Q9HC98 (NEK6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase Nek6
EC=2.7.11.1

Alternative name(s):
Never in mitosis A-related kinase 6
Short name=NimA-related protein kinase 6
Protein kinase SID6-1512

Gene names

Name:

NEK6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein kinase which plays an important role in mitotic cell cycle progression. Required for chromosome segregation at metaphase-anaphase transition, robust mitotic spindle formation and cytokinesis. Phosphorylates ATF4, CIR1, PTN, RAD26L, RBBP6, RPS7, RPS6KB1, TRIP4, STAT3 and histones H1 and H3. Phosphorylates KIF11 to promote mitotic spindle formation. Involved in G2/M phase cell cycle arrest induced by DNA damage. Inhibition of activity results in apoptosis. May contribute to tumorigenesis by suppressing p53/TP53-induced cancer cell senescence. Ref.1 Ref.9 Ref.12 Ref.13 Ref.15 Ref.17 Ref.18 Ref.19
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.13
Cofactor	Magnesium.
Enzyme regulation	Binding to NEK9 stimulates its activity by releasing the autoinhibitory function of Tyr-108. Ref.14
Subunit structure	Interacts with STAT3 and RPS6KB1 By similarity. Interacts with NEK9, predominantly in mitosis. Interacts with KIF11 (via C-terminus). Interacts with APBB1 (via WW domain). Interacts with ANKRA2, ATF4, ARHGAP33, CDC42, CIR1, PRAM1, PTN, PRDX3, PIN1, RAD26L, RBBP6, RPS7 and TRIP4. Ref.10 Ref.11 Ref.13 Ref.15 Ref.18
Subcellular location	Cytoplasm. Nucleus. Nucleus speckle. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle pole. Note: Co-localizes with APBB1 at the nuclear speckles. Co-localizes with PIN1 in the nucleus. Co-localizes with ATF4, CIR1, ARHGAP33, ANKRA2, CDC42, NEK9, RAD26L, RBBP6, RPS7, TRIP4, RELB and PHF1 in the centrosome. Localizes to spindle microtubules in metaphase and anaphase and to the midbody during cytokinesis. Ref.1 Ref.10 Ref.11 Ref.15
Tissue specificity	Ubiquitous, with highest expression in heart and skeletal muscle. Up-regulated in a variety of malignant cancers, such as breast, colon, lung, and gastric cancers. Ref.1 Ref.19
Induction	Up-regulated during the M phase of cell cycle progression. Down-regulated in both replicative and premature senescence of cancer cells. Ref.9 Ref.14 Ref.17
Domain	Displays an autoinhibited conformation: Tyr-108 side chain points into the active site, interacts with the activation loop, and blocks the alphaC helix. The autoinhibitory conformation is released upon binding with NEK9. Ref.14
Post-translational modification	Autophosphorylated. Phosphorylation at Ser-206 is required for its activation. Phosphorylated upon IR or UV-induced DNA damage. Phosphorylated by CHEK1 and CHEK2. Interaction with APBB1 down-regulates phosphorylation at Thr-210. Ref.8 Ref.9 Ref.11 Ref.12 Ref.18
Sequence similarities	Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence AAG13417.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part. The sequence AAH00101.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH04174.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH04209.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAA85045.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle Cell division Chromosome partition Mitosis
Cellular component	Cytoplasm Cytoskeleton Microtubule Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2 DNA damage checkpoint Inferred from mutant phenotype Ref.12. Source: UniProtKB apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW chromosome segregation Inferred from direct assay Ref.9. Source: UniProtKB cytokinesis Traceable author statement Ref.21. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-serine phosphorylation Inferred from direct assay Ref.13. Source: UniProtKB positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.9Ref.18. Source: UniProtKB regulation of cellular senescence Traceable author statement Ref.21. Source: UniProtKB regulation of mitotic metaphase/anaphase transition Inferred from direct assay Ref.9. Source: UniProtKB spindle assembly Traceable author statement Ref.21. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay Ref.1. Source: UniProtKB microtubule Inferred from electronic annotation. Source: UniProtKB-KW microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.1. Source: UniProtKB spindle pole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from direct assay Ref.9. Source: UniProtKB magnesium ion binding Inferred from direct assay Ref.9. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.9Ref.13Ref.18. Source: UniProtKB signal transducer activity Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PIN1	Q13526	3	EBI-740364,EBI-714158

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9HC98-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9HC98-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPRREVCWEAAHFRQEEQSLPRPRVRALVRLACRM

Isoform 3 (identifier: Q9HC98-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGRRRPAPFRALVRLACRM

Isoform 4 (identifier: Q9HC98-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEATGWDSRCSPGTQVRALVRLACRM

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 313	313	Serine/threonine-protein kinase Nek6		PRO_0000086427
Regions
	Domain	45 – 310	266	Protein kinase
	Nucleotide binding	51 – 59	9	ATP By similarity
	Region	1 – 44	44	Interaction with ARHGAP33, ANKRA2, CDC42, PRDX3, RAD26L, RBBP6, RPS7 and TRIP4
	Region	267 – 270	4	Interaction with APBB1
Sites
	Active site	172	1	Proton acceptor By similarity
	Binding site	74	1	ATP By similarity
	Site	108	1	Autoinhibitory
Amino acid modifications
	Modified residue	37	1	Phosphoserine Ref.8
	Modified residue	202	1	Phosphothreonine Ref.8
	Modified residue	206	1	Phosphoserine; by NEK9 Ref.8 Ref.16 Ref.18
	Modified residue	210	1	Phosphothreonine Ref.11
Natural variations
	Alternative sequence	1	1	M → MPRREVCWEAAHFRQEEQSL PRPRVRALVRLACRM in isoform 2.		VSP_041798
	Alternative sequence	1	1	M → MGRRRPAPFRALVRLACRM in isoform 3.		VSP_041799
	Alternative sequence	1	1	M → MEATGWDSRCSPGTQVRALV RLACRM in isoform 4.		VSP_041800
Experimental info
	Mutagenesis	74	1	K → M: Loss of autophosphorylation and of kinase activity and induction of apoptosis; when associated with M-75. Ref.9 Ref.13
	Mutagenesis	75	1	K → M: Loss of autophosphorylation and of kinase activity and induction of apoptosis; when associated with M-74. Ref.9 Ref.13
	Mutagenesis	108	1	Y → A: Increase in catalytic activity. Ref.14
	Sequence conflict	88	1	Q → W in CAG33372. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 3, 2003. Version 2. Checksum: B898DC57407A8C16	FASTA	313	35,714
	10 20 30 40 50 60 MAGQPGHMPH GGSSNNLCHT LGPVHPPDPQ RHPNTLSFRC SLADFQIEKK IGRGQFSEVY 70 80 90 100 110 120 KATCLLDRKT VALKKVQIFE MMDAKARQDC VKEIGLLKQL NHPNIIKYLD SFIEDNELNI 130 140 150 160 170 180 VLELADAGDL SQMIKYFKKQ KRLIPERTVW KYFVQLCSAV EHMHSRRVMH RDIKPANVFI 190 200 210 220 230 240 TATGVVKLGD LGLGRFFSSE TTAAHSLVGT PYYMSPERIH ENGYNFKSDI WSLGCLLYEM 250 260 270 280 290 300 AALQSPFYGD KMNLFSLCQK IEQCDYPPLP GEHYSEKLRE LVSMCICPDP HQRPDIGYVH 310 QVAKQMHIWM SST
	Isoform 2 [UniParc]. Checksum: 2CA3B83E91024B8A	FASTA	347	39,844
	10 20 30 40 50 60 MPRREVCWEA AHFRQEEQSL PRPRVRALVR LACRMAGQPG HMPHGGSSNN LCHTLGPVHP 70 80 90 100 110 120 PDPQRHPNTL SFRCSLADFQ IEKKIGRGQF SEVYKATCLL DRKTVALKKV QIFEMMDAKA 130 140 150 160 170 180 RQDCVKEIGL LKQLNHPNII KYLDSFIEDN ELNIVLELAD AGDLSQMIKY FKKQKRLIPE 190 200 210 220 230 240 RTVWKYFVQL CSAVEHMHSR RVMHRDIKPA NVFITATGVV KLGDLGLGRF FSSETTAAHS 250 260 270 280 290 300 LVGTPYYMSP ERIHENGYNF KSDIWSLGCL LYEMAALQSP FYGDKMNLFS LCQKIEQCDY 310 320 330 340 PPLPGEHYSE KLRELVSMCI CPDPHQRPDI GYVHQVAKQM HIWMSST
	Isoform 3 [UniParc]. Checksum: DF83ECFFE6F5B2F6	FASTA	331	37,823
	10 20 30 40 50 60 MGRRRPAPFR ALVRLACRMA GQPGHMPHGG SSNNLCHTLG PVHPPDPQRH PNTLSFRCSL 70 80 90 100 110 120 ADFQIEKKIG RGQFSEVYKA TCLLDRKTVA LKKVQIFEMM DAKARQDCVK EIGLLKQLNH 130 140 150 160 170 180 PNIIKYLDSF IEDNELNIVL ELADAGDLSQ MIKYFKKQKR LIPERTVWKY FVQLCSAVEH 190 200 210 220 230 240 MHSRRVMHRD IKPANVFITA TGVVKLGDLG LGRFFSSETT AAHSLVGTPY YMSPERIHEN 250 260 270 280 290 300 GYNFKSDIWS LGCLLYEMAA LQSPFYGDKM NLFSLCQKIE QCDYPPLPGE HYSEKLRELV 310 320 330 SMCICPDPHQ RPDIGYVHQV AKQMHIWMSS T
	Isoform 4 [UniParc]. Checksum: 2B680899AE6D5765	FASTA	338	38,460
