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VCAN (versican)

Written2010-10Daniel Hernández, Maria José Docampo, Anna Bassols
Departament de Bioquimica i Biologia Molecular, Facultat de Veterinaria, Universitat Autonoma de Barcelona, 08193 Bellaterra, Spain

(Note : for Links provided by Atlas : click)


HGNC Alias symbPG-M
HGNC Alias nameversican proteoglycan
HGNC Previous nameCSPG2
HGNC Previous namechondroitin sulfate proteoglycan 2
LocusID (NCBI) 1462
Atlas_Id 40173
Location 5q14.2  [Link to chromosome band 5q14]
Location_base_pair Starts at 83471744 and ends at 83582302 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping VCAN.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
LGMN (14q32.12)::VCAN (5q14.2)VCAN (5q14.2)::ST6GALNAC2 (17q25.1)


  Adapted from Naso et al., 2004.
Description Versican is encoded by a single gene and is located on chromosome 5q12-14 in the human genome. The human VCAN gene is divided into 15 exons over 90-100 kb. The structure of versican was originally deduced by the analysis of cDNA from a human placental library (Naso et al., 1994). The entire primary structures of versican have been generated from human, murine, bovine and chick cDNA clones. The chick form was originally named PG-M (Shinomura et al., 1993).
Transcription RNA splicing occurs in the two large exons encoding the GAG attachment sites. The region encoded by exon 7 is called GAG alpha, the region encoded by exon 8, GAG beta. Four mRNA transcripts arise from alternative splicing, giving rise to V0, V1, V2 and V3. V0 possesses both exon 7 and exon 8, V1 possesses exon 8 but not exon 7, V2 possesses exon 7 but not exon 8; and V3 possesses neither exon 7 nor exon 8 (Wight, 2002).
The expression of the versican gene (CSPG2) is regulated by a promoter that harbors a typical TATA box and potential binding sites for several transcription factors, including AP1, AP2, CCAAT enhancer protein, TCF-4 and cAMP-responsive element (Naso et al., 1994; Rahmani et al., 2006; Domenzain-Reyna et al., 2009). Regulation of the versican gene through an androgen response element in the proximal promoter has been reported in prostate (Read et al., 2007).


  Versican isoforms
Description Versican belongs to the extracellular matrix chondroitin sulphate proteoglycan family.
The largest versican isoform (V0) consists of 3396 aa. The core protein can be divided into three domains: the globular N-terminal domain (G1), the central domain (G2) where glycosaminoglycan (GAG) chains attach, and the globular C-terminal domain (G3). The G1 domain is composed of an immunoglobulin-like motif, followed by two tandem repeats which bind hyaluronan (HA). The G3 domain contains two EGF-like repeats, a lectin-like subdomain and a complement binding protein (CBP)-like subdomain. The central domain G2 can be alternatively spliced to give rise to the four versican isoforms: V0 (containing both GAG alpha and GAG beta), V1 (containing GAG beta), V2 (containing GAG alpha) and V3, lacking any GAG subdomain (Wight, 2002).
A new alternatively spliced versican isoform, referred to as V4, has been identified and found to be upregulated in human breast cancer (Kischel et al., 2010).

Posttranslational modifications (PTM): the consensus sequence for chondroitin sulphate attachment sites reveals the number of potential GAG attachment sites: the number of GAG chains attached to the protein core depends on the isoforms since the GAG alpha subdomain bears 12-17 chondroitin sulphate (CS) chains, whereas the GAG beta subdomain bears 5-8 CS chains (Ricciardelli et al., 2009).

