Syntenin-1

SDCBP
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1N99, 1NTE, 1OBX, 1OBY, 1OBZ, 1R6J, 1V1T, 1W9E, 1W9O, 1W9Q, 1YBO, 4Z33
Identifiers
Aliases	SDCBP, MDA-9, ST1, SYCL, TACIP18, MDA9, syndecan binding protein
External IDs	OMIM: 602217; MGI: 1337026; HomoloGene: 4110; GeneCards: SDCBP; OMA:SDCBP - orthologs
Gene location (Human) Chr. Chromosome 8 (human) Band 8q12.1 Start 58,552,924 bp End 58,582,859 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4|4 A1 Start 6,365,650 bp End 6,408,423 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in retinal pigment epithelium visceral pleura amniotic fluid palpebral conjunctiva parietal pleura germinal epithelium blood skin of hip ganglionic eminence monocyte Top expressed in stroma of bone marrow gastrula fetal liver hematopoietic progenitor cell pyloric antrum calvaria tibiofemoral joint atrioventricular valve right lung mucous cell of stomach submandibular gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein N-terminus binding frizzled binding protein binding identical protein binding cytoskeletal anchor activity interleukin-5 receptor binding phosphatidylinositol-4,5-bisphosphate binding lipid binding cadherin binding syndecan binding protein heterodimerization activity Cellular component cytoplasm extracellular vesicle blood microparticle endoplasmic reticulum membrane membrane focal adhesion melanosome adherens junction plasma membrane cell junction endoplasmic reticulum membrane raft extracellular exosome cytoskeleton nucleus extracellular region extracellular space nucleoplasm cytosol interleukin-5 receptor nuclear membrane azurophil granule lumen intracellular membrane-bounded organelle Biological process positive regulation of transforming growth factor beta receptor signaling pathway intracellular signal transduction positive regulation of extracellular exosome assembly negative regulation of receptor internalization protein targeting to membrane ephrin receptor signaling pathway substrate-dependent cell migration, cell extension positive regulation of pathway-restricted SMAD protein phosphorylation positive regulation of JNK cascade positive regulation of epithelial to mesenchymal transition regulation of mitotic cell cycle negative regulation of proteasomal ubiquitin-dependent protein catabolic process positive regulation of exosomal secretion positive regulation of phosphorylation actin cytoskeleton organization chemical synaptic transmission positive regulation of cell population proliferation positive regulation of cell growth positive regulation of cell migration neutrophil degranulation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6386 53378 Ensembl ENSG00000137575 ENSMUSG00000028249 UniProt O00560 O08992 RefSeq (mRNA) NM_001007067 NM_001007068 NM_001007069 NM_001007070 NM_005625 NM_001330537 NM_001348339 NM_001348340 NM_001348341 NM_001098227 NM_016807 RefSeq (protein) NP_001007068 NP_001007069 NP_001007070 NP_001007071 NP_001317466 NP_005616 NP_001335268 NP_001335269 NP_001335270 NP_001091697 NP_058087 Location (UCSC) Chr 8: 58.55 – 58.58 Mb Chr 4: 6.37 – 6.41 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Syntenin-1 is a protein that in humans is encoded by the SDCBP gene.

Function

The protein encoded by this gene was initially identified as a molecule linking syndecan-mediated signaling to the cytoskeleton. The syntenin protein contains tandemly repeated PDZ domains that bind the cytoplasmic, C-terminal domains of a variety of transmembrane proteins. This protein may also affect cytoskeletal-membrane organization, cell adhesion, protein trafficking, and the activation of transcription factors. The protein is primarily localized to membrane-associated adherens junctions and focal adhesions but is also found at the endoplasmic reticulum and nucleus. Alternative splicing results in multiple transcript variants encoding different isoforms.

Interactions

SDCBP has been shown to interact with:

• EFNB1,
• GRIK1,
• GRIK2,
• Interleukin 5 receptor alpha subunit,
• Merlin,
• RAB5A,
• SOX4,
• TRAF6,
• ULK1. and
• ERICH2

