DVL2

Human protein and coding gene
DVL2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2REY, 3CBX, 3CBY, 3CBZ, 3CC0, 4WIP

Identifiers
AliasesDVL2, dishevelled segment polarity protein 2
External IDsOMIM: 602151; MGI: 106613; HomoloGene: 20927; GeneCards: DVL2; OMA:DVL2 - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for DVL2
Genomic location for DVL2
Band17p13.1Start7,225,342 bp[1]
End7,234,517 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for DVL2
Genomic location for DVL2
Band11 B3|11 42.96 cMStart69,891,421 bp[2]
End69,903,127 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • ventricular zone

  • stromal cell of endometrium

  • left ovary

  • ectocervix

  • right ovary

  • body of uterus

  • right hemisphere of cerebellum

  • canal of the cervix

  • anterior pituitary

  • ganglionic eminence
Top expressed in
  • yolk sac

  • ventricular zone

  • granulocyte

  • epiblast

  • superior frontal gyrus

  • neural layer of retina

  • spermatocyte

  • genital tubercle

  • tail of embryo

  • dermis
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • protein-macromolecule adaptor activity
  • protein domain specific binding
  • frizzled binding
  • protein self-association
  • protein binding
  • identical protein binding
  • protein kinase binding
Cellular component
  • membrane
  • clathrin-coated endocytic vesicle
  • plasma membrane
  • apical part of cell
  • clathrin-coated vesicle
  • cytoplasm
  • cytoplasmic vesicle
  • nucleus
  • cytosol
  • nucleoplasm
  • aggresome
  • lateral plasma membrane
  • nuclear body
Biological process
  • non-canonical Wnt signaling pathway
  • positive regulation of protein phosphorylation
  • intracellular signal transduction
  • positive regulation of protein tyrosine kinase activity
  • heart morphogenesis
  • canonical Wnt signaling pathway involved in regulation of cell proliferation
  • positive regulation of DNA-binding transcription factor activity
  • transcription by RNA polymerase II
  • hippo signaling
  • positive regulation of transcription, DNA-templated
  • multicellular organism development
  • positive regulation of GTPase activity
  • protein complex oligomerization
  • cochlea morphogenesis
  • convergent extension involved in neural plate elongation
  • negative regulation of canonical Wnt signaling pathway
  • segmentation
  • convergent extension involved in organogenesis
  • positive regulation of canonical Wnt signaling pathway
  • neural tube closure
  • heart development
  • Wnt signaling pathway
  • outflow tract morphogenesis
  • canonical Wnt signaling pathway
  • segment specification
  • positive regulation of JUN kinase activity
  • planar cell polarity pathway involved in neural tube closure
  • Wnt signaling pathway, planar cell polarity pathway
  • beta-catenin destruction complex disassembly
  • membrane organization
  • positive regulation of neuron projection arborization
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

1856

13543

Ensembl

ENSG00000004975

ENSMUSG00000020888

UniProt

O14641

Q60838

RefSeq (mRNA)

NM_004422

NM_007888

RefSeq (protein)

NP_004413

NP_031914

Location (UCSC)Chr 17: 7.23 – 7.23 MbChr 11: 69.89 – 69.9 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Segment polarity protein dishevelled homolog DVL-2 is a protein that in humans is encoded by the DVL2 gene.[5][6]

This gene encodes a member of the dishevelled (dsh) protein family. The vertebrate dsh proteins have approximately 40% amino acid sequence similarity with Drosophila dsh. This gene encodes a 90-kD protein that undergoes posttranslational phosphorylation to form a 95-kD cytoplasmic protein, which may play a role in the signal transduction pathway mediated by multiple Wnt proteins. The mechanisms of dishevelled function in Wnt signaling are likely to be conserved among metazoans.[6]

