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Disabled homolog 2-interacting protein (DAB2-interacting protein) (ASK-interacting protein 1) (DOC-2/DAB-2 interactive protein)

 DAB2P_MOUSE             Reviewed;        1189 AA.
Q3UHC7; A2AUW9; A2AUX2; A5X2X2; B7ZD28; Q3TPD5; Q3UH44; Q6JTV1;
Q6Y636; Q80T97;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 1.
22-NOV-2017, entry version 124.
RecName: Full=Disabled homolog 2-interacting protein;
Short=DAB2-interacting protein;
AltName: Full=ASK-interacting protein 1;
AltName: Full=DOC-2/DAB-2 interactive protein;
Name=Dab2ip; Synonyms=Kiaa1743;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), ALTERNATIVE
SPLICING, AND TISSUE SPECIFICITY.
STRAIN=129S6/SvEvTac; TISSUE=Spleen;
PubMed=16629596; DOI=10.1089/dna.2006.25.232;
Chen H., Karam J.A., Schultz R., Zhang Z., Duncan C., Hsieh J.-T.;
"Cloning of mouse Dab2ip gene, a novel member of the RasGTPase-
activating protein family and characterization of its regulatory
region in prostate.";
DNA Cell Biol. 25:232-245(2006).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, SUBCELLULAR
LOCATION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=23326475; DOI=10.1371/journal.pone.0053635;
Qiao S., Kim S.H., Heck D., Goldowitz D., LeDoux M.S., Homayouni R.;
"Dab2IP GTPase activating protein regulates dendrite development and
synapse number in cerebellum.";
PLoS ONE 8:E53635-E53635(2013).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Brain, and Heart;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 328-1189 (ISOFORM 3).
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"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.";
DNA Res. 10:35-48(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 586-1189 (ISOFORM 4),
INTERACTION WITH DAB2, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=C57BL/6J;
PubMed=12877983; DOI=10.1016/S0169-328X(03)00176-1;
Homayouni R., Magdaleno S., Keshvara L., Rice D.S., Curran T.;
"Interaction of Disabled-1 and the GTPase activating protein Dab2IP in
mouse brain.";
Brain Res. Mol. Brain Res. 115:121-129(2003).
[8]
FUNCTION, AND INTERACTION WITH ERN1 AND TRAF2.
PubMed=18281285; DOI=10.1074/jbc.M710557200;
Luo D., He Y., Zhang H., Yu L., Chen H., Xu Z., Tang S., Urano F.,
Min W.;
"AIP1 is critical in transducing IRE1-mediated endoplasmic reticulum
stress response.";
J. Biol. Chem. 283:11905-11912(2008).
[9]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=19033661; DOI=10.1172/JCI36168;
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.;
"AIP1 functions as an endogenous inhibitor of VEGFR2-mediated
signaling and inflammatory angiogenesis in mice.";
J. Clin. Invest. 118:3904-3916(2008).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19903888; DOI=10.1073/pnas.0908458106;
Xie D., Gore C., Zhou J., Pong R.C., Zhang H., Yu L., Vessella R.L.,
Min W., Hsieh J.T.;
"DAB2IP coordinates both PI3K-Akt and ASK1 pathways for cell survival
and apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 106:19878-19883(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
FUNCTION.
PubMed=19948740; DOI=10.1074/jbc.M109.069385;
Wan T., Liu T., Zhang H., Tang S., Min W.;
"AIP1 functions as Arf6-GAP to negatively regulate TLR4 signaling.";
J. Biol. Chem. 285:3750-3757(2010).
[13]
FUNCTION IN PROSTATE CANCER.
PubMed=20154697; DOI=10.1038/nm.2100;
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.;
"An oncogene-tumor suppressor cascade drives metastatic prostate
cancer by coordinately activating Ras and nuclear factor-kappaB.";
Nat. Med. 16:286-294(2010).
[14]
FUNCTION IN PROSTATE CANCER.
PubMed=20080667; DOI=10.1073/pnas.0908133107;
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.;
"Role of DAB2IP in modulating epithelial-to-mesenchymal transition and
prostate cancer metastasis.";
Proc. Natl. Acad. Sci. U.S.A. 107:2485-2490(2010).
[15]
FUNCTION.
