SLIT2

SLIT2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2V70, 2V9S, 2V9T, 2WFH
Identifiers
Aliases	SLIT2, SLIL3, Slit-2, slit guidance ligand 2
External IDs	MGI: 1315205 HomoloGene: 3516 GeneCards: SLIT2
Gene location (Human)
Chr.	Chromosome 4 (human)[1]
End	20,620,561 bp[1]
Gene location (Mouse)
Chr.	Chromosome 5 (mouse)[2]
End	48,307,733 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• calcium ion binding; • heparin binding; • protein homodimerization activity; • GTPase inhibitor activity; • laminin-1 binding; • protein binding; • identical protein binding; • Roundabout binding; • proteoglycan binding;
Cellular component	• cytoplasm; • membrane; • extracellular region; • cell surface; • extracellular exosome; • plasma membrane; • extracellular space;
Biological process	• negative regulation of protein phosphorylation; • negative regulation of chemokine-mediated signaling pathway; • negative regulation of neutrophil chemotaxis; • negative regulation of cellular response to growth factor stimulus; • chemorepulsion involved in embryonic olfactory bulb interneuron precursor migration; • cell differentiation; • ureteric bud development; • negative chemotaxis; • negative regulation of actin filament polymerization; • negative regulation of small GTPase mediated signal transduction; • negative regulation of retinal ganglion cell axon guidance; • negative regulation of mononuclear cell migration; • corticospinal neuron axon guidance through spinal cord; • negative regulation of smooth muscle cell migration; • Roundabout signaling pathway; • positive regulation of axonogenesis; • nervous system development; • cell migration involved in sprouting angiogenesis; • negative regulation of endothelial cell migration; • axon guidance; • multicellular organism development; • chemotaxis; • negative regulation of smooth muscle cell chemotaxis; • cellular response to hormone stimulus; • negative regulation of cell migration; • negative regulation of monocyte chemotaxis; • negative regulation of cell growth; • response to cortisol; • apoptotic process involved in luteolysis; • positive regulation of apoptotic process; • induction of negative chemotaxis; • cellular response to heparin; • motor neuron axon guidance; • branching morphogenesis of an epithelial tube; • negative regulation of leukocyte chemotaxis; • chemorepulsion involved in postnatal olfactory bulb interneuron migration; • axon extension involved in axon guidance; • negative regulation of lamellipodium assembly; • negative regulation of vascular permeability; • retinal ganglion cell axon guidance; • negative regulation of GTPase activity;
	Sources:Amigo / QuickGO
Orthologs
	9353
	20563
	ENSG00000145147
	ENSMUSG00000031558
	O94813
	Q9R1B9
	NM_001289135; NM_001289136; NM_004787
	NM_001291227; NM_001291228; NM_178804
	NP_001276064; NP_001276065; NP_004778
	NP_001278156; NP_001278157; NP_848919
	Wikidata
View/Edit Human	View/Edit Mouse

Slit homolog 2 protein is a protein that in humans is encoded by the SLIT2 gene.^[5]^[6]^[7]

Interactions

SLIT2 has been shown to interact with Glypican 1.^[8]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000145147 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031558 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Itoh A; Miyabayashi T; Ohno M; Sakano S (February 1999). "Cloning and expressions of three mammalian homologues of Drosophila slit suggest possible roles for Slit in the formation and maintenance of the nervous system". Brain Res Mol Brain Res. 62 (2): 175–86. doi:10.1016/S0169-328X(98)00224-1. PMID 9813312.
↑ Chedotal A (February 2008). "Slits and their receptors". Adv Exp Med Biol. 621: 65–80. doi:10.1007/978-0-387-76715-4_5. PMID 18269211.
↑ "Entrez Gene: SLIT2 slit homolog 2 (Drosophila)".
↑ Ronca, F; Andersen J S; Paech V; Margolis R U (August 2001). "Characterization of Slit protein interactions with glypican-1". J. Biol. Chem. United States. 276 (31): 29141–7. doi:10.1074/jbc.M100240200. ISSN 0021-9258. PMID 11375980.

