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Protein

Disabled homolog 2-interacting protein

Gene

Dab2ip

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

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

GO - Molecular functioni

GO - Biological processi

  • activation of JUN kinase activity Source: MGI
  • activation of MAPKKK activity Source: UniProtKB
  • 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 interleukin-1 Source: UniProtKB
  • cellular response to lipopolysaccharide Source: UniProtKB
  • cellular response to tumor necrosis factor Source: BHF-UCL
  • cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
  • extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
  • 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: MGI
  • negative regulation of catenin import into nucleus Source: BHF-UCL
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of cyclin catabolic process Source: UniProtKB
  • negative regulation of endothelial cell migration Source: UniProtKB
  • negative regulation of epithelial cell migration Source: UniProtKB
  • negative regulation of epithelial cell proliferation Source: UniProtKB
  • 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: UniProtKB
  • negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • negative regulation of MAP kinase activity Source: UniProtKB
  • negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • 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: 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 from RNA polymerase II promoter Source: UniProtKB
  • 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: BHF-UCL
  • positive regulation of apoptotic signaling pathway Source: UniProtKB
  • positive regulation of cell cycle arrest Source: UniProtKB
  • positive regulation of dendrite development Source: UniProtKB
  • positive regulation of epithelial cell proliferation Source: UniProtKB
  • 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 serine/threonine kinase activity Source: BHF-UCL
  • positive regulation of synapse maturation Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • 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
  • regulation of protein heterodimerization activity Source: MGI
  • response to unfolded protein Source: UniProtKB-KW
  • tube formation Source: UniProtKB
  • vascular endothelial growth factor receptor-2 signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, GTPase activation

Keywords - Biological processi

Angiogenesis, Apoptosis, Cell cycle, Growth regulation, Immunity, Inflammatory response, Innate immunity, Stress response, Unfolded protein response

Enzyme and pathway databases

ReactomeiR-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.

Names & Taxonomyi

Protein namesi
Recommended name:
Disabled homolog 2-interacting protein
Short name:
DAB2-interacting protein
Alternative name(s):
ASK-interacting protein 1
DOC-2/DAB-2 interactive protein
Gene namesi
Name:Dab2ip
Synonyms:Kiaa1743
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1916851. Dab2ip.

Subcellular locationi

  • Cytoplasm
  • Cell membrane Curated; Peripheral membrane protein Curated
  • Cell projectiondendrite

  • Note: 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). Localized in soma and dendrites of Purkinje cells as well as in scattered cell bodies in the molecular layer of the cerebellum.By similarity

GO - Cellular componenti

  • 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
  • extracellular exosome Source: MGI
  • neuronal cell body Source: UniProtKB
  • neuronal cell body membrane Source: UniProtKB
  • parallel fiber Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are viable and fertile but show a number of cerebellar abnormalities such as a delay in the Purkinje cell (PC) dendrites development and a disruption of late-born cortical neurons migration. Develope a prostate hyperplasia in epithelial compartment at 6 months of age. Show normal vasculature development but enhanced inflammatory angiogenesis.4 Publications

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11891189Disabled homolog 2-interacting proteinPRO_0000252408Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei728 – 7281Phosphoserine; by MAP3K5 and RIPK1By similarity
Modified residuei747 – 7471PhosphoserineCombined sources
Modified residuei978 – 9781PhosphoserineBy similarity

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.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ3UHC7.
MaxQBiQ3UHC7.
PaxDbiQ3UHC7.
PRIDEiQ3UHC7.

PTM databases

iPTMnetiQ3UHC7.
PhosphoSiteiQ3UHC7.

Expressioni

Tissue specificityi

Expressed in vascular endothelium of muscle and aorta, in smooth muscle cells of aorta and epithelial cells of lung. Expressed throughout the brain, including olfactory bulb, hypothalamus, cerebellum and cerebral cortex. Expressed in the soma and processes of neurons in a variety of brain structures, including the developing cerebral cortex, CA1 pyramidal neurons and Purkinje cells. Poorly expressed in medulloblastoma cells compared to cerebellar precursor proliferating progenitor cells (at protein level). Highly expressed in the brain, salivary gland, and testis; moderate expression in kidney and heart. Low expression in the lung, seminal vesicle, ventral prostate, epididymis, liver, and bladder. Very low expression in the coagulation gland and skeleton muscles. Lowest expression seen in spleen.5 Publications

Developmental stagei

Expressed in cortical plate neurons at 16 dpc. Expressed in the neocortex, including the cortical plate (CP) at 16.5 dpc, onward (at protein level). Expressed in brain at 13.5 dpc, onward. Expressed during embryogenesis in the vasculature.3 Publications

Inductioni

Down-regulated in prostate cancer and medulloblastoma.1 Publication

Gene expression databases

BgeeiQ3UHC7.
ExpressionAtlasiQ3UHC7. baseline and differential.
GenevisibleiQ3UHC7. MM.

