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SDC1 (syndecan 1)

Written2008-03Anurag Purushothaman, Ralph D Sanderson
Dept. of Pathology, University of Alabama at Birmingham, 814 SHEL, 1530 Third Ave. S., Birmingham, AL 35294, USA

(Note : for Links provided by Atlas : click)


Alias (NCBI)CD138
HGNC (Hugo) SDC1
HGNC Alias symbCD138
HGNC Alias namesyndecan proteoglycan 1
HGNC Previous nameSDC
LocusID (NCBI) 6382
Atlas_Id 42223
Location 2p24.1  [Link to chromosome band 2p24]
Location_base_pair Starts at 20200797 and ends at 20225130 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping SDC1.png]
Local_order Human syndecan1 gene is localized to 2p23-24, just centromeric to the N-myc gene at 2p24.1.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
ERVV-2 (19q13.41)::SDC1 (2p24.1)LAPTM4A (2p24.1)::SDC1 (2p24.1)RAB10 (2p23.3)::SDC1 (2p24.1)
SDC1 (2p24.1)::PROS1 (3q11.1)SDC1 (2p24.1)::PRRC2B (9q34.13)TRIM29 (11q23.3)::SDC1 (2p24.1)
Note Syndecan 1, a cell surface heparan sulfate proteoglycan, is one of the four members of the syndecan family.


  Genomic structure of the two alternative transcript variants of SDC1. Black boxes indicate exons and red boxes indicate untranslated exons.
Description The SDC1 gene contains 9 exons and spans 24, 6366 bases (start 20,264,039 bp from pter to end 20,288,675) oriented at the minus strand.
Transcription While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. These two represent the major variants of this gene and encode the same protein. Variant 1 (NM_001006946) represents the longer transcript and variant 2 (NM_002997) differs in the 5' UTR compared to variant 1.
Variant 1: exons-6; transcript length-3309 bp and translation length -310 residues.
Variant 2: exons-5; transcript length-3217 bp and translation length -310 residues.
Pseudogene None


  Schematic representation of the core protein structure of SDC1. C1 and C2 represent highly conserved regions and V represents the central variable region. Lines at amino acids 37, 45 and 47 represents heparan sulfate chain attachment sites and lines at amino acids 210 and 220 represents chondroitin sulfate chain attachment sites.
Description 310 amino acids; 32477 Da; charge -19.5; isoelectric point 4.2618.
The core protein contains 3 domains, an ectodomain (extracellular domain), transmembrane domain and cytoplasmic domain. The ectodomain contains a cleavable amino terminal single peptide and the glycosaminoglycan attachment sites. There are 3 highly conserved serine-glycine sites for heparan sulfate attachment (amino acids 37,45 and 47) near the N terminal of the core protein and 2 highly conserved serine-glycine sites for chondroitin sulfate attachment ( amino acids 210 and 220), adjacent to the cell membrane. Shedding of the ectodomain occurs via protease sensitive sites near the plasma membrane. The transmembrane domain, which is highly conserved among the syndecan family members, contains an unusual motif of glycine/alanine that aligns on one face of the domain in the outer membrane leaflet. The non-catalytic COOH-terminal, cytoplasmic domain, which is relatively short (30 amino acids) contains 2 highly conserved regions (C1 and C2) which are identical in each of the 4 syndecan family members (the exception being a conservative substitution of arginine for lysine in syndecan 2). These flank a central variable region (V) that is distant for each family member. The sequence for variable domain (V) for SDC1 is SLEEPKQANGGAYQKPTKQE. The cytoplasmic domain of SDC1 is required for linking the molecule to the cytoskeleton and this interaction is dependent on a tyrosine residue that is conserved among all known syndecan family sequences. The cytoplasmic V region plays critical role in lamellipodial spreading, actin bundling and cell migration.
Expression SDC1 is expressed predominantly on epithelial cells but is also found on distinct stages of differentiation of normal lymphoid cells (pre-B), mesenchymal cells during development and in mature plasma cells.
Localisation Membrane; Single-pass type I membrane protein.
