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{{ | '''Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2''' is a [[protein]] that in humans is encoded by the ''ASAP2'' [[gene]].<ref name="pmid10022920">{{cite journal | vauthors = Andreev J, Simon JP, Sabatini DD, Kam J, Plowman G, Randazzo PA, Schlessinger J | title = Identification of a New Pyk2 Target Protein with Arf-GAP Activity | journal = Mol Cell Biol | volume = 19 | issue = 3 | pages = 2338–50 |date=Mar 1999 | pmid = 10022920 | pmc = 84026 | doi = }}</ref><ref name="pmid9455477">{{cite journal | vauthors = Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O | title = Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro | journal = DNA Res | volume = 4 | issue = 5 | pages = 307–13 |date=Feb 1998 | pmid = 9455477 | pmc = | doi =10.1093/dnares/4.5.307 }}</ref><ref name="entrez"/> | ||
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| summary_text = This gene encodes a multidomain protein containing an N-terminal alpha-helical region with a coiled-coil motif, followed by a pleckstrin homology (PH) domain, an Arf-GAP domain, an ankyrin homology region, a proline-rich region, and a C-terminal Src homology 3 (SH3) domain. The protein localizes in the Golgi apparatus and at the plasma membrane, where it colocalizes with protein tyrosine kinase 2-beta (PYK2). The encoded protein forms a stable complex with PYK2 in vivo. This interaction appears to be mediated by binding of its SH3 domain to the C-terminal proline-rich domain of PYK2. The encoded protein is tyrosine phosphorylated by activated PYK2. In vitro it shows strong GTPase-activating protein (GAP) activity towards the small GTPases ADP-ribosylation factor (ARF) 1 and ARF5 and weak activity towards ARF6. The encoded protein is believed to function as an ARF GAP that controls ARF-mediated vesicle budding when recruited to Golgi membranes. In addition, it functions as a substrate and downstream target for PYK2 and SRC, a pathway that may be involved in the regulation of vesicular transport.<ref name="entrez">{{cite web | title = Entrez Gene: DDEF2 development and differentiation enhancing factor 2| url = | | summary_text = This gene encodes a multidomain protein containing an N-terminal alpha-helical region with a coiled-coil motif, followed by a pleckstrin homology (PH) domain, an Arf-GAP domain, an ankyrin homology region, a proline-rich region, and a C-terminal Src homology 3 (SH3) domain. The protein localizes in the Golgi apparatus and at the plasma membrane, where it colocalizes with protein tyrosine kinase 2-beta (PYK2). The encoded protein forms a stable complex with PYK2 in vivo. This interaction appears to be mediated by binding of its SH3 domain to the C-terminal proline-rich domain of PYK2. The encoded protein is tyrosine phosphorylated by activated PYK2. In vitro it shows strong GTPase-activating protein (GAP) activity towards the small GTPases ADP-ribosylation factor (ARF) 1 and ARF5 and weak activity towards ARF6. The encoded protein is believed to function as an ARF GAP that controls ARF-mediated vesicle budding when recruited to Golgi membranes. In addition, it functions as a substrate and downstream target for PYK2 and SRC, a pathway that may be involved in the regulation of vesicular transport.<ref name="entrez">{{cite web | title = Entrez Gene: DDEF2 development and differentiation enhancing factor 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8853| accessdate = }}</ref> | ||
}} | }} | ||
==Interactions== | |||
DDEF2 has been shown to [[Protein-protein interaction|interact]] with [[PTK2B]].<ref name=autogenerated1>{{cite journal |last=Andreev |first=J |author2=Simon J P |author3=Sabatini D D |author4=Kam J |author5=Plowman G |author6=Randazzo P A |author7=Schlessinger J |date=Mar 1999 |title=Identification of a New Pyk2 Target Protein with Arf-GAP Activity |journal=Mol. Cell. Biol. |volume=19 |issue=3 |pages=2338–50 |publisher= |location = UNITED STATES| issn = 0270-7306| pmid = 10022920 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=84026 }}</ref> | |||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | | *{{cite journal | vauthors=Brown MT, Andrade J, Radhakrishna H |title=ASAP1, a Phospholipid-Dependent Arf GTPase-Activating Protein That Associates with and Is Phosphorylated by Src |journal=Mol. Cell. Biol. |volume=18 |issue= 12 |pages= 7038–51 |year= 1998 |pmid= 9819391 |doi= | pmc=109286 |display-authors=etal}} | ||
