Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Disabled homolog 2

Gene

DAB2

Organism
Homo sapiens (Human)
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. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. 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. May act as a tumor suppressor.8 Publications

GO - Molecular functioni

  • cargo receptor activity Source: UniProtKB
  • clathrin adaptor activity Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • SMAD binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell proliferation Source: ProtInc
  • leading edge cell differentiation Source: UniProtKB
  • multicellular organism development Source: UniProtKB-KW
  • negative regulation of androgen receptor signaling pathway Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
  • negative regulation of protein binding Source: BHF-UCL
  • negative regulation of protein localization to plasma membrane Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: BHF-UCL
  • 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: UniProtKB
  • positive regulation of endocytosis Source: UniProtKB
  • positive regulation of epithelial to mesenchymal transition Source: UniProtKB
  • positive regulation of pathway-restricted SMAD protein phosphorylation Source: UniProtKB
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
  • positive regulation of protein phosphorylation Source: BHF-UCL
  • positive regulation of SMAD protein import into nucleus Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: BHF-UCL
  • positive regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
  • positive regulation of Wnt signaling pathway, planar cell polarity pathway Source: BHF-UCL
  • 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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000153071-MONOMER.
ReactomeiR-HSA-190873. Gap junction degradation.
R-HSA-196025. Formation of annular gap junctions.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
SignaLinkiP98082.
SIGNORiP98082.

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
Differentially-expressed protein 2
Gene namesi
Name:DAB2
Synonyms:DOC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:2662. DAB2.

Subcellular locationi

GO - Cellular componenti

  • clathrin-coated pit Source: UniProtKB
  • clathrin-coated vesicle Source: UniProtKB
  • clathrin-coated vesicle membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • lysosomal membrane Source: Reactome
  • nucleolus Source: HPA
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Cytoplasm, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi166F → A: Impairs TGF-beta receptor signaling, no effect on interaction with SMAD2. 1 Publication1
Mutagenesisi684 – 686SYF → AAA: Greatly reduced binding to MYO6. 1 Publication3
Mutagenesisi720R → A: Abolishes interaction with SH3KBP1. 1 Publication1

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNETi1601.
OpenTargetsiENSG00000153071.
PharmGKBiPA27132.

Polymorphism and mutation databases

BioMutaiDAB2.
DMDMi145559465.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000797702 – 770Disabled homolog 2Add BLAST769

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineBy similarity1
Modified residuei170PhosphotyrosineBy similarity1
Modified residuei193PhosphoserineBy similarity1
Modified residuei326Phosphoserine; in mitosisBy similarity1
Modified residuei328Phosphoserine; in mitosisBy similarity1
Modified residuei401PhosphoserineCombined sources1
Modified residuei675PhosphoserineCombined sources1
Modified residuei723PhosphoserineCombined sources1
Modified residuei729PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated. Phosphorylation during mitosis is leading to membrane displacement (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP98082.
MaxQBiP98082.
PaxDbiP98082.
PeptideAtlasiP98082.
PRIDEiP98082.

PTM databases

iPTMnetiP98082.
PhosphoSitePlusiP98082.

Expressioni

Tissue specificityi

Expressed in deep invaginations, inclusion cysts and the surface epithelial cells of the ovary. Also expressed in breast epithelial cells, spleen, thymus, prostate, testis, macrophages, fibroblasts, lung epithelial cells, placenta, brain stem, heart and small intestine. Expressed in kidney proximal tubular epithelial cells (at protein level).3 Publications

Gene expression databases

BgeeiENSG00000153071.
CleanExiHS_DAB2.
ExpressionAtlasiP98082. baseline and differential.
GenevisibleiP98082. HS.

Organism-specific databases

HPAiCAB009314.
HPA028888.

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, EPS15, ITSN1 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. 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.Curated9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GRB2P629932EBI-1171238,EBI-401755
LRP6O7558120EBI-1171238,EBI-910915
MYO6Q9UM543EBI-1171238,EBI-350606
NCK1P163332EBI-1171238,EBI-389883
SMAD2Q157964EBI-1171238,EBI-1040141
SMAD3P840223EBI-1171238,EBI-347161

GO - Molecular functioni

  • clathrin adaptor activity Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • SMAD binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107971. 94 interactors.
DIPiDIP-45617N.
IntActiP98082. 57 interactors.
MINTiMINT-5006053.
STRINGi9606.ENSP00000313391.

Structurei

Secondary structure

1770
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 31Combined sources3
Helixi39 – 43Combined sources5
Turni44 – 46Combined sources3
Helixi47 – 55Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LSWNMR-A24-58[»]
ProteinModelPortaliP98082.
SMRiP98082.
ModBaseiSearch...
MobiDBiSearch...

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 pitsBy similarityAdd BLAST218
Regioni604 – 732Sufficient for interaction with GRB2By similarityAdd BLAST129
Regioni619 – 627Required for interaction with CSKBy similarity9
Regioni649 – 770Required for interaction with MYO6By similarityAdd BLAST122
Regioni663 – 671Required for interaction with GRB2 and CSKBy similarity9
Regioni709 – 725Sufficient for interaction with SH3KBP1 SH3 domainBy similarityAdd 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.By similarity
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.By similarity

Sequence similaritiesi

Contains 1 PID domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3535. Eukaryota.
ENOG410XZ1H. LUCA.
GeneTreeiENSGT00520000055585.
HOGENOMiHOG000060158.
HOVERGENiHBG018945.
InParanoidiP98082.
KOiK12475.
OMAiIPQENAD.
OrthoDBiEOG091G0382.
PhylomeDBiP98082.
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 1 (identifier: P98082-1) [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
MSNEVETSAT NGQPDQQAAP KAPSKKEKKK GPEKTDEYLL 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 NVKKKEEEKK KIEEASKAVE NGSEALMILD
210 220 230 240 250
DQTNKLKSGV DQMDLFGDMS TPPDLNSPTE SKDILLVDLN SEIDTNQNSL
260 270 280 290 300
RENPFLTNGI TSCSLPRPTP QASFLPENAF SANLNFFPTP NPDPFRDDPF
310 320 330 340 350
TQPDQSTPSS FDSLKSPDQK KENSSSSSTP LSNGPLNGDV DYFGQQFDQI
360 370 380 390 400
SNRTGKQEAQ AGPWPFSSSQ TQPAVRTQNG VSEREQNGFS VKSSPNPFVG
410 420 430 440 450
SPPKGLSIQN GVKQDLESSV QSSPHDSIAI IPPPQSTKPG RGRRTAKSSA
460 470 480 490 500
NDLLASDIFA PPVSEPSGQA SPTGQPTALQ PNPLDLFKTS APAPVGPLVG
510 520 530 540 550
LGGVTVTLPQ AGPWNTASLV FNQSPSMAPG AMMGGQPSGF SQPVIFGTSP
560 570 580 590 600
AVSGWNQPSP FAASTPPPVP VVWGPSASVA PNAWSTTSPL GNPFQSNIFP
610 620 630 640 650
APAVSTQPPS MHSSLLVTPP QPPPRAGPPK DISSDAFTAL DPLGDKEIKD
660 670 680 690 700
VKEMFKDFQL RQPPAVPARK GEQTSSGTLS AFASYFNSKV GIPQENADHD
710 720 730 740 750
DFDANQLLNK INEPPKPAPR QVSLPVTKST DNAFENPFFK DSFGSSQASV
760 770
ASSQPVSSEM YRDPFGNPFA
Length:770
Mass (Da):82,448
Last modified:April 17, 2007 - v3
Checksum:i5B2F8B510A580A77
GO
Isoform 2 (identifier: P98082-2) [UniParc]FASTAAdd to basket

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

Show »
Length:552
Mass (Da):58,861
Checksum:i2F25868284E3757F
GO
Isoform 3 (identifier: P98082-3) [UniParc]FASTAAdd to basket

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

Show »
Length:749
Mass (Da):80,228
Checksum:iD52B66BB7CA45240
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti44 – 47KGDG → PRVC in AAA93195 (PubMed:8314147).Curated4
Sequence conflicti82A → R in AAC50824 (PubMed:8660969).Curated1
Sequence conflicti82A → R in AAB19032 (PubMed:8660969).Curated1
Sequence conflicti82A → R in AAA98975 (PubMed:9620555).Curated1
Sequence conflicti82A → R in AAF23161 (PubMed:11161789).Curated1
Sequence conflicti82A → R in AAA93195 (PubMed:8314147).Curated1
Sequence conflicti148A → T in AAA98975 (PubMed:9620555).Curated1
Sequence conflicti197M → R in AAA98975 (PubMed:9620555).Curated1
Sequence conflicti230 – 232ESK → VCF in AAF05540 (PubMed:10340382).Curated3
Sequence conflicti230 – 232ESK → VCF in AAA93195 (PubMed:8314147).Curated3
Sequence conflicti275L → S in AAC50824 (PubMed:8660969).Curated1
Sequence conflicti302 – 304QPD → HTR in AAA93195 (PubMed:8314147).Curated3
Sequence conflicti498L → Q in AAF05540 (PubMed:10340382).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031705586T → I.Corresponds to variant rs700241dbSNPEnsembl.1
Natural variantiVAR_050942634S → N.Corresponds to variant rs3733801dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_038401209 – 229Missing in isoform 3. 2 PublicationsAdd BLAST21
Alternative sequenceiVSP_004181230 – 447Missing in isoform 2. CuratedAdd BLAST218