PubMed=21700930; DOI=10.1161/CIRCRESAHA.111.248245;
Yu L., Qin L., Zhang H., He Y., Chen H., Pober J.S., Tellides G.,
Min W.;
"AIP1 prevents graft arteriosclerosis by inhibiting interferon-gamma-
dependent smooth muscle cell proliferation and intimal expansion.";
Circ. Res. 109:418-427(2011).
[16]
FUNCTION IN MEDULLOBLASTOMA DEVELOPMENT, INDUCTION, AND TISSUE
SPECIFICITY.
PubMed=22696229; DOI=10.1158/1078-0432.CCR-12-0399;
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.;
"EZH2-regulated DAB2IP is a medulloblastoma tumor suppressor and a
positive marker for survival.";
Clin. Cancer Res. 18:4048-4058(2012).
[17]
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
DEVELOPMENTAL STAGE.
PubMed=23056358; DOI=10.1371/journal.pone.0046592;
Lee G.H., Kim S.H., Homayouni R., D'Arcangelo G.;
"Dab2ip regulates neuronal migration and neurite outgrowth in the
developing neocortex.";
PLoS ONE 7:E46592-E46592(2012).
-!- FUNCTION: 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. {ECO:0000269|PubMed:18281285,
ECO:0000269|PubMed:19033661, ECO:0000269|PubMed:19903888,
ECO:0000269|PubMed:19948740, ECO:0000269|PubMed:20080667,
ECO:0000269|PubMed:20154697, ECO:0000269|PubMed:21700930,
ECO:0000269|PubMed:22696229, ECO:0000269|PubMed:23056358,
ECO:0000269|PubMed:23326475}.
-!- SUBUNIT: 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. 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).
{ECO:0000250, ECO:0000269|PubMed:12877983,
ECO:0000269|PubMed:18281285}.
-!- INTERACTION:
P97318:Dab1; NbExp=3; IntAct=EBI-6306507, EBI-81680;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000305};
Peripheral membrane protein {ECO:0000305}. Cell projection,
dendrite. 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. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q3UHC7-1; Sequence=Displayed;
Name=2;
IsoId=Q3UHC7-2; Sequence=VSP_020956;
Name=3;
IsoId=Q3UHC7-3; Sequence=VSP_020957;
Note=No experimental confirmation available.;
Name=4; Synonyms=Dab2IP-L;
IsoId=Q3UHC7-4; Sequence=VSP_046519, VSP_046520;
-!- TISSUE SPECIFICITY: 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. {ECO:0000269|PubMed:12877983, ECO:0000269|PubMed:16629596,
ECO:0000269|PubMed:19033661, ECO:0000269|PubMed:22696229,
ECO:0000269|PubMed:23326475}.
-!- DEVELOPMENTAL STAGE: 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.
{ECO:0000269|PubMed:12877983, ECO:0000269|PubMed:19033661,
ECO:0000269|PubMed:23056358}.
-!- INDUCTION: Down-regulated in prostate cancer and medulloblastoma.
{ECO:0000269|PubMed:22696229}.
-!- DOMAIN: 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. {ECO:0000250}.
-!- PTM: 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.
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: 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.
{ECO:0000269|PubMed:19033661, ECO:0000269|PubMed:19903888,
ECO:0000269|PubMed:23056358, ECO:0000269|PubMed:23326475}.
-!- SEQUENCE CAUTION:
Sequence=AAQ77379.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAQ77380.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAQ77381.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AY305656; AAQ77379.1; ALT_INIT; mRNA.
EMBL; AY305657; AAQ77380.1; ALT_INIT; mRNA.
EMBL; AY305658; AAQ77381.1; ALT_INIT; mRNA.
EMBL; DQ473307; ABF13290.1; -; mRNA.
EMBL; AK147464; BAE27930.1; -; mRNA.
EMBL; AK147593; BAE28013.1; -; mRNA.
EMBL; AK164475; BAE37801.1; -; mRNA.
EMBL; AL929241; CAX15340.1; -; Genomic_DNA.
EMBL; AL929241; CAM25773.2; -; Genomic_DNA.
EMBL; AL929241; CAM25777.1; -; Genomic_DNA.
EMBL; BC118530; AAI18531.1; -; mRNA.
