DAB2

From Wikipedia, the free encyclopedia

Disabled homolog 2, mitogen-responsive phosphoprotein (Drosophila)

PDB rendering based on 1m7e.

Available structures: 1m7e, 1p3r

Identifiers

Symbol(s)

DAB2; DOC-2; DOC2; FLJ26626

External IDs

OMIM: 601236 MGI: 109175 HomoloGene: 1026

Gene ontology
Molecular Function:	• protein C-terminus binding
Cellular Component:	• coated pit
Biological Process:	• cell proliferation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_001343 (mRNA)
NP_001334 (protein)

NM_001008702 (mRNA)
NP_001008702 (protein)

Location

Chr 5: 39.41 - 39.46 Mb

n/a

Pubmed search

[1]

[2]

Disabled homolog 2, mitogen-responsive phosphoprotein (Drosophila), also known as DAB2, is a human gene.

DAB2 mRNA is expressed in normal ovarian epithelial cells but is down-regulated or absent from ovarian carcinoma cell lines. The 770-amino acid predicted protein has an overall 83% identity with the mouse p96 protein, a putative mitogen-responsive phosphoprotein; homology is strongest in the amino-terminal end of the protein in a region corresponding to the phosphotyrosine interaction domain. The down-regulation of DAB2 may play an important role in ovarian carcinogenesis. This gene was initially named DOC2 (for Differentially expressed in Ovarian Cancer) and is distinct from the DOC2A and DOC2B genes (for double C2-like domains, alpha and beta).^[1]

[edit] References

^ Entrez Gene: DAB2 disabled homolog 2, mitogen-responsive phosphoprotein (Drosophila).

[edit] Further reading

Mok SC, Wong KK, Chan RK, et al. (1994). "Molecular cloning of differentially expressed genes in human epithelial ovarian cancer.". Gynecol. Oncol. 52 (2): 247–52. doi:10.1006/gyno.1994.1040. PMID 8314147.
Albertsen HM, Smith SA, Melis R, et al. (1997). "Sequence, genomic structure, and chromosomal assignment of human DOC-2.". Genomics 33 (2): 207–13. doi:10.1006/geno.1996.0185. PMID 8660969.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
Xu XX, Yi T, Tang B, Lambeth JD (1998). "Disabled-2 (Dab2) is an SH3 domain-binding partner of Grb2.". Oncogene 16 (12): 1561–9. doi:10.1038/sj.onc.1201678. PMID 9569023.
Mok SC, Chan WY, Wong KK, et al. (1998). "DOC-2, a candidate tumor suppressor gene in human epithelial ovarian cancer.". Oncogene 16 (18): 2381–7. doi:10.1038/sj.onc.1201769. PMID 9620555.
Fazili Z, Sun W, Mittelstaedt S, et al. (1999). "Disabled-2 inactivation is an early step in ovarian tumorigenicity.". Oncogene 18 (20): 3104–13. doi:10.1038/sj.onc.1202649. PMID 10340382.
Tseng CP, Ely BD, Pong RC, et al. (1999). "The role of DOC-2/DAB2 protein phosphorylation in the inhibition of AP-1 activity. An underlying mechanism of its tumor-suppressive function in prostate cancer.". J. Biol. Chem. 274 (45): 31981–6. PMID 10542228.
Oleinikov AV, Zhao J, Makker SP (2000). "Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic receptor gp600/megalin.". Biochem. J. 347 Pt 3: 613–21. PMID 10769163.
Sheng Z, Sun W, Smith E, et al. (2000). "Restoration of positioning control following Disabled-2 expression in ovarian and breast tumor cells.". Oncogene 19 (42): 4847–54. doi:10.1038/sj.onc.1203853. PMID 11039902.
Sheng Z, He J, Tuppen JA, et al. (2001). "Structure, sequence, and promoter analysis of human disabled-2 gene (DAB2).". Genomics 70 (3): 381–6. doi:10.1006/geno.2000.6383. PMID 11161789.
Morris SM, Cooper JA (2001). "Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2.". Traffic 2 (2): 111–23. PMID 11247302.
Zhou J, Hsieh JT (2001). "The inhibitory role of DOC-2/DAB2 in growth factor receptor-mediated signal cascade. DOC-2/DAB2-mediated inhibition of ERK phosphorylation via binding to Grb2.". J. Biol. Chem. 276 (30): 27793–8. doi:10.1074/jbc.M102803200. PMID 11371563.
Hocevar BA, Smine A, Xu XX, Howe PH (2001). "The adaptor molecule Disabled-2 links the transforming growth factor beta receptors to the Smad pathway.". EMBO J. 20 (11): 2789–801. doi:10.1093/emboj/20.11.2789. PMID 11387212.
Wang Z, Tseng CP, Pong RC, et al. (2002). "The mechanism of growth-inhibitory effect of DOC-2/DAB2 in prostate cancer. Characterization of a novel GTPase-activating protein associated with N-terminal domain of DOC-2/DAB2.". J. Biol. Chem. 277 (15): 12622–31. doi:10.1074/jbc.M110568200. PMID 11812785.
Inoue A, Sato O, Homma K, Ikebe M (2002). "DOC-2/DAB2 is the binding partner of myosin VI.". Biochem. Biophys. Res. Commun. 292 (2): 300–7. doi:10.1006/bbrc.2002.6636. PMID 11906161.
Mishra SK, Keyel PA, Hawryluk MJ, Agostinelli NR, Watkins SC, Traub LM. (2002). "Disabled-2 exhibits the properties of a cargo-selective endocytic clathrin adaptor.". EMBO J. 21 (18): 4915–4926. PMID 12234931.
Morris SM, Tallquist MD, Rock CO, Cooper JA (2002). "Dual roles for the Dab2 adaptor protein in embryonic development and kidney transport.". EMBO J. 21 (7): 1555–64. doi:10.1093/emboj/21.7.1555. PMID 11927540.
Morris SM, Arden SD, Roberts RC, et al. (2002). "Myosin VI binds to and localises with Dab2, potentially linking receptor-mediated endocytosis and the actin cytoskeleton.". Traffic 3 (5): 331–41. PMID 11967127.
Zhou J, Scholes J, Hsieh JT (2003). "Characterization of a novel negative regulator (DOC-2/DAB2) of c-Src in normal prostatic epithelium and cancer.". J. Biol. Chem. 278 (9): 6936–41. doi:10.1074/jbc.M210628200. PMID 12473651.
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. doi:10.1073/pnas.242603899. PMID 12477932.
Calderwood DA, Fujioka Y, de Pereda JM, et al. (2003). "Integrin beta cytoplasmic domain interactions with phosphotyrosine-binding domains: a structural prototype for diversity in integrin signaling.". Proc. Natl. Acad. Sci. U.S.A. 100 (5): 2272–7. doi:10.1073/pnas.262791999. PMID 12606711.