAA19585/AAA19594/AAA19595)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="E -> R (in Ref. 1; AAA19585/AAA19594/AAA19595)"
FT /evidence="ECO:0000305"
FT CONFLICT 682
FT /note="D -> E (in Ref. 1; AAA19585/AAA19594/AAA19595)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9UQ88-2:109
FT /note="C -> R (in Ref. 1; AAA19594)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9UQ88-2:112
FT /note="H -> R (in Ref. 1; AAA19594)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9UQ88-3:158
FT /note="F -> V (in Ref. 1; AAA19595)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 783 AA; 91362 MW; 1BCF67EB180F37C6 CRC64;
MGDEKDSWKV KTLDEILQEK KRRKEQEEKA EIKRLKNSDD RDSKRDSLEE GELRDHCMEI
TIRNSPYRRE DSMEDRGEED DSLAIKPPQQ MSRKEKVHHR KDEKRKEKWK HARVKEREHE
RRKRHREEQD KARREWERQK RREMAREHSR RERDRLEQLE RKRERERKMR EQQKEQREQK
ERERRAEERR KEREARREVS AHHRTMREDY SDKVKASHWS RSPPRPPRER FELGDGRKPG
EARPAPAQKP AQLKEEKMEE RDLLSDLQDI SDSERKTSSA ESSSAESGSG SEEEEEEEEE
EEEEGSTSEE SEEEEEEEEE EEEETGSNSE EASEQSAEEV SEEEMSEDEE RENENHLLVV
PESRFDRDSG ESEEAEEEVG EGTPQSSALT EGDYVPDSPA LLPIELKQEL PKYLPALQGC
RSVEEFQCLN RIEEGTYGVV YRAKDKKTDE IVALKRLKME KEKEGFPITS LREINTILKA
QHPNIVTVRE IVVGSNMDKI YIVMNYVEHD LKSLMETMKQ PFLPGEVKTL MIQLLRGVKH
LHDNWILHRD LKTSNLLLSH AGILKVGDFG LAREYGSPLK AYTPVVVTQW YRAPELLLGA
KEYSTAVDMW SVGCIFGELL TQKPLFPGNS EIDQINKVFK ELGTPSEKIW PGYSELPVVK
KMTFSEHPYN NLRKRFGALL SDQGFDLMNK FLTYFPGRRI SAEDGLKHEY FRETPLPIDP
SMFPTWPAKS EQQRVKRGTS PRPPEGGLGY SQLGDDDLKE TGFHLTTTNQ GASAAGPGFS
LKF
