Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 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)

 CDK13_HUMAN             Reviewed;        1512 AA.
Q14004; Q53G78; Q6DKQ9; Q75MH4; Q75MH5; Q96JN4; Q9H4A0; Q9H4A1;
Q9UDR4;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 2.
25-OCT-2017, entry version 178.
RecName: Full=Cyclin-dependent kinase 13;
EC=2.7.11.22;
EC=2.7.11.23;
AltName: Full=CDC2-related protein kinase 5;
AltName: Full=Cell division cycle 2-like protein kinase 5;
AltName: Full=Cell division protein kinase 13;
Short=hCDK13;
AltName: Full=Cholinesterase-related cell division controller;
Name=CDK13; Synonyms=CDC2L, CDC2L5, CHED, KIAA1791;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS LEU-700
AND MET-1170.
TISSUE=Placenta;
PubMed=11162436; DOI=10.1006/bbrc.2000.4042;
Marques F., Moreau J.L., Peaucellier G., Lozano J.C., Schatt P.,
Picard A., Callebaut I., Perre E., Geneviere A.M.;
"A new subfamily of high molecular mass CDC2-related kinases with
PITAI/VRE.";
Biochem. Biophys. Res. Commun. 279:832-837(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-356; PHE-403;
GLN-410; ALA-500; GLY-624 AND MET-1062.
NIEHS SNPs program;
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 361-1078, FUNCTION, AND VARIANT LEU-700.
TISSUE=Glioblastoma;
PubMed=1731328; DOI=10.1073/pnas.89.2.579;
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. Natl. Acad. Sci. U.S.A. 89:579-583(1992).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 856-1512 (ISOFORM 2).
TISSUE=Thyroid;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 860-1512 (ISOFORM 1).
TISSUE=Brain;
PubMed=11347906; DOI=10.1093/dnares/8.2.85;
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 8:85-95(2001).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1246, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH C1QBP.
PubMed=16721827; DOI=10.1002/jcb.20986;
Even Y., Durieux S., Escande M.L., Lozano J.C., Peaucellier G.,
Weil D., Geneviere A.M.;
"CDC2L5, a Cdk-like kinase with RS domain, interacts with the ASF/SF2-
associated protein p32 and affects splicing in vivo.";
J. Cell. Biochem. 99:890-904(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[12]
FUNCTION, AND INTERACTION WITH HIV-1 TAT.
PubMed=18480452; DOI=10.1128/JVI.02543-07;
Berro R., Pedati C., Kehn-Hall K., Wu W., Klase Z., Even Y.,
Geneviere A.M., Ammosova T., Nekhai S., Kashanchi F.;
"CDK13, a new potential human immunodeficiency virus type 1 inhibitory
factor regulating viral mRNA splicing.";
J. Virol. 82:7155-7166(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1246, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-317; SER-325;
SER-340; SER-342; SER-383; SER-395; SER-397; SER-400; SER-437; SER-439
AND THR-871, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1048, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-556, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[19]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=20952539; DOI=10.1101/gad.1968210;
Bartkowiak B., Liu P., Phatnani H.P., Fuda N.J., Cooper J.J.,
Price D.H., Adelman K., Lis J.T., Greenleaf A.L.;
"CDK12 is a transcription elongation-associated CTD kinase, the
metazoan ortholog of yeast Ctk1.";
Genes Dev. 24:2303-2316(2010).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-437; SER-439;
SER-525 AND THR-871, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
RNA EDITING OF POSITION 103.
PubMed=21835166; DOI=10.1016/j.bbrc.2011.07.075;
Maas S., Godfried Sie C.P., Stoev I., Dupuis D.E., Latona J.,
Porman A.M., Evans B., Rekawek P., Kluempers V., Mutter M.,
Gommans W.M., Lopresti D.;
"Genome-wide evaluation and discovery of vertebrate A-to-I RNA editing
sites.";
Biochem. Biophys. Res. Commun. 412:407-412(2011).
[23]
INTERACTION WITH CCNK.
