DAB2IP

Functionⁱ

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. Plays also 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 proinflammatory 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-alpha-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. Mediates also 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) and Ras. 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. Functions also 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.10 Publications

Miscellaneous

The DAB2IP gene is found epigenetically silenced in numerous aggressive cancers, like prostate cancers and medulloblastoma tumors. Epigenetic suppression of DAB2IP by EZH2 is a major mechanism of DAB2IP inactivation in human prostate cancer and increases metastatic potential (PubMed:20154697, PubMed:22696229).2 Publications

GO - Molecular functionⁱ

14-3-3 protein binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 17389591
cadherin binding
Source: BHF-UCL
Inferred from high throughput direct assayⁱ
- 25468996
death receptor binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 15310755
GTPase activator activity Source: UniProtKB-KW
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 12813029
kinase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17389591
mitogen-activated protein kinase kinase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17389591
mitogen-activated protein kinase kinase kinase binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 12813029
phosphatidylinositol 3-kinase binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19033661
phosphatidylinositol 3-kinase regulatory subunit binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19903888
phosphatidylinositol-3-phosphate binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19948740
phosphatidylinositol-4-phosphate binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19948740
protein-containing complex binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19903888
protein homodimerization activity
Source: BHF-UCL
Inferred from physical interactionⁱ
- 12813029
protein kinase binding
Source: ParkinsonsUK-UCL
Inferred from direct assayⁱ
- 18281285
protein phosphatase 2A binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 20080667
SH3 domain binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19033661
- 19903888
signaling adaptor activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 20080667
vascular endothelial growth factor receptor 2 binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 19033661

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

activation of JUN kinase activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 12813029
activation of MAPKKK activity
Source: UniProtKB
Inferred from direct assayⁱ
- 19903888
angiogenesis Source: UniProtKB-KW
cell cycle Source: UniProtKB-KW
cell motility involved in cerebral cortex radial glia guided migration Source: UniProtKB
cellular protein catabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 17389591
cellular response to epidermal growth factor stimulus
Source: BHF-UCL
Inferred from sequence or structural similarityⁱ
- 11812785
cellular response to interleukin-1
Source: UniProtKB
Inferred from direct assayⁱ
- 19948740
cellular response to lipopolysaccharide
Source: UniProtKB
Inferred from direct assayⁱ
- 19948740
cellular response to tumor necrosis factor
Source: UniProtKB
Inferred from direct assayⁱ
- 17389591
cellular response to unfolded protein
Source: ParkinsonsUK-UCL
Traceable author statementⁱ
- 22013210
cellular response to vascular endothelial growth factor stimulus
Source: UniProtKB
Inferred from direct assayⁱ
- 19033661
endothelial cell apoptotic process
Source: BHF-UCL
Traceable author statementⁱ
- 19903888
extrinsic apoptotic signaling pathway via death domain receptors
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 19903888
I-kappaB phosphorylation Source: UniProtKB
inflammatory response Source: UniProtKB-KW
innate immune response Source: UniProtKB-KW
intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress
Source: BHF-UCL
Inferred from sequence or structural similarityⁱ
- 18281285
layer formation in cerebral cortex Source: UniProtKB
MAPK cascade Source: Reactome
negative regulation of angiogenesis
Source: UniProtKB
Inferred from direct assayⁱ
- 19033661
negative regulation of canonical Wnt signaling pathway
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 20080667
negative regulation of cell proliferation
Source: UniProtKB
Inferred from direct assayⁱ
- 19903888
negative regulation of cellular protein catabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 19903888
negative regulation of endothelial cell migration
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 19033661
negative regulation of epidermal growth factor receptor signaling pathway
Source: BHF-UCL
Inferred from sequence or structural similarityⁱ
- 11812785
negative regulation of epithelial cell migration
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20080667
negative regulation of epithelial cell proliferation
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 20154697
negative regulation of epithelial to mesenchymal transition
Source: UniProtKB
Inferred from direct assayⁱ
- 20154697
negative regulation of ERK1 and ERK2 cascade
Source: UniProtKB
Inferred from direct assayⁱ
- 19903888
negative regulation of fibroblast proliferation Source: BHF-UCL
negative regulation of G0 to G1 transition
Source: UniProtKB
Inferred from direct assayⁱ
- 19903888
negative regulation of GTPase activity
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 20154697
negative regulation of I-kappaB kinase/NF-kappaB signaling
Source: UniProtKB
Inferred from direct assayⁱ
- 17389591
negative regulation of MAP kinase activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 12813029
negative regulation of NF-kappaB transcription factor activity
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 20154697
negative regulation of phosphatidylinositol 3-kinase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 19903888
negative regulation of phosphatidylinositol 3-kinase signaling
Source: UniProtKB
Inferred from direct assayⁱ
- 19903888
negative regulation of protein phosphorylation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20080667
negative regulation of protein serine/threonine kinase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 19903888
negative regulation of Ras protein signal transduction
Source: BHF-UCL
Inferred by curatorⁱ
- 20154697
negative regulation of toll-like receptor 4 signaling pathway
Source: UniProtKB
Inferred from direct assayⁱ
- 19948740
negative regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20080667
negative regulation of transcription by RNA polymerase II
Source: BHF-UCL
Inferred from direct assayⁱ
- 15310755
negative regulation of vascular endothelial growth factor receptor signaling pathway
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 19033661
negative regulation of vascular endothelial growth factor signaling pathway Source: UniProtKB
neuron projection morphogenesis Source: UniProtKB
positive regulation of apoptotic process
Source: UniProtKB
Inferred from direct assayⁱ
- 17389591
- 19903888
positive regulation of apoptotic signaling pathway
Source: UniProtKB
Inferred from direct assayⁱ
- 19903888
positive regulation of cell cycle arrest
Source: UniProtKB
Inferred from direct assayⁱ
- 19903888
positive regulation of dendrite development Source: UniProtKB
positive regulation of IRE1-mediated unfolded protein response
Source: ParkinsonsUK-UCL
Traceable author statementⁱ
- 22013210
positive regulation of JNK cascade
Source: UniProtKB
Inferred from direct assayⁱ
- 17389591
- 19903888
positive regulation of JUN kinase activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 15310755
positive regulation of MAPK cascade
Source: UniProtKB
Inferred from direct assayⁱ
- 19903888
positive regulation of neuron migration Source: UniProtKB
positive regulation of neuron projection development Source: UniProtKB
positive regulation of proteasomal protein catabolic process
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20080667
positive regulation of protein catabolic process Source: UniProtKB
positive regulation of protein serine/threonine kinase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 19903888
positive regulation of synapse maturation Source: UniProtKB
positive regulation of transcription by RNA polymerase II
Source: UniProtKB
Inferred from direct assayⁱ
- 17389591
reelin-mediated signaling pathway Source: InterPro
regulation of growth Source: UniProtKB-KW
regulation of GTPase activity Source: UniProtKB
regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
regulation of p38MAPK cascade Source: UniProtKB
regulation of protein complex assembly
Source: UniProtKB
Inferred from direct assayⁱ
- 19948740
regulation of protein heterodimerization activity
Source: ParkinsonsUK-UCL
Inferred from direct assayⁱ
- 18281285
tube formation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 19033661
vascular endothelial growth factor receptor-2 signaling pathway Source: UniProtKB

