ID CD11B_HUMAN Reviewed; 795 AA. AC P21127; B7ZVY7; J3KTL7; J3QR29; J3QR44; O95265; Q12817; Q12818; Q12819; AC Q12820; Q12822; Q8N530; Q9NZS5; Q9UBJ0; Q9UBQ1; Q9UBR0; Q9UNY2; Q9UP57; AC Q9UP58; Q9UP59; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2018, sequence version 4. DT 27-MAR-2024, entry version 237. DE RecName: Full=Cyclin-dependent kinase 11B; DE EC=2.7.11.22; DE AltName: Full=Cell division cycle 2-like protein kinase 1; DE Short=CLK-1; DE AltName: Full=Cell division protein kinase 11B; DE AltName: Full=Galactosyltransferase-associated protein kinase p58/GTA; DE AltName: Full=PITSLRE serine/threonine-protein kinase CDC2L1; DE AltName: Full=p58 CLK-1; GN Name=CDK11B; Synonyms=CDC2L1, CDK11, PITSLREA, PK58; 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] (ISOFORM 7), AND FUNCTION. RC TISSUE=Liver; RX PubMed=2217177; DOI=10.1073/pnas.87.19.7467; RA Bunnell B.A., Heath L.S., Adams D.E., Lahti J.M., Kidd V.J.; RT "Increased expression of a 58-kDa protein kinase leads to changes in the RT CHO cell cycle."; RL Proc. Natl. Acad. Sci. U.S.A. 87:7467-7471(1990). RN [2] RP ERRATUM OF PUBMED:2217177, AND SEQUENCE REVISION. RX PubMed=2006197; DOI=10.1073/pnas.88.6.2612-e; RA Bunnell B.A., Heath L.S., Adams D.E., Lahti J.M., Kidd V.J.; RL Proc. Natl. Acad. Sci. U.S.A. 88:2612-2612(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 7), AND VARIANT GLN-601. RC TISSUE=Hematopoietic; RX PubMed=1639388; DOI=10.1016/0888-7543(92)90132-c; RA Eipers P.G., Lahti J.M., Kidd V.J.; RT "Structure and expression of the human p58clk-1 protein kinase chromosomal RT gene."; RL Genomics 13:613-621(1992). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SV1; 2; 3; 8 AND SV11), VARIANT RP CYS-57, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS SV1; SV4; SV5; SV9; SV10 RP AND SV11), AND TISSUE SPECIFICITY. 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SV11). RC TISSUE=Placenta; RA Govindan M.V., Warriar N.; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SV1). RC TISSUE=Brain; 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 [9] RP INTERACTION WITH RNPS1. RX PubMed=9580558; DOI=10.1242/jcs.111.11.1495; RA Loyer P., Trembley J.H., Lahti J.M., Kidd V.J.; RT "The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2- RT related PITSLRE protein kinases in vivo."; RL J. Cell Sci. 111:1495-1506(1998). RN [10] RP ALTERNATIVE INITIATION (ISOFORM 7), 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 [11] RP INTERACTION WITH RANBP9, AUTOPHOSPHORYLATION, AND SUBCELLULAR LOCATION. RX PubMed=14511641; DOI=10.1016/j.bbrc.2003.08.116; RA Mikolajczyk M., Shi J., Vaillancourt R.R., Sachs N.A., Nelson M.; RT "The cyclin-dependent kinase 11(p46) isoform interacts with RanBPM."; RL Biochem. Biophys. Res. Commun. 310:14-18(2003). RN [12] 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 [13] 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). RN [14] RP PHOSPHORYLATION AT SER-115. RX PubMed=15883043; DOI=10.1016/j.bbrc.2005.04.078; RA Feng Y., Qi W., Martinez J., Nelson M.A.; RT "The cyclin-dependent kinase 11 interacts with 14-3-3 proteins."; RL Biochem. Biophys. Res. Commun. 