Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 DAB2P_HUMAN             Reviewed;        1189 AA.
Q5VWQ8; A6H8V2; A6NHI9; B0QZB1; G3XA90; Q8TDL2; Q96SE1; Q9C0C0;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
22-NOV-2017, entry version 139.
RecName: Full=Disabled homolog 2-interacting protein;
Short=DAB2 interaction protein;
Short=DAB2-interacting protein;
AltName: Full=ASK-interacting protein 1;
Short=AIP-1;
AltName: Full=DOC-2/DAB-2 interactive protein;
Name=DAB2IP; Synonyms=AF9Q34, AIP1, KIAA1743;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
PubMed=11944990; DOI=10.1006/geno.2002.6739;
Chen H., Pong R.-C., Wang Z., Hsieh J.-T.;
"Differential regulation of the human gene DAB2IP in normal and
malignant prostatic epithelia: cloning and characterization.";
Genomics 79:573-581(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND CHROMOSOMAL TRANSLOCATION
WITH KMT2A/MLL1.
PubMed=14978793; DOI=10.1002/gcc.20004;
von Bergh A.R.M., Wijers P.M., Groot A.J., van Zelderen-Bhola S.,
Falkenburg J.H.F., Kluin P.M., Schuuring E.;
"Identification of a novel RAS GTPase-activating protein (RASGAP) gene
at 9q34 as an MLL fusion partner in a patient with de novo acute
myeloid leukemia.";
Genes Chromosomes Cancer 39:324-334(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Brain;
PubMed=11214970; DOI=10.1093/dnares/7.6.347;
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:347-355(2000).
[4]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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).
[8]
FUNCTION, INTERACTION WITH MAP3K5, AND MUTAGENESIS OF
228-LYS--LYS-230; 281-LYS--LYS-284 AND ARG-413.
PubMed=12813029; DOI=10.1172/JCI200317790;
Zhang R., He X., Liu W., Lu M., Hsieh J.-T., Min W.;
"AIP1 mediates TNF-alpha-induced ASK1 activation by facilitating
dissociation of ASK1 from its inhibitor 14-3-3.";
J. Clin. Invest. 111:1933-1943(2003).
[9]
SUBCELLULAR LOCATION, AND INTERACTION WITH TNFR1; MAP3K5; TRADD;
RALBP1 AND TRAF2.
PubMed=15310755; DOI=10.1074/jbc.M407617200;
Zhang H., Zhang R., Luo Y., D'Alessio A., Pober J.S., Min W.;
"AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-
induced ASK1-JNK activation.";
J. Biol. Chem. 279:44955-44965(2004).
[10]
INTERACTION WITH HIPK1, AND SUBCELLULAR LOCATION.
PubMed=15701637; DOI=10.1074/jbc.M414262200;
Li X., Zhang R., Luo D., Park S.-J., Wang Q., Kim Y., Min W.;
"Tumor necrosis factor alpha-induced desumoylation and cytoplasmic
translocation of homeodomain-interacting protein kinase 1 are critical
for apoptosis signal-regulating kinase 1-JNK/p38 activation.";
J. Biol. Chem. 280:15061-15070(2005).
[11]
FUNCTION, INTERACTION WITH 14-3-3 PROTEINS; MAP3K5; RIPK1 AND TRAF2,
PHOSPHORYLATION AT SER-728, MUTAGENESIS OF SER-728 AND THR-935, AND
TISSUE SPECIFICITY.
PubMed=17389591; DOI=10.1074/jbc.M701148200;
Zhang H., Zhang H., Lin Y., Li J., Pober J.S., Min W.;
"RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is
critical for tumor necrosis factor-induced ASK1-JNK/p38 activation.";
J. Biol. Chem. 282:14788-14796(2007).
[12]
FUNCTION, AND MUTAGENESIS OF SER-728.
PubMed=18292600; DOI=10.1161/CIRCRESAHA.107.168153;
Min W., Lin Y., Tang S., Yu L., Zhang H., Wan T., Luhn T., Fu H.,
Chen H.;
"AIP1 recruits phosphatase PP2A to ASK1 in tumor necrosis factor-
induced ASK1-JNK activation.";
Circ. Res. 102:840-848(2008).
