Selected-GenAtlas references SOURCE GeneCards NCBI Gene Swiss-Prot Ensembl
HGNC UniGene Nucleotide OMIM UCSC
Home Page
Symbol SDCBP contributors: mct/pgu - updated : 23-08-2016
HGNC name syndecan binding protein (syntenin)
HGNC id 10662
Location 8q12.1      Physical location : 59.465.727 - 59.495.418
Synonym name
  • melanoma differentiation associated gene 9
  • scaffold protein Pbp1
  • syntenin
  • syntenin-1
  • pro-TGF-alpha cytoplasmic domain-interacting protein 18
  • Synonym symbol(s) ST1, SYCL, MDA-9, TACIP18, SYNTENIN
    TYPE functioning gene
    STRUCTURE 29.70 kb     9 Exon(s)
    10 Kb 5' upstream gene genomic sequence study
    MAPPING cloned Y linked N status provisional
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    9 - 2173 - 298 - 2006 16908530
    9 - 2170 - 298 - 2006 16908530
    9 - 2155 - 292 - 2006 16908530
    9 - 2170 - 297 - 2006 16908530
    9 - 2167 - 297 - 2006 16908530
    Type ubiquitous
       expressed in (based on citations)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Cardiovascularheart   highly
    Digestiveesophagus   highly
    Endocrineparathyroid   highly
    Lymphoid/Immunespleen   highly
     thymus   highly
    SystemCellPubmedSpeciesStageRna symbol
    Nervousepithelial cell
    cell lineage
    cell lines
    at STAGE
    Text fetal kidney, liver, lung and brain, placenta
  • an autoinhibitory peptide stretch in the N-terminus that might be regulated by phosphorylation
  • two PDZ (PSD95, Dlg, Z0-1/2) motifs, (DHR) domains, tandem PDZ domains of 83 and 80 AAs, respectively (PDZ1 and PDZ2), that are required for the assembly and organization of diverse cell signaling processes occurring at the plasma membrane; both PDZ domains, with PDZ2 being the dominant module, are required for activating downstream signaling pathways, including MAPK14 and NF-kappaB
  • this two PDZ domains interacting with various receptors and phosphoinositides, and are flanked by N- and C-terminal regions (
  • C terminus having a stabilizing role in the CD63-SDCBP interaction
  • mono polymer homomer , heteromer
    CATEGORY adaptor
    SUBCELLULAR LOCALIZATION     plasma membrane,junction,adherens
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    basic FUNCTION
  • regulation of plasma membrane dynamics
  • PDZ domain-containing protein, playing a potential role in nuclear processes
  • in adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components
  • playing a role in controlling membrane organization and through interaction with kainate receptors in determining the formation and maturation of synapses
  • functions as a positive regulator of cancer cell progression in human melanoma and other tumors
  • can counteract the AP-2-dependent internalization and identify this tandem PDZ protein as a new regulator of endocytosis
  • enhancing the assembly of stableSRC-FAK signaling complexes, initiating a signaling cascade that results in enhanced anchorage independence, cell motility, and metastatic competence in melanoma cells
  • plays a role in the migration of oligodendroglial precursors, suggesting thatCSPG4-SDCBP interactions contribute to this
  • might play an active role in tumor cell invasion and metastasis
  • tandem PDZ protein that binds a diverse array of signaling molecules that are often associated with cell adhesion and intracellular trafficking
  • adaptor modulating the activity of lysyl-tRNA synthetase
  • mediates adhesion-mediated activation of protein kinase Calpha (PRKCA) and focal adhesion kinase (FAK) by fibronectin (FN) in human breast cancer and melanoma cells
  • acts as a molecular adaptor linking PRKCA and FAK activation in a pathway of FN adhesion by human breast cancer and melanoma cells
  • regulates a cellular process involving endocytosis and intracellular transport
  • may play an important role via interaction with ubiquitin in the regulation of cancer metastasis and invasion
  • functioned as a cytosolic signal effector downstream from SDC2