331:1503-1509(2005). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-595, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [17] RP PHOSPHORYLATION AT SER-482 AND THR-488 BY CDK7. RX PubMed=16327805; DOI=10.1038/nsmb1028; RA Larochelle S., Batliner J., Gamble M.J., Barboza N.M., Kraybill B.C., RA Blethrow J.D., Shokat K.M., Fisher R.P.; RT "Dichotomous but stringent substrate selection by the dual-function Cdk7 RT complex revealed by chemical genetics."; RL Nat. Struct. Mol. Biol. 13:55-62(2006). RN [18] RP FUNCTION, AND INTERACTION WITH CCNL1 AND CCNL2. RX PubMed=18216018; DOI=10.1074/jbc.m708188200; RA Loyer P., Trembley J.H., Grenet J.A., Busson A., Corlu A., Zhao W., RA Kocak M., Kidd V.J., Lahti J.M.; RT "Characterization of cyclin L1 and L2 interactions with CDK11 and splicing RT factors: influence of cyclin L isoforms on splice site selection."; RL J. Biol. Chem. 283:7721-7732(2008). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-594 AND THR-595, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589 AND THR-595, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-595, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-595, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-595, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [26] RP INTERACTION WITH MYO18A. RX PubMed=25965346; DOI=10.1371/journal.pone.0126576; RA Yang L., Carrillo M., Wu Y.M., DiAngelo S.L., Silveyra P., Umstead T.M., RA Halstead E.S., Davies M.L., Hu S., Floros J., McCormack F.X., RA Christensen N.D., Chroneos Z.C.; RT "SP-R210 (Myo18A) isoforms as intrinsic modulators of macrophage priming RT and activation."; RL PLoS ONE 10:E0126576-E0126576(2015). RN [27] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-641, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [28] RP INTERACTION WITH HHV-1 TRANSCRIPTIONAL REGULATOR ICP22 (MICROBIAL RP INFECTION). RX PubMed=34696162; DOI=10.3390/vaccines9101054; RA Isa N.F., Bensaude O., Aziz N.C., Murphy S.; RT "HSV-1 ICP22 Is a Selective Viral Repressor of Cellular RNA Polymerase II- RT Mediated Transcription Elongation."; RL Vaccines (Basel) 9:0-0(2021). RN [29] RP VARIANTS [LARGE SCALE ANALYSIS] CYS-57; TRP-201; LEU-414; ALA-452; VAL-463; RP SER-506; GLN-601; ASN-641 AND VAL-670. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). 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. Isoform 7 may act as a negative regulator of normal CC cell cycle progression. {ECO:0000269|PubMed:12501247, CC ECO:0000269|PubMed:12624090, ECO:0000269|PubMed:18216018, CC ECO:0000269|PubMed:2217177}. 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-448 or Tyr-449 inactivates CC the enzyme, while phosphorylation at Thr-595 activates it. CC {ECO:0000250|UniProtKB:P06493}. CC -!- SUBUNIT: Cleaved isoform SV9 (p110C) binds to the serine/threonine CC kinase PAK1 and RANBP9. p110C interacts with RNPS1. Isoform 7, but not CC isoform SV9, nor its cleavage product p110C, interacts with CCND3. CC Interacts with CCNL1 and CCNL2. Forms complexes with pre-mRNA-splicing CC factors, including at least SRSF1, SRSF2 and SRSF7/SLU7. Interacts with CC isoform 5 of MYO18A (PubMed:25965346). {ECO:0000269|PubMed:12501247, CC ECO:0000269|PubMed:12624090, ECO:0000269|PubMed:14511641, CC ECO:0000269|PubMed:25965346, ECO:0000269|PubMed:9580558}. CC -!