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Protein

Disabled homolog 2

Gene

Dab2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 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.12 Publications

GO - Molecular functioni

  • AP-2 adaptor complex binding Source: UniProtKB
  • cargo receptor activity Source: UniProtKB
  • clathrin adaptor activity Source: UniProtKB
  • clathrin binding Source: UniProtKB
  • integrin binding Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  • phosphatidylinositol binding Source: UniProtKB
  • protein C-terminus binding Source: MGI
  • SMAD binding Source: MGI

GO - Biological processi

  • activation of JUN kinase activity Source: UniProtKB
  • apoptotic process Source: UniProtKB-KW
  • cell morphogenesis involved in differentiation Source: MGI
  • cellular response to transforming growth factor beta stimulus Source: UniProtKB
  • clathrin coat assembly Source: UniProtKB
  • endoderm development Source: MGI
  • excretion Source: MGI
  • in utero embryonic development Source: MGI
  • leading edge cell differentiation Source: MGI
  • myeloid cell differentiation Source: UniProtKB
  • negative regulation of androgen receptor signaling pathway Source: MGI
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of canonical Wnt signaling pathway Source: MGI
  • negative regulation of extrinsic apoptotic signaling pathway Source: MGI
  • negative regulation of protein binding Source: MGI
  • negative regulation of protein localization to plasma membrane Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: MGI
  • pinocytosis Source: MGI
  • positive regulation of cell adhesion Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of clathrin-dependent endocytosis Source: UniProtKB
  • positive regulation of early endosome to late endosome transport Source: MGI
  • positive regulation of endocytosis Source: MGI
  • positive regulation of epithelial to mesenchymal transition Source: UniProtKB
  • positive regulation of integrin-mediated signaling pathway Source: UniProtKB
  • positive regulation of pathway-restricted SMAD protein phosphorylation Source: UniProtKB
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
  • positive regulation of protein phosphorylation Source: MGI
  • positive regulation of receptor internalization Source: CACAO
  • positive regulation of receptor recycling Source: UniProtKB
  • positive regulation of SMAD protein import into nucleus Source: MGI
  • positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of transforming growth factor beta receptor signaling pathway Source: MGI
  • positive regulation of Wnt signaling pathway, planar cell polarity pathway Source: MGI
  • protein transport Source: UniProtKB-KW
  • Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Apoptosis, Differentiation, Endocytosis, Protein transport, Transport, Wnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Disabled homolog 2
Alternative name(s):
Adaptor molecule disabled-2
Differentially expressed in ovarian carcinoma 2
Short name:
DOC-2
Mitogen-responsive phosphoprotein
Gene namesi
Name:Dab2
Synonyms:Doc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:109175. Dab2.

Subcellular locationi

Isoform p96 :
Isoform p67 :
  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

  • Note: Diffuse localization in the cytoplasm; does not localize to clathrin-coated pits.

GO - Cellular componenti

  • apical plasma membrane Source: MGI
  • clathrin-coated pit Source: MGI
  • clathrin-coated vesicle Source: MGI
  • clathrin-coated vesicle membrane Source: UniProtKB-SubCell
  • clathrin coat of coated pit Source: UniProtKB
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • focal adhesion Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • nucleolus Source: MGI
  • nucleus Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi53K → A: Abolishes binding to PtdIns(4,5)P2. 2 Publications1
Mutagenesisi53K → Q: Abolishes LDLR endocytosis. 2 Publications1
Mutagenesisi90K → A: Abolishes binding to PtdIns(4,5)P2. 1 Publication1
Mutagenesisi122S → T: Abolishes LDLR endocytosis. 2 Publications1
Mutagenesisi122S → Y: Impairs LDLR endocytosis. 2 Publications1
Mutagenesisi255F → V: Abolishes interaction with ITSN1, fails to internalize integrin beta-1; when associated with V-398, V-589, V-736 and V-765. 1 Publication1
Mutagenesisi294P → A: Loss of interaction with FCHO2; when associated with A-299. 1 Publication1
Mutagenesisi299P → A: Loss of interaction with FCHO2; when associated with A-294. 1 Publication1
Mutagenesisi398F → V: Abolishes interaction with ITSN1, fails to internalize integrin beta-1; when associated with V-255, V-589, V-736 and V-765. 1 Publication1
Mutagenesisi589F → 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. 1 Publication1
Mutagenesisi736F → 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. 1 Publication1
Mutagenesisi765F → 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. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000797712 – 766Disabled homolog 2Add BLAST765

