CDK13_HUMAN
ID CDK13_HUMAN Reviewed; 1512 AA.
AC Q14004; Q53G78; Q6DKQ9; Q75MH4; Q75MH5; Q96JN4; Q9H4A0; Q9H4A1; Q9UDR4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Cyclin-dependent kinase 13;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
DE AltName: Full=CDC2-related protein kinase 5;
DE AltName: Full=Cell division cycle 2-like protein kinase 5;
DE AltName: Full=Cell division protein kinase 13;
DE Short=hCDK13;
DE AltName: Full=Cholinesterase-related cell division controller;
GN Name=CDK13; Synonyms=CDC2L, CDC2L5, CHED, KIAA1791;
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 1 AND 2), AND VARIANTS LEU-700 AND
RP MET-1170.
RC TISSUE=Placenta;
RX PubMed=11162436; DOI=10.1006/bbrc.2000.4042;
RA Marques F., Moreau J.L., Peaucellier G., Lozano J.C., Schatt P., Picard A.,
RA Callebaut I., Perre E., Geneviere A.M.;
RT "A new subfamily of high molecular mass CDC2-related kinases with
RT PITAI/VRE.";
RL Biochem. Biophys. Res. Commun. 279:832-837(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-356; PHE-403; GLN-410;
RP ALA-500; GLY-624 AND MET-1062.
RG NIEHS SNPs program;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 361-1078, FUNCTION, AND VARIANT LEU-700.
RC TISSUE=Glioblastoma;
RX PubMed=1731328; DOI=10.1073/pnas.89.2.579;
RA Lapidot-Lifson Y., Patinkin D., Prody C.A., Ehrlich G., Seidman S.,
RA Ben-Aziz R., Benseler F., Eckstein F., Zakut H., Soreq H.;
RT "Cloning and antisense oligodeoxynucleotide inhibition of a human homolog
RT of cdc2 required in hematopoiesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:579-583(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 856-1512 (ISOFORM 2).
RC TISSUE=Thyroid;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 860-1512 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1246, AND IDENTIFICATION BY
RP 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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH C1QBP.
RX PubMed=16721827; DOI=10.1002/jcb.20986;
RA Even Y., Durieux S., Escande M.L., Lozano J.C., Peaucellier G., Weil D.,
RA Geneviere A.M.;
RT "CDC2L5, a Cdk-like kinase with RS domain, interacts with the ASF/SF2-
RT associated protein p32 and affects splicing in vivo.";
RL J. Cell. Biochem. 99:890-904(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
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 [12]
RP FUNCTION, AND INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION).
RX PubMed=18480452; DOI=10.1128/jvi.02543-07;
RA Berro R., Pedati C., Kehn-Hall K., Wu W., Klase Z., Even Y.,
RA Geneviere A.M., Ammosova T., Nekhai S., Kashanchi F.;
RT "CDK13, a new potential human immunodeficiency virus type 1 inhibitory
RT factor regulating viral mRNA splicing.";
RL J. Virol. 82:7155-7166(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1246, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-317; SER-325;
RP SER-340; SER-342; SER-383; SER-395; SER-397; SER-400; SER-437; SER-439 AND
RP THR-871, AND 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1048, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [17]
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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-556, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [19]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20952539; DOI=10.1101/gad.1968210;
RA Bartkowiak B., Liu P., Phatnani H.P., Fuda N.J., Cooper J.J., Price D.H.,
RA Adelman K., Lis J.T., Greenleaf A.L.;
RT "CDK12 is a transcription elongation-associated CTD kinase, the metazoan
RT ortholog of yeast Ctk1.";
RL Genes Dev. 24:2303-2316(2010).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-437; SER-439;
RP SER-525 AND THR-871, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP RNA EDITING OF POSITION 103.
