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{{Infobox_gene}}
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'''AP-1 complex subunit gamma-like 2''' is a [[protein]] that in humans is encoded by the ''AP1G2'' [[gene]].<ref name="pmid9733768">{{cite journal |vauthors=Takatsu H, Sakurai M, Shin HW, Murakami K, Nakayama K | title = Identification and characterization of novel clathrin adaptor-related proteins | journal = J Biol Chem | volume = 273 | issue = 38 | pages = 24693–700 |date=Oct 1998 | pmid = 9733768 | pmc =  | doi =10.1074/jbc.273.38.24693  }}</ref><ref name="pmid9762922">{{cite journal |vauthors=Lewin DA, Sheff D, Ooi CE, Whitney JA, Yamamoto E, Chicione LM, Webster P, Bonifacino JS, Mellman I | title = Cloning, expression, and localization of a novel gamma-adaptin-like molecule | journal = FEBS Lett | volume = 435 | issue = 2-3 | pages = 263–8 |date=Oct 1998 | pmid = 9762922 | pmc =  | doi =10.1016/S0014-5793(98)01083-7 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: AP1G2 adaptor-related protein complex 1, gamma 2 subunit| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8906| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Adaptor-related protein complex 1, gamma 2 subunit
| HGNCid = 556
| Symbol = AP1G2
| AltSymbols =; G2AD
| OMIM = 603534
| ECnumber =
| Homologene = 49141
| MGIid = 1328307
  | Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}  
| Component = {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005798 |text = Golgi-associated vesicle}} {{GNF_GO|id=GO:0005905 |text = coated pit}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0030121 |text = AP-1 adaptor complex}} {{GNF_GO|id=GO:0030133 |text = transport vesicle}}
| Process = {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0006886 |text = intracellular protein transport}} {{GNF_GO|id=GO:0006897 |text = endocytosis}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8906
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_003908
    | Hs_RefseqmRNA = NM_003917
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 11766
    | Mm_Ensembl = ENSMUSG00000040701
    | Mm_RefseqmRNA = XM_989916
    | Mm_RefseqProtein = XP_995010
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 14
    | Mm_GenLoc_start = 54052926
    | Mm_GenLoc_end = 54060199
    | Mm_Uniprot = Q2YDV3
  }}
}}
'''Adaptor-related protein complex 1, gamma 2 subunit''', also known as '''AP1G2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AP1G2 adaptor-related protein complex 1, gamma 2 subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8906| accessdate = }}</ref>


