UniProtKB - Q5VWQ8 (DAB2P_HUMAN)
Disabled homolog 2-interacting protein
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 PublicationsMiscellaneous
GO - Molecular functioni
- 14-3-3 protein binding Source: BHF-UCL
- cadherin binding Source: BHF-UCL
- death receptor binding Source: BHF-UCL
- GTPase activator activity Source: UniProtKB-KW
- identical protein binding Source: IntAct
- kinase binding Source: UniProtKB
- mitogen-activated protein kinase kinase binding Source: UniProtKB
- mitogen-activated protein kinase kinase kinase binding Source: BHF-UCL
- phosphatidylinositol 3-kinase binding Source: UniProtKB
- phosphatidylinositol 3-kinase regulatory subunit binding Source: UniProtKB
- phosphatidylinositol-3-phosphate binding Source: UniProtKB
- phosphatidylinositol-4-phosphate binding Source: UniProtKB
- protein-containing complex binding Source: UniProtKB
- protein homodimerization activity Source: BHF-UCL
- protein kinase binding Source: ParkinsonsUK-UCL
- protein phosphatase 2A binding Source: BHF-UCL
- protein serine/threonine kinase activator activity Source: GO_Central
- SH3 domain binding Source: UniProtKB
- signaling adaptor activity Source: GO_Central
- vascular endothelial growth factor receptor 2 binding Source: UniProtKB
GO - Biological processi
- 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
- cellular response to epidermal growth factor stimulus Source: BHF-UCL
- cellular response to interleukin-1 Source: UniProtKB
- cellular response to lipopolysaccharide Source: UniProtKB
- cellular response to tumor necrosis factor Source: UniProtKB
- cellular response to unfolded protein Source: ParkinsonsUK-UCL
- cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
- endothelial cell apoptotic process Source: BHF-UCL
- extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
- 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
- layer formation in cerebral cortex Source: UniProtKB
- negative regulation of angiogenesis Source: UniProtKB
- negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
- negative regulation of cell population proliferation Source: UniProtKB
- negative regulation of cellular protein catabolic process Source: UniProtKB
- negative regulation of endothelial cell migration Source: UniProtKB
- negative regulation of epidermal growth factor receptor signaling pathway Source: BHF-UCL
- negative regulation of epithelial cell migration Source: UniProtKB
- negative regulation of epithelial cell proliferation Source: BHF-UCL
- negative regulation of epithelial to mesenchymal transition Source: UniProtKB
- negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
- negative regulation of fibroblast proliferation Source: BHF-UCL
- negative regulation of G0 to G1 transition Source: UniProtKB
- negative regulation of GTPase activity Source: BHF-UCL
- negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
- negative regulation of MAP kinase activity Source: BHF-UCL
- negative regulation of NF-kappaB transcription factor activity Source: BHF-UCL
- negative regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
- negative regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
- negative regulation of protein phosphorylation Source: UniProtKB
- negative regulation of protein serine/threonine kinase activity Source: UniProtKB
- negative regulation of Ras protein signal transduction Source: BHF-UCL
- negative regulation of toll-like receptor 4 signaling pathway Source: UniProtKB
- negative regulation of transcription, DNA-templated Source: UniProtKB
- negative regulation of transcription by RNA polymerase II Source: BHF-UCL
- negative regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
- negative regulation of vascular endothelial growth factor signaling pathway Source: UniProtKB
- neuron projection morphogenesis Source: UniProtKB
- positive regulation of apoptotic process Source: UniProtKB
- positive regulation of apoptotic signaling pathway Source: UniProtKB
