CD11B_HUMAN
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 03-AUG-2022, entry version 228.
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.88.6.2612d;
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 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 -!- 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};
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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 AlphaFoldDB; P21127; -.
DR SMR; P21127; -.
DR BioGRID; 107421; 117.
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; 31.
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 EPD; P21127; -.
DR jPOST; P21127; -.
DR MassIVE; P21127; -.
DR MaxQB; P21127; -.
DR PaxDb; P21127; -.
DR PeptideAtlas; P21127; -.
DR PRIDE; 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 Antibodypedia; 62301; 125 antibodies from 20 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 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; MLDNWDD; -.
DR OrthoDB; 925637at2759; -.
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; 43 hits in 260 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 93 other tissues.
DR ExpressionAtlas; P21127; baseline and differential.
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; IBA:GO_Central.
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; 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: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; Isopeptide bond; Kinase; Nucleotide-binding;
KW 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/
FT 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; AAA19582/AAA19583/AAA19584/
FT 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; AAA19582/AAA19581/AAA19583/
FT 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"
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
