SYT2

In this article, we will explore the fascinating world of SYT2 and all the implications this topic has in today's environment. From its history to its impact on society, through its different perspectives and applications, we will analyze in depth all the relevant aspects of SYT2. In addition, we will delve into the latest research and discoveries on this topic, as well as the opinions of experts on the subject. Without a doubt, SYT2 is an exciting and constantly evolving topic, so this article aims to be a guide to better understand its importance and meaning today.

Protein-coding gene in the species Homo sapiens

SYT2
Identifiers
Aliases	SYT2, SytII, CMS7, MYSPC, synaptotagmin 2, CMS7A, CMS7B
External IDs	OMIM: 600104; MGI: 99666; HomoloGene: 22516; GeneCards: SYT2; OMA:SYT2 - orthologs
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q32.1 Start 202,590,596 bp[1] End 202,710,454 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1 E4|1 58.24 cM Start 134,574,415 bp[2] End 134,690,331 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Pons external globus pallidus paraflocculus of cerebellum cerebellar vermis lateral nuclear group of thalamus right hemisphere of cerebellum superior vestibular nucleus pars compacta dorsal motor nucleus of vagus nerve pars reticulata Top expressed in cerebellar cortex inferior colliculi Medulla Oblongata deep cerebellar nuclei pontine nuclei medial vestibular nucleus facial motor nucleus anterior horn of spinal cord cerebellar vermis lobe of cerebellum More reference expression data BioGPS More reference expression data
Gene ontology Molecular function metal ion binding calcium ion binding inositol 1,3,4,5 tetrakisphosphate binding clathrin binding syntaxin binding protein binding calcium-dependent phospholipid binding SNARE binding phosphatidylserine binding Cellular component cell junction chromaffin granule membrane synaptic vesicle membrane cytoplasmic vesicle synapse integral component of membrane synaptic vesicle membrane plasma membrane clathrin-coated vesicle membrane axon dense core granule exocytic vesicle Biological process synaptic vesicle endocytosis cell differentiation neurotransmitter secretion positive regulation of dendrite extension vesicle fusion regulation of calcium ion-dependent exocytosis calcium ion-regulated exocytosis of neurotransmitter membrane organization regulation of dopamine secretion synaptic vesicle exocytosis vesicle-mediated transport calcium-ion regulated exocytosis cellular response to calcium ion Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 127833 20980 Ensembl ENSG00000143858 ENSMUSG00000026452 UniProt Q8N9I0 P46097 RefSeq (mRNA) NM_001136504 NM_177402 NM_009307 NM_001355726 RefSeq (protein) NP_001129976 NP_796376 NP_033333 NP_001342655 Location (UCSC) Chr 1: 202.59 – 202.71 Mb Chr 1: 134.57 – 134.69 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Synaptotagmin-2 is a protein that in humans is encoded by the SYT2 gene.^[5][6]

References

1. ^ ^{a b c} GRCh38: Ensembl release 89: ENSG00000143858 – Ensembl, May 2017
2. ^ ^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000026452 – Ensembl, May 2017
3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ Jones JM, Popma SJ, Mizuta M, Seino S, Meisler MH (March 1995). "Synaptotagmin genes on mouse chromosomes 1, 7, and 10 and human chromosome 19". Mammalian Genome. 6 (3): 212–3. doi:10.1007/BF00293017. hdl:2027.42/47020. PMID 7749232. S2CID 24653745.
6. ^ "Entrez Gene: SYT2 synaptotagmin II".

Further reading

• Fukuda M, Aruga J, Niinobe M, Aimoto S, Mikoshiba K (November 1994). "Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II". The Journal of Biological Chemistry. 269 (46): 29206–11. doi:10.1016/S0021-9258(19)62031-4. PMID 7961887.
• Perin MS (October 1996). "Mirror image motifs mediate the interaction of the COOH terminus of multiple synaptotagmins with the neurexins and calmodulin". Biochemistry. 35 (43): 13808–16. doi:10.1021/bi960853x. PMID 8901523.
• Baram D, Adachi R, Medalia O, Tuvim M, Dickey BF, Mekori YA, Sagi-Eisenberg R (May 1999). "Synaptotagmin II negatively regulates Ca2+-triggered exocytosis of lysosomes in mast cells". The Journal of Experimental Medicine. 189 (10): 1649–58. doi:10.1084/jem.189.10.1649. PMC 2193646. PMID 10330444.
• Mizutani A, Fukuda M, Ibata K, Shiraishi Y, Mikoshiba K (March 2000). "SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear ribonucleoprotein R, interacts with ubiquitous synaptotagmin isoforms". The Journal of Biological Chemistry. 275 (13): 9823–31. doi:10.1074/jbc.275.13.9823. PMID 10734137.
• Kida Y, Sakaguchi M, Fukuda M, Mikoshiba K, Mihara K (August 2000). "Membrane topogenesis of a type I signal-anchor protein, mouse synaptotagmin II, on the endoplasmic reticulum". The Journal of Cell Biology. 150 (4): 719–30. doi:10.1083/jcb.150.4.719. PMC 2175286. PMID 10952998.
• Martina JA, Bonangelino CJ, Aguilar RC, Bonifacino JS (May 2001). "Stonin 2: an adaptor-like protein that interacts with components of the endocytic machinery". The Journal of Cell Biology. 153 (5): 1111–20. doi:10.1083/jcb.153.5.1111. PMC 2174325. PMID 11381094.
• Kida Y, Sakaguchi M, Fukuda M, Mikoshiba K, Mihara K (November 2001). "Amino acid residues before the hydrophobic region which are critical for membrane translocation of the N-terminal domain of synaptotagmin II". FEBS Letters. 507 (3): 341–5. doi:10.1016/S0014-5793(01)03000-9. PMID 11696368. S2CID 29026112.
• Lindmark IM, Karlsson A, Serrander L, Francois P, Lew D, Rasmusson B, Stendahl O, Nüsse O (June 2002). "Synaptotagmin II could confer Ca(2+) sensitivity to phagocytosis in human neutrophils". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1590 (1–3): 159–66. doi:10.1016/S0167-4889(02)00209-4. PMID 12063179.
• Rickman C, Archer DA, Meunier FA, Craxton M, Fukuda M, Burgoyne RD, Davletov B (March 2004). "Synaptotagmin interaction with the syntaxin/SNAP-25 dimer is mediated by an evolutionarily conserved motif and is sensitive to inositol hexakisphosphate". The Journal of Biological Chemistry. 279 (13): 12574–9. doi:10.1074/jbc.M310710200. PMID 14709554.
• Lee BH, Min X, Heise CJ, Xu BE, Chen S, Shu H, Luby-Phelps K, Goldsmith EJ, Cobb MH (September 2004). "WNK1 phosphorylates synaptotagmin 2 and modulates its membrane binding". Molecular Cell. 15 (5): 741–51. doi:10.1016/j.molcel.2004.07.018. PMID 15350218.

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