- SUBUNIT: (Microbial infection) Interacts with human herpes virus 1 CC (HHV-1) transcriptional regulator ICP22. {ECO:0000269|PubMed:34696162}. CC -!- INTERACTION: CC P21127; O00303: EIF3F; NbExp=3; IntAct=EBI-1298, EBI-711990; CC P21127; Q13153: PAK1; NbExp=4; IntAct=EBI-1298, EBI-1307; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=10; CC Name=SV9; Synonyms=CDK11-p110; CC IsoId=P21127-1; Sequence=Displayed; CC Name=SV1; Synonyms=Alpha 2-1; CC IsoId=P21127-2; Sequence=VSP_008280; CC Name=2; Synonyms=Alpha 2-2; CC IsoId=P21127-3; Sequence=VSP_008278, VSP_008279, VSP_008280; CC Name=3; Synonyms=Alpha 1; CC IsoId=P21127-4; Sequence=VSP_008276; CC Name=SV4; CC IsoId=P21127-5; Sequence=VSP_008275; CC Name=SV5; CC IsoId=P21127-6; Sequence=VSP_008273, VSP_008277, VSP_008278, CC VSP_008280; CC Name=8; Synonyms=Alpha 2-3; CC IsoId=P21127-8; Sequence=VSP_008278, VSP_008280; CC Name=SV10; CC IsoId=P21127-9; Sequence=VSP_008273, VSP_008277, VSP_008280; CC Name=SV11; Synonyms=Alpha 2-4; CC IsoId=P21127-10; Sequence=VSP_008274, VSP_008280; CC Name=7; Synonyms=CDK11-p58; CC IsoId=P21127-12; Sequence=VSP_018834; CC -!- TISSUE SPECIFICITY: Expressed ubiquitously. Some evidence of isoform- CC specific tissue distribution. {ECO:0000269|PubMed:8195233, CC ECO:0000269|PubMed:9750192}. CC -!- INDUCTION: Isoform 7 is induced in G2/M phase of the cell cycle. CC {ECO:0000269|PubMed:10882096}. CC -!- PTM: During FAS- or TNF-induced apoptosis, isoform SV9 is cleaved by CC caspases to produce p110C, a fragment that contains the C-terminal CC kinase domain. CC -!- PTM: Phosphorylation at Ser-115 creates a binding site for 14-3-3 CC proteins. p110C can be autophosphorylated. CC {ECO:0000269|PubMed:15883043, ECO:0000269|PubMed:16327805}. 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 7]: Produced by alternative initiation at Met- CC 357 of isoform SV9 via an internal ribosomal entry site (IRES). CC {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=AAB59449.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=AAC83664.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=AAF36538.1; 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; M37712; AAA36406.1; -; mRNA. DR EMBL; M88563; AAB59449.1; ALT_SEQ; Genomic_DNA. DR EMBL; M88553; AAB59449.1; JOINED; Genomic_DNA. DR EMBL; M88554; AAB59449.1; JOINED; Genomic_DNA. DR EMBL; M88555; AAB59449.1; JOINED; Genomic_DNA. DR EMBL; M88558; AAB59449.1; JOINED; Genomic_DNA. DR EMBL; M88559; AAB59449.1; JOINED; Genomic_DNA. DR EMBL; M88560; AAB59449.1; JOINED; Genomic_DNA. DR EMBL; M88561; AAB59449.1; JOINED; Genomic_DNA. DR EMBL; M88562; AAB59449.1; JOINED; Genomic_DNA. DR EMBL; U04815; AAA19581.1; -; mRNA. DR EMBL; U04816; AAA19582.1; -; mRNA. DR EMBL; U04817; AAA19583.1; -; mRNA. DR EMBL; U04818; AAA19584.1; -; mRNA. DR EMBL; U04824; AAA19586.1; -; mRNA. DR EMBL; AF067512; AAC72077.1; -; mRNA. DR EMBL; AF067513; AAC72078.1; -; mRNA. DR EMBL; AF067514; AAC72079.1; -; mRNA. DR