GGA2_HUMAN
ID GGA2_HUMAN Reviewed; 613 AA.
AC Q9UJY4; D3DWF0; O14564; Q9NYN2; Q9UPS2;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=ADP-ribosylation factor-binding protein GGA2;
DE AltName: Full=Gamma-adaptin-related protein 2;
DE AltName: Full=Golgi-localized, gamma ear-containing, ARF-binding protein 2;
DE AltName: Full=VHS domain and ear domain of gamma-adaptin;
DE Short=Vear;
GN Name=GGA2; Synonyms=KIAA1080;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-424, AND SUBCELLULAR LOCATION.
RX PubMed=10749927; DOI=10.1091/mbc.11.4.1241;
RA Boman A.L., Zhang C.-J., Zhu X., Kahn R.A.;
RT "A family of ADP-ribosylation factor effectors that can alter transport
RT through the trans-Golgi.";
RL Mol. Biol. Cell 11:1241-1255(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-424, FUNCTION, AND DOMAIN.
RX PubMed=10747088; DOI=10.1083/jcb.149.1.67;
RA Hirst J., Lui W.W.Y., Bright N.A., Totty N., Seaman M.N.J., Robinson M.S.;
RT "A family of proteins with gamma-adaptin and VHS domains that facilitate
RT trafficking between the trans-Golgi network and the vacuole/lysosome.";
RL J. Cell Biol. 149:67-80(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10702286; DOI=10.1074/jbc.275.10.7176;
RA Poussu A., Lohi O., Lehto V.-P.;
RT "Vear, a novel Golgi-associated protein with VHS and gamma-adaptin 'ear'
RT domains.";
RL J. Biol. Chem. 275:7176-7183(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-424.
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-455, VARIANT PRO-424, AND INTERACTION WITH
RP SORT1.
RC TISSUE=Mammary gland;
RX PubMed=11331584; DOI=10.1093/emboj/20.9.2180;
RA Nielsen M.S., Madsen P., Christensen E.I., Nykjaer A., Gliemann J.,
RA Kasper D., Pohlmann R., Petersen C.M.;
RT "The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds
RT the VHS domain of the GGA2 sorting protein.";
RL EMBO J. 20:2180-2190(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-613.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [9]
RP INTERACTION WITH SYNRG.
RX PubMed=10814529; DOI=10.1006/bbrc.2000.2700;
RA Takatsu H., Yoshino K., Nakayama K.;
RT "Adaptor gamma ear homology domain conserved in gamma-adaptin and GGA
RT proteins that interact with gamma-synergin.";
RL Biochem. Biophys. Res. Commun. 271:719-725(2000).
RN [10]
RP INTERACTION WITH CLATHRIN, MUTAGENESIS OF 349-LEU--GLU-353, AND DOMAIN.
RX PubMed=11301005; DOI=10.1016/s0092-8674(01)00299-9;
RA Puertollano R., Randazzo P.A., Presley J.F., Hartnell L.M.,
RA Bonifacino J.S.;
RT "The GGAs promote ARF-dependent recruitment of clathrin to the TGN.";
RL Cell 105:93-102(2001).
RN [11]
RP INTERACTION WITH SORT1; LRP3 AND IGF2R.
RX PubMed=11390366; DOI=10.1074/jbc.c100218200;
RA Takatsu H., Katoh Y., Shiba Y., Nakayama K.;
RT "Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation
RT factor-binding (GGA) proteins interact with acidic dileucine sequences
RT within the cytoplasmic domains of sorting receptors through their
RT Vps27p/Hrs/STAM (VHS) domains.";
RL J. Biol. Chem. 276:28541-28545(2001).
RN [12]
RP INTERACTION WITH IGF2R.
RX PubMed=11387475; DOI=10.1126/science.1060750;
RA Puertollano R., Aguilar R.C., Gorshkova I., Crouch R.J., Bonifacino J.S.;
RT "Sorting of mannose 6-phosphate receptors mediated by the GGAs.";
RL Science 292:1712-1716(2001).
RN [13]
RP INTERACTION WITH ARF1; ARF5 AND ARF6, AND SUBCELLULAR LOCATION.
RX PubMed=11950392; DOI=10.1042/bj20020428;
RA Takatsu H., Yoshino K., Toda K., Nakayama K.;
RT "GGA proteins associate with Golgi membranes through interaction between
RT their GGAH domains and ADP-ribosylation factors.";
RL Biochem. J. 365:369-378(2002).
