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Serine/threonine-protein kinase Nek3 (EC 2.7.11.1) (HSPK 36) (Never in mitosis A-related kinase 3) (NimA-related protein kinase 3)

 NEK3_HUMAN              Reviewed;         506 AA.
P51956; A8K2J4; Q5TAP2; Q8J023; Q8WUN5;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
16-APR-2002, sequence version 2.
12-SEP-2018, entry version 178.
RecName: Full=Serine/threonine-protein kinase Nek3;
EC=2.7.11.1;
AltName: Full=HSPK 36;
AltName: Full=Never in mitosis A-related kinase 3;
Short=NimA-related protein kinase 3;
Name=NEK3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=12063396;
Kimura M., Okano Y.;
"Molecular cloning and characterization of the human NIMA-related
protein kinase 3 gene (NEK3).";
Cytogenet. Cell Genet. 95:177-182(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 48-506 (ISOFORM 1).
TISSUE=Placenta;
PubMed=7522034;
Schultz S.J., Fry A.M., Suetterlin C., Ried T., Nigg E.A.;
"Cell cycle-dependent expression of Nek2, a novel human protein kinase
related to the NIMA mitotic regulator of Aspergillus nidulans.";
Cell Growth Differ. 5:625-635(1994).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 76-189.
PubMed=8274451;
Schultz S.J., Nigg E.A.;
"Identification of 21 novel human protein kinases, including 3 members
of a family related to the cell cycle regulator nimA of Aspergillus
nidulans.";
Cell Growth Differ. 4:821-830(1993).
[8]
FUNCTION, INTERACTION WITH PRLR; VAV1 AND VAV2, AND ACTIVITY
REGULATION.
PubMed=15618286; DOI=10.1210/me.2004-0443;
Miller S.L., DeMaria J.E., Freier D.O., Riegel A.M., Clevenger C.V.;
"Novel association of Vav2 and Nek3 modulates signaling through the
human prolactin receptor.";
Mol. Endocrinol. 19:939-949(2005).
[9]
FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH PXN.
PubMed=17297458; DOI=10.1038/sj.onc.1210264;
Miller S.L., Antico G., Raghunath P.N., Tomaszewski J.E.,
Clevenger C.V.;
"Nek3 kinase regulates prolactin-mediated cytoskeletal reorganization
and motility of breast cancer cells.";
Oncogene 26:4668-4678(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, 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).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[12]
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).
[13]
VARIANTS [LARGE SCALE ANALYSIS] LEU-23; ARG-60; HIS-122; LEU-170;
GLY-259; ASP-305; ASN-461 AND LYS-477.
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).
-!- FUNCTION: Protein kinase which influences neuronal morphogenesis
and polarity through effects on microtubules. Regulates
microtubule acetylation in neurons. Contributes to prolactin-
mediated phosphorylation of PXN and VAV2. Implicated in prolactin-
mediated cytoskeletal reorganization and motility of breast cancer
cells through mechanisms involving RAC1 activation and
phosphorylation of PXN and VAV2. {ECO:0000269|PubMed:15618286,
ECO:0000269|PubMed:17297458}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ACTIVITY REGULATION: Prolactin stimulates its activity.
{ECO:0000269|PubMed:15618286}.
-!- SUBUNIT: Interacts with PXN, PRLR, VAV1 and VAV2 and this
interaction is prolactin-dependent. {ECO:0000269|PubMed:15618286,
ECO:0000269|PubMed:17297458}.
-!- INTERACTION:
P52735:VAV2; NbExp=3; IntAct=EBI-476041, EBI-297549;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection,
axon {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P51956-1; Sequence=Displayed;
Name=2;
IsoId=P51956-2; Sequence=VSP_035427;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Up-regulated in malignant versus normal breast
tissue. Isoform 2 shows a high level of expression in testis,
ovary and brain. {ECO:0000269|PubMed:12063396,
ECO:0000269|PubMed:17297458}.
-!- PTM: Phosphorylation at Thr-479 regulates its catalytic activity.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
protein kinase family. NIMA subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=EAX08907.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AB072828; BAC15599.1; -; mRNA.
EMBL; AK290259; BAF82948.1; -; mRNA.
EMBL; AL139082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471075; EAX08907.1; ALT_SEQ; Genomic_DNA.
EMBL; BC019916; AAH19916.2; -; mRNA.
EMBL; Z29067; CAA82310.1; -; mRNA.
EMBL; Z25434; CAA80921.1; -; mRNA.
CCDS; CCDS73576.1; -. [P51956-1]
PIR; I38224; I38224.
