DAB2IP
entrez
153090
canonical
uniprot
Q5VWQ8
canonical
ensembl
ENSG00000136848
resolver
ensp
ENSP00000259371
resolver
ensp
ENSP00000310827
resolver
ensp
ENSP00000386183
resolver
genesymbol
DAB2IP
resolver
genesymbol_syn
AF9Q34
resolver
genesymbol_syn
AIP1
resolver
genesymbol_syn
KIAA1743
resolver
hgnc
HGNC:17294
resolver
uniprot
A6H8V2
resolver
uniprot
A6NHI9
resolver
uniprot
B0QZB1
resolver
uniprot
G3XA90
resolver
uniprot
Q8TDL2
resolver
uniprot
Q96SE1
resolver
uniprot
Q9C0C0
resolver
uniprot_entry
DAB2P_HUMAN
resolver
uniprot_sec
A6H8V2
resolver
uniprot_sec
A6NHI9
resolver
uniprot_sec
B0QZB1
resolver
uniprot_sec
G3XA90
resolver
uniprot_sec
Q8TDL2
resolver
uniprot_sec
Q96SE1
resolver
uniprot_sec
Q9C0C0
resolver
amino_acid_sequence
MSAGGSARKSTGRSSYYYRLLRRPRLQRQRSRSRSRTRPARESPQERPGSRRSLPGSLSEKSPSMEPSAATPFRVTGFLSRRLKGSIKRTKSQPKLDRNHSFRHILPGFRSAAAAAADNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEEVVIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVEHILKLWVIEAKDLPAKKKYLCELCLDDVLYARTTGKLKTDNVFWGEHFEFHNLPPLRTVTVHLYRETDKKKKKERNSYLGLVSLPAASVAGRQFVEKWYPVVTPNPKGGKGPGPMIRIKARYQTITILPMEMYKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDNEHLIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSAADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSRGRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLEQSIVSKLGPLPRILRDVHTALSTPGSGQLPGTNDLASTPGSGSSSISAGLQKMVIENDLSGLIDFTRLPSPTPENKDLFFVTRSSGVQPSPARSSSYSEANEPDLQMANGGKSLSMVDLQDARTLDGEAGSPAGPDVLPTDGQAAAAQLVAGWPARATPVNLAGLATVRRAGQTPTTPGTSEGAPGRPQLLAPLSFQNPVYQMAAGLPLSPRGLGDSGSEGHSSLSSHSNSEELAAAAKLGSFSTAAEELARRPGELARRQMSLTEKGGQPTVPRQNSAGPQRRIDQPPPPPPPPPPAPRGRTPPNLLSTLQYPRPSSGTLASASPDWVGPSTRLRQQSSSSKGDSPELKPRAVHKQGPSPVSPNALDRTAAWLLTMNAQLLEDEGLGPDPPHRDRLRSKDELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQARLEEGEERLRRQQEDKDIQMKGIISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMQARNGISPTNPTKLQITENGEFRNSSNC
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving DAB2IP is found in a patient with acute myeloid leukemia (AML). Translocation t(9;11)(q34;q23) with KMT2A/MLL1. May give rise to a KMT2A/MLL1-DAB2IP fusion protein lacking the PH domain (PubMed:14978793). {ECO:0000269|PubMed:14978793}.
uniprot
proteins
function
FUNCTION: Functions as a scaffold protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Involved in several processes such as innate immune response, inflammation and cell growth inhibition, apoptosis, cell survival, angiogenesis, cell migration and maturation. Also plays a role in cell cycle checkpoint control; reduces G1 phase cyclin levels resulting in G0/G1 cell cycle arrest. Mediates signal transduction by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF), interferon (IFN) or lipopolysaccharide (LPS). Modulates the balance between phosphatidylinositol 3-kinase (PI3K)-AKT-mediated cell survival and apoptosis stimulated kinase (MAP3K5)-JNK signaling pathways; sequesters both AKT1 and MAP3K5 and counterbalances the activity of each kinase by modulating their phosphorylation status in response to pro-inflammatory stimuli. Acts as a regulator of the endoplasmic reticulum (ER) unfolded protein response (UPR) pathway; specifically involved in transduction of the ER stress-response to the JNK cascade through ERN1. Mediates TNF-induced apoptosis activation by facilitating dissociation of inhibitor 14-3-3 from MAP3K5; recruits the PP2A phosphatase complex which dephosphorylates MAP3K5 on 'Ser-966', leading to the dissociation of 13-3-3 proteins and activation of the MAP3K5-JNK signaling pathway in endothelial cells. Also mediates TNF/TRAF2-induced MAP3K5-JNK activation, while it inhibits CHUK-NF-kappa-B signaling. Acts a negative regulator in the IFN-gamma-mediated JAK-STAT signaling cascade by inhibiting smooth muscle cell (VSMCs) proliferation and intimal expansion, and thus, prevents graft arteriosclerosis (GA). Acts as a GTPase-activating protein (GAP) for the ADP ribosylation factor 6 (ARF6), Ras and RAB40C (PubMed:29156729). Promotes hydrolysis of the ARF6-bound GTP and thus, negatively regulates phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent TLR4-TIRAP-MyD88 and NF-kappa-B signaling pathways in endothelial cells in response to lipopolysaccharides (LPS). Binds specifically to phosphatidylinositol 4-phosphate (PtdIns4P) and phosphatidylinositol 3-phosphate (PtdIns3P). In response to vascular endothelial growth factor (VEGFA), acts as a negative regulator of the VEGFR2-PI3K-mediated angiogenic signaling pathway by inhibiting endothelial cell migration and tube formation. In the developing brain, promotes both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex in a glial-dependent locomotion process. Probable downstream effector of the Reelin signaling pathway; promotes Purkinje cell (PC) dendrites development and formation of cerebellar synapses. Also functions as a tumor suppressor protein in prostate cancer progression; prevents cell proliferation and epithelial-to-mesenchymal transition (EMT) through activation of the glycogen synthase kinase-3 beta (GSK3B)-induced beta-catenin and inhibition of PI3K-AKT and Ras-MAPK survival downstream signaling cascades, respectively. {ECO:0000269|PubMed:12813029, ECO:0000269|PubMed:17389591, ECO:0000269|PubMed:18292600, ECO:0000269|PubMed:19033661, ECO:0000269|PubMed:19903888, ECO:0000269|PubMed:19948740, ECO:0000269|PubMed:20080667, ECO:0000269|PubMed:20154697, ECO:0000269|PubMed:21700930, ECO:0000269|PubMed:22696229, ECO:0000269|PubMed:29156729}.
