Q19469

SS
Gene name
sad-1 (F15A2.6)
Protein name
Serine/threonine kinase SAD-1
Names
EC 2.7.11.1 , Synapses of Amphids Defective
Species
Caenorhabditis elegans
KEGG Pathway
cel:CELE_F15A2.6
EC number
2.7.11.1: Protein-serine/threonine kinases
Protein Class

Descriptions

SAD-B is a serine/threonine kinase involved in neuronal development, cell cycle, and energy metabolism. It is highly expressed in the brain and plays a role in axonal arborization, nerve terminal maturation, and neurotransmitter release. SAD-B contains an AIS near the KA1 domain that regulates its activity. This sequence is flexible and solvent-accessible, allowing it to interact with the kinase domain (KD) and ubiquitin-associated (UBA) domain to inhibit SAD-B activity. The crystal structure of the mouse SAD-B AIS-KA1 fragment reveals that the AIS is highly flexible in its isolated state, suggesting its readiness to bind to the KD-UBA junction for autoinhibition. Furthermore, the biochemical experiments demonstrate that the AIS of SAD-B non-competitively inhibits the kinase activity of SAD-B, similar to the autoinhibition observed in SAD-A, indicating a conserved mechanism between these kinases.

Autoinhibitory domains (AIDs)

634-648 (Autoinhibitory sequence, AIS) SS

Target domain

47-368 (KD-UBA domains)

Relief mechanism

Ligand binding, Others

Assay

314-370 (UBA domain) SS

Target domain

649-757 (KA1 domain)

Relief mechanism

Ligand binding, Others

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

0 structures for Q19469

Entry ID Method Resolution Chain Position Source
No available structures

No variants for Q19469

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q19469

No associated diseases with Q19469

4 regional properties for Q19469

Type Name Position InterPro Accession
domain Protein kinase domain 47 - 298 IPR000719
active_site Serine/threonine-protein kinase, active site 165 - 177 IPR008271
binding_site Protein kinase, ATP binding site 53 - 76 IPR017441
domain BRSK1/2-like, UBA domain 327 - 379 IPR048622

Functions

Description
EC Number 2.7.11.1 Protein-serine/threonine kinases
Subcellular Localization
  • Synapse
  • Synapse localization is regulated by strd-1
  • Co-localizes with strd-1 in synapses
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
axon The long process of a neuron that conducts nerve impulses, usually away from the cell body to the terminals and varicosities, which are sites of storage and release of neurotransmitter.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
dendrite A neuron projection that has a short, tapering, morphology. Dendrites receive and integrate signals from other neurons or from sensory stimuli, and conduct nerve impulses towards the axon or the cell body. In most neurons, the impulse is conveyed from dendrites to axon via the cell body, but in some types of unipolar neuron, the impulse does not travel via the cell body.
synapse The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.

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 activity Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction
protein serine kinase activity Catalysis of the reactions
protein serine/threonine kinase activity Catalysis of the reactions
tau-protein kinase activity Catalysis of the reaction

14 GO annotations of biological process

Name Definition
axo-dendritic transport The directed movement of organelles or molecules along microtubules in neuron projections.
axon guidance The chemotaxis process that directs the migration of an axon growth cone to a specific target site in response to a combination of attractive and repulsive cues.
axonogenesis De novo generation of a long process of a neuron, including the terminal branched region. Refers to the morphogenesis or creation of shape or form of the developing axon, which carries efferent (outgoing) action potentials from the cell body towards target cells.
establishment of cell polarity The specification and formation of anisotropic intracellular organization or cell growth patterns.
establishment or maintenance of cell polarity Any cellular process that results in the specification, formation or maintenance of anisotropic intracellular organization or cell growth patterns.
intracellular signal transduction The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell.
microtubule cytoskeleton organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising microtubules and their associated proteins.
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.
presynapse organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a presynapse.
protein localization Any process in which a protein is transported to, or maintained in, a specific location.
regulation of axon extension Any process that modulates the rate, direction or extent of axon extension.
synapse assembly The aggregation, arrangement and bonding together of a set of components to form a synapse. This process ends when the synapse is mature (functional).
synapse organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a synapse, the junction between a neuron and a target (neuron, muscle, or secretory cell).
synaptic vesicle transport The directed movement of synaptic vesicles.