[13]
FUNCTION, INTERACTION WITH KDR AND P85 SUBUNIT OF PI3K, AND
MUTAGENESIS OF 228-LYS--LYS-230 AND 281-LYS--LYS-284.
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).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
FUNCTION, INTERACTION WITH AKT1 AND P85 SUBUNIT OF PI3K,
PHOSPHORYLATION AT SER-728, AND MUTAGENESIS OF ARG-413; SER-728 AND
920-PRO--PRO-929.
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).
[16]
FUNCTION, INTERACTION WITH PHOSPHATIDYLINOSITOL, SUBCELLULAR LOCATION,
AND MUTAGENESIS OF ARG-413.
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).
[17]
FUNCTION IN PROSTATE CANCER, INDUCTION, AND MUTAGENESIS OF ARG-413 AND
SER-728.
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).
[18]
FUNCTION IN PROSTATE CANCER, AND INTERACTION WITH GSK3B AND PPP2CA.
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).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
FUNCTION, INTERACTION WITH JAK2, AND TISSUE SPECIFICITY.
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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-978, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747; SER-978 AND
SER-995, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- 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:12813029,
ECO:0000269|PubMed:17389591, ECO:0000269|PubMed:18292600,
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}.
-!- 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. 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.
{ECO:0000250, ECO:0000269|PubMed:12813029,
ECO:0000269|PubMed:15310755, ECO:0000269|PubMed:15701637,
ECO:0000269|PubMed:17389591, ECO:0000269|PubMed:19033661,
ECO:0000269|PubMed:19903888, ECO:0000269|PubMed:19948740,
ECO:0000269|PubMed:20080667, ECO:0000269|PubMed:21700930}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-2871881, EBI-2871881;
O15169:AXIN1; NbExp=2; IntAct=EBI-9543020, EBI-710484;
P49841:GSK3B; NbExp=2; IntAct=EBI-9543020, EBI-373586;
Q99683:MAP3K5; NbExp=2; IntAct=EBI-2871881, EBI-476263;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000305};
Peripheral membrane protein {ECO:0000305}. Membrane. Cell
projection, dendrite {ECO:0000250}. 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. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q5VWQ8-1; Sequence=Displayed;
Note=Gene prediction based on EST data.;
Name=2;
IsoId=Q5VWQ8-2; Sequence=VSP_020953;
Name=3;
IsoId=Q5VWQ8-3; Sequence=VSP_020952, VSP_020954;
Name=4;
IsoId=Q5VWQ8-4; Sequence=VSP_020953, VSP_020954;
Name=5;
IsoId=Q5VWQ8-5; Sequence=VSP_047361, VSP_020954;
Note=Gene prediction based on EST data.;
-!- TISSUE SPECIFICITY: Expressed in endothelial and vascular smooth
muscle cells (VSMCs). Expressed in prostate epithelial but poorly
in prostate cancer cells. Poorly expressed in medulloblastoma
cells compared to cerebellar precursor proliferating progenitor
cells (at protein level). Low expression in prostate. Down-
regulated in prostate cancer. {ECO:0000269|PubMed:11944990,
ECO:0000269|PubMed:17389591, ECO:0000269|PubMed:21700930,
ECO:0000269|PubMed:22696229}.
-!- INDUCTION: Down-regulated in prostate cancer and medulloblastoma.
{ECO:0000269|PubMed:20154697, ECO:0000269|PubMed:22696229}.
-!- DOMAIN: The C2 and Ras-GAP domains constitutively bind to MAP3K5
and facilitate the release of 14-3-3 proteins from MAP3K5. The PH
and Ras-GAP domains, but not the NPXY motif, are crucial for its
cell membrane localization and neuronal migration function. The PH
domain is necessary but not sufficient to activate the JNK
signaling pathway through ERN1 (By similarity). Exists in a closed
inactive form by an intramolecular interaction between the N- and
the C-terminal domains. The proline-rich motif is critical both
for PI3K-AKT activity inhibition and MAP3K5 activation. The PH and
C2 domains are necessary for the binding to phosphatidylinositol
phosphate. The Ras-GAP domain is necessary for its tumor-
suppressive function. {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:0000269|PubMed:17389591, ECO:0000269|PubMed:19903888}.
