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Disabled homolog 2 (Adaptor molecule disabled-2) (Differentially expressed in ovarian carcinoma 2) (DOC-2) (Differentially-expressed protein 2)

 DAB2_HUMAN              Reviewed;         770 AA.
P98082; A6NES5; Q13598; Q9BTY0; Q9UK04;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
17-APR-2007, sequence version 3.
02-JUN-2021, entry version 192.
RecName: Full=Disabled homolog 2;
AltName: Full=Adaptor molecule disabled-2;
AltName: Full=Differentially expressed in ovarian carcinoma 2;
Short=DOC-2;
AltName: Full=Differentially-expressed protein 2;
Name=DAB2; Synonyms=DOC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
PubMed=8660969; DOI=10.1006/geno.1996.0185;
Albertsen H.M., Smith S.A., Melis R., Williams B., Holik P., Stevens J.,
White R.;
"Sequence, genomic structure, and chromosomal assignment of human DOC-2.";
Genomics 33:207-213(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND ALTERNATIVE
SPLICING.
TISSUE=Ovary;
PubMed=9620555; DOI=10.1038/sj.onc.1201769;
Mok S.C., Chan W.Y., Wong K.-K., Cheung K.K., Lau C.C., Ng S.W.,
Baldini A., Colitti C.V., Rock C.O., Berkowitz R.S.;
"DOC-2, a candidate tumor suppressor gene in human epithelial ovarian
cancer.";
Oncogene 16:2381-2387(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
PubMed=10340382; DOI=10.1038/sj.onc.1202649;
Fazili Z., Sun W., Mittelstaedt S., Cohen C., Xu X.-X.;
"Disabled-2 inactivation is an early step in ovarian tumorigenicity.";
Oncogene 18:3104-3113(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 3).
PubMed=11161789; DOI=10.1006/geno.2000.6383;
Sheng Z., He J., Tuppen J.A., Sun W., Fazili Z., Smith E.R., Dong F.B.,
Xu X.-X.;
"Structure, sequence, and promoter analysis of human disabled-2 gene
(DAB2).";
Genomics 70:381-386(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 44-304 (ISOFORM 1).
TISSUE=Ovary;
PubMed=8314147; DOI=10.1006/gyno.1994.1040;
Mok S.C., Wong K.-K., Chan R.K.W., Lau C.C., Tsao S.-W., Knapp R.C.,
Berkowitz R.S.;
"Molecular cloning of differentially expressed genes in human epithelial
ovarian cancer.";
Gynecol. Oncol. 52:247-252(1994).
[9]
INTERACTION WITH LRP2.
PubMed=10769163; DOI=10.1042/bj3470613;
Oleinikov A.V., Zhao J., Makker S.P.;
"Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic
receptor gp600/megalin.";
Biochem. J. 347:613-621(2000).
[10]
FUNCTION, INTERACTION WITH SMAD2; SMAD3; TGFBR1 AND TGFBR2, AND MUTAGENESIS
OF PHE-166.
PubMed=11387212; DOI=10.1093/emboj/20.11.2789;
Hocevar B.A., Smine A., Xu X.X., Howe P.H.;
"The adaptor molecule Disabled-2 links the transforming growth factor beta
receptors to the Smad pathway.";
EMBO J. 20:2789-2801(2001).
[11]
INTERACTION WITH MYO6, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
684-SER--PHE-686.
PubMed=11967127; DOI=10.1034/j.1600-0854.2002.30503.x;
Morris S.M., Arden S.D., Roberts R.C., Kendrick-Jones J., Cooper J.A.,
Luzio J.P., Buss F.;
"Myosin VI binds to and localises with Dab2, potentially linking receptor-
mediated endocytosis and the actin cytoskeleton.";
Traffic 3:331-341(2002).
[12]
FUNCTION, AND INTERACTION WITH DVL3 AND AXIN1.
PubMed=12805222; DOI=10.1093/emboj/cdg286;
Howe P.H.;
"Regulation of the Wnt signaling pathway by disabled-2 (Dab2).";
EMBO J. 22:3084-3094(2003).
[13]
INTERACTION WITH SH3KBP1, AND MUTAGENESIS OF ARG-720.
PubMed=14596919; DOI=10.1016/s0014-5793(03)01111-6;
Kowanetz K., Terzic J., Dikic I.;
"Dab2 links CIN85 with clathrin-mediated receptor internalization.";
FEBS Lett. 554:81-87(2003).
[14]
INTERACTION WITH LRP2, AND TISSUE SPECIFICITY.
PubMed=15134832; DOI=10.1016/j.biochi.2004.03.001;
Gallagher H., Oleinikov A.V., Fenske C., Newman D.J.;
"The adaptor disabled-2 binds to the third psi xNPxY sequence on the
cytoplasmic tail of megalin.";
Biochimie 86:179-182(2004).
[15]
FUNCTION.
PubMed=16267015; DOI=10.1158/0008-5472.can-05-1481;
Zhoul J., Hernandez G., Tu S.W., Huang C.L., Tseng C.P., Hsieh J.T.;
"The role of DOC-2/DAB2 in modulating androgen receptor-mediated cell
growth via the nongenomic c-Src-mediated pathway in normal prostatic
epithelium and cancer.";
Cancer Res. 65:9906-9913(2005).
[16]
FUNCTION.
PubMed=16984970; DOI=10.1242/jcs.03217;
Maurer M.E., Cooper J.A.;
"The adaptor protein Dab2 sorts LDL receptors into coated pits
independently of AP-2 and ARH.";
J. Cell Sci. 119:4235-4246(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation
analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND 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).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
FUNCTION.
PubMed=19306879; DOI=10.1016/j.febslet.2009.03.037;
Chao W.T., Kunz J.;
"Focal adhesion disassembly requires clathrin-dependent endocytosis of
integrins.";
FEBS Lett. 583:1337-1343(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
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).
[23]
SUBCELLULAR LOCATION.
PubMed=21097498; DOI=10.1074/jbc.m110.161851;
Chetrit D., Barzilay L., Horn G., Bielik T., Smorodinsky N.I., Ehrlich M.;
"Negative regulation of the endocytic adaptor disabled-2 (Dab2) in
mitosis.";
J. Biol. Chem. 286:5392-5403(2011).
[24]
FUNCTION.
PubMed=21995445; DOI=10.1042/bj20111566;
Fu L., Rab A., Tang L.P., Rowe S.M., Bebok Z., Collawn J.F.;
"Dab2 is a key regulator of endocytosis and post-endocytic trafficking of
the cystic fibrosis transmembrane conductance regulator.";
Biochem. J. 441:633-643(2012).
[25]
FUNCTION, AND INTERACTION WITH LRP6.
PubMed=22491013; DOI=10.1038/emboj.2012.83;
Jiang Y., He X., Howe P.H.;
"Disabled-2 (Dab2) inhibits Wnt/beta-catenin signalling by binding LRP6 and
promoting its internalization through clathrin.";
EMBO J. 31:2336-2349(2012).
[26]
FUNCTION IN ENDOCYTOSIS, AND INTERACTION WITH FCHO2.
PubMed=22323290; DOI=10.1091/mbc.e11-09-0812;
Mulkearns E.E., Cooper J.A.;
"FCH domain only-2 organizes clathrin-coated structures and interacts with
Disabled-2 for low-density lipoprotein receptor endocytosis.";
Mol. Biol. Cell 23:1330-1342(2012).
[27]
INTERACTION WITH FCHO1.
PubMed=22484487; DOI=10.1038/ncb2473;
Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
Tsang M., Traub L.M.;
"Distinct and separable activities of the endocytic clathrin-coat
components Fcho1/2 and AP-2 in developmental patterning.";
Nat. Cell Biol. 14:488-501(2012).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401; SER-675 AND SER-723, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Adapter protein that functions as clathrin-associated sorting
protein (CLASP) required for clathrin-mediated endocytosis of selected
cargo proteins. Can bind and assemble clathrin, and binds
simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2)
and cargos containing non-phosphorylated NPXY internalization motifs,
such as the LDL receptor, to recruit them to clathrin-coated pits. Can
function in clathrin-mediated endocytosis independently of the AP-2
complex. Involved in endocytosis of integrin beta-1; this function
seems to redundant with the AP-2 complex and seems to require DAB2
binding to endocytosis accessory EH domain-containing proteins such as
EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis
transmembrane conductance regulator/CFTR. Involved in endocytosis of
megalin/LRP2 lipoprotein receptor during embryonal development.
Required for recycling of the TGF-beta receptor. Involved in CFTR
trafficking to the late endosome. Involved in several receptor-mediated
signaling pathways. Involved in TGF-beta receptor signaling and
facilitates phosphorylation of the signal transducer SMAD2. Mediates
TFG-beta-stimulated JNK activation. May inhibit the canoniocal
Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin
destruction complex through a competing association with axin
preventing its dephosphorylation through protein phosphatase 1 (PP1).
Sequesters LRP6 towards clathrin-mediated endocytosis, leading to
inhibition of Wnt/beta-catenin signaling. May activate non-canonical
Wnt signaling. In cell surface growth factor/Ras signaling pathways
proposed to inhibit ERK activation by interrupting the binding of GRB2
to SOS1 and to inhibit SRC by preventing its activating phosphorylation
at 'Tyr-419'. Proposed to be involved in modulation of androgen
receptor (AR) signaling mediated by SRC activation; seems to compete
with AR for interaction with SRC. Plays a role in the CSF-1 signal
transduction pathway. Plays a role in cellular differentiation.
Involved in cell positioning and formation of visceral endoderm (VE)
during embryogenesis and proposed to be required in the VE to respond
to Nodal signaling coming from the epiblast. Required for the
epithelial to mesenchymal transition, a process necessary for proper
embryonic development. May be involved in myeloid cell differentiation
and can induce macrophage adhesion and spreading. May act as a tumor
suppressor. {ECO:0000269|PubMed:11387212, ECO:0000269|PubMed:12805222,
ECO:0000269|PubMed:16267015, ECO:0000269|PubMed:16984970,
ECO:0000269|PubMed:19306879, ECO:0000269|PubMed:21995445,
ECO:0000269|PubMed:22323290, ECO:0000269|PubMed:22491013}.
-!- SUBUNIT: Interacts (via NPXY motif) with DAB2 (via PID domain). Can
interact (via PID domain) with LDLR, APP, APLP1 and APLP2, and weakly
with INPP5D (via NPXY motifs); the interaction is impaired by tyrosine
phosphorylation of the respective NPXY motifs. Can weakly interact (via
PID domain) with LRP1 (via NPXY motif); the interaction is enhanced by
tyrosine phosphorylation of the NPXY motif. Interacts with LRP2 (via
NPXY motif); the interaction is not affected by tyrosine
phosphorylation of the NPXY motif. Interacts with clathrin; in vitro
can assemble clathrin triskelia into polyhedral coats. Interacts with
AP2A2, ITGB1, ITGB3, ITGB5, PIAS2, DAB2IP, NOSTRIN, FCHO1, DVL3, EPS15,
ITSN1 and EPS15L1. Interacts with SH3KBP1 (via SH3 domains). Interacts
with GRB2; competes with SOS1 for binding to GRB2 and the interaction
is enhanced by EGF and NT-3 stimulation. Interacts with MAP3K7; the
interaction is induced by TGF-beta stimulation and may mediate TGF-beta
stimulated JNK activation. Interacts with AXIN1 and PPP1CA; the
interactions are mutually exclusive. Interacts with the globular tail
of MYO6. Interacts (via DPF motifs) with FCHO2; the interaction is
direct and required for DAB2-mediated LDLR endocytosis. Interacts with
LRP6; the interaction involves LRP6 phosphorylation by CK2 and
sequesters LRP6 towards clathrin-mediated endocytosis. Associates with
the TGF-beta receptor complex (Probable). Interacts with SMAD2 and
SMAD3; the interactions are enhanced upon TGF-beta stimulation.
Interacts with GRB2; the interaction is enhanced by EGF and NT-3
stimulation. Interacts with SRC; the interaction is enhanced by EGF
stimulation. {ECO:0000269|PubMed:10769163, ECO:0000269|PubMed:11387212,
ECO:0000269|PubMed:11967127, ECO:0000269|PubMed:12805222,
ECO:0000269|PubMed:14596919, ECO:0000269|PubMed:15134832,
ECO:0000269|PubMed:22323290, ECO:0000269|PubMed:22484487,
ECO:0000269|PubMed:22491013, ECO:0000305}.
-!- INTERACTION:
P98082; P05067: APP; NbExp=3; IntAct=EBI-1171238, EBI-77613;
P98082; P62993: GRB2; NbExp=2; IntAct=EBI-1171238, EBI-401755;
P98082; O75581: LRP6; NbExp=20; IntAct=EBI-1171238, EBI-910915;
P98082; Q9UM54: MYO6; NbExp=3; IntAct=EBI-1171238, EBI-350606;
P98082; P16333: NCK1; NbExp=2; IntAct=EBI-1171238, EBI-389883;
P98082; Q15796: SMAD2; NbExp=4; IntAct=EBI-1171238, EBI-1040141;
P98082; P84022: SMAD3; NbExp=3; IntAct=EBI-1171238, EBI-347161;
P98082; P00441: SOD1; NbExp=3; IntAct=EBI-1171238, EBI-990792;
P98082-1; Q29122: MYO6; Xeno; NbExp=2; IntAct=EBI-15804617, EBI-15804516;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle, clathrin-coated
vesicle membrane. Membrane, clathrin-coated pit. Note=Colocalizes with
large insert-containing isoforms of MYO6 at clathrin-coated
pits/vesicles. During mitosis is progressively displaced from the
membrane and translocated to the cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P98082-1; Sequence=Displayed;
Name=2;
IsoId=P98082-2; Sequence=VSP_004181;
Name=3;
IsoId=P98082-3; Sequence=VSP_038401;
-!- TISSUE SPECIFICITY: Expressed in deep invaginations, inclusion cysts
and the surface epithelial cells of the ovary. Also expressed in breast
epithelial cells, spleen, thymus, prostate, testis, macrophages,
fibroblasts, lung epithelial cells, placenta, brain stem, heart and
small intestine. Expressed in kidney proximal tubular epithelial cells
(at protein level). {ECO:0000269|PubMed:10340382,
ECO:0000269|PubMed:15134832, ECO:0000269|PubMed:9620555}.