Further reading

• Bass MD, Humphries MJ (2002). "Cytoplasmic interactions of syndecan-4 orchestrate adhesion receptor and growth factor receptor signalling". Biochem. J. 368 (Pt 1): 1–15. doi:10.1042/BJ20021228. PMC 1222989. PMID 12241528.
• Harrod TR, Justement LB (2003). "Evaluating function of transmembrane protein tyrosine phosphatase CD148 in lymphocyte biology". Immunol. Res. 26 (1–3): 153–66. doi:10.1385/IR:26:1-3:153. PMID 12403354. S2CID 26502472.
• Sarkar D, Boukerche H, Su ZZ, Fisher PB (2005). "mda-9/syntenin: recent insights into a novel cell signaling and metastasis-associated gene". Pharmacol. Ther. 104 (2): 101–15. doi:10.1016/j.pharmthera.2004.08.004. PMID 15518882.
• "Letter: The condition of psychiatry". N. Engl. J. Med. 292 (18): 982. 1975. doi:10.1056/NEJM197505012921826. PMID 1117941.
• Lin JJ, Jiang H, Fisher PB (1998). "Melanoma differentiation associated gene-9, mda-9, is a human gamma interferon responsive gene". Gene. 207 (2): 105–10. doi:10.1016/S0378-1119(97)00562-3. PMID 9511750.
• Torres R, Firestein BL, Dong H, Staudinger J, Olson EN, Huganir RL, Bredt DS, Gale NW, Yancopoulos GD (1999). "PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands". Neuron. 21 (6): 1453–63. doi:10.1016/S0896-6273(00)80663-7. PMID 9883737. S2CID 15441813.
• Lin D, Gish GD, Songyang Z, Pawson T (1999). "The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif". J. Biol. Chem. 274 (6): 3726–33. doi:10.1074/jbc.274.6.3726. PMID 9920925.
• Fernández-Larrea J, Merlos-Suárez A, Ureña JM, Baselga J, Arribas J (1999). "A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-alpha to the cell surface". Mol. Cell. 3 (4): 423–33. doi:10.1016/S1097-2765(00)80470-0. PMID 10230395.
• Fialka I, Steinlein P, Ahorn H, Böck G, Burbelo PD, Haberfellner M, Lottspeich F, Paiha K, Pasquali C, Huber LA (1999). "Identification of syntenin as a protein of the apical early endocytic compartment in Madin-Darby canine kidney cells". J. Biol. Chem. 274 (37): 26233–9. doi:10.1074/jbc.274.37.26233. PMID 10473577.
• Grootjans JJ, Reekmans G, Ceulemans H, David G (2000). "Syntenin-syndecan binding requires syndecan-synteny and the co-operation of both PDZ domains of syntenin". J. Biol. Chem. 275 (26): 19933–41. doi:10.1074/jbc.M002459200. PMID 10770943.
• Koroll M, Rathjen FG, Volkmer H (2001). "The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity". J. Biol. Chem. 276 (14): 10646–54. doi:10.1074/jbc.M010647200. PMID 11152476.
• Zimmermann P, Tomatis D, Rosas M, Grootjans J, Leenaerts I, Degeest G, Reekmans G, Coomans C, David G (2001). "Characterization of syntenin, a syndecan-binding PDZ protein, as a component of cell adhesion sites and microfilaments". Mol. Biol. Cell. 12 (2): 339–50. doi:10.1091/mbc.12.2.339. PMC 30947. PMID 11179419.
• Jannatipour M, Dion P, Khan S, Jindal H, Fan X, Laganière J, Chishti AH, Rouleau GA (2001). "Schwannomin isoform-1 interacts with syntenin via PDZ domains". J. Biol. Chem. 276 (35): 33093–100. doi:10.1074/jbc.M105792200. PMID 11432873.
• Geijsen N, Uings IJ, Pals C, Armstrong J, McKinnon M, Raaijmakers JA, Lammers JW, Koenderman L, Coffer PJ (2001). "Cytokine-specific transcriptional regulation through an IL-5Ralpha interacting protein". Science. 293 (5532): 1136–8. doi:10.1126/science.1059157. PMID 11498591. S2CID 28003281.
• Hirbec H, Perestenko O, Nishimune A, Meyer G, Nakanishi S, Henley JM, Dev KK (2002). "The PDZ proteins PICK1, GRIP, and syntenin bind multiple glutamate receptor subtypes. Analysis of PDZ binding motifs" (PDF). J. Biol. Chem. 277 (18): 15221–4. doi:10.1074/jbc.C200112200. PMID 11891216. S2CID 13732968.
• Koo TH, Lee JJ, Kim EM, Kim KW, Kim HD, Lee JH (2002). "Syntenin is overexpressed and promotes cell migration in metastatic human breast and gastric cancer cell lines". Oncogene. 21 (26): 4080–8. doi:10.1038/sj.onc.1205514. PMID 12037664.
• Biederer T, Sara Y, Mozhayeva M, Atasoy D, Liu X, Kavalali ET, Südhof TC (2002). "SynCAM, a synaptic adhesion molecule that drives synapse assembly". Science. 297 (5586): 1525–31. Bibcode:2002Sci...297.1525B. doi:10.1126/science.1072356. PMID 12202822. S2CID 14529914.