-!- DISEASE: Note=A chromosomal aberration involving DAB2IP is found
in a patient with acute myeloid leukemia (AML). Translocation
t(9;11)(q34;q23) with KMT2A/MLL1. May give rise to a KMT2A/MLL1-
DAB2IP fusion protein lacking the PH domain (PubMed:14978793).
{ECO:0000269|PubMed:14978793}.
-!- MISCELLANEOUS: The DAB2IP gene is found epigenetically silenced in
numerous aggressive cancers, like prostate cancers and
medulloblastoma tumors. Epigenetic suppression of DAB2IP by EZH2
is a major mechanism of DAB2IP inactivation in human prostate
cancer and increases metastatic potential (PubMed:20154697,
PubMed:22696229). {ECO:0000305|PubMed:20154697,
ECO:0000305|PubMed:22696229}.
-!- SEQUENCE CAUTION:
Sequence=CAH72155.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/AF9q34ID316.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF367051; AAM00371.1; -; mRNA.
EMBL; AY032952; AAK50336.1; -; mRNA.
EMBL; AB051530; BAB21834.2; -; mRNA.
EMBL; AL357936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL365274; CAH72155.3; ALT_SEQ; Genomic_DNA.
EMBL; AL365274; CAQ10385.1; -; Genomic_DNA.
EMBL; AL365274; CAH72158.1; -; Genomic_DNA.
EMBL; CH471090; EAW87503.1; -; Genomic_DNA.
EMBL; CH471090; EAW87504.1; -; Genomic_DNA.
EMBL; BC146762; AAI46763.1; -; mRNA.
CCDS; CCDS6832.1; -. [Q5VWQ8-2]
CCDS; CCDS6833.2; -. [Q5VWQ8-5]
RefSeq; NP_115941.2; NM_032552.3. [Q5VWQ8-5]
RefSeq; NP_619723.1; NM_138709.2. [Q5VWQ8-2]
RefSeq; XP_005251776.1; XM_005251719.4. [Q5VWQ8-1]
RefSeq; XP_011516572.1; XM_011518270.2. [Q5VWQ8-2]
RefSeq; XP_011516573.1; XM_011518271.2. [Q5VWQ8-2]
RefSeq; XP_016869789.1; XM_017014300.1. [Q5VWQ8-2]
UniGene; Hs.522378; -.
ProteinModelPortal; Q5VWQ8; -.
SMR; Q5VWQ8; -.
BioGrid; 127478; 43.
DIP; DIP-41721N; -.
IntAct; Q5VWQ8; 7.
MINT; MINT-268247; -.
STRING; 9606.ENSP00000259371; -.
iPTMnet; Q5VWQ8; -.
PhosphoSitePlus; Q5VWQ8; -.
DMDM; 116247768; -.
EPD; Q5VWQ8; -.
MaxQB; Q5VWQ8; -.
PaxDb; Q5VWQ8; -.
PeptideAtlas; Q5VWQ8; -.
PRIDE; Q5VWQ8; -.
Ensembl; ENST00000259371; ENSP00000259371; ENSG00000136848. [Q5VWQ8-5]
Ensembl; ENST00000309989; ENSP00000310827; ENSG00000136848. [Q5VWQ8-2]
Ensembl; ENST00000408936; ENSP00000386183; ENSG00000136848. [Q5VWQ8-1]
GeneID; 153090; -.
KEGG; hsa:153090; -.
UCSC; uc004bln.5; human. [Q5VWQ8-1]
CTD; 153090; -.
DisGeNET; 153090; -.
EuPathDB; HostDB:ENSG00000136848.16; -.
GeneCards; DAB2IP; -.