Interactioni

Subunit structurei

On plasma membrane, exists in an inactive form complexed with TNFR1; in response to TNF-alpha, dissociates from TNFR1 complex, tranlocates to cytoplasm and forms part of an intracellular signaling complex comprising TRADD, RALBP1, TRAF2 and MAP3K5. Interacts with DAB1. 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 similarity). Interacts (via PH domain) with ERN1. Interacts with TRAF2. Interacts (via NPXY motif) with DAB2 (via PID domain).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dab1P973183EBI-6306507,EBI-81680

GO - Molecular functioni

Protein-protein interaction databases

BioGridi213562. 1 interaction.
IntActiQ3UHC7. 1 interaction.
MINTiMINT-136025.
STRINGi10090.ENSMUSP00000088532.

Structurei

3D structure databases

ProteinModelPortaliQ3UHC7.
SMRiQ3UHC7. Positions 329-662.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini101 – 202102PHPROSITE-ProRule annotationAdd
BLAST
Domaini200 – 29596C2Add
BLAST
Domaini371 – 563193Ras-GAPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni646 – 943298Necessary for interaction with AKT1By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1025 – 1159135Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi8 – 5245Arg-richAdd
BLAST
Compositional biasi112 – 1176Poly-Ala
Compositional biasi867 – 8704Poly-Ala
Compositional biasi903 – 94846Pro-richAdd
BLAST

Domaini

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). The C2 and 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

Sequence similaritiesi

Contains 1 C2 domain.Curated
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 Ras-GAP domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3508. Eukaryota.
ENOG410XPU1. LUCA.
GeneTreeiENSGT00760000119092.
HOGENOMiHOG000231979.
HOVERGENiHBG006492.
InParanoidiQ3UHC7.
KOiK19901.
OMAiDWVGPST.
PhylomeDBiQ3UHC7.
TreeFamiTF105303.

Family and domain databases

Gene3Di1.10.506.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR030403. DAB2IP.
IPR021887. DUF3498.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR023152. RasGAP_CS.
IPR001936. RasGAP_dom.
IPR008936. Rho_GTPase_activation_prot.
[Graphical view]
PANTHERiPTHR10194:SF26. PTHR10194:SF26. 1 hit.
PfamiPF00168. C2. 1 hit.
PF12004. DUF3498. 1 hit.
PF00616. RasGAP. 2 hits.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00323. RasGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q3UHC7-1) [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
MSAGGNARKS TGRPSYYYRL LRRPRLQRQR SRSRSRTRPA RESPQERPGS
60 70 80 90 100
RRSLPGSMSE KNPSMEPSAS TPFRVTGFLS RRLKGSIKRT KSQPKLDRNH
110 120 130 140 150
SFRHILPGFR SAAAAAADNE RSHLMPRLKE SRSHESLLSP SSAVEALDLS
160 170 180 190 200
MEEEVIIKPV HSSILGQDYC FEVTTSSGSK CFSCRSAAER DKWMENLRRA
210 220 230 240 250
VHPNKDNSRR VEHILKLWVI EAKDLPAKKK YLCELCLDDV LYARTTSKLK
260 270 280 290 300
TDNVFWGEHF EFHNLPPLRT VTVHLYRETD KKKKKERNSY LGLVSLPAAS
310 320 330 340 350
VAGRQFVEKW YPVVTPNPKG GKGPGPMIRI KARYQTVSIL 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 SADLPEHQGN 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 LDQSVVSKLG PLPRILRDVH
660 670 680 690 700
TALSTPGSGQ LPGTNDLAST PGSGSSSVSA GLQKMVIEND LSGLIDFTRL
710 720 730 740 750
PSPTPENKDL FFVTRSSGVQ PSPARSSSYS EANEPDLQMA NGSKSLSMVD
760 770 780 790 800
LQDARTLDGE AGSPVGPDAL PADGQVPATQ LLAGWPARAA PVSLAGLATV
810 820 830 840 850
RRAVPTPTTP GTSEGAPGRP QLLAPLSFQN PVYQMAAGLP LSPRGLGDSG
860 870 880 890 900
SEGHSSLSSH SNSEELAAAA KLGSFSTAAE ELARRPGELA RRQMSLTEKG
910 920 930 940 950
GQPTVPRQNS AGPQRRIDQP PPPPPPPPPA PRGRTPPTLL STLQYPRPSS
960 970 980 990 1000
GTLASASPDW AGPGTRLRQQ SSSSKGDSPE LKPRAMHKQG PSPVSPNALD
1010 1020 1030 1040 1050
RTAAWLLTMN AQLLEDEGLG PDPPHRDRLR SKEELSQAEK 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 MQARNGVSPT NPTKLQITEN GEFRNSSNC
Length:1,189
Mass (Da):131,726
Last modified:October 11, 2005 - v1
Checksum:iE3AF3FDA71FF96C3
GO
Isoform 2 (identifier: Q3UHC7-2) [UniParc]FASTAAdd to basket