11 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8TDC3 BRSK1 Serine/threonine-protein kinase BRSK1 Homo sapiens (Human) SS
Q8IWQ3 BRSK2 Serine/threonine-protein kinase BRSK2 Homo sapiens (Human) PR
Q69Z98 Brsk2 Serine/threonine-protein kinase BRSK2 Mus musculus (Mouse) EV
Q5RJI5 Brsk1 Serine/threonine-protein kinase BRSK1 Mus musculus (Mouse) EV
D3ZML2 Brsk2 Serine/threonine-protein kinase BRSK2 Rattus norvegicus (Rat) SS
B2DD29 Brsk1 Serine/threonine-protein kinase BRSK1 Rattus norvegicus (Rat) SS
Q10GB1 NEK1 Serine/threonine-protein kinase Nek1 Oryza sativa subsp japonica (Rice) PR
Q6ZEZ5 NEK3 Serine/threonine-protein kinase Nek3 Oryza sativa subsp japonica (Rice) PR
Q21017 kin-29 Serine/threonine-protein kinase kin-29 Caenorhabditis elegans SS
P45894 aak-1 5'-AMP-activated protein kinase catalytic subunit alpha-1 Caenorhabditis elegans SS
Q95ZQ4 aak-2 5'-AMP-activated protein kinase catalytic subunit alpha-2 Caenorhabditis elegans SS
10 20 30 40 50 60
MFEALKEVLG EINSKLAAVN NELSSKIMSE NIVSTRPVAQ AQYCGPYKLE KTLGKGQTGL
70 80 90 100 110 120
VKTGTHCITG RKVAIKIVNK EKLSESVLQK VEREIAIMKL IEHPHVLHLY DVYENKKYLY
130 140 150 160 170 180
LLLEHVSGGE LFDYLVRKGR LMSKEARKFF RQIISALDFC HAHNICHRDL KPENLLLDER
190 200 210 220 230 240
NNIKVADFGM ASLQVEGSML ETSCGSPHYA CPEVIRGEKY DGRKADVWSC GVILYALLVG
250 260 270 280 290 300
ALPFDDDNLR NLLEKVKRGV FHIPHFVPAD VQSLLRAMIE VDPGKRYSLA DVFKHPWVSG
310 320 330 340 350 360
TTKADPELEL PMSQVVQTHV IPGEDSIDPD VLRHMNCLGC FKDKQKLINE LLSPKHNTEK
370 380 390 400 410 420
MVYFLLLDRK RRRPAQEDDT EIVLRGAAQN NDPPKKRTDS SRTSRYPMGS IADGSPINPR
430 440 450 460 470 480
KTYGRNQKSG RHSSLGGSPT ESPRSSTRDL FGSSSSGSYS ARAGEDRDRG RSASRSTNSY
490 500 510 520 530 540
HYYTQPVDPQ TLAEAARHVR DAQERRESRD SGRGSSRKES KDRSDKSASS SSCKNDASST
550 560 570 580 590 600
SSVPHKYSPP SVMSESVVVS SSTMNSTNSS TNSLIAGNSQ TSIGSTSGPW RSKLNNIKNS
610 620 630 640 650 660
FLGTPRFHRR KMSNGTAESD SEDSQMIDTT DLVKKSWFGS LASSMSVERD DTHCVPVQGK
670 680 690 700 710 720
TLNSIKAELI RAFLQIHELS HSVVGQNCFR VEYKRGPTVG GSVFSRGIKM NVDIIPSPQQ
730 740 750 760 770 780
VVIAGETPTY VVQFVLLAGP VRRFKRLVEH LSAILQNSTQ QRADRQQQAA LMVRPRRLSD
790 800 810 820 830 840
SSVGSACSDS ESNASSINMI ARHSDKTETT SATSSDPYGP SPSMRSVGSG TANSYKSPTP
850 860 870 880 890 900
HRRNTTAVTA SSSSASNRYG PSSSSSGSYS NNADYSYHPE YSQRSNGSSA PKNQYSPGSQ
910
RSFAFSMFNK ADKV