Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q16623

Entry ID Method Resolution Chain Position Source
AF-Q16623-F1 Predicted AlphaFoldDB

161 variants for Q16623

Variant ID(s) Position Change Description Diseaes Association Provenance
RCV001264639
rs200456346
RCV002226530
145 C>W Intellectual disability [ClinVar] Yes ClinVar
dbSNP
CA367838343
rs1305622716
2 K>R No ClinGen
TOPMed
CA367838323
rs1274838274
3 D>H No ClinGen
TOPMed
rs1343856512
CA367838287
5 T>S No ClinGen
TOPMed
CA367838271
rs1208045282
6 Q>R No ClinGen
TOPMed
rs547690713
CA367838246
7 E>D No ClinGen
1000Genomes
ExAC
TOPMed
gnomAD
CA367837199
rs1554617572
11 A>V No ClinGen
gnomAD
TCGA novel 13 D>N Variant assessed as Somatic; impact. [NCI-TCGA] No NCI-TCGA
rs782202692
CA4290860
13 D>V No ClinGen
ExAC
TOPMed
gnomAD
rs782455881
CA4290858
15 D>N Variant assessed as Somatic; 0.0 impact. [NCI-TCGA] No ClinGen
ExAC
NCI-TCGA
TOPMed
gnomAD
CA4290857
rs781810772
16 D>N No ClinGen
ExAC
gnomAD
TCGA novel 16 D>Y Variant assessed as Somatic; impact. [NCI-TCGA] No NCI-TCGA
rs1289948694
CA367837130
17 D>H No ClinGen
TOPMed
rs782671628
CA4290856
18 D>E No ClinGen
ExAC
gnomAD
CA4290853
rs782653375
21 A>S No ClinGen
ExAC
TOPMed
gnomAD
CA4290854
rs782653375
21 A>T No ClinGen
ExAC
TOPMed
gnomAD
rs567231961
CA4290852
21 A>V No ClinGen
1000Genomes
ExAC
gnomAD
rs1271164067
CA367837046
23 T>S No ClinGen
TOPMed
gnomAD
COSM3768472
rs369814636
CA4290850
24 V>M liver [Cosmic] No ClinGen
cosmic curated
ESP
ExAC
TOPMed
gnomAD
rs267601564
CA160087749
26 R>* No ClinGen
Ensembl
rs1364135079
CA367837019
26 R>Q No ClinGen
TOPMed
gnomAD
CA4290849
rs782703876
28 R>C Variant assessed as Somatic; 0.0 impact. [NCI-TCGA] No ClinGen
ExAC
NCI-TCGA
gnomAD
CA160087748
rs375523583
28 R>H No ClinGen
ESP
TOPMed
TCGA novel 33 F>C Variant assessed as Somatic; impact. [NCI-TCGA] No NCI-TCGA
CA367836853
rs1178632016
37 V>G No ClinGen
TOPMed
CA367836829
rs1554617460
39 E>D No ClinGen
gnomAD
CA367836834
rs1584250219
39 E>G No ClinGen
Ensembl
rs1554617458
CA367836812
COSM3833184
41 R>Q Variant assessed as Somatic; impact. breast [NCI-TCGA, Cosmic] No ClinGen
cosmic curated
NCI-TCGA
gnomAD
CA367836802
rs1554617455
42 G>A No ClinGen
gnomAD
rs1343838866
CA367836806
42 G>S No ClinGen
TOPMed
rs1584250193
CA367836786
44 I>V No ClinGen
Ensembl
rs144945504
CA367836740
48 A>S No ClinGen
ESP
ExAC
TOPMed
gnomAD
rs144945504
CA4290832
48 A>T No ClinGen
ESP
ExAC
TOPMed
gnomAD
rs1554617450
CA367836733
49 E>Q No ClinGen
gnomAD
rs2229854
CA4290831
50 N>K No ClinGen
1000Genomes
ESP
ExAC
TOPMed
gnomAD
rs1554617448