HGNC; HGNC:17294; DAB2IP.
MIM; 609205; gene.
neXtProt; NX_Q5VWQ8; -.
OpenTargets; ENSG00000136848; -.
PharmGKB; PA27133; -.
eggNOG; KOG3508; Eukaryota.
eggNOG; ENOG410XPU1; LUCA.
GeneTree; ENSGT00760000119092; -.
HOVERGEN; HBG006492; -.
InParanoid; Q5VWQ8; -.
KO; K19901; -.
OMA; PTMPRQN; -.
OrthoDB; EOG091G00ZZ; -.
PhylomeDB; Q5VWQ8; -.
TreeFam; TF105303; -.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
ChiTaRS; DAB2IP; human.
GeneWiki; DAB2IP; -.
GenomeRNAi; 153090; -.
PRO; PR:Q5VWQ8; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000136848; -.
CleanEx; HS_DAB2IP; -.
ExpressionAtlas; Q5VWQ8; baseline and differential.
Genevisible; Q5VWQ8; HS.
GO; GO:1990597; C:AIP1-IRE1 complex; IDA:ParkinsonsUK-UCL.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0044300; C:cerebellar mossy fiber; ISS:UniProtKB.
GO; GO:0044301; C:climbing fiber; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
GO; GO:1990032; C:parallel fiber; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0071889; F:14-3-3 protein binding; IDA:BHF-UCL.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0005123; F:death receptor binding; IPI:BHF-UCL.
GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:UniProtKB.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:BHF-UCL.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IDA:UniProtKB.
GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IDA:UniProtKB.
GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IDA:ParkinsonsUK-UCL.
GO; GO:0051721; F:protein phosphatase 2A binding; IDA:BHF-UCL.
GO; GO:0017124; F:SH3 domain binding; IDA:UniProtKB.
GO; GO:0035591; F:signaling adaptor activity; IDA:BHF-UCL.
GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IPI:UniProtKB.
GO; GO:0007257; P:activation of JUN kinase activity; IDA:BHF-UCL.
GO; GO:0000185; P:activation of MAPKKK activity; IDA:UniProtKB.
GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:ParkinsonsUK-UCL.
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; ISS:UniProtKB.
GO; GO:0044257; P:cellular protein catabolic process; IDA:UniProtKB.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:BHF-UCL.
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; IDA:UniProtKB.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:UniProtKB.
GO; GO:0072577; P:endothelial cell apoptotic process; TAS:BHF-UCL.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IMP:BHF-UCL.
GO; GO:0007252; P:I-kappaB phosphorylation; ISS: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; ISS:BHF-UCL.
GO; GO:0021819; P:layer formation in cerebral cortex; ISS:UniProtKB.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
GO; GO:0035414; P:negative regulation of catenin import into nucleus; ISS:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:1903363; P:negative regulation of cellular protein catabolic process; IDA:UniProtKB.
GO; GO:0010596; P:negative regulation of endothelial cell migration; IMP:UniProtKB.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:BHF-UCL.
GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IDA:UniProtKB.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISS:BHF-UCL.
GO; GO:0070317; P:negative regulation of G0 to G1 transition; IDA:UniProtKB.
GO; GO:0034260; P:negative regulation of GTPase activity; IMP:BHF-UCL.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:BHF-UCL.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
GO; GO:0043553; P:negative regulation of phosphatidylinositol 3-kinase activity; IDA:UniProtKB.
GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP: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; ISS:UniProtKB.
GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IDA:UniProtKB.
GO; GO:1900006; P:positive regulation of dendrite development; ISS:UniProtKB.
GO; GO:1903896; P:positive regulation of IRE1-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
GO; GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:BHF-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
GO; GO:2001224; P:positive regulation of neuron migration; ISS:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IMP:UniProtKB.
GO; GO:0045732; P:positive regulation of protein catabolic process; ISS:UniProtKB.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0090129; P:positive regulation of synapse maturation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA: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; ISS:UniProtKB.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:1900744; P:regulation of p38MAPK cascade; ISS:UniProtKB.
