Q8NG66 (NEK11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase Nek11
EC=2.7.11.1

Alternative name(s):
Never in mitosis A-related kinase 11
Short name=NimA-related protein kinase 11

Gene names

Name:

NEK11

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	645 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein kinase which plays an important role in the G2/M checkpoint response to DNA damage. Controls degradation of CDC25A by directly phosphorylating it on residues whose phosphorylation is required for BTRC-mediated polyubiquitination and degradation. Ref.1 Ref.8 Ref.9
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.1 Ref.7
Cofactor	Manganese or magnesium. Ref.1 Ref.7
Enzyme regulation	Autorepressed by intramolecular binding of the C-terminus which dissociates following phosphorylation by NEK2 isoform 1 in G1/S-arrested cells. NEK2 isoform 2 is largely not present in the nucleolus, and does not appear to phosphorylate NEK11. Activated in response to DNA damage. Inhibited by zinc. Ref.1 Ref.7
Subunit structure	Interacts with isoform 1 of NEK2. Ref.7
Subcellular location	Nucleus. Nucleus › nucleolus. Note: Nuclear during interphase but moves to the polar microtubules during prometaphase and metaphase. Accumulates in the nucleolus in G1/S-arrested cells. Ref.1 Ref.7
Tissue specificity	Poorly expressed in cerebellum, trachea, lung, appendix, and uterus. Ref.1
Developmental stage	Predominantly expressed at S/G2/M phase. Ref.1
Post-translational modification	Phosphorylated by NEK2. Phosphorylation at Ser-273 is important for its activation. Ref.1 Ref.7 Ref.8 Ref.9
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 BAB15672.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Magnesium Manganese 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.8. Source: UniProtKB intra-S DNA damage checkpoint Inferred from direct assay Ref.7. Source: UniProtKB intracellular protein kinase cascade Inferred from direct assay Ref.7. Source: UniProtKB
Cellular_component	nucleolus Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	ATP binding Inferred from direct assay Ref.7. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay Ref.7Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NEK2	P51955	5	EBI-633195,EBI-633182
NEK2	P51955-1	2	EBI-633195,EBI-687792

Alternative products

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

Isoform 1 Ref.1 (identifier: Q8NG66-1)

Also known as: Long;

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 Ref.1 (identifier: Q8NG66-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     467-470: EIPE → ATHS
     471-645: Missing.

Isoform 3 (identifier: Q8NG66-3)

The sequence of this isoform differs from the canonical sequence as follows:
     467-482: EIPEDPLVAEEYYADA → GDCNLISLDEYWKNEK
     483-645: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: Q8NG66-4)