CA367836707
51 V>A No ClinGen
gnomAD
rs782757103
CA4290829
51 V>L No ClinGen
ExAC
gnomAD
CA160087498
rs782757103
51 V>M No ClinGen
ExAC
gnomAD
rs1346014749
CA367836694
52 E>D No ClinGen
TOPMed
gnomAD
CA4290828
rs782092932
56 R>Q No ClinGen
ExAC
TOPMed
gnomAD
CA367836623
rs1316169178
59 S>G No ClinGen
TOPMed
gnomAD
CA4290825
rs782151306
61 I>V No ClinGen
ExAC
gnomAD
CA367836576
rs1554617440
63 A>V No ClinGen
gnomAD
rs1554617438
CA367836566
64 S>Y No ClinGen
gnomAD
CA4290822
rs782259113
65 P>T No ClinGen
ExAC
gnomAD
rs2228607
CA367836523
68 D>E No ClinGen
1000Genomes
ESP
ExAC
TOPMed
gnomAD
CA4290820
rs782309912
68 D>N No ClinGen
ExAC
TOPMed
gnomAD
CA4290818
rs782665420
69 E>K No ClinGen
ExAC
gnomAD
rs1554616681
CA367836338
70 K>R No ClinGen
gnomAD
TCGA novel 70 K>T Variant assessed as Somatic; impact. [NCI-TCGA] No NCI-TCGA
COSM195749
rs781904935
CA4290787
71 T>M Variant assessed as Somatic; 0.0 impact. large_intestine [NCI-TCGA, Cosmic] No ClinGen
cosmic curated
ExAC
NCI-TCGA
gnomAD
rs781950897
CA4290784
76 E>G No ClinGen
ExAC
gnomAD
TCGA novel 77 E>* Variant assessed as Somatic; impact. [NCI-TCGA] No NCI-TCGA
CA367836293
rs1315627336
77 E>K No ClinGen
TOPMed
CA4290782
rs782043152
79 M>T No ClinGen
ExAC
TOPMed
gnomAD
CA4290781
rs781939626
80 S>F No ClinGen
ExAC
gnomAD
rs147048336
CA4290779
81 D>N No ClinGen
1000Genomes
ESP
ExAC
TOPMed
gnomAD
CA367836265
rs147048336
81 D>Y No ClinGen
1000Genomes
ESP
ExAC
TOPMed
gnomAD
rs371575027
CA4290777
85 T>A No ClinGen
ESP
ExAC
TOPMed
gnomAD
CA367836227
rs1469008260
86 A>G No ClinGen
TOPMed
CA367836201
rs1192968907
90 R>C No ClinGen
TOPMed
gnomAD
rs944672566
CA160086042
90 R>H No ClinGen
Ensembl
TCGA novel 94 K>A Variant assessed as Somatic; impact. [NCI-TCGA] No NCI-TCGA
CA367836167
rs782219643
94 K>N No ClinGen
ExAC
TOPMed
gnomAD
CA367836131
rs1554616488
97 E>D No ClinGen
gnomAD
CA367836119
rs1390792461
99 S>A No ClinGen
TOPMed
rs782236446
CA4290756
100 I>F No ClinGen
ExAC
TCGA novel 100 I>V Variant assessed as Somatic; impact. [NCI-TCGA] No NCI-TCGA
CA4290755
rs782657148
101 E>Q No ClinGen
ExAC
gnomAD
rs907617478
CA160085679
105 G>A No ClinGen
Ensembl
rs782226371
CA4290753
108 R>C No ClinGen
ExAC
gnomAD
CA367836034
rs1584244001
112 D>A No ClinGen
Ensembl
rs1554616484
CA367836030
112 D>E No ClinGen
gnomAD
CA367836029
rs1554616482
113 L>V No ClinGen
gnomAD
CA4290748
rs782517349
116 R>Q No ClinGen
ExAC
gnomAD
rs1554616478
CA367835997
118 T>S No ClinGen
gnomAD
CA4290727
rs376660582
129 E>D No ClinGen
ESP
ExAC
TOPMed
gnomAD
rs1554616439
CA367835884
132 S>L No ClinGen
gnomAD
CA367835887