EMBL; AK122548; BAC65830.1; -; mRNA.
EMBL; AY178784; AAP31233.1; -; mRNA.
CCDS; CCDS50577.1; -. [Q3UHC7-4]
CCDS; CCDS50578.1; -. [Q3UHC7-1]
CCDS; CCDS71045.1; -. [Q3UHC7-2]
RefSeq; NP_001001602.2; NM_001001602.2.
RefSeq; NP_001107596.1; NM_001114124.2. [Q3UHC7-1]
RefSeq; NP_001107597.1; NM_001114125.1. [Q3UHC7-4]
RefSeq; NP_001277568.1; NM_001290639.1. [Q3UHC7-2]
RefSeq; NP_001277569.1; NM_001290640.1.
RefSeq; NP_001277570.1; NM_001290641.1. [Q3UHC7-2]
RefSeq; XP_006498370.2; XM_006498307.2. [Q3UHC7-2]
UniGene; Mm.29629; -.
ProteinModelPortal; Q3UHC7; -.
SMR; Q3UHC7; -.
BioGrid; 213562; 4.
IntAct; Q3UHC7; 1.
MINT; MINT-136025; -.
STRING; 10090.ENSMUSP00000088532; -.
iPTMnet; Q3UHC7; -.
PhosphoSitePlus; Q3UHC7; -.
MaxQB; Q3UHC7; -.
PaxDb; Q3UHC7; -.
PeptideAtlas; Q3UHC7; -.
PRIDE; Q3UHC7; -.
Ensembl; ENSMUST00000091010; ENSMUSP00000088532; ENSMUSG00000026883. [Q3UHC7-1]
Ensembl; ENSMUST00000112983; ENSMUSP00000108607; ENSMUSG00000026883. [Q3UHC7-2]
Ensembl; ENSMUST00000112986; ENSMUSP00000108610; ENSMUSG00000026883. [Q3UHC7-4]
Ensembl; ENSMUST00000112992; ENSMUSP00000108616; ENSMUSG00000026883. [Q3UHC7-3]
GeneID; 69601; -.
KEGG; mmu:69601; -.
UCSC; uc008jkr.2; mouse. [Q3UHC7-1]
UCSC; uc008jkv.2; mouse. [Q3UHC7-3]
UCSC; uc008jkx.2; mouse. [Q3UHC7-4]
CTD; 153090; -.
MGI; MGI:1916851; Dab2ip.
eggNOG; KOG3508; Eukaryota.
eggNOG; ENOG410XPU1; LUCA.
GeneTree; ENSGT00760000119092; -.
HOGENOM; HOG000231979; -.
HOVERGEN; HBG006492; -.
InParanoid; Q3UHC7; -.
KO; K19901; -.
OMA; PTMPRQN; -.
OrthoDB; EOG091G00ZZ; -.
PhylomeDB; Q3UHC7; -.
TreeFam; TF105303; -.
Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
PRO; PR:Q3UHC7; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026883; -.
ExpressionAtlas; Q3UHC7; baseline and differential.
Genevisible; Q3UHC7; MM.
GO; GO:1990597; C:AIP1-IRE1 complex; IPI:ParkinsonsUK-UCL.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0044300; C:cerebellar mossy fiber; IDA:UniProtKB.
GO; GO:0044301; C:climbing fiber; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0032809; C:neuronal cell body membrane; IDA:UniProtKB.
GO; GO:1990032; C:parallel fiber; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0071889; F:14-3-3 protein binding; ISO:MGI.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0005123; F:death receptor binding; ISO:MGI.
GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0019900; F:kinase binding; ISO:MGI.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; ISO:MGI.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:MGI.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISS:UniProtKB.
GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; ISS:UniProtKB.
GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
GO; GO:0032403; F:protein complex binding; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI.
GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB.
GO; GO:0035591; F:signaling adaptor activity; ISO:MGI.
GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; ISO:MGI.
GO; GO:0007257; P:activation of JUN kinase activity; ISO:MGI.
GO; GO:0000185; P:activation of MAPKKK activity; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0021814; P:cell motility involved in cerebral cortex radial glia guided migration; IMP:UniProtKB.
GO; GO:0044257; P:cellular protein catabolic process; ISS:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:BHF-UCL.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:UniProtKB.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
GO; GO:0007252; P:I-kappaB phosphorylation; IMP:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:BHF-UCL.
GO; GO:0021819; P:layer formation in cerebral cortex; IMP:UniProtKB.
GO; GO:0016525; P:negative regulation of angiogenesis; IMP:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
GO; GO:0035414; P:negative regulation of catenin import into nucleus; IMP:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:1903363; P:negative regulation of cellular protein catabolic process; ISS:UniProtKB.
GO; GO:0010596; P:negative regulation of endothelial cell migration; IMP:UniProtKB.
GO; GO:0010633; P:negative regulation of epithelial cell migration; ISS:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:BHF-UCL.
GO; GO:0070317; P:negative regulation of G0 to G1 transition; ISS:UniProtKB.
GO; GO:0034260; P:negative regulation of GTPase activity; IMP:UniProtKB.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0043553; P:negative regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IMP:BHF-UCL.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IBA:GO_Central.
GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; IMP:UniProtKB.
GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IDA:UniProtKB.
GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:BHF-UCL.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:0071158; P:positive regulation of cell cycle arrest; ISS:UniProtKB.
GO; GO:1900006; P:positive regulation of dendrite development; IMP:UniProtKB.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IMP:BHF-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
GO; GO:2001224; P:positive regulation of neuron migration; IMP:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; ISS:UniProtKB.
GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:UniProtKB.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:BHF-UCL.
GO; GO:0090129; P:positive regulation of synapse maturation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0038026; P:reelin-mediated signaling pathway; IEA:InterPro.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0043087; P:regulation of GTPase activity; IMP:UniProtKB.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:1900744; P:regulation of p38MAPK cascade; IMP:UniProtKB.
GO; GO:0043254; P:regulation of protein complex assembly; IMP:UniProtKB.
GO; GO:0043497; P:regulation of protein heterodimerization activity; ISO:MGI.
GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
GO; GO:0035148; P:tube formation; IMP:UniProtKB.
GO; GO:0036324; P:vascular endothelial growth factor receptor-2 signaling pathway; IMP:UniProtKB.
Gene3D; 2.20.170.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR030403; DAB2IP.
InterPro; IPR021887; DUF3498.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR023152; RasGAP_CS.
InterPro; IPR001936; RasGAP_dom.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR023315; SynGAP_C2_N.
PANTHER; PTHR10194:SF26; PTHR10194:SF26; 1.
Pfam; PF00168; C2; 1.
Pfam; PF12004; DUF3498; 1.
Pfam; PF00616; RasGAP; 2.
SMART; SM00239; C2; 1.
SMART; SM00233; PH; 1.
SMART; SM00323; RasGAP; 1.
SUPFAM; SSF48350; SSF48350; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
1: Evidence at protein level;
Alternative splicing; Angiogenesis; Apoptosis; Cell cycle;
Cell membrane; Cell projection; Coiled coil; Complete proteome;
Cytoplasm; Developmental protein; Growth regulation;
GTPase activation; Immunity; Inflammatory response; Innate immunity;
Membrane; Phosphoprotein; Reference proteome; Stress response;
Tumor suppressor; Unfolded protein response.
CHAIN 1 1189 Disabled homolog 2-interacting protein.
/FTId=PRO_0000252408.
DOMAIN 101 202 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 200 295 C2.
DOMAIN 371 563 Ras-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00167}.
REGION 646 943 Necessary for interaction with AKT1.
{ECO:0000250}.
COILED 1025 1159 {ECO:0000255}.
COMPBIAS 8 52 Arg-rich.
COMPBIAS 112 117 Poly-Ala.
COMPBIAS 867 870 Poly-Ala.
COMPBIAS 903 948 Pro-rich.
MOD_RES 728 728 Phosphoserine; by MAP3K5 and RIPK1.
{ECO:0000250|UniProtKB:Q5VWQ8}.
MOD_RES 747 747 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 978 978 Phosphoserine.
{ECO:0000250|UniProtKB:Q5VWQ8}.
MOD_RES 995 995 Phosphoserine.
{ECO:0000250|UniProtKB:Q5VWQ8}.
VAR_SEQ 1 124 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:16629596}.
/FTId=VSP_020956.
VAR_SEQ 1 42 MSAGGNARKSTGRPSYYYRLLRRPRLQRQRSRSRSRTRPAR
E -> MEPDSLLDPGDSYE (in isoform 4).
{ECO:0000303|PubMed:12877983,
ECO:0000303|PubMed:23326475}.
/FTId=VSP_046519.
VAR_SEQ 990 1040 Missing (in isoform 3).
{ECO:0000303|PubMed:12693553}.
/FTId=VSP_020957.
VAR_SEQ 1157 1189 ERYSMQARNGVSPTNPTKLQITENGEFRNSSNC -> ESMH
(in isoform 4).
{ECO:0000303|PubMed:12877983,
ECO:0000303|PubMed:23326475}.
/FTId=VSP_046520.
CONFLICT 282 282 K -> E (in Ref. 2; ABF13290).
{ECO:0000305}.
CONFLICT 517 517 I -> V (in Ref. 2; ABF13290).
{ECO:0000305}.
CONFLICT 880 880 E -> G (in Ref. 2; ABF13290).
{ECO:0000305}.
CONFLICT 1058 1058 E -> K (in Ref. 2; ABF13290).
{ECO:0000305}.
CONFLICT 1108 1108 S -> P (in Ref. 2; ABF13290).
{ECO:0000305}.
SEQUENCE 1189 AA; 131726 MW; E3AF3FDA71FF96C3 CRC64;
MSAGGNARKS TGRPSYYYRL LRRPRLQRQR SRSRSRTRPA RESPQERPGS RRSLPGSMSE
KNPSMEPSAS TPFRVTGFLS RRLKGSIKRT KSQPKLDRNH SFRHILPGFR SAAAAAADNE
RSHLMPRLKE SRSHESLLSP SSAVEALDLS MEEEVIIKPV HSSILGQDYC FEVTTSSGSK
CFSCRSAAER DKWMENLRRA VHPNKDNSRR VEHILKLWVI EAKDLPAKKK YLCELCLDDV
LYARTTSKLK TDNVFWGEHF EFHNLPPLRT VTVHLYRETD KKKKKERNSY LGLVSLPAAS
VAGRQFVEKW YPVVTPNPKG GKGPGPMIRI KARYQTVSIL PMEMYKEFAE HITNHYLGLC
AALEPILSAK TKEEMASALV HILQSTGKVK DFLTDLMMSE VDRCGDNEHL IFRENTLATK
AIEEYLKLVG QKYLQDALGE FIKALYESDE NCEVDPSKCS SADLPEHQGN LKMCCELAFC
KIINSYCVFP RELKEVFASW RQECSSRGRP DISERLISAS LFLRFLCPAI MSPSLFNLLQ
EYPDDRTART LTLIAKVTQN LANFAKFGSK EEYMSFMNQF LEHEWTNMQR FLLEISNPET
LSNTAGFEGY IDLGRELSSL HSLLWEAVSQ LDQSVVSKLG PLPRILRDVH TALSTPGSGQ
LPGTNDLAST PGSGSSSVSA GLQKMVIEND LSGLIDFTRL PSPTPENKDL FFVTRSSGVQ
PSPARSSSYS EANEPDLQMA NGSKSLSMVD LQDARTLDGE AGSPVGPDAL PADGQVPATQ
LLAGWPARAA PVSLAGLATV RRAVPTPTTP GTSEGAPGRP QLLAPLSFQN PVYQMAAGLP
LSPRGLGDSG SEGHSSLSSH SNSEELAAAA KLGSFSTAAE ELARRPGELA RRQMSLTEKG
GQPTVPRQNS AGPQRRIDQP PPPPPPPPPA PRGRTPPTLL STLQYPRPSS GTLASASPDW
AGPGTRLRQQ SSSSKGDSPE LKPRAMHKQG PSPVSPNALD RTAAWLLTMN AQLLEDEGLG
PDPPHRDRLR SKEELSQAEK DLAVLQDKLR ISTKKLEEYE TLFKCQEETT QKLVLEYQAR
LEEGEERLRR QQEDKDIQMK GIISRLMSVE EELKKDHAEM QAAVDSKQKI IDAQEKRIAS
LDAANARLMS ALTQLKERYS MQARNGVSPT NPTKLQITEN GEFRNSSNC


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