Function The syndecan-1 proteoglycan regulates cell proliferation, cell migration, cell signaling, cytoskeletal organization and mediates both cell-cell and cell-extracellular matrix interactions. Additionally, via its heparan sulfate chains, it binds a wide range of bioactive molecules (e.g., growth factors, chemokines) that regulate cell behaviors important in normal and pathological processes. For example, it can function as trans HIV receptors via binding of HIV-1 gp120 to the syndecan heparan sulfate chains and also serves as a primary receptor for natural HPV infection of keratinocytes. SDC1 is required for Wnt-1 - induced mammary tumorigenesis and can function as either tumor suppressor or tumor promoter depending on tumor type and specific location of the proteoglycan (either cell surface or shed into the microenvironment). Core proteins also have functions independent of the heparan sulfate chains. The cytoplasmic domains can transmit signals and they also bind to anchoring molecules including PDZ family members. The extracellular domains bear the attached heparan sulfate chains but also interact with, and regulate, other cell adhesion molecules and cell surface receptors independent of their heparan sulfate chains. It was recently demonstrated that a domain within the syndecan-1 core protein is required for activation of alphaV/beta3 and alphaV/beta5 integrins and mutational analysis of SDC1 has identified a stretch of 5 hydrophobic amino acids, AVAAV (amino acids 222-226), which are critical for the SDC1 mediated inhibition of tumor cell invasion.
Homology Belongs to the syndecan family; four members, syndecan- 1, syndecan-2, syndecan-3 and syndecan-4 , have been identified in mammalians. SDC1 orthologs are found in mouse, rat, dog, chimpanzee, guinea pig, Chinese hamster, Hedgehog, cat, Pika, Platypus, Bushbaby, Tree Shrew, and chicken. The extracellular domains of human and mouse SDC1 show 70% sequence identity while the transmembrane domain and cytoplasmic domain show 96 % and 100% identity respectively (see MapViewer).


Note No mutations in the SDC1 gene have been reported.

Implicated in

Entity Multiple Myelomas
Note Syndecan-1 (CD138) is the dominant heparan sulfate proteoglycan expressed on the surface of myeloma cells both in bone marrow and in peripheral blood, and is used as a standard marker by many labs for identification and purification of myeloma cells. On normal cells, syndecan-1 is not expressed on mature B lymphocytes but becomes present at the onset of plasma cell differentiation.
Disease Myeloma resides predominantly within the bone and is marked by fatigue, intractable bone pain, renal failure and recurrent infections. These effects result from high tumor burden with accompanying cytokine dysregulation, osteolytic bone disease and from the deposition in some patients of high levels of immunoglobulin light chain. Cell surface SDC1 mediates adhesion of myeloma cells to collagen, inhibits invasion through collagen gels and also can mediate myeloma cell-cell adhesion. In contrast, shed syndecan-1 actively promotes myeloma tumor growth and metastasis.
Prognosis Shedding of syndecan-1 from the myeloma cell surface occurs actively via proteolytic sheddases and a high level of syndecan-1 in the serum is an independent predictor of poor prognosis in myeloma. Patients with high serum SDC1 had a median survival of 20 months, whereas those with a low serum SDC1 had a median survival of 44 months.
Entity Haematological malignancies
Note SDC1 (CD138) is detectable on B-cell chronic lymphocytic leukemia (B-CLL) cells, acute lymphoblastic leukemia (ALL) cells and acute myeloblastic leukemia (AML) cells.
Disease The serum levels of syndecan-1 were elevated in patients with B-cell chronic lymphocytic leukemia (CLL) and Hodgkin disease (HL).
Prognosis Serum CD138 level is higher in early stage B-CLL patients than in healthy controls, correlates negatively with peripheral blood lymphocyte count, and is higher in patients with more indolent disease course. Serum CD138 levels increase in early stage B-CLL patients and may have a positive prognostic value as to the dynamics of the disease. The serum levels of syndecan-1 were elevated in patients with HL but did not correlate with markers of tumor burden and prognosis, including serum interleukin-10 and soluble CD30.
Entity Breast tumors
Note Syndecan-1 is expressed at high levels in a significant percentage of breast carcinomas and is related to an aggressive phenotype and poor prognosis. High syndecan-1 expression contributes to the identification of a patient population at particularly high risk of relapse and death.
Disease High syndecan-1 expression in breast tumors is associated with an aggressive phenotype characterized by larger tumor size, higher tumor grade, higher mitotic count, negative steroid status, and over expression of c-erbB-2 and p53.