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei2PhosphoserineBy similarity1
Modified residuei170PhosphotyrosineCombined sources1
Modified residuei193PhosphoserineCombined sources1
Modified residuei323PhosphoserineCombined sources1
Modified residuei326Phosphoserine; in mitosisBy similarity1
Modified residuei328Phosphoserine; in mitosisBy similarity1
Modified residuei401PhosphoserineBy similarity1
Modified residuei671PhosphothreonineCombined sources1
Modified residuei727PhosphoserineCombined sources1
Modified residuei759PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated on serine residues in response to mitogenic growth-factor stimulation. Phosphorylation during mitosis is leading to membrane displacement (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP98078.
PaxDbiP98078.
PeptideAtlasiP98078.
PRIDEiP98078.

PTM databases

iPTMnetiP98078.
PhosphoSitePlusiP98078.
SwissPalmiP98078.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

At E6.5 specifically expressed in the cells of the visceral endoderm.2 Publications

Gene expression databases

BgeeiENSMUSG00000022150.
CleanExiMM_DAB2.

Interactioni

Subunit structurei

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.Curated14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AP2A2O949732EBI-1391846,EBI-1642835From a different organism.
Axin1O356254EBI-1391846,EBI-2365912
DVL3Q929972EBI-1391846,EBI-739789From a different organism.
Eps15P425672EBI-1391846,EBI-443923
Eps15l1Q609022EBI-1391846,EBI-443931
FCHO2Q0JRZ94EBI-1391846,EBI-2609756From a different organism.
GRB2P629934EBI-1391846,EBI-401755From a different organism.
Grb2Q606314EBI-1391846,EBI-1688
MYO6Q9I8D12EBI-1391846,EBI-6307292From a different organism.
MYO6Q9UM544EBI-1391846,EBI-350606From a different organism.
Necap1Q9CR952EBI-1391846,EBI-7592476
NostrinQ6WKZ72EBI-1391846,EBI-1391878
Pias2Q8C5D83EBI-6305891,EBI-6305825
SH3KBP1Q96B979EBI-1391846,EBI-346595From a different organism.

GO - Molecular functioni

  • AP-2 adaptor complex binding Source: UniProtKB
  • clathrin adaptor activity Source: UniProtKB
  • clathrin binding Source: UniProtKB
  • integrin binding Source: UniProtKB
  • protein C-terminus binding Source: MGI
  • SMAD binding Source: MGI

Protein-protein interaction databases

BioGridi199043. 11 interactors.
DIPiDIP-39422N.
IntActiP98078. 52 interactors.
MINTiMINT-259116.
STRINGi10090.ENSMUSP00000079689.

Structurei

Secondary structure

1766
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi36 – 43Combined sources8
Beta strandi48 – 63Combined sources16
Helixi66 – 84Combined sources19
Turni85 – 87Combined sources3
Beta strandi91 – 98Combined sources8
Beta strandi101 – 106Combined sources6
Turni107 – 109Combined sources3
Beta strandi112 – 116Combined sources5
Helixi118 – 120Combined sources3
Beta strandi121 – 126Combined sources6
Beta strandi133 – 140Combined sources8
Beta strandi144 – 153Combined sources10
Helixi156 – 177Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M7EX-ray2.45A/B/C33-191[»]
1P3RX-ray2.10A/B/C32-191[»]
ProteinModelPortaliP98078.
SMRiP98078.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP98078.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini45 – 196PIDPROSITE-ProRule annotationAdd BLAST152