PubMed=22012619; DOI=10.1101/gad.16962311;
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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-317; SER-383;
SER-395; SER-397; SER-400; SER-437; SER-439; THR-871 AND THR-1246, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-317; SER-325;
SER-358; SER-360; SER-383; SER-437; SER-439; SER-525; THR-588;
THR-871; SER-1048 AND THR-1246, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-519 AND LYS-547, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[28]
VARIANTS [LARGE SCALE ANALYSIS] ALA-494; ALA-500; ARG-670 AND
MET-1170.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[29]
INVOLVEMENT IN CHDFIDD, AND VARIANTS CHDFIDD ARG-714; ARG-717; GLN-751
AND SER-842.
PubMed=27479907; DOI=10.1038/ng.3627;
INTERVAL Study;
UK10K Consortium;
Deciphering Developmental Disorders Study;
Sifrim A., Hitz M.P., Wilsdon A., Breckpot J., Turki S.H.,
Thienpont B., McRae J., Fitzgerald T.W., Singh T., Swaminathan G.J.,
Prigmore E., Rajan D., Abdul-Khaliq H., Banka S., Bauer U.M.,
Bentham J., Berger F., Bhattacharya S., Bu'Lock F., Canham N.,
Colgiu I.G., Cosgrove C., Cox H., Daehnert I., Daly A., Danesh J.,
Fryer A., Gewillig M., Hobson E., Hoff K., Homfray T., Kahlert A.K.,
Ketley A., Kramer H.H., Lachlan K., Lampe A.K., Louw J.J.,
Manickara A.K., Manase D., McCarthy K.P., Metcalfe K., Moore C.,
Newbury-Ecob R., Omer S.O., Ouwehand W.H., Park S.M., Parker M.J.,
Pickardt T., Pollard M.O., Robert L., Roberts D.J., Sambrook J.,
Setchfield K., Stiller B., Thornborough C., Toka O., Watkins H.,
Williams D., Wright M., Mital S., Daubeney P.E., Keavney B.,
Goodship J., Abu-Sulaiman R.M., Klaassen S., Wright C.F., Firth H.V.,
Barrett J.C., Devriendt K., FitzPatrick D.R., Brook J.D., Hurles M.E.;
"Distinct genetic architectures for syndromic and nonsyndromic
congenital heart defects identified by exome sequencing.";
Nat. Genet. 48:1060-1065(2016).
-!- FUNCTION: Cyclin-dependent kinase which displays CTD kinase
activity and is required for RNA splicing. Has CTD kinase activity
by hyperphosphorylating the C-terminal heptapeptide repeat domain
(CTD) of the largest RNA polymerase II subunit RPB1, thereby
acting as a key regulator of transcription elongation. Required
for RNA splicing, probably by phosphorylating SRSF1/SF2. Required
during hematopoiesis. In case of infection by HIV-1 virus,
interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-
51', thereby increasing HIV-1 mRNA splicing and promoting the
production of the doubly spliced HIV-1 protein Nef.
{ECO:0000269|PubMed:16721827, ECO:0000269|PubMed:1731328,
ECO:0000269|PubMed:18480452, ECO:0000269|PubMed:20952539}.
-!- CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP +
[DNA-directed RNA polymerase] phosphate.
{ECO:0000269|PubMed:20952539}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:20952539}.
-!- SUBUNIT: Interacts with CCNL1 and CCNL2 (By similarity). Interacts
with CCNK. Interacts with C1QBP. Interacts with HIV-1 Tat.
{ECO:0000250, ECO:0000269|PubMed:16721827,
ECO:0000269|PubMed:18480452, ECO:0000269|PubMed:22012619}.
-!- INTERACTION:
Q07021:C1QBP; NbExp=6; IntAct=EBI-6375898, EBI-347528;
O75909:CCNK; NbExp=6; IntAct=EBI-968626, EBI-739806;
-!- SUBCELLULAR LOCATION: Nucleus speckle
{ECO:0000269|PubMed:16721827}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q14004-1; Sequence=Displayed;
Name=2;
IsoId=Q14004-2; Sequence=VSP_013579;
-!- TISSUE SPECIFICITY: Expressed in fetal brain, liver, muscle and in
adult brain. Also expressed in neuroblastoma and glioblastoma
tumors.