Prognosis In breast cancer, increased expression of SDC1 correlates with an unfavorable prognosis and poor response to chemotherapy.
Entity Pancreatic cancer
Note Syndecan-1 is upregulated in the stroma of pancreatic cancer. Pancreatic cancer tissues express significantly higher levels of syndecan-1 mRNA and protein. SDC1 over expression is an early event in pancreatic carcinogenesis.
Disease Carcinoma of the pancreas is the 4th leading cause of cancer death in Western countries, with a very short patient survival after diagnosis. Pancreatic cancers over-express a variety of mitogenic growth factors and their receptors and they exhibit tumor-suppressor gene mutations such as p53, p16 and Smad4 and proto-oncogene mutations such as k-ras.
Prognosis Patients with stromal syndecan-1-positive pancreatic cancer had a worse outcome than patients with stromal syndecan-1 negative tumors. Stromal expression of syndecan-1 seems to be an independent prognostic factor in pancreatic cancer.
Entity Gastric cancer
Note Stromal syndecan-1 expression correlates with deep tumor penetration and larger tumor size. Positive stromal syndecan-1 immunoreactivity correlated with decreased epithelial syndecan-1 expression.
Disease Risk factors for gastric cancer include: Helicobacter pylori gastric infection, advanced age, male gender, diet including dry salted foods, atrophic gastritis, pernicious anemia, cigarette smoking, Menetrier's disease, and familial polyposis. The prognosis of patients with gastric cancer is related to tumor extent and includes both nodal involvement and direct tumor extension beyond the gastric wall.
Prognosis High expression of syndecan-1 in the stroma in gastric carcinoma is a tumor characteristic associated with a poor prognosis independent of tumor size. Patients with low epithelial syndecan-1 expression in cancer cells had worse overall survival than patients with strong epithelial syndecan-1 staining. Stromal syndecan-1-positive patients had a worse outcome than patients with syndecan-1 negative stroma.
Entity Prostrate cancer
Note Expression of syndecan-1 is associated with established features of biologically aggressive prostate cancer including high PSA levels and lymph node metastases.
Disease Prostate cancer is the most common noncutaneous malignancy affecting males in the USA. The disease course is variable and about a third of patients eventually fail treatment, as evidenced by a detectable and rising PSA levels.
Prognosis Patients with features of aggressive progression were more likely to exhibit increased syndecan-1 expression compared with those with features of non aggressive progression.
Entity Endometrial Cancer
Note Stromal syndecan-1 expression is elevated in high-grade endometrial cancer.
Disease Endometrial cancer is the most common disease among gynecological malignancies and remains a major health concern worldwide.
Prognosis Loss of epithelial syndecan-1 expression and induction of stromal syndecan-1 expression are associated with reduced survival outcomes in patients with endometrial cancer. Stromal syndecan-1 expression serves as an indicator of poor prognosis in patients with endometrial cancer.
Entity Ovary carcinoma
Note Syndecan-1 is present in the epithelial cells, cancer cells, and stromal cells of benign, borderline, and malignant ovarian tumor sections. Stromal syndecan-1 expression is observed in the most invasive areas of ovarian cancer.
Disease Epithelial carcinoma of the ovary is one of the most common gynecologic malignancies. The most important risk factor for ovarian cancer is a family history of a first-degree relative (mother, daughter, or sister) with the disease.
Prognosis Stromal syndecan-1 expression is associated with decreased survival in patients with ovarian carcinoma.
Entity Lung cancers
Note Serum syndecan-1 is a powerful prognostic factor in lung cancer. Lung cancer patients have high serum syndecan 1. High levels of circulating syndecan-1 also in part reflect the presence of a large tumor mass and are associated with advanced cancer.
Disease Lung cancers are neuroendocrine lung tumors (small cell lung carcinomas, carcinoids, large cell neuroendocrine carcinomas) or non neuroendocrine lung tumors (squamous carcinomas, adenocarcinomas, large cell carcinomas).
Prognosis High serum syndecan-1 levels at diagnosis are associated with an advanced stage and poor outcome in lung cancer.


Localization of gene for human syndecan, an integral membrane proteoglycan and a matrix receptor, to chromosome 2.
Ala-Kapee M, Nevanlinna H, Mali M, Jalkanen M, Schroder J.
Somat Cell Mol Genet. 1990 Sep;16(5):501-5.
