[1]
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NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH CRK.
TISSUE=Placenta;
PubMed=8657152 [NCBI, ExPASy, EBI, Israel, Japan]
Hasegawa H.,
Kiyokawa E.,
Tanaka S.,
Nagashima K.,
Gotoh N.,
Shibuya M.,
Kurata T.,
Matsuda M.;
"DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane.";
Mol. Cell. Biol. 16:1770-1776(1996).
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[2]
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INTERACTION WITH CRK.
DOI=10.1074/jbc.271.24.14468; PubMed=8662907 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuda M.,
Ota S.,
Tanimura R.,
Nakamura H.,
Matuoka K.,
Takenawa T.,
Nagashima K.,
Kurata T.;
"Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins.";
J. Biol. Chem. 271:14468-14472(1996).
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[3]
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GEF ACTIVITY, AND INTERACTION WITH RAC1.
PubMed=9808620 [NCBI, ExPASy, EBI, Israel, Japan]
Kiyokawa E.,
Hashimoto Y.,
Kobayashi S.,
Sugimura H.,
Kurata T.,
Matsuda M.;
"Activation of Rac1 by a Crk SH3-binding protein, DOCK180.";
Genes Dev. 12:3331-3336(1998).
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[4]
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INTERACTION WITH NCK2.
DOI=10.1016/S0014-5793(01)02195-0; PubMed=11240126 [NCBI, ExPASy, EBI, Israel, Japan]
Tu Y.,
Kucik D.F.,
Wu C.;
"Identification and kinetic analysis of the interaction between Nck-2 and DOCK180.";
FEBS Lett. 491:193-199(2001).
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[5]
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INTERACTION WITH PTDINS(3,4,5)P3.
DOI=10.1042/0264-6021:3540073; PubMed=11171081 [NCBI, ExPASy, EBI, Israel, Japan]
Kobayashi S.,
Shirai T.,
Kiyokawa E.,
Mochizuki N.,
Matsuda M.,
Fukui Y.;
"Membrane recruitment of DOCK180 by binding to PtdIns(3,4,5)P3.";
Biochem. J. 354:73-78(2001).
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[6]
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GEF ACTIVITY, INTERACTION WITH RAC1; ELMO1 AND ELMO2, SUBUNIT OF A COMPLEX CONTAINING ELMO1 AND DOCK1, AND MUTAGENESIS OF 1401-TYR-ILE-1402 AND 1487-ILE--PRO-1489.
DOI=10.1038/ncb824; PubMed=12134158 [NCBI, ExPASy, EBI, Israel, Japan]
Brugnera E.,
Haney L.,
Grimsley C.,
Lu M.,
Walk S.F.,
Tosello-Trampont A.-C.,
Macara I.G.,
Madhani H.,
Fink G.R.,
Ravichandran K.S.;
"Unconventional Rac-GEF activity is mediated through the Dock180-ELMO complex.";
Nat. Cell Biol. 4:574-582(2002).
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[7]
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NOMENCLATURE, AND GEF ACTIVITY.
DOI=10.1242/jcs.00219; PubMed=12432077 [NCBI, ExPASy, EBI, Israel, Japan]
Cote J.-F.,
Vuori K.;
"Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity.";
J. Cell Sci. 115:4901-4913(2002).
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[8]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1858, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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- FUNCTION: Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Functions as a guanine nucleotide exchange factor (GEF), which activates Rac Rho small GTPases by exchanging bound GDP for free GTP. Its GEF activity may be enhanced by ELMO1.
- SUBUNIT: Interacts with the SH3 domains of CRK and NCK2 via multiple sites. Interacts with nucleotide-free RAC1 via its DHR-2 domain. Interacts with ELMO1, ELMO2 and probably ELMO3 via its SH3 domain. Interacts with RAC1.
- INTERACTION:
Q92556:ELMO1; NbExp=2; IntAct=EBI-446740, EBI-346417;
P63000:RAC1; NbExp=3; IntAct=EBI-446740, EBI-413628;
- SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane (Probable). Note=Recruited to membranes via its interaction with phosphatidylinositol 3,4,5-triphosphate (Probable).
- TISSUE SPECIFICITY: Highly expressed in placenta, lung, kidney, pancreas and ovary. Expressed at intermediate level in thymus, testes and colon.
- DOMAIN: The DHR-2 domain is necessary and sufficient for the GEF activity.
- SIMILARITY: Belongs to the DOCK family.
- SIMILARITY: Contains 1 DHR-1 (CZH-1) domain.
- SIMILARITY: Contains 1 DHR-2 (CZH-2) domain.
- SIMILARITY: Contains 1 SH3 domain.
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