-!- RNA EDITING: Modified_positions=103 {ECO:0000269|PubMed:21835166};
Note=Edited at about 88%.;
-!- DISEASE: Congenital heart defects, dysmorphic facial features, and
intellectual developmental disorder (CHDFIDD) [MIM:617360]: An
autosomal dominant syndrome characterized by atrial and/or
ventricular septal congenital heart defects, facial dysmorphism
with hypertelorism, upslanted palpebral fissures, epicanthal
folds, ptosis, strabismus, posteriorly rotated ears, thin upper
lip, and small mouth. Patients manifest global developmental
delay, delayed walking and speech acquisition, and intellectual
disability. Some patients have mild microcephaly, a small cerebral
cortex, and agenesis of corpus callosum. More variable features
include clinodactyly and/or camptodactyly of the fingers,
hypotonia, and joint hypermobility. {ECO:0000269|PubMed:27479907}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA58424.1; Type=Frameshift; Positions=1006; Evidence={ECO:0000305};
Sequence=AAS07490.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdc2l5/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ297709; CAC10400.1; -; mRNA.
EMBL; AJ297710; CAC10401.1; -; mRNA.
EMBL; AY679523; AAT74623.1; -; Genomic_DNA.
EMBL; AC072061; AAS07490.1; ALT_SEQ; Genomic_DNA.
EMBL; AC072061; AAS07491.1; -; Genomic_DNA.
EMBL; AC006023; AAD54514.1; -; Genomic_DNA.
EMBL; M80629; AAA58424.1; ALT_FRAME; mRNA.
EMBL; AK223053; BAD96773.1; -; mRNA.
EMBL; AB058694; BAB47420.1; -; mRNA.
CCDS; CCDS5461.1; -. [Q14004-1]
CCDS; CCDS5462.1; -. [Q14004-2]
PIR; A38197; A38197.
RefSeq; NP_003709.3; NM_003718.4. [Q14004-1]
RefSeq; NP_112557.2; NM_031267.3. [Q14004-2]
UniGene; Hs.233552; -.
PDB; 5EFQ; X-ray; 2.00 A; A/C=694-1039.
PDBsum; 5EFQ; -.
ProteinModelPortal; Q14004; -.
SMR; Q14004; -.
BioGrid; 114176; 62.
IntAct; Q14004; 15.
MINT; MINT-1197921; -.
STRING; 9606.ENSP00000181839; -.
BindingDB; Q14004; -.
ChEMBL; CHEMBL1795192; -.
GuidetoPHARMACOLOGY; 1966; -.
iPTMnet; Q14004; -.
PhosphoSitePlus; Q14004; -.
BioMuta; CDK13; -.
DMDM; 66774048; -.
EPD; Q14004; -.
MaxQB; Q14004; -.
PaxDb; Q14004; -.
PeptideAtlas; Q14004; -.
PRIDE; Q14004; -.
DNASU; 8621; -.
Ensembl; ENST00000181839; ENSP00000181839; ENSG00000065883. [Q14004-1]
Ensembl; ENST00000340829; ENSP00000340557; ENSG00000065883. [Q14004-2]
GeneID; 8621; -.
KEGG; hsa:8621; -.
UCSC; uc003thh.5; human. [Q14004-1]
CTD; 8621; -.
DisGeNET; 8621; -.
EuPathDB; HostDB:ENSG00000065883.14; -.
GeneCards; CDK13; -.
HGNC; HGNC:1733; CDK13.
HPA; HPA059241; -.
MalaCards; CDK13; -.
MIM; 603309; gene.
MIM; 617360; phenotype.
neXtProt; NX_Q14004; -.
OpenTargets; ENSG00000065883; -.
PharmGKB; PA26264; -.
eggNOG; KOG0600; Eukaryota.
eggNOG; ENOG410XPIR; LUCA.
GeneTree; ENSGT00890000139396; -.
HOVERGEN; HBG050851; -.
InParanoid; Q14004; -.
KO; K08819; -.
OMA; NVAPVKT; -.
OrthoDB; EOG091G08Z8; -.
PhylomeDB; Q14004; -.
TreeFam; TF101060; -.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SignaLink; Q14004; -.
SIGNOR; Q14004; -.
ChiTaRS; CDK13; human.
GeneWiki; CDC2L5; -.
GenomeRNAi; 8621; -.
PMAP-CutDB; Q14004; -.
PRO; PR:Q14004; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000065883; -.
CleanEx; HS_CDC2L5; -.
ExpressionAtlas; Q14004; baseline and differential.
Genevisible; Q14004; HS.