*{{cite journal | vauthors=Kondo A, Hashimoto S, Yano H |title=A New Paxillin-binding Protein, PAG3/Papα/KIAA0400, Bearing an ADP-Ribosylation Factor GTPase-activating Protein Activity, Is Involved in Paxillin Recruitment to Focal Adhesions and Cell Migration |journal=Mol. Biol. Cell |volume=11 |issue= 4 |pages= 1315–27 |year= 2000 |pmid= 10749932 |doi= 10.1091/mbc.11.4.1315| pmc=14849 |display-authors=etal}} | |||
*{{cite journal | vauthors=Uchida H, Kondo A, Yoshimura Y |title=Pag3/Papα/Kiaa0400, a Gtpase-Activating Protein for Adp-Ribosylation Factor (Arf), Regulates Arf6 in Fcγ Receptor–Mediated Phagocytosis of Macrophages |journal=J. Exp. Med. |volume=193 |issue= 8 |pages= 955–66 |year= 2001 |pmid= 11304556 |doi=10.1084/jem.193.8.955 | pmc=2193405 |display-authors=etal}} | |||
*{{cite journal | | *{{cite journal | vauthors=Kim H, Lee Y |title=Interaction of poly(A) polymerase with the 25-kDa subunit of cleavage factor I |journal=Biochem. Biophys. Res. Commun. |volume=289 |issue= 2 |pages= 513–8 |year= 2002 |pmid= 11716503 |doi= 10.1006/bbrc.2001.5992 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Oshiro T, Koyama S, Sugiyama S |title=Interaction of POB1, a downstream molecule of small G protein Ral, with PAG2, a paxillin-binding protein, is involved in cell migration |journal=J. Biol. Chem. |volume=277 |issue= 41 |pages= 38618–26 |year= 2002 |pmid= 12149250 |doi= 10.1074/jbc.M203453200 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Hashimoto S, Hashimoto A, Yamada A |title=A novel mode of action of an ArfGAP, AMAP2/PAG3/Papa lpha, in Arf6 function |journal=J. Biol. Chem. |volume=279 |issue= 36 |pages= 37677–84 |year= 2004 |pmid= 15231847 |doi= 10.1074/jbc.M404196200 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Kojima C, Hashimoto A, Yabuta I |title=Regulation of Bin1 SH3 domain binding by phosphoinositides |journal=EMBO J. |volume=23 |issue= 22 |pages= 4413–22 |year= 2005 |pmid= 15483625 |doi= 10.1038/sj.emboj.7600442 | pmc=526460 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Onodera Y, Hashimoto S, Hashimoto A |title=Expression of AMAP1, an ArfGAP, provides novel targets to inhibit breast cancer invasive activities |journal=EMBO J. |volume=24 |issue= 5 |pages= 963–73 |year= 2005 |pmid= 15719014 |doi= 10.1038/sj.emboj.7600588 | pmc=554134 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Olsen JV, Blagoev B, Gnad F |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Ewing RM, Chu P, Elisma F |title=Large-scale mapping of human protein–protein interactions by mass spectrometry |journal=Mol. Syst. Biol. |volume=3 |issue= 1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 | pmc=1847948 |display-authors=etal}} | ||
*{{cite journal | | |||
*{{cite journal | | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=8853}} | |||
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Revision as of 18:18, 30 August 2017
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Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 is a protein that in humans is encoded by the ASAP2 gene.[1][2][3]
This gene encodes a multidomain protein containing an N-terminal alpha-helical region with a coiled-coil motif, followed by a pleckstrin homology (PH) domain, an Arf-GAP domain, an ankyrin homology region, a proline-rich region, and a C-terminal Src homology 3 (SH3) domain. The protein localizes in the Golgi apparatus and at the plasma membrane, where it colocalizes with protein tyrosine kinase 2-beta (PYK2). The encoded protein forms a stable complex with PYK2 in vivo. This interaction appears to be mediated by binding of its SH3 domain to the C-terminal proline-rich domain of PYK2. The encoded protein is tyrosine phosphorylated by activated PYK2. In vitro it shows strong GTPase-activating protein (GAP) activity towards the small GTPases ADP-ribosylation factor (ARF) 1 and ARF5 and weak activity towards ARF6. The encoded protein is believed to function as an ARF GAP that controls ARF-mediated vesicle budding when recruited to Golgi membranes. In addition, it functions as a substrate and downstream target for PYK2 and SRC, a pathway that may be involved in the regulation of vesicular transport.[3]
Interactions
DDEF2 has been shown to interact with PTK2B.[4]
References
- ↑ Andreev J, Simon JP, Sabatini DD, Kam J, Plowman G, Randazzo PA, Schlessinger J (Mar 1999). "Identification of a New Pyk2 Target Protein with Arf-GAP Activity". Mol Cell Biol. 19 (3): 2338–50. PMC 84026. PMID 10022920.
