DDEF2: Difference between revisions

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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.

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.

This article on a gene on human chromosome 2 is a stub. You can help Wikipedia by expanding it.

[pmid10022920-1] 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.

[pmid9455477-2] 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.

[entrez-3] 3.0 ^3.1 "Entrez Gene: DDEF2 development and differentiation enhancing factor 2".

[autogenerated1-4] 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.

[1]

[2]

[3]

[4]

@@ Line 1: / Line 1: @@
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+{{Infobox_gene}}
-{{PBB_Controls
+'''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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-{{GNF_Protein_box
- | image = PBB_Protein_DDEF2_image.jpg
- | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dcq.
- | PDB = {{PDB2|1dcq}}
- | Name = Development and differentiation enhancing factor 2
- | HGNCid = 2721
- | Symbol = DDEF2
- | AltSymbols =; PAP; AMAP2; FLJ42910; KIAA0400; PAG3; Pap-alpha; SHAG1
- | OMIM = 603817
- | ECnumber =
- | Homologene = 2888
- | MGIid = 2685438
- | GeneAtlas_image1 = PBB_GE_DDEF2_206414_s_at_tn.png
- | Function = {{GNF_GO|id=GO:0005096 |text = GTPase activator activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
- | Component =
- | Process = {{GNF_GO|id=GO:0043087 |text = regulation of GTPase activity}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 8853
-    | Hs_Ensembl = ENSG00000151693
-    | Hs_RefseqProtein = NP_003878
-    | Hs_RefseqmRNA = NM_003887
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 2
-    | Hs_GenLoc_start = 9264345
-    | Hs_GenLoc_end = 9463257
-    | Hs_Uniprot = O43150
-    | Mm_EntrezGene = 211914
-    | Mm_Ensembl = ENSMUSG00000052632
-    | Mm_RefseqmRNA = XM_001005781
-    | Mm_RefseqProtein = XP_001005781
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 12
-    | Mm_GenLoc_start = 21358246
-    | Mm_GenLoc_end = 21516663
-    | Mm_Uniprot = Q3UH05
-  }}
-}}
-'''Development and differentiation enhancing factor 2''', also known as '''DDEF2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DDEF2 development and differentiation enhancing factor 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8853| accessdate = }}</ref>
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
 {{PBB_Summary
 | section_title =
-| 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 = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8853| accessdate = }}</ref>
+| 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==
-{{reflist|2}}
+{{reflist}}
 ==Further reading==
 {{refbegin | 2}}
 {{PBB_Further_reading
 | citations =
-*{{cite journal  | author=Ishikawa K, Nagase T, Nakajima D, ''et al.'' |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 |year= 1998 |pmid= 9455477 |doi=  }}
+*{{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  | author=Brown MT, Andrade J, Radhakrishna H, ''et al.'' |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=  }}
+*{{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  | author=Andreev J, Simon JP, Sabatini DD, ''et al.'' |title=Identification of a new Pyk2 target protein with Arf-GAP activity. |journal=Mol. Cell. Biol. |volume=19 |issue= 3 |pages= 2338-50 |year= 1999 |pmid= 10022920 |doi=  }}
+*{{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  | author=Kondo A, Hashimoto S, Yano H, ''et al.'' |title=A new paxillin-binding protein, PAG3/Papalpha/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=  }}
+*{{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  | author=Uchida H, Kondo A, Yoshimura Y, ''et al.'' |title=PAG3/Papalpha/KIAA0400, a GTPase-activating protein for ADP-ribosylation factor (ARF), regulates ARF6 in Fcgamma receptor-mediated phagocytosis of macrophages. |journal=J. Exp. Med. |volume=193 |issue= 8 |pages= 955-66 |year= 2001 |pmid= 11304556 |doi=  }}
+*{{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  | author=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  | 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  | author=Oshiro T, Koyama S, Sugiyama S, ''et al.'' |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 }}
+*{{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  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
+*{{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  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |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 }}
+*{{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  | author=Hashimoto S, Hashimoto A, Yamada A, ''et al.'' |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 }}
+*{{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  | author=Kojima C, Hashimoto A, Yabuta I, ''et al.'' |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 }}
+*{{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  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |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 }}
+*{{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  | author=Onodera Y, Hashimoto S, Hashimoto A, ''et al.'' |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 }}
+*{{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  | author=Olsen JV, Blagoev B, Gnad F, ''et al.'' |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 }}
-*{{cite journal  | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
 }}
 {{refend}}
+{{PDB Gallery|geneid=8853}}
+<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{PBB_Controls
+| update_page = yes
+| require_manual_inspection = no
+| update_protein_box = yes
+| update_summary = yes
+| update_citations = yes
+}}
-{{protein-stub}}
+{{gene-2-stub}}
-{{WikiDoc Sources}}

DDEF2: Difference between revisions

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