- positive regulation of dendrite development Source: UniProtKB
- positive regulation of IRE1-mediated unfolded protein response Source: ParkinsonsUK-UCL
- positive regulation of JNK cascade Source: UniProtKB
- positive regulation of JUN kinase activity Source: BHF-UCL
- positive regulation of MAPK cascade Source: UniProtKB
- positive regulation of neuron migration Source: UniProtKB
- positive regulation of neuron projection development Source: UniProtKB
- positive regulation of proteasomal protein catabolic process Source: UniProtKB
- positive regulation of protein catabolic process Source: UniProtKB
- positive regulation of protein-containing complex assembly Source: ParkinsonsUK-UCL
- positive regulation of protein serine/threonine kinase activity Source: UniProtKB
- positive regulation of synapse maturation Source: UniProtKB
- positive regulation of transcription by RNA polymerase II Source: UniProtKB
- reelin-mediated signaling pathway Source: InterPro
- regulation of cell cycle Source: UniProtKB
- 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-containing complex assembly Source: UniProtKB
- tube formation Source: UniProtKB
- vascular endothelial growth factor receptor-2 signaling pathway Source: UniProtKB
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
PathwayCommonsi | Q5VWQ8 |
Reactomei | R-HSA-5658442, Regulation of RAS by GAPs |
SignaLinki | Q5VWQ8 |
SIGNORi | Q5VWQ8 |
Names & Taxonomyi
Protein namesi | Recommended name: Disabled homolog 2-interacting proteinShort 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 | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:17294, DAB2IP |
MIMi | 609205, gene |
neXtProti | NX_Q5VWQ8 |
VEuPathDBi | HostDB:ENSG00000136848 |
Subcellular locationi
Plasma membrane
- Cell membrane Curated; Peripheral membrane protein Curated
Cytoplasm and Cytosol
Other locations
Note: Localized in soma and dendrites of Purkinje cells as well as in scattered cell bodies in the molecular layer of the cerebellum (By similarity). Colocalizes with TIRAP at the plasma membrane. Colocalizes with ARF6 at the plasma membrane and endocytic vesicles. Translocates from the plasma membrane to the cytoplasm in response to TNF-alpha. Phosphatidylinositol 4-phosphate (PtdIns4P) binding is essential for plasma membrane localization.By similarity
Cytosol
- cytosol Source: Reactome
Plasma Membrane
- neuronal cell body membrane Source: UniProtKB
- plasma membrane Source: UniProtKB
Other locations
- AIP1-IRE1 complex Source: ParkinsonsUK-UCL
- axon Source: UniProtKB
- cerebellar mossy fiber Source: UniProtKB
- climbing fiber Source: UniProtKB
- cytoplasm Source: UniProtKB
- dendrite Source: UniProtKB-SubCell
- endocytic vesicle Source: UniProtKB
- neuronal cell body Source: UniProtKB
- parallel fiber Source: UniProtKB
Keywords - Cellular componenti
Cell membrane, Cell projection, Cytoplasm, MembranePathology & Biotechi
Involvement in diseasei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | 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 suppressorOrganism-specific databases
DisGeNETi | 153090 |
OpenTargetsi | ENSG00000136848 |
PharmGKBi | PA27133 |
Miscellaneous databases
Pharosi | Q5VWQ8, Tbio |
Chemistry databases
ChEMBLi | CHEMBL4523330 |
Genetic variation databases
BioMutai | DAB2IP |
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 | Graphical view | 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
Keywords - PTMi
PhosphoproteinProteomic databases
EPDi | Q5VWQ8 |
jPOSTi | Q5VWQ8 |
MassIVEi | Q5VWQ8 |
MaxQBi | Q5VWQ8 |
PaxDbi | Q5VWQ8 |
PeptideAtlasi | Q5VWQ8 |
PRIDEi | Q5VWQ8 |
ProteomicsDBi | 33682 65554 [Q5VWQ8-1] 65555 [Q5VWQ8-2] 65556 [Q5VWQ8-3] 65557 [Q5VWQ8-4] |
PTM databases
CarbonylDBi | Q5VWQ8 |
iPTMneti | Q5VWQ8 |
PhosphoSitePlusi | Q5VWQ8 |
Expressioni
Tissue specificityi
Inductioni
Gene expression databases
Bgeei | ENSG00000136848, Expressed in cerebellum and 205 other tissues |