Wong K; Park HT; Wu JY; Rao Y (2003). "Slit proteins: molecular guidance cues for cells ranging from neurons to leukocytes". Curr. Opin. Genet. Dev. 12 (5): 583–91. doi:10.1016/S0959-437X(02)00343-X. PMID 12200164.
Zhao XC; Zhang LM; Li Q; Tong DY; Fan LC; An P; Wu XY; Chen WM; Zhao P; Wang J. (2013). "Isoflurane post-conditioning protects primary cultures of cortical neurons against oxygen and glucose deprivation injury via upregulation of Slit2/Robo1". Brain Res. 1537: 283–9. doi:10.1016/j.brainres.2013.08.036. PMC 3820100. PMID 23994690.
Wang KH, Brose K, Arnott D, et al. (1999). "Biochemical purification of a mammalian slit protein as a positive regulator of sensory axon elongation and branching". Cell. 96 (6): 771–84. doi:10.1016/S0092-8674(00)80588-7. PMID 10102266.
Brose K, Bland KS, Wang KH, et al. (1999). "Slit proteins bind Robo receptors and have an evolutionarily conserved role in repulsive axon guidance". Cell. 96 (6): 795–806. doi:10.1016/S0092-8674(00)80590-5. PMID 10102268.
Li HS, Chen JH, Wu W, et al. (1999). "Vertebrate slit, a secreted ligand for the transmembrane protein roundabout, is a repellent for olfactory bulb axons". Cell. 96 (6): 807–18. doi:10.1016/S0092-8674(00)80591-7. PMID 10102269.
Nguyen Ba-Charvet KT, Brose K, Marillat V, et al. (1999). "Slit2-Mediated chemorepulsion and collapse of developing forebrain axons". Neuron. 22 (3): 463–73. doi:10.1016/S0896-6273(00)80702-3. PMID 10197527.
Holmes GP, Negus K, Burridge L, et al. (1999). "Distinct but overlapping expression patterns of two vertebrate slit homologs implies functional roles in CNS development and organogenesis". Mech. Dev. 79 (1–2): 57–72. doi:10.1016/S0925-4773(98)00174-9. PMID 10349621.
Liang Y, Annan RS, Carr SA, et al. (1999). "Mammalian homologues of the Drosophila slit protein are ligands of the heparan sulfate proteoglycan glypican-1 in brain". J. Biol. Chem. 274 (25): 17885–92. doi:10.1074/jbc.274.25.17885. PMID 10364234.
Wu W, Wong K, Chen J, et al. (1999). "Directional guidance of neuronal migration in the olfactory system by the protein Slit". Nature. 400 (6742): 331–6. Bibcode:1999Natur.400..331W. doi:10.1038/22477. PMC 2041931. PMID 10432110.
Georgas K, Burridge L, Smith K, et al. (2000). "Assignment of the human slit homologue SLIT2 to human chromosome band 4p15.2". Cytogenet. Cell Genet. 86 (3–4): 246–7. doi:10.1159/000015351. PMID 10575218.
Niclou SP; Jia L; Raper JA (2000). "Slit2 is a repellent for retinal ganglion cell axons". J. Neurosci. 20 (13): 4962–74. PMID 10864954.
Zou Y; Stoeckli E; Chen H; Tessier-Lavigne M (2000). "Squeezing axons out of the gray matter: a role for slit and semaphorin proteins from midline and ventral spinal cord". Cell. 102 (3): 363–75. doi:10.1016/S0092-8674(00)00041-6. PMID 10975526.
Chen JH, Wen L, Dupuis S, et al. (2001). "The N-terminal leucine-rich regions in Slit are sufficient to repel olfactory bulb axons and subventricular zone neurons". J. Neurosci. 21 (5): 1548–56. PMID 11222645.
Stein E; Tessier-Lavigne M (2001). "Hierarchical organization of guidance receptors: silencing of netrin attraction by slit through a Robo/DCC receptor complex". Science. 291 (5510): 1928–38. Bibcode:2001Sci...291.1928S. doi:10.1126/science.1058445. PMID 11239147.
Wu JY, Feng L, Park HT, et al. (2001). "The neuronal repellent Slit inhibits leukocyte chemotaxis induced by chemotactic factors". Nature. 410 (6831): 948–52. doi:10.1038/35073616. PMC 2072862. PMID 11309622.
Ronca F; Andersen JS; Paech V; Margolis RU (2001). "Characterization of Slit protein interactions with glypican-1". J. Biol. Chem. 276 (31): 29141–7. doi:10.1074/jbc.M100240200. PMID 11375980.
Nguyen Ba-Charvet KT, Brose K, Ma L, et al. (2001). "Diversity and specificity of actions of Slit2 proteolytic fragments in axon guidance". J. Neurosci. 21 (12): 4281–9. PMID 11404413.
Little M, Rumballe B, Georgas K, et al. (2003). "Conserved modularity and potential for alternate splicing in mouse and human Slit genes". Int. J. Dev. Biol. 46 (4): 385–91. PMID 12141424.
Dallol A, Da Silva NF, Viacava P, et al. (2002). "SLIT2, a human homologue of the Drosophila Slit2 gene, has tumor suppressor activity and is frequently inactivated in lung and breast cancers". Cancer Res. 62 (20): 5874–80. PMID 12384551.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000145147 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031558 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid9813312-5] Itoh A; Miyabayashi T; Ohno M; Sakano S (February 1999). "Cloning and expressions of three mammalian homologues of Drosophila slit suggest possible roles for Slit in the formation and maintenance of the nervous system". Brain Res Mol Brain Res. 62 (2): 175–86. doi:10.1016/S0169-328X(98)00224-1. PMID 9813312.

[pmid18269211-6] Chedotal A (February 2008). "Slits and their receptors". Adv Exp Med Biol. 621: 65–80. doi:10.1007/978-0-387-76715-4_5. PMID 18269211.

[entrez-7] "Entrez Gene: SLIT2 slit homolog 2 (Drosophila)".

[pmid11375980-8] Ronca, F; Andersen J S; Paech V; Margolis R U (August 2001). "Characterization of Slit protein interactions with glypican-1". J. Biol. Chem. United States. 276 (31): 29141–7. doi:10.1074/jbc.M100240200. ISSN 0021-9258. PMID 11375980.

SLIT2

Interactions

References

Further reading