The sequence of this isoform differs from the canonical sequence as follows:
     542-599: TKTITTMAED...YLKRARHQNA → QPCRSWGQKY...TSSCTLKSSC
     600-645: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 645	645	Serine/threonine-protein kinase Nek11		PRO_0000086438
Regions
	Domain	29 – 287	259	Protein kinase
	Nucleotide binding	35 – 43	9	ATP By similarity UniProtKB P51957
	Coiled coil	346 – 385	40	Potential UniProtKB P51957
Sites
	Active site	158	1	Proton acceptor By similarity UniProtKB P51957
	Binding site	61	1	ATP Ref.1
Amino acid modifications
	Modified residue	273	1	Phosphoserine; by CHEK1 Ref.8 Ref.9
Natural variations
	Alternative sequence	467 – 482	16	EIPED…YYADA → GDCNLISLDEYWKNEK in isoform 3.		VSP_051820
	Alternative sequence	467 – 470	4	EIPE → ATHS in isoform 2. Ref.1		VSP_051821
	Alternative sequence	471 – 645	175	Missing in isoform 2. Ref.1		VSP_051822
	Alternative sequence	483 – 645	163	Missing in isoform 3.		VSP_051823
	Alternative sequence	542 – 599	58	TKTIT…RHQNA → QPCRSWGQKYLKRSIITSRE QGIRMLAKQRSASVWKKWCL KPATVLKWTSSCTLKSSC in isoform 4.		VSP_040080
	Alternative sequence	600 – 645	46	Missing in isoform 4.		VSP_040081
	Natural variant	108	1	T → M in a colorectal adenocarcinoma sample; somatic mutation. Ref.10		VAR_040935
	Natural variant	123	1	Y → C. Ref.10 Corresponds to variant rs55806123 [ dbSNP | Ensembl ].		VAR_040936
	Natural variant	213	1	S → L. Ref.10 Corresponds to variant rs55920129 [ dbSNP | Ensembl ].		VAR_040937
	Natural variant	263	1	I → V. Ref.10 Corresponds to variant rs35567155 [ dbSNP | Ensembl ].		VAR_040938
	Natural variant	451	1	E → K. Ref.10 Corresponds to variant rs35409692 [ dbSNP | Ensembl ].		VAR_040939
	Natural variant	488	1	E → V. Ref.1 Ref.2 Ref.6 Ref.10 Corresponds to variant rs3738000 [ dbSNP | Ensembl ].		VAR_040940
	Natural variant	492	1	E → K in a colorectal adenocarcinoma sample; somatic mutation. Ref.10		VAR_040941
	Natural variant	548	1	M → T. Ref.10 Corresponds to variant rs55813244 [ dbSNP | Ensembl ].		VAR_040942
	Natural variant	562	1	V → A. Ref.10 Corresponds to variant rs16836266 [ dbSNP | Ensembl ].		VAR_033907
	Natural variant	606	1	E → K. Ref.10 Corresponds to variant rs55944737 [ dbSNP | Ensembl ].		VAR_040943
	Natural variant	617	1	D → N in a colorectal adenocarcinoma sample; somatic mutation. Ref.10		VAR_040944
Experimental info
	Mutagenesis	61	1	K → R: Loss of kinase activity. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified November 30, 2010. Version 2. Checksum: 7D11AE1D89711DEC	FASTA	645	74,192
	10 20 30 40 50 60 MLKFQEAAKC VSGSTAISTY PKTLIARRYV LQQKLGSGSF GTVYLVSDKK AKRGEELKVL 70 80 90 100 110 120 KEISVGELNP NETVQANLEA QLLSKLDHPA IVKFHASFVE QDNFCIITEY CEGRDLDDKI 130 140 150 160 170 180 QEYKQAGKIF PENQIIEWFI QLLLGVDYMH ERRILHRDLK SKNVFLKNNL LKIGDFGVSR 190 200 210 220 230 240 LLMGSCDLAT TLTGTPHYMS PEALKHQGYD TKSDIWSLAC ILYEMCCMNH AFAGSNFLSI 250 260 270 280 290 300 VLKIVEGDTP SLPERYPKEL NAIMESMLNK NPSLRPSAIE ILKIPYLDEQ LQNLMCRYSE 310 320 330 340 350 360 MTLEDKNLDC QKEAAHIINA MQKRIHLQTL RALSEVQKMT PRERMRLRKL QAADEKARKL 370 380 390 400 410 420 KKIVEEKYEE NSKRMQELRS RNFQQLSVDV LHEKTHLKGM EEKEEQPEGR LSCSPQDEDE 430 440 450 460 470 480 ERWQGREEES DEPTLENLPE SQPIPSMDLH ELESIVEDAT SDLGYHEIPE DPLVAEEYYA 490 500 510 520 530 540 DAFDSYCEES DEEEEEIALE RPEKEIRNEG SQPAYRTNQQ DSDIEALARC LENVLGCTSL 550 560 570 580 590 600 DTKTITTMAE DMSPGPPIFN SVMARTKMKR MRESAMQKLG TEVFEEVYNY LKRARHQNAS 610 620 630 640 EAEIRECLEK VVPQASDCFE VDQLLYFEEQ LLITMGKEPT LQNHL
	Isoform 2 (Short) [UniParc]. Checksum: F52B82ED2B096FFB	FASTA	470	54,007
	10 20 30 40 50 60 MLKFQEAAKC VSGSTAISTY PKTLIARRYV LQQKLGSGSF GTVYLVSDKK AKRGEELKVL 70 80 90 100 110 120 KEISVGELNP NETVQANLEA QLLSKLDHPA IVKFHASFVE QDNFCIITEY CEGRDLDDKI 130 140 150 160 170 180 QEYKQAGKIF PENQIIEWFI QLLLGVDYMH ERRILHRDLK SKNVFLKNNL LKIGDFGVSR 190 200 210 220 230 240 LLMGSCDLAT TLTGTPHYMS PEALKHQGYD TKSDIWSLAC ILYEMCCMNH AFAGSNFLSI 250 260 270 280 290 300 VLKIVEGDTP SLPERYPKEL NAIMESMLNK NPSLRPSAIE ILKIPYLDEQ LQNLMCRYSE 310 320 330 340 350 360 MTLEDKNLDC QKEAAHIINA MQKRIHLQTL RALSEVQKMT PRERMRLRKL QAADEKARKL 370 380 390 400 410 420 KKIVEEKYEE NSKRMQELRS RNFQQLSVDV LHEKTHLKGM EEKEEQPEGR LSCSPQDEDE 430 440 450 460 470 ERWQGREEES DEPTLENLPE SQPIPSMDLH ELESIVEDAT SDLGYHATHS
	Isoform 3 [UniParc]. Checksum: FA6D89E50C0223A5	FASTA	482	55,519
	10 20 30 40 50 60 MLKFQEAAKC VSGSTAISTY PKTLIARRYV LQQKLGSGSF GTVYLVSDKK AKRGEELKVL 70 80 90 100 110 120 KEISVGELNP NETVQANLEA QLLSKLDHPA IVKFHASFVE QDNFCIITEY CEGRDLDDKI 130 140 150 160 170 180 QEYKQAGKIF PENQIIEWFI QLLLGVDYMH ERRILHRDLK SKNVFLKNNL LKIGDFGVSR 190 200 210 220 230 240 LLMGSCDLAT TLTGTPHYMS PEALKHQGYD TKSDIWSLAC ILYEMCCMNH AFAGSNFLSI 250 260 270 280 290 300 VLKIVEGDTP SLPERYPKEL NAIMESMLNK NPSLRPSAIE ILKIPYLDEQ LQNLMCRYSE 310 320 330 340 350 360 MTLEDKNLDC QKEAAHIINA MQKRIHLQTL RALSEVQKMT PRERMRLRKL QAADEKARKL 370 380 390 400 410 420 KKIVEEKYEE NSKRMQELRS RNFQQLSVDV LHEKTHLKGM EEKEEQPEGR LSCSPQDEDE 430 440 450 460 470 480 ERWQGREEES DEPTLENLPE SQPIPSMDLH ELESIVEDAT SDLGYHGDCN LISLDEYWKN EK
	Isoform 4 [UniParc]. Checksum: D9080C265940829F	FASTA	599	68,880
	10 20 30 40 50 60 MLKFQEAAKC VSGSTAISTY PKTLIARRYV LQQKLGSGSF GTVYLVSDKK AKRGEELKVL 70 80 90 100 110 120 KEISVGELNP NETVQANLEA QLLSKLDHPA IVKFHASFVE QDNFCIITEY CEGRDLDDKI 130 140 150 160 170 180 QEYKQAGKIF PENQIIEWFI QLLLGVDYMH ERRILHRDLK SKNVFLKNNL LKIGDFGVSR 190 200 210 220 230 240 LLMGSCDLAT TLTGTPHYMS PEALKHQGYD TKSDIWSLAC ILYEMCCMNH AFAGSNFLSI 250 260 270 280 290 300 VLKIVEGDTP SLPERYPKEL NAIMESMLNK NPSLRPSAIE ILKIPYLDEQ LQNLMCRYSE 310 320 330 340 350 360 MTLEDKNLDC QKEAAHIINA MQKRIHLQTL RALSEVQKMT PRERMRLRKL QAADEKARKL 370 380 390 400 410 420 KKIVEEKYEE NSKRMQELRS RNFQQLSVDV LHEKTHLKGM EEKEEQPEGR LSCSPQDEDE 430 440 450 460 470 480 ERWQGREEES DEPTLENLPE SQPIPSMDLH ELESIVEDAT SDLGYHEIPE DPLVAEEYYA 490 500 510 520 530 540 DAFDSYCEES DEEEEEIALE RPEKEIRNEG SQPAYRTNQQ DSDIEALARC LENVLGCTSL 550 560 570 580 590 DQPCRSWGQK YLKRSIITSR EQGIRMLAKQ RSASVWKKWC LKPATVLKWT SSCTLKSSC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nek11, a new member of the NIMA family of kinases, involved in DNA replication and genotoxic stress responses." Noguchi K., Fukazawa H., Murakami Y., Uehara Y. J. Biol. Chem. 277:39655-39665(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ENZYME REGULATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-61, VARIANT VAL-488. Tissue: Cervix carcinoma.
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT VAL-488. Tissue: Cervix.
[3]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORM 3). Tissue: Testis.
