P98078 (DAB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified November 13, 2013. Version 124. History...
Names and origin
|Protein names||Recommended name:|
Disabled homolog 2
|Organism||Mus musculus (Mouse) [Reference proteome]|
|Taxonomic identifier||10090 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus|
|Sequence length||766 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Adapter protein that functions as 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 containg 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. Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.24 Ref.25
Interacts (via NPXY motif) with DAB2 (via PID domain). Can interact (via PID domain) with LDLR, APP, APLP1 and APLP2, and weakly with INPP5D (via NPXY motifs); the interaction is impaired by tyrosine phosphorylation of the respective NPXY motifs. Can weakly interact (via PID domain) with LRP1 (via NPXY motif); the interaction is enhanced by tyrosine phosphorylation of the NPXY motif. Interacts with LRP2 (via NPXY motif); the interaction is not affected by tyrosine phosphorylation of the NPXY motif. Interacts with clathrin; in vitro can assemble clathrin triskelia into polyhedral coats. Interacts with AP2A2, ITGB1, ITGB3, ITGB5, PIAS2, DAB2IP, NOSTRIN, FCHO1, DVL3 and EPS15L1. Interacts with SH3KBP1 (via SH3 domains). Interacts with GRB2; competes with SOS1 for binding to GRB2 and the interaction is enhanced by EGF and NT-3 stimulation. Isoform p96 interacts with EPS15 and ITSN1; isoform p67 does not interact with EPS15 and only weakly interacts with ITSN1. Interacts with MAP3K7; the interaction is induced by TGF-beta stimulation and may mediate TGF-beta stimulated JNK activation. Interacts with AXIN1 and PPP1CA; the interactions are mutually exclusive. Interacts with the globular tail of MYO6. Interacts (via DPF motifs) with FCHO2; the interaction is direct and required for DAB2-mediated LDLR endocytosis. Interacts with LRP6; the interaction involves LRP6 phosphorylation by CK2 and sequesters LRP6 towards clathrin-mediated endocytosis. Associates with the TGF-beta receptor complex Probable. Interacts with SMAD2 and SMAD3; the interactions are enhanced upon TGF-beta stimulation. Interacts with GRB2; the interaction is enhanced by EGF and NT-3 stimulation. Interacts with SRC; the interaction is enhanced by EGF stimulation. Ref.5 Ref.6 Ref.7 Ref.8 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.24 Ref.26 Ref.27
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. Ref.6 Ref.7 Ref.12
Isoform p96 and isoform p67 are expressed in adult kidney and fibroblasts with isoform p96 being the predominant form. Isoform p67 is the predominant isoform expressed in embryonic visceral endoderm. Ref.19
The PID domain binds to predominantly non-phosphorylated NPXY internalization motifs present in members of the LDLR and APP family; it also mediates simultaneous binding to phosphatidylinositol 4,5-bisphosphate (Ref.7, Ref.12). Ref.7 Ref.12
Phosphorylated on serine residues in response to mitogenic growth-factor stimulation. Phosphorylation during mitosis is leading to membrane displacement By similarity.
Embryonic lethal; embryos arrest prior to gastrulation and show lack of endodermal organization, failure to thin the distal tip visceral endoderm (VE), elongate the extra-embryonic portion of the egg cylinder and properly organize the epiblast. Loss of the specific megalin/LRP2 lipoprotein receptor distribution at the brush border at the apical cell edge in presumptive VE cells. Conditionally mutant mice are overtly normal, but have reduced clathrin-coated pits in kidney proximal tubule cells and excrete specific plasma proteins in the urine, consistent with reduced transport by LRP2 in the proximal tubule. Ref.9 Ref.11
Contains 1 PID domain.
