Stx1a (syntaxin 1A) - Rat Genome Database

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Gene: Stx1a (syntaxin 1A) Rattus norvegicus
Analyze
Symbol: Stx1a
Name: syntaxin 1A
RGD ID: 69430
Description: Enables several functions, including ATP-dependent protein binding activity; calcium-dependent protein binding activity; and transmembrane transporter binding activity. Involved in several processes, including SNARE complex assembly; positive regulation of secretion by cell; and synaptic vesicle exocytosis. Located in several cellular components, including actomyosin; postsynaptic density; and secretory granule. Part of several cellular components, including synaptobrevin 2-SNAP-25-syntaxin-1a complex; synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; and synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex. Is active in several cellular components, including Schaffer collateral - CA1 synapse; synaptic membrane; and synaptic vesicle membrane. Human ortholog(s) of this gene implicated in Creutzfeldt-Jakob disease and Hirschsprung's disease. Orthologous to human STX1A (syntaxin 1A); PARTICIPATES IN insulin secretion pathway; INTERACTS WITH (S)-amphetamine; 2,3,7,8-tetrachlorodibenzodioxine; 6-propyl-2-thiouracil.
Type: protein-coding
RefSeq Status: PROVISIONAL
Previously known as: neuron-specific antigen HPC-1; P35A; synaptotagmin-associated 35 kDa protein; syntaxin 1 a; syntaxin 1 A (brain); syntaxin 1A (brain); syntaxin 1A (brain)-like; syntaxin-1A
RGD Orthologs
Human
Mouse
Chinchilla
Bonobo
Dog
Squirrel
Green Monkey
Naked Mole-Rat
Alliance Genes
More Info more info ...
Is Marker For: Strains:   BB/OK  
Latest Assembly: mRatBN7.2 - mRatBN7.2 Assembly
Position:
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCr81227,278,517 - 27,306,547 (-)NCBIGRCr8
mRatBN7.21221,641,971 - 21,670,022 (-)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl1221,641,969 - 21,669,930 (-)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx1222,782,666 - 22,810,512 (-)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.01223,394,983 - 23,422,828 (-)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.01222,463,210 - 22,491,166 (-)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.01224,682,050 - 24,710,002 (-)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl1224,682,041 - 24,710,019 (-)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.01226,682,320 - 26,710,272 (-)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.41222,737,112 - 22,765,064 (-)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
Celera1223,405,260 - 23,432,900 (-)NCBICelera
Cytogenetic Map12q12NCBI
JBrowse: View Region in Genome Browser (JBrowse)
Model


Gene-Chemical Interaction Annotations     Click to see Annotation Detail View
(S)-amphetamine  (EXP)
1,2-dichloroethane  (ISO)
1,2-dimethylhydrazine  (ISO)
17beta-estradiol  (ISO)
2,3,7,8-tetrachlorodibenzodioxine  (EXP,ISO)
3,4-methylenedioxymethamphetamine  (ISO)
6-propyl-2-thiouracil  (EXP)
acrolein  (ISO)
aflatoxin B1  (ISO)
all-trans-retinoic acid  (ISO)
alpha-pinene  (ISO)
ammonium chloride  (EXP)
amphetamine  (EXP)
antirheumatic drug  (ISO)
aristolochic acid A  (ISO)
arsane  (ISO)
arsenic atom  (ISO)
Asiaticoside  (EXP)
atrazine  (EXP)
barium chloride  (EXP)
benzo[a]pyrene  (ISO)
bisphenol A  (EXP,ISO)
cisplatin  (ISO)
clozapine  (EXP)
copper(II) sulfate  (ISO)
crocidolite asbestos  (ISO)
cyclosporin A  (ISO)
cylindrospermopsin  (ISO)
decabromodiphenyl ether  (EXP)
dextran sulfate  (ISO)
diazinon  (ISO)
diethylstilbestrol  (EXP)
doxorubicin  (ISO)
ethanol  (EXP,ISO)
etomidate  (EXP)
fenvalerate  (EXP)
fisetin  (EXP)
flavonoids  (EXP)
furan  (EXP)
gamma-tocopherol  (ISO)
gentamycin  (EXP)
haloperidol  (EXP)
hydrogen peroxide  (ISO)
ivermectin  (ISO)
lead diacetate  (EXP)
lipopolysaccharide  (ISO)
maneb  (ISO)
methylmercury chloride  (EXP)
methylseleninic acid  (ISO)
ozone  (ISO)
paracetamol  (EXP,ISO)
paraquat  (EXP,ISO)
PD 0325901  (ISO)
phenobarbital  (ISO)
pravastatin  (ISO)
pregabalin  (ISO)
propofol  (EXP)
quercetin  (ISO)
raloxifene  (ISO)
rotenone  (EXP)
S-(1,2-dichlorovinyl)-L-cysteine  (ISO)
silicon dioxide  (ISO)
sodium arsenate  (ISO)
sodium arsenite  (ISO)
sunitinib  (ISO)
tamibarotene  (ISO)
temozolomide  (ISO)
tetrachloromethane  (EXP)
thapsigargin  (EXP)
titanium dioxide  (ISO)
tocopherol  (ISO)
trichostatin A  (EXP)
triptonide  (ISO)
troglitazone  (ISO)
trovafloxacin  (ISO)

