NEK11_HUMAN
ID NEK11_HUMAN Reviewed; 645 AA.
AC Q8NG66; A6NHD7; Q5JPC0; Q8NG65; Q8TBY1; Q9H5F4;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Serine/threonine-protein kinase Nek11;
DE EC=2.7.11.1 {ECO:0000269|PubMed:12154088, ECO:0000269|PubMed:15161910};
DE AltName: Full=Never in mitosis A-related kinase 11;
DE Short=NimA-related protein kinase 11;
GN Name=NEK11 {ECO:0000312|HGNC:HGNC:18593};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAC06350.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, ACTIVITY REGULATION, DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-61, AND VARIANT
RP VAL-488.
RC TISSUE=Cervix carcinoma;
RX PubMed=12154088; DOI=10.1074/jbc.m204599200;
RA Noguchi K., Fukazawa H., Murakami Y., Uehara Y.;
RT "Nek11, a new member of the NIMA family of kinases, involved in DNA
RT replication and genotoxic stress responses.";
RL J. Biol. Chem. 277:39655-39665(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT VAL-488.
RC TISSUE=Cervix;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4] {ECO:0000305, ECO:0000312|EMBL:CAI46114.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAH28587.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis {ECO:0000312|EMBL:AAH28587.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6] {ECO:0000305, ECO:0000312|EMBL:BAB15672.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 162-645 (ISOFORM 1), AND VARIANT
RP VAL-488.
RC TISSUE=Lung {ECO:0000312|EMBL:BAB15672.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7] {ECO:0000305}
RP CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, ACTIVITY REGULATION,
RP AND INTERACTION WITH NEK2.
RX PubMed=15161910; DOI=10.1074/jbc.m404104200;
RA Noguchi K., Fukazawa H., Murakami Y., Uehara Y.;
RT "Nucleolar Nek11 is a novel target of Nek2A in G1/S-arrested cells.";
RL J. Biol. Chem. 279:32716-32727(2004).
RN [8]
RP FUNCTION, AND PHOSPHORYLATION AT SER-273.
RX PubMed=19734889; DOI=10.1038/ncb1969;
RA Melixetian M., Klein D.K., Soerensen C.S., Helin K.;
RT "NEK11 regulates CDC25A degradation and the IR-induced G2/M checkpoint.";
RL Nat. Cell Biol. 11:1247-1253(2009).
RN [9]
RP FUNCTION, AND PHOSPHORYLATION AT SER-273.
RX PubMed=20090422; DOI=10.4161/cc.9.3.10513;
RA Soerensen C.S., Melixetian M., Klein D.K., Helin K.;
RT "NEK11: linking CHK1 and CDC25A in DNA damage checkpoint signaling.";
RL Cell Cycle 9:450-455(2010).
RN [10]
RP VARIANTS [LARGE SCALE ANALYSIS] MET-108; CYS-123; LEU-213; VAL-263;
RP LYS-451; VAL-488; LYS-492; THR-548; ALA-562; LYS-606 AND ASN-617.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Protein kinase which plays an important role in the G2/M
CC checkpoint response to DNA damage. Controls degradation of CDC25A by
CC directly phosphorylating it on residues whose phosphorylation is
CC required for BTRC-mediated polyubiquitination and degradation.
CC {ECO:0000269|PubMed:12154088, ECO:0000269|PubMed:19734889,
CC ECO:0000269|PubMed:20090422}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:12154088, ECO:0000269|PubMed:15161910};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:12154088,
CC ECO:0000269|PubMed:15161910};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12154088, ECO:0000269|PubMed:15161910};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12154088, ECO:0000269|PubMed:15161910};
CC -!- ACTIVITY REGULATION: Autorepressed by intramolecular binding of the C-
CC terminus which dissociates following phosphorylation by NEK2 isoform 1
CC in G1/S-arrested cells. NEK2 isoform 2 is largely not present in the
CC nucleolus, and does not appear to phosphorylate NEK11. Activated in
CC response to DNA damage. Inhibited by zinc.