GO; GO:0043254; P:regulation of protein complex assembly; IDA:UniProtKB.
GO; GO:0043497; P:regulation of protein heterodimerization activity; IDA:ParkinsonsUK-UCL.
GO; GO:0035148; P:tube formation; IMP:UniProtKB.
GO; GO:0036324; P:vascular endothelial growth factor receptor-2 signaling pathway; ISS: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; Chromosomal rearrangement;
Coiled coil; Complete proteome; Cytoplasm; Developmental protein;
Growth regulation; GTPase activation; Immunity; Inflammatory response;
Innate immunity; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Stress response; Tumor suppressor;
Unfolded protein response.
CHAIN 1 1189 Disabled homolog 2-interacting protein.
/FTId=PRO_0000252407.
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:0000269|PubMed:19903888}.
COILED 1026 1159 {ECO:0000255}.
COMPBIAS 8 52 Arg-rich.
COMPBIAS 112 117 Poly-Ala.
COMPBIAS 867 870 Poly-Ala.
COMPBIAS 903 948 Pro-rich.
SITE 172 173 Breakpoint for translocation to form
KMT2A/MLL1-DAB2IP.
MOD_RES 728 728 Phosphoserine; by MAP3K5 and RIPK1.
{ECO:0000269|PubMed:17389591,
ECO:0000269|PubMed:19903888}.
MOD_RES 747 747 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 978 978 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 995 995 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 193 Missing (in isoform 3).
{ECO:0000303|PubMed:11944990}.
/FTId=VSP_020952.
VAR_SEQ 1 124 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:11214970,
ECO:0000303|PubMed:14978793,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_020953.
VAR_SEQ 2 41 SAGGSARKSTGRSSYYYRLLRRPRLQRQRSRSRSRTRPAR
-> EPDSLLDQDDSY (in isoform 5).
{ECO:0000305}.
/FTId=VSP_047361.
VAR_SEQ 1158 1189 RYSMQARNGISPTNPTKLQITENGEFRNSSNC -> SMH
(in isoform 3, isoform 4 and isoform 5).
{ECO:0000303|PubMed:11214970,
ECO:0000303|PubMed:11944990,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_020954.
VARIANT 59 59 S -> F (in dbSNP:rs7027492).
/FTId=VAR_056858.
MUTAGEN 228 230 KKK->AAA: Reduces interaction with
KDR/VEGFR2. Does not inhibit interaction
with MAP3K5.
{ECO:0000269|PubMed:12813029,
ECO:0000269|PubMed:19033661}.
MUTAGEN 281 284 KKKK->AAAA: Significantly reduces
interaction with MAP3K5. Does not reduce
interaction with KDR/VEGFR2.
{ECO:0000269|PubMed:12813029,
ECO:0000269|PubMed:19033661}.
MUTAGEN 413 413 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.
{ECO:0000269|PubMed:12813029,
ECO:0000269|PubMed:19903888,
ECO:0000269|PubMed:19948740,
ECO:0000269|PubMed:20154697}.
MUTAGEN 728 728 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.
{ECO:0000269|PubMed:17389591,
ECO:0000269|PubMed:18292600,
ECO:0000269|PubMed:19903888,
ECO:0000269|PubMed:20154697}.
MUTAGEN 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.
{ECO:0000269|PubMed:19903888}.
MUTAGEN 935 935 T->A: Does not reduce interaction with
14-3-3 proteins.
{ECO:0000269|PubMed:17389591}.
CONFLICT 482 482 I -> T (in Ref. 1; AAM00371).
{ECO:0000305}.
CONFLICT 921 921 P -> S (in Ref. 1; AAM00371).
{ECO:0000305}.
CONFLICT 1091 1092 QQ -> HE (in Ref. 1; AAM00371).
{ECO:0000305}.
