DVL1

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DVL1
Protein DVL1 PDB 1fsh.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases DVL1, DVL, DVL1L1, DVL1P1, DRS2, dishevelled segment polarity protein 1
External IDs MGI: 94941 HomoloGene: 20926 GeneCards: DVL1
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004421
NM_181870
NM_182779
NM_001330311

NM_010091
NM_001302342

RefSeq (protein)

NP_001317240
NP_004412

NP_001289271.1
NP_034221.3
NP_001289271
NP_034221

Location (UCSC) Chr 1: 1.34 – 1.35 Mb Chr 4: 155.85 – 155.86 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Segment polarity protein dishevelled homolog DVL-1 is a protein that in humans is encoded by the DVL1 gene.[3][4]

Function[edit]

DVL1, the human homolog of the Drosophila dishevelled gene (dsh) encodes a cytoplasmic phosphoprotein that regulates cell proliferation, acting as a transducer molecule for developmental processes, including segmentation and neuroblast specification. DVL1 is a candidate gene for processes involved in cell transformations involved in neuroblastoma. The Schwartz-Jampel syndrome and Charcot-Marie-Tooth disease type 2A have been mapped to the same region as DVL1. The phenotypes of these diseases may be consistent with defects which might be expected from aberrant expression of a DVL gene during development. Three transcript variants encoding three different isoforms have been found for this gene.[4]

Interactions[edit]

DVL1 has been shown to interact with:

See also[edit]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Pizzuti A, Amati F, Calabrese G, Mari A, Colosimo A, Silani V, Giardino L, Ratti A, Penso D, Calzà L, Palka G, Scarlato G, Novelli G, Dallapiccola B (Jan 1997). "cDNA characterization and chromosomal mapping of two human homologues of the Drosophila dishevelled polarity gene". Hum Mol Genet. 5 (7): 953–8. doi:10.1093/hmg/5.7.953. PMID 8817329. 
  4. ^ a b "Entrez Gene: DVL1 dishevelled, dsh homolog 1 (Drosophila)". 
  5. ^ Li L, Yuan H, Weaver CD, Mao J, Farr GH, Sussman DJ, Jonkers J, Kimelman D, Wu D (Aug 1999). "Axin and Frat1 interact with dvl and GSK, bridging Dvl to GSK in Wnt-mediated regulation of LEF-1". EMBO J. 18 (15): 4233–40. doi:10.1093/emboj/18.15.4233. PMC 1171499Freely accessible. PMID 10428961. 
  6. ^ Kim MJ, Chia IV, Costantini F (Nov 2008). "SUMOylation target sites at the C terminus protect Axin from ubiquitination and confer protein stability". FASEB J. 22 (11): 3785–94. doi:10.1096/fj.08-113910. PMC 2574027Freely accessible. PMID 18632848. 
  7. ^ Kishida S, Yamamoto H, Hino S, Ikeda S, Kishida M, Kikuchi A (Jun 1999). "DIX domains of Dvl and axin are necessary for protein interactions and their ability to regulate beta-catenin stability". Mol. Cell. Biol. 19 (6): 4414–22. doi:10.1128/mcb.19.6.4414. PMC 104400Freely accessible. PMID 10330181. 
  8. ^ Inobe M, Katsube Ki, Miyagoe Y, Nabeshima Yi, Takeda S (Dec 1999). "Identification of EPS8 as a Dvl1-associated molecule". Biochem. Biophys. Res. Commun. 266 (1): 216–21. doi:10.1006/bbrc.1999.1782. PMID 10581192. 
  9. ^ Warner DR, Pisano MM, Roberts EA, Greene RM (Mar 2003). "Identification of three novel Smad binding proteins involved in cell polarity". FEBS Lett. 539 (1-3): 167–73. doi:10.1016/s0014-5793(03)00155-8. PMID 12650946. 

Further reading[edit]

External links[edit]