RN [14]
RP INTERACTION WITH SORL1.
RX PubMed=11821067; DOI=10.1016/s0014-5793(01)03299-9;
RA Jacobsen L., Madsen P., Nielsen M.S., Geraerts W.P.M., Gliemann J.,
RA Smit A.B., Petersen C.M.;
RT "The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines
RT minimum requirements for GGA binding.";
RL FEBS Lett. 511:155-158(2002).
RN [15]
RP INTERACTION WITH M6PR AND IGF2R.
RX PubMed=11886874; DOI=10.1074/jbc.m201879200;
RA Doray B., Bruns K., Ghosh P., Kornfeld S.;
RT "Interaction of the cation-dependent mannose 6-phosphate receptor with GGA
RT proteins.";
RL J. Biol. Chem. 277:18477-18482(2002).
RN [16]
RP INTERACTION WITH EPN4.
RX PubMed=12429846; DOI=10.1091/mbc.e02-03-0171;
RA Kalthoff C., Groos S., Kohl R., Mahrhold S., Ungewickell E.J.;
RT "Clint: a novel clathrin-binding ENTH-domain protein at the Golgi.";
RL Mol. Biol. Cell 13:4060-4073(2002).
RN [17]
RP INTERACTION WITH BACE1.
RX PubMed=14567678; DOI=10.1021/bi035199h;
RA He X., Zhu G., Koelsch G., Rodgers K.K., Zhang X.C., Tang J.;
RT "Biochemical and structural characterization of the interaction of memapsin
RT 2 (beta-secretase) cytosolic domain with the VHS domain of GGA proteins.";
RL Biochemistry 42:12174-12180(2003).
RN [18]
RP INTERACTION WITH RABEP1 AND RABGEF1.
RX PubMed=12505986; DOI=10.1093/emboj/cdg015;
RA Mattera R., Arighi C.N., Lodge R., Zerial M., Bonifacino J.S.;
RT "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex.";
RL EMBO J. 22:78-88(2003).
RN [19]
RP INTERACTION WITH CCDC91; P200 AND SYNRG.
RX PubMed=12808037; DOI=10.1091/mbc.e02-11-0735;
RA Lui W.W.Y., Collins B.M., Hirst J., Motley A., Millar C., Schu P.,
RA Owen D.J., Robinson M.S.;
RT "Binding partners for the COOH-terminal appendage domains of the GGAs and
RT gamma-adaptin.";
RL Mol. Biol. Cell 14:2385-2398(2003).
RN [20]
RP INTERACTION WITH GGA1 AND GGA3.
RX PubMed=14638859; DOI=10.1083/jcb.200308038;
RA Ghosh P., Griffith J., Geuze H.J., Kornfeld S.;
RT "Mammalian GGAs act together to sort mannose 6-phosphate receptors.";
RL J. Cell Biol. 163:755-766(2003).
RN [21]
RP INTERACTION WITH NECAP2.
RX PubMed=14665628; DOI=10.1074/jbc.m311873200;
RA Mattera R., Ritter B., Sidhu S.S., McPherson P.S., Bonifacino J.S.;
RT "Definition of the consensus motif recognized by gamma-adaptin ear
RT domains.";
RL J. Biol. Chem. 279:8018-8028(2004).
RN [22]
RP SUBCELLULAR LOCATION.
RX PubMed=15039775; DOI=10.1038/ncb1106;
RA Puertollano R., Bonifacino J.S.;
RT "Interactions of GGA3 with the ubiquitin sorting machinery.";
RL Nat. Cell Biol. 6:244-251(2004).
RN [23]
RP FUNCTION.
RX PubMed=15615712; DOI=10.1074/jbc.m411296200;
RA He X., Li F., Chang W.P., Tang J.;
RT "GGA proteins mediate the recycling pathway of memapsin 2 (BACE).";
RL J. Biol. Chem. 280:11696-11703(2005).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [28]
RP FUNCTION, AND INTERACTION WITH ADRA2B.
RX PubMed=27901063; DOI=10.1038/srep37921;
RA Zhang M., Huang W., Gao J., Terry A.V., Wu G.;
RT "Regulation of alpha2B-Adrenergic Receptor Cell Surface Transport by GGA1
RT and GGA2.";
RL Sci. Rep. 6:37921-37921(2016).
RN [29]
RP INTERACTION WITH PI4KB, AND SUBCELLULAR LOCATION.