CC {ECO:0000269|PubMed:12154088, ECO:0000269|PubMed:15161910}.
CC -!- SUBUNIT: Interacts with isoform 1 of NEK2.
CC {ECO:0000269|PubMed:15161910}.
CC -!- INTERACTION:
CC Q8NG66; P08238: HSP90AB1; NbExp=2; IntAct=EBI-633195, EBI-352572;
CC Q8NG66; P51955: NEK2; NbExp=5; IntAct=EBI-633195, EBI-633182;
CC Q8NG66; P51955-1: NEK2; NbExp=2; IntAct=EBI-633195, EBI-687792;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12154088}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:15161910}. Note=Nuclear during interphase
CC but moves to the polar microtubules during prometaphase and metaphase
CC (PubMed:12154088). Accumulates in the nucleolus in G1/S-arrested cells
CC (PubMed:15161910). {ECO:0000269|PubMed:12154088,
CC ECO:0000269|PubMed:15161910}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:12154088}; Synonyms=Long
CC {ECO:0000303|PubMed:12154088};
CC IsoId=Q8NG66-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:12154088}; Synonyms=Short
CC {ECO:0000303|PubMed:12154088};
CC IsoId=Q8NG66-2; Sequence=VSP_051821, VSP_051822;
CC Name=3 {ECO:0000305};
CC IsoId=Q8NG66-3; Sequence=VSP_051820, VSP_051823;
CC Name=4;
CC IsoId=Q8NG66-4; Sequence=VSP_040080, VSP_040081;
CC -!- TISSUE SPECIFICITY: Poorly expressed in cerebellum, trachea, lung,
CC appendix, and uterus. {ECO:0000269|PubMed:12154088}.
CC -!- DEVELOPMENTAL STAGE: Predominantly expressed at S/G2/M phase.
CC {ECO:0000269|PubMed:12154088}.
CC -!- PTM: Phosphorylated by NEK2. Phosphorylation at Ser-273 is important
CC for its activation. {ECO:0000269|PubMed:19734889,
CC ECO:0000269|PubMed:20090422}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15672.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB071996; BAC06350.1; -; mRNA.
DR EMBL; AB071997; BAC06351.1; -; mRNA.
DR EMBL; AL833472; CAI46114.1; -; mRNA.
DR EMBL; AC055733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79213.1; -; Genomic_DNA.
DR EMBL; BC028587; AAH28587.1; -; mRNA.
DR EMBL; AK027148; BAB15672.1; ALT_INIT; mRNA.
DR CCDS; CCDS3069.1; -. [Q8NG66-1]
DR CCDS; CCDS46915.1; -. [Q8NG66-2]
DR CCDS; CCDS54639.1; -. [Q8NG66-4]
DR CCDS; CCDS82836.1; -. [Q8NG66-3]
DR RefSeq; NP_001139475.1; NM_001146003.1. [Q8NG66-4]
DR RefSeq; NP_001308149.1; NM_001321220.1. [Q8NG66-1]
DR RefSeq; NP_001308150.1; NM_001321221.1.
DR RefSeq; NP_001308151.1; NM_001321222.1.
DR RefSeq; NP_001308152.1; NM_001321223.1. [Q8NG66-3]
DR RefSeq; NP_001308153.1; NM_001321224.1.
DR RefSeq; NP_079076.3; NM_024800.4. [Q8NG66-1]
DR RefSeq; NP_665917.1; NM_145910.3. [Q8NG66-2]
DR RefSeq; XP_011511469.1; XM_011513167.2.
DR RefSeq; XP_016862702.1; XM_017007213.1.
DR RefSeq; XP_016862703.1; XM_017007214.1.
DR AlphaFoldDB; Q8NG66; -.
DR SMR; Q8NG66; -.
DR BioGRID; 122947; 25.
DR CORUM; Q8NG66; -.
DR IntAct; Q8NG66; 16.
DR STRING; 9606.ENSP00000372857; -.
DR BindingDB; Q8NG66; -.
DR ChEMBL; CHEMBL5638; -.