Expression Versican was initially identified in the culture medium of human IMR-90 lung fibroblasts (Zimmermann and Ruoslahti, 1989).
Versican is highly expressed in tissue compartments undergoing active cell proliferation and migration. V0 and V1 isoforms are highly expressed during embryonic development, and their expression decreases after tissue maturation. In adult tissues, versican is present in the loose connective tissues of various organs and often associated with the elastic fibre network. It is localized in most smooth muscle tissues, in cartilage, in the basal layer of the epidermis, and in blood vessels (Bode-Lesniewska et al., 1996). Versican V2 is abundant in the central nervous system (Schmalfeldt et al., 2000). The V3 isoform has been identified at the mRNA levels but very scarcely at the protein level (Cattaruzza et al., 2002).
Localisation Versican is a component of the extracellular matrix.
Function The name versican comes from versatile, with regard to the diversity of biological actions of this highly interactive molecule that can be attributed both to the amino- and carboxy-terminal domains and to the GAGs side chains attached to the middle portion of the core protein. Versican is involved in the control of cell adhesion, proliferation, migration, apoptosis and in ECM assembly (Wight, 2002; Theocharis, 2008; Ricciardelli et al., 2009). Its domain organization allows modulation of a large variety of cell behaviours through interaction with a wide range of binding partners, including ECM components (HA, type I collagen, tenascin and fibronectin among others), chemokines, and cell surface proteins (CD44, integrin beta1, epidermal growth factor receptor) (Wu et al., 2005).

Versican belongs to the hyalectan family, characterized by its ability to bind hyaluronan. The overall consensus is that versican together with hyaluronan forms a pericellular matrix that modulates cell proliferation, adhesion and migration in conditions such as in development and wound healing cell. Some of these actions have been ascribed to specific domains in the molecule. Thus, overexpression of versican G1 domain can enhance cell proliferation and reduce cell adhesion (Ang et al., 1999; Zhang et al., 1999). G3 domain has also been involved in several processes like cell proliferation and invasion (Zhang et al., 1998; Yang et al., 2003; Zheng et al., 2004; Yee et al., 2007), and GAG chains have been considered partially responsible for the antiadhesive properties of versican (Yamagata and Kimata, 1994; Sakko et al., 2003).

Cell proliferation. Versican is associated with a proliferative cell phenotype and it is often found in tissues showing elevated proliferation such as in development and in a variety of tumours (Wight, 2002; Ricciardelli et al., 2009). Purified versican added to the culture media in a melanoma cell line induces proliferation (Touab et al., 2002). Silencing experiments with siRNA have lead to the same conclusion in vascular smooth muscle cells (Huang et al., 2006) and preadipocytes (Zizola et al., 2007).

Cell adhesion. Versican is an anti-adhesive substrate (Yamagata and Kimata, 1994). The anti-adhesive role of versican has been also shown in melanoma cells (Touab et al., 2002), prostate carcinoma cells (Sakko et al., 2003) or neural crest cells (Dutt et al., 2006). This inhibitory effect on cell adhesion may be mainly due to the presence of the GAG chains that might create a more hydrated extracellular matrix less suitable for cell adhesion.
Nevertheless, the G3 domain of versican has pro-adhesive properties raising the possibility that different breakdown products might differentially affect cell adhesion (Wu et al., 2002).

Cell migration and invasion. Versican can increase cell motility in embryonic as well as tumour cells. This activity may be mostly associated with its antiadhesive activities. Silencing of V0/V1 versican expression reduces cell migration in wound healing assays in smooth muscle cells (Huang et al., 2006), or in prostate cancer cells, where addition of purified versican to the cells caused an increase in the invasion ability (Ricciardelli et al., 2007). In glioma, treatment of the cells with TGF-beta2 caused an increase in cell migration associated to an increase in versican production (Arslan et al., 2007). In the nervous system and in axonal growth, the V2 splice variant inhibits axonal growth and migration (Schmalfeldt et al., 2000).

Apoptosis. The effect of versican on apoptosis is complex and anti- as well as pro-apoptotic functions have been reported. Overexpression of the V1 versican isoform in cultured fibroblasts increases apoptotic resistance, but cells were also sensitized to a wide range of cytotoxic agents (LaPierre et al., 2007).

Cell differentiation and epithelial-mesenchymal transition (EMT). Versican modulates cell differentiation and morphogenesis, since it is involved in EMT interactions and in mesenchymal cell condensation required for organogenesis. V1 (but not V2) has been shown to trigger MET in fibroblasts by inducing a switch from N-cadherin to E-cadherin and subsequent acquirement of epithelioid phenotype. Silencing of endogenous versican prevents condensation and MET in metanephric mesenchyme (Sheng et al., 2006). Versican is highly expressed in the mesenchymal cell condensation area during development of cartilage, heart, hair follicles and kidney, and in vitro evidences show that versican V0 and V1 isoforms are involved in the process of precartilage mesenchymal condensation and subsequent chondrogenesis (Kamiya et al., 2006). The requirement of versican in development is highlighted by the finding that deficiency of versican in a transgenic mouse model is embryonic lethal, due to defects on cardiac formation, limb mesenchymal aggregation and chondrogenesis (Williams et al., 2005).

