Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P18827 (SDC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Syndecan-1

Short name=SYND1
Alternative name(s):
CD_antigen=CD138
Gene names
Name:SDC1
Synonyms:SDC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell surface proteoglycan that bears both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix.

Subunit structure

Interacts with CDCP1. Interacts (via C-terminus) with TIAM1 (via PDZ domain). Ref.9 Ref.11

Subcellular location

Membrane; Single-pass type I membrane protein. Secreted. Note: Shedding of the ectodomain produces a soluble form.

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.

Sequence similarities

Belongs to the syndecan proteoglycan family.

Ontologies

Keywords
   Cellular componentMembrane
Secreted
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   PTMGlycoprotein
Heparan sulfate
Proteoglycan
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSertoli cell development

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

carbohydrate metabolic process

Traceable author statement. Source: Reactome

chondroitin sulfate metabolic process

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

glycosaminoglycan biosynthetic process

Traceable author statement. Source: Reactome

glycosaminoglycan catabolic process

Traceable author statement. Source: Reactome

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

inflammatory response

Inferred from electronic annotation. Source: Ensembl

lipoprotein metabolic process

Traceable author statement. Source: Reactome

myoblast development

Inferred from sequence or structural similarity. Source: UniProtKB

odontogenesis

Inferred from electronic annotation. Source: Ensembl

phototransduction, visible light

Traceable author statement. Source: Reactome

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

retinoid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

striated muscle cell development

Inferred from expression pattern PubMed 9566955. Source: UniProtKB

ureteric bud development

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

cytoplasm

Inferred from direct assay. Source: HPA

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

focal adhesion

Inferred from direct assay. Source: HPA

integral component of plasma membrane

Traceable author statement Ref.2. Source: ProtInc

lysosomal lumen

Traceable author statement. Source: Reactome

plasma membrane

Traceable author statement. Source: Reactome

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein C-terminus binding

Inferred from physical interaction PubMed 16982797. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 310288Syndecan-1
PRO_0000033499

Regions

Topological domain23 – 254232Extracellular Potential
Transmembrane255 – 27521Helical; Potential
Topological domain276 – 31035Cytoplasmic Potential

Sites

Site242 – 2432Cleavage By similarity

Amino acid modifications

Glycosylation371O-linked (Xyl...) (chondroitin sulfate) By similarity
Glycosylation431N-linked (GlcNAc...) Potential
Glycosylation451O-linked (Xyl...) (heparan sulfate) By similarity
Glycosylation471O-linked (Xyl...) (heparan sulfate) By similarity
Glycosylation2061O-linked (Xyl...) (chondroitin sulfate) By similarity
Glycosylation2161O-linked (Xyl...) (chondroitin sulfate) By similarity

Natural variations

Natural variant761T → M.
Corresponds to variant rs2230922 [ dbSNP | Ensembl ].
VAR_052242
Natural variant1361L → Q. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.7
Corresponds to variant rs10205485 [ dbSNP | Ensembl ].
VAR_052243

Experimental info

Sequence conflict191P → L in AAA60605. Ref.2
Sequence conflict2591G → V in AAH08765. Ref.6

Secondary structure

... 310
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18827 [UniParc].

Last modified May 5, 2009. Version 3.
Checksum: 8E9EF4A57F5FDBD0

FASTA31032,462
        10         20         30         40         50         60 
MRRAALWLWL CALALSLQPA LPQIVATNLP PEDQDGSGDD SDNFSGSGAG ALQDITLSQQ 

        70         80         90        100        110        120 
TPSTWKDTQL LTAIPTSPEP TGLEATAAST STLPAGEGPK EGEAVVLPEV EPGLTAREQE 

       130        140        150        160        170        180 
ATPRPRETTQ LPTTHLASTT TATTAQEPAT SHPHRDMQPG HHETSTPAGP SQADLHTPHT 

       190        200        210        220        230        240 
EDGGPSATER AAEDGASSQL PAAEGSGEQD FTFETSGENT AVVAVEPDRR NQSPVDQGAT 

       250        260        270        280        290        300 
GASQGLLDRK EVLGGVIAGG LVGLIFAVCL VGFMLYRMKK KDEGSYSLEE PKQANGGAYQ 

