DAB2IP

DAB2IP
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2LSW
Identifiers
Aliases	DAB2IP, AF9Q34, AIP-1, AIP1, DIP1/2, DAB2 interacting protein
External IDs	MGI: 1916851 HomoloGene: 13058 GeneCards: DAB2IP
Gene location (Human)
Chr.	Chromosome 9 (human)[1]
End	121,785,530 bp[1]
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)[2]
End	35,730,994 bp[2]
Gene ontology
Molecular function	• phosphatidylinositol-3-phosphate binding; • GTPase activator activity; • SH3 domain binding; • phosphatidylinositol 3-kinase regulatory subunit binding; • phosphatidylinositol-4-phosphate binding; • Toll-like receptor 4 binding; • kinase binding; • protein phosphatase 2A binding; • mitogen-activated protein kinase kinase binding; • vascular endothelial growth factor receptor 2 binding; • protein homodimerization activity; • mitogen-activated protein kinase kinase kinase binding; • 14-3-3 protein binding; • protein binding; • protein kinase binding; • death receptor binding; • signaling adaptor activity; • phosphatidylinositol 3-kinase binding; • identical protein binding; • cadherin binding; • macromolecular complex binding;
Cellular component	• cytoplasm; • cytosol; • membrane; • intrinsic component of the cytoplasmic side of the plasma membrane; • cerebellar mossy fiber; • cell projection; • neuronal cell body membrane; • plasma membrane; • endocytic vesicle; • axon; • neuronal cell body; • parallel fiber; • climbing fiber; • AIP1-IRE1 complex; • dendrite;
Biological process	• negative regulation of epidermal growth factor receptor signaling pathway; • positive regulation of protein catabolic process; • positive regulation of JNK cascade; • cellular protein catabolic process; • negative regulation of Ras protein signal transduction; • negative regulation of endothelial cell migration; • positive regulation of protein serine/threonine kinase activity; • positive regulation of synapse maturation; • positive regulation of IRE1-mediated unfolded protein response; • negative regulation of GTPase activity; • angiogenesis; • negative regulation of epithelial cell proliferation; • cell cycle; • regulation of protein complex assembly; • regulation of I-kappaB kinase/NF-kappaB signaling; • apoptotic process; • activation of signaling protein activity involved in unfolded protein response; • negative regulation of G0 to G1 transition; • activation of JUN kinase activity; • regulation of GTPase activity; • positive regulation of apoptotic signaling pathway; • I-kappaB phosphorylation; • positive regulation of neuron migration; • response to unfolded protein; • negative regulation of MAP kinase activity; • negative regulation of phosphatidylinositol 3-kinase activity; • inflammatory response; • regulation of p38MAPK cascade; • negative regulation of fibroblast proliferation; • activation of MAPKKK activity; • positive regulation of MAPK cascade; • negative regulation of protein phosphorylation; • neuron projection morphogenesis; • vascular endothelial growth factor receptor-2 signaling pathway; • regulation of protein heterodimerization activity; • immune system process; • positive regulation of JUN kinase activity; • negative regulation of transcription from RNA polymerase II promoter; • negative regulation of I-kappaB kinase/NF-kappaB signaling; • cellular response to interleukin-1; • negative regulation of protein serine/threonine kinase activity; • endothelial cell apoptotic process; • negative regulation of transcription, DNA-templated; • negative regulation of NF-kappaB transcription factor activity; • positive regulation of proteasomal protein catabolic process; • negative regulation of vascular endothelial growth factor receptor signaling pathway; • cellular response to tumor necrosis factor; • positive regulation of dendrite development; • cell motility involved in cerebral cortex radial glia guided migration; • MAPK cascade; • negative regulation of phosphatidylinositol 3-kinase signaling; • cellular response to epidermal growth factor stimulus; • multicellular organism development; • tube formation; • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; • layer formation in cerebral cortex; • positive regulation of neuron projection development; • positive regulation of apoptotic process; • negative regulation of ERK1 and ERK2 cascade; • negative regulation of angiogenesis; • regulation of growth; • cellular response to vascular endothelial growth factor stimulus; • negative regulation of vascular endothelial growth factor signaling pathway; • cellular response to lipopolysaccharide; • negative regulation of epithelial cell migration; • extrinsic apoptotic signaling pathway via death domain receptors; • negative regulation of epithelial to mesenchymal transition; • negative regulation of toll-like receptor 4 signaling pathway; • positive regulation of transcription from RNA polymerase II promoter; • signal transduction; • positive regulation of cell cycle arrest; • positive regulation of GTPase activity; • innate immune response; • negative regulation of cellular protein catabolic process; • negative regulation of cell proliferation; • reelin-mediated signaling pathway; • negative regulation of canonical Wnt signaling pathway;
	Sources:Amigo / QuickGO
Orthologs
	153090
	69601
	ENSG00000136848
	ENSMUSG00000026883
	Q5VWQ8
	Q3UHC7
	NM_032552; NM_138709
NM_001001602; NM_001114124; NM_001114125; NM_001290637; NM_001290639;
	NM_001290640; NM_001290641
	NP_115941; NP_619723
NP_001001602; NP_001107596; NP_001107597; NP_001277566; NP_001277568;
	NP_001277569; NP_001277570
	Wikidata
View/Edit Human	View/Edit Mouse