DR DrugBank; DB08912; Dabrafenib.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q8NG66; -.
DR GuidetoPHARMACOLOGY; 2116; -.
DR iPTMnet; Q8NG66; -.
DR PhosphoSitePlus; Q8NG66; -.
DR BioMuta; NEK11; -.
DR DMDM; 313104142; -.
DR jPOST; Q8NG66; -.
DR MassIVE; Q8NG66; -.
DR PaxDb; Q8NG66; -.
DR PeptideAtlas; Q8NG66; -.
DR PRIDE; Q8NG66; -.
DR ProteomicsDB; 73438; -. [Q8NG66-1]
DR ProteomicsDB; 73439; -. [Q8NG66-2]
DR ProteomicsDB; 73440; -. [Q8NG66-3]
DR ProteomicsDB; 73441; -. [Q8NG66-4]
DR Antibodypedia; 2071; 298 antibodies from 25 providers.
DR DNASU; 79858; -.
DR Ensembl; ENST00000356918.8; ENSP00000349389.5; ENSG00000114670.14. [Q8NG66-2]
DR Ensembl; ENST00000383366.9; ENSP00000372857.4; ENSG00000114670.14. [Q8NG66-1]
DR Ensembl; ENST00000507910.5; ENSP00000426662.1; ENSG00000114670.14. [Q8NG66-3]
DR Ensembl; ENST00000508196.5; ENSP00000421851.1; ENSG00000114670.14. [Q8NG66-1]
DR Ensembl; ENST00000510688.5; ENSP00000423458.1; ENSG00000114670.14. [Q8NG66-4]
DR Ensembl; ENST00000511262.5; ENSP00000425114.1; ENSG00000114670.14. [Q8NG66-2]
DR GeneID; 79858; -.
DR KEGG; hsa:79858; -.
DR MANE-Select; ENST00000383366.9; ENSP00000372857.4; NM_024800.5; NP_079076.3.
DR UCSC; uc003enx.4; human. [Q8NG66-1]
DR CTD; 79858; -.
DR DisGeNET; 79858; -.
DR GeneCards; NEK11; -.
DR HGNC; HGNC:18593; NEK11.
DR HPA; ENSG00000114670; Tissue enhanced (choroid plexus, fallopian tube).
DR MIM; 609779; gene.
DR neXtProt; NX_Q8NG66; -.
DR OpenTargets; ENSG00000114670; -.
DR PharmGKB; PA38595; -.
DR VEuPathDB; HostDB:ENSG00000114670; -.
DR eggNOG; KOG0589; Eukaryota.
DR GeneTree; ENSGT00940000160525; -.
DR HOGENOM; CLU_000288_63_39_1; -.
DR InParanoid; Q8NG66; -.
DR OrthoDB; 1290401at2759; -.
DR PhylomeDB; Q8NG66; -.
DR TreeFam; TF106472; -.
DR PathwayCommons; Q8NG66; -.
DR SignaLink; Q8NG66; -.
DR SIGNOR; Q8NG66; -.
DR BioGRID-ORCS; 79858; 11 hits in 1104 CRISPR screens.
DR ChiTaRS; NEK11; human.
DR GenomeRNAi; 79858; -.
DR Pharos; Q8NG66; Tchem.
DR PRO; PR:Q8NG66; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8NG66; protein.
DR Bgee; ENSG00000114670; Expressed in right uterine tube and 135 other tissues.
DR ExpressionAtlas; Q8NG66; baseline and differential.
DR Genevisible; Q8NG66; HS.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0016572; P:histone phosphorylation; IMP:CACAO.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; IMP:CACAO.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell cycle; Coiled coil; Kinase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..645
FT /note="Serine/threonine-protein kinase Nek11"
FT /id="PRO_0000086438"
FT DOMAIN 29..287
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 399..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 346..385
FT /evidence="ECO:0000250|UniProtKB:P51957, ECO:0000255"
FT COMPBIAS 399..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P51957,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 35..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P51957,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:12154088"
FT MOD_RES 273
FT /note="Phosphoserine; by CHEK1"
FT /evidence="ECO:0000269|PubMed:19734889,
FT ECO:0000269|PubMed:20090422"
FT VAR_SEQ 467..482
FT /note="EIPEDPLVAEEYYADA -> GDCNLISLDEYWKNEK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051820"
FT VAR_SEQ 467..470
FT /note="EIPE -> ATHS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12154088"
FT /id="VSP_051821"
FT VAR_SEQ 471..645
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12154088"
FT /id="VSP_051822"
FT VAR_SEQ 483..645
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051823"
FT VAR_SEQ 542..599
FT /note="TKTITTMAEDMSPGPPIFNSVMARTKMKRMRESAMQKLGTEVFEEVYNYLKR
FT ARHQNA -> QPCRSWGQKYLKRSIITSREQGIRMLAKQRSASVWKKWCLKPATVLKWT
FT SSCTLKSSC (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_040080"
FT VAR_SEQ 600..645
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_040081"
FT VARIANT 108
FT /note="T -> M (in a colorectal adenocarcinoma sample;
FT somatic mutation; dbSNP:rs200709914)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040935"
FT VARIANT 123
FT /note="Y -> C (in dbSNP:rs55806123)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040936"
FT VARIANT 213
FT /note="S -> L (in dbSNP:rs55920129)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040937"
FT VARIANT 263
FT /note="I -> V (in dbSNP:rs35567155)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040938"
FT VARIANT 451
FT /note="E -> K (in dbSNP:rs35409692)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040939"
FT VARIANT 488
FT /note="E -> V (in dbSNP:rs3738000)"
FT /evidence="ECO:0000269|PubMed:12154088,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_040940"
FT VARIANT 492
FT /note="E -> K (in a colorectal adenocarcinoma sample;
FT somatic mutation; dbSNP:rs140599545)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040941"
FT VARIANT 548
FT /note="M -> T (in dbSNP:rs55813244)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040942"
FT VARIANT 562
FT /note="V -> A (in dbSNP:rs16836266)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_033907"
FT VARIANT 606
FT /note="E -> K (in dbSNP:rs55944737)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040943"
FT VARIANT 617
FT /note="D -> N (in a colorectal adenocarcinoma sample;
FT somatic mutation; dbSNP:rs765563230)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040944"
FT MUTAGEN 61
FT /note="K->R: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:12154088"
SQ SEQUENCE 645 AA; 74192 MW; 7D11AE1D89711DEC CRC64;
MLKFQEAAKC VSGSTAISTY PKTLIARRYV LQQKLGSGSF GTVYLVSDKK AKRGEELKVL
KEISVGELNP NETVQANLEA QLLSKLDHPA IVKFHASFVE QDNFCIITEY CEGRDLDDKI
QEYKQAGKIF PENQIIEWFI QLLLGVDYMH ERRILHRDLK SKNVFLKNNL LKIGDFGVSR
LLMGSCDLAT TLTGTPHYMS PEALKHQGYD TKSDIWSLAC ILYEMCCMNH AFAGSNFLSI
VLKIVEGDTP SLPERYPKEL NAIMESMLNK NPSLRPSAIE ILKIPYLDEQ LQNLMCRYSE
MTLEDKNLDC QKEAAHIINA MQKRIHLQTL RALSEVQKMT PRERMRLRKL QAADEKARKL
KKIVEEKYEE NSKRMQELRS RNFQQLSVDV LHEKTHLKGM EEKEEQPEGR LSCSPQDEDE
ERWQGREEES DEPTLENLPE SQPIPSMDLH ELESIVEDAT SDLGYHEIPE DPLVAEEYYA
DAFDSYCEES DEEEEEIALE RPEKEIRNEG SQPAYRTNQQ DSDIEALARC LENVLGCTSL
DTKTITTMAE DMSPGPPIFN SVMARTKMKR MRESAMQKLG TEVFEEVYNY LKRARHQNAS
EAEIRECLEK VVPQASDCFE VDQLLYFEEQ LLITMGKEPT LQNHL