|AP2A2||O94973||2||EBI-1391846,EBI-1642835||From a different organism.|
|DVL3||Q92997||2||EBI-1391846,EBI-739789||From a different organism.|
|FCHO2||Q0JRZ9||4||EBI-1391846,EBI-2609756||From a different organism.|
|GRB2||P62993||4||EBI-1391846,EBI-401755||From a different organism.|
|MYO6||Q9I8D1||2||EBI-1391846,EBI-6307292||From a different organism.|
|MYO6||Q9UM54||4||EBI-1391846,EBI-350606||From a different organism.|
|SH3KBP1||Q96B97||9||EBI-1391846,EBI-346595||From a different organism.|
|This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]|
|Isoform p96 (identifier: P98078-1) |
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
|Isoform p93 (identifier: P98078-2) |
The sequence of this isoform differs from the canonical sequence as follows:
|Isoform p67 (identifier: P98078-3) |
The sequence of this isoform differs from the canonical sequence as follows:
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Initiator methionine||1||1||Removed By similarity|
|Chain||2 – 766||765||Disabled homolog 2||PRO_0000079771|
|Domain||45 – 196||152||PID|
|Region||230 – 447||218||Required for localization to clathrin-coated pits|
|Region||600 – 730||131||Sufficient for interaction with GRB2|
|Region||617 – 625||9||Required for interaction with CSK By similarity|
|Region||647 – 766||120||Required for interaction with MYO6|
|Region||661 – 669||9||Required for interaction with GRB2 and CSK By similarity|
|Region||707 – 723||17||Sufficient for interaction with SH3KBP1 SH3 domain|
|Motif||293 – 295||3||DPF 1|
|Motif||298 – 300||3||DPF 2|
Amino acid modifications
|Modified residue||2||1||N-acetylserine By similarity|
|Modified residue||323||1||Phosphoserine Ref.23|
|Modified residue||326||1||Phosphoserine; in mitosis By similarity|
|Modified residue||328||1||Phosphoserine; in mitosis By similarity|
|Modified residue||401||1||Phosphoserine By similarity|
|Modified residue||727||1||Phosphoserine Ref.23|
|Alternative sequence||209 – 229||21||Missing in isoform p93.||VSP_004182|
|Alternative sequence||230 – 447||218||Missing in isoform p67.||VSP_004183|
|Mutagenesis||53||1||K → A: Abolishes binding to PtdIns(4,5)P2. Ref.21 Ref.28|
|Mutagenesis||53||1||K → Q: Abolishes LDLR endocytosis. Ref.21 Ref.28|
|Mutagenesis||90||1||K → A: Abolishes binding to PtdIns(4,5)P2. Ref.28|
|Mutagenesis||122||1||S → T: Abolishes LDLR endocytosis. Ref.21 Ref.22|
|Mutagenesis||122||1||S → Y: Impairs LDLR endocytosis. Ref.21 Ref.22|
|Mutagenesis||255||1||F → V: Abolishes interaction with ITSN1, fails to internalize integrin beta-1; when associated with V-398, V-589, V-736 and V-765. Ref.27|
|Mutagenesis||294||1||P → A: Loss of interaction with FCHO2; when associated with A-299. Ref.26|
|Mutagenesis||299||1||P → A: Loss of interaction with FCHO2; when associated with A-294. Ref.26|
|Mutagenesis||398||1||F → V: Abolishes interaction with ITSN1, fails to internalize integrin beta-1; when associated with V-255, V-589, V-736 and V-765. Ref.27|
|Mutagenesis||589||1||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. Ref.27|
|Mutagenesis||736||1||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. Ref.27|
|Mutagenesis||765||1||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. Ref.27|
|Sequence conflict||10||1||T → A in AAH06588. Ref.4|
|Sequence conflict||224||1||D → G in AAH06588. Ref.4|
|Sequence conflict||338||1||G → V in AAB02646. Ref.1|
|Sequence conflict||338||1||G → V in AAB02645. Ref.1|
|Sequence conflict||454||1||L → P in AAB02645. Ref.1|
|Sequence conflict||454||1||L → P in AAB02646. Ref.1|
|Sequence conflict||454||1||L → P in AAB02647. Ref.1|
|Sequence conflict||454||1||L → P in AAG44669. Ref.2|
|Sequence conflict||490||1||A → P in AAB02645. Ref.1|
|Sequence conflict||490||1||A → P in AAB02646. Ref.1|
|Sequence conflict||490||1||A → P in AAB02647. Ref.1|
|Sequence conflict||490||1||A → P in AAG44669. Ref.2|
|Sequence conflict||536||1||R → G in BAE32784. Ref.3|
|Sequence conflict||536||1||R → G in AAH16887. Ref.4|
|Sequence conflict||536||1||R → G in AAH06588. Ref.4|
|Sequence conflict||553||1||S → P in AAH06588. Ref.4|
Helix Strand Turn
|Helix||36 – 43||8|
|Beta strand||48 – 63||16|
|Helix||66 – 84||19|
|Turn||85 – 87||3|
|Beta strand||91 – 98||8|
|Beta strand||101 – 106||6|
|Turn||107 – 109||3|
|Beta strand||112 – 116||5|
|Helix||118 – 120||3|
|Beta strand||121 – 126||6|
|Beta strand||133 – 140||8|
|Beta strand||144 – 153||10|
|Helix||156 – 177||22|
|||"Cloning of a novel phosphoprotein regulated by colony-stimulating factor 1 shares a domain with the Drosophila disabled gene product."|
Xu X.-X., Yang W., Jackowski S., Rock C.O.
J. Biol. Chem. 270:14184-14191(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P67; P93 AND P96).
|||"Chromosomal location of murine disabled-2 gene and structural comparison with its human ortholog."|
Sheng Z., Smith E.R., He J., Tuppen J.A., Martin W.D., Dong F.B., Xu X.X.
Gene 268:31-39(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM P96).
|||"The transcriptional landscape of the mammalian genome."|
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P96).
Tissue: Dendritic cell.
|||"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."|
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P67).
|||"Disabled-2 (Dab2) is an SH3 domain-binding partner of Grb2."|
Xu X.X., Yi T., Tang B., Lambeth J.D.
Oncogene 16:1561-1569(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRB2.
|||"p67 isoform of mouse disabled 2 protein acts as a transcriptional activator during the differentiation of F9 cells."|
Cho S.-Y., Jeon J.W., Lee S.H., Park S.-S.
Biochem. J. 352:645-650(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (ISOFORM P67), SUBCELLULAR LOCATION (ISOFORM P67), INTERACTION WITH PIAS2.
|||"Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2."|
Morris S.M., Cooper J.A.
Traffic 2:111-123(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LDLR; APP; APLP; APLP2; INPP5D; LRP1 AND AP2A2, DOMAIN.
|||"DOC-2/DAB2 is the binding partner of myosin VI."|
Inoue A., Sato O., Homma K., Ikebe M.
Biochem. Biophys. Res. Commun. 292:300-307(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYO6.
|||"Disabled-2 is essential for endodermal cell positioning and structure formation during mouse embryogenesis."|
Yang D.H., Smith E.R., Roland I.H., Sheng Z., He J., Martin W.D., Hamilton T.C., Lambeth J.D., Xu X.X.
Dev. Biol. 251:27-44(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
|||"Disabled-2 is transcriptionally regulated by ICSBP and augments macrophage spreading and adhesion."|
Rosenbauer F., Kallies A., Scheller M., Knobeloch K.P., Rock C.O., Schwieger M., Stocking C., Horak I.
EMBO J. 21:211-220(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
|||"Dual roles for the Dab2 adaptor protein in embryonic development and kidney transport."|
Morris S.M., Tallquist M.D., Rock C.O., Cooper J.A.
EMBO J. 21:1555-1564(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
|||"Disabled-2 exhibits the properties of a cargo-selective endocytic clathrin adaptor."|
Mishra S.K., Keyel P.A., Hawryluk M.J., Agostinelli N.R., Watkins S.C., Traub L.M.
EMBO J. 21:4915-4926(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CLATHRIN AND PHOSPHATIDYLINOSITIDES, DOMAIN.
|||"Interaction of Disabled-1 and the GTPase activating protein Dab2IP in mouse brain."|
Homayouni R., Magdaleno S., Keshvara L., Rice D.S., Curran T.
Brain Res. Mol. Brain Res. 115:121-129(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAB2IP.
|||"Dab2 links CIN85 with clathrin-mediated receptor internalization."|
Kowanetz K., Terzic J., Dikic I.
FEBS Lett. 554:81-87(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SH3KBP1.
|||"Integrin beta cytoplasmic domain interactions with phosphotyrosine-binding domains: a structural prototype for diversity in integrin signaling."|
Calderwood D.A., Fujioka Y., de Pereda J.M., Garcia-Alvarez B., Nakamoto T., Margolis B., McGlade C.J., Liddington R.C., Ginsberg M.H.
Proc. Natl. Acad. Sci. U.S.A. 100:2272-2277(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGB3 AND ITGB5.
|||"Cloning and characterization of mouse disabled 2-interacting protein 2, a mouse orthologue of human NOSTRIN."|
Choi Y.-J., Cho S.-Y., Kim H.-W., Kim J.-A., Bae S.-H., Park S.-S.
Biochem. Biophys. Res. Commun. 326:594-599(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NOSTRIN.
|||"Disabled-2 (Dab2) is required for transforming growth factor beta-induced epithelial to mesenchymal transition (EMT)."|
Prunier C., Howe P.H.