Disabled homolog 2-interacting protein is a protein that in humans is encoded by the DAB2IP gene.^[5]^[6]^[7]

DAB2IP is a Ras (MIM 190020) GTPase-activating protein (GAP) that acts as a tumor suppressor gene and is inactivated by methylation in prostate and breast cancers (Yano et al., 2005).[supplied by OMIM]^[7]

Interactions

DAB2IP has been shown to interact with DAB2.^[8]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000136848 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026883 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Chen H, Pong RC, Wang Z, Hsieh JT (April 2002). "Differential regulation of the human gene DAB2IP in normal and malignant prostatic epithelia: cloning and characterization". Genomics. 79 (4): 573–81. doi:10.1006/geno.2002.6739. PMID 11944990.
↑ Wang Z, Tseng CP, Pong RC, Chen H, McConnell JD, Navone N, Hsieh JT (April 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.
1 2 "Entrez Gene: DAB2IP DAB2 interacting protein".
↑ Wang, Zhi; Tseng Ching-Ping; Pong Rey-Chen; Chen Hong; McConnell John D; Navone Nora; Hsieh Jer-Tsong (April 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. United States. 277 (15): 12622–31. doi:10.1074/jbc.M110568200. ISSN 0021-9258. PMID 11812785.

Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. doi:10.1093/dnares/9.3.99. PMID 12168954.
Nagase T, Kikuno R, Hattori A, et al. (2001). "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (6): 347–55. doi:10.1093/dnares/7.6.347. PMID 11214970.
Chen H, Toyooka S, Gazdar AF, Hsieh JT (2003). "Epigenetic regulation of a novel tumor suppressor gene (hDAB2IP) in prostate cancer cell lines". J. Biol. Chem. 278 (5): 3121–30. doi:10.1074/jbc.M208230200. PMID 12446720.
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.
Zhang R, He X, Liu W, et al. (2003). "AIP1 mediates TNF-α–induced ASK1 activation by facilitating dissociation of ASK1 from its inhibitor 14-3-3". J. Clin. Invest. 111 (12): 1933–43. doi:10.1172/JCI17790. PMC 161425. PMID 12813029.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
von Bergh AR, Wijers PM, Groot AJ, et al. (2004). "Identification of a novel RAS GTPase-activating protein (RASGAP) gene at 9q34 as an MLL fusion partner in a patient with de novo acute myeloid leukemia". Genes Chromosomes Cancer. 39 (4): 324–34. doi:10.1002/gcc.20004. PMID 14978793.
Dote H, Toyooka S, Tsukuda K, et al. (2004). "Aberrant promoter methylation in human DAB2 interactive protein (hDAB2IP) gene in breast cancer". Clin. Cancer Res. 10 (6): 2082–9. doi:10.1158/1078-0432.CCR-03-0236. PMID 15041729.
Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9". Nature. 429 (6990): 369–74. Bibcode:2004Natur.429..369H. doi:10.1038/nature02465. PMC 2734081. PMID 15164053.
Zhang H, Zhang R, Luo Y, et al. (2004). "AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation". J. Biol. Chem. 279 (43): 44955–65. doi:10.1074/jbc.M407617200. PMID 15310755.
Yano M, Toyooka S, Tsukuda K, et al. (2004). "Aberrant promoter methylation of human DAB2 interactive protein (hDAB2IP) gene in lung cancers". Int. J. Cancer. 113 (1): 59–66. doi:10.1002/ijc.20531. PMID 15386433.
Chen H, Tu SW, Hsieh JT (2005). "Down-regulation of human DAB2IP gene expression mediated by polycomb Ezh2 complex and histone deacetylase in prostate cancer". J. Biol. Chem. 280 (23): 22437–44. doi:10.1074/jbc.M501379200. PMID 15817459.
Kunze E, Von Bonin F, Werner C, et al. (2006). "Transitional cell carcinomas and nonurothelial carcinomas of the urinary bladder differ in the promoter methylation status of the caveolin-1, hDAB2IP and p53 genes, but not in the global methylation of Alu elements". Int. J. Mol. Med. 17 (1): 3–13. doi:10.3892/ijmm.17.1.3. PMID 16328005.
Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000136848 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026883 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid11944990-5] Chen H, Pong RC, Wang Z, Hsieh JT (April 2002). "Differential regulation of the human gene DAB2IP in normal and malignant prostatic epithelia: cloning and characterization". Genomics. 79 (4): 573–81. doi:10.1006/geno.2002.6739. PMID 11944990.

[pmid11812785-6] Wang Z, Tseng CP, Pong RC, Chen H, McConnell JD, Navone N, Hsieh JT (April 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.

[entrez-7] 1 2 "Entrez Gene: DAB2IP DAB2 interacting protein".

[autogenerated1-8] Wang, Zhi; Tseng Ching-Ping; Pong Rey-Chen; Chen Hong; McConnell John D; Navone Nora; Hsieh Jer-Tsong (April 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. United States. 277 (15): 12622–31. doi:10.1074/jbc.M110568200. ISSN 0021-9258. PMID 11812785.

DAB2IP

Interactions

References

Further reading