	10 20 30 40 50 60 MEATGWDSRC SPGTQVRALV RLACRMAGQP GHMPHGGSSN NLCHTLGPVH PPDPQRHPNT 70 80 90 100 110 120 LSFRCSLADF QIEKKIGRGQ FSEVYKATCL LDRKTVALKK VQIFEMMDAK ARQDCVKEIG 130 140 150 160 170 180 LLKQLNHPNI IKYLDSFIED NELNIVLELA DAGDLSQMIK YFKKQKRLIP ERTVWKYFVQ 190 200 210 220 230 240 LCSAVEHMHS RRVMHRDIKP ANVFITATGV VKLGDLGLGR FFSSETTAAH SLVGTPYYMS 250 260 270 280 290 300 PERIHENGYN FKSDIWSLGC LLYEMAALQS PFYGDKMNLF SLCQKIEQCD YPPLPGEHYS 310 320 330 EKLRELVSMC ICPDPHQRPD IGYVHQVAKQ MHIWMSST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of Nek6 protein kinase, a potential human homolog of NIMA histone H3 kinase." Hashimoto Y., Akita H., Hibino M., Kohri K., Nakanishi M. Biochem. Biophys. Res. Commun. 293:753-758(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]	"A protein kinase weakly similar to nek1." Saito T., Saito R., Saito S. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4). Tissue: Brain and Hippocampus.
[4]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). Tissue: Kidney and Pancreas.
[7]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-313 (ISOFORMS 1/2/3/4).
[8]	"A mitotic cascade of NIMA family kinases. Nercc1/Nek9 activates the Nek6 and Nek7 kinases." Belham C., Roig J., Caldwell J.A., Aoyama Y., Kemp B.E., Comb M., Avruch J. J. Biol. Chem. 278:34897-34909(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-37; THR-202 AND SER-206.
[9]	"The serine/threonine kinase Nek6 is required for cell cycle progression through mitosis." Yin M.J., Shao L., Voehringer D., Smeal T., Jallal B. J. Biol. Chem. 278:52454-52460(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-74 AND LYS-75, INDUCTION.
[10]	"Interaction of Pin1 with Nek6 and characterization of their expression correlation in Chinese hepatocellular carcinoma patients." Chen J., Li L., Zhang Y., Yang H., Wei Y., Zhang L., Liu X., Yu L. Biochem. Biophys. Res. Commun. 341:1059-1065(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PIN1.
[11]	"Human NIMA-related kinase 6 is one of the Fe65 WW domain binding proteins." Lee E.J., Hyun S.H., Chun J., Kang S.S. Biochem. Biophys. Res. Commun. 358:783-788(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH APBB1, PHOSPHORYLATION AT THR-210.
[12]	"Nek6 is involved in G2/M phase cell cycle arrest through DNA damage-induced phosphorylation." Lee M.Y., Kim H.J., Kim M.A., Jee H.J., Kim A.J., Bae Y.S., Park J.I., Chung J.H., Yun J. Cell Cycle 7:2705-2709(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION.
[13]	"The NIMA-family kinase Nek6 phosphorylates the kinesin Eg5 at a novel site necessary for mitotic spindle formation." Rapley J., Nicolas M., Groen A., Regue L., Bertran M.T., Caelles C., Avruch J., Roig J. J. Cell Sci. 121:3912-3921(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH KIF11 AND NEK9, MUTAGENESIS OF LYS-74 AND LYS-75.
[14]	"An autoinhibitory tyrosine motif in the cell-cycle-regulated Nek7 kinase is released through binding of Nek9." Richards M.W., O'Regan L., Mas-Droux C., Blot J.M., Cheung J., Hoelder S., Fry A.M., Bayliss R. Mol. Cell 36:560-570(2009) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN, ENZYME REGULATION, MUTAGENESIS OF TYR-108.
[15]	"The Nek6 and Nek7 protein kinases are required for robust mitotic spindle formation and cytokinesis." O'Regan L., Fry A.M. Mol. Cell. Biol. 29:3975-3990(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NEK9.
[16]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, MASS SPECTROMETRY.
[17]	"Nek6 overexpression antagonizes p53-induced senescence in human cancer cells." Jee H.J., Kim A.J., Song N., Kim H.J., Kim M., Koh H., Yun J. Cell Cycle 9:4703-4710(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
[18]	"Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome." Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J. J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ANKRA2; ATF4; ARHGAP33; CDC42; CIR1; NEK9; PRAM1; PTN; PRDX3; RAD26L; RBBP6; RPS7 AND TRIP4, PHOSPHORYLATION AT SER-206, AUTOPHOSPHORYLATION.