Others. In neural cells, versican plays an important role in regulating axonal guidance (Perissinotto et al., 2000). It is also an important molecule in inflammatory processes since it is able to interact with immune cell receptors and chemokines (Hirose et al., 2001).

Homology Versican belongs to the hyalectan gene family of proteoglycans that include aggrecan, neurocan and brevican.


Note No missense, regulatory, small and gross deletions and insertions, complex rearrangements, or repeat variations have been described.
In this context, disruption of the versican gene in mouse and chick leads to severe cardiac defects and alterations in chondrogenesis in the hdf (heart defect) mouse. This animal model has lead to the conclusion that normal expression of the VCAN (Cspg2) gene is required for the successful development of the heart and for cartilage differentiation, leading to correct limb chondrogenesis (Mjaatvedt et al., 1998).

Only mutations affecting the splicing of exons 7 and 8 have been described associated to Wagner syndrome, a rare disorder belonging to the group of hereditary vitreoretinal degenerations (Miyamoto et al., 2005; Kloeckener-Gruissem et al., 2006).

Implicated in

Entity Various cancers
Note Versican, specially the large V0 and V1 isoforms, is overproduced by many cancer types of all kind of origins: brain tumours, melanoma, osteosarcoma, breast, prostate, colon, lung, pancreatic, endometrial, oral and ovarian cancers. Versican is expressed by tumour stromal cells as fibroblasts, and also by tumour cells in melanoma, prostate, pancreatic, endometrial and ovarian carcinomas. Versican has a positive effect on cell proliferation, migration and invasion, and exerts a negative effect on cell adhesion. In cancer cells, it is also involved in the control of the epithelial-mesenchymal transition. The expression of particular domains enhances angiogenesis and metastasis in several tumour models (Ricciardelli et al., 2009). Versican has also been involved in metastasis by playing a role in the immune response. Versican acts on macrophages through the Toll-receptor 2 (TLR2) inducing TNF-alpha secretion and provoking lung metastatic growth (Kim et al., 2009).
Prognosis Elevated levels of versican are usually associated with relapse and poor patient outcome in many cancer types, including breast and prostate.
Entity Brain tumours
Disease V2 is the major versican isoform of brain ECM and it is usually decreased in glioma ECM, whereas it is increased in tumour vessels. Since versican is antiadhesive, this may be related to marked local invasivity and rarity of extracranial metastasis of gliomas (Paulus et al., 1996). It has been described that versican in brain tumours originates from fibroblasts and monocytes of tumour stroma (Delpech et al., 1997).
Entity Melanoma
Disease Versican is absent in benign melanocytic nevi, weakly to strongly positive in dysplastic nevi, being proportional to the degree of nuclear atypia, and intensely positive in primary malignant melanomas and metastatic melanomas. Versican is involved in the progression of melanomas and may be a reliable marker for clinical diagnosis (Touab et al., 2002; Touab et al., 2003; Gambichler et al., 2008).
Oncogenesis In melanoma, AP-1 and TCF-4 binding sites are the main regulatory regions directing versican production in undifferentiated cell lines (Domenzain-Reyna et al., 2009).
Entity Breast tumour
Disease Versican is overexpressed in breast carcinoma, and it is specially localized in the proliferating interstitial tissues, and in vascular and perivascular elastic tissues involved in carcinoma invasion (Nara et al., 1997). Relapse in women with node-negative breast cancer is related to the level of versican deposited in peritumoral stroma by mammary fibroblasts (Ricciardelli et al., 2002).
Entity Prostate tumours
Disease Versican is localized to the periacinar and peritumoral fibromuscular stroma in sections of nonmalignant and malignant human prostate tissues. Versican is increased in early-stage prostate cancer. Patients with low versican concentration had significantly better progression-free survival than patients with high levels of versican (Ricciardelli et al., 1998). Versican is also overexpressed in benign prostate hyperplasia (BPH) (True et al., 2009).
Entity Colon tumours
Disease DNA isolated from human colon carcinoma tissue exhibits a selective hypomethylation of versican gene, three times lower than that found in either normal colon or ulcerative colitis tissues (Adany and Iozzo, 1990). Colon adenocarcinoma is characterized by a remarkable increase in the concentration of versican, which is significantly modified at the post-translational level, i.e. the type, length and the sulphation pattern of the GAG chains (Theocharis, 2002).
Oncogenesis Hypomethylation of the VCAN gene occurs in benign and malignant colon cancer compared to normal colon. These changes in methylation may occur prior to malignant transformation and may be associated to increased versican levels in colon cancer.
Entity Lung carcinoma
Disease Increased stromal versican is associated with tumour recurrence, higher tumour stage, and lymph node metastases (Pirinen et al., 2005).
Entity Pancreatic tumours
Disease Versican presents a great increase (27-fold) in comparison to normal pancreas, which may be closely associated with the growth and aggressiveness of this carcinoma. Significant specific post-translational modifications were also observed regarding the type, hydrodynamic size, sulphation pattern and extent of uronate epimerization of the GAG chains (Skandalis et al., 2006).
Entity Endometrial tumours
Disease Stromal versican expression was significantly higher in the advanced-stage and high-grade cancers, lymph node metastasis and ovarian metastasis. Epithelial versican expression was significantly higher in patients with lymph node metastasis and lymph-vascular space involvement. The disease-free survival and overall survival rates of patients exhibiting high stromal versican expression were significantly lower than those of patients exhibiting low stromal versican expression (Kodama et al., 2007).
Entity Ovarian tumours
Disease Elevated levels of versican have been associated with a poor prognosis of ovarian cancers (Ricciardelli and Rodgers, 2006). Ovarian clear cell carcinoma (OCCC) microarray signature contains versican, which is in part in part epigenetically regulated, as it was hypomethylated in OCCC cell lines (Yamaguchi et al., 2010). VCAN overexpression is associated with increased microvessel density (MVD) and invasion potential, which may lead to poorer overall and progression-free survival and platinum resistance (Ghosh et al., 2010).
Entity Oral carcinoma
Disease High stromal versican expression predicts unfavourable outcome in oral squamous cell carcinoma (Pukkila et al., 2007).
Entity Lymphoma
Disease Tumoral environment induces aberrant expression of versican in EL4 lymphoma cells (Rottiers et al., 1998).
Entity Atherosclerosis
Disease Versican accumulates in atherosclerotic lesions and restenosis. Versican is also prominent at the borders of lipid-filled necrotic cores and at the plaque-thrombus interface of the atherosclerotic lesion, suggesting roles in lipid accumulation, inflammation, and thrombosis (Wight and Merrilees, 2004).


Altered methylation of versican proteoglycan gene in human colon carcinoma.
Adany R, Iozzo RV.
Biochem Biophys Res Commun. 1990 Sep 28;171(3):1402-13.
PMID 2222452
Versican enhances locomotion of astrocytoma cells and reduces cell adhesion through its G1 domain.
Ang LC, Zhang Y, Cao L, Yang BL, Young B, Kiani C, Lee V, Allan K, Yang BB.
J Neuropathol Exp Neurol. 1999 Jun;58(6):597-605.
PMID 10374750
The role of versican isoforms V0/V1 in glioma migration mediated by transforming growth factor-beta2.
Arslan F, Bosserhoff AK, Nickl-Jockschat T, Doerfelt A, Bogdahn U, Hau P.
Br J Cancer. 2007 May 21;96(10):1560-8. Epub 2007 Apr 24.
PMID 17453002
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PMID 8601689
Distribution of PG-M/versican variants in human tissues and de novo expression of isoform V3 upon endothelial cell activation, migration, and neoangiogenesis in vitro.
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PMID 12221092
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PMID 9378555
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PMID 19269971
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PMID 16964367
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PMID 19073385
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PMID 20619446
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PMID 11083865
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PMID 16385080
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PMID 16257955
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PMID 19122641
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PMID 19662655
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PMID 16636652
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PMID 17065588
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Cancer Res. 2007 May 15;67(10):4742-50.
PMID 17510402
Identification of a novel splice site mutation of the CSPG2 gene in a Japanese family with Wagner syndrome.
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PMID 16043844
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PMID 9758703
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PMID 9088942
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PMID 7528742
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PMID 8627343
Avian neural crest cell migration is diversely regulated by the two major hyaluronan-binding proteoglycans PG-M/versican and aggrecan.
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PMID 10851128
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PMID 15712181
High stromal versican expression predicts unfavourable outcome in oral squamous cell carcinoma.
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PMID 16731595
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PMID 16845893
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PMID 17728259
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PMID 19160015
Differentiation of EL4 lymphoma cells by tumoral environment is associated with inappropriate expression of the large chondroitin sulfate proteoglycan PG-M and the tumor-associated antigen HTgp-175.
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PMID 9797141
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PMID 12941795
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PMID 10671370
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PMID 16452631
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PMID 8314802
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PMID 16730906
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PMID 18661349
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PMID 12710131
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PMID 11839575
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PMID 18819099
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PMID 15142969
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PMID 12231358
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PMID 16039617
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PMID 20062075
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PMID 14572881
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PMID 17662123
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PMID 10733339
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PMID 2583089
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PMID 17513099


This paper should be referenced as such :
Hernandez, D ; Docampo, MJ ; Bassols, A
VCAN (versican)
Atlas Genet Cytogenet Oncol Haematol. 2011;15(6):520-526.
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HGNC (Hugo)VCAN   2464
Entrez_Gene (NCBI)VCAN    versican
AliasesCSPG2; ERVR; GHAP; PG-M; 
GeneCards (Weizmann)VCAN
Ensembl hg19 (Hinxton)ENSG00000038427 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000038427 [Gene_View]  ENSG00000038427 [Sequence]  chr5:83471744-83582302 [Contig_View]  VCAN [Vega]
ICGC DataPortalENSG00000038427
Genatlas (Paris)VCAN
SOURCE (Princeton)VCAN
Genetics Home Reference (NIH)VCAN
Genomic and cartography
GoldenPath hg38 (UCSC)VCAN  -     chr5:83471744-83582302 +  5q14.2-q14.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)VCAN  -     5q14.2-q14.3   [Description]    (hg19-Feb_2009)
GoldenPathVCAN - 5q14.2-q14.3 [CytoView hg19]  VCAN - 5q14.2-q14.3 [CytoView hg38]
Genome Data Viewer NCBIVCAN [Mapview hg19]  
OMIM118661   143200   
Gene and transcription
Genbank (Entrez)AA320958 AA426499 AA478645 AB209491 AF084545
RefSeq transcript (Entrez)NM_001126336 NM_001164097 NM_001164098 NM_004385
Consensus coding sequences : CCDS (NCBI)VCAN
Gene ExpressionVCAN [ NCBI-GEO ]   VCAN [ EBI - ARRAY_EXPRESS ]   VCAN [ SEEK ]   VCAN [ MEM ]
Gene Expression Viewer (FireBrowse)VCAN [ Firebrowse - Broad ]
GenevisibleExpression of VCAN in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)1462
GTEX Portal (Tissue expression)VCAN
Human Protein AtlasENSG00000038427-VCAN [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP13611   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP13611  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP13611
Domaine pattern : Prosite (Expaxy)ASX_HYDROXYL (PS00010)    C_TYPE_LECTIN_1 (PS00615)    C_TYPE_LECTIN_2 (PS50041)    EGF_1 (PS00022)    EGF_2 (PS01186)    EGF_3 (PS50026)    EGF_CA (PS01187)    IG_LIKE (PS50835)    LINK_1 (PS01241)    LINK_2 (PS50963)    SUSHI (PS50923)   
Domains : Interpro (EBI)C-type_lectin-like    C-type_lectin-like/link_sf    C-type_lectin_CS    CSPG_CTLD    CTDL_fold    EGF-like_Ca-bd_dom    EGF-like_dom    EGF-type_Asp/Asn_hydroxyl_site    EGF_Ca-bd_CS    Ig-like_dom    Ig-like_dom_sf    Ig-like_fold    Ig_sub    Ig_V-set    Link_dom    Sushi/SCR/CCP_sf    Sushi_SCR_CCP_dom   
Domain families : Pfam (Sanger)EGF (PF00008)    Lectin_C (PF00059)    Sushi (PF00084)    V-set (PF07686)    Xlink (PF00193)   
Domain families : Pfam (NCBI)pfam00008    pfam00059    pfam00084    pfam07686    pfam00193   
Domain families : Smart (EMBL)CCP (SM00032)  CLECT (SM00034)  EGF (SM00181)  EGF_CA (SM00179)  IG (SM00409)  LINK (SM00445)  
Conserved Domain (NCBI)VCAN
AlphaFold pdb e-kbP13611   
Human Protein Atlas [tissue]ENSG00000038427-VCAN [tissue]
Protein Interaction databases
IntAct (EBI)P13611
Ontologies - Pathways
Ontology : AmiGOskeletal system development  osteoblast differentiation  photoreceptor outer segment  calcium ion binding  protein binding  glycosaminoglycan binding  hyaluronic acid binding  extracellular region  extracellular region  extracellular space  endoplasmic reticulum lumen  Golgi lumen  cell adhesion  multicellular organism development  central nervous system development  cell recognition  membrane  extracellular matrix structural constituent conferring compression resistance  extracellular matrix structural constituent conferring compression resistance  extracellular matrix organization  chondroitin sulfate biosynthetic process  chondroitin sulfate catabolic process  dermatan sulfate biosynthetic process  carbohydrate binding  extracellular matrix  interphotoreceptor matrix  lysosomal lumen  post-translational protein modification  cellular protein metabolic process  collagen-containing extracellular matrix  collagen-containing extracellular matrix  collagen-containing extracellular matrix  
Ontology : EGO-EBIskeletal system development  osteoblast differentiation  photoreceptor outer segment  calcium ion binding  protein binding  glycosaminoglycan binding  hyaluronic acid binding  extracellular region  extracellular region  extracellular space  endoplasmic reticulum lumen  Golgi lumen  cell adhesion  multicellular organism development  central nervous system development  cell recognition  membrane  extracellular matrix structural constituent conferring compression resistance  extracellular matrix structural constituent conferring compression resistance  extracellular matrix organization  chondroitin sulfate biosynthetic process  chondroitin sulfate catabolic process  dermatan sulfate biosynthetic process  carbohydrate binding  extracellular matrix  interphotoreceptor matrix  lysosomal lumen  post-translational protein modification  cellular protein metabolic process  collagen-containing extracellular matrix  collagen-containing extracellular matrix  collagen-containing extracellular matrix  
Pathways : KEGGCell adhesion molecules (CAMs)   
REACTOMEP13611 [protein]
REACTOME PathwaysR-HSA-8957275 [pathway]   
NDEx NetworkVCAN
Atlas of Cancer Signalling NetworkVCAN
Wikipedia pathwaysVCAN
Orthology - Evolution
GeneTree (enSembl)ENSG00000038427
Phylogenetic Trees/Animal Genes : TreeFamVCAN
Homologs : HomoloGeneVCAN
Homology/Alignments : Family Browser (UCSC)VCAN
Gene fusions - Rearrangements
Fusion : QuiverVCAN
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerVCAN [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)VCAN
Exome Variant ServerVCAN
GNOMAD BrowserENSG00000038427
Varsome BrowserVCAN
ACMGVCAN variants
Genomic Variants (DGV)VCAN [DGVbeta]
DECIPHERVCAN [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisVCAN 
ICGC Data PortalVCAN 
TCGA Data PortalVCAN 
Broad Tumor PortalVCAN
OASIS PortalVCAN [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICVCAN  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DVCAN
Mutations and Diseases : HGMDVCAN
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)VCAN
DoCM (Curated mutations)VCAN
CIViC (Clinical Interpretations of Variants in Cancer)VCAN
NCG (London)VCAN
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
OMIM118661    143200   
Genetic Testing Registry VCAN
NextProtP13611 [Medical]
Target ValidationVCAN
Huge Navigator VCAN [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDVCAN
Pharm GKB GenePA162408788
Clinical trialVCAN
DataMed IndexVCAN
PubMed196 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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indexed on : Fri Oct 8 21:30:33 CEST 2021

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