SLIT2

Protein-coding gene in the species Homo sapiens
SLIT2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2V70, 2V9S, 2V9T, 2WFH

Identifiers
AliasesSLIT2, SLIL3, Slit-2, slit guidance ligand 2
External IDsOMIM: 603746; MGI: 1315205; HomoloGene: 3516; GeneCards: SLIT2; OMA:SLIT2 - orthologs
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for SLIT2
Genomic location for SLIT2
Band4p15.31Start20,251,905 bp[1]
End20,620,561 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for SLIT2
Genomic location for SLIT2
Band5|5 B3Start48,140,480 bp[2]
End48,465,075 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • lower lobe of lung

  • olfactory bulb

  • vena cava

  • trigeminal ganglion

  • right lung

  • spinal ganglia

  • urethra

  • pericardium

  • parietal pleura

  • middle temporal gyrus
Top expressed in
  • floor plate

  • ciliary body

  • sciatic nerve

  • vas deferens

  • Epithelium of choroid plexus

  • body of femur

  • iris

  • left lung lobe

  • medullary collecting duct

  • mammillary body
More reference expression data
BioGPS
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
  • aortic valve morphogenesis
  • pulmonary valve morphogenesis
  • ventricular septum morphogenesis
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

9353

20563

Ensembl

ENSG00000145147

ENSMUSG00000031558

UniProt

O94813

Q9R1B9

RefSeq (mRNA)

NM_001289135
NM_001289136
NM_004787

NM_001291227
NM_001291228
NM_178804

RefSeq (protein)

NP_001276064
NP_001276065
NP_004778

NP_001278156
NP_001278157
NP_848919

Location (UCSC)Chr 4: 20.25 – 20.62 MbChr 5: 48.14 – 48.47 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. ^ a b c GRCh38: Ensembl release 89: ENSG00000145147 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031558 – 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. ^ 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.
  6. ^ Chedotal A (February 2008). "Slits and Their Receptors". Axon Growth and Guidance. Advances in Experimental Medicine and Biology. Vol. 621. pp. 65–80. doi:10.1007/978-0-387-76715-4_5. ISBN 978-0-387-76714-7. PMID 18269211.
  7. ^ "Entrez Gene: SLIT2 slit homolog 2 (Drosophila)".
  8. ^ Ronca F, Andersen J S, Paech V, Margolis R U (August 2001). "Characterization of Slit protein interactions with glypican-1". J. Biol. Chem. 276 (31). United States: 29141–7. doi:10.1074/jbc.M100240200. ISSN 0021-9258. PMID 11375980.

Further reading

  • 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. S2CID 16810644.
  • 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. S2CID 16301178.
  • 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. S2CID 18663762.
  • 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. S2CID 6057216.
  • 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. S2CID 6028258.
  • Niclou SP, Jia L, Raper JA (2000). "Slit2 is a repellent for retinal ganglion cell axons". J. Neurosci. 20 (13): 4962–74. doi:10.1523/JNEUROSCI.20-13-04962.2000. PMC 6772294. 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" (PDF). Cell. 102 (3): 363–75. doi:10.1016/S0092-8674(00)00041-6. PMID 10975526. S2CID 14174593. Archived from the original (PDF) on 2018-11-01. Retrieved 2020-09-11.
  • 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. doi:10.1523/JNEUROSCI.21-05-01548.2001. PMC 6762944. PMID 11222645.
  • 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. Bibcode:2001Natur.410..948W. 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. doi:10.1523/JNEUROSCI.21-12-04281.2001. PMC 6762758. 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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