RefSeq; NP_001139571.1; NM_001146099.1. [P51956-2]
RefSeq; NP_002489.1; NM_002498.2. [P51956-1]
RefSeq; NP_689933.1; NM_152720.2. [P51956-1]
UniGene; Hs.409989; -.
ProteinModelPortal; P51956; -.
SMR; P51956; -.
BioGrid; 110827; 8.
IntAct; P51956; 6.
STRING; 9606.ENSP00000383210; -.
BindingDB; P51956; -.
ChEMBL; CHEMBL5679; -.
GuidetoPHARMACOLOGY; 2118; -.
iPTMnet; P51956; -.
PhosphoSitePlus; P51956; -.
BioMuta; NEK3; -.
DMDM; 20178297; -.
EPD; P51956; -.
MaxQB; P51956; -.
PaxDb; P51956; -.
PeptideAtlas; P51956; -.
PRIDE; P51956; -.
ProteomicsDB; 56457; -.
ProteomicsDB; 56458; -. [P51956-2]
DNASU; 4752; -.
Ensembl; ENST00000610828; ENSP00000480328; ENSG00000136098. [P51956-1]
Ensembl; ENST00000611833; ENSP00000484086; ENSG00000136098. [P51956-2]
Ensembl; ENST00000618534; ENSP00000484443; ENSG00000136098. [P51956-1]
GeneID; 4752; -.
KEGG; hsa:4752; -.
UCSC; uc032agd.2; human. [P51956-1]
CTD; 4752; -.
DisGeNET; 4752; -.
EuPathDB; HostDB:ENSG00000136098.16; -.
GeneCards; NEK3; -.
HGNC; HGNC:7746; NEK3.
HPA; HPA019062; -.
HPA; HPA043230; -.
MIM; 604044; gene.
neXtProt; NX_P51956; -.
OpenTargets; ENSG00000136098; -.
PharmGKB; PA31547; -.
eggNOG; KOG0589; Eukaryota.
eggNOG; ENOG410Y7JF; LUCA.
GeneTree; ENSGT00760000118997; -.
HOGENOM; HOG000261617; -.
HOVERGEN; HBG003063; -.
InParanoid; P51956; -.
KO; K20873; -.
OMA; YTIYRPG; -.
OrthoDB; EOG091G0GU4; -.
PhylomeDB; P51956; -.
TreeFam; TF106472; -.
BRENDA; 2.7.11.1; 2681.
SignaLink; P51956; -.
ChiTaRS; NEK3; human.
GeneWiki; NEK3; -.
GenomeRNAi; 4752; -.
PRO; PR:P51956; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000136098; Expressed in 198 organ(s), highest expression level in testis.
CleanEx; HS_NEK3; -.
ExpressionAtlas; P51956; baseline and differential.
Genevisible; P51956; HS.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; NAS:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
GO; GO:0000278; P:mitotic cell cycle; NAS:UniProtKB.
GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0090043; P:regulation of tubulin deacetylation; IEA:Ensembl.
InterPro; IPR011009; Kinase-like_dom_sf.
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;
Acetylation; Alternative splicing; ATP-binding; Cell cycle;
Cell division; Cell projection; Complete proteome; Cytoplasm; Kinase;
Magnesium; Metal-binding; Mitosis; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Transferase.
CHAIN 1 506 Serine/threonine-protein kinase Nek3.
/FTId=PRO_0000086423.
DOMAIN 4 257 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 10 18 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 285 Interaction with VAV2.
{ECO:0000269|PubMed:15618286}.
ACT_SITE 127 127 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 33 33 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 161 161 Phosphothreonine; by autocatalysis.
{ECO:0000250}.
MOD_RES 479 479 Phosphothreonine.
{ECO:0000244|PubMed:19369195}.
VAR_SEQ 293 309 Missing (in isoform 2).
{ECO:0000303|PubMed:12063396}.
/FTId=VSP_035427.
VARIANT 23 23 H -> L (in dbSNP:rs17482764).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_033906.
VARIANT 60 60 P -> R (in dbSNP:rs55946204).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040908.
VARIANT 122 122 R -> H (in dbSNP:rs56190615).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040909.
VARIANT 170 170 P -> L (in dbSNP:rs56021040).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040910.
VARIANT 259 259 R -> G (in dbSNP:rs34077016).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040911.
VARIANT 305 305 E -> D (in dbSNP:rs55969405).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040912.
VARIANT 461 461 D -> N (in dbSNP:rs34076988).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040913.
VARIANT 477 477 E -> K (in dbSNP:rs34488913).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040914.
CONFLICT 14 14 S -> F (in Ref. 1; BAC15599).
{ECO:0000305}.
CONFLICT 54 54 L -> S (in Ref. 6; CAA82310).
