P18827 · SDC1_HUMAN
- ProteinSyndecan-1
- GeneSDC1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids310 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cell surface proteoglycan that contains both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix (By similarity).
Regulates exosome biogenesis in concert with SDCBP and PDCD6IP (PubMed:22660413).
Able to induce its own expression in dental mesenchymal cells and also in the neighboring dental epithelial cells via an MSX1-mediated pathway (By similarity).
Regulates exosome biogenesis in concert with SDCBP and PDCD6IP (PubMed:22660413).
Able to induce its own expression in dental mesenchymal cells and also in the neighboring dental epithelial cells via an MSX1-mediated pathway (By similarity).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 242-243 | Cleavage | ||||
Sequence: AS |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Cellular Component | external side of plasma membrane | |
Cellular Component | extracellular exosome | |
Cellular Component | Golgi lumen | |
Cellular Component | lysosomal lumen | |
Cellular Component | plasma membrane | |
Cellular Component | protein-containing complex | |
Molecular Function | cargo receptor activity | |
Molecular Function | identical protein binding | |
Biological Process | canonical Wnt signaling pathway | |
Biological Process | cell migration | |
Biological Process | myoblast development | |
Biological Process | positive regulation of exosomal secretion | |
Biological Process | positive regulation of extracellular exosome assembly | |
Biological Process | receptor-mediated endocytosis | |
Biological Process | response to calcium ion | |
Biological Process | response to cAMP | |
Biological Process | response to glucocorticoid | |
Biological Process | response to hydrogen peroxide | |
Biological Process | response to toxic substance | |
Biological Process | Sertoli cell development | |
Biological Process | striated muscle cell development | |
Biological Process | ureteric bud development |
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSyndecan-1
- Short namesSYND1
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP18827
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type I membrane protein
Note: Shedding of the ectodomain produces a soluble form.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 23-254 | Extracellular | ||||
Sequence: QIVATNLPPEDQDGSGDDSDNFSGSGAGALQDITLSQQTPSTWKDTQLLTAIPTSPEPTGLEATAASTSTLPAGEGPKEGEAVVLPEVEPGLTAREQEATPRPRETTQLPTTHLASTTTATTAQEPATSHPHRDMQPGHHETSTPAGPSQADLHTPHTEDGGPSATERAAEDGASSQLPAAEGSGEQDFTFETSGENTAVVAVEPDRRNQSPVDQGATGASQGLLDRKEVLG | ||||||
Transmembrane | 255-275 | Helical | ||||
Sequence: GVIAGGLVGLIFAVCLVGFML | ||||||
Topological domain | 276-310 | Cytoplasmic | ||||
Sequence: YRMKKKDEGSYSLEEPKQANGGAYQKPTKQEEFYA |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_052242 | 76 | in dbSNP:rs2230922 | |||
Sequence: T → M | ||||||
Natural variant | VAR_052243 | 136 | in dbSNP:rs10205485 | |||
Sequence: L → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 429 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-22 | UniProt | |||||
Sequence: MRRAALWLWLCALALSLQPALP | |||||||
Chain | PRO_0000033499 | 23-310 | UniProt | Syndecan-1 | |||
Sequence: QIVATNLPPEDQDGSGDDSDNFSGSGAGALQDITLSQQTPSTWKDTQLLTAIPTSPEPTGLEATAASTSTLPAGEGPKEGEAVVLPEVEPGLTAREQEATPRPRETTQLPTTHLASTTTATTAQEPATSHPHRDMQPGHHETSTPAGPSQADLHTPHTEDGGPSATERAAEDGASSQLPAAEGSGEQDFTFETSGENTAVVAVEPDRRNQSPVDQGATGASQGLLDRKEVLGGVIAGGLVGLIFAVCLVGFMLYRMKKKDEGSYSLEEPKQANGGAYQKPTKQEEFYA | |||||||