-!- DOMAIN: The PID domain binds to predominantly non-phosphorylated NPXY
internalization motifs present in members of the LDLR and APP family;
it also mediates simultaneous binding to phosphatidylinositol 4,5-
bisphosphate. {ECO:0000250}.
-!- DOMAIN: The Asn-Pro-Phe (NPF) motifs, which are found in proteins
involved in the endocytic pathway, mediate the interaction with the EH
domain of EPS15, EPS15R and ITSN1. {ECO:0000250}.
-!- PTM: Phosphorylated. Phosphorylation during mitosis is leading to
membrane displacement (By similarity). {ECO:0000250}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/DAB2ID40258ch5p13.html";
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EMBL; U39050; AAC50824.1; -; mRNA.
EMBL; AH003698; AAB19032.1; -; Genomic_DNA.
EMBL; U53446; AAA98975.1; -; mRNA.
EMBL; AF188298; AAF05540.1; -; mRNA.
EMBL; AF205890; AAF23161.1; -; Genomic_DNA.
EMBL; AC008916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471119; EAW55989.1; -; Genomic_DNA.
EMBL; BC003064; AAH03064.1; -; mRNA.
EMBL; L16886; AAA93195.1; -; mRNA.
CCDS; CCDS34149.1; -. [P98082-1]
CCDS; CCDS58946.1; -. [P98082-3]
PIR; G02228; G02228.
RefSeq; NP_001231800.1; NM_001244871.1. [P98082-3]
RefSeq; NP_001334.2; NM_001343.3. [P98082-1]
PDB; 2LSW; NMR; -; A=24-58.
PDB; 6O5O; X-ray; 1.75 A; A/B=31-191.
PDB; 6OVF; X-ray; 1.95 A; A/B=31-191.
PDBsum; 2LSW; -.
PDBsum; 6O5O; -.
PDBsum; 6OVF; -.
BMRB; P98082; -.
SMR; P98082; -.
BioGRID; 107971; 109.
DIP; DIP-45617N; -.
ELM; P98082; -.
IntAct; P98082; 67.
MINT; P98082; -.
STRING; 9606.ENSP00000313391; -.
iPTMnet; P98082; -.
MetOSite; P98082; -.
PhosphoSitePlus; P98082; -.
BioMuta; DAB2; -.
DMDM; 145559465; -.
EPD; P98082; -.
jPOST; P98082; -.
MassIVE; P98082; -.
MaxQB; P98082; -.
PaxDb; P98082; -.
PeptideAtlas; P98082; -.
PRIDE; P98082; -.
ProteomicsDB; 57786; -. [P98082-1]
ProteomicsDB; 57787; -. [P98082-2]
ProteomicsDB; 57788; -. [P98082-3]
Antibodypedia; 3987; 305 antibodies.
DNASU; 1601; -.
Ensembl; ENST00000320816; ENSP00000313391; ENSG00000153071. [P98082-1]
Ensembl; ENST00000339788; ENSP00000345508; ENSG00000153071. [P98082-2]
Ensembl; ENST00000509337; ENSP00000426245; ENSG00000153071. [P98082-3]
Ensembl; ENST00000545653; ENSP00000439919; ENSG00000153071. [P98082-3]
GeneID; 1601; -.
KEGG; hsa:1601; -.
UCSC; uc003jlw.4; human. [P98082-1]
CTD; 1601; -.
DisGeNET; 1601; -.
GeneCards; DAB2; -.
HGNC; HGNC:2662; DAB2.
HPA; ENSG00000153071; Tissue enhanced (placenta).
MIM; 601236; gene.
neXtProt; NX_P98082; -.
OpenTargets; ENSG00000153071; -.
PharmGKB; PA27132; -.
VEuPathDB; HostDB:ENSG00000153071.14; -.
eggNOG; KOG3535; Eukaryota.
GeneTree; ENSGT00940000155567; -.
HOGENOM; CLU_020747_1_0_1; -.
InParanoid; P98082; -.
OMA; GKQFDQI; -.
PhylomeDB; P98082; -.
TreeFam; TF316724; -.
PathwayCommons; P98082; -.
Reactome; R-HSA-190873; Gap junction degradation.
Reactome; R-HSA-196025; Formation of annular gap junctions.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
SignaLink; P98082; -.
SIGNOR; P98082; -.
BioGRID-ORCS; 1601; 5 hits in 1002 CRISPR screens.
ChiTaRS; DAB2; human.