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Developmental protein, GTPase activation
Biological process	Angiogenesis, Apoptosis, Cell cycle, Growth regulation, Immunity, Inflammatory response, Innate immunity, Stress response, Unfolded protein response

Enzyme and pathway databases

Reactomeⁱ	R-HSA-5658442 Regulation of RAS by GAPs R-HSA-6802949 Signaling by RAS mutants
SIGNORⁱ	Q5VWQ8

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Disabled homolog 2-interacting protein Short name: DAB2 interaction protein Short name: DAB2-interacting protein Alternative name(s): ASK-interacting protein 1 Short name: AIP-1 DOC-2/DAB-2 interactive protein
Gene namesⁱ	Name:DAB2IP Synonyms:AF9Q34, AIP1, KIAA1743
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 9

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000136848.16
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:17294 DAB2IP
MIMⁱ	609205 gene
neXtProtⁱ	NX_Q5VWQ8

Keywords - Cellular componentⁱ

Cell membrane, Cell projection, Cytoplasm, Membrane

Pathology & Biotechⁱ

Involvement in diseaseⁱ

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).1 Publication

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	228 – 230	KKK → AAA: Reduces interaction with KDR/VEGFR2. Does not inhibit interaction with MAP3K5. 2 Publications	3
Mutagenesisⁱ	281 – 284	KKKK → AAAA: Significantly reduces interaction with MAP3K5. Does not reduce interaction with KDR/VEGFR2. 2 Publications	4
Mutagenesisⁱ	413	R → L: Does not inhibit interaction with MAP3K5. Does not reduce GSK3B-induced beta-catenin transcription activity, TNF-alpha-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. 4 Publications	1
Mutagenesisⁱ	728	S → A: Inhibits phosphorylation and TNF-alpha-induced MAP3K5 dephosphorylation. Reduces interaction with 14-3-3 proteins, AKT1, a regulatory p85 subunit, MAP3K5, RIPK1, TRAF2 and TNF-alpha-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. 4 Publications	1
Mutagenesisⁱ	920 – 929	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. 1 Publication	10
Mutagenesisⁱ	935	T → A: Does not reduce interaction with 14-3-3 proteins. 1 Publication	1

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	172 – 173	Breakpoint for translocation to form KMT2A/MLL1-DAB2IP		2

Keywords - Diseaseⁱ

Tumor suppressor

Organism-specific databases

DisGeNET More...DisGeNETⁱ	153090
Open Targets More...OpenTargetsⁱ	ENSG00000136848
PharmGKBⁱ	PA27133

Polymorphism and mutation databases

DMDMⁱ	116247768

DMDMⁱ

116247768

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000252407	1 – 1189	Disabled homolog 2-interacting proteinAdd BLAST		1189

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	728	Phosphoserine; by MAP3K5 and RIPK12 Publications	1
Modified residueⁱ	747	PhosphoserineCombined sources	1
Modified residueⁱ	978	PhosphoserineCombined sources	1
Modified residueⁱ	995	PhosphoserineCombined sources	1

Post-translational modificationⁱ

In response to TNF-alpha-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.2 Publications

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

EPDⁱ	Q5VWQ8
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q5VWQ8
PaxDbⁱ	Q5VWQ8
PeptideAtlas More...PeptideAtlasⁱ	Q5VWQ8
PRIDEⁱ	Q5VWQ8
ProteomicsDBⁱ	65554 65555 [Q5VWQ8-2] 65556 [Q5VWQ8-3] 65557 [Q5VWQ8-4]

PTM databases

CarbonylDBⁱ	Q5VWQ8
iPTMnetⁱ	Q5VWQ8
PhosphoSitePlusⁱ	Q5VWQ8

Expressionⁱ

Tissue specificityⁱ

Expressed in endothelial and vascular smooth muscle cells (VSMCs). Expressed in prostate epithelial but poorly in prostate cancer cells. Poorly expressed in medulloblastoma cells compared to cerebellar precursor proliferating progenitor cells (at protein level). Low expression in prostate. Down-regulated in prostate cancer.4 Publications

Inductionⁱ

Down-regulated in prostate cancer and medulloblastoma.2 Publications

Gene expression databases

Bgeeⁱ	ENSG00000136848 Expressed in 193 organ(s), highest expression level in cerebellum
CleanExⁱ	HS_DAB2IP
ExpressionAtlasⁱ	Q5VWQ8 baseline and differential
Genevisibleⁱ	Q5VWQ8 HS

Interactionⁱ

Subunit structureⁱ

On plasma membrane, exists in an inactive form complexed with TNFR1; in response to TNF-alpha, dissociates from TNFR1 complex, translocates to cytoplasm and forms part of an intracellular signaling complex comprising TRADD, RALBP1, TRAF2 and MAP3K5. Interacts with DAB1. Interacts (via NPXY motif) with DAB2 (via PID domain). Interacts (via PH domain) with ERN1 (By similarity). Part of a cytoplasmic complex made of HIPK1, DAB2IP and MAP3K5 in response to TNF-alpha; this complex formation promotes MAP3K5-JNK activation and subsequent apoptosis. Interacts (via N-terminal domain) with JAK2; the interaction occurs in a IFNG/IFN-gamma-dependent manner and inhibits JAK2 autophosphorylation activity. Interacts (via C2 domain) with GSK3B; the interaction stimulates GSK3B kinase activation. Interacts (via C2 domain) with PPP2CA. Interacts (via proline-rich motif) with a regulatory p85 subunit (via SH3 domain) of the PI3K complex; the interaction inhibits the PI3K-AKT complex activity in a TNF-alpha-dependent manner in prostate cancer (PCa) cells. Interacts with AKT1; the interaction is increased in a TNF-alpha-induced manner. Interacts (via C2 domain and active form preferentially) with KDR/VEGFR2 (tyrosine-phosphorylated active form preferentially); the interaction occurs at the late phase of VEGFA response and inhibits KDR/VEGFR2 activity. Interacts (via N-terminus C2 domain) with MAP3K5 ('Ser-966' dephosphorylated form preferentially); the interaction occurs in a TNF-alpha-induced manner. Interacts (via Ras-GAP domain) with the catalytic subunit of protein phosphatase PP2A; the interaction occurs in resting endothelial cells, is further enhanced by TNF-alpha stimulation and is required to bridge PP2A to MAP3K5. Interacts (via C-terminus PER domain) with TRAF2 (via zinc fingers); the interaction occurs in a TNF-alpha-dependent manner. Interacts with 14-3-3 proteins; the interaction occurs in a TNF-alpha-dependent manner. Interacts (via Ras-GAP domain) with RIPK1 (via kinase domain); the interaction occurs in a TNF-alpha-dependent manner.By similarity9 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
itself		2	EBI-2871881,EBI-2871881
AXIN1	O15169	2	EBI-9543020,EBI-710484
GSK3B	P49841	2	EBI-2871881,EBI-373586
MAP3K5	Q99683	2	EBI-2871881,EBI-476263

GO - Molecular functionⁱ

14-3-3 protein binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 17389591
cadherin binding
Source: BHF-UCL
Inferred from high throughput direct assayⁱ
- 25468996
death receptor binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 15310755
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 12813029
kinase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17389591
mitogen-activated protein kinase kinase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17389591
mitogen-activated protein kinase kinase kinase binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 12813029
phosphatidylinositol 3-kinase binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19033661
phosphatidylinositol 3-kinase regulatory subunit binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19903888
protein homodimerization activity
Source: BHF-UCL
Inferred from physical interactionⁱ
- 12813029
protein kinase binding
Source: ParkinsonsUK-UCL
Inferred from direct assayⁱ
- 18281285
protein phosphatase 2A binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 20080667
SH3 domain binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19033661
- 19903888
vascular endothelial growth factor receptor 2 binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 19033661

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	127478, 44 interactors
Database of interacting proteins More...DIPⁱ	DIP-41721N
IntActⁱ	Q5VWQ8, 7 interactors
STRINGⁱ	9606.ENSP00000259371

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q5VWQ8
SMRⁱ	Q5VWQ8
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	101 – 202	PHPROSITE-ProRule annotationAdd BLAST	102
Domainⁱ	200 – 295	C2Add BLAST	96
Domainⁱ	371 – 563	Ras-GAPPROSITE-ProRule annotationAdd BLAST	193

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	646 – 943	Necessary for interaction with AKT11 PublicationAdd BLAST		298

Coiled coil

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Coiled coilⁱ	1026 – 1159	Sequence analysisAdd BLAST		134

Compositional bias

Feature key	Position(s)	DescriptionActions	Length
Compositional biasⁱ	8 – 52	Arg-richAdd BLAST	45
Compositional biasⁱ	112 – 117	Poly-Ala	6
Compositional biasⁱ	867 – 870	Poly-Ala	4
Compositional biasⁱ	903 – 948	Pro-richAdd BLAST	46

Domainⁱ

The C2 and Ras-GAP domains constitutively bind to MAP3K5 and facilitate the release of 14-3-3 proteins from MAP3K5. The PH and Ras-GAP domains, but not the NPXY motif, are crucial for its cell membrane localization and neuronal migration function. The PH domain is necessary but not sufficient to activate the JNK signaling pathway through ERN1 (By similarity). Exists in a closed inactive form by an intramolecular interaction between the N- and the C-terminal domains. The proline-rich motif is critical both for PI3K-AKT activity inhibition and MAP3K5 activation. The PH and C2 domains are necessary for the binding to phosphatidylinositol phosphate. The Ras-GAP domain is necessary for its tumor-suppressive function.By similarity

Keywords - Domainⁱ

Coiled coil

Phylogenomic databases

eggNOGⁱ	KOG3508 Eukaryota ENOG410XPU1 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000119092
HOVERGENⁱ	HBG006492
InParanoidⁱ	Q5VWQ8
KEGG Orthology (KO) More...KOⁱ	K19901
OMAⁱ	NNYMVLC
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G00ZZ
PhylomeDBⁱ	Q5VWQ8
TreeFamⁱ	TF105303

Family and domain databases

Gene3Dⁱ	2.30.29.30, 1 hit 2.60.40.150, 1 hit
InterProⁱ	View protein in InterPro IPR000008 C2_dom IPR035892 C2_domain_sf IPR030403 DAB2IP IPR021887 DUF3498 IPR011993 PH-like_dom_sf IPR001849 PH_domain IPR039360 Ras_GTPase IPR023152 RasGAP_CS IPR001936 RasGAP_dom IPR008936 Rho_GTPase_activation_prot
PANTHERⁱ	PTHR10194 PTHR10194, 1 hit PTHR10194:SF26 PTHR10194:SF26, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00168 C2, 1 hit PF12004 DUF3498, 1 hit PF00616 RasGAP, 2 hits
SMARTⁱ	View protein in SMART SM00239 C2, 1 hit SM00233 PH, 1 hit SM00323 RasGAP, 1 hit
SUPFAMⁱ	SSF48350 SSF48350, 1 hit
PROSITEⁱ	View protein in PROSITE PS50003 PH_DOMAIN, 1 hit PS00509 RAS_GTPASE_ACTIV_1, 1 hit PS50018 RAS_GTPASE_ACTIV_2, 1 hit

Sequences (5+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 5 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 5 described isoforms and 3 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q5VWQ8-1) [UniParc]FASTA Add 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
MSAGGSARKS TGRSSYYYRL LRRPRLQRQR SRSRSRTRPA RESPQERPGS 
        60         70         80         90        100
RRSLPGSLSE KSPSMEPSAA TPFRVTGFLS RRLKGSIKRT KSQPKLDRNH 
       110        120        130        140        150
SFRHILPGFR SAAAAAADNE RSHLMPRLKE SRSHESLLSP SSAVEALDLS 
       160        170        180        190        200
MEEEVVIKPV HSSILGQDYC FEVTTSSGSK CFSCRSAAER DKWMENLRRA 
       210        220        230        240        250
VHPNKDNSRR VEHILKLWVI EAKDLPAKKK YLCELCLDDV LYARTTGKLK 
       260        270        280        290        300
TDNVFWGEHF EFHNLPPLRT VTVHLYRETD KKKKKERNSY LGLVSLPAAS 
       310        320        330        340        350
VAGRQFVEKW YPVVTPNPKG GKGPGPMIRI KARYQTITIL PMEMYKEFAE 
       360        370        380        390        400
HITNHYLGLC AALEPILSAK TKEEMASALV HILQSTGKVK DFLTDLMMSE 
       410        420        430        440        450
VDRCGDNEHL IFRENTLATK AIEEYLKLVG QKYLQDALGE FIKALYESDE 
       460        470        480        490        500
NCEVDPSKCS AADLPEHQGN LKMCCELAFC KIINSYCVFP RELKEVFASW 
       510        520        530        540        550
RQECSSRGRP DISERLISAS LFLRFLCPAI MSPSLFNLLQ EYPDDRTART 
       560        570        580        590        600
LTLIAKVTQN LANFAKFGSK EEYMSFMNQF LEHEWTNMQR FLLEISNPET 
       610        620        630        640        650
LSNTAGFEGY IDLGRELSSL HSLLWEAVSQ LEQSIVSKLG PLPRILRDVH 
       660        670        680        690        700
TALSTPGSGQ LPGTNDLAST PGSGSSSISA GLQKMVIEND LSGLIDFTRL 
       710        720        730        740        750
PSPTPENKDL FFVTRSSGVQ PSPARSSSYS EANEPDLQMA NGGKSLSMVD 
       760        770        780        790        800
LQDARTLDGE AGSPAGPDVL PTDGQAAAAQ LVAGWPARAT PVNLAGLATV 
       810        820        830        840        850
RRAGQTPTTP GTSEGAPGRP QLLAPLSFQN PVYQMAAGLP LSPRGLGDSG 
       860        870        880        890        900
SEGHSSLSSH SNSEELAAAA KLGSFSTAAE ELARRPGELA RRQMSLTEKG 
       910        920        930        940        950
GQPTVPRQNS AGPQRRIDQP PPPPPPPPPA PRGRTPPNLL STLQYPRPSS 
       960        970        980        990       1000
GTLASASPDW VGPSTRLRQQ SSSSKGDSPE LKPRAVHKQG PSPVSPNALD 
      1010       1020       1030       1040       1050
RTAAWLLTMN AQLLEDEGLG PDPPHRDRLR SKDELSQAEK DLAVLQDKLR 
      1060       1070       1080       1090       1100
ISTKKLEEYE TLFKCQEETT QKLVLEYQAR LEEGEERLRR QQEDKDIQMK 
      1110       1120       1130       1140       1150
GIISRLMSVE EELKKDHAEM QAAVDSKQKI IDAQEKRIAS LDAANARLMS 
      1160       1170       1180 
ALTQLKERYS MQARNGISPT NPTKLQITEN GEFRNSSNC

Note: Gene prediction based on EST data.

Length:1,189

Mass (Da):131,625

Last modified:October 17, 2006 - v2

Checksum:ⁱ7494FF05AACF3320

GO

Isoform 2 (identifier: Q5VWQ8-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-124: Missing.

« Hide

        10         20         30         40         50
MPRLKESRSH ESLLSPSSAV EALDLSMEEE VVIKPVHSSI LGQDYCFEVT 
        60         70         80         90        100
TSSGSKCFSC RSAAERDKWM ENLRRAVHPN KDNSRRVEHI LKLWVIEAKD 
       110        120        130        140        150
LPAKKKYLCE LCLDDVLYAR TTGKLKTDNV FWGEHFEFHN LPPLRTVTVH 
       160        170        180        190        200
LYRETDKKKK KERNSYLGLV SLPAASVAGR QFVEKWYPVV TPNPKGGKGP 
       210        220        230        240        250
GPMIRIKARY QTITILPMEM YKEFAEHITN HYLGLCAALE PILSAKTKEE 
       260        270        280        290        300
MASALVHILQ STGKVKDFLT DLMMSEVDRC GDNEHLIFRE NTLATKAIEE 
       310        320        330        340        350
YLKLVGQKYL QDALGEFIKA LYESDENCEV DPSKCSAADL PEHQGNLKMC 
       360        370        380        390        400
CELAFCKIIN SYCVFPRELK EVFASWRQEC SSRGRPDISE RLISASLFLR 
       410        420        430        440        450
FLCPAIMSPS LFNLLQEYPD DRTARTLTLI AKVTQNLANF AKFGSKEEYM 
       460        470        480        490        500
SFMNQFLEHE WTNMQRFLLE ISNPETLSNT AGFEGYIDLG RELSSLHSLL 
       510        520        530        540        550
WEAVSQLEQS IVSKLGPLPR ILRDVHTALS TPGSGQLPGT NDLASTPGSG 
       560        570        580        590        600
SSSISAGLQK MVIENDLSGL IDFTRLPSPT PENKDLFFVT RSSGVQPSPA 
       610        620        630        640        650
RSSSYSEANE PDLQMANGGK SLSMVDLQDA RTLDGEAGSP AGPDVLPTDG 
       660        670        680        690        700
QAAAAQLVAG WPARATPVNL AGLATVRRAG QTPTTPGTSE GAPGRPQLLA 
       710        720        730        740        750
PLSFQNPVYQ MAAGLPLSPR GLGDSGSEGH SSLSSHSNSE ELAAAAKLGS 
       760        770        780        790        800
FSTAAEELAR RPGELARRQM SLTEKGGQPT VPRQNSAGPQ RRIDQPPPPP 
       810        820        830        840        850
PPPPPAPRGR TPPNLLSTLQ YPRPSSGTLA SASPDWVGPS TRLRQQSSSS 
       860        870        880        890        900
KGDSPELKPR AVHKQGPSPV SPNALDRTAA WLLTMNAQLL EDEGLGPDPP 
       910        920        930        940        950
HRDRLRSKDE LSQAEKDLAV LQDKLRISTK KLEEYETLFK CQEETTQKLV 
       960        970        980        990       1000
LEYQARLEEG EERLRRQQED KDIQMKGIIS RLMSVEEELK KDHAEMQAAV 
      1010       1020       1030       1040       1050
DSKQKIIDAQ EKRIASLDAA NARLMSALTQ LKERYSMQAR NGISPTNPTK 
      1060 
LQITENGEFR NSSNC

Show »

Length:1,065

Mass (Da):117,651

Checksum:ⁱ4787F41F02108AA3

GO

Isoform 3 (identifier: Q5VWQ8-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-193: Missing.
1158-1189: RYSMQARNGISPTNPTKLQITENGEFRNSSNC → SMH

« Hide

        10         20         30         40         50
MENLRRAVHP NKDNSRRVEH ILKLWVIEAK DLPAKKKYLC ELCLDDVLYA 
        60         70         80         90        100
RTTGKLKTDN VFWGEHFEFH NLPPLRTVTV HLYRETDKKK KKERNSYLGL 
       110        120        130        140        150
VSLPAASVAG RQFVEKWYPV VTPNPKGGKG PGPMIRIKAR YQTITILPME 
       160        170        180        190        200
MYKEFAEHIT NHYLGLCAAL EPILSAKTKE EMASALVHIL QSTGKVKDFL 
       210        220        230        240        250
TDLMMSEVDR CGDNEHLIFR ENTLATKAIE EYLKLVGQKY LQDALGEFIK 
       260        270        280        290        300
ALYESDENCE VDPSKCSAAD LPEHQGNLKM CCELAFCKII NSYCVFPREL 
       310        320        330        340        350
KEVFASWRQE CSSRGRPDIS ERLISASLFL RFLCPAIMSP SLFNLLQEYP 
       360        370        380        390        400
DDRTARTLTL IAKVTQNLAN FAKFGSKEEY MSFMNQFLEH EWTNMQRFLL 
       410        420        430        440        450
EISNPETLSN TAGFEGYIDL GRELSSLHSL LWEAVSQLEQ SIVSKLGPLP 
       460        470        480        490        500
RILRDVHTAL STPGSGQLPG TNDLASTPGS GSSSISAGLQ KMVIENDLSG 
       510        520        530        540        550
LIDFTRLPSP TPENKDLFFV TRSSGVQPSP ARSSSYSEAN EPDLQMANGG 
       560        570        580        590        600
KSLSMVDLQD ARTLDGEAGS PAGPDVLPTD GQAAAAQLVA GWPARATPVN 
       610        620        630        640        650
LAGLATVRRA GQTPTTPGTS EGAPGRPQLL APLSFQNPVY QMAAGLPLSP 
       660        670        680        690        700
RGLGDSGSEG HSSLSSHSNS EELAAAAKLG SFSTAAEELA RRPGELARRQ 
       710        720        730        740        750
MSLTEKGGQP TVPRQNSAGP QRRIDQPPPP PPPPPPAPRG RTPPNLLSTL 
       760        770        780        790        800
QYPRPSSGTL ASASPDWVGP STRLRQQSSS SKGDSPELKP RAVHKQGPSP 
       810        820        830        840        850
VSPNALDRTA AWLLTMNAQL LEDEGLGPDP PHRDRLRSKD ELSQAEKDLA 
       860        870        880        890        900
VLQDKLRIST KKLEEYETLF KCQEETTQKL VLEYQARLEE GEERLRRQQE 
       910        920        930        940        950
DKDIQMKGII SRLMSVEEEL KKDHAEMQAA VDSKQKIIDA QEKRIASLDA 
       960 
ANARLMSALT QLKESMH

Show »

Length:967

Mass (Da):106,764

Checksum:ⁱE69CEB1FB00A2219

GO

Isoform 4 (identifier: Q5VWQ8-4) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-124: Missing.
1158-1189: RYSMQARNGISPTNPTKLQITENGEFRNSSNC → SMH