Glycosylation | 37 | UniProt | O-linked (Xyl...) (chondroitin sulfate) serine | ||||
Sequence: S | |||||||
Glycosylation | 43 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 45 | UniProt | O-linked (Xyl...) (heparan sulfate) serine | ||||
Sequence: S | |||||||
Glycosylation | 47 | UniProt | O-linked (Xyl...) (heparan sulfate) serine | ||||
Sequence: S | |||||||
Glycosylation | 206 | UniProt | O-linked (Xyl...) (chondroitin sulfate) serine | ||||
Sequence: S | |||||||
Glycosylation | 216 | UniProt | O-linked (Xyl...) (chondroitin sulfate) serine | ||||
Sequence: S | |||||||
Modified residue | 285 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 285 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 286 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 287 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 299 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 309 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Shedding is enhanced by a number of factors such as heparanase, thrombin or EGF. Also by stress and wound healing. PMA-mediated shedding is inhibited by TIMP3.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with CDCP1. Interacts (via C-terminus) with TIAM1 (via PDZ domain). Interacts with MDK (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P18827 | APP P05067 | 3 | EBI-2855248, EBI-77613 | |
BINARY | P18827 | SDC1 P18827 | 2 | EBI-2855248, EBI-2855248 | |
BINARY | P18827 | SDC2 P34741 | 3 | EBI-2855248, EBI-1172957 | |
BINARY | P18827 | TIAM1 Q13009 | 5 | EBI-2855248, EBI-1050007 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 27-100 | Disordered | ||||
Sequence: TNLPPEDQDGSGDDSDNFSGSGAGALQDITLSQQTPSTWKDTQLLTAIPTSPEPTGLEATAASTSTLPAGEGPK | ||||||
Compositional bias | 40-76 | Polar residues | ||||
Sequence: DSDNFSGSGAGALQDITLSQQTPSTWKDTQLLTAIPT | ||||||
Region | 114-212 | Disordered | ||||
Sequence: LTAREQEATPRPRETTQLPTTHLASTTTATTAQEPATSHPHRDMQPGHHETSTPAGPSQADLHTPHTEDGGPSATERAAEDGASSQLPAAEGSGEQDFT | ||||||
Compositional bias | 125-151 | Polar residues | ||||
Sequence: PRETTQLPTTHLASTTTATTAQEPATS | ||||||
Region | 284-310 | Disordered | ||||
Sequence: GSYSLEEPKQANGGAYQKPTKQEEFYA |
Sequence similarities
Belongs to the syndecan proteoglycan family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length310
- Mass (Da)32,462
- Last updated2009-05-05 v3
- Checksum8E9EF4A57F5FDBD0
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 19 | in Ref. 2; AAA60605 | ||||
Sequence: P → L | ||||||
Compositional bias | 40-76 | Polar residues | ||||
Sequence: DSDNFSGSGAGALQDITLSQQTPSTWKDTQLLTAIPT | ||||||
Compositional bias | 125-151 | Polar residues | ||||
Sequence: PRETTQLPTTHLASTTTATTAQEPATS | ||||||
Sequence conflict | 259 | in Ref. 6; AAH08765 | ||||
Sequence: G → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X60306 EMBL· GenBank· DDBJ | CAA42851.1 EMBL· GenBank· DDBJ | mRNA | ||
J05392 EMBL· GenBank· DDBJ | AAA60605.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ551176 EMBL· GenBank· DDBJ | CAD80245.1 EMBL· GenBank· DDBJ | mRNA | ||
AC104792 EMBL· GenBank· DDBJ | AAX93151.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471053 EMBL· GenBank· DDBJ | EAX00828.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471053 EMBL· GenBank· DDBJ | EAX00829.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471053 EMBL· GenBank· DDBJ | EAX00830.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471053 EMBL· GenBank· DDBJ | EAX00831.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC008765 EMBL· GenBank· DDBJ | AAH08765.1 EMBL· GenBank· DDBJ | mRNA | ||
Z48199 EMBL· GenBank· DDBJ | CAA88235.1 EMBL· GenBank· DDBJ | Genomic DNA |