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 27-MAR-2024, entry version 217. 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 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] 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 [30] 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 [31] 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: (Microbial infection) Interacts with human herpes virus 1 CC (HHV-1) transcriptional regulator ICP22. {ECO:0000269|PubMed:34696162}. 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/"; 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; 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; 136. DR ComplexPortal; CPX-359; Cyclin K-CDK13 complex. DR IntAct; Q14004; 56. DR MINT; Q14004; -. DR STRING; 9606.ENSP00000181839; -. DR BindingDB; Q14004; -. DR ChEMBL; CHEMBL1795192; -. DR GuidetoPHARMACOLOGY; 1966; -. DR GlyCosmos; Q14004; 6 sites, 2 glycans. DR GlyGen; Q14004; 9 sites, 2 O-linked glycans (9 sites). DR iPTMnet; Q14004; -. DR PhosphoSitePlus; Q14004; -. DR SwissPalm; Q14004; -. DR BioMuta; CDK13; -. DR DMDM; 66774048; -. DR CPTAC; non-CPTAC-2883; -. DR CPTAC; non-CPTAC-2884; -. DR EPD; Q14004; -. DR jPOST; Q14004; -. DR MassIVE; Q14004; -. DR MaxQB; Q14004; -. DR PaxDb; 9606-ENSP00000181839; -. DR PeptideAtlas; Q14004; -. DR ProteomicsDB; 59786; -. [Q14004-1] DR ProteomicsDB; 59787; -. [Q14004-2] DR Pumba; Q14004; -. DR Antibodypedia; 26726; 222 antibodies from 28 providers. DR DNASU; 8621; -. DR Ensembl; ENST00000181839.10; ENSP00000181839.4; ENSG00000065883.18. [Q14004-1] DR Ensembl; ENST00000340829.10; ENSP00000340557.5; ENSG00000065883.18. [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 AGR; HGNC:1733; -. 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 Orphanet; 646278; CDK13-related congenital heart defects-intellectual disability-facial dysmorphism syndrome. 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; 5402490at2759; -. 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; 72 hits in 1189 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 213 other cell types or tissues. DR ExpressionAtlas; Q14004; baseline and differential. DR GO; GO:0002945; C:cyclin K-CDK13 complex; IPI:MGI. 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:HPA. 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; IEA:UniProtKB-EC. 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0009966; P:regulation of signal transduction; IDA:ComplexPortal. DR CDD; cd07864; STKc_CDK12; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR IDEAL; IID00723; -. 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 PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1. DR PANTHER; PTHR24056:SF459; CYCLIN-DEPENDENT KINASE 13; 1. DR Pfam; PF12330; Haspin_kinase; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q14004; HS. 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 //