GO; GO:0005694; C:chromosome; IBA:GO_Central.
GO; GO:0002945; C:cyclin K-CDK13 complex; IPI:MGI.
GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0019908; C:nuclear cyclin-dependent protein kinase holoenzyme complex; ISS:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0030332; F:cyclin binding; IPI:MGI.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0008353; F:RNA polymerase II carboxy-terminal domain kinase activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
GO; GO:0030097; P:hemopoiesis; IMP:UniProtKB.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:2000737; P:negative regulation of stem cell differentiation; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0007088; P:regulation of mitotic nuclear division; TAS:ProtInc.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Disease mutation; Host-virus interaction;
Isopeptide bond; Kinase; Mental retardation; mRNA processing;
mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; RNA editing;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
CHAIN 1 1512 Cyclin-dependent kinase 13.
/FTId=PRO_0000085711.
DOMAIN 705 998 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 711 719 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 837 837 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 734 734 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 317 317 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 340 340 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 342 342 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 358 358 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 360 360 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 383 383 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 400 400 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 525 525 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 556 556 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 588 588 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 871 871 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1048 1048 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 1058 1058 Phosphothreonine.
{ECO:0000250|UniProtKB:Q69ZA1}.
MOD_RES 1246 1246 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 519 519 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 547 547 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1079 1138 Missing (in isoform 2).
{ECO:0000303|PubMed:11162436,
ECO:0000303|Ref.5}.
/FTId=VSP_013579.
VARIANT 103 103 Q -> R (in RNA edited version).
/FTId=VAR_066526.
VARIANT 340 340 S -> F (in dbSNP:rs13622).
/FTId=VAR_053926.
VARIANT 356 356 P -> A (in dbSNP:rs17537669).
{ECO:0000269|Ref.2}.
/FTId=VAR_022381.
VARIANT 403 403 L -> F (in dbSNP:rs3735137).
{ECO:0000269|Ref.2}.
/FTId=VAR_022382.
VARIANT 410 410 R -> Q (in dbSNP:rs17496261).
{ECO:0000269|Ref.2}.
/FTId=VAR_022383.
VARIANT 494 494 T -> A (in dbSNP:rs34624759).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041965.
VARIANT 500 500 T -> A (in dbSNP:rs3735135).
{ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.2}.
/FTId=VAR_022384.
VARIANT 624 624 S -> G (in dbSNP:rs17496275).
{ECO:0000269|Ref.2}.
/FTId=VAR_022385.
VARIANT 670 670 T -> R (in dbSNP:rs34775357).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041966.
VARIANT 700 700 R -> L (in dbSNP:rs1057000).
{ECO:0000269|PubMed:11162436,
ECO:0000269|PubMed:1731328}.
/FTId=VAR_022386.
VARIANT 714 714 G -> R (in CHDFIDD).
{ECO:0000269|PubMed:27479907}.
/FTId=VAR_078598.
VARIANT 717 717 G -> R (in CHDFIDD).
{ECO:0000269|PubMed:27479907}.
/FTId=VAR_078599.
VARIANT 751 751 R -> Q (in CHDFIDD).
{ECO:0000269|PubMed:27479907}.
/FTId=VAR_078600.
VARIANT 842 842 N -> S (in CHDFIDD; dbSNP:rs878853160).
{ECO:0000269|PubMed:27479907}.
/FTId=VAR_078601.
VARIANT 1062 1062 V -> M (in dbSNP:rs17496712).
{ECO:0000269|Ref.2}.
/FTId=VAR_022387.
VARIANT 1170 1170 V -> M (in dbSNP:rs3204309).
{ECO:0000269|PubMed:11162436,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_041967.
CONFLICT 21 21 K -> R (in Ref. 1; CAC10400/CAC10401).
{ECO:0000305}.
CONFLICT 671 671 A -> T (in Ref. 1; CAC10400/CAC10401 and
4; AAA58424). {ECO:0000305}.
CONFLICT 810 810 N -> Y (in Ref. 4; AAA58424).
{ECO:0000305}.
CONFLICT 862 866 YSSEE -> FSVFF (in Ref. 5; BAB47420).
{ECO:0000305}.
CONFLICT 1180 1180 Q -> R (in Ref. 5; BAD96773).
{ECO:0000305}.
