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Q8NG66 (NEK11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length645 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Nucleusnucleolus. 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.

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 645645Serine/threonine-protein kinase Nek11
PRO_0000086438

Regions

Domain29 – 287259Protein kinase
Nucleotide binding35 – 439ATP By similarity UniProtKB P51957
Coiled coil346 – 38540 Potential UniProtKB P51957

Sites

Active site1581Proton acceptor By similarity UniProtKB P51957
Binding site611ATP Ref.1

Amino acid modifications

Modified residue2731Phosphoserine; by CHEK1 Ref.8 Ref.9

Natural variations

Alternative sequence467 – 48216EIPED…YYADA → GDCNLISLDEYWKNEK in isoform 3.
VSP_051820
Alternative sequence467 – 4704EIPE → ATHS in isoform 2. Ref.1
VSP_051821
Alternative sequence471 – 645175Missing in isoform 2. Ref.1
VSP_051822
Alternative sequence483 – 645163Missing in isoform 3.
VSP_051823
Alternative sequence542 – 59958TKTIT…RHQNA → QPCRSWGQKYLKRSIITSRE QGIRMLAKQRSASVWKKWCL KPATVLKWTSSCTLKSSC in isoform 4.
VSP_040080
Alternative sequence600 – 64546Missing in isoform 4.
VSP_040081
Natural variant1081T → M in a colorectal adenocarcinoma sample; somatic mutation. Ref.10
VAR_040935
Natural variant1231Y → C. Ref.10
Corresponds to variant rs55806123 [ dbSNP | Ensembl ].
VAR_040936
Natural variant2131S → L. Ref.10
Corresponds to variant rs55920129 [ dbSNP | Ensembl ].
VAR_040937
Natural variant2631I → V. Ref.10
Corresponds to variant rs35567155 [ dbSNP | Ensembl ].
VAR_040938
Natural variant4511E → K. Ref.10
Corresponds to variant rs35409692 [ dbSNP | Ensembl ].
VAR_040939
Natural variant4881E → V. Ref.1 Ref.2 Ref.6 Ref.10
Corresponds to variant rs3738000 [ dbSNP | Ensembl ].
VAR_040940
Natural variant4921E → K in a colorectal adenocarcinoma sample; somatic mutation. Ref.10
VAR_040941
Natural variant5481M → T. Ref.10
Corresponds to variant rs55813244 [ dbSNP | Ensembl ].
VAR_040942
Natural variant5621V → A. Ref.10
Corresponds to variant rs16836266 [ dbSNP | Ensembl ].
VAR_033907
Natural variant6061E → K. Ref.10
Corresponds to variant rs55944737 [ dbSNP | Ensembl ].
VAR_040943
Natural variant6171D → N in a colorectal adenocarcinoma sample; somatic mutation. Ref.10
VAR_040944

Experimental info

Mutagenesis611K → R: Loss of kinase activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: 7D11AE1D89711DEC

FASTA64574,192
        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 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: F52B82ED2B096FFB
Show »

FASTA47054,007
Isoform 3 [UniParc].

Checksum: FA6D89E50C0223A5
Show »

FASTA48255,519
Isoform 4 [UniParc].

Checksum: D9080C265940829F
Show »

FASTA59968,880

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqNP_001139475.1. NM_001146003.1.
NP_079076.3. NM_024800.4.
NP_665917.1. NM_145910.3.
XP_005247840.1. XM_005247783.1.
UniGeneHs.657336.

3D structure databases

ProteinModelPortalQ8NG66.
SMRQ8NG66. Positions 26-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122947. 3 interactions.
IntActQ8NG66. 3 interactions.
STRING9606.ENSP00000372857.

Chemistry

BindingDBQ8NG66.
ChEMBLCHEMBL5638.
GuidetoPHARMACOLOGY2116.

PTM databases

PhosphoSiteQ8NG66.

Polymorphism databases

DMDM313104142.

Proteomic databases

PaxDbQ8NG66.
PRIDEQ8NG66.

Protocols and materials databases

DNASU79858.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356918; ENSP00000349389; ENSG00000114670. [Q8NG66-3]
ENST00000383366; ENSP00000372857; ENSG00000114670. [Q8NG66-1]
ENST00000429253; ENSP00000397180; ENSG00000114670. [Q8NG66-1]
ENST00000507910; ENSP00000426662; ENSG00000114670. [Q8NG66-3]
ENST00000508196; ENSP00000421851; ENSG00000114670. [Q8NG66-1]
ENST00000510688; ENSP00000423458; ENSG00000114670. [Q8NG66-4]
ENST00000511262; ENSP00000425114; ENSG00000114670. [Q8NG66-2]
GeneID79858.
KEGGhsa:79858.
UCSCuc003enx.3. human. [Q8NG66-2]
uc003eny.3. human. [Q8NG66-1]
uc003eoa.3. human. [Q8NG66-4]
uc011blm.2. human. [Q8NG66-3]

Organism-specific databases

CTD79858.
GeneCardsGC03P130745.
HGNCHGNC:18593. NEK11.
HPAHPA016908.
MIM609779. gene.
neXtProtNX_Q8NG66.
PharmGKBPA38595.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000293260.
HOVERGENHBG082016.
InParanoidQ8NG66.
KOK08857.
OrthoDBEOG7WMCJ7.
PhylomeDBQ8NG66.
TreeFamTF106472.

Enzyme and pathway databases

SignaLinkQ8NG66.

Gene expression databases

ArrayExpressQ8NG66.
BgeeQ8NG66.
CleanExHS_NEK11.
GenevestigatorQ8NG66.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi79858.
NextBio69585.
PROQ8NG66.
SOURCESearch...

Entry information

Entry nameNEK11_HUMAN
AccessionPrimary (citable) accession number: Q8NG66
Secondary accession number(s): A6NHD7 expand/collapse secondary AC list , Q5JPC0, Q8NG65, Q8TBY1, Q9H5F4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM