NEK11_MACFA
ID NEK11_MACFA Reviewed; 637 AA.
AC Q8WNU8;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 98.
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; ORFNames=QtsA-11749;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000312|EMBL:BAB83539.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:BAB83539.1};
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
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-273 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; AB064997; BAB83539.1; -; mRNA.
DR RefSeq; NP_001270591.1; NM_001283662.1.
DR AlphaFoldDB; Q8WNU8; -.
DR SMR; Q8WNU8; -.
DR STRING; 9541.XP_005545802.1; -.
DR GeneID; 101926480; -.
DR CTD; 79858; -.
DR eggNOG; KOG0589; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
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: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 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..637
FT /note="Serine/threonine-protein kinase Nek11"
FT /id="PRO_0000086439"
FT DOMAIN 29..287
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 399..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 302..385
FT /evidence="ECO:0000255"
FT COMPBIAS 399..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..435
FT /note="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:0000250|UniProtKB:Q8NG66,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 273
FT /note="Phosphoserine; by CHEK1"
FT /evidence="ECO:0000250|UniProtKB:Q8NG66"
SQ SEQUENCE 637 AA; 73337 MW; FA3A5C3CEE5AD16F CRC64;
MLKFQEAAKC VSGSTAISTY PKTLIARRYV LQQKLGSGSF GTVYLVSDKK AKRGEELKVL
KEISVGELNP NETVQANLEA QLLSKLDHPA IVKFHASFVE QDNFCIITEY CEGRDLDYKI
QEYKEAGKIF PDNQIIEWFI QLLLGVDYMH ERRILHRDLK SKNIFLKNNL LKIGDFGVSR
LLMGSCDLAT TLTGTPHYMS PEALKHQGYD TKSDIWSLAC ILYEMCCMNH AFAGSNFLSI
VLKIVEGDTP SLPERYPKEL NTIMESMLNK NPSLRPSAIE ILKIPYIDEQ LQHLMCRHSE
MTLEDKNLDC QKEAARLINA MQKRIHLQTL RALSEVQKMT PRERMRLRKL QAADERARKL
KKIVEEKYEE NSKRMQELRS RNFQQLSVDV LHEKTHLIGM EEKEEQPEGR PSCSPQDEDE
ERWQDREEEF DEPTLENLSE PQPIPSMDLR KLESIVEDAT SDLGYHEIPE DPLVAEEYYA
DAFDSYCEES DEEEEEIVLA GPEKEIKNEG SQPTYRTNQQ DSDIEALARC LENVLGCTSL
DTKTIPSMAA DVSPGPTIFN SVMARTKMKR MRESAMQKLG TEVFEEVYNY LKRARHQNAS
EAEIRERLEK VVPRASDCFE VDQLLYFEEQ LLITMGK