CONFLICT 1356 1356 G -> E (in Ref. 5; BAD96773).
{ECO:0000305}.
HELIX 702 704 {ECO:0000244|PDB:5EFQ}.
STRAND 705 713 {ECO:0000244|PDB:5EFQ}.
STRAND 715 724 {ECO:0000244|PDB:5EFQ}.
TURN 725 727 {ECO:0000244|PDB:5EFQ}.
STRAND 730 736 {ECO:0000244|PDB:5EFQ}.
STRAND 739 741 {ECO:0000244|PDB:5EFQ}.
HELIX 747 758 {ECO:0000244|PDB:5EFQ}.
STRAND 767 772 {ECO:0000244|PDB:5EFQ}.
STRAND 787 792 {ECO:0000244|PDB:5EFQ}.
STRAND 795 797 {ECO:0000244|PDB:5EFQ}.
HELIX 798 804 {ECO:0000244|PDB:5EFQ}.
HELIX 811 830 {ECO:0000244|PDB:5EFQ}.
HELIX 840 842 {ECO:0000244|PDB:5EFQ}.
STRAND 843 845 {ECO:0000244|PDB:5EFQ}.
STRAND 851 853 {ECO:0000244|PDB:5EFQ}.
HELIX 856 858 {ECO:0000244|PDB:5EFQ}.
STRAND 864 866 {ECO:0000244|PDB:5EFQ}.
HELIX 877 879 {ECO:0000244|PDB:5EFQ}.
HELIX 882 885 {ECO:0000244|PDB:5EFQ}.
HELIX 894 908 {ECO:0000244|PDB:5EFQ}.
STRAND 909 911 {ECO:0000244|PDB:5EFQ}.
HELIX 919 930 {ECO:0000244|PDB:5EFQ}.
TURN 935 937 {ECO:0000244|PDB:5EFQ}.
HELIX 939 943 {ECO:0000244|PDB:5EFQ}.
TURN 945 950 {ECO:0000244|PDB:5EFQ}.
HELIX 960 963 {ECO:0000244|PDB:5EFQ}.
TURN 964 966 {ECO:0000244|PDB:5EFQ}.
HELIX 969 978 {ECO:0000244|PDB:5EFQ}.
TURN 983 985 {ECO:0000244|PDB:5EFQ}.
HELIX 989 994 {ECO:0000244|PDB:5EFQ}.
TURN 996 1000 {ECO:0000244|PDB:5EFQ}.
HELIX 1003 1005 {ECO:0000244|PDB:5EFQ}.
HELIX 1019 1024 {ECO:0000244|PDB:5EFQ}.
HELIX 1026 1030 {ECO:0000244|PDB:5EFQ}.
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


Related products :

Catalog number Product name Quantity
EIAAB06507 CDC2L,CDC2L5,CDC2-related protein kinase 5,CDK13,Cell division cycle 2-like protein kinase 5,Cell division protein kinase 13,CHED,Cholinesterase-related cell division controller,Cyclin-dependent kinas
EIAAB06522 CDC2L6,CDC2-related protein kinase 6,CDK11,CDK19,Cell division cycle 2-like protein kinase 6,Cell division protein kinase 19,Cyclin-dependent kinase 11,Cyclin-dependent kinase 19,Death-preventing kina
EIAAB06521 Cdc2l6,CDC2-related protein kinase 6,Cdk19,Cell division cycle 2-like protein kinase 6,Cell division protein kinase 19,Cyclin-dependent kinase 19,Kiaa1028,Mouse,Mus musculus
EIAAB06506 Bos taurus,Bovine,CDC2L,CDC2L5,CDC2-related protein kinase 5,CDK13,Cell division cycle 2-like protein kinase 5,Cell division protein kinase 13,Cyclin-dependent kinase 13
EIAAB06505 Cdc2l5,CDC2-related protein kinase 5,Cdk13,Cell division cycle 2-like protein kinase 5,Cell division protein kinase 13,Cyclin-dependent kinase 13,Kiaa1791,Mouse,Mus musculus
EIAAB06501 Cdc2-related kinase, arginine_serine-rich,CDC2-related protein kinase 7,Cdk12,Cell division cycle 2-related protein kinase 7,Cell division protein kinase 12,Crk7,CrkRS,Crkrs,Cyclin-dependent kinase 12
EIAAB06503 Cdc2-related kinase, arginine_serine-rich,CDC2-related protein kinase 7,CDK12,Cell division cycle 2-related protein kinase 7,Cell division protein kinase 12,CRK7,CrkRS,CRKRS,Cyclin-dependent kinase 12
EIAAB06502 Cdc2-related kinase, arginine_serine-rich,CDC2-related protein kinase 7,Cdk12,Cell division cycle 2-related protein kinase 7,Cell division protein kinase 12,Crk7,CrkRS,Crkrs,Cyclin-dependent kinase 12