« Hide

        10         20         30         40         50
MPRLKESRSH ESLLSPSSAV EALDLSMEEE VVIKPVHSSI LGQDYCFEVT 
        60         70         80         90        100
TSSGSKCFSC RSAAERDKWM ENLRRAVHPN KDNSRRVEHI LKLWVIEAKD 
       110        120        130        140        150
LPAKKKYLCE LCLDDVLYAR TTGKLKTDNV FWGEHFEFHN LPPLRTVTVH 
       160        170        180        190        200
LYRETDKKKK KERNSYLGLV SLPAASVAGR QFVEKWYPVV TPNPKGGKGP 
       210        220        230        240        250
GPMIRIKARY QTITILPMEM YKEFAEHITN HYLGLCAALE PILSAKTKEE 
       260        270        280        290        300
MASALVHILQ STGKVKDFLT DLMMSEVDRC GDNEHLIFRE NTLATKAIEE 
       310        320        330        340        350
YLKLVGQKYL QDALGEFIKA LYESDENCEV DPSKCSAADL PEHQGNLKMC 
       360        370        380        390        400
CELAFCKIIN SYCVFPRELK EVFASWRQEC SSRGRPDISE RLISASLFLR 
       410        420        430        440        450
FLCPAIMSPS LFNLLQEYPD DRTARTLTLI AKVTQNLANF AKFGSKEEYM 
       460        470        480        490        500
SFMNQFLEHE WTNMQRFLLE ISNPETLSNT AGFEGYIDLG RELSSLHSLL 
       510        520        530        540        550
WEAVSQLEQS IVSKLGPLPR ILRDVHTALS TPGSGQLPGT NDLASTPGSG 
       560        570        580        590        600
SSSISAGLQK MVIENDLSGL IDFTRLPSPT PENKDLFFVT RSSGVQPSPA 
       610        620        630        640        650
RSSSYSEANE PDLQMANGGK SLSMVDLQDA RTLDGEAGSP AGPDVLPTDG 
       660        670        680        690        700
QAAAAQLVAG WPARATPVNL AGLATVRRAG QTPTTPGTSE GAPGRPQLLA 
       710        720        730        740        750
PLSFQNPVYQ MAAGLPLSPR GLGDSGSEGH SSLSSHSNSE ELAAAAKLGS 
       760        770        780        790        800
FSTAAEELAR RPGELARRQM SLTEKGGQPT VPRQNSAGPQ RRIDQPPPPP 
       810        820        830        840        850
PPPPPAPRGR TPPNLLSTLQ YPRPSSGTLA SASPDWVGPS TRLRQQSSSS 
       860        870        880        890        900
KGDSPELKPR AVHKQGPSPV SPNALDRTAA WLLTMNAQLL EDEGLGPDPP 
       910        920        930        940        950
HRDRLRSKDE LSQAEKDLAV LQDKLRISTK KLEEYETLFK CQEETTQKLV 
       960        970        980        990       1000
LEYQARLEEG EERLRRQQED KDIQMKGIIS RLMSVEEELK KDHAEMQAAV 
      1010       1020       1030 
DSKQKIIDAQ EKRIASLDAA NARLMSALTQ LKESMH

Show »

Length:1,036

Mass (Da):114,410

Checksum:ⁱ1B07D8D3B9DEA76A

GO

Isoform 5 (identifier: Q5VWQ8-5) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
2-41: SAGGSARKSTGRSSYYYRLLRRPRLQRQRSRSRSRTRPAR → EPDSLLDQDDSY
1158-1189: RYSMQARNGISPTNPTKLQITENGEFRNSSNC → SMH

« Hide

        10         20         30         40         50
MEPDSLLDQD DSYESPQERP GSRRSLPGSL SEKSPSMEPS AATPFRVTGF 
        60         70         80         90        100
LSRRLKGSIK RTKSQPKLDR NHSFRHILPG FRSAAAAAAD NERSHLMPRL 
       110        120        130        140        150
KESRSHESLL SPSSAVEALD LSMEEEVVIK PVHSSILGQD YCFEVTTSSG 
       160        170        180        190        200
SKCFSCRSAA ERDKWMENLR RAVHPNKDNS RRVEHILKLW VIEAKDLPAK 
       210        220        230        240        250
KKYLCELCLD DVLYARTTGK LKTDNVFWGE HFEFHNLPPL RTVTVHLYRE 
       260        270        280        290        300
TDKKKKKERN SYLGLVSLPA ASVAGRQFVE KWYPVVTPNP KGGKGPGPMI 
       310        320        330        340        350
RIKARYQTIT ILPMEMYKEF AEHITNHYLG LCAALEPILS AKTKEEMASA 
       360        370        380        390        400
LVHILQSTGK VKDFLTDLMM SEVDRCGDNE HLIFRENTLA TKAIEEYLKL 
       410        420        430        440        450
VGQKYLQDAL GEFIKALYES DENCEVDPSK CSAADLPEHQ GNLKMCCELA 
       460        470        480        490        500
FCKIINSYCV FPRELKEVFA SWRQECSSRG RPDISERLIS ASLFLRFLCP 
       510        520        530        540        550
AIMSPSLFNL LQEYPDDRTA RTLTLIAKVT QNLANFAKFG SKEEYMSFMN 
       560        570        580        590        600
QFLEHEWTNM QRFLLEISNP ETLSNTAGFE GYIDLGRELS SLHSLLWEAV 
       610        620        630        640        650
SQLEQSIVSK LGPLPRILRD VHTALSTPGS GQLPGTNDLA STPGSGSSSI 
       660        670        680        690        700
SAGLQKMVIE NDLSGLIDFT RLPSPTPENK DLFFVTRSSG VQPSPARSSS 
       710        720        730        740        750
YSEANEPDLQ MANGGKSLSM VDLQDARTLD GEAGSPAGPD VLPTDGQAAA 
       760        770        780        790        800
AQLVAGWPAR ATPVNLAGLA TVRRAGQTPT TPGTSEGAPG RPQLLAPLSF 
       810        820        830        840        850
QNPVYQMAAG LPLSPRGLGD SGSEGHSSLS SHSNSEELAA AAKLGSFSTA 
       860        870        880        890        900
AEELARRPGE LARRQMSLTE KGGQPTVPRQ NSAGPQRRID QPPPPPPPPP 
       910        920        930        940        950
PAPRGRTPPN LLSTLQYPRP SSGTLASASP DWVGPSTRLR QQSSSSKGDS 
       960        970        980        990       1000
PELKPRAVHK QGPSPVSPNA LDRTAAWLLT MNAQLLEDEG LGPDPPHRDR 
      1010       1020       1030       1040       1050
LRSKDELSQA EKDLAVLQDK LRISTKKLEE YETLFKCQEE TTQKLVLEYQ 
      1060       1070       1080       1090       1100
ARLEEGEERL RRQQEDKDIQ MKGIISRLMS VEEELKKDHA EMQAAVDSKQ 
      1110       1120       1130 
KIIDAQEKRI ASLDAANARL MSALTQLKES MH

Note: Gene prediction based on EST data.