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni230 – 447Required for localization to clathrin-coated pitsAdd BLAST218
Regioni600 – 730Sufficient for interaction with GRB21 PublicationAdd BLAST131
Regioni617 – 625Required for interaction with CSKBy similarity9
Regioni647 – 766Required for interaction with MYO61 PublicationAdd BLAST120
Regioni661 – 669Required for interaction with GRB2 and CSKBy similarity9
Regioni707 – 723Sufficient for interaction with SH3KBP1 SH3 domainAdd BLAST17

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi293 – 295DPF 13
Motifi298 – 300DPF 23

Domaini

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 (PubMed:11247302, PubMed:12234931).2 Publications
The Asn-Pro-Phe (NPF) motifs, which are found in proteins involved in the endocytic pathway, mediate the interaction with the EH domain of EPS15, EPS15R and ITSN1.1 Publication

Sequence similaritiesi

Contains 1 PID domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3535. Eukaryota.
ENOG410XZ1H. LUCA.
HOGENOMiHOG000060158.
HOVERGENiHBG018945.
InParanoidiP98078.
KOiK12475.
PhylomeDBiP98078.
TreeFamiTF316724.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR006020. PTB/PI_dom.
[Graphical view]
PfamiPF00640. PID. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS01179. PID. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform p96 (identifier: P98078-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSNEVETSTT NGQPDQQAAP KAPSKKEKKK GSEKTDEYLL ARFKGDGVKY
60 70 80 90 100
KAKLIGIDDV PDARGDKMSQ DSMMKLKGMA AAGRSQGQHK QRIWVNISLS
110 120 130 140 150
GIKIIDEKTG VIEHEHPVNK ISFIARDVTD NRAFGYVCGG EGQHQFFAIK
160 170 180 190 200
TGQQAEPLVV DLKDLFQVIY NVKKKEEDKK KVEEANKAEE NGSEALMTLD
210 220 230 240 250
DQANKLKLGV DQMDLFGDMS TPPDLNSPTE SKDILLVDLN SEIDTNQNSL
260 270 280 290 300
RENPFLTNGV TSCSLPRPKP QASFLPENAF SANLNFFPTP NPDPFRDDPF
310 320 330 340 350
AQPDQSAPSS FDSLTSPDQK KASLSSSSTP QSKGPLNGDT DYFGQQFDQL
360 370 380 390 400
SNRTGKPEAQ GGPWPYPSSQ TQQAVRTQNG VSEREQNGFH IKSSPNPFVG
410 420 430 440 450
SPPKGLSVPN GVKQDLESSV QSSAHDSIAI IPPPQSTKPG RGRRTAKSSA
460 470 480 490 500
NDLLASDIFA SEPPGQMSPT GQPAVPQSNF LDLFKGNAPA PVGPLVGLGT
510 520 530 540 550
VPVTPPQAGP WTPVVYSPST TVVPGAIISG QPPSFRQPLV FGTTPAVQVW
560 570 580 590 600
NQSPSFATPA SPPPPTVWCP TTSVAPNAWS STSPLGNPFQ SNNIFPPPTM
610 620 630 640 650
STQSSPQPMM SSVLATPPQP PPRNGPLKDI PSDAFTGLDP LGDKEVKEVK
660 670 680 690 700
EMFKDFQLRQ PPLVPSRKGE TPPSGTSSAF SSYFNNKVGI PQEHVDHDDF
710 720 730 740 750
DANQLLNKIN EPPKPAPRQG VLLGTKSADN SLENPFSKGF SSSNPSVVSQ
760
PASSDPHRSP FGNPFA
Length:766
Mass (Da):82,312
Last modified:January 10, 2006 - v2
Checksum:i856C946BD43C4B07
GO
Isoform p93 (identifier: P98078-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     209-229: Missing.

Show »
Length:745
Mass (Da):80,092
Checksum:iB47489C90FF80532
GO
Isoform p67 (identifier: P98078-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     230-447: Missing.