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

Show »
Length:1,065
Mass (Da):117,655
Checksum:iD5F64197BB7C5755
GO
Isoform 3 (identifier: Q3UHC7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     990-1040: Missing.

Note: No experimental confirmation available.
Show »
Length:1,138
Mass (Da):126,136
Checksum:iE77E300B7C3E2A55
GO
Isoform 4 (identifier: Q3UHC7-4) [UniParc]FASTAAdd to basket

Also known as: Dab2IP-L

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: MSAGGNARKSTGRPSYYYRLLRRPRLQRQRSRSRSRTRPARE → MEPDSLLDPGDSYE
     1157-1189: ERYSMQARNGVSPTNPTKLQITENGEFRNSSNC → ESMH

Show »
Length:1,132
Mass (Da):125,030
Checksum:iEBF820B19C418428
GO

Sequence cautioni

The sequence AAQ77379.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAQ77380.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAQ77381.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti282 – 2821K → E in ABF13290 (PubMed:23326475).Curated
Sequence conflicti517 – 5171I → V in ABF13290 (PubMed:23326475).Curated
Sequence conflicti880 – 8801E → G in ABF13290 (PubMed:23326475).Curated
Sequence conflicti1058 – 10581E → K in ABF13290 (PubMed:23326475).Curated
Sequence conflicti1108 – 11081S → P in ABF13290 (PubMed:23326475).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 124124Missing in isoform 2. 3 PublicationsVSP_020956Add
BLAST
Alternative sequencei1 – 4242MSAGG…RPARE → MEPDSLLDPGDSYE in isoform 4. 2 PublicationsVSP_046519Add
BLAST
Alternative sequencei990 – 104051Missing in isoform 3. 1 PublicationVSP_020957Add
BLAST
Alternative sequencei1157 – 118933ERYSM…NSSNC → ESMH in isoform 4. 2 PublicationsVSP_046520Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY305656 mRNA. Translation: AAQ77379.1. Different initiation.
AY305657 mRNA. Translation: AAQ77380.1. Different initiation.
AY305658 mRNA. Translation: AAQ77381.1. Different initiation.
DQ473307 mRNA. Translation: ABF13290.1.
AK147464 mRNA. Translation: BAE27930.1.
AK147593 mRNA. Translation: BAE28013.1.
AK164475 mRNA. Translation: BAE37801.1.
AL929241 Genomic DNA. Translation: CAX15340.1.
AL929241 Genomic DNA. Translation: CAM25773.2.
AL929241 Genomic DNA. Translation: CAM25777.1.
BC118530 mRNA. Translation: AAI18531.1.
AK122548 mRNA. Translation: BAC65830.1.
AY178784 mRNA. Translation: AAP31233.1.
CCDSiCCDS50577.1. [Q3UHC7-4]
CCDS50578.1. [Q3UHC7-1]
CCDS71045.1. [Q3UHC7-2]
RefSeqiNP_001001602.2. NM_001001602.2.
NP_001107596.1. NM_001114124.2. [Q3UHC7-1]
NP_001107597.1. NM_001114125.1. [Q3UHC7-4]
NP_001277568.1. NM_001290639.1. [Q3UHC7-2]
NP_001277569.1. NM_001290640.1.
NP_001277570.1. NM_001290641.1. [Q3UHC7-2]
XP_006498370.2. XM_006498307.2. [Q3UHC7-2]
UniGeneiMm.29629.

Genome annotation databases

EnsembliENSMUST00000091010; ENSMUSP00000088532; ENSMUSG00000026883. [Q3UHC7-1]
ENSMUST00000112983; ENSMUSP00000108607; ENSMUSG00000026883. [Q3UHC7-2]
ENSMUST00000112986; ENSMUSP00000108610; ENSMUSG00000026883. [Q3UHC7-4]
ENSMUST00000112992; ENSMUSP00000108616; ENSMUSG00000026883. [Q3UHC7-3]
GeneIDi69601.
KEGGimmu:69601.
UCSCiuc008jkr.2. mouse. [Q3UHC7-1]
uc008jkv.2. mouse. [Q3UHC7-3]
uc008jkx.2. mouse. [Q3UHC7-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY305656 mRNA. Translation: AAQ77379.1. Different initiation.
AY305657 mRNA. Translation: AAQ77380.1. Different initiation.
AY305658 mRNA. Translation: AAQ77381.1. Different initiation.
DQ473307 mRNA. Translation: ABF13290.1.
AK147464 mRNA. Translation: BAE27930.1.
AK147593 mRNA. Translation: BAE28013.1.
AK164475 mRNA. Translation: BAE37801.1.
AL929241 Genomic DNA. Translation: CAX15340.1.
AL929241 Genomic DNA. Translation: CAM25773.2.
AL929241 Genomic DNA. Translation: CAM25777.1.
BC118530 mRNA. Translation: AAI18531.1.
AK122548 mRNA. Translation: BAC65830.1.
AY178784 mRNA. Translation: AAP31233.1.
CCDSiCCDS50577.1. [Q3UHC7-4]
CCDS50578.1. [Q3UHC7-1]
CCDS71045.1. [Q3UHC7-2]
RefSeqiNP_001001602.2. NM_001001602.2.
NP_001107596.1. NM_001114124.2. [Q3UHC7-1]
NP_001107597.1. NM_001114125.1. [Q3UHC7-4]
NP_001277568.1. NM_001290639.1. [Q3UHC7-2]
NP_001277569.1. NM_001290640.1.
NP_001277570.1. NM_001290641.1. [Q3UHC7-2]
XP_006498370.2. XM_006498307.2. [Q3UHC7-2]
UniGeneiMm.29629.

3D structure databases

ProteinModelPortaliQ3UHC7.
SMRiQ3UHC7. Positions 329-662.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213562. 1 interaction.
IntActiQ3UHC7. 1 interaction.
MINTiMINT-136025.
STRINGi10090.ENSMUSP00000088532.

PTM databases

iPTMnetiQ3UHC7.
PhosphoSiteiQ3UHC7.

Proteomic databases

EPDiQ3UHC7.
MaxQBiQ3UHC7.
PaxDbiQ3UHC7.
PRIDEiQ3UHC7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000091010; ENSMUSP00000088532; ENSMUSG00000026883. [Q3UHC7-1]
ENSMUST00000112983; ENSMUSP00000108607; ENSMUSG00000026883. [Q3UHC7-2]
ENSMUST00000112986; ENSMUSP00000108610; ENSMUSG00000026883. [Q3UHC7-4]
ENSMUST00000112992; ENSMUSP00000108616; ENSMUSG00000026883. [Q3UHC7-3]
GeneIDi69601.
KEGGimmu:69601.
UCSCiuc008jkr.2. mouse. [Q3UHC7-1]
uc008jkv.2. mouse. [Q3UHC7-3]
uc008jkx.2. mouse. [Q3UHC7-4]

Organism-specific databases

CTDi153090.
MGIiMGI:1916851. Dab2ip.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG3508. Eukaryota.
ENOG410XPU1. LUCA.
GeneTreeiENSGT00760000119092.
HOGENOMiHOG000231979.
HOVERGENiHBG006492.
InParanoidiQ3UHC7.
KOiK19901.
OMAiDWVGPST.
PhylomeDBiQ3UHC7.
TreeFamiTF105303.

Enzyme and pathway databases

ReactomeiR-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.

Miscellaneous databases

PROiQ3UHC7.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UHC7.
ExpressionAtlasiQ3UHC7. baseline and differential.
GenevisibleiQ3UHC7. MM.

Family and domain databases

Gene3Di1.10.506.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR030403. DAB2IP.
IPR021887. DUF3498.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR023152. RasGAP_CS.
IPR001936. RasGAP_dom.
IPR008936. Rho_GTPase_activation_prot.
[Graphical view]
PANTHERiPTHR10194:SF26. PTHR10194:SF26. 1 hit.
PfamiPF00168. C2. 1 hit.
PF12004. DUF3498. 1 hit.
PF00616. RasGAP. 2 hits.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00323. RasGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of mouse Dab2ip gene, a novel member of the RasGTPase-activating protein family and characterization of its regulatory region in prostate."
    Chen H., Karam J.A., Schultz R., Zhang Z., Duncan C., Hsieh J.-T.
    DNA Cell Biol. 25:232-245(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    Strain: 129S6/SvEvTac.
    Tissue: Spleen.
  2. "Dab2IP GTPase activating protein regulates dendrite development and synapse number in cerebellum."
    Qiao S., Kim S.H., Heck D., Goldowitz D., LeDoux M.S., Homayouni R.
    PLoS ONE 8:E53635-E53635(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Brain and Heart.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  6. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 328-1189 (ISOFORM 3).
    Tissue: Brain.
  7. "Interaction of Disabled-1 and the GTPase activating protein Dab2IP in mouse brain."
    Homayouni R., Magdaleno S., Keshvara L., Rice D.S., Curran T.
    Brain Res. Mol. Brain Res. 115:121-129(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 586-1189 (ISOFORM 4), INTERACTION WITH DAB2, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: C57BL/6J.
  8. "AIP1 is critical in transducing IRE1-mediated endoplasmic reticulum stress response."
    Luo D., He Y., Zhang H., Yu L., Chen H., Xu Z., Tang S., Urano F., Min W.
    J. Biol. Chem. 283:11905-11912(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ERN1 AND TRAF2.
  9. "AIP1 functions as an endogenous inhibitor of VEGFR2-mediated signaling and inflammatory angiogenesis in mice."
    Zhang H., He Y., Dai S., Xu Z., Luo Y., Wan T., Luo D., Jones D., Tang S., Chen H., Sessa W.C., Min W.
    J. Clin. Invest. 118:3904-3916(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  10. "DAB2IP coordinates both PI3K-Akt and ASK1 pathways for cell survival and apoptosis."
    Xie D., Gore C., Zhou J., Pong R.C., Zhang H., Yu L., Vessella R.L., Min W., Hsieh J.T.
    Proc. Natl. Acad. Sci. U.S.A. 106:19878-19883(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas and Testis.
  12. "AIP1 functions as Arf6-GAP to negatively regulate TLR4 signaling."
    Wan T., Liu T., Zhang H., Tang S., Min W.
    J. Biol. Chem. 285:3750-3757(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "An oncogene-tumor suppressor cascade drives metastatic prostate cancer by coordinately activating Ras and nuclear factor-kappaB."
    Min J., Zaslavsky A., Fedele G., McLaughlin S.K., Reczek E.E., De Raedt T., Guney I., Strochlic D.E., Macconaill L.E., Beroukhim R., Bronson R.T., Ryeom S., Hahn W.C., Loda M., Cichowski K.
    Nat. Med. 16:286-294(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PROSTATE CANCER.
  14. "Role of DAB2IP in modulating epithelial-to-mesenchymal transition and prostate cancer metastasis."
    Xie D., Gore C., Liu J., Pong R.C., Mason R., Hao G., Long M., Kabbani W., Yu L., Zhang H., Chen H., Sun X., Boothman D.A., Min W., Hsieh J.T.
    Proc. Natl. Acad. Sci. U.S.A. 107:2485-2490(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PROSTATE CANCER.
  15. "AIP1 prevents graft arteriosclerosis by inhibiting interferon-gamma-dependent smooth muscle cell proliferation and intimal expansion."
    Yu L., Qin L., Zhang H., He Y., Chen H., Pober J.S., Tellides G., Min W.
    Circ. Res. 109:418-427(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "EZH2-regulated DAB2IP is a medulloblastoma tumor suppressor and a positive marker for survival."
    Smits M., van Rijn S., Hulleman E., Biesmans D., van Vuurden D.G., Kool M., Haberler C., Aronica E., Vandertop W.P., Noske D.P., Wurdinger T.
    Clin. Cancer Res. 18:4048-4058(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MEDULLOBLASTOMA DEVELOPMENT, INDUCTION, TISSUE SPECIFICITY.
  17. "Dab2ip regulates neuronal migration and neurite outgrowth in the developing neocortex."
    Lee G.H., Kim S.H., Homayouni R., D'Arcangelo G.
    PLoS ONE 7:E46592-E46592(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiDAB2P_MOUSE
AccessioniPrimary (citable) accession number: Q3UHC7
Secondary accession number(s): A2AUW9
, A2AUX2, A5X2X2, B7ZD28, Q3TPD5, Q3UH44, Q6JTV1, Q6Y636, Q80T97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 11, 2005
Last modified: June 8, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.