- ↑ Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Feb 1998). "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 4 (5): 307–13. doi:10.1093/dnares/4.5.307. PMID 9455477.
- ↑ 3.0 3.1 "Entrez Gene: DDEF2 development and differentiation enhancing factor 2".
- ↑ Andreev, J; Simon J P; Sabatini D D; Kam J; Plowman G; Randazzo P A; Schlessinger J (Mar 1999). "Identification of a New Pyk2 Target Protein with Arf-GAP Activity". Mol. Cell. Biol. UNITED STATES. 19 (3): 2338–50. ISSN 0270-7306. PMC 84026. PMID 10022920.
Further reading
- Brown MT, Andrade J, Radhakrishna H, et al. (1998). "ASAP1, a Phospholipid-Dependent Arf GTPase-Activating Protein That Associates with and Is Phosphorylated by Src". Mol. Cell. Biol. 18 (12): 7038–51. PMC 109286. PMID 9819391.
- Kondo A, Hashimoto S, Yano H, et al. (2000). "A New Paxillin-binding Protein, PAG3/Papα/KIAA0400, Bearing an ADP-Ribosylation Factor GTPase-activating Protein Activity, Is Involved in Paxillin Recruitment to Focal Adhesions and Cell Migration". Mol. Biol. Cell. 11 (4): 1315–27. doi:10.1091/mbc.11.4.1315. PMC 14849. PMID 10749932.
- Uchida H, Kondo A, Yoshimura Y, et al. (2001). "Pag3/Papα/Kiaa0400, a Gtpase-Activating Protein for Adp-Ribosylation Factor (Arf), Regulates Arf6 in Fcγ Receptor–Mediated Phagocytosis of Macrophages". J. Exp. Med. 193 (8): 955–66. doi:10.1084/jem.193.8.955. PMC 2193405. PMID 11304556.
- Kim H, Lee Y (2002). "Interaction of poly(A) polymerase with the 25-kDa subunit of cleavage factor I". Biochem. Biophys. Res. Commun. 289 (2): 513–8. doi:10.1006/bbrc.2001.5992. PMID 11716503.
- Oshiro T, Koyama S, Sugiyama S, et al. (2002). "Interaction of POB1, a downstream molecule of small G protein Ral, with PAG2, a paxillin-binding protein, is involved in cell migration". J. Biol. Chem. 277 (41): 38618–26. doi:10.1074/jbc.M203453200. PMID 12149250.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Hashimoto S, Hashimoto A, Yamada A, et al. (2004). "A novel mode of action of an ArfGAP, AMAP2/PAG3/Papa lpha, in Arf6 function". J. Biol. Chem. 279 (36): 37677–84. doi:10.1074/jbc.M404196200. PMID 15231847.
- Kojima C, Hashimoto A, Yabuta I, et al. (2005). "Regulation of Bin1 SH3 domain binding by phosphoinositides". EMBO J. 23 (22): 4413–22. doi:10.1038/sj.emboj.7600442. PMC 526460. PMID 15483625.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Onodera Y, Hashimoto S, Hashimoto A, et al. (2005). "Expression of AMAP1, an ArfGAP, provides novel targets to inhibit breast cancer invasive activities". EMBO J. 24 (5): 963–73. doi:10.1038/sj.emboj.7600588. PMC 554134. PMID 15719014.
- Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
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