{ECO:0000305}.
CONFLICT 77 78 IV -> LY (in Ref. 7; CAA80921).
{ECO:0000305}.
CONFLICT 187 189 SLG -> PSV (in Ref. 7; CAA80921).
{ECO:0000305}.
SEQUENCE 506 AA; 57705 MW; 4437EB4A41A44777 CRC64;
MDDYMVLRMI GEGSFGRALL VQHESSNQMF AMKEIRLPKS FSNTQNSRKE AVLLAKMKHP
NIVAFKESFE AEGHLYIVME YCDGGDLMQK IKQQKGKLFP EDMILNWFTQ MCLGVNHIHK
KRVLHRDIKS KNIFLTQNGK VKLGDFGSAR LLSNPMAFAC TYVGTPYYVP PEIWENLPYN
NKSDIWSLGC ILYELCTLKH PFQANSWKNL ILKVCQGCIS PLPSHYSYEL QFLVKQMFKR
NPSHRPSATT LLSRGIVARL VQKCLPPEII MEYGEEVLEE IKNSKHNTPR KKTNPSRIRI
ALGNEASTVQ EEEQDRKGSH TDLESINENL VESALRRVNR EEKGNKSVHL RKASSPNLHR
RQWEKNVPNT ALTALENASI LTSSLTAEDD RGGSVIKYSK NTTRKQWLKE TPDTLLNILK
NADLSLAFQT YTIYRPGSEG FLKGPLSEET EASDSVDGGH DSVILDPERL EPGLDEEDTD
FEEEDDNPDW VSELKKRAGW QGLCDR


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10-782-55072 Serine_threonine-protein kinase Nek2 - EC 2.7.11.1; NimA-related protein kinase 2; NimA-like protein kinase 1; HSPK 21 N_A 0.001 mg
10-782-55072 Serine_threonine-protein kinase Nek2 - EC 2.7.11.1; NimA-related protein kinase 2; NimA-like protein kinase 1; HSPK 21 N_A 0.01 mg
EIAAB26884 Homo sapiens,Human,KIAA1901,NEK1,Never in mitosis A-related kinase 1,NimA-related protein kinase 1,Renal carcinoma antigen NY-REN-55,Serine_threonine-protein kinase Nek1
EIAAB31334 Bos taurus,Bovine,PKN,PKN1,PRK1,PRKCL1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine
EIAAB31332 Mouse,Mus musculus,Pkn,Pkn1,Prk1,Prkcl1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine protein kinase N
EIAAB26903 Homo sapiens,Human,NEK7,Never in mitosis A-related kinase 7,NimA-related protein kinase 7,Serine_threonine-protein kinase Nek7
EIAAB26887 Homo sapiens,Human,NEK10,Never in mitosis A-related kinase 10,NimA-related protein kinase 10,Serine_threonine-protein kinase Nek10
EIAAB26886 Gm282,Mouse,Mus musculus,Nek10,Never in mitosis A-related kinase 10,NimA-related protein kinase 10,Serine_threonine-protein kinase Nek10
EIAAB26889 Homo sapiens,Human,NEK11,Never in mitosis A-related kinase 11,NimA-related protein kinase 11,Serine_threonine-protein kinase Nek11
EIAAB26896 Homo sapiens,Human,NEK5,Never in mitosis A-related kinase 5,NimA-related protein kinase 5,Serine_threonine-protein kinase Nek5
EIAAB26894 Homo sapiens,Human,NEK4,Never in mitosis A-related kinase 4,NimA-related protein kinase 4,Serine_threonine-protein kinase 2,Serine_threonine-protein kinase Nek4,Serine_threonine-protein kinase NRK2,ST
EIAAB26885 Mouse,Mus musculus,Nek1,Never in mitosis A-related kinase 1,NimA-related protein kinase 1,Serine_threonine-protein kinase Nek1
EIAAB26906 Jck,Mouse,Mus musculus,Nek8,Never in mitosis A-related kinase 8,NimA-related protein kinase 8,Serine_threonine-protein kinase Nek8
EIAAB26901 Nek6,Never in mitosis A-related kinase 6,NimA-related protein kinase 6,Rat,Rattus norvegicus,Serine_threonine-protein kinase Nek6
EIAAB26897 Mouse,Mus musculus,Nek5,Never in mitosis A-related kinase 5,NimA-related protein kinase 5,Serine_threonine-protein kinase Nek5
EIAAB26902 Nek7,Never in mitosis A-related kinase 7,NimA-related protein kinase 7,Rat,Rattus norvegicus,Serine_threonine-protein kinase Nek7


 

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