RX PubMed=21835166; DOI=10.1016/j.bbrc.2011.07.075;
RA Maas S., Godfried Sie C.P., Stoev I., Dupuis D.E., Latona J., Porman A.M.,
RA Evans B., Rekawek P., Kluempers V., Mutter M., Gommans W.M., Lopresti D.;
RT "Genome-wide evaluation and discovery of vertebrate A-to-I RNA editing
RT sites.";
RL Biochem. Biophys. Res. Commun. 412:407-412(2011).
RN [23]
RP INTERACTION WITH CCNK.
RX PubMed=22012619; DOI=10.1101/gad.16962311;
RA Blazek D., Kohoutek J., Bartholomeeusen K., Johansen E., Hulinkova P.,
RA Luo Z., Cimermancic P., Ule J., Peterlin B.M.;
RT "The Cyclin K/Cdk12 complex maintains genomic stability via regulation of
RT expression of DNA damage response genes.";
RL Genes Dev. 25:2158-2172(2011).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-317; SER-383;
RP SER-395; SER-397; SER-400; SER-437; SER-439; THR-871 AND THR-1246, AND
RP IDENTIFICATION BY 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-317; SER-325;
RP SER-358; SER-360; SER-383; SER-437; SER-439; SER-525; THR-588; THR-871;
RP SER-1048 AND THR-1246, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [26]
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 [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-519 AND LYS-547, AND
RP IDENTIFICATION BY MASS 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] ALA-494; ALA-500; ARG-670 AND MET-1170.
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).
RN [29]
RP INVOLVEMENT IN CHDFIDD, AND VARIANTS CHDFIDD ARG-714; ARG-717; GLN-751 AND
RP SER-842.
RX PubMed=27479907; DOI=10.1038/ng.3627;
RG INTERVAL Study;
RG UK10K Consortium;
RG Deciphering Developmental Disorders Study;
RA Sifrim A., Hitz M.P., Wilsdon A., Breckpot J., Turki S.H., Thienpont B.,
RA McRae J., Fitzgerald T.W., Singh T., Swaminathan G.J., Prigmore E.,
RA Rajan D., Abdul-Khaliq H., Banka S., Bauer U.M., Bentham J., Berger F.,
RA Bhattacharya S., Bu'Lock F., Canham N., Colgiu I.G., Cosgrove C., Cox H.,
RA Daehnert I., Daly A., Danesh J., Fryer A., Gewillig M., Hobson E., Hoff K.,
RA Homfray T., Kahlert A.K., Ketley A., Kramer H.H., Lachlan K., Lampe A.K.,
RA Louw J.J., Manickara A.K., Manase D., McCarthy K.P., Metcalfe K., Moore C.,
RA Newbury-Ecob R., Omer S.O., Ouwehand W.H., Park S.M., Parker M.J.,
RA Pickardt T., Pollard M.O., Robert L., Roberts D.J., Sambrook J.,
RA Setchfield K., Stiller B., Thornborough C., Toka O., Watkins H.,
RA Williams D., Wright M., Mital S., Daubeney P.E., Keavney B., Goodship J.,
RA Abu-Sulaiman R.M., Klaassen S., Wright C.F., Firth H.V., Barrett J.C.,
RA Devriendt K., FitzPatrick D.R., Brook J.D., Hurles M.E.;
RT "Distinct genetic architectures for syndromic and nonsyndromic congenital
RT heart defects identified by exome sequencing.";
RL Nat. Genet. 48:1060-1065(2016).
RN [30]
RP VARIANTS CHDFIDD GLU-734; ASP-842 AND SER-842.
RX PubMed=28807008; DOI=10.1186/s13073-017-0463-8;
RA Bostwick B.L., McLean S., Posey J.E., Streff H.E., Gripp K.W., Blesson A.,
RA Powell-Hamilton N., Tusi J., Stevenson D.A., Farrelly E., Hudgins L.,
RA Yang Y., Xia F., Wang X., Liu P., Walkiewicz M., McGuire M., Grange D.K.,
RA Andrews M.V., Hummel M., Madan-Khetarpal S., Infante E., Coban-Akdemir Z.,
RA Miszalski-Jamka K., Jefferies J.L., Rosenfeld J.A., Emrick L., Nugent K.M.,
RA Lupski J.R., Belmont J.W., Lee B., Lalani S.R.;
RT "Phenotypic and molecular characterisation of CDK13-related congenital
RT heart defects, dysmorphic facial features and intellectual developmental
RT disorders.";
RL Genome Med. 9:73-73(2017).
CC -!- FUNCTION: Cyclin-dependent kinase which displays CTD kinase activity
CC and is required for RNA splicing. Has CTD kinase activity by
CC hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of
CC the largest RNA polymerase II subunit RPB1, thereby acting as a key
CC regulator of transcription elongation. Required for RNA splicing,
CC probably by phosphorylating SRSF1/SF2. Required during hematopoiesis.
CC In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein
CC acetylated at 'Lys-50' and 'Lys-51', thereby increasing HIV-1 mRNA
CC splicing and promoting the production of the doubly spliced HIV-1
CC protein Nef. {ECO:0000269|PubMed:16721827, ECO:0000269|PubMed:1731328,
CC ECO:0000269|PubMed:18480452, ECO:0000269|PubMed:20952539}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC ChEBI:CHEBI:456216; EC=2.7.11.23;
CC Evidence={ECO:0000269|PubMed:20952539};
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 Evidence={ECO:0000269|PubMed:20952539};
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; Evidence={ECO:0000269|PubMed:20952539};
CC -!- SUBUNIT: Interacts with CCNL1 and CCNL2 (By similarity). Interacts with
CC CCNK. Interacts with C1QBP. {ECO:0000250, ECO:0000269|PubMed:16721827,
CC ECO:0000269|PubMed:22012619}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat.
CC {ECO:0000269|PubMed:18480452}.
CC -!- INTERACTION:
CC Q14004; O75909: CCNK; NbExp=7; IntAct=EBI-968626, EBI-739806;
CC Q14004; Q16543: CDC37; NbExp=2; IntAct=EBI-968626, EBI-295634;
CC Q14004-2; Q07021: C1QBP; NbExp=6; IntAct=EBI-6375898, EBI-347528;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:16721827}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14004-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14004-2; Sequence=VSP_013579;
CC -!- TISSUE SPECIFICITY: Expressed in fetal brain, liver, muscle and in
CC adult brain. Also expressed in neuroblastoma and glioblastoma tumors.
CC -!- RNA EDITING: Modified_positions=103 {ECO:0000269|PubMed:21835166};
CC Note=Edited at about 88%.;
CC -!- DISEASE: Congenital heart defects, dysmorphic facial features, and
CC intellectual developmental disorder (CHDFIDD) [MIM:617360]: An
CC autosomal dominant syndrome characterized by atrial and/or ventricular
CC septal congenital heart defects, facial dysmorphism with hypertelorism,
CC upslanted palpebral fissures, epicanthal folds, ptosis, strabismus,
CC posteriorly rotated ears, thin upper lip, and small mouth. Patients
CC manifest global developmental delay, delayed walking and speech
CC acquisition, and intellectual disability. Some patients have mild
CC microcephaly, a small cerebral cortex, and agenesis of corpus callosum.
CC More variable features include clinodactyly and/or camptodactyly of the
CC fingers, hypotonia, and joint hypermobility.
CC {ECO:0000269|PubMed:27479907, ECO:0000269|PubMed:28807008}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58424.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAS07490.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cdc2l5/";
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DR EMBL; AJ297709; CAC10400.1; -; mRNA.
DR EMBL; AJ297710; CAC10401.1; -; mRNA.
DR EMBL; AY679523; AAT74623.1; -; Genomic_DNA.
DR EMBL; AC072061; AAS07490.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC072061; AAS07491.1; -; Genomic_DNA.
DR EMBL; AC006023; AAD54514.1; -; Genomic_DNA.
DR EMBL; M80629; AAA58424.1; ALT_FRAME; mRNA.
DR EMBL; AK223053; BAD96773.1; -; mRNA.
DR EMBL; AB058694; BAB47420.1; -; mRNA.
DR CCDS; CCDS5461.1; -. [Q14004-1]
DR CCDS; CCDS5462.1; -. [Q14004-2]
DR PIR; A38197; A38197.
DR RefSeq; NP_003709.3; NM_003718.4. [Q14004-1]
DR RefSeq; NP_112557.2; NM_031267.3. [Q14004-2]
DR PDB; 5EFQ; X-ray; 2.00 A; A/C=694-1039.
DR PDB; 7NXJ; X-ray; 2.36 A; A/C=694-1039.
DR PDBsum; 5EFQ; -.
DR PDBsum; 7NXJ; -.
DR AlphaFoldDB; Q14004; -.
DR SMR; Q14004; -.
DR BioGRID; 114176; 109.
DR ComplexPortal; CPX-359; Cyclin K-CDK13 complex.
DR IntAct; Q14004; 58.
DR MINT; Q14004; -.
DR STRING; 9606.ENSP00000181839; -.
DR BindingDB; Q14004; -.
DR ChEMBL; CHEMBL1795192; -.
DR GuidetoPHARMACOLOGY; 1966; -.
DR GlyGen; Q14004; 6 sites, 2 O-linked glycans (6 sites).
DR iPTMnet; Q14004; -.
DR PhosphoSitePlus; Q14004; -.
DR BioMuta; CDK13; -.
DR DMDM; 66774048; -.
DR EPD; Q14004; -.
DR jPOST; Q14004; -.
DR MassIVE; Q14004; -.
DR MaxQB; Q14004; -.
DR PaxDb; Q14004; -.
DR PeptideAtlas; Q14004; -.
DR PRIDE; Q14004; -.
DR ProteomicsDB; 59786; -. [Q14004-1]
DR ProteomicsDB; 59787; -. [Q14004-2]
DR Antibodypedia; 26726; 208 antibodies from 28 providers.
DR DNASU; 8621; -.
DR Ensembl; ENST00000181839.10; ENSP00000181839.4; ENSG00000065883.17. [Q14004-1]
DR Ensembl; ENST00000340829.10; ENSP00000340557.5; ENSG00000065883.17. [Q14004-2]
DR GeneID; 8621; -.
DR KEGG; hsa:8621; -.
DR MANE-Select; ENST00000181839.10; ENSP00000181839.4; NM_003718.5; NP_003709.3.
DR UCSC; uc003thh.5; human. [Q14004-1]
DR CTD; 8621; -.
DR DisGeNET; 8621; -.
DR GeneCards; CDK13; -.
DR GeneReviews; CDK13; -.
DR HGNC; HGNC:1733; CDK13.
DR HPA; ENSG00000065883; Low tissue specificity.
DR MalaCards; CDK13; -.
DR MIM; 603309; gene.
DR MIM; 617360; phenotype.
DR neXtProt; NX_Q14004; -.
DR OpenTargets; ENSG00000065883; -.
DR PharmGKB; PA26264; -.
DR VEuPathDB; HostDB:ENSG00000065883; -.
DR eggNOG; KOG0600; Eukaryota.
DR GeneTree; ENSGT00940000157852; -.
DR HOGENOM; CLU_004166_3_0_1; -.
DR InParanoid; Q14004; -.
DR OrthoDB; 925637at2759; -.
DR PhylomeDB; Q14004; -.
DR TreeFam; TF101060; -.
DR BRENDA; 2.7.11.22; 2681.
DR BRENDA; 2.7.11.23; 2681.
DR PathwayCommons; Q14004; -.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q14004; -.
DR SIGNOR; Q14004; -.
DR BioGRID-ORCS; 8621; 67 hits in 1112 CRISPR screens.
DR ChiTaRS; CDK13; human.
DR GeneWiki; CDC2L5; -.
DR GenomeRNAi; 8621; -.
