A2BD05

SS
Gene name
NEK6
Protein name
Serine/threonine-protein kinase Nek6
Names
Never in mitosis A-related kinase 6, NimA-related protein kinase 6
Species
Mus musculus (Mouse)
KEGG Pathway
ssc:100514624
EC number
2.7.11.1: Protein-serine/threonine kinases
Protein Class

Descriptions

MARK1 is a Ser/Thr protein kinase involved in various cellular processes. It is part of the CAMK-like kinase family and has roles in diseases like Alzheimer’s and cancer. The kinase’s autoinhibition is mediated by its C-terminal KA1 domain, which interacts with the kinase domain to prevent substrate binding and activation. The KA1 domain binds to the αD-helix, blocking the peptide substrate binding site and inhibiting the kinase. This autoinhibition is alleviated by the binding of anionic phospholipid membranes to the KA1 domain, which reverses MARK1 autoinhibition and stimulates kinase activity.

Autoinhibitory domains (AIDs)

108-114 (Tyrosine motif) SS

Target domain

31-41 (N-terminal extension of kinase domain)

Relief mechanism

Partner binding

Assay

Accessory elements

189-212 (Activation loop from InterPro)

Target domain

45-310 (Protein kinase domain)

Relief mechanism

Assay

References

Autoinhibited structure

Activated structure

1 structures for A2BD05

Entry ID Method Resolution Chain Position Source
AF-A2BD05-F1 Predicted AlphaFoldDB

2 variants for A2BD05

Variant ID(s) Position Change Description Diseaes Association Provenance
rs709730499 90 C>F No Ensembl
rs699445173 301 Q>H No Ensembl

No associated diseases with A2BD05

6 regional properties for A2BD05

Type Name Position InterPro Accession
domain Protein kinase domain 56 - 307 IPR000719
domain Kinase associated domain 1 (KA1) 704 - 753 IPR001772
active_site Serine/threonine-protein kinase, active site 174 - 186 IPR008271
domain Ubiquitin-associated domain 326 - 365 IPR015940
binding_site Protein kinase, ATP binding site 62 - 85 IPR017441
domain Serine/threonine-protein kinase MARK 1-4, catalytic domain 55 - 307 IPR049508

Functions

Description
EC Number 2.7.11.1 Protein-serine/threonine kinases
Subcellular Localization
  • Cell membrane ; Peripheral membrane protein
  • Cell projection, dendrite
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 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.
nuclear speck A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.
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.

6 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 kinase binding Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
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
apoptotic process A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
cell cycle The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division.
cell division The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
chromosome segregation The process in which genetic material, in the form of chromosomes, is organized into specific structures and then physically separated and apportioned to two or more sets. In eukaryotes, chromosome segregation begins with the condensation of chromosomes, includes chromosome separation, and ends when chromosomes have completed movement to the spindle poles.
protein autophosphorylation The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
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
Q8TDX7 NEK7 Serine/threonine-protein kinase Nek7 Homo sapiens (Human) EV
Q9HC98 NEK6 Serine/threonine-protein kinase Nek6 Homo sapiens (Human) EV
Q9ES74 Nek7 Serine/threonine-protein kinase Nek7 Mus musculus (Mouse) SS
Q9ES70 Nek6 Serine/threonine-protein kinase Nek6 Mus musculus (Mouse) SS
D3ZBE5 Nek7 Serine/threonine-protein kinase Nek7 Rattus norvegicus (Rat) SS
P59895 Nek6 Serine/threonine-protein kinase Nek6 Rattus norvegicus (Rat) SS
G5EFM9 nekl-3 Serine/threonine-protein kinase nekl-3 Caenorhabditis elegans PR
10 20 30 40 50 60
MSTRTPLPTV NERDTENHIS HGDGRQEVTS RTGRSGARCR NSIASCADEQ PHIGNYRLLK
70 80 90 100 110 120
TIGKGNFAKV KLARHILTGR EVAIKIIDKT QLNPTSLQKL FREVRIMKIL NHPNIVKLFE
130 140 150 160 170 180
VIETEKTLYL IMEYASGGEV FDYLVAHGRM KEKEARAKFR QIVSAVQYCH QKRIVHRDLK
190 200 210 220 230 240
AENLLLDADM NIKIADFGFS NEFTVGSKLD TFCGSPPYAA PELFQGKKYD GPEVDVWSLG
250 260 270 280 290 300
VILYTLVSGS LPFDGQNLKE LRERVLRGKY RIPFYMSTDC ENLLKRFLVL NPVKRGTLEQ
310 320 330 340 350 360
IMKDRWINAG HEEDELKPFV EPELDISDQK RIDIMVGMGY SQEEIQESLS KMKYDEITAT
370 380 390 400 410 420
YLLLGRKSAE LDASDSSSSS NLSLAKVRPN SDLSNSTGQS PHHKGQRSVS SSQKQRRYSD
430 440 450 460 470 480
HAGPAIPSVV AYPKRSQTST ADSDLKEDGI PSRKSSSSAV GGKGIAPASP MLGNAGNPNK
490 500 510 520 530 540
ADIPERKKSP AVPSSNTASG GMTRRNTYVC SERCAADRHS VIQNGKENSA IPDERTPVAS
550 560 570 580 590 600
THSISSATTP DRIRFPRGTA SRSTFHGQPR ERRTATYNGP PASPSLSHEA TPLSQTRSRG
610 620 630 640 650 660
STNLFSKLTS KLTRRNMSFR FIKRLPTEYE RNGRYEGSSR NVSSEQKDEN REAKPRSLRF
670 680 690 700 710 720
TWSMKTTSSM DPSDMMREIR KVLDANNCDY EQRERFLLFC VHGDGHAENL VQWEMEVCKL
730 740 750
PRLSLNGVRF KRISGTSIAF KNIASKIANE LKL