J. Biol. Chem. 280:17540-17548(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ITGB1.
|||"Disabled-2 (Dab2) mediates transforming growth factor beta (TGFbeta)-stimulated fibronectin synthesis through TGFbeta-activated kinase 1 and activation of the JNK pathway."|
Hocevar B.A., Prunier C., Howe P.H.
J. Biol. Chem. 280:25920-25927(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAP3K7.
|||"Endocytosis of megalin by visceral endoderm cells requires the Dab2 adaptor protein."|
Maurer M.E., Cooper J.A.
J. Cell Sci. 118:5345-5355(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
|||"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."|
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
|||"The adaptor protein Dab2 sorts LDL receptors into coated pits independently of AP-2 and ARH."|
Maurer M.E., Cooper J.A.
J. Cell Sci. 119:4235-4246(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-53 AND SER-122.
|||"A single common portal for clathrin-mediated endocytosis of distinct cargo governed by cargo-selective adaptors."|
Keyel P.A., Mishra S.K., Roth R., Heuser J.E., Watkins S.C., Traub L.M.
Mol. Biol. Cell 17:4300-4317(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-122.
|||"The phagosomal proteome in interferon-gamma-activated macrophages."|
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND SER-727, MASS SPECTROMETRY.
|||"Dab2 stabilizes Axin and attenuates Wnt/beta-catenin signaling by preventing protein phosphatase 1 (PP1)-Axin interactions."|
Jiang Y., Luo W., Howe P.H.
Oncogene 28:2999-3007(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH AXIN1 AND PPP1CA.
|||"Type II transforming growth factor-beta receptor recycling is dependent upon the clathrin adaptor protein Dab2."|
Penheiter S.G., Singh R.D., Repellin C.E., Wilkes M.C., Edens M., Howe P.H., Pagano R.E., Leof E.B.
Mol. Biol. Cell 21:4009-4019(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
|||"FCH domain only-2 organizes clathrin-coated structures and interacts with Disabled-2 for low-density lipoprotein receptor endocytosis."|
Mulkearns E.E., Cooper J.A.
Mol. Biol. Cell 23:1330-1342(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCHO2, MUTAGENESIS OF PRO-294 AND PRO-299.
|||"The clathrin adaptor Dab2 recruits EH domain scaffold proteins to regulate integrin beta1 endocytosis."|
Teckchandani A., Mulkearns E.E., Randolph T.W., Toida N., Cooper J.A.
Mol. Biol. Cell 23:2905-2916(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPS15, EPS15L1 AND ITSN1, MUTAGENESIS OF PHE-255; PHE-398; PHE-589; PHE-736 AND PHE-765.
|||"Crystal structures of the Dab homology domains of mouse disabled 1 and 2."|
Yun M., Keshvara L., Park C.G., Zhang Y.M., Dickerson J.B., Zheng J., Rock C.O., Curran T., Park H.W.
J. Biol. Chem. 278:36572-36581(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 33-191, MUTAGENESIS OF LYS-53 AND LYS-90.
|+||Additional computationally mapped references.|
|U18869 mRNA. Translation: AAB02646.1.|
U18869 mRNA. Translation: AAB02647.1.
U18869 mRNA. Translation: AAB02645.1.
AF260580 Genomic DNA. Translation: AAG44669.1.
AK154716 mRNA. Translation: BAE32784.1.
BC016887 mRNA. Translation: AAH16887.1.
BC006588 mRNA. Translation: AAH06588.1.
|RefSeq||NP_001008702.1. NM_001008702.2. |
3D structure databases
|SMR||P98078. Positions 33-180, 674-711. |
Protein-protein interaction databases
|IntAct||P98078. 52 interactions.|
Protocols and materials databases
Genome annotation databases
|Ensembl||ENSMUST00000080880; ENSMUSP00000079689; ENSMUSG00000022150. |
|UCSC||uc007vde.1. mouse. |
|MGI||MGI:109175. Dab2. |
Gene expression databases
Family and domain databases
|Gene3D||126.96.36.199. 1 hit. |
|InterPro||IPR011993. PH_like_dom. |
|Pfam||PF00640. PID. 1 hit. |
|SMART||SM00462. PTB. 1 hit. |
|PROSITE||PS01179. PID. 1 hit. |
|Accession||Primary (citable) accession number: P98078|
Secondary accession number(s): Q3U3K1, Q91W56, Q923E1
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|