Show »
Length:548
Mass (Da):58,822
Checksum:iC21F04C80C860424
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10T → A in AAH06588 (PubMed:15489334).Curated1
Sequence conflicti224D → G in AAH06588 (PubMed:15489334).Curated1
Sequence conflicti338G → V in AAB02646 (PubMed:7775479).Curated1
Sequence conflicti338G → V in AAB02645 (PubMed:7775479).Curated1
Sequence conflicti454L → P in AAB02645 (PubMed:7775479).Curated1
Sequence conflicti454L → P in AAB02646 (PubMed:7775479).Curated1
Sequence conflicti454L → P in AAB02647 (PubMed:7775479).Curated1
Sequence conflicti454L → P in AAG44669 (PubMed:11368898).Curated1
Sequence conflicti490A → P in AAB02645 (PubMed:7775479).Curated1
Sequence conflicti490A → P in AAB02646 (PubMed:7775479).Curated1
Sequence conflicti490A → P in AAB02647 (PubMed:7775479).Curated1
Sequence conflicti490A → P in AAG44669 (PubMed:11368898).Curated1
Sequence conflicti536R → G in BAE32784 (PubMed:16141072).Curated1
Sequence conflicti536R → G in AAH16887 (PubMed:15489334).Curated1
Sequence conflicti536R → G in AAH06588 (PubMed:15489334).Curated1
Sequence conflicti553S → P in AAH06588 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_004182209 – 229Missing in isoform p93. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_004183230 – 447Missing in isoform p67. 2 PublicationsAdd BLAST218

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS37029.1. [P98078-1]
CCDS37030.1. [P98078-3]
CCDS79357.1. [P98078-2]
RefSeqiNP_001008702.1. NM_001008702.2.
NP_001032994.1. NM_001037905.3.
NP_075607.2. NM_023118.5.
XP_011243626.1. XM_011245324.1.
XP_017171913.1. XM_017316424.1.
UniGeneiMm.240830.

Genome annotation databases

GeneIDi13132.
KEGGimmu:13132.
UCSCiuc007vde.1. mouse. [P98078-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS37029.1. [P98078-1]
CCDS37030.1. [P98078-3]
CCDS79357.1. [P98078-2]
RefSeqiNP_001008702.1. NM_001008702.2.
NP_001032994.1. NM_001037905.3.
NP_075607.2. NM_023118.5.
XP_011243626.1. XM_011245324.1.
XP_017171913.1. XM_017316424.1.
UniGeneiMm.240830.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M7EX-ray2.45A/B/C33-191[»]
1P3RX-ray2.10A/B/C32-191[»]
ProteinModelPortaliP98078.
SMRiP98078.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199043. 11 interactors.
DIPiDIP-39422N.
IntActiP98078. 52 interactors.
MINTiMINT-259116.
STRINGi10090.ENSMUSP00000079689.

PTM databases

iPTMnetiP98078.
PhosphoSitePlusiP98078.
SwissPalmiP98078.

Proteomic databases

MaxQBiP98078.
PaxDbiP98078.
PeptideAtlasiP98078.
PRIDEiP98078.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi13132.
KEGGimmu:13132.
UCSCiuc007vde.1. mouse. [P98078-1]

Organism-specific databases

CTDi1601.
MGIiMGI:109175. Dab2.

Phylogenomic databases

eggNOGiKOG3535. Eukaryota.
ENOG410XZ1H. LUCA.
HOGENOMiHOG000060158.
HOVERGENiHBG018945.
InParanoidiP98078.
KOiK12475.
PhylomeDBiP98078.
TreeFamiTF316724.

Miscellaneous databases

ChiTaRSiDab2. mouse.
EvolutionaryTraceiP98078.
PROiP98078.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022150.
CleanExiMM_DAB2.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR006020. PTB/PI_dom.
[Graphical view]
PfamiPF00640. PID. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS01179. PID. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDAB2_MOUSE
AccessioniPrimary (citable) accession number: P98078
Secondary accession number(s): Q3U3K1, Q91W56, Q923E1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 10, 2006
Last modified: November 2, 2016
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.