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| section_title =  
| section_title =  
| summary_text = Adaptins are important components of clathrin-coated vesicles transporting ligand-receptor complexes from the plasma membrane or from the trans-Golgi network to lysosomes. The adaptin family of proteins is compsed of four classes of molecules named alpha, beta-, beta prime- and gamma- adaptins. Adaptins, together with medium and small subunits, form a heterotetrameric complex called an adaptor, whose role is to promote the formation of clathrin-coated pits and vesicles. The protein encoded by this gene is a gamma-adaptin protein and it belongs to the adaptor complexes large subunits family. This protein along with the complex is thought to function at some trafficking step in the complex pathways between the trans-Golgi network and the cell surface. There are two alternatively spliced transcript variants of this gene encoding the same protein.<ref name="entrez">{{cite web | title = Entrez Gene: AP1G2 adaptor-related protein complex 1, gamma 2 subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8906| accessdate = }}</ref>
| summary_text = Adaptins are important components of clathrin-coated vesicles transporting ligand-receptor complexes from the plasma membrane or from the trans-Golgi network to lysosomes. The adaptin family of proteins is composed of four classes of molecules named alpha, beta-, beta prime- and gamma- adaptins. Adaptins, together with medium and small subunits, form a heterotetrameric complex called an adaptor, whose role is to promote the formation of clathrin-coated pits and vesicles. The protein encoded by this gene is a gamma-adaptin protein and it belongs to the adaptor complexes large subunits family. This protein along with the complex is thought to function at some trafficking step in the complex pathways between the trans-Golgi network and the cell surface. There are two alternatively spliced transcript variants of this gene encoding the same protein.<ref name="entrez" />
}}
}}
==Interactions==
AP1G2 has been shown to [[Protein-protein interaction|interact]] with [[NEDD4]].<ref name=pmid18772139>{{cite journal |last=Rost |first=Martina |authorlink= |author2=Döring Tatjana |author3=Prange Reinhild  |date=Nov 2008 |title=gamma2-Adaptin, a ubiquitin-interacting adaptor, is a substrate to coupled ubiquitination by the ubiquitin ligase Nedd4 and functions in the endosomal pathway |journal=J. Biol. Chem. |volume=283 |issue=46 |pages=32119–30 |publisher= |location = United States| issn = 0021-9258| pmid = 18772139 |doi = 10.1074/jbc.M802632200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|AP1G2}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Geyer M, Fackler OT, Peterlin BM |title=Structure--function relationships in HIV-1 Nef. |journal=EMBO Rep. |volume=2 |issue= 7 |pages= 580-5 |year= 2001 |pmid= 11463741 |doi= 10.1093/embo-reports/kve141 }}
*{{cite journal  |vauthors=Geyer M, Fackler OT, Peterlin BM |title=Structure--function relationships in HIV-1 Nef. |journal=EMBO Rep. |volume=2 |issue= 7 |pages= 580–5 |year= 2001 |pmid= 11463741 |doi= 10.1093/embo-reports/kve141 | pmc=1083955 }}
*{{cite journal  | author=Bénichou S, Benmerah A |title=[The HIV nef and the Kaposi-sarcoma-associated virus K3/K5 proteins: "parasites"of the endocytosis pathway] |journal=Med Sci (Paris) |volume=19 |issue= 1 |pages= 100-6 |year= 2003 |pmid= 12836198 |doi=  }}
*{{cite journal  |vauthors=Bénichou S, Benmerah A |title=[The HIV nef and the Kaposi-sarcoma-associated virus K3/K5 proteins: "parasites"of the endocytosis pathway] |journal=Med Sci (Paris) |volume=19 |issue= 1 |pages= 100–6 |year= 2003 |pmid= 12836198 |doi=  10.1051/medsci/2003191100}}
*{{cite journal  | author=Takatsu H, Sakurai M, Shin HW, ''et al.'' |title=Identification and characterization of novel clathrin adaptor-related proteins. |journal=J. Biol. Chem. |volume=273 |issue= 38 |pages= 24693-700 |year= 1998 |pmid= 9733768 |doi=  }}
*{{cite journal  |vauthors=Craig HM, Pandori MW, Guatelli JC |title=Interaction of HIV-1 Nef with the cellular dileucine-based sorting pathway is required for CD4 down-regulation and optimal viral infectivity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 19 |pages= 11229–34 |year= 1998 |pmid= 9736718 |doi=10.1073/pnas.95.19.11229  | pmc=21624 }}
*{{cite journal  | author=Craig HM, Pandori MW, Guatelli JC |title=Interaction of HIV-1 Nef with the cellular dileucine-based sorting pathway is required for CD4 down-regulation and optimal viral infectivity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 19 |pages= 11229-34 |year= 1998 |pmid= 9736718 |doi= }}
*{{cite journal  |vauthors=Bresnahan PA, Yonemoto W, Ferrell S |title=A dileucine motif in HIV-1 Nef acts as an internalization signal for CD4 downregulation and binds the AP-1 clathrin adaptor. |journal=Curr. Biol. |volume=8 |issue= 22 |pages= 1235–8 |year= 1999 |pmid= 9811606 |doi=10.1016/S0960-9822(07)00517-9 |display-authors=etal}}
*{{cite journal  | author=Lewin DA, Sheff D, Ooi CE, ''et al.'' |title=Cloning, expression, and localization of a novel gamma-adaptin-like molecule. |journal=FEBS Lett. |volume=435 |issue= 2-3 |pages= 263-8 |year= 1998 |pmid= 9762922 |doi=  }}
*{{cite journal  |vauthors=Greenberg M, DeTulleo L, Rapoport I |title=A dileucine motif in HIV-1 Nef is essential for sorting into clathrin-coated pits and for downregulation of CD4. |journal=Curr. Biol. |volume=8 |issue= 22 |pages= 1239–42 |year= 1999 |pmid= 9811611 |doi=10.1016/S0960-9822(07)00518-0 |display-authors=etal}}
*{{cite journal  | author=Bresnahan PA, Yonemoto W, Ferrell S, ''et al.'' |title=A dileucine motif in HIV-1 Nef acts as an internalization signal for CD4 downregulation and binds the AP-1 clathrin adaptor. |journal=Curr. Biol. |volume=8 |issue= 22 |pages= 1235-8 |year= 1999 |pmid= 9811606 |doi=  }}
*{{cite journal  |vauthors=Berlioz-Torrent C, Shacklett BL, Erdtmann L |title=Interactions of the cytoplasmic domains of human and simian retroviral transmembrane proteins with components of the clathrin adaptor complexes modulate intracellular and cell surface expression of envelope glycoproteins. |journal=J. Virol. |volume=73 |issue= 2 |pages= 1350–61 |year= 1999 |pmid= 9882340 |doi=  | pmc=103959  |display-authors=etal}}
*{{cite journal  | author=Greenberg M, DeTulleo L, Rapoport I, ''et al.'' |title=A dileucine motif in HIV-1 Nef is essential for sorting into clathrin-coated pits and for downregulation of CD4. |journal=Curr. Biol. |volume=8 |issue= 22 |pages= 1239-42 |year= 1999 |pmid= 9811611 |doi=  }}
*{{cite journal  |vauthors=Page LJ, Sowerby PJ, Lui WW, Robinson MS |title=Gamma-synergin: an EH domain-containing protein that interacts with gamma-adaptin. |journal=J. Cell Biol. |volume=146 |issue= 5 |pages= 993–1004 |year= 1999 |pmid= 10477754 |doi=10.1083/jcb.146.5.993  | pmc=2169493 }}
*{{cite journal  | author=Berlioz-Torrent C, Shacklett BL, Erdtmann L, ''et al.'' |title=Interactions of the cytoplasmic domains of human and simian retroviral transmembrane proteins with components of the clathrin adaptor complexes modulate intracellular and cell surface expression of envelope glycoproteins. |journal=J. Virol. |volume=73 |issue= 2 |pages= 1350-61 |year= 1999 |pmid= 9882340 |doi=  }}
*{{cite journal  |vauthors=Wyss S, Berlioz-Torrent C, Boge M |title=The highly conserved C-terminal dileucine motif in the cytosolic domain of the human immunodeficiency virus type 1 envelope glycoprotein is critical for its association with the AP-1 clathrin adaptor [correction of adapter]. |journal=J. Virol. |volume=75 |issue= 6 |pages= 2982–92 |year= 2001 |pmid= 11222723 |doi= 10.1128/JVI.75.6.2982-2992.2001 | pmc=115924 |display-authors=etal}}
*{{cite journal  | author=Page LJ, Sowerby PJ, Lui WW, Robinson MS |title=Gamma-synergin: an EH domain-containing protein that interacts with gamma-adaptin. |journal=J. Cell Biol. |volume=146 |issue= 5 |pages= 993-1004 |year= 1999 |pmid= 10477754 |doi=  }}
*{{cite journal  |vauthors=Hartmann-Stühler C, Prange R |title=Hepatitis B virus large envelope protein interacts with gamma2-adaptin, a clathrin adaptor-related protein. |journal=J. Virol. |volume=75 |issue= 11 |pages= 5343–51 |year= 2001 |pmid= 11333915 |doi= 10.1128/JVI.75.11.5343-5351.2001 | pmc=114939 }}
*{{cite journal  | author=Wyss S, Berlioz-Torrent C, Boge M, ''et al.'' |title=The highly conserved C-terminal dileucine motif in the cytosolic domain of the human immunodeficiency virus type 1 envelope glycoprotein is critical for its association with the AP-1 clathrin adaptor [correction of adapter]. |journal=J. Virol. |volume=75 |issue= 6 |pages= 2982-92 |year= 2001 |pmid= 11222723 |doi= 10.1128/JVI.75.6.2982-2992.2001 }}
*{{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=Hartmann-Stühler C, Prange R |title=Hepatitis B virus large envelope protein interacts with gamma2-adaptin, a clathrin adaptor-related protein. |journal=J. Virol. |volume=75 |issue= 11 |pages= 5343-51 |year= 2001 |pmid= 11333915 |doi= 10.1128/JVI.75.11.5343-5351.2001 }}
*{{cite journal  |vauthors=Janvier K, Craig H, Hitchin D |title=HIV-1 Nef stabilizes the association of adaptor protein complexes with membranes. |journal=J. Biol. Chem. |volume=278 |issue= 10 |pages= 8725–32 |year= 2003 |pmid= 12486136 |doi= 10.1074/jbc.M210115200 |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=Mattera R, Arighi CN, Lodge R |title=Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex. |journal=EMBO J. |volume=22 |issue= 1 |pages= 78–88 |year= 2003 |pmid= 12505986 |doi= 10.1093/emboj/cdg015 | pmc=140067 |display-authors=etal}}
*{{cite journal  | author=Janvier K, Craig H, Hitchin D, ''et al.'' |title=HIV-1 Nef stabilizes the association of adaptor protein complexes with membranes. |journal=J. Biol. Chem. |volume=278 |issue= 10 |pages= 8725-32 |year= 2003 |pmid= 12486136 |doi= 10.1074/jbc.M210115200 }}
*{{cite journal  |vauthors=Mattera R, Ritter B, Sidhu SS |title=Definition of the consensus motif recognized by gamma-adaptin ear domains. |journal=J. Biol. Chem. |volume=279 |issue= 9 |pages= 8018–28 |year= 2004 |pmid= 14665628 |doi= 10.1074/jbc.M311873200 |display-authors=etal}}
*{{cite journal  | author=Mattera R, Arighi CN, Lodge R, ''et al.'' |title=Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex. |journal=EMBO J. |volume=22 |issue= 1 |pages= 78-88 |year= 2003 |pmid= 12505986 |doi= 10.1093/emboj/cdg015 }}
*{{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=Mattera R, Ritter B, Sidhu SS, ''et al.'' |title=Definition of the consensus motif recognized by gamma-adaptin ear domains. |journal=J. Biol. Chem. |volume=279 |issue= 9 |pages= 8018-28 |year= 2004 |pmid= 14665628 |doi= 10.1074/jbc.M311873200 }}
*{{cite journal  |vauthors=Lehner B, Sanderson CM |title=A protein interaction framework for human mRNA degradation. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1315–23 |year= 2004 |pmid= 15231747 |doi= 10.1101/gr.2122004 | pmc=442147 }}
*{{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=Coleman SH, Van Damme N, Day JR |title=Leucine-specific, functional interactions between human immunodeficiency virus type 1 Nef and adaptor protein complexes. |journal=J. Virol. |volume=79 |issue= 4 |pages= 2066–78 |year= 2005 |pmid= 15681409 |doi= 10.1128/JVI.79.4.2066-2078.2005 | pmc=546596 |display-authors=etal}}
*{{cite journal  | author=Lehner B, Sanderson CM |title=A protein interaction framework for human mRNA degradation. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1315-23 |year= 2004 |pmid= 15231747 |doi= 10.1101/gr.2122004 }}
*{{cite journal  | author=Coleman SH, Van Damme N, Day JR, ''et al.'' |title=Leucine-specific, functional interactions between human immunodeficiency virus type 1 Nef and adaptor protein complexes. |journal=J. Virol. |volume=79 |issue= 4 |pages= 2066-78 |year= 2005 |pmid= 15681409 |doi= 10.1128/JVI.79.4.2066-2078.2005 }}
}}
}}
{{refend}}
{{refend}}
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Revision as of 18:04, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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Wikidata
View/Edit Human