ExpressionAtlasi | Q5VWQ8, baseline and differential |
Genevisiblei | Q5VWQ8, HS |
Organism-specific databases
HPAi | ENSG00000136848, Low tissue specificity |
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, RIPK1, 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 PublicationsBinary interactionsi
Q5VWQ8
With | #Exp. | IntAct |
---|---|---|
itself | 2 | EBI-2871881,EBI-2871881 |
GSK3B [P49841] | 2 | EBI-2871881,EBI-373586 |
MAP3K5 [Q99683] | 2 | EBI-2871881,EBI-476263 |
Isoform 2 [Q5VWQ8-2]
With | #Exp. | IntAct |
---|---|---|
AXIN1 [O15169] | 2 | EBI-9543020,EBI-710484 |
GSK3B [P49841] | 2 | EBI-9543020,EBI-373586 |
Isoform 5 [Q5VWQ8-5]
With | #Exp. | IntAct |
---|---|---|
ANKS1A [Q49AR9] | 3 | EBI-12196395,EBI-11954519 |
GO - Molecular functioni
- 14-3-3 protein binding Source: BHF-UCL
- cadherin binding Source: BHF-UCL
- death receptor binding Source: BHF-UCL
- identical protein binding Source: IntAct
- kinase binding Source: UniProtKB
- mitogen-activated protein kinase kinase binding Source: UniProtKB
- mitogen-activated protein kinase kinase kinase binding Source: BHF-UCL
- phosphatidylinositol 3-kinase binding Source: UniProtKB
- phosphatidylinositol 3-kinase regulatory subunit binding Source: UniProtKB
- protein homodimerization activity Source: BHF-UCL
- protein kinase binding Source: ParkinsonsUK-UCL
- protein phosphatase 2A binding Source: BHF-UCL
- SH3 domain binding Source: UniProtKB
- vascular endothelial growth factor receptor 2 binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 127478, 64 interactors |
DIPi | DIP-41721N |
IntActi | Q5VWQ8, 21 interactors |
MINTi | Q5VWQ8 |
STRINGi | 9606.ENSP00000259371 |
Miscellaneous databases
RNActi | Q5VWQ8, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 101 – 202 | PHPROSITE-ProRule annotationAdd BLAST | 102 | |
Domaini | 193 – 311 | C2PROSITE-ProRule annotationAdd BLAST | 119 | |
Domaini | 371 – 563 | Ras-GAPPROSITE-ProRule annotationAdd BLAST | 193 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 75 | DisorderedSequence analysisAdd BLAST | 75 | |
Regioni | 646 – 943 | Necessary for interaction with AKT11 PublicationAdd BLAST | 298 | |
Regioni | 653 – 678 | DisorderedSequence analysisAdd BLAST | 26 | |
Regioni | 715 – 742 | DisorderedSequence analysisAdd BLAST | 28 | |
Regioni | 803 – 823 | DisorderedSequence analysisAdd BLAST | 21 | |
Regioni | 843 – 865 | DisorderedSequence analysisAdd BLAST | 23 | |
Regioni | 895 – 998 | DisorderedSequence analysisAdd BLAST | 104 | |
Regioni | 1015 – 1035 | DisorderedSequence analysisAdd BLAST | 21 | |
Regioni | 1164 – 1189 | DisorderedSequence analysisAdd BLAST | 26 |
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 | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 50 – 66 | Polar residuesSequence analysisAdd BLAST | 17 | |
Compositional biasi | 715 – 735 | Polar residuesSequence analysisAdd BLAST | 21 | |
Compositional biasi | 849 – 865 | Polar residuesSequence analysisAdd BLAST | 17 | |
Compositional biasi | 897 – 915 | Polar residuesSequence analysisAdd BLAST | 19 | |
Compositional biasi | 916 – 935 | Pro residuesSequence analysisAdd BLAST | 20 | |
Compositional biasi | 937 – 978 | Polar residuesSequence analysisAdd BLAST | 42 | |
Compositional biasi | 1019 – 1035 | Basic and acidic residuesSequence analysisAdd BLAST | 17 |
Domaini
Keywords - Domaini
Coiled coilPhylogenomic databases
eggNOGi | KOG3508, Eukaryota |
GeneTreei | ENSGT00940000155853 |
HOGENOMi | CLU_001727_1_0_1 |
InParanoidi | Q5VWQ8 |
OMAi | PMTRGRT |
OrthoDBi | 69536at2759 |
PhylomeDBi | Q5VWQ8 |
TreeFami | TF105303 |
Family and domain databases
Gene3Di | 1.10.506.10, 2 hits 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 SSF49562, SSF49562, 1 hit |
PROSITEi | View protein in PROSITE PS50004, C2, 1 hit PS50003, PH_DOMAIN, 1 hit PS00509, RAS_GTPASE_ACTIV_1, 1 hit PS50018, RAS_GTPASE_ACTIV_2, 1 hit |
s (5+)i Sequence
Sequence statusi: Complete.