Interactions

DVL2 has been shown to interact with Zinc finger protein 165,[7] DAB2[8] and Arrestin beta 1.[9]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000004975 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020888 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Greco TL, Sussman DJ, Camper SA (January 1997). "Dishevelled-2 maps to human chromosome 17 and distal to Wnt3a and vestigial tail (vt) on mouse chromosome 11". Mamm Genome. 7 (6): 475–6. doi:10.1007/s003359900144. PMID 8662242. S2CID 39619679.
  6. ^ a b "Entrez Gene: DVL2 dishevelled, dsh homolog 2 (Drosophila)".
  7. ^ Rual, Jean-François; Venkatesan Kavitha; Hao Tong; Hirozane-Kishikawa Tomoko; Dricot Amélie; Li Ning; Berriz Gabriel F; Gibbons Francis D; Dreze Matija; Ayivi-Guedehoussou Nono; Klitgord Niels; Simon Christophe; Boxem Mike; Milstein Stuart; Rosenberg Jennifer; Goldberg Debra S; Zhang Lan V; Wong Sharyl L; Franklin Giovanni; Li Siming; Albala Joanna S; Lim Janghoo; Fraughton Carlene; Llamosas Estelle; Cevik Sebiha; Bex Camille; Lamesch Philippe; Sikorski Robert S; Vandenhaute Jean; Zoghbi Huda Y; Smolyar Alex; Bosak Stephanie; Sequerra Reynaldo; Doucette-Stamm Lynn; Cusick Michael E; Hill David E; Roth Frederick P; Vidal Marc (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  8. ^ Hocevar, B A; Mou F; Rennolds J L; Morris S M; Cooper J A; Howe P H (June 2003). "Regulation of the Wnt signaling pathway by disabled-2 (Dab2)". EMBO J. 22 (12): 3084–94. doi:10.1093/emboj/cdg286. ISSN 0261-4189. PMC 162138. PMID 12805222.
  9. ^ Chen, W; Hu L A; Semenov M V; Yanagawa S; Kikuchi A; Lefkowitz R J; Miller W E (December 2001). "β-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins". Proc. Natl. Acad. Sci. U.S.A. 98 (26): 14889–94. Bibcode:2001PNAS...9814889C. doi:10.1073/pnas.211572798. ISSN 0027-8424. PMC 64954. PMID 11742073.

Further reading

  • Pizzuti A, Amati F, Calabrese G, et al. (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.
  • Klingensmith J, Yang Y, Axelrod JD, et al. (1997). "Conservation of dishevelled structure and function between flies and mice: isolation and characterization of Dvl2". Mech. Dev. 58 (1–2): 15–26. doi:10.1016/S0925-4773(96)00549-7. PMID 8887313. S2CID 16004832.
  • Semënov MV, Snyder M (1997). "Human dishevelled genes constitute a DHR-containing multigene family". Genomics. 42 (2): 302–10. doi:10.1006/geno.1997.4713. PMID 9192851.
  • Strovel ET, Wu D, Sussman DJ (2000). "Protein phosphatase 2Calpha dephosphorylates axin and activates LEF-1-dependent transcription". J. Biol. Chem. 275 (4): 2399–403. doi:10.1074/jbc.275.4.2399. PMID 10644691.
  • Song DH, Sussman DJ, Seldin DC (2000). "Endogenous protein kinase CK2 participates in Wnt signaling in mammary epithelial cells". J. Biol. Chem. 275 (31): 23790–7. doi:10.1074/jbc.M909107199. PMID 10806215.
  • Zhang Y, Neo SY, Han J, Lin SC (2000). "Dimerization choices control the ability of axin and dishevelled to activate c-Jun N-terminal kinase/stress-activated protein kinase". J. Biol. Chem. 275 (32): 25008–14. doi:10.1074/jbc.M002491200. PMID 10829020.
  • Chen W, Hu LA, Semenov MV, et al. (2002). "β-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins". Proc. Natl. Acad. Sci. U.S.A. 98 (26): 14889–94. Bibcode:2001PNAS...9814889C. doi:10.1073/pnas.211572798. PMC 64954. PMID 11742073.
  • Habas R, Kato Y, He X (2002). "Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and requires a novel Formin homology protein Daam1". Cell. 107 (7): 843–54. doi:10.1016/S0092-8674(01)00614-6. PMID 11779461. S2CID 16894557.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Habas R, Dawid IB, He X (2003). "Coactivation of Rac and Rho by Wnt/Frizzled signaling is required for vertebrate gastrulation". Genes Dev. 17 (2): 295–309. doi:10.1101/gad.1022203. PMC 195976. PMID 12533515.
  • Chen W, ten Berge D, Brown J, et al. (2003). "Dishevelled 2 recruits beta-arrestin 2 to mediate Wnt5A-stimulated endocytosis of Frizzled 4". Science. 301 (5638): 1391–4. Bibcode:2003Sci...301.1391C. doi:10.1126/science.1082808. PMID 12958364. S2CID 34975427.
  • Wong CK, Luo W, Deng Y, et al. (2004). "The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal kinase activation by Axin and dishevelled through distinct mechanisms". J. Biol. Chem. 279 (38): 39366–73. doi:10.1074/jbc.M404598200. PMID 15262978.
  • Torban E, Wang HJ, Groulx N, Gros P (2005). "Independent mutations in mouse Vangl2 that cause neural tube defects in looptail mice impair interaction with members of the Dishevelled family". J. Biol. Chem. 279 (50): 52703–13. doi:10.1074/jbc.M408675200. PMID 15456783.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Zhang L, Gao X, Wen J, et al. (2006). "Dapper 1 antagonizes Wnt signaling by promoting dishevelled degradation". J. Biol. Chem. 281 (13): 8607–12. doi:10.1074/jbc.M600274200. PMID 16446366.
  • Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569. S2CID 13709685.
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