Show »

Length:1,132

Mass (Da):125,041

Checksum:ⁱ85C487CD98660B19

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

H0Y3A3	H0Y3A3_HUMAN	Disabled homolog 2-interacting prot... Disabled homolog 2-interacting protein	DAB2IP	1,069	Annotation score:
F6R503	F6R503_HUMAN	Disabled homolog 2-interacting prot... Disabled homolog 2-interacting protein	DAB2IP	229	Annotation score:
F8WA47	F8WA47_HUMAN	Disabled homolog 2-interacting prot... Disabled homolog 2-interacting protein	DAB2IP	291	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	482	I → T in AAM00371 (PubMed:11944990).Curated	1
Sequence conflictⁱ	921	P → S in AAM00371 (PubMed:11944990).Curated	1
Sequence conflictⁱ	1091 – 1092	QQ → HE in AAM00371 (PubMed:11944990).Curated	2

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_056858	59	S → F. Corresponds to variant dbSNP:rs7027492Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_020952	1 – 193	Missing in isoform 3. 1 PublicationAdd BLAST	193
Alternative sequenceⁱVSP_020953	1 – 124	Missing in isoform 2 and isoform 4. 3 PublicationsAdd BLAST	124
Alternative sequenceⁱVSP_047361	2 – 41	SAGGS…TRPAR → EPDSLLDQDDSY in isoform 5. CuratedAdd BLAST	40
Alternative sequenceⁱVSP_020954	1158 – 1189	RYSMQ…NSSNC → SMH in isoform 3, isoform 4 and isoform 5. 3 PublicationsAdd BLAST	32

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF367051 mRNA Translation: AAM00371.1 AY032952 mRNA Translation: AAK50336.1 AB051530 mRNA Translation: BAB21834.2 AL357936 Genomic DNA No translation available. AL365274 Genomic DNA No translation available. CH471090 Genomic DNA Translation: EAW87503.1 CH471090 Genomic DNA Translation: EAW87504.1 BC146762 mRNA Translation: AAI46763.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS6832.1 [Q5VWQ8-2] CCDS6833.2 [Q5VWQ8-5]
NCBI Reference Sequences More...RefSeqⁱ	NP_115941.2, NM_032552.3 [Q5VWQ8-5] NP_619723.1, NM_138709.2 [Q5VWQ8-2] XP_005251776.1, XM_005251719.4 [Q5VWQ8-1] XP_011516572.1, XM_011518270.2 [Q5VWQ8-2] XP_011516573.1, XM_011518271.2 [Q5VWQ8-2] XP_016869789.1, XM_017014300.1 [Q5VWQ8-2]
UniGeneⁱ	Hs.522378

Genome annotation databases

Ensemblⁱ	ENST00000259371; ENSP00000259371; ENSG00000136848 [Q5VWQ8-5] ENST00000309989; ENSP00000310827; ENSG00000136848 [Q5VWQ8-2] ENST00000408936; ENSP00000386183; ENSG00000136848 [Q5VWQ8-1]
GeneIDⁱ	153090
KEGGⁱ	hsa:153090
UCSC genome browser More...UCSCⁱ	uc004bln.5 human [Q5VWQ8-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Chromosomal rearrangement, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q5VWQ8	DAB2 interacting protein		PANTR		1189	UniRef100_Q5VWQ8
Isoform 2 of Disabled homolog 2-interacting protein		HUMAN		1065
DAB2 interacting protein		PANTR		1065
UPI0007DBAF21		HUMAN		1125
Q5VWQ8-3	Isoform 4 of Disabled homolog 2-interacting protein		HUMAN		1036	UniRef100_Q5VWQ8-4
DAB2IP isoform 3 (Fragment)		PANTR		1069
Disabled homolog 2-interacting protein (Fragment)		HUMAN		1069
UPI00004589B1		PANTR		1160
Q5VWQ8-4	Disabled homolog 2-interacting protein (Fragment)		HUMAN		1069	UniRef100_Q5VWQ8-4
DAB2IP isoform 3 (Fragment)		PANTR		1069
Isoform 3 of Disabled homolog 2-interacting protein		HUMAN		967
UPI00004589B1		PANTR		1160
Q5VWQ8-5	DAB2 interacting protein		PANTR		1132	UniRef100_K7BAH1

Protein	Similar proteins		Species	Score	Length	Source
Q5VWQ8	Disabled homolog 2-interacting protein		MOUSE		1189	UniRef90_Q5VWQ8
DAB2 interacting protein		PANTR		1189
Isoform 2 of Disabled homolog 2-interacting protein		HUMAN		1065
LOW QUALITY PROTEIN: disabled homolog 2-interacting protein		ODORO		1338
Disabled homolog 2-interacting protein (Fragment)		NEOVI		100
+463

Protein	Similar proteins		Species	Score	Length	Source
Q5VWQ8	Disabled homolog 2-interacting protein		MOUSE		1189	UniRef50_Q5VWQ8
Disabled homolog 2-interacting protein		RAT		996
DAB2 interacting protein		PANTR		1189
Isoform 2 of Disabled homolog 2-interacting protein		HUMAN		1065
LOW QUALITY PROTEIN: disabled homolog 2-interacting protein		ODORO		1338
+1362

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF367051 mRNA Translation: AAM00371.1 AY032952 mRNA Translation: AAK50336.1 AB051530 mRNA Translation: BAB21834.2 AL357936 Genomic DNA No translation available. AL365274 Genomic DNA No translation available. CH471090 Genomic DNA Translation: EAW87503.1 CH471090 Genomic DNA Translation: EAW87504.1 BC146762 mRNA Translation: AAI46763.1
CCDSⁱ	CCDS6832.1 [Q5VWQ8-2] CCDS6833.2 [Q5VWQ8-5]
RefSeqⁱ	NP_115941.2, NM_032552.3 [Q5VWQ8-5] NP_619723.1, NM_138709.2 [Q5VWQ8-2] XP_005251776.1, XM_005251719.4 [Q5VWQ8-1] XP_011516572.1, XM_011518270.2 [Q5VWQ8-2] XP_011516573.1, XM_011518271.2 [Q5VWQ8-2] XP_016869789.1, XM_017014300.1 [Q5VWQ8-2]
UniGeneⁱ	Hs.522378

3D structure databases

ProteinModelPortalⁱ	Q5VWQ8
SMRⁱ	Q5VWQ8
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	127478, 44 interactors
DIPⁱ	DIP-41721N
IntActⁱ	Q5VWQ8, 7 interactors
STRINGⁱ	9606.ENSP00000259371

PTM databases

CarbonylDBⁱ	Q5VWQ8
iPTMnetⁱ	Q5VWQ8
PhosphoSitePlusⁱ	Q5VWQ8

Polymorphism and mutation databases

DMDMⁱ	116247768

DMDMⁱ

116247768

Proteomic databases

EPDⁱ	Q5VWQ8
MaxQBⁱ	Q5VWQ8
PaxDbⁱ	Q5VWQ8
PeptideAtlasⁱ	Q5VWQ8
PRIDEⁱ	Q5VWQ8
ProteomicsDBⁱ	65554 65555 [Q5VWQ8-2] 65556 [Q5VWQ8-3] 65557 [Q5VWQ8-4]

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000259371; ENSP00000259371; ENSG00000136848 [Q5VWQ8-5] ENST00000309989; ENSP00000310827; ENSG00000136848 [Q5VWQ8-2] ENST00000408936; ENSP00000386183; ENSG00000136848 [Q5VWQ8-1]
GeneIDⁱ	153090
KEGGⁱ	hsa:153090
UCSCⁱ	uc004bln.5 human [Q5VWQ8-1]

Organism-specific databases

CTDⁱ	153090
DisGeNETⁱ	153090
EuPathDBⁱ	HostDB:ENSG00000136848.16
GeneCardsⁱ	DAB2IP
HGNCⁱ	HGNC:17294 DAB2IP
MIMⁱ	609205 gene
neXtProtⁱ	NX_Q5VWQ8
OpenTargetsⁱ	ENSG00000136848
PharmGKBⁱ	PA27133
HUGEⁱ	Search...
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3508 Eukaryota ENOG410XPU1 LUCA
GeneTreeⁱ	ENSGT00760000119092
HOVERGENⁱ	HBG006492
InParanoidⁱ	Q5VWQ8
KOⁱ	K19901
OMAⁱ	NNYMVLC
OrthoDBⁱ	EOG091G00ZZ
PhylomeDBⁱ	Q5VWQ8
TreeFamⁱ	TF105303

Enzyme and pathway databases

Reactomeⁱ	R-HSA-5658442 Regulation of RAS by GAPs R-HSA-6802949 Signaling by RAS mutants
SIGNORⁱ	Q5VWQ8

Miscellaneous databases

ChiTaRSⁱ	DAB2IP human
GeneWikiⁱ	DAB2IP
GenomeRNAiⁱ	153090
Protein Ontology More...PROⁱ	PR:Q5VWQ8
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000136848 Expressed in 193 organ(s), highest expression level in cerebellum
CleanExⁱ	HS_DAB2IP
ExpressionAtlasⁱ	Q5VWQ8 baseline and differential
Genevisibleⁱ	Q5VWQ8 HS

Family and domain databases

Gene3Dⁱ	2.30.29.30, 1 hit 2.60.40.150, 1 hit
InterProⁱ	View protein in InterPro IPR000008 C2_dom IPR035892 C2_domain_sf IPR030403 DAB2IP IPR021887 DUF3498 IPR011993 PH-like_dom_sf IPR001849 PH_domain IPR039360 Ras_GTPase IPR023152 RasGAP_CS IPR001936 RasGAP_dom IPR008936 Rho_GTPase_activation_prot
PANTHERⁱ	PTHR10194 PTHR10194, 1 hit PTHR10194:SF26 PTHR10194:SF26, 1 hit
Pfamⁱ	View protein in Pfam PF00168 C2, 1 hit PF12004 DUF3498, 1 hit PF00616 RasGAP, 2 hits
SMARTⁱ	View protein in SMART SM00239 C2, 1 hit SM00233 PH, 1 hit SM00323 RasGAP, 1 hit
SUPFAMⁱ	SSF48350 SSF48350, 1 hit
PROSITEⁱ	View protein in PROSITE PS50003 PH_DOMAIN, 1 hit PS00509 RAS_GTPASE_ACTIV_1, 1 hit PS50018 RAS_GTPASE_ACTIV_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DAB2P_HUMAN
Accessionⁱ	Q5VWQ8Primary (citable) accession number: Q5VWQ8 Secondary accession number(s): A6H8V2 Q9C0C0
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 17, 2006
	Last sequence update:	October 17, 2006
	Last modified:	November 7, 2018
	This is version 148 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

Complete proteome, Reference proteome

Documents

Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Human chromosome 9
Human chromosome 9: entries, gene names and cross-references to MIM

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Supporting data

UniProtKB - Q5VWQ8 (DAB2P_HUMAN)

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Disabled homolog 2-interacting protein

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Plasma membrane

Other locations

Cytosol

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

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Keywords - Diseasei

Organism-specific databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Coiled coil

Compositional bias

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