AP-1 complex subunit gamma-like 2 is a protein that in humans is encoded by the AP1G2 gene.[1][2][3]

Adaptins are important components of clathrin-coated vesicles transporting ligand-receptor complexes from the plasma membrane or from the trans-Golgi network to lysosomes. The adaptin family of proteins is composed of four classes of molecules named alpha, beta-, beta prime- and gamma- adaptins. Adaptins, together with medium and small subunits, form a heterotetrameric complex called an adaptor, whose role is to promote the formation of clathrin-coated pits and vesicles. The protein encoded by this gene is a gamma-adaptin protein and it belongs to the adaptor complexes large subunits family. This protein along with the complex is thought to function at some trafficking step in the complex pathways between the trans-Golgi network and the cell surface. There are two alternatively spliced transcript variants of this gene encoding the same protein.[3]

Interactions

AP1G2 has been shown to interact with NEDD4.[4]

References

  1. ↑ Takatsu H, Sakurai M, Shin HW, Murakami K, Nakayama K (Oct 1998). "Identification and characterization of novel clathrin adaptor-related proteins". J Biol Chem. 273 (38): 24693–700. doi:10.1074/jbc.273.38.24693. PMID 9733768.
  2. ↑ Lewin DA, Sheff D, Ooi CE, Whitney JA, Yamamoto E, Chicione LM, Webster P, Bonifacino JS, Mellman I (Oct 1998). "Cloning, expression, and localization of a novel gamma-adaptin-like molecule". FEBS Lett. 435 (2–3): 263–8. doi:10.1016/S0014-5793(98)01083-7. PMID 9762922.
  3. ↑ 3.0 3.1 "Entrez Gene: AP1G2 adaptor-related protein complex 1, gamma 2 subunit".
  4. ↑ Rost, Martina; Döring Tatjana; Prange Reinhild (Nov 2008). "gamma2-Adaptin, a ubiquitin-interacting adaptor, is a substrate to coupled ubiquitination by the ubiquitin ligase Nedd4 and functions in the endosomal pathway". J. Biol. Chem. United States. 283 (46): 32119–30. doi:10.1074/jbc.M802632200. ISSN 0021-9258. PMID 18772139.

External links

Further reading



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