This entry describes 5 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 5 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketH0Y3A3 | H0Y3A3_HUMAN | Disabled homolog 2-interacting prot... | DAB2IP | 1,069 | Annotation score: | ||
A0A3B3ITG3 | A0A3B3ITG3_HUMAN | Disabled homolog 2-interacting prot... | DAB2IP | 1,128 | Annotation score: | ||
F8WA47 | F8WA47_HUMAN | Disabled homolog 2-interacting prot... | DAB2IP | 291 | Annotation score: | ||
F6R503 | F6R503_HUMAN | Disabled homolog 2-interacting prot... | DAB2IP | 229 | Annotation score: | ||
A0A3B3IUB7 | A0A3B3IUB7_HUMAN | Disabled homolog 2-interacting prot... | DAB2IP | 48 | Annotation score: | ||
A0A3B3ITC7 | A0A3B3ITC7_HUMAN | Disabled homolog 2-interacting prot... | DAB2IP | 69 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | 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 | Graphical view | 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 |
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] |
Genome annotation databases
Ensembli | ENST00000259371; ENSP00000259371; ENSG00000136848 [Q5VWQ8-5] ENST00000309989; ENSP00000310827; ENSG00000136848 [Q5VWQ8-2] ENST00000408936; ENSP00000386183; ENSG00000136848 |
GeneIDi | 153090 |
KEGGi | hsa:153090 |
UCSCi | uc004bln.5, human [Q5VWQ8-1] |
Keywords - Coding sequence diversityi
Alternative splicing, Chromosomal rearrangementSimilar proteinsi
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] |
3D structure databases
SMRi | Q5VWQ8 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 127478, 64 interactors |
DIPi | DIP-41721N |
IntActi | Q5VWQ8, 21 interactors |
MINTi | Q5VWQ8 |
STRINGi | 9606.ENSP00000259371 |
Chemistry databases
ChEMBLi | CHEMBL4523330 |
PTM databases
CarbonylDBi | Q5VWQ8 |
iPTMneti | Q5VWQ8 |
PhosphoSitePlusi | Q5VWQ8 |
Genetic variation databases
BioMutai | DAB2IP |
DMDMi | 116247768 |
Proteomic databases
EPDi | Q5VWQ8 |
jPOSTi | Q5VWQ8 |
MassIVEi | Q5VWQ8 |
MaxQBi | Q5VWQ8 |
PaxDbi | Q5VWQ8 |
PeptideAtlasi | Q5VWQ8 |
PRIDEi | Q5VWQ8 |
ProteomicsDBi | 33682 65554 [Q5VWQ8-1] 65555 [Q5VWQ8-2] 65556 [Q5VWQ8-3] 65557 [Q5VWQ8-4] |
Protocols and materials databases
Antibodypediai | 48362, 106 antibodies from 21 providers |
DNASUi | 153090 |
Genome annotation databases
Ensembli | ENST00000259371; ENSP00000259371; ENSG00000136848 [Q5VWQ8-5] ENST00000309989; ENSP00000310827; ENSG00000136848 [Q5VWQ8-2] ENST00000408936; ENSP00000386183; ENSG00000136848 |
GeneIDi | 153090 |
KEGGi | hsa:153090 |
UCSCi | uc004bln.5, human [Q5VWQ8-1] |
Organism-specific databases
CTDi | 153090 |
DisGeNETi | 153090 |
GeneCardsi | DAB2IP |
HGNCi | HGNC:17294, DAB2IP |
HPAi | ENSG00000136848, Low tissue specificity |
MIMi | 609205, gene |
neXtProti | NX_Q5VWQ8 |
OpenTargetsi | ENSG00000136848 |
PharmGKBi | PA27133 |
VEuPathDBi | HostDB:ENSG00000136848 |
HUGEi | Search... |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3508, Eukaryota |
GeneTreei | ENSGT00940000155853 |
HOGENOMi | CLU_001727_1_0_1 |
InParanoidi | Q5VWQ8 |
OMAi | PMTRGRT |
OrthoDBi | 69536at2759 |
PhylomeDBi | Q5VWQ8 |
TreeFami | TF105303 |
Enzyme and pathway databases
PathwayCommonsi | Q5VWQ8 |
Reactomei | R-HSA-5658442, Regulation of RAS by GAPs |
SignaLinki | Q5VWQ8 |
SIGNORi | Q5VWQ8 |
Miscellaneous databases
BioGRID-ORCSi | 153090, 5 hits in 1036 CRISPR screens |
ChiTaRSi | DAB2IP, human |
GeneWikii | DAB2IP |
GenomeRNAii | 153090 |
Pharosi | Q5VWQ8, Tbio |
PROi | PR:Q5VWQ8 |
RNActi | Q5VWQ8, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000136848, Expressed in cerebellum and 205 other tissues |
ExpressionAtlasi | Q5VWQ8, baseline and differential |
Genevisiblei | Q5VWQ8, HS |
Family and domain databases
Gene3Di | 1.10.506.10, 2 hits 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 SSF49562, SSF49562, 1 hit |
PROSITEi | View protein in PROSITE PS50004, C2, 1 hit PS50003, PH_DOMAIN, 1 hit PS00509, RAS_GTPASE_ACTIV_1, 1 hit PS50018, RAS_GTPASE_ACTIV_2, 1 hit |
MobiDBi | 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: | February 23, 2022 | |
This is version 167 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
Reference proteomeDocuments
- Human chromosome 9
Human chromosome 9: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot