NEK7
entrez
140609
canonical
uniprot
Q8TDX7
canonical
ensembl
ENSG00000151414
resolver
ensp
ENSP00000356355
resolver
ensp
ENSP00000546137
resolver
ensp
ENSP00000546139
resolver
ensp
ENSP00000546143
resolver
ensp
ENSP00000546144
resolver
ensp
ENSP00000546145
resolver
ensp
ENSP00000546152
resolver
ensp
ENSP00000546158
resolver
ensp
ENSP00000546159
resolver
ensp
ENSP00000546160
resolver
ensp
ENSP00000631694
resolver
ensp
ENSP00000754166
resolver
genesymbol
NEK7
resolver
hgnc
HGNC:13386
resolver
uniprot
A6NGT8
resolver
uniprot
B2R8K8
resolver
uniprot_entry
B2R8K8_HUMAN
resolver
uniprot_entry
NEK7_HUMAN
resolver
uniprot_sec
A6NGT8
resolver
activity_regulation
ACTIVITY REGULATION: Binding to NEK9 stimulates its activity by releasing the autoinhibitory function of Tyr-97. {ECO:0000269|PubMed:19941817, ECO:0000269|PubMed:26522158}.
uniprot
proteins
amino_acid_sequence
MDEQSQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRAACLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPERTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNMCINPDPEKRPDVTYVYDVAKRMHACTASS
uniprot
proteins
ec_number
2.7.11.34
uniprot
proteins
function
FUNCTION: Protein kinase which plays an important role in mitotic cell cycle progression (PubMed:17101132, PubMed:19941817, PubMed:31409757). Required for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis (PubMed:17586473, PubMed:19414596, PubMed:19941817, PubMed:26522158, PubMed:31409757). Phosphorylates EML4 at 'Ser-146', promoting its dissociation from microtubules during mitosis which is required for efficient chromosome congression (PubMed:31409757). Phosphorylates RPS6KB1 (By similarity). Acts as an essential activator of the NLRP3 inflammasome assembly independently of its kinase activity (PubMed:26642356, PubMed:36442502, PubMed:39173637). Acts by unlocking NLRP3 following NLRP3 tranlocation into the microtubule organizing center (MTOC), relieving NLRP3 autoinhibition and promoting formation of the NLRP3:PYCARD complex, and activation of CASP1 (PubMed:26642356, PubMed:31189953, PubMed:36442502, PubMed:39173637, PubMed:40450990). Serves as a cellular switch that enforces mutual exclusivity of the inflammasome response and cell division: interaction with NEK9 prevents interaction with NLRP3 and activation of the inflammasome during mitosis (PubMed:26642356, PubMed:31189953). {ECO:0000250|UniProtKB:D3ZBE5, ECO:0000269|PubMed:17101132, ECO:0000269|PubMed:17586473, ECO:0000269|PubMed:19414596, ECO:0000269|PubMed:19941817, ECO:0000269|PubMed:26522158, ECO:0000269|PubMed:26642356, ECO:0000269|PubMed:31189953, ECO:0000269|PubMed:31409757, ECO:0000269|PubMed:36442502, ECO:0000269|PubMed:39173637, ECO:0000269|PubMed:40450990}.
uniprot
proteins
mass_dalton
34551
uniprot
proteins
mutagenesis
MUTAGEN 28; /note="Y->A: Significant decrease in catalytic activity; when associated with A-31."; /evidence="ECO:0000269|PubMed:19941817"; MUTAGEN 31; /note="L->A: Significant decrease in catalytic activity; when associated with A-28."; /evidence="ECO:0000269|PubMed:19941817"; MUTAGEN 33; /note="N->D: Significant decrease in catalytic activity."; /evidence="ECO:0000269|PubMed:19941817"; MUTAGEN 90; /note="N->A: Reduced protein kinase activity."; /evidence="ECO:0000269|PubMed:26522158"; MUTAGEN 90; /note="N->R,K: Strongly reduced protein kinase activity."; /evidence="ECO:0000269|PubMed:26522158"; MUTAGEN 96; /note="K->E: Strongly increased protein kinase activity."; /evidence="ECO:0000269|PubMed:26522158"; MUTAGEN 97; /note="Y->A: 5-fold increase in catalytic activity."; /evidence="ECO:0000269|PubMed:19941817, ECO:0000269|PubMed:26522158"; MUTAGEN 97; /note="Y->F,L: Moderate increase in catalytic activity."; /evidence="ECO:0000269|PubMed:19941817"; MUTAGEN 122; /note="M->A,R: Decreased interaction with NEK9 and subsequent activation of NEK7 kinase activity."; /evidence="ECO:0000269|PubMed:26522158"; MUTAGEN 125; /note="H->A: Does not affect interaction with NEK9."; /evidence="ECO:0000269|PubMed:26522158"; MUTAGEN 128; /note="K->E: Does not affect interaction with NLRP3."; /evidence="ECO:0000269|PubMed:31189953"; MUTAGEN 129; /note="Q->R: Decreased interaction with NLRP3."; /evidence="ECO:0000269|PubMed:31189953"; MUTAGEN 130; /note="K->A,E: Does not affect interaction with NEK9."; /evidence="ECO:0000269|PubMed:26522158"; MUTAGEN 131; /note="R->A,D: Abolished interaction with NEK9 and subsequent activation of NEK7 kinase activity."; /evidence="ECO:0000269|PubMed:26522158"; MUTAGEN 131; /note="R->E: Decreased interaction with NLRP3."; /evidence="ECO:0000269|PubMed:31189953"; MUTAGEN 132; /note="L->D: Abolished interaction with NEK9 and subsequent activation of NEK7 kinase activity."; /evidence="ECO:0000269|PubMed:26522158"; MUTAGEN 132; /note="L->W: Does not affect interaction with NEK9."; /evidence="ECO:0000269|PubMed:26522158"; MUTAGEN 136; /note="R->E: Decreased interaction with NLRP3."; /evidence="ECO:0000269|PubMed:31189953"; MUTAGEN 155; /note="R->E: Strongly reduced protein kinase activity."; /evidence="ECO:0000269|PubMed:26522158"; MUTAGEN 169; /note="I->F: Does not affect interaction with NEK9."; /evidence="ECO:0000269|PubMed:26522158"; MUTAGEN 172; /note="T->A: Does not affect interaction with NEK9."; /evidence="ECO:0000269|PubMed:26522158"; MUTAGEN 195; /note="S->A: Abolished phosphorylation with NEK9 and protein kinase activity."; /evidence="ECO:0000269|PubMed:26522158"; MUTAGEN 260..265; /note="SDHYSE->ARHYSR: Decreased interaction with NLRP3."; /evidence="ECO:0000269|PubMed:31189953"; MUTAGEN 260..261; /note="SD->AR: Decreased interaction with NLRP3."; /evidence="ECO:0000269|PubMed:31189953"; MUTAGEN 261; /note="D->A: Does not affect interaction with NEK9."; /evidence="ECO:0000269|PubMed:26522158"; MUTAGEN 262; /note="H->A: Does not affect interaction with NEK9."; /evidence="ECO:0000269|PubMed:26522158"; MUTAGEN 280; /note="E->V,R: Does not affect interaction with NLRP3."; /evidence="ECO:0000269|PubMed:31189953"; MUTAGEN 290; /note="D->R: Does not affect interaction with NLRP3."; /evidence="ECO:0000269|PubMed:31189953"; MUTAGEN 294; /note="R->E: Does not affect interaction with NLRP3."; /evidence="ECO:0000269|PubMed:31189953
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-195 required for its activation. {ECO:0000269|PubMed:12840024, ECO:0000269|PubMed:26522158}.
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
11701951
uniprot
proteins
pubmed
12840024
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17101132
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17586473
uniprot
proteins
pubmed
17727698
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19414596
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19941817
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21320329
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
26188091
uniprot
proteins
pubmed
26522158
uniprot
proteins
pubmed
26642356
uniprot
proteins
pubmed
31189953
uniprot
proteins
pubmed
31409757
uniprot
proteins
pubmed
36442502
uniprot
proteins
pubmed
39173637
uniprot
proteins
pubmed
40450990
uniprot
proteins
sequence_length
302
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ES74}. Cytoplasm {ECO:0000269|PubMed:17586473}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:19414596}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17101132, ECO:0000269|PubMed:17586473}. Note=Present at centrosome throughout the cell cycle (PubMed:17586473). Also detected at spindle midzone of the anaphase cells and eventually concentrates at the midbody (PubMed:17586473). Interaction with ANKS3 prevents its translocation to the nucleus (By similarity). {ECO:0000250|UniProtKB:Q9ES74, ECO:0000269|PubMed:17586473}.
uniprot
proteins