[19]	"Nek6 mediates human cancer cell transformation and is a potential cancer therapeutic target." Nassirpour R., Shao L., Flanagan P., Abrams T., Jallal B., Smeal T., Yin M.J. Mol. Cancer Res. 8:717-728(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[20]	"Caught Nek-ing: cilia and centrioles." Quarmby L.M., Mahjoub M.R. J. Cell Sci. 118:5161-5169(2005) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[21]	"A role for Nek6 kinase activity in preventing senescence?" Fry A.M. Cell Cycle 10:19-20(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF087909 mRNA. Translation: AAG13417.1. Sequence problems. AB026289 mRNA. Translation: BAA85045.1. Different initiation. AK294614 mRNA. Translation: BAH11825.1. AK313071 mRNA. Translation: BAG35899.1. AL162724, AL137846 Genomic DNA. Translation: CAH70247.1. AL162724, AL137846 Genomic DNA. Translation: CAH70254.1. AL137846, AL162724 Genomic DNA. Translation: CAI10876.1. AL137846, AL162724 Genomic DNA. Translation: CAI10883.1. CH471090 Genomic DNA. Translation: EAW87579.1. CH471090 Genomic DNA. Translation: EAW87581.1. BC000101 mRNA. Translation: AAH00101.2. Different initiation. BC004174 mRNA. Translation: AAH04174.2. Different initiation. BC004209 mRNA. Translation: AAH04209.2. Different initiation. BC012761 mRNA. Translation: AAH12761.1. CR457091 mRNA. Translation: CAG33372.1. CR542222 mRNA. Translation: CAG47018.1.
IPI	IPI00396662. IPI00550738. IPI00946494. IPI00946980.
PIR	JC7838.
RefSeq	NP_001138473.1. NM_001145001.2. NP_001159639.1. NM_001166167.1. NP_001159640.1. NM_001166168.1. NP_001159641.1. NM_001166169.1. NP_001159642.1. NM_001166170.1. NP_001159643.1. NM_001166171.1. NP_055212.2. NM_014397.5.
UniGene	Hs.197071.
3D structure databases
ProteinModelPortal	Q9HC98.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9HC98. 5 interactions.
STRING	9606.ENSP00000362702.
PTM databases
PhosphoSite	Q9HC98.
Polymorphism databases
DMDM	37537993.
Proteomic databases
PaxDb	Q9HC98.
PRIDE	Q9HC98.
Protocols and materials databases
DNASU	10783.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000320246; ENSP00000319734; ENSG00000119408. ENST00000373600; ENSP00000362702; ENSG00000119408. ENST00000373603; ENSP00000362705; ENSG00000119408. ENST00000394199; ENSP00000377749; ENSG00000119408. ENST00000539416; ENSP00000439651; ENSG00000119408. ENST00000540326; ENSP00000441469; ENSG00000119408. ENST00000545174; ENSP00000442636; ENSG00000119408. ENST00000546191; ENSP00000441426; ENSG00000119408.
GeneID	10783.
KEGG	hsa:10783.
UCSC	uc004bof.3. human. uc004bog.3. human. uc004boh.3. human. uc022bng.1. human.
Organism-specific databases
CTD	10783.
GeneCards	GC09P127019.
HGNC	HGNC:7749. NEK6.
HPA	CAB045993.
MIM	604884. gene.
neXtProt	NX_Q9HC98.
PharmGKB	PA31550.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOVERGEN	HBG105886.
InParanoid	Q9HC98.
KO	K08857.
OMA	TLADFQI.
OrthoDB	EOG4NVZKN.
PhylomeDB	Q9HC98.
Gene expression databases
ArrayExpress	Q9HC98.
Bgee	Q9HC98.
CleanEx	HS_NEK6.
Genevestigator	Q9HC98.
GermOnline	ENSG00000119408. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
PRINTS	PR00109. TYRKINASE.
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9HC98.
ChEMBL	CHEMBL4309.
ChiTaRS	NEK6. human.
GenomeRNAi	10783.
NextBio	40956.
SOURCE	Search...

Entry information

Entry name

NEK6_HUMAN

Accession

Primary (citable) accession number: Q9HC98
Secondary accession number(s): B7Z2D9 , Q5TBG3, Q5TBG9, Q6FG86, Q6IAR3, Q96E83, Q9ULX2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	October 3, 2003
Last modified:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.