uniprot
proteins
mass_dalton
131625
uniprot
proteins
mutagenesis
MUTAGEN 228..230; /note="KKK->AAA: Reduces interaction with KDR/VEGFR2. Does not inhibit interaction with MAP3K5."; /evidence="ECO:0000269|PubMed:12813029, ECO:0000269|PubMed:19033661"; MUTAGEN 281..284; /note="KKKK->AAAA: Significantly reduces interaction with MAP3K5. Does not reduce interaction with KDR/VEGFR2."; /evidence="ECO:0000269|PubMed:12813029, ECO:0000269|PubMed:19033661"; MUTAGEN 413; /note="R->L: Decreased GAP activity toward RAB40C. Does not inhibit interaction with MAP3K5. Does not reduce GSK3B-induced beta-catenin transcription activity, TNF-induced apoptosis, ARF6-mediated TLR4-TIRAP-MyD88 signaling inhibition, Ras and NF-kappa-B activities and tumor development. Does not suppress tumor development; when associated with A-728."; /evidence="ECO:0000269|PubMed:12813029, ECO:0000269|PubMed:19903888, ECO:0000269|PubMed:19948740, ECO:0000269|PubMed:20154697, ECO:0000269|PubMed:29156729"; MUTAGEN 728; /note="S->A: Inhibits phosphorylation and TNF-induced MAP3K5 dephosphorylation. Reduces interaction with 14-3-3 proteins, AKT1, a regulatory p85 subunit, MAP3K5, RIPK1, TRAF2 and TNF-induced MAP3K5-JNK signaling and apoptosis. Reduces RAS activity. Does not reduce GSK3B-induced beta catenin-mediated transcription activity. Does not reduce NF-kappa-B activity, cell invasion, epithelial-to-mesenchymal transition (EMT) and tumor development. Does not suppress tumor development; when associated with R-413."; /evidence="ECO:0000269|PubMed:17389591, ECO:0000269|PubMed:18292600, ECO:0000269|PubMed:19903888, ECO:0000269|PubMed:20154697"; MUTAGEN 920..929; /note="PPPPPPPPPP->AAAAAAAAAA: Reduces interaction with a regulatory p85 subunit of the PI3K complex. Inhibits MAP3K5 active form increase, AKT1 active form decrease, PI3K-p85 complex activity inhibition and TNF-induced apoptosis."; /evidence="ECO:0000269|PubMed:19903888"; MUTAGEN 935; /note="T->A: Does not reduce interaction with 14-3-3 proteins."; /evidence="ECO:0000269|PubMed:17389591
uniprot
proteins
post_translational_modification
PTM: In response to TNF-induction, phosphorylated at Ser-728; phosphorylation leads to a conformational change, and thus, increases its association with 14-3-3 proteins, MAP3K5, RIPK1 and TRAF2 in endothelial cells; also stimulates regulatory p85 subunit sequestring and PI3K-p85 complex activity inhibition. {ECO:0000269|PubMed:17389591, ECO:0000269|PubMed:19903888}.
uniprot
proteins
pubmed
11214970
uniprot
proteins
pubmed
11944990
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
12813029
uniprot
proteins
pubmed
14978793
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15310755
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15701637
uniprot
proteins
pubmed
17389591
uniprot
proteins
pubmed
18292600
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19033661
uniprot
proteins
pubmed
19903888
uniprot
proteins
pubmed
19948740
uniprot
proteins
pubmed
20080667
uniprot
proteins
pubmed
20154697
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21700930
uniprot
proteins
pubmed
22696229
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
29156729
uniprot
proteins
sequence_length
1189
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29156729}. Cell membrane {ECO:0000269|PubMed:29156729}; Peripheral membrane protein {ECO:0000305}. Membrane {ECO:0000269|PubMed:29156729}. Cell projection, dendrite {ECO:0000250}. Note=Localized in soma and dendrites of Purkinje cells as well as in scattered cell bodies in the molecular layer of the cerebellum (By similarity). Colocalizes with TIRAP at the plasma membrane. Colocalizes with ARF6 at the plasma membrane and endocytic vesicles. Translocates from the plasma membrane to the cytoplasm in response to TNF. Phosphatidylinositol 4-phosphate (PtdIns4P) binding is essential for plasma membrane localization. Localized in the cytoplasmic space in close proximity to lipid droplets (PubMed:29156729). {ECO:0000250, ECO:0000269|PubMed:29156729}.
uniprot
proteins