P61267
Gene name |
STX1B (STX1B2) |
Protein name |
Syntaxin-1B |
Names |
Synaptocanalin I, Syntaxin-1B2 |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:282377 |
EC number |
|
Protein Class |
|
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 P61267
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P61267-F1 | Predicted | AlphaFoldDB |
37 variants for P61267
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs453807456 | 3 | D>N | No | EVA | |
| rs440173392 | 8 | L>R | No | EVA | |
| rs471700875 | 9 | R>G | No | EVA | |
| rs451492110 | 10 | S>G | No | EVA | |
| rs437996331 | 10 | S>R | No | EVA | |
| rs463812737 | 11 | A>V | No | EVA | |
| rs443856280 | 16 | D>A | No | EVA | |
| rs475164671 | 17 | E>D | No | EVA | |
| rs461657845 | 18 | E>* | No | EVA | |
| rs472822295 | 21 | V>F | No | EVA | |
| rs432722533 | 27 | H>P | No | EVA | |
| rs443193282 | 36 | V>E | No | EVA | |
| rs469572446 | 95 | I>M | No | EVA | |
| rs449514632 | 96 | E>* | No | EVA | |
| rs435907512 | 107 | R>S | No | EVA | |
| rs467244825 | 111 | D>G | No | EVA | |
| rs447331524 | 114 | I>T | No | EVA | |
| rs465032896 | 115 | R>S | No | EVA | |
| rs444902426 | 117 | T>A | No | EVA | |
| rs479957759 | 122 | L>P | No | EVA | |
| rs459828428 | 123 | S>C | No | EVA | |
| rs471130033 | 128 | E>K | No | EVA | |
| rs475089986 | 140 | Y>S | No | EVA | |
| rs455198409 | 142 | D>A | No | EVA | |
| rs472946942 | 150 | R>W | No | EVA | |
| rs432973582 | 152 | L>M | No | EVA | |
| rs432973582 | 152 | L>V | No | EVA | |
| rs464294836 | 153 | E>D | No | EVA | |
| rs458782776 | 242 | Y>* | No | EVA | |
| rs438563753 | 243 | V>G | No | EVA | |
| rs483014840 | 245 | R>G | No | EVA | |
| rs519951461 | 247 | V>A | No | EVA | |
| rs462643087 | 261 | R>G | No | EVA | |
| rs442782296 | 262 | R>G | No | EVA | |
| rs471336777 | 270 | C>F | No | EVA | |
| rs451269223 | 271 | C>S | No | EVA | |
| rs437685366 | 276 | V>M | No | EVA |
No associated diseases with P61267
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
| 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. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| 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. |
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| exocytic insertion of neurotransmitter receptor to postsynaptic membrane | The exocytic fusion of neurotransmitter receptor containing vesicles with the postsynaptic membrane resulting in the integration of NT receptors, enabling them to participate in neurotransmitter reception. This process includes tethering and docking steps that prepare vesicles for fusion. |
| 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. |
| 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. |
| regulation of exocytosis | Any process that modulates the frequency, rate or extent of exocytosis. |
| 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 |
| P32850 | STX1A | Syntaxin-1A | Bos taurus (Bovine) | PR |
| Q3ZBT5 | STX7 | Syntaxin-7 | Bos taurus (Bovine) | PR |
| Q7KVY7 | Syx4 | Syntaxin-4 | Drosophila melanogaster (Fruit fly) | PR |
| Q24547 | Syx1A | Syntaxin-1A | Drosophila melanogaster (Fruit fly) | PR |
| Q16623 | STX1A | Syntaxin-1A | Homo sapiens (Human) | PR |
| Q12846 | STX4 | Syntaxin-4 | Homo sapiens (Human) | PR |
| O75558 | STX11 | Syntaxin-11 | Homo sapiens (Human) | PR |
| P61266 | STX1B | Syntaxin-1B | Homo sapiens (Human) | PR |
| O35526 | Stx1a | Syntaxin-1A | Mus musculus (Mouse) | 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 |
| P50279 | Stx2 | Syntaxin-2 | Rattus norvegicus (Rat) | PR |
| Q08850 | Stx4 | Syntaxin-4 | Rattus norvegicus (Rat) | PR |
| P32851 | Stx1a | Syntaxin-1A | Rattus norvegicus (Rat) | PR |
| P61265 | Stx1b | Syntaxin-1B | 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 |
| MKDRTQELRS | AKDSDDEEEV | VHVDRDHFMD | EFFEQVEEIR | GCIEKLSEDV | EQVKKQHSAI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LAAPNPDEKT | KQELEDLTTD | IKKTANKVRS | KLKAIEQSIE | QEEGLNRSSA | DLRIRKTQHS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TLSRKFVEVM | TEYNATQSKY | RDRCKDRIQR | QLEITGRTTT | NEELEDMLES | GKLAIFTDDI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KMDSQMTKQA | LNEIETRHNE | IIKLETSIRE | LHDMFVDMAM | LVESQGEMID | RIEYNVEHSV |
| 250 | 260 | 270 | 280 | ||
| DYVERAVSDT | KKAVKYQSKA | RRKKIMIIIC | CVVLGVVLAS | SIGGTLGL |