  • serves as a scaffolding regulator in syndecan-2-mediated colon cancer cell migration
  • positively regulates the activation of AKT1 protein by facilitating integrin-linked kinase adaptor function during adhesion to type I collagen
  • key role of SDCBP in the generation of functional asymmetry in T cells
  • is a novel and important mediator of invasion in glioblastoma multiforme (GBM) and a key regulator of pathogenesis
  • intracellular PDZ protein that binds multiple proteins and regulates protein trafficking, cancer metastasis, exosome production, synaptic formation, and IL5 signaling
  • likely negatively regulates the intestinal immunoglobulin production and has a function to maintain the intestinal homeostasis
  • tandem PDZ domain containing scaffold protein, functions as a positive regulator of cancer cell progression in several human cancers
  • role of the syndecan (SDC1) heparan sulphate proteoglycans, the small intracellular adaptor SDCBP and associated regulators in the biogenesis and loading of exosomes with cargo
    a component
  • component of adherens junctions with syndecans 1,E-cadherin, beta and alpha-catenins
  • forming homodimers and heterodimers with SDCBP2
  • component of TERM (tetraspanin-enriched microdomains)
  • key role for syndecan-syntenin-PDCD6IP in membrane transport and signalling processes
    small molecule
  • associating with the cytoplasmic tail of ILR5R alpha
  • interacting with the FYA motif of syndecan
  • interacting with the cytoplasmic tail of neurofascin
  • specifically interacts with the tetraspanin CD63 (interaction mediated by the C-terminal cytoplasmic region of the tetraspanin and the PDZ domains of SDCBP)
  • interacts with CSPG4 and is necessary for normal rates of migration
  • physically interacts with SRC and this communication correlates with an increase in FAK/SRC complex formation and SRC activation
  • interaction with lysyl-tRNA synthetase (KARS), which contains a PDZ binding motif at its C-terminus (motif is important for the interaction of the entire complex with syntenin-1)
  • binds to ubiquitin by a non-covalent bond and is ubiquitinated covalently
  • interacts with the C-terminal EFYA sequence of SDC2, and thus regulates SDC2-mediated Rac activation and subsequent colon cancer cell migration
  • SDCBP, a SOX4 binding partner, associates with C-terminal 33 AAs of SOX4 and was found to stabilize SOX4 expression
  • controls RAC1 through a specific association with the myosin phosphatase Rho interacting protein (MPRIP), which occurs in response to phosphorylation of SDCBP by SRC at Tyr4
  • interacts directly with PDCD6IP through LYPX(n)L motifs, similarly to retroviral proteins
  • ALCAM stably interacts with actin by binding to SDCBP and EZR, and interaction with the ligand CD6 further enhances these multiple interactions
  • HPSE stimulates the exosomal secretion of SDCBP, SDC1 and certain other exosomal cargo, such as CD63, in a concentration-dependent manner
  • PDZ protein SDCBP preferentially binds to the GDP-bound form of RHEB
  • SDCBP may act as an important positive regulator of TGFB1 signaling by regulating caveolin-1-mediated internalization of TGFBR1
  • cell & other
    induced by gamma interferon in melanoma cells
    Other phosphorylated on tyrosine residues
    potentially tyrosine dephosphorylation of SDC1 may regulate syntenin-1 association with cytoskeleton components
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    tumoral     --low  
    by RNA interference could provide a means of inhibiting tumor invasion and possibly metastasis in different cancers
    tumoral     --over  
    in melanoma, and breast and gastric cancer cells (
    tumoral     --over  
    in high-grade astrocytomas
    Variant & Polymorphism
    Candidate gene
    Therapy target
    PDZ domains of SDCBP is a promising potential therapeutic targets for intervening in a decisive component of cancer progression, namely, metastatic tumor spread
    a potential cancer biomarker and drug target