DR Pharos; Q14004; Tchem.
DR PRO; PR:Q14004; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q14004; protein.
DR Bgee; ENSG00000065883; Expressed in buccal mucosa cell and 211 other tissues.
DR ExpressionAtlas; Q14004; baseline and differential.
DR Genevisible; Q14004; HS.
DR GO; GO:0002945; C:cyclin K-CDK13 complex; IPI:MGI.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0019908; C:nuclear cyclin-dependent protein kinase holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030332; F:cyclin binding; IPI:MGI.
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:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IDA:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; IMP:UniProtKB.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IEA:Ensembl.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009966; P:regulation of signal transduction; IDA:ComplexPortal.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Disease variant; Host-virus interaction; Intellectual disability;
KW Isopeptide bond; Kinase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA editing; Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..1512
FT /note="Cyclin-dependent kinase 13"
FT /id="PRO_0000085711"
FT DOMAIN 705..998
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1468..1512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..60
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..433
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 837
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 711..719
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 734
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 556
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 588
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 871
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1048
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1058
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZA1"
FT MOD_RES 1246
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 519
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 547
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1079..1138
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11162436, ECO:0000303|Ref.5"
FT /id="VSP_013579"
FT VARIANT 103
FT /note="Q -> R (in RNA edited version)"
FT /id="VAR_066526"
FT VARIANT 340
FT /note="S -> F (in dbSNP:rs13622)"
FT /id="VAR_053926"
FT VARIANT 356
FT /note="P -> A (in dbSNP:rs17537669)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_022381"
FT VARIANT 403
FT /note="L -> F (in dbSNP:rs3735137)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_022382"
FT VARIANT 410
FT /note="R -> Q (in dbSNP:rs17496261)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_022383"
FT VARIANT 494
FT /note="T -> A (in dbSNP:rs34624759)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041965"