PMID 2173154
Syndecan-1 is required for Wnt-1-induced mammary tumorigenesis in mice.
Alexander CM, Reichsman F, Hinkes MT, Lincecum J, Becker KA, Cumberledge S, Bernfield M.
Nat Genet. 2000 Jul;25(3):329-32.Click here to read
PMID 10888884
Syndecan-1 expression is regulated in an isoform-specific manner by the farnesoid-X receptor.
Anisfeld AM, Kast-Woelbern HR, Meyer ME, Jones SA, Zhang Y, Williams KJ, Willson T, Edwards PA.
J Biol Chem. 2003 May 30;278(22):20420-8. Epub 2003 Mar 26.
PMID 12660231
High syndecan-1 expression in breast carcinoma is related to an aggressive phenotype and to poorer prognosis.
Barbareschi M, Maisonneuve P, Aldovini D, Cangi MG, Pecciarini L, Angelo Mauri F, Veronese S, Caffo O, Lucenti A, Palma PD, Galligioni E, Doglioni C.
Cancer. 2003 Aug 1;98(3):474-83.
PMID 12879463
Syndecan-1-mediated cell spreading requires signaling by alphavbeta3 integrins in human breast carcinoma cells.
Beauvais DM, Rapraeger AC.
Exp Cell Res. 2003 Jun 10;286(2):219-32.
PMID 12749851
Functions of cell surface heparan sulfate proteoglycans.
Bernfield M, Gotte M, Park PW, Reizes O, Fitzgerald ML, Lincecum J, Zako M.
Annu Rev Biochem. 1999;68:729-77.
PMID 10872465
The cytoplasmic domain of syndecan-1 is required for cytoskeleton association but not detergent insolubility. Identification of essential cytoplasmic domain residues.
Carey DJ, Bendt KM, Stahl RC.
J Biol Chem. 1996 Jun 21;271(25):15253-60.
PMID 8662979
Functional role of syndecan-1 cytoplasmic V region in lamellipodial spreading, actin bundling, and cell migration.
Chakravarti R, Sapountzi V, Adams JC.
Mol Biol Cell. 2005 Aug;16(8):3678-91. Epub 2005 Jun 1.
PMID 15930135
Syndecan-1 (CD 138) in myeloma and lymphoid malignancies: a multifunctional regulator of cell behavior within the tumor microenvironment.
Dhodapkar MV, Sanderson RD.
Leuk Lymphoma. 1999 Jun;34(1-2):35-43.
PMID 10350330
Prognostic significance of syndecan-1 expression in human endometrial cancer.
Hasengaowa , Kodama J, Kusumoto T, Shinyo Y, Seki N, Hiramatsu Y.
Ann Oncol. 2005 Jul;16(7):1109-15. Epub 2005 Apr 22.
PMID 15851381
Syndecan-1 expression--a novel prognostic marker in pancreatic cancer.
Juuti A, Nordling S, Lundin J, Louhimo J, Haglund C.
Oncology. 2005;68(2-3):97-106. Epub 2005 May 9.
PMID 15886501
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. 1997 Mar;99(3):295-7.
PMID 9050911
Identification of an invasion regulatory domain within the core protein of syndecan-1.
Langford JK, Yang Y, Kieber-Emmons T, Sanderson RD.
J Biol Chem. 2005 Feb 4;280(5):3467-73. Epub 2004 Nov 24.
PMID 15563454
Differential expression of cell surface heparan sulfate proteoglycans in human mammary epithelial cells and lung fibroblasts.
Lories V, Cassiman JJ, Van den Berghe H, David G.
J Biol Chem. 1992 Jan 15;267(2):1116-22.
PMID 1339431
Induction of syndecan-1 expression in stromal fibroblasts promotes proliferation of human breast cancer cells.
Maeda T, Alexander CM, Friedl A.
Cancer Res. 2004 Jan 15;64(2):612-21.
PMID 14744776
Sequence of human syndecan indicates a novel gene family of integral membrane proteoglycan.
Mali M, Jaakkola P, Arvilommi AM, Jalkanen M.
J Biol Chem. 1990 Apr 25;265(12):6884-9.
PMID 2324102
Shift of syndecan-1 expression from epithelial to stromal cells during progression of solid tumours.
