Full text data of CDK13
CDK13
(CDC2L, CDC2L5, CHED, KIAA1791)
[Confidence: low (only semi-automatic identification from reviews)]
Cyclin-dependent kinase 13; 2.7.11.22; 2.7.11.23 (CDC2-related protein kinase 5; Cell division cycle 2-like protein kinase 5; Cell division protein kinase 13; hCDK13; Cholinesterase-related cell division controller)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cyclin-dependent kinase 13; 2.7.11.22; 2.7.11.23 (CDC2-related protein kinase 5; Cell division cycle 2-like protein kinase 5; Cell division protein kinase 13; hCDK13; Cholinesterase-related cell division controller)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q14004
ID CDK13_HUMAN Reviewed; 1512 AA.
AC Q14004; Q53G78; Q6DKQ9; Q75MH4; Q75MH5; Q96JN4; Q9H4A0; Q9H4A1;
read moreAC Q9UDR4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 22-JAN-2014, entry version 138.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS LEU-700
RP AND 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.,
RA Picard A., 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;
RP GLN-410; 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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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
RT homolog 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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large 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
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1246, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling 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.,
RA Weil D., 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,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP FUNCTION, AND INTERACTION WITH HIV-1 TAT.
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 MASS
RP SPECTROMETRY.
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
RT the 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
RP AND THR-871, AND MASS SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1048, AND MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Price D.H., Adelman K., Lis J.T., Greenleaf A.L.;
RT "CDK12 is a transcription elongation-associated CTD kinase, the
RT metazoan 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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.,
RA Porman A.M., Evans B., Rekawek P., Kluempers V., Mutter M.,
RA 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 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 MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP VARIANTS [LARGE SCALE ANALYSIS] ALA-494; ALA-500; ARG-670 AND
RP MET-1170.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Cyclin-dependent kinase which displays CTD kinase
CC activity and is required for RNA splicing. Has CTD kinase activity
CC by hyperphosphorylating the C-terminal heptapeptide repeat domain
CC (CTD) of the largest RNA polymerase II subunit RPB1, thereby
CC acting as a key regulator of transcription elongation. Required
CC for RNA splicing, probably by phosphorylating SRSF1/SF2. Required
CC during hematopoiesis. In case of infection by HIV-1 virus,
CC interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-
CC 51', thereby increasing HIV-1 mRNA splicing and promoting the
CC production of the doubly spliced HIV-1 protein Nef.
CC -!- CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP +
CC [DNA-directed RNA polymerase] phosphate.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- SUBUNIT: Interacts with CCNL1 and CCNL2 (By similarity). Interacts
CC with C1QBP. Interacts with HIV-1 Tat.
CC -!- INTERACTION:
CC Q07021:C1QBP; NbExp=6; IntAct=EBI-6375898, EBI-347528;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle.
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
CC tumors.
CC -!- RNA EDITING: Modified_positions=103; Note=Edited at about 88%.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC Ser/Thr protein kinase family. CDC2/CDKX subfamily.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58424.1; Type=Frameshift; Positions=1006;
CC Sequence=AAS07490.1; Type=Erroneous gene model prediction;
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 PIR; A38197; A38197.
DR RefSeq; NP_003709.3; NM_003718.4.
DR RefSeq; NP_112557.2; NM_031267.3.
DR UniGene; Hs.233552; -.
DR ProteinModelPortal; Q14004; -.
DR SMR; Q14004; 677-1031.
DR IntAct; Q14004; 5.
DR MINT; MINT-1197921; -.
DR STRING; 9606.ENSP00000181839; -.
DR BindingDB; Q14004; -.
DR ChEMBL; CHEMBL1795192; -.
DR GuidetoPHARMACOLOGY; 1966; -.
DR PhosphoSite; Q14004; -.
DR DMDM; 66774048; -.
DR PaxDb; Q14004; -.
DR PRIDE; Q14004; -.
DR DNASU; 8621; -.
DR Ensembl; ENST00000181839; ENSP00000181839; ENSG00000065883.
DR Ensembl; ENST00000340829; ENSP00000340557; ENSG00000065883.