FT VARIANT 500
FT /note="T -> A (in dbSNP:rs3735135)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.2"
FT /id="VAR_022384"
FT VARIANT 624
FT /note="S -> G (in dbSNP:rs17496275)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_022385"
FT VARIANT 670
FT /note="T -> R (in dbSNP:rs34775357)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041966"
FT VARIANT 700
FT /note="R -> L (in dbSNP:rs1057000)"
FT /evidence="ECO:0000269|PubMed:11162436,
FT ECO:0000269|PubMed:1731328"
FT /id="VAR_022386"
FT VARIANT 714
FT /note="G -> R (in CHDFIDD; dbSNP:rs1057519633)"
FT /evidence="ECO:0000269|PubMed:27479907"
FT /id="VAR_078598"
FT VARIANT 717
FT /note="G -> R (in CHDFIDD; dbSNP:rs1057519632)"
FT /evidence="ECO:0000269|PubMed:27479907"
FT /id="VAR_078599"
FT VARIANT 734
FT /note="K -> E (in CHDFIDD; dbSNP:rs1064795731)"
FT /evidence="ECO:0000269|PubMed:28807008"
FT /id="VAR_079422"
FT VARIANT 751
FT /note="R -> Q (in CHDFIDD; dbSNP:rs1057519634)"
FT /evidence="ECO:0000269|PubMed:27479907"
FT /id="VAR_078600"
FT VARIANT 842
FT /note="N -> D (in CHDFIDD; dbSNP:rs1554333853)"
FT /evidence="ECO:0000269|PubMed:28807008"
FT /id="VAR_079423"
FT VARIANT 842
FT /note="N -> S (in CHDFIDD; dbSNP:rs878853160)"
FT /evidence="ECO:0000269|PubMed:27479907,
FT ECO:0000269|PubMed:28807008"
FT /id="VAR_078601"
FT VARIANT 1062
FT /note="V -> M (in dbSNP:rs17496712)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_022387"
FT VARIANT 1170
FT /note="V -> M (in dbSNP:rs3204309)"
FT /evidence="ECO:0000269|PubMed:11162436,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_041967"
FT CONFLICT 21
FT /note="K -> R (in Ref. 1; CAC10400/CAC10401)"
FT /evidence="ECO:0000305"
FT CONFLICT 671
FT /note="A -> T (in Ref. 1; CAC10400/CAC10401 and 4;
FT AAA58424)"
FT /evidence="ECO:0000305"
FT CONFLICT 810
FT /note="N -> Y (in Ref. 4; AAA58424)"
FT /evidence="ECO:0000305"
FT CONFLICT 862..866
FT /note="YSSEE -> FSVFF (in Ref. 5; BAB47420)"
FT /evidence="ECO:0000305"
FT CONFLICT 1180
FT /note="Q -> R (in Ref. 5; BAD96773)"
FT /evidence="ECO:0000305"
FT CONFLICT 1356
FT /note="G -> E (in Ref. 5; BAD96773)"
FT /evidence="ECO:0000305"
FT HELIX 702..704
FT /evidence="ECO:0007829|PDB:5EFQ"
FT STRAND 705..713
FT /evidence="ECO:0007829|PDB:5EFQ"
FT STRAND 715..724
FT /evidence="ECO:0007829|PDB:5EFQ"
FT TURN 725..727
FT /evidence="ECO:0007829|PDB:5EFQ"
FT STRAND 730..736
FT /evidence="ECO:0007829|PDB:5EFQ"
FT STRAND 739..741
FT /evidence="ECO:0007829|PDB:5EFQ"
FT HELIX 747..758
FT /evidence="ECO:0007829|PDB:5EFQ"
FT STRAND 767..772
FT /evidence="ECO:0007829|PDB:5EFQ"
FT STRAND 787..792
FT /evidence="ECO:0007829|PDB:5EFQ"
FT STRAND 795..797
FT /evidence="ECO:0007829|PDB:5EFQ"
FT HELIX 798..804
FT /evidence="ECO:0007829|PDB:5EFQ"
FT HELIX 811..830
FT /evidence="ECO:0007829|PDB:5EFQ"
FT HELIX 840..842
FT /evidence="ECO:0007829|PDB:5EFQ"
FT STRAND 843..845