[6]	"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] OF 162-645 (ISOFORM 1), VARIANT VAL-488. Tissue: Lung.
[7]	"Nucleolar Nek11 is a novel target of Nek2A in G1/S-arrested cells." Noguchi K., Fukazawa H., Murakami Y., Uehara Y. J. Biol. Chem. 279:32716-32727(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, ENZYME REGULATION, INTERACTION WITH NEK2.
[8]	"NEK11 regulates CDC25A degradation and the IR-induced G2/M checkpoint." Melixetian M., Klein D.K., Soerensen C.S., Helin K. Nat. Cell Biol. 11:1247-1253(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-273.
[9]	"NEK11: linking CHK1 and CDC25A in DNA damage checkpoint signaling." Soerensen C.S., Melixetian M., Klein D.K., Helin K. Cell Cycle 9:450-455(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-273.
[10]	"Patterns of somatic mutation in human cancer genomes." 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. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-108; CYS-123; LEU-213; VAL-263; LYS-451; VAL-488; LYS-492; THR-548; ALA-562; LYS-606 AND ASN-617.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB071996 mRNA. Translation: BAC06350.1. AB071997 mRNA. Translation: BAC06351.1. AL833472 mRNA. Translation: CAI46114.1. AC055733 Genomic DNA. No translation available. CH471052 Genomic DNA. Translation: EAW79213.1. BC028587 mRNA. Translation: AAH28587.1. AK027148 mRNA. Translation: BAB15672.1. Different initiation.
IPI	IPI00398836. IPI00745302. IPI00745916. IPI00789673.
RefSeq	NP_001139475.1. NM_001146003.1. NP_079076.3. NM_024800.4. NP_665917.1. NM_145910.3.
UniGene	Hs.657336.
3D structure databases
ProteinModelPortal	Q8NG66.
SMR	Q8NG66. Positions 26-313.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8NG66. 3 interactions.
STRING	9606.ENSP00000372857.
PTM databases
PhosphoSite	Q8NG66.
Polymorphism databases
DMDM	74715639.
Proteomic databases
PaxDb	Q8NG66.
PRIDE	Q8NG66.
Protocols and materials databases
DNASU	79858.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000356918; ENSP00000349389; ENSG00000114670. ENST00000383366; ENSP00000372857; ENSG00000114670. ENST00000429253; ENSP00000397180; ENSG00000114670. ENST00000507910; ENSP00000426662; ENSG00000114670. ENST00000508196; ENSP00000421851; ENSG00000114670. ENST00000510688; ENSP00000423458; ENSG00000114670. ENST00000511262; ENSP00000425114; ENSG00000114670.
GeneID	79858.
KEGG	hsa:79858.
UCSC	uc003enx.3. human. uc003eny.3. human. uc003eoa.3. human. uc011blm.2. human.
Organism-specific databases
CTD	79858.
GeneCards	GC03P130745.
HGNC	HGNC:18593. NEK11.
HPA	HPA016908.
MIM	609779. gene.
neXtProt	NX_Q8NG66.
PharmGKB	PA38595.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000293260.
HOVERGEN	HBG082016.
InParanoid	Q8NG66.
KO	K08857.
PhylomeDB	Q8NG66.
Enzyme and pathway databases
SignaLink	Q8NG66.
Gene expression databases
ArrayExpress	Q8NG66.
Bgee	Q8NG66.
CleanEx	HS_NEK11.
Genevestigator	Q8NG66.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q8NG66.
ChEMBL	CHEMBL5638.
GenomeRNAi	79858.
NextBio	69585.
SOURCE	Search...

Entry information

Entry name

NEK11_HUMAN

Accession

Primary (citable) accession number: Q8NG66
Secondary accession number(s): A6NHD7 , Q5JPC0, Q8NG65, Q8TBY1, Q9H5F4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	November 30, 2010
Last modified:	May 29, 2013
This is version 101 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.