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SDCBP

Available structures

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)^[1]

Band	8q12.1	Start	58,552,924 bp^[1]
Band	8q12.1	End	58,582,859 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 4 (mouse)^[2]

Band	4\|4 A1	Start	6,365,650 bp^[2]
Band	4\|4 A1	End	6,408,423 bp^[2]

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

^[3]

^[4]

Wikidata

View/Edit Human

View/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:

EFNB1,^[7]
GRIK1,^[8]
GRIK2,^[8]^[9]
Interleukin 5 receptor alpha subunit,^[10]
Merlin,^[11]
RAB5A,^[12]
SOX4,^[10]
TRAF6,^[13]
ULK1.^[12] and
ERICH2^[14]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000137575 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028249 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ "Entrez Gene: SDCBP syndecan binding protein (syntenin)".
^ 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.
^ ^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.
^ 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.
^ ^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.
^ 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.
^ ^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.
^ 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.
^ "Results - mentha: the interactome browser". mentha.uniroma2.it. Retrieved 2017-05-04.

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.

PDB gallery

1n99: CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN 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.
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.
1r6j: Ultrahigh resolution Crystal Structure of syntenin PDZ2
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
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
1ybo: Crystal structure of the PDZ tandem of human syntenin with syndecan peptide