SEQUENCE 1189 AA; 131625 MW; 7494FF05AACF3320 CRC64;
MSAGGSARKS TGRSSYYYRL LRRPRLQRQR SRSRSRTRPA RESPQERPGS RRSLPGSLSE
KSPSMEPSAA TPFRVTGFLS RRLKGSIKRT KSQPKLDRNH SFRHILPGFR SAAAAAADNE
RSHLMPRLKE SRSHESLLSP SSAVEALDLS MEEEVVIKPV HSSILGQDYC FEVTTSSGSK
CFSCRSAAER DKWMENLRRA VHPNKDNSRR VEHILKLWVI EAKDLPAKKK YLCELCLDDV
LYARTTGKLK TDNVFWGEHF EFHNLPPLRT VTVHLYRETD KKKKKERNSY LGLVSLPAAS
VAGRQFVEKW YPVVTPNPKG GKGPGPMIRI KARYQTITIL PMEMYKEFAE HITNHYLGLC
AALEPILSAK TKEEMASALV HILQSTGKVK DFLTDLMMSE VDRCGDNEHL IFRENTLATK
AIEEYLKLVG QKYLQDALGE FIKALYESDE NCEVDPSKCS AADLPEHQGN LKMCCELAFC
KIINSYCVFP RELKEVFASW RQECSSRGRP DISERLISAS LFLRFLCPAI MSPSLFNLLQ
EYPDDRTART LTLIAKVTQN LANFAKFGSK EEYMSFMNQF LEHEWTNMQR FLLEISNPET
LSNTAGFEGY IDLGRELSSL HSLLWEAVSQ LEQSIVSKLG PLPRILRDVH TALSTPGSGQ
LPGTNDLAST PGSGSSSISA GLQKMVIEND LSGLIDFTRL PSPTPENKDL FFVTRSSGVQ
PSPARSSSYS EANEPDLQMA NGGKSLSMVD LQDARTLDGE AGSPAGPDVL PTDGQAAAAQ
LVAGWPARAT PVNLAGLATV RRAGQTPTTP GTSEGAPGRP QLLAPLSFQN PVYQMAAGLP
LSPRGLGDSG SEGHSSLSSH SNSEELAAAA KLGSFSTAAE ELARRPGELA RRQMSLTEKG
GQPTVPRQNS AGPQRRIDQP PPPPPPPPPA PRGRTPPNLL STLQYPRPSS GTLASASPDW
VGPSTRLRQQ SSSSKGDSPE LKPRAVHKQG PSPVSPNALD RTAAWLLTMN AQLLEDEGLG
PDPPHRDRLR SKDELSQAEK DLAVLQDKLR ISTKKLEEYE TLFKCQEETT QKLVLEYQAR
LEEGEERLRR QQEDKDIQMK GIISRLMSVE EELKKDHAEM QAAVDSKQKI IDAQEKRIAS
LDAANARLMS ALTQLKERYS MQARNGISPT NPTKLQITEN GEFRNSSNC


Related products :

Catalog number Product name Quantity
EIAAB10371 AF9Q34,AIP1,ASK-interacting protein 1,DAB2 interaction protein,DAB2-interacting protein,DAB2IP,Disabled homolog 2-interacting protein,Homo sapiens,Human,KIAA1743
EIAAB10370 DAB2-interacting protein,Dab2ip,DIP1_2,Disabled homolog 2-interacting protein,DOC-2_DAB2 interactive protein,Rat,Rattus norvegicus
EIAAB10372 DAB2-interacting protein,Dab2ip,Disabled homolog 2-interacting protein,Kiaa1743,Mouse,Mus musculus
EIAAB27543 Dab2-interacting protein 2,Daip2,Disabled homolog 2-interacting protein 2,eNOS-trafficking inducer,Mouse,Mus musculus,Nitric oxide synthase trafficker,Nostrin,Nostrin
EIAAB31034 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Homo sapiens,Human,Miz1,Msx-interacting zinc finger protein,PIAS2,PIAS-NY protein,PIASX,Protein
EIAAB31033 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Miz1,Mouse,Msx-interacting zinc finger protein,Mus musculus,Pias2,Piasx,Protein inhibitor of act
EIAAB31032 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Miz1,Msx-interacting-zinc finger protein,Pias2,Piasx,Protein inhibitor of activated STAT x,Prote
18-003-42690 Protein inhibitor of activated STAT2 - Protein inhibitor of activated STAT x; Msx-interacting zinc finger protein; Miz1; DAB2-interacting protein; DIP; Androgen receptor-interacting protein 3; ARIP3; 0.1 mg Protein A
18-003-42689 Protein inhibitor of activated STAT2 - Protein inhibitor of activated STAT x; Msx-interacting zinc finger protein; Miz1; DAB2-interacting protein; DIP; Androgen receptor-interacting protein 3; ARIP3; 0.1 mg Protein A
