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UniProtKB/Swiss-Prot entry Q8NG66


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NEK11_HUMAN
Primary accession number Q8NG66
Secondary accession numbers Q5JPC0 Q8NG65 Q8TBY1 Q9H5F4
Integrated into Swiss-Prot on September 13, 2005
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 56)
Name and origin of the protein
Protein name Serine/threonine-protein kinase Nek11
Synonyms EC 2.7.11.1
Never in mitosis A-related kinase 11
NimA-related protein kinase 11
Gene name
Name: NEK11
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ENZYME REGULATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-61.
TISSUE=Cervix carcinoma;
DOI=10.1074/jbc.M204599200; PubMed=12154088 [NCBI, ExPASy, EBI, Israel, Japan]
Noguchi K., Fukazawa H., Murakami Y., Uehara Y.;
"Nek11, a new member of the NIMA family of kinases, involved in DNA replication and genotoxic stress responses.";
J. Biol. Chem. 277:39655-39665(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cervix;
The German cDNA consortium;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 162-645 (ISOFORM 1).
TISSUE=Lung;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
SUBCELLULAR LOCATION, AND ENZYME REGULATION.
DOI=10.1074/jbc.M404104200; PubMed=15161910 [NCBI, ExPASy, EBI, Israel, Japan]
Noguchi K., Fukazawa H., Murakami Y., Uehara Y.;
"Nucleolar Nek11 is a novel target of Nek2A in G1/S-arrested cells.";
J. Biol. Chem. 279:32716-32727(2004).
[6]
VARIANTS [LARGE SCALE ANALYSIS] MET-108; CYS-123; LEU-213; VAL-263; LYS-451; GLU-488; LYS-492; THR-548; ALA-562; LYS-606 AND ASN-617.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB071996; BAC06350.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB071997; BAC06351.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL833472; CAI46114.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC028587; AAH28587.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK027148; BAB15672.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_079076.2; -.
NP_665917.1; -.
UniGene Hs.657336
3D structure databases
HSSP Q03656; 1Q99. [HSSP ENTRY / PDB]
ModBase Q8NG66.
Protein-protein interaction databases
IntAct Q8NG66; -.
Organism-specific databases
H-InvDB HIX0003682; -.
HGNC HGNC:18593; NEK11.
GenAtlas NEK11.
HPA HPA016908; -.
MIM 609779; gene. [NCBI / EBI]
PharmGKB PA38595; -.
GeneCards Q8NG66.
Gene expression databases
ArrayExpress Q8NG66; -.
CleanEx HS_NEK11; -.
Ontologies
GO
GO:0005730; Cellular component: nucleolus (inferred from direct assay from UniProtKB).
GO:0005524; Molecular function: ATP binding (inferred from direct assay from UniProtKB).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004674; Molecular function: protein serine/threonine kinase activity (inferred from direct assay from UniProtKB).
GO:0031573; Biological process: intra-S DNA damage checkpoint (inferred from direct assay from UniProtKB).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from direct assay from UniProtKB).
GO:0007243; Biological process: protein kinase cascade (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q8NG66.
Genome annotation databases
Ensembl ENSG00000114670; Homo sapiens. [Contig view]
GeneID 79858; -.
KEGG hsa:79858; -.
Phylogenomic databases
HOVERGEN Q8NG66; -.
Other
NextBio 69585; -.
SOURCE NEK11; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; ATP-binding; Cell cycle; Coiled coil; Kinase; Magnesium; Manganese; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   645  645     Serine/threonine-protein kinase Nek11. PRO_0000086438
DOMAIN   29   287  259     Protein kinase. 
NP_BIND   35    43  9     ATP (By similarity). 
COILED   346   385  40     Potential. 
ACT_SITE   158   158        Proton acceptor (By similarity). 
BINDING   61    61        ATP. 
VAR_SEQ   467   482        EIPEDPLVAEEYYADA -> GDCNLISLDEYWKNEK (in isoform 3). VSP_051820
VAR_SEQ   467   470        EIPE -> ATHS (in isoform 2). VSP_051821
VAR_SEQ   471   645        Missing (in isoform 2). VSP_051822
VAR_SEQ   483   645        Missing (in isoform 3). VSP_051823
VARIANT   108   108  1     T -> M (in a colorectal adenocarcinoma sample; somatic mutation). VAR_040935 
VARIANT   123   123  1     Y -> C. VAR_040936 
VARIANT   213   213  1     S -> L. VAR_040937 
VARIANT   263   263  1     I -> V. VAR_040938 
VARIANT   451   451  1     E -> K. VAR_040939 
VARIANT   488   488  1     V -> E. VAR_040940 
VARIANT   492   492  1     E -> K (in a colorectal adenocarcinoma sample; somatic mutation). VAR_040941 
VARIANT   548   548  1     M -> T. VAR_040942 
VARIANT   562   562  1     V -> A (in dbSNP:rs16836266 [NCBI]). VAR_033907 
VARIANT   606   606  1     E -> K. VAR_040943 
VARIANT   617   617  1     D -> N (in a colorectal adenocarcinoma sample; somatic mutation). VAR_040944 
MUTAGEN   61    61        K->R: Loss of kinase activity. 
Sequence information
Length: 645 AA [This is the length of the unprocessed precursor] Molecular weight: 74162 Da [This is the MW of the unprocessed precursor] CRC64: FE957E05C5FFB059 [This is a checksum on the sequence]
        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 
DAFDSYCVES 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 

Q8NG66 in FASTA format

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