GeneWiki; DAB2; -.
GenomeRNAi; 1601; -.
Pharos; P98082; Tbio.
PRO; PR:P98082; -.
Proteomes; UP000005640; Chromosome 5.
RNAct; P98082; protein.
Bgee; ENSG00000153071; Expressed in placenta and 240 other tissues.
ExpressionAtlas; P98082; baseline and differential.
Genevisible; P98082; HS.
GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0038024; F:cargo receptor activity; IMP:UniProtKB.
GO; GO:0035615; F:clathrin adaptor activity; IMP:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0046332; F:SMAD binding; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0035026; P:leading edge cell differentiation; IMP:UniProtKB.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
GO; GO:0032091; P:negative regulation of protein binding; IMP:BHF-UCL.
GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IMP:UniProtKB.
GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IMP:UniProtKB.
GO; GO:0045807; P:positive regulation of endocytosis; IMP:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:UniProtKB.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:UniProtKB.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:BHF-UCL.
GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; IMP:BHF-UCL.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR006020; PTB/PI_dom.
Pfam; PF00640; PID; 1.
SMART; SM00462; PTB; 1.
PROSITE; PS01179; PID; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis; Coated pit;
Cytoplasm; Cytoplasmic vesicle; Developmental protein; Differentiation;
Endocytosis; Membrane; Phosphoprotein; Protein transport;
Reference proteome; Transport; Tumor suppressor; Wnt signaling pathway.
INIT_MET 1
/note="Removed"
/evidence="ECO:0007744|PubMed:19413330"
CHAIN 2..770
/note="Disabled homolog 2"
/id="PRO_0000079770"
DOMAIN 45..196
/note="PID"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
REGION 1..38
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 230..447
/note="Required for localization to clathrin-coated pits"
/evidence="ECO:0000250"
REGION 284..482
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 604..732
/note="Sufficient for interaction with GRB2"
/evidence="ECO:0000250"
REGION 604..629
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 619..627
/note="Required for interaction with CSK"
/evidence="ECO:0000250"
REGION 649..770
/note="Required for interaction with MYO6"
/evidence="ECO:0000250"
REGION 663..671
/note="Required for interaction with GRB2 and CSK"
/evidence="ECO:0000250"
REGION 709..725
/note="Sufficient for interaction with SH3KBP1 SH3 domain"
/evidence="ECO:0000250"
REGION 742..770
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOTIF 293..295
/note="DPF 1"
MOTIF 298..300
/note="DPF 2"
COMPBIAS 1..18
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 21..38
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 300..335
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 344..397
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 407..430
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 466..482
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 615..629
/note="Pro residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 742..760
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 2
/note="N-acetylserine"
/evidence="ECO:0007744|PubMed:19413330"
MOD_RES 2
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O88797"
MOD_RES 170
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P98078"
MOD_RES 193
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P98078"
MOD_RES 326
/note="Phosphoserine; in mitosis"
/evidence="ECO:0000250|UniProtKB:O88797"
MOD_RES 328
/note="Phosphoserine; in mitosis"
/evidence="ECO:0000250|UniProtKB:O88797"
MOD_RES 401
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:16964243,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
MOD_RES 675
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 723
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 729
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P98078"
VAR_SEQ 209..229
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:10340382,
ECO:0000303|PubMed:11161789"
/id="VSP_038401"
VAR_SEQ 230..447
/note="Missing (in isoform 2)"
/evidence="ECO:0000305"
/id="VSP_004181"
VARIANT 586
/note="T -> I (in dbSNP:rs700241)"
/id="VAR_031705"
VARIANT 634
/note="S -> N (in dbSNP:rs3733801)"
/id="VAR_050942"
MUTAGEN 166
/note="F->A: Impairs TGF-beta receptor signaling, no effect
on interaction with SMAD2."
/evidence="ECO:0000269|PubMed:11387212"
MUTAGEN 684..686
/note="SYF->AAA: Greatly reduced binding to MYO6."
/evidence="ECO:0000269|PubMed:11967127"
MUTAGEN 720
/note="R->A: Abolishes interaction with SH3KBP1."