18-003-43466 E3 SUMO-protein ligase PIAS2 - Protein inhibitor of activated STAT2; Protein inhibitor of activated STAT x; Msx-interacting zinc finger protein; DAB2-interacting protein; DIP; Androgen receptor-intera 0.05 mg Aff Pur
EIAAB39347 Mouse,Mus musculus,Spata24,Spermatogenesis-associated protein 24,TATA-binding protein-like factor-interacting protein,Testis protein T6441 homolog,Tipt,Tipt2,TLF-interacting protein,TRF2-interacting p
EIAAB27017 45 kDa NF-AT-interacting protein,45 kDa NFAT-interacting protein,Homo sapiens,Human,NFATC2-interacting protein,NFATC2IP,NIP45,Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
EIAAB27018 45 kDa NF-AT-interacting protein,45 kDa NFAT-interacting protein,Mouse,Mus musculus,NFATC2-interacting protein,Nfatc2ip,Nip45,Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
15-288-22308F GIPC PDZ domain-containing protein 1 - RGS19-interacting protein 1; GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; Tax interaction protein 2; TIP-2 Polyclonal 0.1 mg
18-003-44197 PDZ domain-containing protein GIPC1 - RGS19-interacting protein 1; GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; Tax interaction protein 2; TIP-2 Polyclonal 0.05 mg Aff Pur
15-288-22308F GIPC PDZ domain-containing protein 1 - RGS19-interacting protein 1; GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; Tax interaction protein 2; TIP-2 Polyclonal 0.05 mg
10-288-22308F GIPC PDZ domain-containing protein 1 - RGS19-interacting protein 1; GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; Tax interaction protein 2; TIP-2 0.05 mg
10-288-22308F GIPC PDZ domain-containing protein 1 - RGS19-interacting protein 1; GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; Tax interaction protein 2; TIP-2 0.1 mg
EIAAB31218 Homo sapiens,hPIP1,Human,p21-activated protein kinase-interacting protein 1,PAK_PLC-interacting protein 1,PAK1-interacting protein 1,PAK1IP1,PIP1,WD repeat-containing protein 84,WDR84
EIAAB46349 Homo sapiens,Human,Protein PRPL-2,WAS_WASL-interacting protein family member 1,WASP-interacting protein,WASPIP,WIP,WIPF1,Wiskott-Aldrich syndrome protein-interacting protein
EIAAB07420 Cdc42-interacting protein 4,CIP4,Homo sapiens,hSTP,Human,Protein Felic,Salt tolerant protein,STOT,STP,Thyroid receptor-interacting protein 10,TR-interacting protein 10,TRIP10,TRIP-10
U1313b CLIA Bos taurus,Bovine,HBV X-interacting protein homolog,HBX-interacting protein homolog,HBXIP,Hepatitis B virus X-interacting protein homolog 96T
E1313b ELISA kit Bos taurus,Bovine,HBV X-interacting protein homolog,HBX-interacting protein homolog,HBXIP,Hepatitis B virus X-interacting protein homolog 96T
E1313m ELISA kit HBV X-interacting protein homolog,HBX-interacting protein homolog,Hbxip,Hepatitis B virus X-interacting protein homolog,Mouse,Mus musculus,Xip 96T
U1313m CLIA HBV X-interacting protein homolog,HBX-interacting protein homolog,Hbxip,Hepatitis B virus X-interacting protein homolog,Mouse,Mus musculus,Xip 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur