NEK11
entrez
79858
canonical
uniprot
Q8NG66
canonical
ensembl
ENSG00000114670
resolver
ensp
ENSP00000372857
resolver
ensp
ENSP00000421549
resolver
ensp
ENSP00000421851
resolver
ensp
ENSP00000423458
resolver
ensp
ENSP00000425114
resolver
ensp
ENSP00000426662
resolver
ensp
ENSP00000521332
resolver
ensp
ENSP00000521334
resolver
ensp
ENSP00000521335
resolver
ensp
ENSP00000521336
resolver
ensp
ENSP00000642183
resolver
ensp
ENSP00000642184
resolver
ensp
ENSP00000642185
resolver
ensp
ENSP00000642186
resolver
ensp
ENSP00000642187
resolver
ensp
ENSP00000642189
resolver
ensp
ENSP00000642190
resolver
ensp
ENSP00000679969
resolver
ensp
ENSP00000679972
resolver
ensp
ENSP00000679974
resolver
enst
ENST00000510769
resolver
enst
ENST00000851273
resolver
genesymbol
NEK11
resolver
hgnc
HGNC:18593
resolver
uniprot
A6NHD7
resolver
uniprot
B4DDN2
resolver
uniprot
B4DM56
resolver
uniprot
E9PHI8
resolver
uniprot
Q5JPC0
resolver
uniprot
Q8NG65
resolver
uniprot
Q8TBY1
resolver
uniprot
Q9H5F4
resolver
uniprot_entry
B4DDN2_HUMAN
resolver
uniprot_entry
B4DM56_HUMAN
resolver
uniprot_entry
E9PHI8_HUMAN
resolver
uniprot_entry
NEK11_HUMAN
resolver
uniprot_sec
A6NHD7
resolver
uniprot_sec
Q5JPC0
resolver
uniprot_sec
Q8NG65
resolver
uniprot_sec
Q8TBY1
resolver
uniprot_sec
Q9H5F4
resolver
activity_regulation
ACTIVITY 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. {ECO:0000269|PubMed:12154088, ECO:0000269|PubMed:15161910}.
uniprot
proteins
amino_acid_sequence
MLKFQEAAKCVSGSTAISTYPKTLIARRYVLQQKLGSGSFGTVYLVSDKKAKRGEELKVLKEISVGELNPNETVQANLEAQLLSKLDHPAIVKFHASFVEQDNFCIITEYCEGRDLDDKIQEYKQAGKIFPENQIIEWFIQLLLGVDYMHERRILHRDLKSKNVFLKNNLLKIGDFGVSRLLMGSCDLATTLTGTPHYMSPEALKHQGYDTKSDIWSLACILYEMCCMNHAFAGSNFLSIVLKIVEGDTPSLPERYPKELNAIMESMLNKNPSLRPSAIEILKIPYLDEQLQNLMCRYSEMTLEDKNLDCQKEAAHIINAMQKRIHLQTLRALSEVQKMTPRERMRLRKLQAADEKARKLKKIVEEKYEENSKRMQELRSRNFQQLSVDVLHEKTHLKGMEEKEEQPEGRLSCSPQDEDEERWQGREEESDEPTLENLPESQPIPSMDLHELESIVEDATSDLGYHEIPEDPLVAEEYYADAFDSYCEESDEEEEEIALERPEKEIRNEGSQPAYRTNQQDSDIEALARCLENVLGCTSLDTKTITTMAEDMSPGPPIFNSVMARTKMKRMRESAMQKLGTEVFEEVYNYLKRARHQNASEAEIRECLEKVVPQASDCFEVDQLLYFEEQLLITMGKEPTLQNHL
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
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. {ECO:0000269|PubMed:12154088, ECO:0000269|PubMed:19734889, ECO:0000269|PubMed:20090422}.
uniprot
proteins
mass_dalton
74192
uniprot
proteins
mutagenesis
MUTAGEN 61; /note="K->R: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:12154088
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by NEK2. Phosphorylation at Ser-273 is important for its activation. {ECO:0000269|PubMed:19734889, ECO:0000269|PubMed:20090422}.
uniprot
proteins
protein_family
NEK Ser/Thr protein kinase family
uniprot
proteins
protein_family
NIMA subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
12154088
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15161910
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19734889
uniprot
proteins
pubmed
20090422
uniprot
proteins
sequence_length
645
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12154088}. Nucleus, nucleolus {ECO:0000269|PubMed:15161910}. Note=Nuclear during interphase but moves to the polar microtubules during prometaphase and metaphase (PubMed:12154088). Accumulates in the nucleolus in G1/S-arrested cells (PubMed:15161910). {ECO:0000269|PubMed:12154088, ECO:0000269|PubMed:15161910}.
uniprot
proteins