EMBL; AF067515; AAC72080.1; -; mRNA. DR EMBL; AF067516; AAC72081.1; -; mRNA. DR EMBL; AF067517; AAC72082.1; -; mRNA. DR EMBL; AF080683; AAC83662.1; -; Genomic_DNA. DR EMBL; AF080685; AAC83662.1; JOINED; Genomic_DNA. DR EMBL; AF080686; AAC83662.1; JOINED; Genomic_DNA. DR EMBL; AF080687; AAC83662.1; JOINED; Genomic_DNA. DR EMBL; AF080688; AAC83662.1; JOINED; Genomic_DNA. DR EMBL; AF092429; AAC83662.1; JOINED; Genomic_DNA. DR EMBL; AF092430; AAC83662.1; JOINED; Genomic_DNA. DR EMBL; AF080678; AAC83662.1; JOINED; Genomic_DNA. DR EMBL; AF080679; AAC83662.1; JOINED; Genomic_DNA. DR EMBL; AF080680; AAC83662.1; JOINED; Genomic_DNA. DR EMBL; AF080681; AAC83662.1; JOINED; Genomic_DNA. DR EMBL; AF080682; AAC83662.1; JOINED; Genomic_DNA. DR EMBL; AF080683; AAC83663.1; -; Genomic_DNA. DR EMBL; AF080685; AAC83663.1; JOINED; Genomic_DNA. DR EMBL; AF080686; AAC83663.1; JOINED; Genomic_DNA. DR EMBL; AF080687; AAC83663.1; JOINED; Genomic_DNA. DR EMBL; AF080688; AAC83663.1; JOINED; Genomic_DNA. DR EMBL; AF092429; AAC83663.1; JOINED; Genomic_DNA. DR EMBL; AF092430; AAC83663.1; JOINED; Genomic_DNA. DR EMBL; AF080678; AAC83663.1; JOINED; Genomic_DNA. DR EMBL; AF080679; AAC83663.1; JOINED; Genomic_DNA. DR EMBL; AF080680; AAC83663.1; JOINED; Genomic_DNA. DR EMBL; AF080681; AAC83663.1; JOINED; Genomic_DNA. DR EMBL; AF080682; AAC83663.1; JOINED; Genomic_DNA. DR EMBL; AF080683; AAC83664.1; ALT_SEQ; Genomic_DNA. DR EMBL; AF080685; AAC83664.1; JOINED; Genomic_DNA. DR EMBL; AF080686; AAC83664.1; JOINED; Genomic_DNA. DR EMBL; AF080687; AAC83664.1; JOINED; Genomic_DNA. DR EMBL; AF080688; AAC83664.1; JOINED; Genomic_DNA. DR EMBL; AF092429; AAC83664.1; JOINED; Genomic_DNA. DR EMBL; AF092430; AAC83664.1; JOINED; Genomic_DNA. DR EMBL; AF080678; AAC83664.1; JOINED; Genomic_DNA. DR EMBL; AF080679; AAC83664.1; JOINED; Genomic_DNA. DR EMBL; AF080680; AAC83664.1; JOINED; Genomic_DNA. DR EMBL; AF080681; AAC83664.1; JOINED; Genomic_DNA. DR EMBL; AF080682; AAC83664.1; JOINED; Genomic_DNA. DR EMBL; AF080683; AAC83665.1; -; Genomic_DNA. DR EMBL; AF080685; AAC83665.1; JOINED; Genomic_DNA. DR EMBL; AF080686; AAC83665.1; JOINED; Genomic_DNA. DR EMBL; AF080687; AAC83665.1; JOINED; Genomic_DNA. DR EMBL; AF080688; AAC83665.1; JOINED; Genomic_DNA. DR EMBL; AF092429; AAC83665.1; JOINED; Genomic_DNA. DR EMBL; AF092430; AAC83665.1; JOINED; Genomic_DNA. DR EMBL; AF080678; AAC83665.1; JOINED; Genomic_DNA. DR EMBL; AF080679; AAC83665.1; JOINED; Genomic_DNA. DR EMBL; AF080680; AAC83665.1; JOINED; Genomic_DNA. DR EMBL; AF080681; AAC83665.1; JOINED; Genomic_DNA. DR EMBL; AF080682; AAC83665.1; JOINED; Genomic_DNA. DR EMBL; AF080683; AAC83666.1; -; Genomic_DNA. DR EMBL; AF092430; AAC83666.1; JOINED; Genomic_DNA. DR EMBL; AF080678; AAC83666.1; JOINED; Genomic_DNA. DR EMBL; AF080679; AAC83666.1; JOINED; Genomic_DNA. DR EMBL; AF080680; AAC83666.1; JOINED; Genomic_DNA. DR EMBL; AF080681; AAC83666.1; JOINED; Genomic_DNA. DR EMBL; AF080682; AAC83666.1; JOINED; Genomic_DNA. DR EMBL; AF174497; AAF36538.1; ALT_INIT; mRNA. DR EMBL; FO704657; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC140714; AAI40715.1; -; mRNA. DR