DR GeneID; 8621; -.
DR KEGG; hsa:8621; -.
DR UCSC; uc003thh.4; human.
DR CTD; 8621; -.
DR GeneCards; GC07P039957; -.
DR HGNC; HGNC:1733; CDK13.
DR MIM; 603309; gene.
DR neXtProt; NX_Q14004; -.
DR PharmGKB; PA26264; -.
DR eggNOG; COG0515; -.
DR HOVERGEN; HBG050851; -.
DR InParanoid; Q14004; -.
DR KO; K08819; -.
DR OMA; NVAPVKT; -.
DR OrthoDB; EOG76DTSM; -.
DR PhylomeDB; Q14004; -.
DR SignaLink; Q14004; -.
DR GeneWiki; CDC2L5; -.
DR GenomeRNAi; 8621; -.
DR NextBio; 32303; -.
DR PMAP-CutDB; Q14004; -.
DR PRO; PR:Q14004; -.
DR Bgee; Q14004; -.
DR CleanEx; HS_CDC2L5; -.
DR Genevestigator; Q14004; -.
DR GO; GO:0002945; C:cyclin K-CDK13 complex; IPI:MGI.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008353; F:RNA polymerase II carboxy-terminal domain 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:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0007088; P:regulation of mitosis; TAS:ProtInc.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR002290; Ser/Thr_dual-sp_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; 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 Acetylation; Alternative splicing; ATP-binding; Complete proteome;
KW Host-virus interaction; Kinase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; RNA editing; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1 1512 Cyclin-dependent kinase 13.
FT /FTId=PRO_0000085711.
FT DOMAIN 705 998 Protein kinase.
FT NP_BIND 711 719 ATP (By similarity).
FT ACT_SITE 837 837 Proton acceptor (By similarity).
FT BINDING 734 734 ATP (By similarity).
FT MOD_RES 315 315 Phosphoserine.
FT MOD_RES 317 317 Phosphoserine.
FT MOD_RES 325 325 Phosphoserine.
FT MOD_RES 340 340 Phosphoserine.
FT MOD_RES 342 342 Phosphoserine.
FT MOD_RES 383 383 Phosphoserine.
FT MOD_RES 395 395 Phosphoserine.
FT MOD_RES 397 397 Phosphoserine.
FT MOD_RES 400 400 Phosphoserine.
FT MOD_RES 437 437 Phosphoserine.
FT MOD_RES 439 439 Phosphoserine.
FT MOD_RES 525 525 Phosphoserine.
FT MOD_RES 556 556 N6-acetyllysine.
FT MOD_RES 871 871 Phosphothreonine.
FT MOD_RES 1048 1048 Phosphoserine.
FT MOD_RES 1246 1246 Phosphothreonine.
FT VAR_SEQ 1079 1138 Missing (in isoform 2).
FT /FTId=VSP_013579.
FT VARIANT 103 103 Q -> R (in RNA edited version).
FT /FTId=VAR_066526.
FT VARIANT 340 340 S -> F (in dbSNP:rs13622).
FT /FTId=VAR_053926.
FT VARIANT 356 356 P -> A (in dbSNP:rs17537669).
FT /FTId=VAR_022381.
FT VARIANT 403 403 L -> F (in dbSNP:rs3735137).
FT /FTId=VAR_022382.
FT VARIANT 410 410 R -> Q (in dbSNP:rs17496261).
FT /FTId=VAR_022383.
FT VARIANT 494 494 T -> A (in dbSNP:rs34624759).
FT /FTId=VAR_041965.
FT VARIANT 500 500 T -> A (in dbSNP:rs3735135).
FT /FTId=VAR_022384.
FT VARIANT 624 624 S -> G (in dbSNP:rs17496275).
FT /FTId=VAR_022385.
FT VARIANT 670 670 T -> R (in dbSNP:rs34775357).
FT /FTId=VAR_041966.
FT VARIANT 700 700 R -> L (in dbSNP:rs1057000).
FT /FTId=VAR_022386.
FT VARIANT 1062 1062 V -> M (in dbSNP:rs17496712).
FT /FTId=VAR_022387.
FT VARIANT 1170 1170 V -> M (in dbSNP:rs3204309).
FT /FTId=VAR_041967.
FT CONFLICT 21 21 K -> R (in Ref. 1; CAC10400/CAC10401).
FT CONFLICT 671 671 A -> T (in Ref. 1; CAC10400/CAC10401 and
FT 4; AAA58424).
FT CONFLICT 810 810 N -> Y (in Ref. 4; AAA58424).
FT CONFLICT 862 866 YSSEE -> FSVFF (in Ref. 5; BAB47420).
FT CONFLICT 1180 1180 Q -> R (in Ref. 5; BAD96773).
FT CONFLICT 1356 1356 G -> E (in Ref. 5; BAD96773).
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
//
ID CDK13_HUMAN Reviewed; 1512 AA.
AC Q14004; Q53G78; Q6DKQ9; Q75MH4; Q75MH5; Q96JN4; Q9H4A0; Q9H4A1;
read moreAC Q9UDR4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 22-JAN-2014, entry version 138.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS LEU-700
RP AND 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.,
RA Picard A., 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;
RP GLN-410; 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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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
RT homolog 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.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large 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
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1246, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling 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.,
RA Weil D., 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,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP FUNCTION, AND INTERACTION WITH HIV-1 TAT.
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 MASS
RP SPECTROMETRY.
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
RT the 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
RP AND THR-871, AND MASS SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1048, AND MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Price D.H., Adelman K., Lis J.T., Greenleaf A.L.;
RT "CDK12 is a transcription elongation-associated CTD kinase, the
RT metazoan 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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.,
RA Porman A.M., Evans B., Rekawek P., Kluempers V., Mutter M.,
RA 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 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 MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP VARIANTS [LARGE SCALE ANALYSIS] ALA-494; ALA-500; ARG-670 AND
RP MET-1170.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Cyclin-dependent kinase which displays CTD kinase
CC activity and is required for RNA splicing. Has CTD kinase activity
CC by hyperphosphorylating the C-terminal heptapeptide repeat domain
CC (CTD) of the largest RNA polymerase II subunit RPB1, thereby
CC acting as a key regulator of transcription elongation. Required
CC for RNA splicing, probably by phosphorylating SRSF1/SF2. Required
CC during hematopoiesis. In case of infection by HIV-1 virus,
CC interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-
CC 51', thereby increasing HIV-1 mRNA splicing and promoting the
CC production of the doubly spliced HIV-1 protein Nef.
CC -!- CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP +
CC [DNA-directed RNA polymerase] phosphate.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- SUBUNIT: Interacts with CCNL1 and CCNL2 (By similarity). Interacts
CC with C1QBP. Interacts with HIV-1 Tat.
CC -!- INTERACTION:
CC Q07021:C1QBP; NbExp=6; IntAct=EBI-6375898, EBI-347528;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle.
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
CC tumors.
CC -!- RNA EDITING: Modified_positions=103; Note=Edited at about 88%.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC Ser/Thr protein kinase family. CDC2/CDKX subfamily.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58424.1; Type=Frameshift; Positions=1006;
CC Sequence=AAS07490.1; Type=Erroneous gene model prediction;
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 PIR; A38197; A38197.
DR RefSeq; NP_003709.3; NM_003718.4.
DR RefSeq; NP_112557.2; NM_031267.3.
DR UniGene; Hs.233552; -.
DR ProteinModelPortal; Q14004; -.
DR SMR; Q14004; 677-1031.
DR IntAct; Q14004; 5.
DR MINT; MINT-1197921; -.
DR STRING; 9606.ENSP00000181839; -.
DR BindingDB; Q14004; -.
DR ChEMBL; CHEMBL1795192; -.
DR GuidetoPHARMACOLOGY; 1966; -.
DR PhosphoSite; Q14004; -.
DR DMDM; 66774048; -.
DR PaxDb; Q14004; -.
DR PRIDE; Q14004; -.
DR DNASU; 8621; -.
DR Ensembl; ENST00000181839; ENSP00000181839; ENSG00000065883.
DR Ensembl; ENST00000340829; ENSP00000340557; ENSG00000065883.
DR GeneID; 8621; -.
DR KEGG; hsa:8621; -.
DR UCSC; uc003thh.4; human.
DR CTD; 8621; -.
DR GeneCards; GC07P039957; -.
DR HGNC; HGNC:1733; CDK13.
DR MIM; 603309; gene.
DR neXtProt; NX_Q14004; -.
DR PharmGKB; PA26264; -.
DR eggNOG; COG0515; -.
DR HOVERGEN; HBG050851; -.
DR InParanoid; Q14004; -.
DR KO; K08819; -.
DR OMA; NVAPVKT; -.
DR OrthoDB; EOG76DTSM; -.
DR PhylomeDB; Q14004; -.
DR SignaLink; Q14004; -.
DR GeneWiki; CDC2L5; -.
DR GenomeRNAi; 8621; -.
DR NextBio; 32303; -.
DR PMAP-CutDB; Q14004; -.
DR PRO; PR:Q14004; -.
DR Bgee; Q14004; -.
DR CleanEx; HS_CDC2L5; -.
DR Genevestigator; Q14004; -.
DR GO; GO:0002945; C:cyclin K-CDK13 complex; IPI:MGI.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008353; F:RNA polymerase II carboxy-terminal domain 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:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0007088; P:regulation of mitosis; TAS:ProtInc.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR002290; Ser/Thr_dual-sp_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; 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 Acetylation; Alternative splicing; ATP-binding; Complete proteome;
KW Host-virus interaction; Kinase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; RNA editing; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1 1512 Cyclin-dependent kinase 13.
FT /FTId=PRO_0000085711.
FT DOMAIN 705 998 Protein kinase.
FT NP_BIND 711 719 ATP (By similarity).
FT ACT_SITE 837 837 Proton acceptor (By similarity).
FT BINDING 734 734 ATP (By similarity).
FT MOD_RES 315 315 Phosphoserine.
FT MOD_RES 317 317 Phosphoserine.
FT MOD_RES 325 325 Phosphoserine.
FT MOD_RES 340 340 Phosphoserine.
FT MOD_RES 342 342 Phosphoserine.
FT MOD_RES 383 383 Phosphoserine.
FT MOD_RES 395 395 Phosphoserine.
FT MOD_RES 397 397 Phosphoserine.
FT MOD_RES 400 400 Phosphoserine.
FT MOD_RES 437 437 Phosphoserine.
FT MOD_RES 439 439 Phosphoserine.
FT MOD_RES 525 525 Phosphoserine.
FT MOD_RES 556 556 N6-acetyllysine.
FT MOD_RES 871 871 Phosphothreonine.
FT MOD_RES 1048 1048 Phosphoserine.
FT MOD_RES 1246 1246 Phosphothreonine.
FT VAR_SEQ 1079 1138 Missing (in isoform 2).
FT /FTId=VSP_013579.
FT VARIANT 103 103 Q -> R (in RNA edited version).
FT /FTId=VAR_066526.
FT VARIANT 340 340 S -> F (in dbSNP:rs13622).
FT /FTId=VAR_053926.
FT VARIANT 356 356 P -> A (in dbSNP:rs17537669).
FT /FTId=VAR_022381.
FT VARIANT 403 403 L -> F (in dbSNP:rs3735137).
FT /FTId=VAR_022382.
FT VARIANT 410 410 R -> Q (in dbSNP:rs17496261).
FT /FTId=VAR_022383.
FT VARIANT 494 494 T -> A (in dbSNP:rs34624759).
FT /FTId=VAR_041965.
FT VARIANT 500 500 T -> A (in dbSNP:rs3735135).
FT /FTId=VAR_022384.
FT VARIANT 624 624 S -> G (in dbSNP:rs17496275).
FT /FTId=VAR_022385.
FT VARIANT 670 670 T -> R (in dbSNP:rs34775357).
FT /FTId=VAR_041966.
FT VARIANT 700 700 R -> L (in dbSNP:rs1057000).
FT /FTId=VAR_022386.
FT VARIANT 1062 1062 V -> M (in dbSNP:rs17496712).
FT /FTId=VAR_022387.
FT VARIANT 1170 1170 V -> M (in dbSNP:rs3204309).
FT /FTId=VAR_041967.
FT CONFLICT 21 21 K -> R (in Ref. 1; CAC10400/CAC10401).
FT CONFLICT 671 671 A -> T (in Ref. 1; CAC10400/CAC10401 and
FT 4; AAA58424).
FT CONFLICT 810 810 N -> Y (in Ref. 4; AAA58424).
FT CONFLICT 862 866 YSSEE -> FSVFF (in Ref. 5; BAB47420).
FT CONFLICT 1180 1180 Q -> R (in Ref. 5; BAD96773).
FT CONFLICT 1356 1356 G -> E (in Ref. 5; BAD96773).
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
//
MIM
603309
*RECORD*
*FIELD* NO
603309
*FIELD* TI
*603309 CYCLIN-DEPENDENT KINASE 13; CDK13
;;CELL DIVISION CYCLE 2-LIKE 5; CDC2L5;;
read moreCELL DIVISION CONTROLLER, CHOLINESTERASE-RELATED; CHED
*FIELD* TX
DESCRIPTION
CDK13 forms a complex with cyclin K (CCNK; 603544) and is predicted to
have a role in gene regulation (Blazek et al., 2011).
CLONING
Lapidot-Lifson et al. (1992) cloned a glioblastoma cDNA encoding a
protein related to the S. pombe cdc2 kinase. They designated the
predicted 418-amino acid protein CHED, for cholinesterase-related cell
division controller. The CHED protein shares 34 to 42% sequence identity
with human CDC2 (116940), S. cerevisiae Cdc28, and S. pombe Cdc2, 3
functionally interchangeable proteins. Northern blot analysis revealed
that CHED is expressed as 2.2- to 2.3-kb mRNAs in several fetal tissues
and tumor cell lines.
GENE FUNCTION
Using an antisense oligonucleotide, Lapidot-Lifson et al. (1992) found
that reduced CHED expression selectively inhibited megakaryocyte
development in murine bone marrow cultures but did not prevent other
hematopoietic pathways. Antisense mRNA inhibition of BCHE (177400)
expression had a similar effect. The authors suggested that CHED and
BCHE are interrelated components responsive to cholinergic signals in
the hematopoietic pathway. They stated that a link between cholinergic
signaling and cell division might be mediated through individual CDC
proteins in a cell lineage-specific manner.
Using mass spectrometric techniques and reciprocal immunoprecipitation
analysis with HEK293 cells, Blazek et al. (2011) found that CYCK
interacted with CDK12 (615514) and CDK13 in separate protein complexes.
Microarray and RT-PCR analyses showed that knockdown of CYCK or CDK12,
but not CDK13, altered expression of long complex genes and induced DNA
damage and cell-cycle checkpoint. Blazek et al. (2011) concluded that
the CYCK-CDK12 and CYCK-CDK13 complexes have unique functions in gene
regulation.
MAPPING
Gross (2012) mapped the CDK13 gene to chromosome 7p14.1 based on an
alignment of the CDK13 sequence (GenBank GENBANK AJ297709) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Blazek, D.; Kohoutek, J.; Bartholomeeusen, K.; Johansen, E.; Hulinkova,
P.; Luo, Z.; Cimermancic, P.; Ule, J.; Peterlin, B. M.: The cyclin
K/Cdk12 complex maintains genomic stability via regulation of expression
of DNA damage response genes. Genes Dev. 25: 2158-2172, 2011.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 6/29/2012.
3. Lapidot-Lifson, Y.; Patinkin, D.; Prody, C. A.; Ehrlich, G.; Seidman,
S.; Ben-Aziz, R.; Benseler, F.; Eckstein, F.; Zakut, H.; Soreq, H.
: Cloning and antisense oligodeoxynucleotide inhibition of a human
homolog of cdc2 required in hematopoiesis. Proc. Nat. Acad. Sci. 89:
579-583, 1992.
