Syntenin-1

Protein found in humans

SDCBP
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1N99, 1NTE, 1OBX, 1OBY, 1OBZ, 1R6J, 1V1T, 1W9E, 1W9O, 1W9Q, 1YBO, 4Z33

Identifiers
AliasesSDCBP, MDA-9, ST1, SYCL, TACIP18, MDA9, syndecan binding protein
External IDsOMIM: 602217; MGI: 1337026; HomoloGene: 4110; GeneCards: SDCBP; OMA:SDCBP - orthologs
Gene location (Human)
Chromosome 8 (human)
Chr.Chromosome 8 (human)[1]
Chromosome 8 (human)
Genomic location for SDCBP
Genomic location for SDCBP
Band8q12.1Start58,552,924 bp[1]
End58,582,859 bp[1]
Gene location (Mouse)
Chromosome 4 (mouse)
Chr.Chromosome 4 (mouse)[2]
Chromosome 4 (mouse)
Genomic location for SDCBP
Genomic location for SDCBP
Band4|4 A1Start6,365,650 bp[2]
End6,408,423 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 4: 6.37 – 6.41 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Syntenin-1 is a protein that in humans is encoded by the SDCBP gene.[5]

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.[6]

Interactions

SDCBP has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000137575 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028249 – 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. ^ Grootjans JJ, Zimmermann P, Reekmans G, Smets A, Degeest G, Dürr J, David G (January 1998). "Syntenin, a PDZ protein that binds syndecan cytoplasmic domains". Proc Natl Acad Sci USA. 94 (25): 13683–8. Bibcode:1997PNAS...9413683G. doi:10.1073/pnas.94.25.13683. PMC 28366. PMID 9391086.
  6. ^ "Entrez Gene: SDCBP syndecan binding protein (syntenin)".
  7. ^ Lin D, Gish GD, Songyang Z, Pawson T (February 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.
  8. ^ a b Hirbec H, Francis JC, Lauri SE, Braithwaite SP, Coussen F, Mulle C, Dev KK, Coutinho V, Meyer G, Isaac JT, Collingridge GL, Henley JM, Couthino V (February 2003). "Rapid and differential regulation of AMPA and kainate receptors at hippocampal mossy fibre synapses by PICK1 and GRIP". Neuron. 37 (4): 625–38. doi:10.1016/s0896-6273(02)01191-1. PMC 3314502. PMID 12597860.
  9. ^ Hirbec H, Perestenko O, Nishimune A, Meyer G, Nakanishi S, Henley JM, Dev KK (May 2002). "The PDZ proteins PICK1, GRIP, and syntenin bind multiple glutamate receptor subtypes. Analysis of PDZ binding motifs". J. Biol. Chem. 277 (18): 15221–4. doi:10.1074/jbc.C200112200. hdl:2262/89271. PMID 11891216.
  10. ^ a b Geijsen N, Uings IJ, Pals C, Armstrong J, McKinnon M, Raaijmakers JA, Lammers JW, Koenderman L, Coffer PJ (August 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.
  11. ^ Jannatipour M, Dion P, Khan S, Jindal H, Fan X, Laganière J, Chishti AH, Rouleau GA (August 2001). "Schwannomin isoform-1 interacts with syntenin via PDZ domains". J. Biol. Chem. 276 (35): 33093–100. doi:10.1074/jbc.M105792200. PMID 11432873.
  12. ^ a b Tomoda T, Kim JH, Zhan C, Hatten ME (March 2004). "Role of Unc51.1 and its binding partners in CNS axon outgrowth". Genes Dev. 18 (5): 541–58. doi:10.1101/gad.1151204. PMC 374236. PMID 15014045.
  13. ^ Chen F, Du Y, Zhang Z, Chen G, Zhang M, Shu HB, Zhai Z, Chen D (April 2008). "Syntenin negatively regulates TRAF6-mediated IL-1R/TLR4 signaling". Cell. Signal. 20 (4): 666–74. doi:10.1016/j.cellsig.2007.12.002. PMID 18234474. S2CID 28812149.
  14. ^ "Results - mentha: the interactome browser". mentha.uniroma2.it. Retrieved 2017-05-04.

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.
  • v
  • t
  • e
  • 1n99: CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN
    1n99: CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN
  • 1nte: CRYSTAL STRUCTURE ANALYSIS OF THE SECOND PDZ DOMAIN OF SYNTENIN
    1nte: CRYSTAL STRUCTURE ANALYSIS OF THE SECOND PDZ DOMAIN OF SYNTENIN
  • 1obx: CRYSTAL STRUCTURE OF THE COMPLEX OF PDZ2 OF SYNTENIN WITH AN INTERLEUKIN 5 RECEPTOR ALPHA PEPTIDE.
    1obx: CRYSTAL STRUCTURE OF THE COMPLEX OF PDZ2 OF SYNTENIN WITH AN INTERLEUKIN 5 RECEPTOR ALPHA PEPTIDE.
  • 1oby: CRYSTAL STRUCTURE OF THE COMPLEX OF PDZ2 OF SYNTENIN WITH A SYNDECAN-4 PEPTIDE.
    1oby: CRYSTAL STRUCTURE OF THE COMPLEX OF PDZ2 OF SYNTENIN WITH A SYNDECAN-4 PEPTIDE.
  • 1obz: CRYSTAL STRUCTURE OF THE COMPLEX OF THE PDZ TANDEM OF SYNTENIN WITH AN INTERLEUKIN 5 RECEPTOR ALPHA PEPTIDE.
    1obz: CRYSTAL STRUCTURE OF THE COMPLEX OF THE PDZ TANDEM OF SYNTENIN WITH AN INTERLEUKIN 5 RECEPTOR ALPHA PEPTIDE.
  • 1r6j: Ultrahigh resolution Crystal Structure of syntenin PDZ2
    1r6j: Ultrahigh resolution Crystal Structure of syntenin PDZ2
  • 1v1t: CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN IN COMPLEX WITH TNEYKV PEPTIDE
    1v1t: CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN IN COMPLEX WITH TNEYKV PEPTIDE
  • 1w9e: CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN IN COMPLEX WITH TNEFYF PEPTIDE
    1w9e: CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN IN COMPLEX WITH TNEFYF PEPTIDE
  • 1w9o: CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN IN COMPLEX WITH TNEYYV PEPTIDE
    1w9o: CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN IN COMPLEX WITH TNEYYV PEPTIDE
  • 1w9q: CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN IN COMPLEX WITH TNEFAF PEPTIDE
    1w9q: CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN IN COMPLEX WITH TNEFAF PEPTIDE
  • 1ybo: Crystal structure of the PDZ tandem of human syntenin with syndecan peptide
    1ybo: Crystal structure of the PDZ tandem of human syntenin with syndecan peptide


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