EIAAB06523 CAK-kinase p42,Ccrk,Cdch,Cdk20,CDK-activating kinase p42,CDK-related protein kinase PNQLARE,Cell cycle-related kinase,Cell division protein kinase 20,Cyclin-dependent kinase 20,Cyclin-dependent protei
EIAAB06263 CDC2L2,CDC2L3,CDK11A,Cell division cycle 2-like protein kinase 2,Cell division protein kinase 11A,Cyclin-dependent kinase 11A,Galactosyltransferase-associated protein kinase p58_GTA,Homo sapiens,Human
EIAAB06533 C-2K,CDC2L4,CDK9,Cell division cycle 2-like protein kinase 4,Cell division protein kinase 9,Cyclin-dependent kinase 9,Homo sapiens,Human,Serine_threonine-protein kinase PITALRE,TAK,Tat-associated kina
EIAAB06500 Cdc2l1,Cdk11,Cell division cycle 2-like protein kinase 1,Cell division protein kinase 11,Cyclin-dependent kinase 11,Galactosyltransferase-associated protein kinase p58_GTA,Mouse,Mus musculus,PITSLRE s
EIAAB06264 CDC2L1,CDK11,CDK11B,Cell division cycle 2-like protein kinase 1,Cell division protein kinase 11B,CLK-1,Cyclin-dependent kinase 11B,Galactosyltransferase-associated protein kinase p58_GTA,Homo sapiens,
EIAAB06499 Cdc2l1,Cdk11,Cell division cycle 2-like protein kinase 1,Cell division protein kinase 11,Cyclin-dependent kinase 11,Galactosyltransferase-associated protein kinase p58_GTA,PITSLRE serine_threonine-pro
EIAAB06525 Ccrk,Cdk20,Cell cycle-related kinase,Cell division protein kinase 20,Cyclin-dependent kinase 20,Rat,Rattus norvegicus
18-003-44328 Cell division protein kinase 9 - EC 2.7.11.22; EC 2.7.11.23; Cyclin-dependent kinase 9; Serine_threonine-protein kinase PITALRE; C-2K; Cell division cycle 2-like protein kinase 4 Polyclonal 0.1 mg Protein A
EIAAB06524 CAK-kinase p42,CCRK,CDCH,CDK20,CDK-activating kinase p42,Cell cycle-related kinase,Cell division protein kinase 20,Cyclin-dependent kinase 20,Cyclin-dependent protein kinase H,Cyclin-kinase-activating
U1888h CLIA kit CDC2,CDC28A,CDK1,CDK1,CDKN1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Homo sapiens,Human,p34 protein kinase,P34CDC2 96T
E1888h ELISA CDC2,CDC28A,CDK1,CDK1,CDKN1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Homo sapiens,Human,p34 protein kinase,P34CDC2 96T
U1888h CLIA CDC2,CDC28A,CDK1,CDK1,CDKN1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Homo sapiens,Human,p34 protein kinase,P34CDC2 96T
E1888h ELISA kit CDC2,CDC28A,CDK1,CDK1,CDKN1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Homo sapiens,Human,p34 protein kinase,P34CDC2 96T
E1888m ELISA Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Mouse,Mus musculus,p34 protein kinase 96T
E1888r ELISA kit Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,p34 protein kinase,Rat,Rattus norvegicus 96T
E1888r ELISA Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,p34 protein kinase,Rat,Rattus norvegicus 96T
E1888m ELISA kit Cdc2,Cdc2a,CDK1,Cdk1,Cdkn1,Cell division control protein 2 homolog,Cell division protein kinase 1,Cyclin-dependent kinase 1,Mouse,Mus musculus,p34 protein kinase 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur