GGA1

GGA1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1J2J, 1JWF, 1JWG, 1NA8, 1NAF, 1NWM, 1O3X, 1OM9, 1OXZ, 1PY1, 1UJJ, 1UJK, 1X79, 2DWX, 2DWY, 3G2S, 3G2T, 3G2U, 3G2V, 3G2W
Identifiers
Aliases	GGA1, golgi associated, gamma adaptin ear containing, ARF binding protein 1
External IDs	OMIM: 606004 MGI: 2146207 HomoloGene: 39250 GeneCards: GGA1
Gene location (Human)
Chr.	Chromosome 22 (human)[1]
End	37,633,564 bp[1]
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)[2]
End	78,894,585 bp[2]
RNA expression pattern
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	• GO:0001948 protein binding; • ADP-ribosylation factor binding; • protein heterodimerization activity; • molecular function;
Cellular component	• endosome; • Golgi apparatus; • endosome membrane; • intracellular; • membrane; • intracellular membrane-bounded organelle; • clathrin adaptor complex; • nucleoplasm; • early endosome membrane; • protein complex; • early endosome; • cytosol; • macromolecular complex; • cell;
Biological process	• protein transport; • cellular protein metabolic process; • intracellular protein transport; • toxin transport; • positive regulation of protein catabolic process; • vesicle-mediated transport; • transport; • Golgi to plasma membrane transport; • protein localization; • protein localization to cell surface; • retrograde transport, endosome to Golgi; • Golgi to plasma membrane protein transport; • protein localization to ciliary membrane;
	Sources:Amigo / QuickGO
Orthologs
	26088
	106039
	ENSG00000100083
	ENSMUSG00000033128
	Q9UJY5
	Q8R0H9
NM_001001560; NM_001001561; NM_001172687; NM_001172688; NM_013365;
	NM_001363771
	NM_145929
	NP_001001560; NP_001166158; NP_001166159; NP_037497; NP_001350700
	NP_666041
	Wikidata
View/Edit Human	View/Edit Mouse

ADP-ribosylation factor-binding protein GGA1 is a protein that in humans is encoded by the GGA1 gene.[5][6][7]

This gene encodes a member of the Golgi-localized, gamma adaptin ear-containing, ARF-binding (GGA) protein family. Members of this family are ubiquitous coat proteins that regulate the trafficking of proteins between the trans-Golgi network and the lysosome. These proteins share an amino-terminal VHS domain which mediates sorting of the mannose 6-phosphate receptors at the trans-Golgi network. They also contain a carboxy-terminal region with homology to the ear domain of gamma-adaptins. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.[8]

Interactions

GGA1 has been shown to interact with Sortilin 1,[9] BACE2,[10] RABEP1[11] and ARF3.[12][13]

References

GRCh38: Ensembl release 89: ENSG00000100083 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000033128 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Hirst J, Lui WW, Bright NA, Totty N, Seaman MN, Robinson MS (May 2000). "A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome". J Cell Biol. 149 (1): 67–80. doi:10.1083/jcb.149.1.67. PMC 2175106. PMID 10747088.
Dell'Angelica EC, Puertollano R, Mullins C, Aguilar RC, Vargas JD, Hartnell LM, Bonifacino JS (May 2000). "GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex". J Cell Biol. 149 (1): 81–94. doi:10.1083/jcb.149.1.81. PMC 2175099. PMID 10747089.
Xie L, Boyle D, Sanford D, Scherer PE, Pessin JE, Mora S (March 2006). "Intracellular trafficking and secretion of adiponectin is dependent on GGA-coated vesicles". J Biol Chem. 281 (11): 7253–9. doi:10.1074/jbc.M511313200. PMID 16407204.
"Entrez Gene: GGA1 golgi associated, gamma adaptin ear containing, ARF binding protein 1".
Jacobsen, Linda; Madsen Peder; Nielsen Morten S; Geraerts Wijnand P M; Gliemann Jørgen; Smit August B; Petersen Claus M (January 2002). "The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding". FEBS Lett. 511 (1–3): 155–8. doi:10.1016/S0014-5793(01)03299-9. ISSN 0014-5793. PMID 11821067.
He, Xiangyuan; Chang Wan-Pin; Koelsch Gerald; Tang Jordan (July 2002). "Memapsin 2 (beta-secretase) cytosolic domain binds to the VHS domains of GGA1 and GGA2: implications on the endocytosis mechanism of memapsin 2". FEBS Lett. 524 (1–3): 183–7. doi:10.1016/S0014-5793(02)03052-1. ISSN 0014-5793. PMID 12135764.
Mattera, Rafael; Arighi Cecilia N; Lodge Robert; Zerial Marino; Bonifacino Juan S (January 2003). "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex". EMBO J. 22 (1): 78–88. doi:10.1093/emboj/cdg015. ISSN 0261-4189. PMC 140067. PMID 12505986.
Boman, Annette L; Salo Paul D; Hauglund Melissa J; Strand Nicole L; Rensink Shelly J; Zhdankina Olga (September 2002). "ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization". Mol. Biol. Cell. 13 (9): 3078–95. doi:10.1091/mbc.E02-02-0078. ISSN 1059-1524. PMC 124144. PMID 12221117.
Boman, A L; Zhang C j; Zhu X; Kahn R A (April 2000). "A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi". Mol. Biol. Cell. 11 (4): 1241–55. doi:10.1091/mbc.11.4.1241. ISSN 1059-1524. PMC 14844. PMID 10749927.

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi:10.1038/990031. PMID 10591208.
Boman AL, Zhang C, Zhu X, Kahn RA (2000). "A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi". Mol. Biol. Cell. 11 (4): 1241–55. doi:10.1091/mbc.11.4.1241. PMC 14844. PMID 10749927.
Takatsu H, Yoshino K, Nakayama K (2000). "Adaptor gamma ear homology domain conserved in gamma-adaptin and GGA proteins that interact with gamma-synergin". Biochem. Biophys. Res. Commun. 271 (3): 719–25. doi:10.1006/bbrc.2000.2700. PMID 10814529.
Zhdankina O, Strand NL, Redmond JM, Boman AL (2001). "Yeast GGA proteins interact with GTP-bound Arf and facilitate transport through the Golgi". Yeast. 18 (1): 1–18. doi:10.1002/1097-0061(200101)18:1<1::AID-YEA644>3.0.CO;2-5. PMID 11124697.
Puertollano R, Randazzo PA, Presley JF, et al. (2001). "The GGAs promote ARF-dependent recruitment of clathrin to the TGN". Cell. 105 (1): 93–102. doi:10.1016/S0092-8674(01)00299-9. PMID 11301005.
Puertollano R, Aguilar RC, Gorshkova I, et al. (2001). "Sorting of mannose 6-phosphate receptors mediated by the GGAs". Science. 292 (5522): 1712–6. Bibcode:2001Sci...292.1712P. doi:10.1126/science.1060750. PMID 11387475.
Takatsu H, Katoh Y, Shiba Y, Nakayama K (2001). "Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains". J. Biol. Chem. 276 (30): 28541–5. doi:10.1074/jbc.C100218200. PMID 11390366.
Jacobsen L, Madsen P, Nielsen MS, et al. (2002). "The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding". FEBS Lett. 511 (1–3): 155–8. doi:10.1016/S0014-5793(01)03299-9. PMID 11821067.
Shiba T, Takatsu H, Nogi T, et al. (2002). "Structural basis for recognition of acidic-cluster dileucine sequence by GGA1". Nature. 415 (6874): 937–41. Bibcode:2002Natur.415..937S. doi:10.1038/415937a. PMID 11859376.
Takatsu H, Yoshino K, Toda K, Nakayama K (2002). "GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors". Biochem. J. 365 (Pt 2): 369–78. doi:10.1042/BJ20020428. PMC 1222692. PMID 11950392.
Doray B, Bruns K, Ghosh P, Kornfeld SA (2002). "Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif". Proc. Natl. Acad. Sci. U.S.A. 99 (12): 8072–7. Bibcode:2002PNAS...99.8072D. doi:10.1073/pnas.082235699. PMC 123022. PMID 12060753.
He X, Chang WP, Koelsch G, Tang J (2002). "Memapsin 2 (beta-secretase) cytosolic domain binds to the VHS domains of GGA1 and GGA2: implications on the endocytosis mechanism of memapsin 2". FEBS Lett. 524 (1–3): 183–7. doi:10.1016/S0014-5793(02)03052-1. PMID 12135764.
Boman AL, Salo PD, Hauglund MJ, et al. (2003). "ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization". Mol. Biol. Cell. 13 (9): 3078–95. doi:10.1091/mbc.E02-02-0078. PMC 124144. PMID 12221117.
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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Mattera R, Arighi CN, Lodge R, et al. (2003). "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex". EMBO J. 22 (1): 78–88. doi:10.1093/emboj/cdg015. PMC 140067. PMID 12505986.
Mills IG, Praefcke GJ, Vallis Y, et al. (2003). "EpsinR: an AP1/clathrin interacting protein involved in vesicle trafficking". J. Cell Biol. 160 (2): 213–22. doi:10.1083/jcb.200208023. PMC 2172650. PMID 12538641.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000100083 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000033128 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10747088-5] Hirst J, Lui WW, Bright NA, Totty N, Seaman MN, Robinson MS (May 2000). "A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome". J Cell Biol. 149 (1): 67–80. doi:10.1083/jcb.149.1.67. PMC 2175106. PMID 10747088.

