NEK11_MOUSE
ID NEK11_MOUSE Reviewed; 628 AA.
AC Q8C0Q4; E9QNC3; Q8BLS6; Q8BW62;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Serine/threonine-protein kinase Nek11;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q8NG66};
DE AltName: Full=Never in mitosis A-related kinase 11;
DE Short=NimA-related protein kinase 11;
GN Name=Nek11 {ECO:0000312|MGI:MGI:2442276};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Oviduct, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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:0000250|UniProtKB:Q8NG66}.
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:0000250|UniProtKB:Q8NG66};
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:0000250|UniProtKB:Q8NG66};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8NG66};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8NG66};
CC -!- ACTIVITY REGULATION: Autorepressed by intramolecular binding of the C-
CC terminus which dissociates following phosphorylation by NEK2. Activated
CC in response to DNA damage. Inhibited by zinc.
CC {ECO:0000250|UniProtKB:Q8NG66}.
CC -!- SUBUNIT: Interacts with NEK2. {ECO:0000250|UniProtKB:Q8NG66}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NG66}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q8NG66}. Note=Nuclear during
CC interphase but moves to the polar microtubules during prometaphase and
CC metaphase. Accumulates in the nucleolus in G1/S-arrested cells.
CC {ECO:0000250|UniProtKB:Q8NG66}.
CC -!- PTM: Phosphorylated by NEK2. Phosphorylation at Ser-274 is important
CC for its activation. {ECO:0000250|UniProtKB:Q8NG66}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000305}.
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DR EMBL; AK030042; BAC26756.1; -; mRNA.
DR EMBL; AK043543; BAC31576.1; -; mRNA.
DR EMBL; AK054237; BAC35699.1; -; mRNA.
DR EMBL; AC113016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23464.1; -.
DR RefSeq; NP_766049.2; NM_172461.3.
DR RefSeq; XP_006511742.1; XM_006511679.3.
DR AlphaFoldDB; Q8C0Q4; -.
DR SMR; Q8C0Q4; -.
DR STRING; 10090.ENSMUSP00000038611; -.
DR iPTMnet; Q8C0Q4; -.
DR PhosphoSitePlus; Q8C0Q4; -.
DR PaxDb; Q8C0Q4; -.
DR PRIDE; Q8C0Q4; -.
DR Antibodypedia; 2071; 298 antibodies from 25 providers.
DR DNASU; 208583; -.
DR Ensembl; ENSMUST00000038648; ENSMUSP00000038611; ENSMUSG00000035032.
DR GeneID; 208583; -.
DR KEGG; mmu:208583; -.
DR UCSC; uc009rhy.2; mouse.
DR CTD; 79858; -.
DR MGI; MGI:2442276; Nek11.
DR VEuPathDB; HostDB:ENSMUSG00000035032; -.
DR eggNOG; KOG0589; Eukaryota.
DR GeneTree; ENSGT00940000160525; -.
DR HOGENOM; CLU_000288_63_39_1; -.
DR InParanoid; Q8C0Q4; -.
DR OMA; QDSDMEA; -.
DR OrthoDB; 1290401at2759; -.
DR PhylomeDB; Q8C0Q4; -.
DR TreeFam; TF106472; -.
DR BioGRID-ORCS; 208583; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Nek11; mouse.
DR PRO; PR:Q8C0Q4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8C0Q4; protein.
DR Bgee; ENSMUSG00000035032; Expressed in spermatid and 43 other tissues.
DR ExpressionAtlas; Q8C0Q4; baseline and differential.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS: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; ISS:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0016572; P:histone phosphorylation; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; ISO:MGI.
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 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Coiled coil; Kinase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..628
FT /note="Serine/threonine-protein kinase Nek11"
FT /id="PRO_0000086440"
FT DOMAIN 30..288
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 452..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 347..385
FT /evidence="ECO:0000255"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P51957,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 36..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P51957,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NG66,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 274
FT /note="Phosphoserine; by CHEK1"
FT /evidence="ECO:0000250|UniProtKB:Q8NG66"
FT CONFLICT 196
FT /note="T -> A (in Ref. 1; BAC31576)"
FT /evidence="ECO:0000305"
FT CONFLICT 433..438
FT /note="IPEDPL -> KRKKER (in Ref. 1; BAC31576)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="H -> R (in Ref. 1; BAC26756)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 628 AA; 71648 MW; 2D8672AA753CEB84 CRC64;
MLKFQETAKC VGRRPTVIPM YPTALIARRY VLQQKLGSGS FGTVYLVSDK KAKPGEELKV
LKEISVGELN PNETVQANVE AQLLSRLHHP AIVRFHASFM EQETFCIITE YCEGRDLDYR
IQEYKEAGKV FAENQIVEWF IQLLLGVDYM HERRILHRDL KSKNIFLKNN LLKIGDFGVS
RLLMGSCELA TTLTGTPHYM SPEALKHQGY DAKSDIWSLA CILYEMCCLD HAFAGSSFLS
VVLNIVEGKT PSLPDRYPRE LNTIMERMLN KSPSLRPSAA DILKAPYMEE QLQLLMCKYP
EMTLEDKNSV CQKEAAHTIN AVQKKLHLQT LQALSDTQKT TPRERMWLRK LQAADERARR
LKKIAEENYK ENDKRMQALR SRNVGSVHAH VLHELDERTL ESLPEPQSLP CLDLDELEPS
LEDTIVDLGH YEIPEDPLVA EQYYSDVFDS CSEDSEEQEE EMIFSEAGGD TKEEESPSVY
RTNQQDSDTA ALVGCLEHVL GYTSLDTKTI TNAVTDMSPG PMVFNSAVAR TKMKRMKESA
VQKLGMETFE EVYDYLKRAR HQNAREAEIW EHLETVVPRA SDCFEVDQLL YFEELLLTME
GKEPSLQNLP CEAAQKKPVK GTHFCDNP