       310 
KPTKQEEFYA 

« Hide

References

« Hide 'large scale' references
[1]"Differential expression of cell surface heparan sulfate proteoglycans in human mammary epithelial cells and lung fibroblasts."
Lories V., Cassiman J.-J., van de Berghe H., David G.
J. Biol. Chem. 267:1116-1122(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-136.
Tissue: Fibroblast.
[2]"Sequence of human syndecan indicates a novel gene family of integral membrane proteoglycans."
Mali M., Jaakkola P., Arvilommi A.-M., Jalkanen M.
J. Biol. Chem. 265:6884-6889(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-136.
Tissue: Mammary gland.
[3]"Shift of syndecan-1 expression from epithelial to stromal cells during progression of solid tumours."
Mennerich D., Vogel A., Klaman I., Dahl E., Lichtner R.B., Rosenthal A., Pohlenz H.D., Thierauch K.H., Sommer A.
Eur. J. Cancer 40:1373-1382(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-136.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-136.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-136.
Tissue: Kidney.
[7]"The mapping and visual ordering of the human syndecan-1 and N-myc genes near the telomeric region of chromosome 2p."
Kaukonen J., Alanen-Kurki L., Jalkanen M., Palotie A.
Hum. Genet. 99:295-297(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-310, VARIANT GLN-136.
Tissue: Placenta.
[8]"Regulated shedding of syndecan-1 and -4 ectodomains by thrombin and growth factor receptor activation."
Subramanian S.V., Fitzgerald M.L., Bernfield M.
J. Biol. Chem. 272:14713-14720(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SHEDDING.
[9]"Adhesion signaling by a novel mitotic substrate of src kinases."
Bhatt A.S., Erdjument-Bromage H., Tempst P., Craik C.S., Moasser M.M.
Oncogene 24:5333-5343(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDCP1.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics."
Liu X., Shepherd T.R., Murray A.M., Xu Z., Fuentes E.J.
Structure 21:342-354(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 303-310 IN COMPLEX WITH TIAM1, INTERACTION WITH TIAM1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60306 mRNA. Translation: CAA42851.1.
J05392 mRNA. Translation: AAA60605.1.
AJ551176 mRNA. Translation: CAD80245.1.
AC104792 Genomic DNA. Translation: AAX93151.1.
CH471053 Genomic DNA. Translation: EAX00828.1.
CH471053 Genomic DNA. Translation: EAX00829.1.
CH471053 Genomic DNA. Translation: EAX00830.1.
CH471053 Genomic DNA. Translation: EAX00831.1.
BC008765 mRNA. Translation: AAH08765.1.
Z48199 Genomic DNA. Translation: CAA88235.1.
PIRA41776.
RefSeqNP_001006947.1. NM_001006946.1.
NP_002988.3. NM_002997.4.
UniGeneHs.224607.
Hs.665958.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4GVCX-ray1.54B303-310[»]
4GVDX-ray1.85C/D303-310[»]
ProteinModelPortalP18827.
SMRP18827. Positions 277-310.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112284. 14 interactions.
DIPDIP-1123N.
IntActP18827. 1 interaction.
MINTMINT-5004100.
STRING9606.ENSP00000254351.

PTM databases

PhosphoSiteP18827.

Polymorphism databases

DMDM229463011.

Proteomic databases

PaxDbP18827.
PRIDEP18827.

Protocols and materials databases

DNASU6382.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254351; ENSP00000254351; ENSG00000115884.
ENST00000381150; ENSP00000370542; ENSG00000115884.
GeneID6382.
KEGGhsa:6382.
UCSCuc002rdo.1. human.

Organism-specific databases

CTD6382.
GeneCardsGC02M020400.
H-InvDBHIX0161948.
HGNCHGNC:10658. SDC1.
HPACAB002424.
HPA006185.
MIM186355. gene.
neXtProtNX_P18827.
PharmGKBPA35588.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG86393.
HOGENOMHOG000133092.
HOVERGENHBG017783.
InParanoidP18827.
KOK06257.
OMAPTKQEEF.
OrthoDBEOG79KPG2.
PhylomeDBP18827.
TreeFamTF320463.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP18827.
BgeeP18827.
CleanExHS_SDC1.
GenevestigatorP18827.

Family and domain databases

InterProIPR003585. Neurexin-like.
IPR001050. Syndecan.
IPR027789. Syndecan/Neurexin_dom.
[Graphical view]
PANTHERPTHR10915. PTHR10915. 1 hit.
PfamPF01034. Syndecan. 1 hit.
[Graphical view]
SMARTSM00294. 4.1m. 1 hit.
[Graphical view]
PROSITEPS00964. SYNDECAN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSDC1. human.
GeneWikiSyndecan_1.
GenomeRNAi6382.
NextBio24782.
PMAP-CutDBP18827.
PROP18827.
SOURCESearch...

Entry information

Entry nameSDC1_HUMAN
AccessionPrimary (citable) accession number: P18827
Secondary accession number(s): D6W523 expand/collapse secondary AC list , Q53QV0, Q546D3, Q96HB7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 5, 2009
Last modified: April 16, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries