Descriptions

Nek7 is a NIMA-related kinase essential for proper mitotic spindle assembly. A human homolog Nek7 (Q8TDX7) is subject to autoinhibition by a tyrosine motif, Tyr97, like Nek6 (Tyr108). This is because the Y97A mutation is more active than wild-type Nek7. A similar tyrosine motif is also found in mouse Nek7.

Autoinhibitory domains (AIDs)

Target domain

20-30 (N-terminal extension of kinase domain)

Relief mechanism

Partner binding

Assay

Accessory elements

178-201 (Activation loop from InterPro)

Target domain

34-299 (Protein kinase domain)

Relief mechanism

Assay

Autoinhibited structure

Activated structure

1 structures for Q9ES74

Entry ID Method Resolution Chain Position Source
AF-Q9ES74-F1 Predicted AlphaFoldDB

No variants for Q9ES74

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9ES74

No associated diseases with Q9ES74

13 regional properties for Q9ES74

Type Name Position InterPro Accession
domain Protein kinase domain 633 - 894 IPR000719
domain Ephrin receptor ligand binding domain 32 - 210 IPR001090
domain Serine-threonine/tyrosine-protein kinase, catalytic domain 633 - 888 IPR001245
conserved_site Tyrosine-protein kinase, receptor class V, conserved site 186 - 206 IPR001426-1
conserved_site Tyrosine-protein kinase, receptor class V, conserved site 250 - 270 IPR001426-2
domain Sterile alpha motif domain 920 - 987 IPR001660
domain Fibronectin type III 331 - 441 IPR003961-1
domain Fibronectin type III 442 - 537 IPR003961-2
active_site Tyrosine-protein kinase, active site 754 - 766 IPR008266
binding_site Protein kinase, ATP binding site 639 - 665 IPR017441
domain Tyrosine-protein kinase, catalytic domain 633 - 890 IPR020635
domain Ephrin receptor, transmembrane domain 560 - 630 IPR027936
domain Ephrin type-A receptor 7, ligand binding domain 30 - 206 IPR034283

Functions

Description
EC Number 2.7.11.34 Protein-serine/threonine kinases
Subcellular Localization
  • Nucleus
  • Cytoplasm
  • Cytoplasm, cytoskeleton, spindle pole
  • Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
  • Present at centrosome throughout the cell cycle (By similarity)
  • Also detected at spindle midzone of the anaphase cells and eventually concentrates at the midbody (By similarity)
  • Interaction with ANKS3 prevents its translocation to the nucleus (PubMed:26188091)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
microtubule organizing center An intracellular structure that can catalyze gamma-tubulin-dependent microtubule nucleation and that can anchor microtubules by interacting with their minus ends, plus ends or sides.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
spindle pole Either of the ends of a spindle, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
protein serine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate.
protein serine/threonine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.
protein serine/threonine/tyrosine kinase activity Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; ATP + a protein threonine = ADP + protein threonine phosphate; and ATP + a protein tyrosine = ADP + protein tyrosine phosphate.

6 GO annotations of biological process

Name Definition
cellular response to potassium ion Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a potassium ion stimulus.
positive regulation of NLRP3 inflammasome complex assembly Any process that activates or increases the frequency, rate or extent of NLRP3 inflammasome complex assembly.
positive regulation of telomerase activity Any process that activates or increases the frequency, rate or extent of telomerase activity, the catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
positive regulation of telomere capping Any process that activates or increases the frequency, rate or extent of telomere capping.
positive regulation of telomere maintenance via telomerase Any process that activates or increases the frequency, rate or extent of the addition of telomeric repeats by telomerase.
protein phosphorylation The process of introducing a phosphate group on to a protein.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9HC98 NEK6 Serine/threonine-protein kinase Nek6 Homo sapiens (Human) EV
Q8TDX7 NEK7 Serine/threonine-protein kinase Nek7 Homo sapiens (Human) EV
Q9ES70 Nek6 Serine/threonine-protein kinase Nek6 Mus musculus (Mouse) SS
A2BD05 NEK6 Serine/threonine-protein kinase Nek6 Sus scrofa (Pig) SS
P59895 Nek6 Serine/threonine-protein kinase Nek6 Rattus norvegicus (Rat) SS
D3ZBE5 Nek7 Serine/threonine-protein kinase Nek7 Rattus norvegicus (Rat) SS
G5EFM9 nekl-3 Serine/threonine-protein kinase nekl-3 Caenorhabditis elegans PR
10 20 30 40 50 60
MDEQSQGMQG PPVTQFQPQK ALRPDMGYNT LANFRIEKKI GRGQFSEVYR ASCLLDGVPV
70 80 90 100 110 120
ALKKVQIFDL MDAKARADCI KEIDLLKQLN HPNVIKYYAS FIEDNELNIV LELADAGDLS
130 140 150 160 170 180
RMIKHFKKQK RLIPERTVWK YFVQLCSALD HMHSRRVMHR DIKPANVFIT ATGVVKLGDL
190 200 210 220 230 240
GLGRFFSSKT TAAHSLVGTP YYMSPERIHE NGYNFKSDIW SLGCLLYEMA ALQSPFYGDK
250 260 270 280 290 300
MNLYSLCKKI EQCDYPPLPS DHYSEELRQL VNICINPDPE KRPDIAYVYD VAKRMHACTA
ST