RX PubMed=28289207; DOI=10.1073/pnas.1615163114;
RA Daboussi L., Costaguta G., Ghukasyan R., Payne G.S.;
RT "Conserved role for Gga proteins in phosphatidylinositol 4-kinase
RT localization to the trans-Golgi network.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:3433-3438(2017).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-167.
RX PubMed=12606052; DOI=10.1016/s0014-5793(03)00095-4;
RA Zhu G., He X., Zhai P., Terzyan S., Tang J., Zhang X.C.;
RT "Crystal structure of GGA2 VHS domain and its implication in plasticity in
RT the ligand binding pocket.";
RL FEBS Lett. 537:171-176(2003).
CC -!- FUNCTION: Plays a role in protein sorting and trafficking between the
CC trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent
CC recruitment of clathrin to the TGN and binds ubiquitinated proteins and
CC membrane cargo molecules with a cytosolic acidic cluster-dileucine
CC (DXXLL) motif (PubMed:10747088). Mediates export of the GPCR receptor
CC ADRA2B to the cell surface (PubMed:27901063). Regulates retrograde
CC transport of phosphorylated form of BACE1 from endosomes to the trans-
CC Golgi network (PubMed:15615712). {ECO:0000269|PubMed:10747088,
CC ECO:0000269|PubMed:15615712, ECO:0000269|PubMed:27901063}.
CC -!- SUBUNIT: Monomer (Probable). Interacts with NECAP1, TSG101, UBC and
CC AFTPH/aftiphilin. Interacts with CNST (By similarity). Interacts with
CC GGA1 and GGA3 (PubMed:14638859). Binds to clathrin and activated ARFs,
CC such as ARF1, ARF5 and ARF6 (PubMed:11301005, PubMed:11950392). Binds
CC RABEP1 and RABGEF1 (PubMed:12505986). Interacts with the type-I
CC membrane proteins LRP3, M6PR/CD-MPR, IGF2R/CI-MPR and BACE1
CC (PubMed:11390366, PubMed:11387475, PubMed:11886874, PubMed:14567678).
CC Interacts (via N-terminal VHS domain) with SORL1/sorLA and SORT1 (via
CC C-terminal cytosolic domain) (PubMed:11331584, PubMed:11390366,
CC PubMed:11821067). Binds the accessory proteins CCDC91, P200, SYNRG,
CC EPN4 and NECAP2 (PubMed:10814529, PubMed:12429846, PubMed:12808037,
CC PubMed:14665628). Interacts with ADRA2B (PubMed:27901063). Interacts
CC (via VHS domain) with PIK4B; the interaction is important for PIK4B
CC location at the Golgi apparatus membrane (PubMed:28289207).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q6P5E6,
CC ECO:0000269|PubMed:10814529, ECO:0000269|PubMed:11301005,
CC ECO:0000269|PubMed:11331584, ECO:0000269|PubMed:11387475,
CC ECO:0000269|PubMed:11390366, ECO:0000269|PubMed:11821067,
CC ECO:0000269|PubMed:11886874, ECO:0000269|PubMed:11950392,
CC ECO:0000269|PubMed:12429846, ECO:0000269|PubMed:12505986,
CC ECO:0000269|PubMed:12808037, ECO:0000269|PubMed:14567678,
CC ECO:0000269|PubMed:14638859, ECO:0000269|PubMed:14665628,
CC ECO:0000269|PubMed:27901063, ECO:0000269|PubMed:28289207, ECO:0000305}.
CC -!- INTERACTION:
CC Q9UJY4; P56817: BACE1; NbExp=2; IntAct=EBI-447646, EBI-2433139;
CC Q9UJY4; P35219: CA8; NbExp=6; IntAct=EBI-447646, EBI-718700;
CC Q9UJY4; Q9UJY5: GGA1; NbExp=7; IntAct=EBI-447646, EBI-447141;
CC Q9UJY4; Q9NZ52: GGA3; NbExp=3; IntAct=EBI-447646, EBI-447404;
CC Q9UJY4; Q9Y316: MEMO1; NbExp=3; IntAct=EBI-447646, EBI-1104564;
CC Q9UJY4; Q15276: RABEP1; NbExp=7; IntAct=EBI-447646, EBI-447043;
CC Q9UJY4; Q8WWV3: RTN4IP1; NbExp=3; IntAct=EBI-447646, EBI-743502;
CC Q9UJY4; Q92673: SORL1; NbExp=5; IntAct=EBI-447646, EBI-1171329;
CC Q9UJY4; Q9NZD8: SPG21; NbExp=4; IntAct=EBI-447646, EBI-742688;
CC Q9UJY4; P19328: Adra2b; Xeno; NbExp=3; IntAct=EBI-447646, EBI-21453893;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:10749927, ECO:0000269|PubMed:15039775,
CC ECO:0000269|PubMed:28289207}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10749927, ECO:0000269|PubMed:15039775}. Endosome
CC membrane {ECO:0000269|PubMed:15039775}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15039775}. Early endosome membrane
CC {ECO:0000269|PubMed:11950392}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DOMAIN: The VHS domain functions as a recognition module for sorting
CC signals composed of an acidic cluster followed by two leucines (DXXLL
CC motif). {ECO:0000269|PubMed:10747088}.
CC -!- DOMAIN: The GAT domain is responsible for interaction with ARF-GTP, UBC
CC and RABEP1. Required for recruitment to the TGN it prevents ARF-GTP
CC hydrolysis.
CC -!- DOMAIN: The unstructured hinge region contains clathrin-binding but no
CC autoinhibitory (DXXLL) motifs. {ECO:0000269|PubMed:11301005}.
CC -!- DOMAIN: The GAE domain binds accessory proteins regulating GGAs
CC function.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GGA protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK38634.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF190863; AAF05708.1; -; mRNA.
DR EMBL; AF233522; AAF35394.1; -; mRNA.
DR EMBL; AF165531; AAF42806.1; -; mRNA.
DR EMBL; AC002400; AAC05813.1; -; Genomic_DNA.
DR EMBL; CH471145; EAW55827.1; -; Genomic_DNA.
DR EMBL; CH471145; EAW55828.1; -; Genomic_DNA.
DR EMBL; BC000284; AAH00284.1; -; mRNA.
DR EMBL; AF323754; AAK38634.1; ALT_FRAME; mRNA.
DR EMBL; AB029003; BAA83032.1; -; mRNA.
DR CCDS; CCDS10611.1; -.
DR PIR; T00744; T00744.
DR RefSeq; NP_055859.1; NM_015044.4.
DR PDB; 1MHQ; X-ray; 2.20 A; A/B=25-172.
DR PDBsum; 1MHQ; -.
DR AlphaFoldDB; Q9UJY4; -.
DR SMR; Q9UJY4; -.
DR BioGRID; 116697; 79.
DR DIP; DIP-31601N; -.
DR ELM; Q9UJY4; -.
DR IntAct; Q9UJY4; 33.
DR MINT; Q9UJY4; -.
DR STRING; 9606.ENSP00000311962; -.
DR GlyGen; Q9UJY4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UJY4; -.
DR PhosphoSitePlus; Q9UJY4; -.
DR BioMuta; GGA2; -.
DR DMDM; 143811397; -.
DR EPD; Q9UJY4; -.
DR jPOST; Q9UJY4; -.
DR MassIVE; Q9UJY4; -.
DR MaxQB; Q9UJY4; -.
DR PaxDb; Q9UJY4; -.
DR PeptideAtlas; Q9UJY4; -.
DR PRIDE; Q9UJY4; -.
DR ProteomicsDB; 84691; -.
DR TopDownProteomics; Q9UJY4; -.
DR Antibodypedia; 12586; 218 antibodies from 31 providers.
DR DNASU; 23062; -.
DR Ensembl; ENST00000309859.8; ENSP00000311962.4; ENSG00000103365.15.
DR GeneID; 23062; -.
DR KEGG; hsa:23062; -.
DR MANE-Select; ENST00000309859.8; ENSP00000311962.4; NM_015044.4; NP_055859.1.
DR UCSC; uc002dlq.3; human.
DR CTD; 23062; -.
DR DisGeNET; 23062; -.
DR GeneCards; GGA2; -.
DR HGNC; HGNC:16064; GGA2.
DR HPA; ENSG00000103365; Low tissue specificity.
DR MIM; 606005; gene.
DR neXtProt; NX_Q9UJY4; -.
DR OpenTargets; ENSG00000103365; -.
DR PharmGKB; PA28658; -.
DR VEuPathDB; HostDB:ENSG00000103365; -.
DR eggNOG; KOG1086; Eukaryota.
DR GeneTree; ENSGT00940000159613; -.
DR HOGENOM; CLU_015010_0_0_1; -.
DR InParanoid; Q9UJY4; -.