EMBL; BC171773; AAI71773.1; -; mRNA. DR CCDS; CCDS72682.1; -. [P21127-9] DR CCDS; CCDS72683.1; -. [P21127-1] DR CCDS; CCDS72684.1; -. [P21127-2] DR PIR; A38282; A38282. DR PIR; B54024; B54024. DR PIR; E54024; E54024. DR PIR; F54024; F54024. DR PIR; H54024; H54024. DR PIR; T09568; T09568. DR RefSeq; NP_001278274.1; NM_001291345.1. [P21127-8] DR RefSeq; NP_001778.2; NM_001787.2. [P21127-1] DR RefSeq; NP_277021.2; NM_033486.2. [P21127-2] DR RefSeq; NP_277022.1; NM_033487.2. [P21127-5] DR RefSeq; NP_277024.2; NM_033489.2. [P21127-9] DR RefSeq; NP_277025.1; NM_033490.2. [P21127-10] DR RefSeq; XP_016858415.1; XM_017002926.1. [P21127-3] DR PDB; 7UKZ; X-ray; 2.60 A; A/B/C/D/E/F=428-736. DR PDBsum; 7UKZ; -. DR AlphaFoldDB; P21127; -. DR SMR; P21127; -. DR BioGRID; 107421; 179. DR ComplexPortal; CPX-345; Cyclin L2-CDK11B(p58) complex. [P21127-12] DR ComplexPortal; CPX-346; Cyclin L1-CDK11B(p58) complex. [P21127-12] DR ComplexPortal; CPX-348; Cyclin L1-CDK11B(p110) complex. [P21127-1] DR ComplexPortal; CPX-349; Cyclin L2-CDK11B(p110) complex. [P21127-1] DR CORUM; P21127; -. DR IntAct; P21127; 32. DR MINT; P21127; -. DR STRING; 9606.ENSP00000464036; -. DR BindingDB; P21127; -. DR ChEMBL; CHEMBL5808; -. DR DrugCentral; P21127; -. DR GlyGen; P21127; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P21127; -. DR PhosphoSitePlus; P21127; -. DR BioMuta; CDK11B; -. DR DMDM; 34978359; -. DR CPTAC; non-CPTAC-6016; -. DR EPD; P21127; -. DR jPOST; P21127; -. DR MassIVE; P21127; -. DR MaxQB; P21127; -. DR PaxDb; 9606-ENSP00000464036; -. DR PeptideAtlas; P21127; -. DR ProteomicsDB; 53836; -. [P21127-1] DR ProteomicsDB; 53837; -. [P21127-10] DR ProteomicsDB; 53838; -. [P21127-12] DR ProteomicsDB; 53839; -. [P21127-2] DR ProteomicsDB; 53840; -. [P21127-3] DR ProteomicsDB; 53841; -. [P21127-4] DR ProteomicsDB; 53842; -. [P21127-5] DR ProteomicsDB; 53843; -. [P21127-6] DR ProteomicsDB; 53844; -. [P21127-8] DR ProteomicsDB; 53845; -. [P21127-9] DR Pumba; P21127; -. DR Antibodypedia; 62301; 158 antibodies from 21 providers. DR DNASU; 984; -. DR Ensembl; ENST00000340677.9; ENSP00000464016.2; ENSG00000248333.9. [P21127-9] DR Ensembl; ENST00000341832.11; ENSP00000463048.2; ENSG00000248333.9. [P21127-2] DR Ensembl; ENST00000407249.7; ENSP00000464036.2; ENSG00000248333.9. [P21127-1] DR GeneID; 984; -. DR KEGG; hsa:984; -. DR MANE-Select; ENST00000341832.11; ENSP00000463048.2; NM_033486.3; NP_277021.2. [P21127-2] DR UCSC; uc031tmi.2; human. DR AGR; HGNC:1729; -. DR CTD; 984; -. DR DisGeNET; 984; -. DR GeneCards; CDK11B; -. DR HGNC; HGNC:1729; CDK11B. DR HPA; ENSG00000248333; Low tissue specificity. DR MIM; 176873; gene. DR neXtProt; NX_P21127; -. DR OpenTargets; ENSG00000248333; -. DR PharmGKB; PA26262; -. DR VEuPathDB; HostDB:ENSG00000248333; -. DR eggNOG; KOG0663; Eukaryota. DR GeneTree; ENSGT00940000158459; -. DR InParanoid; P21127; -. DR OMA; EGYYNVM; -. DR OrthoDB; 244018at2759; -. DR PhylomeDB; P21127; -. DR TreeFam; TF101035; -. DR BRENDA; 2.7.11.22; 2681. DR PathwayCommons; P21127; -. DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes. DR SignaLink; P21127; -. DR SIGNOR; P21127; -. DR BioGRID-ORCS; 984; 46 hits in 316 CRISPR screens. DR ChiTaRS; CDK11B; human. DR GeneWiki; CDC2L1; -. DR GenomeRNAi; 984; -. DR Pharos; P21127; Tchem. DR PRO; PR:P21127; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P21127; Protein. DR Bgee; ENSG00000248333; Expressed in sural nerve and 95 other cell types or tissues. DR ExpressionAtlas; P21127; baseline and differential. DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISS:ComplexPortal. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. 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; IEA:UniProtKB-EC. DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc. 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:0003723; F:RNA binding; HDA: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; NAS:ComplexPortal. DR GO; GO:0051726; P:regulation of cell cycle; NAS:ComplexPortal. DR GO; GO:0001558; P:regulation of cell growth; IEP:UniProtKB. DR GO; GO:0046605; P:regulation of centrosome cycle; NAS:ComplexPortal. DR GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:UniProtKB. 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; ISS:ComplexPortal. 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 3D-structure; Alternative initiation; Alternative splicing; Apoptosis; KW ATP-binding; Cell cycle; Cytoplasm; Isopeptide bond; Kinase; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase; Ubl conjugation. FT CHAIN 1..795 FT /note="Cyclin-dependent kinase 11B" FT /id="PRO_0000024311" FT DOMAIN 438..723 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 17..412 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 733..795 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 17..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..251 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 262..288 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 300..362 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 363..382 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 562 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 444..452 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 467 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 115 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15883043" FT MOD_RES 283 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P24788" FT MOD_RES 482 FT /note="Phosphoserine; by CDK7" FT /evidence="ECO:0000269|PubMed:16327805" FT MOD_RES 488 FT /note="Phosphothreonine; by CDK7" FT /evidence="ECO:0000269|PubMed:16327805" FT MOD_RES 589 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 594 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 595 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 751 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P24788" FT MOD_RES 752 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P24788" FT CROSSLNK 641 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..356 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:2217177" FT /id="VSP_018834" FT VAR_SEQ 1..269 FT /note="Missing (in isoform SV4)" FT /evidence="ECO:0000303|PubMed:9750192" FT /id="VSP_008275" FT VAR_SEQ 1..217 FT /note="Missing (in isoform