DDEF2

ASAP2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1DCQ
Identifiers
Aliases	ASAP2, AMAP2, CENTB3, DDEF2, PAG3, PAP, Pap-alpha, SHAG1, ArfGAP with SH3 domain, ankyrin repeat and PH domain 2
External IDs	MGI: 2685438 HomoloGene: 2888 GeneCards: ASAP2
Gene ontology Molecular function • enzyme activator activity • protein binding • metal ion binding • GTPase activator activity Cellular component • cytoplasm • Golgi cisterna membrane • plasma membrane • Golgi apparatus • membrane Biological process • positive regulation of GTPase activity • positive regulation of catalytic activity Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8853	211914
Ensembl	ENSG00000151693	ENSMUSG00000052632
UniProt	O43150	Q7SIG6
RefSeq (mRNA)	NM_001135191 NM_003887	NM_001004364 NM_001098168 NM_001135192
RefSeq (protein)	NP_001128663.1 NP_003878.1	NP_001004364.2 NP_001091637.1 NP_001128664.1
Location (UCSC)	Chr 2: 9.21 – 9.41 Mb	Chr 12: 21.11 – 21.27 Mb
PubMed search	[1]	[2]
Wikidata

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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.^[3][4][5]

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.^[5]

Interactions

DDEF2 has been shown to interact with PTK2B.^[6]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. 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.
4. 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.
5. "Entrez Gene: DDEF2 development and differentiation enhancing factor 2".
6. 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.