rs1361778002
132 S>T No ClinGen
TOPMed
CA367835877
rs1554616436
133 E>D No ClinGen
gnomAD
TCGA novel 133 E>K Variant assessed as Somatic; impact. [NCI-TCGA] No NCI-TCGA
CA367835857
rs1159515604
136 A>T No ClinGen
TOPMed
gnomAD
CA4290724
rs782758639
138 Q>L No ClinGen
ExAC
gnomAD
CA367835835
rs1438131669
139 S>F No ClinGen
TOPMed
gnomAD
rs782129449
CA367835834
140 D>H No ClinGen
ExAC
gnomAD
rs782129449
CA4290723
140 D>N No ClinGen
ExAC
gnomAD
CA367835818
rs1554616427
142 R>S No ClinGen
gnomAD
rs144263690
CA4290720
144 R>C No ClinGen
ESP
ExAC
TOPMed
gnomAD
rs144263690
CA4290719
144 R>G No ClinGen
ESP
ExAC
TOPMed
gnomAD
CA367835802
rs1554616422
144 R>H No ClinGen
gnomAD
CA4290717
rs782171983
145 C>S No ClinGen
ExAC
gnomAD
CA367835777
rs1554616419
148 R>H No ClinGen
gnomAD
CA367835748
rs1554616416
152 Q>R No ClinGen
gnomAD
CA4290714
rs782217059
154 E>A No ClinGen
ExAC
gnomAD
rs1554616412
CA367835725
155 I>M No ClinGen
gnomAD
rs1025168062 156 T>= Variant assessed as Somatic; impact. [NCI-TCGA] No NCI-TCGA
rs373330016
CA4290692
157 G>C No ClinGen
ESP
ExAC
TOPMed
gnomAD
CA367835705
rs373330016
157 G>S No ClinGen
ESP
ExAC
TOPMed
gnomAD
CA4290691
rs370111355
157 G>V No ClinGen
ESP
ExAC
TOPMed
gnomAD
CA367835659
rs1554616291
164 E>K No ClinGen
gnomAD
CA4290689
rs782404923
165 L>P No ClinGen
ExAC
gnomAD
CA367835603
rs782343806
CA4290686
171 S>R No ClinGen
ExAC
gnomAD
CA367835582
rs1350740883
175 A>T No ClinGen
TOPMed
gnomAD
CA367835560
rs1229777156
178 A>T No ClinGen
TOPMed
rs782316927
CA4290642
182 I>M No ClinGen
ExAC
TOPMed
gnomAD
rs1325188922
CA367835487
183 M>L No ClinGen
TOPMed
gnomAD
CA4290641
rs567608089
187 I>V No ClinGen
1000Genomes
ExAC
TOPMed
gnomAD
rs1194587551
CA367835424
188 S>L No ClinGen
TOPMed
rs149588890
CA4290640
191 A>D No ClinGen
ESP
ExAC
gnomAD
CA367835338
rs1199098748
196 E>A No ClinGen
TOPMed
TCGA novel 196 E>D Variant assessed as Somatic; impact. [NCI-TCGA] No NCI-TCGA
CA367835320
rs1430272820
197 T>M Variant assessed as Somatic; impact. [NCI-TCGA] No ClinGen
NCI-TCGA
TOPMed
gnomAD
rs782589459
CA4290637
198 R>L No ClinGen
ExAC
gnomAD
CA367835207
rs1554616127
207 N>K No ClinGen
gnomAD
CA367835179
rs1384422759
210 R>C Variant assessed as Somatic; impact. [NCI-TCGA] No ClinGen
NCI-TCGA
TOPMed
CA367835177
rs1401337421
COSM1240336
210 R>H oesophagus [Cosmic] No ClinGen
cosmic curated
TOPMed
gnomAD
rs782529244
CA4290633
213 H>Y No ClinGen
ExAC
TOPMed
gnomAD
COSM1091595
CA367835136
rs1435523092
214 D>N Variant assessed as Somatic; 0.0 impact. endometrium [NCI-TCGA, Cosmic] No ClinGen
cosmic curated
NCI-TCGA
TOPMed
gnomAD
rs1435523092
CA367835139
214 D>Y No ClinGen
TOPMed
gnomAD
rs139237669
CA4290631
217 M>T No ClinGen
ESP
ExAC
TOPMed
gnomAD
rs1283617158
CA367835099
217 M>V No ClinGen
TOPMed
gnomAD
rs782121987
CA4290630
219 M>T No ClinGen
ExAC
gnomAD
rs370963256
CA4290628
221 M>T No ClinGen
ESP
ExAC
gnomAD
rs781827788
CA4290629
221 M>V No ClinGen
ExAC
TOPMed
gnomAD
CA367835033
rs782057252
222 L>F No ClinGen
ExAC
TOPMed
gnomAD
CA4290627
rs782057252
222 L>I No ClinGen
ExAC
TOPMed
gnomAD
rs782057252
CA367835035
222 L>V No ClinGen
ExAC
TOPMed
gnomAD
CA367835026
rs1554616102
223 V>L No ClinGen
gnomAD
TCGA novel 229 M>I Variant assessed as Somatic; impact. [NCI-TCGA] No NCI-TCGA
rs1187928316
CA367833939
230 I>T No ClinGen
TOPMed
rs529603065
CA4290572
231 D>N No ClinGen
1000Genomes
ExAC
gnomAD
rs782584153
CA4290571
233 I>V No ClinGen
ExAC
gnomAD
rs782747612
CA4290568
237 V>L No ClinGen
ExAC
gnomAD
CA367833868
rs1333991998
240 A>S No ClinGen
TOPMed
gnomAD
CA367833869
rs1333991998
240 A>T No ClinGen
TOPMed
gnomAD
CA4290565
rs782756808
241 V>I No ClinGen
ExAC
gnomAD
CA367833855
rs1554615742
242 D>H No ClinGen
gnomAD
rs1554615733
CA367833811
247 A>T No ClinGen
gnomAD
CA367833803
rs782801540
248 V>L No ClinGen
ExAC
gnomAD
CA4290562
rs782801540
248 V>M No ClinGen
ExAC
gnomAD
rs782658280
CA4290560
255 V>I No ClinGen
ExAC
gnomAD
CA367833732
rs1554615726
256 K>T No ClinGen
gnomAD
rs782212937
CA4290558
262 R>C No ClinGen
ExAC
TOPMed
gnomAD
rs202064998
CA4290557
262 R>H No ClinGen
1000Genomes
ExAC
gnomAD
rs202064998
CA367833680
262 R>P No ClinGen
1000Genomes
ExAC
gnomAD
CA160083585
rs782153036
263 R>Q No ClinGen
TOPMed
gnomAD
rs782058423
CA4290540
267 M>V No ClinGen
ExAC
gnomAD
rs991448424
CA160083462
269 I>F No ClinGen
Ensembl
rs1554615661
CA367833606
270 I>T No ClinGen
gnomAD
CA367833590
rs1554615659
272 C>S No ClinGen
gnomAD
rs782413114
CA4290537
274 I>V No ClinGen
ExAC
gnomAD
rs1554615657
CA367833569
276 G>S No ClinGen
gnomAD
CA367833562
rs1554615654
277 I>V No ClinGen
gnomAD
CA4290534
rs782341932
278 V>A No ClinGen
ExAC
gnomAD
CA4290535
rs201037992
278 V>I Variant assessed as Somatic; 0.0 impact. [NCI-TCGA] No ClinGen
1000Genomes
ExAC
NCI-TCGA
TOPMed
gnomAD
CA4290533
rs782224823
279 I>V No ClinGen
ExAC
gnomAD
rs782328797
CA4290531
280 A>T Variant assessed as Somatic; 0.0 impact. [NCI-TCGA] No ClinGen
ExAC
NCI-TCGA
gnomAD
CA4290530
rs782275853
284 G>A No ClinGen
ExAC
gnomAD
CA4290528
rs782504771
286 I>T No ClinGen
ExAC
TOPMed
gnomAD
rs1311585207
CA367833504
287 F>I No ClinGen
TOPMed
CA4290526
rs782606855
288 A>T No ClinGen
ExAC
gnomAD