*FIELD* CN
Patricia A. Hartz - updated: 11/5/2013
Matthew B. Gross - updated: 6/29/2012
*FIELD* CD
Rebekah S. Rasooly: 11/23/1998
*FIELD* ED
mgross: 11/20/2013
mcolton: 11/5/2013
mgross: 6/29/2012
carol: 6/21/2012
mgross: 1/18/2000
alopez: 11/23/1998
*RECORD*
*FIELD* NO
603309
*FIELD* TI
*603309 CYCLIN-DEPENDENT KINASE 13; CDK13
;;CELL DIVISION CYCLE 2-LIKE 5; CDC2L5;;
read moreCELL DIVISION CONTROLLER, CHOLINESTERASE-RELATED; CHED
*FIELD* TX
DESCRIPTION
CDK13 forms a complex with cyclin K (CCNK; 603544) and is predicted to
have a role in gene regulation (Blazek et al., 2011).
CLONING
Lapidot-Lifson et al. (1992) cloned a glioblastoma cDNA encoding a
protein related to the S. pombe cdc2 kinase. They designated the
predicted 418-amino acid protein CHED, for cholinesterase-related cell
division controller. The CHED protein shares 34 to 42% sequence identity
with human CDC2 (116940), S. cerevisiae Cdc28, and S. pombe Cdc2, 3
functionally interchangeable proteins. Northern blot analysis revealed
that CHED is expressed as 2.2- to 2.3-kb mRNAs in several fetal tissues
and tumor cell lines.
GENE FUNCTION
Using an antisense oligonucleotide, Lapidot-Lifson et al. (1992) found
that reduced CHED expression selectively inhibited megakaryocyte
development in murine bone marrow cultures but did not prevent other
hematopoietic pathways. Antisense mRNA inhibition of BCHE (177400)
expression had a similar effect. The authors suggested that CHED and
BCHE are interrelated components responsive to cholinergic signals in
the hematopoietic pathway. They stated that a link between cholinergic
signaling and cell division might be mediated through individual CDC
proteins in a cell lineage-specific manner.
Using mass spectrometric techniques and reciprocal immunoprecipitation
analysis with HEK293 cells, Blazek et al. (2011) found that CYCK
interacted with CDK12 (615514) and CDK13 in separate protein complexes.
Microarray and RT-PCR analyses showed that knockdown of CYCK or CDK12,
but not CDK13, altered expression of long complex genes and induced DNA
damage and cell-cycle checkpoint. Blazek et al. (2011) concluded that
the CYCK-CDK12 and CYCK-CDK13 complexes have unique functions in gene
regulation.
MAPPING
Gross (2012) mapped the CDK13 gene to chromosome 7p14.1 based on an
alignment of the CDK13 sequence (GenBank GENBANK AJ297709) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Blazek, D.; Kohoutek, J.; Bartholomeeusen, K.; Johansen, E.; Hulinkova,
P.; Luo, Z.; Cimermancic, P.; Ule, J.; Peterlin, B. M.: The cyclin
K/Cdk12 complex maintains genomic stability via regulation of expression
of DNA damage response genes. Genes Dev. 25: 2158-2172, 2011.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 6/29/2012.
3. Lapidot-Lifson, Y.; Patinkin, D.; Prody, C. A.; Ehrlich, G.; Seidman,
S.; Ben-Aziz, R.; Benseler, F.; Eckstein, F.; Zakut, H.; Soreq, H.
: Cloning and antisense oligodeoxynucleotide inhibition of a human
homolog of cdc2 required in hematopoiesis. Proc. Nat. Acad. Sci. 89:
579-583, 1992.
*FIELD* CN
Patricia A. Hartz - updated: 11/5/2013
Matthew B. Gross - updated: 6/29/2012
*FIELD* CD
Rebekah S. Rasooly: 11/23/1998
*FIELD* ED
mgross: 11/20/2013
mcolton: 11/5/2013
mgross: 6/29/2012
carol: 6/21/2012
mgross: 1/18/2000
alopez: 11/23/1998