Mennerich D, Vogel A, Klaman I, Dahl E, Lichtner RB, Rosenthal A, Pohlenz HD, Thierauch KH, Sommer A.
Eur J Cancer. 2004 Jun;40(9):1373-82.
PMID 15177497
Serum levels of syndecan-1 in B-cell chronic lymphocytic leukemia: correlation with the extent of angiogenesis and disease-progression risk in early disease.
Molica S, Vitelli G, Mirabelli R, Digiesu G, Giannarelli D, Cuneo A, Ribatti D, Vacca A.
Leuk Lymphoma. 2006 Jun;47(6):1034-40.
PMID 16840194
Expression of extracellular matrix proteins in ovarian serous tumors.
Salani R, Neuberger I, Kurman RJ, Bristow RE, Chang HW, Wang TL, Shih IeM.
Int J Gynecol Pathol. 2007 Apr;26(2):141-6.
PMID 17413980
Syndecan-1: a dynamic regulator of the myeloma microenvironment.
Sanderson RD, Yang Y.
Clin Exp Metastasis. 2008;25(2):149-59. Epub 2007 Nov 20.
PMID 18027090
Different heparan sulfate proteoglycans serve as cellular receptors for human papillomaviruses.
Shafti-Keramat S, Handisurya A, Kriehuber E, Meneguzzi G, Slupetzky K, Kirnbauer R.
J Virol. 2003 Dec;77(24):13125-35.
PMID 14645569
Prognostic value of syndecan-1 expression in patients treated with radical prostatectomy.
Shariat SF, Svatek RS, Kabbani W, Walz J, Lotan Y, Karakiewicz PI, Roehrborn CG.
BJU Int. 2008 Jan;101(2):232-7. Epub 2007 Sep 13.
PMID 17868422
Soluble syndecan-1 promotes growth of myeloma tumors in vivo.
Yang Y, Yaccoby S, Liu W, Langford JK, Pumphrey CY, Theus A, Epstein J, Sanderson RD.
Blood. 2002 Jul 15;100(2):610-7.
PMID 12091355


This paper should be referenced as such :
Purushothaman, A ; Sanderson, RD
SDC1 (syndecan 1)
Atlas Genet Cytogenet Oncol Haematol. 2009;13(1):57-61.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)SDC1   10658
Atlas Explorer : (Salamanque)SDC1
Entrez_Gene (NCBI)SDC1    syndecan 1
AliasesCD138; SDC; SYND1; syndecan
GeneCards (Weizmann)SDC1
Ensembl hg19 (Hinxton)ENSG00000115884 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000115884 [Gene_View]  ENSG00000115884 [Sequence]  chr2:20200797-20225130 [Contig_View]  SDC1 [Vega]
ICGC DataPortalENSG00000115884
TCGA cBioPortalSDC1
AceView (NCBI)SDC1
Genatlas (Paris)SDC1
SOURCE (Princeton)SDC1
Genetics Home Reference (NIH)SDC1
Genomic and cartography
GoldenPath hg38 (UCSC)SDC1  -     chr2:20200797-20225130 -  2p24.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)SDC1  -     2p24.1   [Description]    (hg19-Feb_2009)
GoldenPathSDC1 - 2p24.1 [CytoView hg19]  SDC1 - 2p24.1 [CytoView hg38]
Genome Data Viewer NCBISDC1 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AJ551176 AK222739 AK299385 AK307313 AK311409
RefSeq transcript (Entrez)NM_001006946 NM_002997
Consensus coding sequences : CCDS (NCBI)SDC1
Gene ExpressionSDC1 [ NCBI-GEO ]   SDC1 [ EBI - ARRAY_EXPRESS ]   SDC1 [ SEEK ]   SDC1 [ MEM ]
Gene Expression Viewer (FireBrowse)SDC1 [ Firebrowse - Broad ]
GenevisibleExpression of SDC1 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)6382
GTEX Portal (Tissue expression)SDC1
Human Protein AtlasENSG00000115884-SDC1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP18827   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP18827  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP18827
Domaine pattern : Prosite (Expaxy)SYNDECAN (PS00964)   
Domains : Interpro (EBI)Neurexin-like    Syndecan    Syndecan-1    Syndecan/Neurexin_dom    Syndecan_CS   
Domain families : Pfam (Sanger)Syndecan (PF01034)   
Domain families : Pfam (NCBI)pfam01034   
Domain families : Smart (EMBL)4.1m (SM00294)  
Conserved Domain (NCBI)SDC1
PDB (RSDB)4GVC    4GVD    6EJE   
PDB Europe4GVC    4GVD    6EJE   
PDB (PDBSum)4GVC    4GVD    6EJE   
PDB (IMB)4GVC    4GVD    6EJE   
Structural Biology KnowledgeBase4GVC    4GVD    6EJE   
SCOP (Structural Classification of Proteins)4GVC    4GVD    6EJE   
CATH (Classification of proteins structures)4GVC    4GVD    6EJE   
AlphaFold pdb e-kbP18827   
Human Protein Atlas [tissue]ENSG00000115884-SDC1 [tissue]
Protein Interaction databases
IntAct (EBI)P18827
Complex Portal (EBI)P18827 CPX-3282 Syndecan-1-syntenin-1-ALIX complex
Ontologies - Pathways
Ontology : AmiGOretinoid metabolic process  ureteric bud development  protein binding  Golgi lumen  plasma membrane  integral component of plasma membrane  glycosaminoglycan biosynthetic process  glycosaminoglycan catabolic process  inflammatory response  protein C-terminus binding  response to toxic substance  external side of plasma membrane  cell surface  cell surface  cell migration  cytokine-mediated signaling pathway  protein-containing complex  wound healing  odontogenesis  response to hydrogen peroxide  identical protein binding  lysosomal lumen  myoblast development  leukocyte migration  response to glucocorticoid  response to cAMP  response to calcium ion  striated muscle cell development  Sertoli cell development  canonical Wnt signaling pathway  extracellular exosome  positive regulation of exosomal secretion  positive regulation of extracellular exosome assembly  
Ontology : EGO-EBIretinoid metabolic process  ureteric bud development  protein binding  Golgi lumen  plasma membrane  integral component of plasma membrane  glycosaminoglycan biosynthetic process  glycosaminoglycan catabolic process  inflammatory response  protein C-terminus binding  response to toxic substance  external side of plasma membrane  cell surface  cell surface  cell migration  cytokine-mediated signaling pathway  protein-containing complex  wound healing  odontogenesis  response to hydrogen peroxide  identical protein binding  lysosomal lumen  myoblast development  leukocyte migration  response to glucocorticoid  response to cAMP  response to calcium ion  striated muscle cell development  Sertoli cell development  canonical Wnt signaling pathway  extracellular exosome  positive regulation of exosomal secretion  positive regulation of extracellular exosome assembly  
Pathways : KEGGECM-receptor interaction    Cell adhesion molecules (CAMs)    Malaria    Proteoglycans in cancer   
REACTOMEP18827 [protein]
REACTOME PathwaysR-HSA-975634 [pathway]   
NDEx NetworkSDC1
Atlas of Cancer Signalling NetworkSDC1
Wikipedia pathwaysSDC1
Orthology - Evolution
GeneTree (enSembl)ENSG00000115884
Phylogenetic Trees/Animal Genes : TreeFamSDC1
Homologs : HomoloGeneSDC1
Homology/Alignments : Family Browser (UCSC)SDC1
Gene fusions - Rearrangements
Fusion : MitelmanLAPTM4A::SDC1 [2p24.1/2p24.1]  
Fusion : MitelmanRAB10::SDC1 [2p23.3/2p24.1]  
Fusion : QuiverSDC1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerSDC1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)SDC1
Exome Variant ServerSDC1
GNOMAD BrowserENSG00000115884
Varsome BrowserSDC1
ACMGSDC1 variants
Genomic Variants (DGV)SDC1 [DGVbeta]
DECIPHERSDC1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisSDC1 
ICGC Data PortalSDC1 
TCGA Data PortalSDC1 
Broad Tumor PortalSDC1
OASIS PortalSDC1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICSDC1  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DSDC1
Mutations and Diseases : HGMDSDC1
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)SDC1
DoCM (Curated mutations)SDC1
CIViC (Clinical Interpretations of Variants in Cancer)SDC1
NCG (London)SDC1
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry SDC1
NextProtP18827 [Medical]
Target ValidationSDC1
Huge Navigator SDC1 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDSDC1
Pharm GKB GenePA35588
Clinical trialSDC1
DataMed IndexSDC1
PubMed372 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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