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39050 mRNA. Translation: AAC50824.1.
AH003698 Genomic DNA. Translation: AAB19032.1.
U53446 mRNA. Translation: AAA98975.1.
AF188298 mRNA. Translation: AAF05540.1.
AF205890 Genomic DNA. Translation: AAF23161.1.
AC008916 Genomic DNA. No translation available.
CH471119 Genomic DNA. Translation: EAW55989.1.
BC003064 mRNA. Translation: AAH03064.1.
L16886 mRNA. Translation: AAA93195.1.
CCDSiCCDS34149.1. [P98082-1]
CCDS58946.1. [P98082-3]
PIRiG02228.
RefSeqiNP_001231800.1. NM_001244871.1. [P98082-3]
NP_001334.2. NM_001343.3. [P98082-1]
UniGeneiHs.696631.

Genome annotation databases

EnsembliENST00000320816; ENSP00000313391; ENSG00000153071. [P98082-1]
ENST00000339788; ENSP00000345508; ENSG00000153071. [P98082-2]
ENST00000509337; ENSP00000426245; ENSG00000153071. [P98082-3]
ENST00000545653; ENSP00000439919; ENSG00000153071. [P98082-3]
GeneIDi1601.
KEGGihsa:1601.
UCSCiuc003jlw.4. human. [P98082-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39050 mRNA. Translation: AAC50824.1.
AH003698 Genomic DNA. Translation: AAB19032.1.
U53446 mRNA. Translation: AAA98975.1.
AF188298 mRNA. Translation: AAF05540.1.
AF205890 Genomic DNA. Translation: AAF23161.1.
AC008916 Genomic DNA. No translation available.
CH471119 Genomic DNA. Translation: EAW55989.1.
BC003064 mRNA. Translation: AAH03064.1.
L16886 mRNA. Translation: AAA93195.1.
CCDSiCCDS34149.1. [P98082-1]
CCDS58946.1. [P98082-3]
PIRiG02228.
RefSeqiNP_001231800.1. NM_001244871.1. [P98082-3]
NP_001334.2. NM_001343.3. [P98082-1]
UniGeneiHs.696631.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LSWNMR-A24-58[»]
ProteinModelPortaliP98082.
SMRiP98082.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107971. 94 interactors.
DIPiDIP-45617N.
IntActiP98082. 57 interactors.
MINTiMINT-5006053.
STRINGi9606.ENSP00000313391.

PTM databases

iPTMnetiP98082.
PhosphoSitePlusiP98082.

Polymorphism and mutation databases

BioMutaiDAB2.
DMDMi145559465.

Proteomic databases

EPDiP98082.
MaxQBiP98082.
PaxDbiP98082.
PeptideAtlasiP98082.
PRIDEiP98082.

Protocols and materials databases

DNASUi1601.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000320816; ENSP00000313391; ENSG00000153071. [P98082-1]
ENST00000339788; ENSP00000345508; ENSG00000153071. [P98082-2]
ENST00000509337; ENSP00000426245; ENSG00000153071. [P98082-3]
ENST00000545653; ENSP00000439919; ENSG00000153071. [P98082-3]
GeneIDi1601.
KEGGihsa:1601.
UCSCiuc003jlw.4. human. [P98082-1]

Organism-specific databases

CTDi1601.
DisGeNETi1601.
GeneCardsiDAB2.
HGNCiHGNC:2662. DAB2.
HPAiCAB009314.
HPA028888.
MIMi601236. gene.
neXtProtiNX_P98082.
OpenTargetsiENSG00000153071.
PharmGKBiPA27132.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3535. Eukaryota.
ENOG410XZ1H. LUCA.
GeneTreeiENSGT00520000055585.
HOGENOMiHOG000060158.
HOVERGENiHBG018945.
InParanoidiP98082.
KOiK12475.
OMAiIPQENAD.
OrthoDBiEOG091G0382.
PhylomeDBiP98082.
TreeFamiTF316724.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000153071-MONOMER.
ReactomeiR-HSA-190873. Gap junction degradation.
R-HSA-196025. Formation of annular gap junctions.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
SignaLinkiP98082.
SIGNORiP98082.

Miscellaneous databases

ChiTaRSiDAB2. human.
GeneWikiiDAB2.
GenomeRNAii1601.
PROiP98082.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000153071.
CleanExiHS_DAB2.
ExpressionAtlasiP98082. baseline and differential.
GenevisibleiP98082. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P98082
Secondary accession number(s): A6NES5
, Q13598, Q9BTY0, Q9UK04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: April 17, 2007
Last modified: November 2, 2016
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.