Gene Ontology Annotations     Click to see Annotation Detail View

Molecular Pathway Annotations     Click to see Annotation Detail View
References

References - curated
# Reference Title Reference Citation
1. Imaging the assembly and disassembly kinetics of cis-SNARE complexes on native plasma membranes. Bar-On D, etal., FEBS Lett. 2008 Oct 15;582(23-24):3563-8. doi: 10.1016/j.febslet.2008.08.040. Epub 2008 Sep 24.
2. The septin CDCrel-1 binds syntaxin and inhibits exocytosis. Beites CL, etal., Nat Neurosci 1999 May;2(5):434-9.
3. Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Bennett MK, etal., Science. 1992 Jul 10;257(5067):255-9.
4. The specificity of SNARE pairing in biological membranes is mediated by both proof-reading and spatial segregation. Bethani I, etal., EMBO J. 2007 Sep 5;26(17):3981-92. Epub 2007 Aug 23.
5. Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin. Betz A, etal., J Biol Chem. 1997 Jan 24;272(4):2520-6.
6. Ca(2+)-synaptotagmin directly regulates t-SNARE function during reconstituted membrane fusion. Bhalla A, etal., Nat Struct Mol Biol. 2006 Apr;13(4):323-30. Epub 2006 Mar 26.
7. Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin. Blasi J, etal., EMBO J. 1993 Dec;12(12):4821-8.
8. Molecular profiling of synaptic vesicle docking sites reveals novel proteins but few differences between glutamatergic and GABAergic synapses. Boyken J, etal., Neuron. 2013 Apr 24;78(2):285-97. doi: 10.1016/j.neuron.2013.02.027.
9. Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide. Burkhardt P, etal., EMBO J. 2008 Apr 9;27(7):923-33. doi: 10.1038/emboj.2008.37. Epub 2008 Mar 13.
10. Structural characterization of full-length NSF and 20S particles. Chang LF, etal., Nat Struct Mol Biol. 2012 Feb 5;19(3):268-75. doi: 10.1038/nsmb.2237.
11. Cellubrevin and synaptobrevins: similar subcellular localization and biochemical properties in PC12 cells. Chilcote TJ, etal., J Cell Biol. 1995 Apr;129(1):219-31.
12. Alpha-synuclein sequesters arachidonic acid to modulate SNARE-mediated exocytosis. Darios F, etal., EMBO Rep. 2010 Jul;11(7):528-33. doi: 10.1038/embor.2010.66. Epub 2010 May 21.
13. Munc18-1 and the Syntaxin-1 N Terminus Regulate Open-Closed States in a t-SNARE Complex. Dawidowski D and Cafiso DS, Structure. 2016 Mar 1;24(3):392-400. doi: 10.1016/j.str.2016.01.005. Epub 2016 Feb 11.
14. Rabphilin regulates SNARE-dependent re-priming of synaptic vesicles for fusion. Deak F, etal., EMBO J. 2006 Jun 21;25(12):2856-66. Epub 2006 Jun 8.
15. Munc18-1 binding to the neuronal SNARE complex controls synaptic vesicle priming. Deak F, etal., J Cell Biol. 2009 Mar 9;184(5):751-64. Epub 2009 Mar 2.
16. Identification of syntaxin-1A sites of phosphorylation by casein kinase I and casein kinase II. Dubois T, etal., Eur J Biochem 2002 Feb;269(3):909-14.
17. Munc18-1 binds directly to the neuronal SNARE complex. Dulubova I, etal., Proc Natl Acad Sci U S A. 2007 Feb 20;104(8):2697-702. Epub 2007 Feb 14.
18. High resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complex. Ernst JA and Brunger AT, J Biol Chem. 2003 Mar 7;278(10):8630-6. Epub 2002 Dec 20.
19. Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly. Fasshauer D, etal., Biochemistry. 1998 Jul 21;37(29):10354-62.
20. Non-conducting function of the Kv2.1 channel enables it to recruit vesicles for release in neuroendocrine and nerve cells. Feinshreiber L, etal., J Cell Sci. 2010 Jun 1;123(Pt 11):1940-7. doi: 10.1242/jcs.063719.
21. Prion protein deposition and abnormal synaptic protein expression in the cerebellum in Creutzfeldt-Jakob disease. Ferrer I, etal., Neuroscience. 2000;97(4):715-26.
22. The V0 sector of the V-ATPase, synaptobrevin, and synaptophysin are associated on synaptic vesicles in a Triton X-100-resistant, freeze-thawing sensitive, complex. Galli T, etal., J Biol Chem. 1996 Jan 26;271(4):2193-8.
23. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Gaudet P, etal., Brief Bioinform. 2011 Sep;12(5):449-62. doi: 10.1093/bib/bbr042. Epub 2011 Aug 27.
24. Conformational switch of syntaxin-1 controls synaptic vesicle fusion. Gerber SH, etal., Science. 2008 Sep 12;321(5895):1507-10. doi: 10.1126/science.1163174. Epub 2008 Aug 14.
25. Rat ISS GO annotations from GOA human gene data--August 2006 GOA data from the GO Consortium
26. Regulation of the serotonin transporter by interacting proteins. Haase J, etal., Biochem Soc Trans. 2001 Nov;29(Pt 6):722-8.
27. A novel ubiquitous form of Munc-18 interacts with multiple syntaxins. Use of the yeast two-hybrid system to study interactions between proteins involved in membrane traffic. Hata Y and Sudhof TC, J Biol Chem 1995 Jun 2;270(22):13022-8.
28. Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin. Hata Y, etal., Nature 1993 Nov 25;366(6453):347-51.
29. Possible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formation. Hu SH, etal., Proc Natl Acad Sci U S A. 2011 Jan 18;108(3):1040-5. doi: 10.1073/pnas.0914906108. Epub 2010 Dec 30.
30. Synaptotagmin-mediated bending of the target membrane is a critical step in Ca(2+)-regulated fusion. Hui E, etal., Cell. 2009 Aug 21;138(4):709-21. doi: 10.1016/j.cell.2009.05.049.
31. SNARE Protein Syntaxin-1 Colocalizes Closely with NMDA Receptor Subunit NR2B in Postsynaptic Spines in the Hippocampus. Hussain S, etal., Front Mol Neurosci. 2016 Feb 5;9:10. doi: 10.3389/fnmol.2016.00010. eCollection 2016.
32. The effect of hypergravity on the inner ear: CREB and syntaxin are up-regulated. Iijima N, etal., Neuroreport. 2004 Apr 29;15(6):965-9.