[pmid10747089-6] Dell'Angelica EC, Puertollano R, Mullins C, Aguilar RC, Vargas JD, Hartnell LM, Bonifacino JS (May 2000). "GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex". J Cell Biol. 149 (1): 81–94. doi:10.1083/jcb.149.1.81. PMC 2175099. PMID 10747089.

[pmid16407204-7] Xie L, Boyle D, Sanford D, Scherer PE, Pessin JE, Mora S (March 2006). "Intracellular trafficking and secretion of adiponectin is dependent on GGA-coated vesicles". J Biol Chem. 281 (11): 7253–9. doi:10.1074/jbc.M511313200. PMID 16407204.

[entrez-8] "Entrez Gene: GGA1 golgi associated, gamma adaptin ear containing, ARF binding protein 1".

[pmid11821067-9] Jacobsen, Linda; Madsen Peder; Nielsen Morten S; Geraerts Wijnand P M; Gliemann Jørgen; Smit August B; Petersen Claus M (January 2002). "The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding". FEBS Lett. 511 (1–3): 155–8. doi:10.1016/S0014-5793(01)03299-9. ISSN 0014-5793. PMID 11821067.

[pmid12135764-10] He, Xiangyuan; Chang Wan-Pin; Koelsch Gerald; Tang Jordan (July 2002). "Memapsin 2 (beta-secretase) cytosolic domain binds to the VHS domains of GGA1 and GGA2: implications on the endocytosis mechanism of memapsin 2". FEBS Lett. 524 (1–3): 183–7. doi:10.1016/S0014-5793(02)03052-1. ISSN 0014-5793. PMID 12135764.

[pmid12505986-11] Mattera, Rafael; Arighi Cecilia N; Lodge Robert; Zerial Marino; Bonifacino Juan S (January 2003). "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex". EMBO J. 22 (1): 78–88. doi:10.1093/emboj/cdg015. ISSN 0261-4189. PMC 140067. PMID 12505986.

[pmid12221117-12] Boman, Annette L; Salo Paul D; Hauglund Melissa J; Strand Nicole L; Rensink Shelly J; Zhdankina Olga (September 2002). "ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization". Mol. Biol. Cell. 13 (9): 3078–95. doi:10.1091/mbc.E02-02-0078. ISSN 1059-1524. PMC 124144. PMID 12221117.

[pmid10749927-13] Boman, A L; Zhang C j; Zhu X; Kahn R A (April 2000). "A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi". Mol. Biol. Cell. 11 (4): 1241–55. doi:10.1091/mbc.11.4.1241. ISSN 1059-1524. PMC 14844. PMID 10749927.

GGA1

Interactions

References

Further reading