DR OMA; NCCKEKK; -.
DR OrthoDB; 594067at2759; -.
DR PhylomeDB; Q9UJY4; -.
DR TreeFam; TF318574; -.
DR PathwayCommons; Q9UJY4; -.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR SignaLink; Q9UJY4; -.
DR BioGRID-ORCS; 23062; 6 hits in 1068 CRISPR screens.
DR ChiTaRS; GGA2; human.
DR EvolutionaryTrace; Q9UJY4; -.
DR GeneWiki; GGA2; -.
DR GenomeRNAi; 23062; -.
DR Pharos; Q9UJY4; Tbio.
DR PRO; PR:Q9UJY4; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9UJY4; protein.
DR Bgee; ENSG00000103365; Expressed in adrenal tissue and 195 other tissues.
DR ExpressionAtlas; Q9UJY4; baseline and differential.
DR Genevisible; Q9UJY4; HS.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IDA:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR GO; GO:0034394; P:protein localization to cell surface; IDA:UniProtKB.
DR Gene3D; 1.20.58.160; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR008153; GAE_dom.
DR InterPro; IPR004152; GAT_dom.
DR InterPro; IPR038425; GAT_sf.
DR InterPro; IPR041198; GGA_N-GAT.
DR InterPro; IPR002014; VHS_dom.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR Pfam; PF03127; GAT; 1.
DR Pfam; PF18308; GGA_N-GAT; 1.
DR Pfam; PF00790; VHS; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR PROSITE; PS50180; GAE; 1.
DR PROSITE; PS50909; GAT; 1.
DR PROSITE; PS50179; VHS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endosome; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..613
FT /note="ADP-ribosylation factor-binding protein GGA2"
FT /id="PRO_0000212682"
FT DOMAIN 33..163
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 188..315
FT /note="GAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00373"
FT DOMAIN 484..605
FT /note="GAE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00093"
FT REGION 316..483
FT /note="Unstructured hinge"
FT REGION 389..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 424
FT /note="A -> P (in dbSNP:rs1135045)"
FT /evidence="ECO:0000269|PubMed:10747088,
FT ECO:0000269|PubMed:10749927, ECO:0000269|PubMed:11331584,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_028275"
FT MUTAGEN 349..353
FT /note="LIDLE->AADAA: Partial loss of clathrin-binding."
FT /evidence="ECO:0000269|PubMed:11301005"
FT CONFLICT 281
FT /note="R -> W (in Ref. 1; AAF05708)"
FT /evidence="ECO:0000305"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:1MHQ"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:1MHQ"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:1MHQ"
FT HELIX 76..92
FT /evidence="ECO:0007829|PDB:1MHQ"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:1MHQ"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:1MHQ"
FT HELIX 125..141
FT /evidence="ECO:0007829|PDB:1MHQ"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:1MHQ"
SQ SEQUENCE 613 AA; 67150 MW; 4B627ABA474A069C CRC64;
MAATAVAAAV AGTESAQGPP GPAASLELWL NKATDPSMSE QDWSAIQNFC EQVNTDPNGP
THAPWLLAHK IQSPQEKEAL YALTVLEMCM NHCGEKFHSE VAKFRFLNEL IKVLSPKYLG
SWATGKVKGR VIEILFSWTV WFPEDIKIRD AYQMLKKQGI IKQDPKLPVD KILPPPSPWP
KSSIFDADEE KSKLLTRLLK SNHPEDLQAA NRLIKNLVKE EQEKSEKVSK RVSAVEEVRS
HVKVLQEMLS MYRRPGQAPP DQEALQVVYE RCEKLRPTLF RLASDTTDDD DALAEILQAN
DLLTQGVLLY KQVMEGRVTF GNRVTSSLGD IPVSRVFQNP AGCMKTCPLI DLEVDNGPAQ
MGTVVPSLLH QDLAALGISD APVTGMVSGQ NCCEEKRNPS SSTLPGGGVQ NPSADRNLLD
LLSAQPAPCP LNYVSQKSVP KEVPPGTKSS PGWSWEAGPL APSPSSQNTP LAQVFVPLES
VKPSSLPPLI VYDRNGFRIL LHFSQTGAPG HPEVQVLLLT MMSTAPQPVW DIMFQVAVPK
SMRVKLQPAS SSKLPAFSPL MPPAVISQML LLDNPHKEPI RLRYKLTFNQ GGQPFSEVGE
VKDFPDLAVL GAA