33. Neuron-specific antigen HPC-1 from bovine brain reveals strong homology to epimorphin, an essential factor involved in epithelial morphogenesis: identification of a novel protein family. Inoue A and Akagawa K, Biochem Biophys Res Commun 1992 Sep 16;187(2):1144-50.
34. Cloning and sequence analysis of cDNA for a neuronal cell membrane antigen, HPC-1. Inoue A, etal., J Biol Chem 1992 May 25;267(15):10613-9.
35. Sept8 controls the binding of vesicle-associated membrane protein 2 to synaptophysin. Ito H, etal., J Neurochem. 2009 Feb;108(4):867-80. doi: 10.1111/j.1471-4159.2008.05849.x.
36. CAPS drives trans-SNARE complex formation and membrane fusion through syntaxin interactions. James DJ, etal., Proc Natl Acad Sci U S A. 2009 Oct 13;106(41):17308-13. doi: 10.1073/pnas.0900755106. Epub 2009 Sep 29.
37. Syntaxin-1A inhibits cardiac KATP channels by its actions on nucleotide binding folds 1 and 2 of sulfonylurea receptor 2A. Kang Y, etal., J Biol Chem. 2004 Nov 5;279(45):47125-31. Epub 2004 Aug 31.
38. Immunoelectron microscopic localization of the HPC-1 antigen in rat cerebellum. Koh S, etal., J Neurocytol. 1993 Nov;22(11):995-1005.
39. A conformational switch in complexin is required for synaptotagmin to trigger synaptic fusion. Krishnakumar SS, etal., Nat Struct Mol Biol. 2011 Jul 24;18(8):934-40. doi: 10.1038/nsmb.2103.
40. The Q-Soluble-N-Ethylmaleimide-Sensitive Factor Attachment Protein Receptor (Q-SNARE) SNAP-47 Regulates Trafficking of Selected Vesicle-Associated Membrane Proteins (VAMPs). Kuster A, etal., J Biol Chem. 2015 Sep 10. pii: jbc.M115.666362.
41. Complexin cross-links prefusion SNAREs into a zigzag array. Kümmel D, etal., Nat Struct Mol Biol. 2011 Jul 24;18(8):927-33. doi: 10.1038/nsmb.2101.
42. SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis. Lang T, etal., EMBO J 2001 May 1;20(9):2202-13.
43. SNAREs in native plasma membranes are active and readily form core complexes with endogenous and exogenous SNAREs. Lang T, etal., J Cell Biol 2002 Aug 19;158(4):751-60.
44. Ca(2+)-dependent and -independent activities of neural and non-neural synaptotagmins. Li C, etal., Nature 1995 Jun 15;375(6532):594-9.
45. Retinal pigment epithelial cells exhibit unique expression and localization of plasma membrane syntaxins which may contribute to their trafficking phenotype. Low SH, etal., J Cell Sci 2002 Dec 1;115(Pt 23):4545-53.
46. ATP dependence of the SNARE/caveolin 1 interaction in the hippocampus. Magga JM, etal., Biochem Biophys Res Commun 2002 Mar 15;291(5):1232-8.
47. A plethora of presynaptic proteins associated with ATP-storing organelles in cultured astrocytes. Maienschein V, etal., Glia. 1999 May;26(3):233-44.
48. The Habc domain and the SNARE core complex are connected by a highly flexible linker. Margittai M, etal., Biochemistry. 2003 Apr 15;42(14):4009-14.
49. Isolation and characterization of a dual prenylated Rab and VAMP2 receptor. Martincic I, etal., J Biol Chem 1997 Oct 24;272(43):26991-8.
50. Complexins: cytosolic proteins that regulate SNAP receptor function. McMahon HT, etal., Cell 1995 Oct 6;83(1):111-9.
51. Rat ISS GO annotations from MGI mouse gene data--August 2006 MGD data from the GO Consortium
52. Reduction of neurotransmitter release by the exogenous H3 domain peptide of HPC-1/syntaxin 1A in cultured rat hippocampal neurons. Mishima T, etal., Neurosci Lett. 2002 Sep 6;329(3):273-6.
53. Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex. Misura KM, etal., Nature. 2000 Mar 23;404(6776):355-62.
54. Electronic Transfer of LocusLink and RefSeq Data NCBI rat LocusLink and RefSeq merged data July 26, 2002
55. A direct interaction between Cdc42 and vesicle-associated membrane protein 2 regulates SNARE-dependent insulin exocytosis. Nevins AK and Thurmond DC, J Biol Chem. 2005 Jan 21;280(3):1944-52. Epub 2004 Nov 9.
56. Altered immunoreactivity of HPC-1/syntaxin 1A in proliferated nerve fibers in the human aganglionic colon of Hirschsprung's disease. Nirasawa Y, etal., J Mol Neurosci. 2001 Feb;16(1):13-9.
57. Regulation of exocytosis through Ca2+/ATP-dependent binding of autophosphorylated Ca2+/calmodulin-activated protein kinase II to syntaxin 1A. Ohyama A, etal., J Neurosci 2002 May 1;22(9):3342-51.
58. Mints, Munc18-interacting proteins in synaptic vesicle exocytosis. Okamoto M and Sudhof TC, J Biol Chem 1997 Dec 12;272(50):31459-64.
59. EHSH1/intersectin, a protein that contains EH and SH3 domains and binds to dynamin and SNAP-25. A protein connection between exocytosis and endocytosis? Okamoto M, etal., J Biol Chem 1999 Jun 25;274(26):18446-54.
60. Synaptotagmin-1 binds to PIP(2)-containing membrane but not to SNAREs at physiological ionic strength. Park Y, etal., Nat Struct Mol Biol. 2015 Oct;22(10):815-23. doi: 10.1038/nsmb.3097. Epub 2015 Sep 21.
61. Syntaxin-1A binds the nucleotide-binding folds of sulphonylurea receptor 1 to regulate the KATP channel. Pasyk EA, etal., J Biol Chem 2004 Feb 6;279(6):4234-40. Epub 2003 Nov 25.
62. Munc 18a binding to syntaxin 1A and 1B isoforms defines its localization at the plasma membrane and blocks SNARE assembly in a three-hybrid system assay. Perez-Branguli F, etal., Mol Cell Neurosci 2002 Jun;20(2):169-80.
63. Mammalian homologues of yeast vacuolar protein sorting (vps) genes implicated in Golgi-to-lysosome trafficking. Pevsner J, etal., Gene 1996 Dec 12;183(1-2):7-14.
64. Structural basis for the inhibitory role of tomosyn in exocytosis. Pobbati AV, etal., J Biol Chem. 2004 Nov 5;279(45):47192-200. Epub 2004 Aug 16.
65. Regulating the conducting states of a mammalian serotonin transporter. Quick MW Neuron. 2003 Oct 30;40(3):537-49.