FT /evidence="ECO:0007829|PDB:5EFQ"
FT STRAND 851..853
FT /evidence="ECO:0007829|PDB:5EFQ"
FT HELIX 856..858
FT /evidence="ECO:0007829|PDB:5EFQ"
FT STRAND 864..866
FT /evidence="ECO:0007829|PDB:5EFQ"
FT HELIX 877..879
FT /evidence="ECO:0007829|PDB:5EFQ"
FT HELIX 882..885
FT /evidence="ECO:0007829|PDB:5EFQ"
FT HELIX 894..908
FT /evidence="ECO:0007829|PDB:5EFQ"
FT STRAND 909..911
FT /evidence="ECO:0007829|PDB:5EFQ"
FT HELIX 919..930
FT /evidence="ECO:0007829|PDB:5EFQ"
FT TURN 935..937
FT /evidence="ECO:0007829|PDB:5EFQ"
FT HELIX 939..943
FT /evidence="ECO:0007829|PDB:5EFQ"
FT TURN 945..950
FT /evidence="ECO:0007829|PDB:5EFQ"
FT HELIX 960..963
FT /evidence="ECO:0007829|PDB:5EFQ"
FT TURN 964..966
FT /evidence="ECO:0007829|PDB:5EFQ"
FT HELIX 969..978
FT /evidence="ECO:0007829|PDB:5EFQ"
FT TURN 983..985
FT /evidence="ECO:0007829|PDB:5EFQ"
FT HELIX 989..994
FT /evidence="ECO:0007829|PDB:5EFQ"
FT TURN 996..1000
FT /evidence="ECO:0007829|PDB:5EFQ"
FT HELIX 1003..1005
FT /evidence="ECO:0007829|PDB:5EFQ"
FT HELIX 1019..1024
FT /evidence="ECO:0007829|PDB:5EFQ"
FT HELIX 1026..1030
FT /evidence="ECO:0007829|PDB:5EFQ"
SQ SEQUENCE 1512 AA; 164923 MW; 3CA54A3585A2943D CRC64;
MPSSSDTALG GGGGLSWAEK KLEERRKRRR FLSPQQPPLL LPLLQPQLLQ PPPPPPPLLF
LAAPGTAAAA AAAAAASSSC FSPGPPLEVK RLARGKRRAG GRQKRRRGPR AGQEAEKRRV
FSLPQPQQDG GGGASSGGGV TPLVEYEDVS SQSEQGLLLG GASAATAATA AGGTGGSGGS
PASSSGTQRR GEGSERRPRR DRRSSSGRSK ERHREHRRRD GQRGGSEASK SRSRHSHSGE
ERAEVAKSGS SSSSGGRRKS ASATSSSSSS RKDRDSKAHR SRTKSSKEPP SAYKEPPKAY
REDKTEPKAY RRRRSLSPLG GRDDSPVSHR ASQSLRSRKS PSPAGGGSSP YSRRLPRSPS
PYSRRRSPSY SRHSSYERGG DVSPSPYSSS SWRRSRSPYS PVLRRSGKSR SRSPYSSRHS
RSRSRHRLSR SRSRHSSISP STLTLKSSLA AELNKNKKAR AAEAARAAEA AKAAEATKAA
EAAAKAAKAS NTSTPTKGNT ETSASASQTN HVKDVKKIKI EHAPSPSSGG TLKNDKAKTK
PPLQVTKVEN NLIVDKATKK AVIVGKESKS AATKEESVSL KEKTKPLTPS IGAKEKEQHV
ALVTSTLPPL PLPPMLPEDK EADSLRGNIS VKAVKKEVEK KLRCLLADLP LPPELPGGDD
LSKSPEEKKT ATQLHSKRRP KICGPRYGET KEKDIDWGKR CVDKFDIIGI IGEGTYGQVY
KARDKDTGEM VALKKVRLDN EKEGFPITAI REIKILRQLT HQSIINMKEI VTDKEDALDF
KKDKGAFYLV FEYMDHDLMG LLESGLVHFN ENHIKSFMRQ LMEGLDYCHK KNFLHRDIKC
SNILLNNRGQ IKLADFGLAR LYSSEESRPY TNKVITLWYR PPELLLGEER YTPAIDVWSC
GCILGELFTK KPIFQANQEL AQLELISRIC GSPCPAVWPD VIKLPYFNTM KPKKQYRRKL
REEFVFIPAA ALDLFDYMLA LDPSKRCTAE QALQCEFLRD VEPSKMPPPD LPLWQDCHEL
WSKKRRRQKQ MGMTDDVSTI KAPRKDLSLG LDDSRTNTPQ GVLPSSQLKS QGSSNVAPVK
TGPGQHLNHS ELAILLNLLQ SKTSVNMADF VQVLNIKVNS ETQQQLNKIN LPAGILATGE
KQTDPSTPQQ ESSKPLGGIQ PSSQTIQPKV ETDAAQAAVQ SAFAVLLTQL IKAQQSKQKD
VLLEERENGS GHEASLQLRP PPEPSTPVSG QDDLIQHQDM RILELTPEPD RPRILPPDQR
PPEPPEPPPV TEEDLDYRTE NQHVPTTSSS LTDPHAGVKA ALLQLLAQHQ PQDDPKREGG
IDYQAGDTYV STSDYKDNFG SSSFSSAPYV SNDGLGSSSA PPLERRSFIG NSDIQSLDNY
STASSHSGGP PQPSAFSESF PSSVAGYGDI YLNAGPMLFS GDKDHRFEYS HGPIAVLANS
SDPSTGPEST HPLPAKMHNY NYGGNLQENP SGPSLMHGQT WTSPAQGPGY SQGYRGHIST
STGRGRGRGL PY