/evidence="ECO:0000269|PubMed:14596919"
CONFLICT 44..47
/note="KGDG -> PRVC (in Ref. 8; AAA93195)"
/evidence="ECO:0000305"
CONFLICT 82
/note="A -> R (in Ref. 1; AAC50824/AAB19032, 2; AAA98975,
4; AAF23161 and 8; AAA93195)"
/evidence="ECO:0000305"
CONFLICT 148
/note="A -> T (in Ref. 2; AAA98975)"
/evidence="ECO:0000305"
CONFLICT 197
/note="M -> R (in Ref. 2; AAA98975)"
/evidence="ECO:0000305"
CONFLICT 230..232
/note="ESK -> VCF (in Ref. 3; AAF05540 and 8; AAA93195)"
/evidence="ECO:0000305"
CONFLICT 275
/note="L -> S (in Ref. 1; AAC50824)"
/evidence="ECO:0000305"
CONFLICT 302..304
/note="QPD -> HTR (in Ref. 8; AAA93195)"
/evidence="ECO:0000305"
CONFLICT 498
/note="L -> Q (in Ref. 3; AAF05540)"
/evidence="ECO:0000305"
STRAND 29..31
/evidence="ECO:0007829|PDB:2LSW"
HELIX 36..43
/evidence="ECO:0007829|PDB:6O5O"
TURN 44..46
/evidence="ECO:0007829|PDB:2LSW"
STRAND 48..59
/evidence="ECO:0007829|PDB:6O5O"
STRAND 61..63
/evidence="ECO:0007829|PDB:6O5O"
HELIX 66..85
/evidence="ECO:0007829|PDB:6O5O"
STRAND 91..98
/evidence="ECO:0007829|PDB:6O5O"
STRAND 101..106
/evidence="ECO:0007829|PDB:6O5O"
TURN 107..109
/evidence="ECO:0007829|PDB:6O5O"
STRAND 112..116
/evidence="ECO:0007829|PDB:6O5O"
HELIX 118..120
/evidence="ECO:0007829|PDB:6O5O"
STRAND 121..126
/evidence="ECO:0007829|PDB:6O5O"
STRAND 133..138
/evidence="ECO:0007829|PDB:6O5O"
STRAND 145..153
/evidence="ECO:0007829|PDB:6O5O"
HELIX 156..180
/evidence="ECO:0007829|PDB:6O5O"
SEQUENCE 770 AA; 82448 MW; 5B2F8B510A580A77 CRC64;
MSNEVETSAT NGQPDQQAAP KAPSKKEKKK GPEKTDEYLL ARFKGDGVKY KAKLIGIDDV
PDARGDKMSQ DSMMKLKGMA AAGRSQGQHK QRIWVNISLS GIKIIDEKTG VIEHEHPVNK
ISFIARDVTD NRAFGYVCGG EGQHQFFAIK TGQQAEPLVV DLKDLFQVIY NVKKKEEEKK
KIEEASKAVE NGSEALMILD DQTNKLKSGV DQMDLFGDMS TPPDLNSPTE SKDILLVDLN
SEIDTNQNSL RENPFLTNGI TSCSLPRPTP QASFLPENAF SANLNFFPTP NPDPFRDDPF
TQPDQSTPSS FDSLKSPDQK KENSSSSSTP LSNGPLNGDV DYFGQQFDQI SNRTGKQEAQ
AGPWPFSSSQ TQPAVRTQNG VSEREQNGFS VKSSPNPFVG SPPKGLSIQN GVKQDLESSV
QSSPHDSIAI IPPPQSTKPG RGRRTAKSSA NDLLASDIFA PPVSEPSGQA SPTGQPTALQ
PNPLDLFKTS APAPVGPLVG LGGVTVTLPQ AGPWNTASLV FNQSPSMAPG AMMGGQPSGF
SQPVIFGTSP AVSGWNQPSP FAASTPPPVP VVWGPSASVA PNAWSTTSPL GNPFQSNIFP
APAVSTQPPS MHSSLLVTPP QPPPRAGPPK DISSDAFTAL DPLGDKEIKD VKEMFKDFQL
RQPPAVPARK GEQTSSGTLS AFASYFNSKV GIPQENADHD DFDANQLLNK INEPPKPAPR
QVSLPVTKST DNAFENPFFK DSFGSSQASV ASSQPVSSEM YRDPFGNPFA


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DEFI6_HUMAN Human ELISA Kit FOR Differentially expressed in FDCP 6 homolog 96T
CSB-EL006651MO Mouse Differentially expressed in FDCP 8 homolog(DEF8) ELISA kit 96T
CSB-EL006650HU Human Differentially expressed in FDCP 6 homolog(DEF6) ELISA kit 96T
CSB-EL006650MO Mouse Differentially expressed in FDCP 6 homolog(DEF6) ELISA kit 96T
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CSB-EL006651HU Human Differentially expressed in FDCP 8 homolog(DEF8) ELISA kit 96T
EIAAB10879 Bos taurus,Bovine,DEF8,DEF-8,Differentially expressed in FDCP 8 homolog
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CSB-EL006650HU Human Differentially expressed in FDCP 6 homolog(DEF6) ELISA kit SpeciesHuman 96T
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Pathways :
WP2292: Chemokine signaling pathway
WP1003: Ovarian Infertility Genes
WP1693: Purine metabolism
WP813: G Protein Signaling Pathways
WP1650: Fluorobenzoate degradation
WP1659: Glycine, serine and threonine metabolism
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP1165: G Protein Signaling Pathways
WP1713: Two-component system
WP1438: Influenza A virus infection
WP1892: Protein folding