66. Substrates regulate gamma-aminobutyric acid transporters in a syntaxin 1A-dependent manner. Quick MW Proc Natl Acad Sci U S A 2002 Apr 16;99(8):5686-91.
67. GOA pipeline RGD automated data pipeline
68. ClinVar Automated Import and Annotation Pipeline RGD automated import pipeline for ClinVar variants, variant-to-disease annotations and gene-to-disease annotations
69. Data Import for Chemical-Gene Interactions RGD automated import pipeline for gene-chemical interactions
70. Cellular and subcellular localization of syntaxin-like immunoreactivity in the rat striatum and cortex. Sesack SR and Snyder CL, Neuroscience. 1995 Aug;67(4):993-1007.
71. K+ channel facilitation of exocytosis by dynamic interaction with syntaxin. Singer-Lahat D, etal., J Neurosci. 2007 Feb 14;27(7):1651-8.
72. Direct interaction of endogenous Kv channels with syntaxin enhances exocytosis by neuroendocrine cells. Singer-Lahat D, etal., PLoS One. 2008 Jan 2;3(1):e1381. doi: 10.1371/journal.pone.0001381.
73. Helical extension of the neuronal SNARE complex into the membrane. Stein A, etal., Nature. 2009 Jul 23;460(7254):525-8. doi: 10.1038/nature08156. Epub 2009 Jul 1.
74. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Sutton RB, etal., Nature. 1998 Sep 24;395(6700):347-53.
75. Functional and biochemical analysis of the C2 domains of synaptotagmin IV. Thomas DM, etal., Mol Biol Cell. 1999 Jul;10(7):2285-95.
76. Direct interaction of SNARE complex binding protein synaphin/complexin with calcium sensor synaptotagmin 1. Tokumaru H, etal., Brain Cell Biol. 2008 Dec;36(5-6):173-89. doi: 10.1007/s11068-008-9032-9. Epub 2009 Jan 9.
77. Cis- and trans-membrane interactions of synaptotagmin-1. Vennekate W, etal., Proc Natl Acad Sci U S A. 2012 Jul 3;109(27):11037-42. doi: 10.1073/pnas.1116326109. Epub 2012 Jun 18.
78. The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling. Walch-Solimena C, etal., J Cell Biol. 1995 Feb;128(4):637-45.
79. Rat and Drosophila synaptotagmin 4 have opposite effects during SNARE-catalyzed membrane fusion. Wang Z and Chapman ER, J Biol Chem. 2010 Oct 1;285(40):30759-66. doi: 10.1074/jbc.M110.137745. Epub 2010 Aug 5.
80. Mechanisms of biphasic insulin-granule exocytosis - roles of the cytoskeleton, small GTPases and SNARE proteins. Wang Z and Thurmond DC, J Cell Sci. 2009 Apr 1;122(Pt 7):893-903.
81. Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A. Watanabe M, etal., Mol Biol Cell. 2005 Oct;16(10):4519-30. Epub 2005 Jul 19.
82. Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex. Weninger K, etal., Structure. 2008 Feb;16(2):308-20. doi: 10.1016/j.str.2007.12.010.
83. Ionic dependence of Ca2+ channel modulation by syntaxin 1A. Wiser O, etal., Proc Natl Acad Sci U S A 2002 Mar 19;99(6):3968-73. Epub 2002 Mar 12.
84. Transcriptome analysis of frontal cortex in alcohol-preferring and nonpreferring rats. Worst TJ, etal., J Neurosci Res 2005 May 15;80(4):529-38.
85. Syntaxin opening by the MUN domain underlies the function of Munc13 in synaptic-vesicle priming. Yang X, etal., Nat Struct Mol Biol. 2015 Jul;22(7):547-54. doi: 10.1038/nsmb.3038. Epub 2015 Jun 1.
86. The Kv2.1 channels mediate neuronal apoptosis induced by excitotoxicity. Yao H, etal., J Neurochem. 2009 Feb;108(4):909-19. doi: 10.1111/j.1471-4159.2008.05834.x. Epub 2008 Dec 10.
87. HPC-1 is associated with synaptotagmin and omega-conotoxin receptor. Yoshida A, etal., J Biol Chem 1992 Dec 15;267(35):24925-8.
88. Mechanistic insights into the recycling machine of the SNARE complex. Zhao M, etal., Nature. 2015 Feb 5;518(7537):61-7. doi: 10.1038/nature14148. Epub 2015 Jan 12.
Additional References at PubMed
PMID:7690687   PMID:7961655   PMID:8108429   PMID:9753330   PMID:10336434   PMID:10468580   PMID:10707983   PMID:10712642   PMID:10722844   PMID:10825299   PMID:10913252   PMID:11092755  
PMID:11118447   PMID:11533035   PMID:11707603   PMID:11832227   PMID:12115694   PMID:12130530   PMID:12145198   PMID:12145319   PMID:12175857   PMID:12221094   PMID:12730201   PMID:12761168  
PMID:12805290   PMID:12949219   PMID:14502428   PMID:14985338   PMID:15016962   PMID:15086514   PMID:15175344   PMID:15202772   PMID:15319413   PMID:15355307   PMID:15485808   PMID:15528447  
PMID:15721169   PMID:15872013   PMID:15935055   PMID:16540102   PMID:16672225   PMID:16720719   PMID:16861228   PMID:16888141   PMID:16959903   PMID:17002520   PMID:17027648   PMID:17447252  
PMID:17502420   PMID:17543282   PMID:17617378   PMID:17717182   PMID:17725325   PMID:18003982   PMID:18077557   PMID:18385322   PMID:18556353   PMID:18570918   PMID:18644890   PMID:18760330  
PMID:19039652   PMID:19364135   PMID:19546860   PMID:19716806   PMID:19748891   PMID:19793988   PMID:19843696   PMID:21040848   PMID:21076040   PMID:21173146   PMID:21209369   PMID:21266332  
PMID:21401123   PMID:21540180   PMID:21543213   PMID:21646859   PMID:21730064   PMID:21763275   PMID:21900493   PMID:21900502   PMID:22008253   PMID:22020284   PMID:22094010   PMID:22131420  
PMID:22411134   PMID:22871113   PMID:23315993   PMID:23341457   PMID:23403573   PMID:23641074   PMID:23643538   PMID:23665582   PMID:23761923   PMID:23801330   PMID:23821748   PMID:23962429  
PMID:24133272   PMID:24429282   PMID:24604356   PMID:24722188   PMID:24835618   PMID:24885604   PMID:25485479   PMID:25517944   PMID:26391271   PMID:26635000   PMID:26884341   PMID:27072493  
PMID:27466336   PMID:28137749   PMID:28483813   PMID:28515322   PMID:28596237   PMID:29133430   PMID:29476059   PMID:30156474   PMID:31308225   PMID:32086964   PMID:32669573   PMID:33498722  
PMID:33843051   PMID:34779769   PMID:34857632   PMID:34948351   PMID:36157213   PMID:37057886  


