Dab2
entrez
13132
canonical
uniprot
P98078
canonical
ensembl
ENSMUSG00000022150
resolver
ensp
ENSMUSP00000077166
resolver
ensp
ENSMUSP00000079689
resolver
ensp
ENSMUSP00000106291
resolver
ensp
ENSMUSP00000106292
resolver
ensp
ENSMUSP00000124478
resolver
ensp
ENSMUSP00000124589
resolver
ensp
ENSMUSP00000269325
resolver
ensp
ENSMUSP00000269338
resolver
enst
ENSMUST00000078019
resolver
enst
ENSMUST00000080880
resolver
enst
ENSMUST00000110663
resolver
enst
ENSMUST00000110664
resolver
enst
ENSMUST00000161040
resolver
enst
ENSMUST00000161812
resolver
genesymbol
Dab2
resolver
genesymbol_syn
Doc2
resolver
uniprot
A0A0R4J104
resolver
uniprot
E9PX84
resolver
uniprot
E9QL31
resolver
uniprot
F6T0E3
resolver
uniprot
F6XM06
resolver
uniprot
Q3TN55
resolver
uniprot
Q3TRE6
resolver
uniprot
Q3TRI2
resolver
uniprot
Q3U3K1
resolver
uniprot
Q91W56
resolver
uniprot
Q923E1
resolver
uniprot
Q9DCE6
resolver
uniprot_entry
A0A0R4J104_MOUSE
resolver
uniprot_entry
DAB2_MOUSE
resolver
uniprot_entry
E9PX84_MOUSE
resolver
uniprot_entry
E9QL31_MOUSE
resolver
uniprot_entry
F6T0E3_MOUSE
resolver
uniprot_entry
F6XM06_MOUSE
resolver
uniprot_entry
Q3TN55_MOUSE
resolver
uniprot_entry
Q3TRE6_MOUSE
resolver
uniprot_entry
Q3TRI2_MOUSE
resolver
uniprot_entry
Q9DCE6_MOUSE
resolver
uniprot_sec
Q3U3K1
resolver
uniprot_sec
Q91W56
resolver
uniprot_sec
Q923E1
resolver
amino_acid_sequence
MSNEVETSTTNGQPDQQAAPKAPSKKEKKKGSEKTDEYLLARFKGDGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKGMAAAGRSQGQHKQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFIARDVTDNRAFGYVCGGEGQHQFFAIKTGQQAEPLVVDLKDLFQVIYNVKKKEEDKKKVEEANKAEENGSEALMTLDDQANKLKLGVDQMDLFGDMSTPPDLNSPTESKDILLVDLNSEIDTNQNSLRENPFLTNGVTSCSLPRPKPQASFLPENAFSANLNFFPTPNPDPFRDDPFAQPDQSAPSSFDSLTSPDQKKASLSSSSTPQSKGPLNGDTDYFGQQFDQLSNRTGKPEAQGGPWPYPSSQTQQAVRTQNGVSEREQNGFHIKSSPNPFVGSPPKGLSVPNGVKQDLESSVQSSAHDSIAIIPPPQSTKPGRGRRTAKSSANDLLASDIFASEPPGQMSPTGQPAVPQSNFLDLFKGNAPAPVGPLVGLGTVPVTPPQAGPWTPVVYSPSTTVVPGAIISGQPPSFRQPLVFGTTPAVQVWNQSPSFATPASPPPPTVWCPTTSVAPNAWSSTSPLGNPFQSNNIFPPPTMSTQSSPQPMMSSVLATPPQPPPRNGPLKDIPSDAFTGLDPLGDKEVKEVKEMFKDFQLRQPPLVPSRKGETPPSGTSSAFSSYFNNKVGIPQEHVDHDDFDANQLLNKINEPPKPAPRQGVLLGTKSADNSLENPFSKGFSSSNPSVVSQPASSDPHRSPFGNPFA
uniprot
proteins
function
FUNCTION: Adapter protein that functions as a clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Isoform p96 is involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Isoform p67 is not involved in LDL receptor endocytosis. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr-419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation; seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. Isoform p67 may be involved in transcriptional regulation. May act as a tumor suppressor. {ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:11823414, ECO:0000269|PubMed:11927540, ECO:0000269|PubMed:12234931, ECO:0000269|PubMed:12413896, ECO:0000269|PubMed:15734730, ECO:0000269|PubMed:15894542, ECO:0000269|PubMed:16263760, ECO:0000269|PubMed:16870701, ECO:0000269|PubMed:16984970, ECO:0000269|PubMed:19581931, ECO:0000269|PubMed:20881059}.
uniprot
proteins
mass_dalton
82312
uniprot
proteins
mutagenesis
MUTAGEN 53; /note="K->A: Abolishes binding to PtdIns(4,5)P2."; /evidence="ECO:0000269|PubMed:12826668, ECO:0000269|PubMed:16984970"; MUTAGEN 53; /note="K->Q: Abolishes LDLR endocytosis."; /evidence="ECO:0000269|PubMed:12826668, ECO:0000269|PubMed:16984970"; MUTAGEN 90; /note="K->A: Abolishes binding to PtdIns(4,5)P2."; /evidence="ECO:0000269|PubMed:12826668"; MUTAGEN 122; /note="S->T: Abolishes LDLR endocytosis."; /evidence="ECO:0000269|PubMed:16870701, ECO:0000269|PubMed:16984970"; MUTAGEN 122; /note="S->Y: Impairs LDLR endocytosis."; /evidence="ECO:0000269|PubMed:16870701, ECO:0000269|PubMed:16984970"; MUTAGEN 255; /note="F->V: Abolishes interaction with ITSN1, fails to internalize integrin beta-1; when associated with V-398, V-589, V-736 and V-765."; /evidence="ECO:0000269|PubMed:22648170"; MUTAGEN 294; /note="P->A: Loss of interaction with FCHO2; when associated with A-299."; /evidence="ECO:0000269|PubMed:22323290"; MUTAGEN 299; /note="P->A: Loss of interaction with FCHO2; when associated with A-294."; /evidence="ECO:0000269|PubMed:22323290"; MUTAGEN 398; /note="F->V: Abolishes interaction with ITSN1, fails to internalize integrin beta-1; when associated with V-255, V-589, V-736 and V-765."; /evidence="ECO:0000269|PubMed:22648170"; MUTAGEN 589; /note="F->V: Abolishes interaction with EPS15 and impairs interaction with ITSN1, fails to internalize integrin beta-1; when associated with V-736 and V-765. Abolishes interaction with ITSN1; when associated with V-255, V-398, V-736 and V-765."; /evidence="ECO:0000269|PubMed:22648170"; MUTAGEN 736; /note="F->V: Abolishes interaction with EPS15 and impairs interaction with ITSN1, fails to internalize integrin beta-1; when associated with V-589 and V-765. Abolishes interaction with ITSN1; when associated with V-255, V-398, V-589, and V-765."; /evidence="ECO:0000269|PubMed:22648170"; MUTAGEN 765; /note="F->V: Abolishes interaction with EPS15 and impairs interaction with ITSN1, fails to internalize integrin beta-1; when associated with V-589 and V-736. Abolishes interaction with ITSN1; when associated with V-255, V-398, V-589 and V-736."; /evidence="ECO:0000269|PubMed:22648170
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine residues in response to mitogenic growth-factor stimulation. Phosphorylation during mitosis is leading to membrane displacement (By similarity). {ECO:0000250}.
uniprot
proteins
pubmed
11104669
uniprot
proteins
pubmed
11247302
uniprot
proteins
pubmed
11368898
uniprot
proteins
pubmed
11823414
uniprot
proteins
pubmed
11906161
uniprot
proteins
pubmed
11927540
uniprot
proteins
pubmed
12234931
uniprot
proteins
pubmed
12413896
uniprot
proteins
pubmed
12606711
uniprot
proteins
pubmed
12826668
uniprot
proteins
pubmed
12877983
uniprot
proteins
pubmed
14596919
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
15596140
uniprot
proteins
pubmed
15734730
uniprot
proteins
pubmed
15894542
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16263760
uniprot
proteins
pubmed
16870701
uniprot
proteins
pubmed
16984970
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19581931
uniprot
proteins
pubmed
20881059
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22323290
uniprot
proteins
pubmed
22648170
uniprot
proteins
pubmed
7775479
uniprot
proteins
pubmed
9569023
uniprot
proteins
sequence_length
766
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane. Membrane, clathrin-coated pit. Note=Colocalizes with large insert-containing isoforms of MYO6 at clathrin-coated pits/vesicles. During mitosis is progressively displaced from the membrane and translocated to the cytoplasm (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform p96]: Membrane, clathrin-coated pit. Note=Colocalizes with LDLR at clathrin-coated pits.; SUBCELLULAR LOCATION: [Isoform p67]: Cytoplasm {ECO:0000269|PubMed:11104669}. Nucleus {ECO:0000269|PubMed:11104669}. Note=Diffuse localization in the cytoplasm; does not localize to clathrin-coated pits.
uniprot
proteins