SV11)" FT /evidence="ECO:0000303|PubMed:8195233, FT ECO:0000303|PubMed:9750192, ECO:0000303|Ref.6" FT /id="VSP_008274" FT VAR_SEQ 1..34 FT /note="Missing (in isoform SV5 and isoform SV10)" FT /evidence="ECO:0000303|PubMed:16710414, FT ECO:0000303|PubMed:9750192" FT /id="VSP_008273" FT VAR_SEQ 2..335 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:8195233" FT /id="VSP_008276" FT VAR_SEQ 35..37 FT /note="LKN -> MSQ (in isoform SV5 and isoform SV10)" FT /evidence="ECO:0000303|PubMed:9750192" FT /id="VSP_008277" FT VAR_SEQ 110..119 FT /note="Missing (in isoform 2, isoform SV5 and isoform 8)" FT /evidence="ECO:0000303|PubMed:8195233, FT ECO:0000303|PubMed:9750192" FT /id="VSP_008278" FT VAR_SEQ 165 FT /note="R -> RGNDGVCLFR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8195233" FT /id="VSP_008279" FT VAR_SEQ 252..265 FT /note="GEARPAPAQKPAQL -> V (in isoform SV1, isoform 2, FT isoform SV5, isoform 8, isoform SV10 and isoform SV11)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16710414, ECO:0000303|PubMed:8195233, FT ECO:0000303|PubMed:9750192, ECO:0000303|Ref.6" FT /id="VSP_008280" FT VARIANT 57 FT /note="R -> C (in dbSNP:rs752740049)" FT /evidence="ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:8195233" FT /id="VAR_041958" FT VARIANT 93 FT /note="R -> W (in dbSNP:rs1059831)" FT /id="VAR_057775" FT VARIANT 109 FT /note="R -> C (in dbSNP:rs1059830)" FT /id="VAR_062199" FT VARIANT 201 FT /note="R -> W (in dbSNP:rs1557687207)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041959" FT VARIANT 414 FT /note="S -> L (in dbSNP:rs1241694892)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041960" FT VARIANT 452 FT /note="V -> A" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_045577" FT VARIANT 463 FT /note="I -> V" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041961" FT VARIANT 506 FT /note="G -> S" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_045578" FT VARIANT 601 FT /note="L -> Q (in dbSNP:rs200190129)" FT /evidence="ECO:0000269|PubMed:1639388, FT ECO:0000269|PubMed:17344846" FT /id="VAR_041962" FT VARIANT 641 FT /note="K -> N (in dbSNP:rs1059815)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041963" FT VARIANT 670 FT /note="A -> V (in dbSNP:rs1059811)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041964" FT CONFLICT 97 FT /note="A -> V (in Ref. 4; AAA19582/AAA19583/AAA19586 and 5; FT AAC72077/AAC72079/AAC72080/AAC72081/AAC83662/AAC83664/AAC83665)" FT CONFLICT 109 FT /note="Missing (in Ref. 4; AAA19582/AAA19583 and 5; FT AAC72079)" FT /evidence="ECO:0000305" FT CONFLICT 126 FT /note="E -> K (in Ref. 4; AAA19582/AAA19583/AAA19586)" FT /evidence="ECO:0000305" FT CONFLICT 258 FT /note="P -> R (in Ref. 5; AAC72080)" FT CONFLICT 320 FT /note="S -> T (in Ref. 6; AAF36538)" FT /evidence="ECO:0000305" FT CONFLICT 324..326 FT /note="Missing (in Ref. 4; FT AAA19582/AAA19583/AAA19584/AAA19586 and 6; AAF36538)" FT /evidence="ECO:0000305" FT CONFLICT 411..412 FT /note="PA -> LP (in Ref. 3; AAB59449)" FT /evidence="ECO:0000305" FT CONFLICT 436 FT /note="E -> D (in Ref. 3; AAB59449)" FT /evidence="ECO:0000305" FT CONFLICT 560 FT /note="H -> Q (in Ref. 6; AAF36538)" FT /evidence="ECO:0000305" FT CONFLICT 567 FT /note="N -> T (in Ref. 6; AAF36538)" FT /evidence="ECO:0000305" FT CONFLICT 678 FT /note="E -> R (in Ref. 4; FT AAA19582/AAA19581/AAA19583/AAA19584 and 6; AAF36538)" FT /evidence="ECO:0000305" FT CONFLICT 694 FT /note="D -> E (in Ref. 3; AAB59449)" FT /evidence="ECO:0000305" FT CONFLICT 697 FT /note="F -> C (in Ref. 6; AAF36538)" FT /evidence="ECO:0000305" FT CONFLICT 712 FT /note="I -> L (in Ref. 3; AAB59449)" FT /evidence="ECO:0000305" FT CONFLICT 715 FT /note="E -> Q (in Ref. 3; AAB59449)" FT /evidence="ECO:0000305" FT CONFLICT 792 FT /note="S -> R (in Ref. 6; AAF36538)" FT /evidence="ECO:0000305" FT STRAND 442..447 FT /evidence="ECO:0007829|PDB:7UKZ" FT STRAND 450..456 FT /evidence="ECO:0007829|PDB:7UKZ" FT STRAND 463..468 FT /evidence="ECO:0007829|PDB:7UKZ" FT HELIX 480..491 FT /evidence="ECO:0007829|PDB:7UKZ" FT STRAND 500..506 FT /evidence="ECO:0007829|PDB:7UKZ" FT TURN 507..510 FT /evidence="ECO:0007829|PDB:7UKZ" FT STRAND 511..517 FT /evidence="ECO:0007829|PDB:7UKZ" FT STRAND 520..522 FT /evidence="ECO:0007829|PDB:7UKZ" FT HELIX 523..528 FT /evidence="ECO:0007829|PDB:7UKZ" FT HELIX 536..555 FT /evidence="ECO:0007829|PDB:7UKZ" FT HELIX 565..567 FT /evidence="ECO:0007829|PDB:7UKZ" FT STRAND 568..570 FT /evidence="ECO:0007829|PDB:7UKZ" FT STRAND 576..578 FT /evidence="ECO:0007829|PDB:7UKZ" FT HELIX 601..603 FT /evidence="ECO:0007829|PDB:7UKZ" FT HELIX 606..609 FT /evidence="ECO:0007829|PDB:7UKZ" FT HELIX 618..633 FT /evidence="ECO:0007829|PDB:7UKZ" FT HELIX 643..654 FT /evidence="ECO:0007829|PDB:7UKZ" FT TURN 659..661 FT /evidence="ECO:0007829|PDB:7UKZ" FT TURN 663..667 FT /evidence="ECO:0007829|PDB:7UKZ" FT HELIX 669..672 FT /evidence="ECO:0007829|PDB:7UKZ" FT STRAND 674..676 FT /evidence="ECO:0007829|PDB:7UKZ" FT TURN 689..691 FT /evidence="ECO:0007829|PDB:7UKZ" FT HELIX 694..703 FT /evidence="ECO:0007829|PDB:7UKZ" FT TURN 708..710 FT /evidence="ECO:0007829|PDB:7UKZ" FT HELIX 714..718 FT /evidence="ECO:0007829|PDB:7UKZ" FT HELIX 721..724 FT /evidence="ECO:0007829|PDB:7UKZ" FT STRAND 725..727 FT /evidence="ECO:0007829|PDB:7UKZ" FT HELIX 732..734 FT /evidence="ECO:0007829|PDB:7UKZ" SQ SEQUENCE 795 AA; 92620 MW; 8CCB0E688E66DF47 CRC64; MGDEKDSWKV KTLDEILQEK KRRKEQEEKA EIKRLKNSDD RDSKRDSLEE GELRDHRMEI TIRNSPYRRE DSMEDRGEED DSLAIKPPQQ MSRKEKAHHR KDEKRKEKRR HRSHSAEGGK HARVKEKERE HERRKRHREE QDKARREWER QKRREMAREH SRRERDRLEQ LERKRERERK MREQQKEQRE QKERERRAEE RRKEREARRE VSAHHRTMRE DYSDKVKASH WSRSPPRPPR ERFELGDGRK PGEARPAPAQ KPAQLKEEKM EERDLLSDLQ DISDSERKTS SAESSSAESG SGSEEEEEEE EEEEEEGSTS EESEEEEEEE EEEEEETGSN SEEASEQSAE EVSEEEMSED EERENENHLL VVPESRFDRD SGESEEAEEE VGEGTPQSSA LTEGDYVPDS PALSPIELKQ ELPKYLPALQ GCRSVEEFQC LNRIEEGTYG VVYRAKDKKT DEIVALKRLK MEKEKEGFPI TSLREINTIL KAQHPNIVTV REIVVGSNMD KIYIVMNYVE HDLKSLMETM KQPFLPGEVK TLMIQLLRGV KHLHDNWILH RDLKTSNLLL SHAGILKVGD FGLAREYGSP LKAYTPVVVT LWYRAPELLL GAKEYSTAVD MWSVGCIFGE LLTQKPLFPG KSEIDQINKV FKDLGTPSEK IWPGYSELPA VKKMTFSEHP YNNLRKRFGA LLSDQGFDLM NKFLTYFPGR RISAEDGLKH EYFRETPLPI DPSMFPTWPA KSEQQRVKRG TSPRPPEGGL GYSQLGDDDL KETGFHLTTT NQGASAAGPG FSLKF //