WP1665: Limonene and pinene degradation
WP263: Ovarian Infertility Genes
WP1675: Nitrogen metabolism
WP34: Ovarian Infertility Genes
WP1531: Vitamin D synthesis
WP2032: TSH signaling pathway
WP1616: ABC transporters
WP2199: Seed Development
WP1685: Peptidoglycan biosynthesis
WP525: Mitochondrial Unfolded-Protein Response
WP1692: Protein export
WP773: Ovarian Infertility Genes
WP1644: DNA replication
WP2272: Pathogenic Escherichia coli infection

Related Genes :
[TPX2 C20orf1 C20orf2 DIL2 HCA519] Targeting protein for Xklp2 (Differentially expressed in cancerous and non-cancerous lung cells 2) (DIL-2) (Hepatocellular carcinoma-associated antigen 519) (Hepatocellular carcinoma-associated antigen 90) (Protein fls353) (Restricted expression proliferation-associated protein 100) (p100)
[DAB2IP AF9Q34 AIP1 KIAA1743] Disabled homolog 2-interacting protein (DAB2 interaction protein) (DAB2-interacting protein) (ASK-interacting protein 1) (AIP-1) (DOC-2/DAB-2 interactive protein)
[Dab2ip] Disabled homolog 2-interacting protein (DAB2-interacting protein) (ASK-interacting protein 1) (AIP-1) (DIP1/2) (DOC-2/DAB2 interactive protein)
[Dab2ip Kiaa1743] Disabled homolog 2-interacting protein (DAB2-interacting protein) (ASK-interacting protein 1) (DOC-2/DAB-2 interactive protein)
[TSPYL2 CDA1 DENTT TSPX HRIHFB2216] Testis-specific Y-encoded-like protein 2 (TSPY-like protein 2) (Cell division autoantigen 1) (Cutaneous T-cell lymphoma-associated antigen se20-4) (CTCL-associated antigen se20-4) (Differentially-expressed nucleolar TGF-beta1 target protein) (Nuclear protein of 79 kDa) (NP79)
[Tspyl2 Cinap Dentt DXBwg1396e Tspx] Testis-specific Y-encoded-like protein 2 (TSPY-like protein 2) (CASK-interacting nucleosome assembly protein) (Differentially-expressed nucleolar TGF-beta1 target protein)
[KLK8 NRPN PRSS19 TADG14 UNQ283/PRO322] Kallikrein-8 (hK8) (EC 3.4.21.118) (Neuropsin) (NP) (Ovasin) (Serine protease 19) (Serine protease TADG-14) (Tumor-associated differentially expressed gene 14 protein)
[AMIGO2 ALI1] Amphoterin-induced protein 2 (AMIGO-2) (Alivin-1) (Differentially expressed in gastric adenocarcinomas) (DEGA)
[Plpp3 Lpp3 Ppap2b] Phospholipid phosphatase 3 (EC 3.1.3.-) (EC 3.1.3.4) (Differentially expressed in rat intestine 42) (Dri42) (Lipid phosphate phosphohydrolase 3) (PAP2-beta) (Phosphatidate phosphohydrolase type 2b) (Phosphatidic acid phosphatase 2b) (PAP-2b) (PAP2b)
[Def6 Ibp Slat] Differentially expressed in FDCP 6 (DEF-6) (IRF4-binding protein) (SWAP-70-like adapter of T-cells)
[DEF6 IBP] Differentially expressed in FDCP 6 homolog (DEF-6) (IRF4-binding protein)
[NEDD9 CASL CASS2] Enhancer of filamentation 1 (hEF1) (CRK-associated substrate-related protein) (CAS-L) (CasL) (Cas scaffolding protein family member 2) (Neural precursor cell expressed developmentally down-regulated protein 9) (NEDD-9) (Renal carcinoma antigen NY-REN-12) (p105) [Cleaved into: Enhancer of filamentation 1 p55]
[MADD DENN IG20 KIAA0358] MAP kinase-activating death domain protein (Differentially expressed in normal and neoplastic cells) (Insulinoma glucagonoma clone 20) (Rab3 GDP/GTP exchange factor) (RabGEF) (Rab3 GDP/GTP exchange protein) (Rab3GEP)
[Dab1] Disabled homolog 1
[BHLHE40 BHLHB2 DEC1 SHARP2 STRA13] Class E basic helix-loop-helix protein 40 (bHLHe40) (Class B basic helix-loop-helix protein 2) (bHLHb2) (Differentially expressed in chondrocytes protein 1) (DEC1) (Enhancer-of-split and hairy-related protein 2) (SHARP-2) (Stimulated by retinoic acid gene 13 protein)
[TMPRSS3 ECHOS1 TADG12 UNQ323/PRO382] Transmembrane protease serine 3 (EC 3.4.21.-) (Serine protease TADG-12) (Tumor-associated differentially-expressed gene 12 protein)
[Ap2a2 Adtab] AP-2 complex subunit alpha-2 (100 kDa coated vesicle protein C) (Adaptor protein complex AP-2 subunit alpha-2) (Adaptor-related protein complex 2 subunit alpha-2) (Alpha-adaptin C) (Alpha2-adaptin) (Clathrin assembly protein complex 2 alpha-C large chain) (Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit)
[SMAD2 MADH2 MADR2] Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (JV18-1) (Mad-related protein 2) (hMAD-2) (SMAD family member 2) (SMAD 2) (Smad2) (hSMAD2)
[Babam2 Bre] BRISC and BRCA1-A complex member 2 (BRCA1-A complex subunit BRE) (BRCA1/BRCA2-containing complex subunit 45) (Brain and reproductive organ-expressed protein)
[AHCYL1 DCAL IRBIT XPVKONA] S-adenosylhomocysteine hydrolase-like protein 1 (DC-expressed AHCY-like molecule) (IP(3)Rs binding protein released with IP(3)) (IRBIT) (Putative adenosylhomocysteinase 2) (S-adenosyl-L-homocysteine hydrolase 2) (AdoHcyase 2)
[Trem2 Trem2a Trem2b Trem2c] Triggering receptor expressed on myeloid cells 2 (TREM-2) (Triggering receptor expressed on monocytes 2)
[NSMCE3 HCA4 MAGEG1 NDNL2] Non-structural maintenance of chromosomes element 3 homolog (Non-SMC element 3 homolog) (Hepatocellular carcinoma-associated protein 4) (MAGE-G1 antigen) (Melanoma-associated antigen G1) (Necdin-like protein 2)
[PHF20 C20orf104 GLEA2 HCA58 NZF TZP] PHD finger protein 20 (Glioma-expressed antigen 2) (Hepatocellular carcinoma-associated antigen 58) (Novel zinc finger protein) (Transcription factor TZP)
[Peg10 Edr Mar2 Mart2 Mef3l1 Rgag3] Retrotransposon-derived protein PEG10 (Embryonal carcinoma differentiation regulated protein) (Mammalian retrotransposon-derived protein 2) (Myelin expression factor 3) (MyEF-3) (Myelin expression factor 3-like protein 1) (MEF3-like protein 1) (Paternally expressed gene 10 protein) (Retrotransposon gag domain-containing protein 3) (Retrotransposon-derived gag-like polyprotein) (Ty3/Gypsy-like protein)
[Havcr2 Tim3 Timd3] Hepatitis A virus cellular receptor 2 homolog (HAVcr-2) (T-cell immunoglobulin and mucin domain-containing protein 3) (TIMD-3) (T-cell immunoglobulin mucin receptor 3) (TIM-3) (T-cell membrane protein 3) (CD antigen CD366)
[PLAAT3 HRASLS3 HREV107 PLA2G16] Phospholipase A and acyltransferase 3 (EC 2.3.1.-) (EC 3.1.1.32) (EC 3.1.1.4) (Adipose-specific phospholipase A2) (AdPLA) (Group XVI phospholipase A1/A2) (H-rev 107 protein homolog) (H-REV107) (HREV107-1) (HRAS-like suppressor 1) (HRAS-like suppressor 3) (HRSL3) (HREV107-3) (Renal carcinoma antigen NY-REN-65)
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (hMAD-3) (JV15-2) (SMAD family member 3) (SMAD 3) (Smad3) (hSMAD3)
[Inpp5d 7a33 Ship Ship1] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC 3.1.3.86) (Inositol polyphosphate-5-phosphatase D) (EC 3.1.3.56) (Inositol polyphosphate-5-phosphatase of 145 kDa) (SIP-145) (Phosphatidylinositol-4,5-bisphosphate 5-phosphatase) (EC 3.1.3.36) (SH2 domain-containing inositol 5'-phosphatase 1) (SH2 domain-containing inositol phosphatase 1) (SHIP-1) (p150Ship)
[ENOX2 COVA1] Ecto-NOX disulfide-thiol exchanger 2 (APK1 antigen) (Cytosolic ovarian carcinoma antigen 1) (Tumor-associated hydroquinone oxidase) (tNOX) [Includes: Hydroquinone [NADH] oxidase (EC 1.-.-.-); Protein disulfide-thiol oxidoreductase (EC 1.-.-.-)]
[shc-1 F54A5.3] SHC-transforming protein homolog 1 (Src homology 2 domain adapter homolog 1)

Bibliography :