Genomics

Comparative Map Data
Stx1a
(Rattus norvegicus - Norway rat)
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCr81227,278,517 - 27,306,547 (-)NCBIGRCr8
mRatBN7.21221,641,971 - 21,670,022 (-)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl1221,641,969 - 21,669,930 (-)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx1222,782,666 - 22,810,512 (-)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.01223,394,983 - 23,422,828 (-)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.01222,463,210 - 22,491,166 (-)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.01224,682,050 - 24,710,002 (-)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl1224,682,041 - 24,710,019 (-)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.01226,682,320 - 26,710,272 (-)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.41222,737,112 - 22,765,064 (-)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
Celera1223,405,260 - 23,432,900 (-)NCBICelera
Cytogenetic Map12q12NCBI
STX1A
(Homo sapiens - human)
Human AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCh38773,699,210 - 73,719,669 (-)NCBIGRCh38GRCh38hg38GRCh38
GRCh38.p14 Ensembl773,699,206 - 73,719,672 (-)EnsemblGRCh38hg38GRCh38
GRCh37773,113,540 - 73,133,999 (-)NCBIGRCh37GRCh37hg19GRCh37
Build 36772,751,476 - 72,771,924 (-)NCBINCBI36Build 36hg18NCBI36
Build 34772,558,190 - 72,578,613NCBI
Celera768,591,739 - 68,612,223 (-)NCBICelera
Cytogenetic Map7q11.23NCBI
HuRef768,995,950 - 69,016,432 (-)NCBIHuRef
CHM1_1773,259,272 - 73,279,754 (-)NCBICHM1_1
T2T-CHM13v2.0774,900,126 - 74,920,586 (-)NCBIT2T-CHM13v2.0
CRA_TCAGchr7v2772,446,607 - 72,467,089 (-)NCBI
Stx1a
(Mus musculus - house mouse)
Mouse AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCm395135,051,473 - 135,079,954 (+)NCBIGRCm39GRCm39mm39
GRCm39 Ensembl5135,052,336 - 135,079,954 (+)EnsemblGRCm39 Ensembl
GRCm385135,023,482 - 135,051,100 (+)NCBIGRCm38GRCm38mm10GRCm38
GRCm38.p6 Ensembl5135,023,482 - 135,051,100 (+)EnsemblGRCm38mm10GRCm38
MGSCv375135,499,442 - 135,526,969 (+)NCBIGRCm37MGSCv37mm9NCBIm37
MGSCv365135,308,199 - 135,335,726 (+)NCBIMGSCv36mm8
Celera5132,033,901 - 132,061,428 (+)NCBICelera
Cytogenetic Map5G2NCBI
cM Map574.95NCBI
Stx1a
(Chinchilla lanigera - long-tailed chinchilla)
Chinchilla AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChiLan1.0 EnsemblNW_00495545614,030,226 - 14,046,456 (+)EnsemblChiLan1.0
ChiLan1.0NW_00495545614,030,233 - 14,046,456 (+)NCBIChiLan1.0ChiLan1.0
STX1A
(Pan paniscus - bonobo/pygmy chimpanzee)
Bonobo AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
NHGRI_mPanPan1-v2691,180,408 - 91,200,924 (+)NCBINHGRI_mPanPan1-v2
NHGRI_mPanPan17139,445,039 - 139,465,555 (+)NCBINHGRI_mPanPan1
PanPan1.1780,852,495 - 80,871,635 (-)NCBIpanpan1.1PanPan1.1panPan2
PanPan1.1 Ensembl780,852,495 - 80,862,255 (-)Ensemblpanpan1.1panPan2
STX1A
(Canis lupus familiaris - dog)
Dog AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
CanFam3.166,574,616 - 6,583,002 (+)NCBICanFam3.1CanFam3.1canFam3CanFam3.1
CanFam3.1 Ensembl66,574,631 - 6,581,833 (+)EnsemblCanFam3.1canFam3CanFam3.1
Dog10K_Boxer_Tasha68,263,577 - 8,280,400 (+)NCBIDog10K_Boxer_Tasha
ROS_Cfam_1.066,381,214 - 6,398,029 (+)NCBIROS_Cfam_1.0
ROS_Cfam_1.0 Ensembl66,381,225 - 6,398,461 (+)EnsemblROS_Cfam_1.0 Ensembl
UMICH_Zoey_3.166,370,709 - 6,387,529 (+)NCBIUMICH_Zoey_3.1
UNSW_CanFamBas_1.066,318,461 - 6,335,266 (+)NCBIUNSW_CanFamBas_1.0
UU_Cfam_GSD_1.066,482,166 - 6,498,979 (+)NCBIUU_Cfam_GSD_1.0
Stx1a
(Ictidomys tridecemlineatus - thirteen-lined ground squirrel)
Squirrel AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HiC_Itri_2NW_024409344131,118,736 - 131,127,007 (+)NCBIHiC_Itri_2
SpeTri2.0 EnsemblNW_0049365432,909,552 - 2,918,770 (-)EnsemblSpeTri2.0SpeTri2.0 Ensembl
SpeTri2.0NW_0049365432,909,560 - 2,918,175 (-)NCBISpeTri2.0SpeTri2.0SpeTri2.0
STX1A
(Chlorocebus sabaeus - green monkey)
Green Monkey AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChlSab1.1289,347,495 - 9,367,948 (+)NCBIChlSab1.1ChlSab1.1chlSab2
ChlSab1.1 Ensembl289,347,532 - 9,368,585 (+)EnsemblChlSab1.1ChlSab1.1 EnsemblchlSab2
Vero_WHO_p1.0NW_0236660707,135,019 - 7,155,486 (-)NCBIVero_WHO_p1.0Vero_WHO_p1.0
Stx1a
(Heterocephalus glaber - naked mole-rat)
Naked Mole-Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HetGla_female_1.0 EnsemblNW_00462474014,104,050 - 14,120,133 (+)EnsemblHetGla_female_1.0HetGla_female_1.0 EnsemblhetGla2
HetGla 1.0NW_00462474014,104,033 - 14,120,133 (+)NCBIHetGla_female_1.0HetGla 1.0hetGla2

Variants

.
Variants in Stx1a
200 total Variants
miRNA Target Status

Confirmed Target Of
miRNA GeneMature miRNAMethod NameResult TypeData TypeSupport TypePMID
Mir24-1rno-miR-24-3pMirtarbaseexternal_infoMicroarrayFunctional MTI (Weak)18258830
Mir298rno-miR-298-5pMirtarbaseexternal_infoMicroarrayFunctional MTI (Weak)18258830
Mir497rno-miR-497-5pMirtarbaseexternal_infoMicroarrayFunctional MTI (Weak)18258830
Mir29arno-miR-29a-3pMirtarbaseexternal_infoMicroarrayFunctional MTI (Weak)18258830

Predicted Target Of
Summary Value
Count of predictions:222
Count of miRNA genes:140
Interacting mature miRNAs:173
Transcripts:ENSRNOT00000049601
Prediction methods:Miranda, Rnahybrid, Targetscan
Result types:miRGate_prediction

The detailed report is available here: Full Report CSV TAB Printer

miRNA Target Status data imported from miRGate (http://mirgate.bioinfo.cnio.es/).
For more information about miRGate, see PMID:25858286 or access the full paper here.


QTLs in Region (mRatBN7.2)
The following QTLs overlap with this region.    Full Report CSV TAB Printer Gviewer
RGD IDSymbolNameLODP ValueTraitSub TraitChrStartStopSpecies
10755457Coatc14Coat color QTL 140.01759coat/hair pigmentation trait (VT:0010463)pigmented ventral coat/hair area to total ventral coat/hair area ratio (CMO:0001812)12122591684Rat
6893681Bw109Body weight QTL 1092.30.004body mass (VT:0001259)body weight (CMO:0000012)12123297788Rat
1581516Cm56Cardiac mass QTL 564.20.05heart left ventricle mass (VT:0007031)heart left ventricle weight to body weight ratio (CMO:0000530)12129333307Rat
1598855Bp294Blood pressure QTL 2943.5arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)12134851688Rat
7411660Foco28Food consumption QTL 2810.90.001eating behavior trait (VT:0001431)feed conversion ratio (CMO:0001312)12142110980Rat
9590086Insglur6Insulin/glucose ratio QTL 618.970.001blood insulin amount (VT:0001560)calculated plasma insulin level (CMO:0002170)12142110980Rat
8694179Bw150Body weight QTL 1502.90.001body mass (VT:0001259)body weight gain (CMO:0000420)12142110980Rat
7411586Foco5Food consumption QTL 55.40.001eating behavior trait (VT:0001431)feed conversion ratio (CMO:0001312)12142110980Rat
7411595Foco9Food consumption QTL 940.001eating behavior trait (VT:0001431)feed conversion ratio (CMO:0001312)12142110980Rat
7411545Bw128Body weight QTL 1285.20.001body mass (VT:0001259)body weight gain (CMO:0000420)12142110980Rat
9590147Scort7Serum corticosterone level QTL 713.610.001blood corticosterone amount (VT:0005345)plasma corticosterone level (CMO:0001173)12142110980Rat
2303575Insul14Insulin level QTL 144blood insulin amount (VT:0001560)blood insulin level (CMO:0000349)12142450532Rat
737979Pia22Pristane induced arthritis QTL 2253.1joint integrity trait (VT:0010548)joint inflammation composite score (CMO:0000919)12144465750Rat
634351Apr5Acute phase response QTL 56.7blood interleukin-6 amount (VT:0008595)plasma interleukin-6 level (CMO:0001927)12144503507Rat
2302042Pia38Pristane induced arthritis QTL 383.50.001blood immunoglobulin amount (VT:0002460)serum immunoglobulin G1 level (CMO:0002115)12144503507Rat
634350Apr4Acute phase response QTL 46orosomucoid 1 amount (VT:0010541)plasma orosomucoid 1 level (CMO:0001467)12117200546172005Rat
8552918Pigfal7Plasma insulin-like growth factor 1 level QTL 7blood insulin-like growth factor amount (VT:0010479)plasma insulin-like growth factor 1 level (CMO:0001299)12556449546669029Rat
7411547Bw129Body weight QTL 1290.001body mass (VT:0001259)body weight gain (CMO:0000420)6556449546669029Rat
7411597Foco10Food consumption QTL 100.001eating behavior trait (VT:0001431)feed conversion ratio (CMO:0001312)12556449546669029Rat
7411641Foco19Food consumption QTL 1927.70.001eating behavior trait (VT:0001431)feed conversion ratio (CMO:0001312)12556449546669029Rat
8552964Pigfal17Plasma insulin-like growth factor 1 level QTL 173.5blood insulin-like growth factor amount (VT:0010479)plasma insulin-like growth factor 1 level (CMO:0001299)12556449546669029Rat
7411588Foco6Food consumption QTL 60.001eating behavior trait (VT:0001431)feed conversion ratio (CMO:0001312)12556449546669029Rat
8552912Pigfal6Plasma insulin-like growth factor 1 level QTL 65blood insulin-like growth factor amount (VT:0010479)plasma insulin-like growth factor 1 level (CMO:0001299)12556449846669029Rat
10059594Kidm46Kidney mass QTL 463.790.025kidney mass (VT:0002707)both kidneys wet weight to body weight ratio (CMO:0000340)12610757946669029Rat
1302792Scl21Serum cholesterol level QTL 213.80.0011blood cholesterol amount (VT:0000180)plasma total cholesterol level (CMO:0000585)12719673046669029Rat
2293086Iddm30Insulin dependent diabetes mellitus QTL 303.82blood glucose amount (VT:0000188)blood glucose level (CMO:0000046)12844949028302290Rat
61331Eau2Experimental allergic uveoretinitis QTL 20.0005uvea integrity trait (VT:0010551)experimental autoimmune uveitis score (CMO:0001504)12852542328064601Rat
1300157Rf21Renal function QTL 214.4renal blood flow trait (VT:2000006)absolute change in renal blood flow rate (CMO:0001168)12931821632103380Rat
1549829Scl48Serum cholesterol level QTL 485blood cholesterol amount (VT:0000180)serum total cholesterol level (CMO:0000363)12960327746669029Rat
2293699Bss49Bone structure and strength QTL 495.610.0001lumbar vertebra size trait (VT:0010518)lumbar vertebra trabecular cross-sectional area (CMO:0001692)121047413746669029Rat
2300186Bmd59Bone mineral density QTL 597.10.0001lumbar vertebra mineral mass (VT:0010511)volumetric bone mineral density (CMO:0001553)121047413746669029Rat
1331786Kidm11Kidney mass QTL 113.571kidney mass (VT:0002707)right kidney wet weight (CMO:0000082)121107382524234895Rat
1331755Bp219Blood pressure QTL 2193.041arterial blood pressure trait (VT:2000000)mean arterial blood pressure (CMO:0000009)121107382528064557Rat
1331761Bp218Blood pressure QTL 2182.973arterial blood pressure trait (VT:2000000)mean arterial blood pressure (CMO:0000009)121107382545055165Rat
61404Bw120Body weight QTL 1205.1body mass (VT:0001259)body mass index (BMI) (CMO:0000105)121235161946669029Rat
1641928Alcrsp5Alcohol response QTL 5response to alcohol trait (VT:0010489)duration of loss of righting reflex (CMO:0002289)121281238546669029Rat
2303569Gluco44Glucose level QTL 442blood glucose amount (VT:0000188)blood glucose level (CMO:0000046)121281238546669029Rat
1549902Bp269Blood pressure QTL 269arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)121318273646669029Rat
1549912Bp268Blood pressure QTL 268arterial blood pressure trait (VT:2000000)diastolic blood pressure (CMO:0000005)101318273646669029Rat
2302060Pia37Pristane induced arthritis QTL 376.10.001blood immunoglobulin amount (VT:0002460)serum immunoglobulin G1 level (CMO:0002115)121319815746669029Rat
61416Pia4Pristane induced arthritis QTL 48.4joint integrity trait (VT:0010548)arthritic paw count (CMO:0001460)121363552330827399Rat
61421Cia12Collagen induced arthritis QTL 124.6joint integrity trait (VT:0010548)joint inflammation composite score (CMO:0000919)121363552335682913Rat
631543Bp83Blood pressure QTL 835.8arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)121555082638478808Rat
2293684Bmd26Bone mineral density QTL 264.40.0002femur mineral mass (VT:0010011)total volumetric bone mineral density (CMO:0001728)121587265332974238Rat
631560Apr1Acute phase response QTL 16.1orosomucoid 1 amount (VT:0010541)plasma orosomucoid 1 level (CMO:0001467)121914436246669029Rat
2306789Ean6Experimental allergic neuritis QTL 64.9nervous system integrity trait (VT:0010566)experimental autoimmune neuritis severity score (CMO:0001528)121961087024139202Rat
737822Alc10Alcohol consumption QTL 102.2consumption behavior trait (VT:0002069)ethanol drink intake rate (CMO:0001407)121961087040218516Rat
5684888Pia42Pristane induced arthritis QTL 42joint integrity trait (VT:0010548)joint inflammation composite score (CMO:0000919)121961087042828880Rat
61324Eae5Experimental allergic encephalomyelitis QTL 514nervous system integrity trait (VT:0010566)percentage of study population developing relapsing-remitting experimental autoimmune encephalomyelitis during a period of time (CMO:0001402)121961087046669029Rat
1298081Cia25Collagen induced arthritis QTL 254.7joint integrity trait (VT:0010548)joint inflammation composite score (CMO:0000919)121961088935682913Rat
70213Niddm27Non-insulin dependent diabetes mellitus QTL 273.72blood glucose amount (VT:0000188)blood glucose level (CMO:0000046)121983578938193007Rat
631521Pia12Pristane induced arthritis QTL 128.9joint integrity trait (VT:0010548)joint inflammation composite score (CMO:0000919)122025941723672083Rat
7411643Foco20Food consumption QTL 200.001eating behavior trait (VT:0001431)feed conversion ratio (CMO:0001312)122032881946669029Rat

Markers in Region
BF397463  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.21221,656,433 - 21,656,907 (+)MAPPERmRatBN7.2
Rnor_6.01224,696,511 - 24,696,984NCBIRnor6.0
Rnor_5.01226,696,781 - 26,697,254UniSTSRnor5.0
RGSC_v3.41222,751,573 - 22,752,046UniSTSRGSC3.4
Celera1223,419,618 - 23,420,091UniSTS
RH 3.4 Map12327.3UniSTS
Cytogenetic Map12q12UniSTS
AU048378  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.21221,650,148 - 21,650,283 (+)MAPPERmRatBN7.2
Rnor_6.01224,690,228 - 24,690,360NCBIRnor6.0
Rnor_5.01226,690,498 - 26,690,630UniSTSRnor5.0
RGSC_v3.41222,745,290 - 22,745,422UniSTSRGSC3.4
Celera1223,413,335 - 23,413,467UniSTS
Cytogenetic Map12q12UniSTS


Related Rat Strains
The following Strains have been annotated to Stx1a
BB/OK    


Expression


RNA-SEQ Expression
High: > 1000 TPM value   Medium: Between 11 and 1000 TPM
Low: Between 0.5 and 10 TPM   Below Cutoff: < 0.5 TPM

alimentary part of gastrointestinal system circulatory system endocrine system exocrine system hemolymphoid system hepatobiliary system integumental system musculoskeletal system nervous system renal system reproductive system respiratory system appendage
High
Medium 68 2 10
Low 3 40 40 24 19 24 3 6 6 33 31 11 3
Below cutoff 3 17 17 17 5 5 5

Sequence


Reference Sequences
RefSeq Acc Id: ENSRNOT00000049601   ⟹   ENSRNOP00000040699
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl1221,641,969 - 21,669,930 (-)Ensembl
Rnor_6.0 Ensembl1224,682,041 - 24,710,019 (-)Ensembl
RefSeq Acc Id: ENSRNOT00000097493   ⟹   ENSRNOP00000096833
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl1221,641,975 - 21,657,386 (-)Ensembl
RefSeq Acc Id: NM_053788   ⟹   NP_446240
RefSeq Status: PROVISIONAL
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr81227,278,517 - 27,306,471 (-)NCBI
mRatBN7.21221,641,975 - 21,669,930 (-)NCBI
Rnor_6.01224,682,050 - 24,710,002 (-)NCBI
Rnor_5.01226,682,320 - 26,710,272 (-)NCBI
RGSC_v3.41222,737,112 - 22,765,064 (-)RGD
Celera1223,405,260 - 23,432,900 (-)RGD
Sequence:
RefSeq Acc Id: XR_005491588
Type: NON-CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr81227,279,790 - 27,306,547 (-)NCBI
mRatBN7.21221,641,971 - 21,670,022 (-)NCBI
RefSeq Acc Id: XR_005491589
Type: NON-CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr81227,279,790 - 27,306,545 (-)NCBI
mRatBN7.21221,643,247 - 21,670,022 (-)NCBI
Reference Protein Sequences
RefSeq Acc Id: NP_446240   ⟸   NM_053788
- UniProtKB: P32851 (UniProtKB/Swiss-Prot),   A0A1E1ERK2 (UniProtKB/TrEMBL),   Q9QXG3 (UniProtKB/TrEMBL)
- Sequence:
RefSeq Acc Id: ENSRNOP00000040699   ⟸   ENSRNOT00000049601
RefSeq Acc Id: ENSRNOP00000096833   ⟸   ENSRNOT00000097493
Protein Domains
t-SNARE coiled-coil homology

Protein Structures
Name Modeler Protein Id AA Range Protein Structure
AF-P32851-F1-model_v2 AlphaFold P32851 1-288 view protein structure

Transcriptome

eQTL   View at Phenogen
WGCNA   View at Phenogen
Tissue/Strain Expression   View at Phenogen

Promoters
RGD ID:13698562
Promoter ID:EPDNEW_R9087
Type:initiation region
Name:Stx1a_1
Description:syntaxin 1A
SO ACC ID:SO:0000170
Source:EPDNEW (Eukaryotic Promoter Database, http://epd.vital-it.ch/)
Experiment Methods:Single-end sequencing.
Position:
Rat AssemblyChrPosition (strand)Source
Rnor_6.01224,709,983 - 24,710,043EPDNEW

Additional Information

Database Acc Id Source(s)
AGR Gene RGD:69430 AgrOrtholog
BIND 130559
  130562
  130563
  130904
  133975
  134453
  134456
  134473
  134475
BioCyc Gene G2FUF-19602 BioCyc
Ensembl Genes ENSRNOG00000029165 Ensembl, ENTREZGENE, UniProtKB/TrEMBL
  ENSRNOG00055000331 UniProtKB/Swiss-Prot
  ENSRNOG00060011988 UniProtKB/Swiss-Prot
  ENSRNOG00065001365 UniProtKB/Swiss-Prot
Ensembl Transcript ENSRNOT00000049601.3 UniProtKB/TrEMBL
  ENSRNOT00000097493 ENTREZGENE
  ENSRNOT00000097493.1 UniProtKB/TrEMBL
  ENSRNOT00055000584 UniProtKB/Swiss-Prot
  ENSRNOT00060020334 UniProtKB/Swiss-Prot
  ENSRNOT00065001813 UniProtKB/Swiss-Prot
Gene3D-CATH 1.20.5.110 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  1.20.58.70 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
InterPro SNARE UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Syntaxin UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Syntaxin/epimorphin_CS UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Syntaxin_N UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  T_SNARE_dom UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
KEGG Report rno:116470 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
NCBI Gene 116470 ENTREZGENE
PANTHER PTHR19957 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  PTHR19957:SF84 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Pfam SNARE UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Syntaxin UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
PhenoGen Stx1a PhenoGen
PROSITE SYNTAXIN UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  T_SNARE UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
RatGTEx ENSRNOG00000029165 RatGTEx
  ENSRNOG00055000331 RatGTEx
  ENSRNOG00060011988 RatGTEx
  ENSRNOG00065001365 RatGTEx
SMART SynN UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  t_SNARE UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Superfamily-SCOP SSF47661 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
UniProt A0A1E1ERK2 ENTREZGENE, UniProtKB/TrEMBL
  A0A8I6AVN2_RAT UniProtKB/TrEMBL
  A0A8L2ULG5_RAT UniProtKB/TrEMBL
  P32851 ENTREZGENE
  Q9QXG3 ENTREZGENE, UniProtKB/TrEMBL
  STX1A_RAT UniProtKB/Swiss-Prot


Nomenclature History
Date Current Symbol Current Name Previous Symbol Previous Name Description Reference Status
2015-12-02 Stx1a  syntaxin 1A  Stx1a  syntaxin 1A (brain)  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2004-09-10 Stx1a  syntaxin 1A (brain)    syntaxin 1a  Name updated 1299863 APPROVED
2002-06-10 Stx1a  syntaxin 1a      Symbol and Name status set to approved 70586 APPROVED

RGD Curation Notes
Note Type Note Reference
gene_cellular_localization concentrated in 200 nm large, cholesterol-dependent clusters at which secretory vesicles preferentially dock and fuse 68723
gene_function participates with syntaxin 1 in locating cholesterol-dependent clusters in the plasmalemma, at which secretory vesicles preferentially dock and fuse 68723
gene_physical_interaction interacts with an omega-conotoxin-sensitive N-type calcium channel and with synaptotagmin 730159
gene_process main component of the exocytotic molecular machinery 625671
gene_process involved in membrane fusion and exocytosis 68723
gene_regulation phosphorylated by casien kinase I on Thr21 and casein kinase II on Ser14 of the N-ternimal domian 70601
gene_regulation during exocytosis calmodulin-activated protein kinase II (CaMKII)-alpha binds to syntaxin and can be released by EGTA or by phosphatase 625671
gene_transcript mRNA upregulated in frontal cortex of AA rat strain compared to ANA rat strain 1358772