1 associated diseases with Q16623

Without disease ID

3 regional properties for Q16623

Type Name Position InterPro Accession
domain Target SNARE coiled-coil homology domain 187 - 279 IPR000727
domain Syntaxin, N-terminal domain 25 - 227 IPR006011
conserved_site Syntaxin/epimorphin, conserved site 198 - 237 IPR006012

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane ; Single-pass type IV membrane protein
  • Synapse, synaptosome
  • Cell membrane
  • Colocalizes with KCNB1 at the cell membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

22 GO annotations of cellular component

Name Definition
actomyosin Any complex of actin, myosin, and accessory proteins.
anchoring junction A cell junction that mechanically attaches a cell (and its cytoskeleton) to neighboring cells or to the extracellular matrix.
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.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
endomembrane system A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles.
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
glutamatergic synapse A synapse that uses glutamate as a neurotransmitter.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
integral component of presynaptic membrane The component of the presynaptic membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
integral component of synaptic vesicle membrane The component of the synaptic vesicle membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
neuron projection A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
nuclear membrane Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
postsynaptic density An electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.
presynaptic active zone membrane The membrane portion of the presynaptic active zone; it is the site where docking and fusion of synaptic vesicles occurs for the release of neurotransmitters.
secretory granule A small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion. Secretory granules move towards the periphery of the cell and upon stimulation, their membranes fuse with the cell membrane, and their protein load is exteriorized. Processing of the contained protein may take place in secretory granules.
SNARE complex A protein complex involved in membrane fusion; a stable ternary complex consisting of a four-helix bundle, usually formed from one R-SNARE and three Q-SNAREs with an ionic layer sandwiched between hydrophobic layers. One well-characterized example is the neuronal SNARE complex formed of synaptobrevin 2, syntaxin 1a, and SNAP-25.
synaptic vesicle A secretory organelle, typically 50 nm in diameter, of presynaptic nerve terminals; accumulates in high concentrations of neurotransmitters and secretes these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
synaptobrevin 2-SNAP-25-syntaxin-1a complex A SNARE complex that contains synaptobrevin 2 (VAMP2), SNAP-25, and syntaxin 1a (or orthologs thereof).
synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex A SNARE complex that contains synaptobrevin 2 (VAMP2), SNAP-25, syntaxin 1a, and complexin I (or orthologs thereof).
synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex A SNARE complex that contains synaptobrevin 2 (VAMP2), SNAP-25, syntaxin 1a, and complexin II (or orthologs thereof).
voltage-gated potassium channel complex A protein complex that forms a transmembrane channel through which potassium ions may cross a cell membrane in response to changes in membrane potential.

13 GO annotations of molecular function

Name Definition
ATP-dependent protein binding Binding to a protein or protein complex using energy from ATP hydrolysis.
calcium channel inhibitor activity Binds to and stops, prevents, or reduces the activity of a calcium channel.
calcium-dependent protein binding Binding to a protein or protein complex in the presence of calcium.
chloride channel inhibitor activity Binds to and stops, prevents, or reduces the activity of a chloride channel.
identical protein binding Binding to an identical protein or proteins.
kinase binding Binding to a kinase, any enzyme that catalyzes the transfer of a phosphate group.
myosin head/neck binding Binding to the head/neck region of a myosin heavy chain.
protein domain specific binding Binding to a specific domain of a protein.
protein N-terminus binding Binding to a protein N-terminus, the end of any peptide chain at which the 2-amino (or 2-imino) function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
protein-containing complex binding Binding to a macromolecular complex.
SNAP receptor activity Acting as a marker to identify a membrane and interacting selectively with one or more SNAREs on another membrane to mediate membrane fusion.
SNARE binding Binding to a SNARE (soluble N-ethylmaleimide-sensitive factor attached protein receptor) protein.
transmembrane transporter binding Binding to a transmembrane transporter, a protein or protein complex that enables the transfer of a substance, usually a specific substance or a group of related substances, from one side of a membrane to the other.

22 GO annotations of biological process

Name Definition
calcium-ion regulated exocytosis The release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle by fusion of the vesicle with the plasma membrane of a cell, induced by a rise in cytosolic calcium-ion levels.
exocytosis A process of secretion by a cell that results in the release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle. Exocytosis can occur either by full fusion, when the vesicle collapses into the plasma membrane, or by a kiss-and-run mechanism that involves the formation of a transient contact, a pore, between a granule (for exemple of chromaffin cells) and the plasma membrane. The latter process most of the time leads to only partial secretion of the granule content. Exocytosis begins with steps that prepare vesicles for fusion with the membrane (tethering and docking) and ends when molecules are secreted from the cell.
insulin secretion The regulated release of proinsulin from secretory granules accompanied by cleavage of proinsulin to form mature insulin. In vertebrates, insulin is secreted from B granules in the B cells of the vertebrate pancreas and from insulin-producing cells in insects.
intracellular protein transport The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic cell.
positive regulation of calcium ion-dependent exocytosis Any process that activates or increases the frequency, rate or extent of calcium ion-dependent exocytosis.
positive regulation of catecholamine secretion Any process that activates or increases the frequency, rate or extent of the regulated release of a catecholamine.
positive regulation of excitatory postsynaptic potential Any process that enhances the establishment or increases the extent of the excitatory postsynaptic potential (EPSP) which is a temporary increase in postsynaptic potential due to the flow of positively charged ions into the postsynaptic cell. The flow of ions that causes an EPSP is an excitatory postsynaptic current (EPSC) and makes it easier for the neuron to fire an action potential.
positive regulation of neurotransmitter secretion Any process that activates or increases the frequency, rate or extent of the regulated release of a neurotransmitter.
positive regulation of norepinephrine secretion Any process that increases the frequency, rate or extent of the regulated release of norepinephrine.
protein localization to membrane A process in which a protein is transported to, or maintained in, a specific location in a membrane.
protein sumoylation The process in which a SUMO protein (small ubiquitin-related modifier) is conjugated to a target protein via an isopeptide bond between the carboxy-terminus of SUMO with an epsilon-amino group of a lysine residue of the target protein.
regulation of insulin secretion Any process that modulates the frequency, rate or extent of the regulated release of insulin.
regulation of synaptic vesicle priming Any process that modulates the frequency, rate or extent of synaptic vesicle priming. Synaptic vesicle priming is the formation of SNARE-containing complexes, bringing synaptic vesicle membrane and plasma membranes into close proximity and thereby facilitating membrane fusion.
response to gravity Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a gravitational stimulus.
secretion by cell The controlled release of a substance by a cell.
SNARE complex assembly The aggregation, arrangement and bonding together of a set of components to form a SNARE complex, a protein complex involved in membrane fusion; a stable ternary complex consisting of a four-helix bundle, usually formed from one R-SNARE and three Q-SNAREs with an ionic layer sandwiched between hydrophobic layers.
synaptic vesicle docking The initial (indirect) attachment of a synaptic vesicle membrane to the presynaptic active zone membrane, mediated by proteins protruding from the membrane and proteins of the presynaptic active zone cytoplasmic component. Synaptic vesicle tethering is the first step in this process.
synaptic vesicle endocytosis A vesicle-mediated transport process, in which the synaptic vesicle membrane constituents are retrieved from the presynaptic membrane on the axon terminal after neurotransmitter secretion by exocytosis. Synaptic vesicle endocytosis can occur via clathrin-dependent and clathrin-independent mechanisms.
synaptic vesicle exocytosis Fusion of intracellular membrane-bounded vesicles with the pre-synaptic membrane of the neuronal cell resulting in release of neurotransmitter into the synaptic cleft.
synaptic vesicle fusion to presynaptic active zone membrane Fusion of the membrane of a synaptic vesicle with the presynaptic active zone membrane, thereby releasing its cargo neurotransmitters into the synaptic cleft.
vesicle docking The initial attachment of a transport vesicle membrane to the target membrane, mediated by proteins protruding from the membrane of the vesicle and the target membrane. Docking requires only that the two membranes come close enough for these proteins to interact and adhere.
vesicle fusion Fusion of the membrane of a transport vesicle with its target membrane.

22 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P32867 SSO1 Protein SSO1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P39926 SSO2 Protein SSO2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q3SWZ3 STX4 Syntaxin-4 Bos taurus (Bovine) PR
P61267 STX1B Syntaxin-1B Bos taurus (Bovine) PR
P32850 STX1A Syntaxin-1A Bos taurus (Bovine) PR
Q7KVY7 Syx4 Syntaxin-4 Drosophila melanogaster (Fruit fly) PR
Q24547 Syx1A Syntaxin-1A Drosophila melanogaster (Fruit fly) PR
Q12846 STX4 Syntaxin-4 Homo sapiens (Human) PR
P61266 STX1B Syntaxin-1B Homo sapiens (Human) PR
O75558 STX11 Syntaxin-11 Homo sapiens (Human) PR
O15400 STX7 Syntaxin-7 Homo sapiens (Human) PR
Q00262 Stx2 Syntaxin-2 Mus musculus (Mouse) PR
P70452 Stx4 Syntaxin-4 Mus musculus (Mouse) PR
Q9D3G5 Stx11 Syntaxin-11 Mus musculus (Mouse) PR
P61264 Stx1b Syntaxin-1B Mus musculus (Mouse) PR
O35526 Stx1a Syntaxin-1A Mus musculus (Mouse) PR
P50279 Stx2 Syntaxin-2 Rattus norvegicus (Rat) PR
P61265 Stx1b Syntaxin-1B Rattus norvegicus (Rat) PR
Q08850 Stx4 Syntaxin-4 Rattus norvegicus (Rat) PR
P32851 Stx1a Syntaxin-1A Rattus norvegicus (Rat) PR
O16000 unc-64 Syntaxin-1A homolog Caenorhabditis elegans PR
Q9ZPV9 SYP112 Syntaxin-112 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MKDRTQELRT AKDSDDDDDV AVTVDRDRFM DEFFEQVEEI RGFIDKIAEN VEEVKRKHSA
70 80 90 100 110 120
ILASPNPDEK TKEELEELMS DIKKTANKVR SKLKSIEQSI EQEEGLNRSS ADLRIRKTQH
130 140 150 160 170 180
STLSRKFVEV MSEYNATQSD YRERCKGRIQ RQLEITGRTT TSEELEDMLE SGNPAIFASG
190 200 210 220 230 240
IIMDSSISKQ ALSEIETRHS EIIKLENSIR ELHDMFMDMA MLVESQGEMI DRIEYNVEHA
250 260 270 280
VDYVERAVSD TKKAVKYQSK ARRKKIMIII CCVILGIVIA STVGGIFA