GGA1_HUMAN
ID GGA1_HUMAN Reviewed; 639 AA.
AC Q9UJY5; A8K3D3; B0QYR7; Q5R3N1; Q5TG07; Q6IC75; Q86YA9; Q8NCS6; Q9BW94;
AC Q9UG00; Q9UGW0; Q9UGW1;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=ADP-ribosylation factor-binding protein GGA1;
DE AltName: Full=Gamma-adaptin-related protein 1;
DE AltName: Full=Golgi-localized, gamma ear-containing, ARF-binding protein 1;
GN Name=GGA1;
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] (ISOFORM 1).
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] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=10747089; DOI=10.1083/jcb.149.1.81;
RA Dell'Angelica E.C., Puertollano R., Mullins C., Aguilar R.C., Vargas J.D.,
RA Hartnell L.M., Bonifacino J.S.;
RT "GGAs: a family of ADP ribosylation factor-binding proteins related to
RT adaptors and associated with the Golgi complex.";
RL J. Cell Biol. 149:81-94(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 275-639 (ISOFORMS 1/2/3).
RC TISSUE=Brain;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-639 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
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 [11]
RP INTERACTION WITH CLATHRIN, FUNCTION, MUTAGENESIS OF 356-LEU--GLU-360, AND
RP 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 [12]
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 [13]
RP INTERACTION WITH M6PR AND 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 [14]
RP INTERACTION WITH ARF1; ARF5 AND ARF6.
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 [15]
RP INTERACTION WITH SORT1 AND 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 [16]
RP MUTAGENESIS OF ASN-92; SER-355; ASP-358 AND 361-LEU-MET-362,
RP PHOSPHORYLATION AT SER-355, AND INTERACTION WITH IGF2R.
RX PubMed=12060753; DOI=10.1073/pnas.082235699;
RA Doray B., Bruns K., Ghosh P., Kornfeld S.A.;
RT "Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an
RT internal acidic cluster-dileucine motif.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:8072-8077(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 REGULATION BY PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PP2A.
RX PubMed=12578827; DOI=10.1074/jbc.m212543200;
RA Ghosh P., Kornfeld S.;
RT "Phosphorylation-induced conformational changes regulate GGAs 1 and 3
RT function at the trans-Golgi network.";
RL J. Biol. Chem. 278:14543-14549(2003).
RN [20]
RP INTERACTION WITH EPN4.
RX PubMed=12538641; DOI=10.1083/jcb.200208023;
RA Mills I.G., Praefcke G.J.K., Vallis Y., Peter B.J., Olesen L.E.,
RA Gallop J.L., Butler P.J.G., Evans P.R., McMahon H.T.;
RT "EpsinR: an AP1/clathrin interacting protein involved in vesicle
RT trafficking.";
RL J. Cell Biol. 160:213-222(2003).
RN [21]
RP INTERACTION WITH GGA2 AND GGA3, AND SUBCELLULAR LOCATION.
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 [22]
RP INTERACTION WITH CCDC91; P200 AND SYNRG, AND MUTAGENESIS OF ALA-563;
RP VAL-564; VAL-570 AND LEU-572.
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 [23]
RP INTERACTION WITH UBC.
RX PubMed=14660606; DOI=10.1074/jbc.m311702200;
RA Shiba Y., Katoh Y., Shiba T., Yoshino K., Takatsu H., Kobayashi H.,
RA Shin H.-W., Wakatsuki S., Nakayama K.;
RT "GAT (GGA and Tom1) domain responsible for ubiquitin binding and
RT ubiquitination.";
RL J. Biol. Chem. 279:7105-7111(2004).
RN [24]
RP INTERACTION WITH RABEP1; NECAP1; NECAP2 AND AFTPH.
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 [25]
RP INTERACTION WITH ARF1; RABEP1; UBC AND TSG101, MUTAGENESIS OF LEU-182;
RP ASN-194; ILE-197; LYS-198; MET-200; ASP-204; MET-259; ARG-260; PHE-264;
RP ALA-267; LEU-277; LEU-281 AND ASN-284, AND DOMAIN.
RX PubMed=15143060; DOI=10.1074/jbc.m402183200;
RA Mattera R., Puertollano R., Smith W.J., Bonifacino J.S.;
RT "The trihelical bundle subdomain of the GGA proteins interacts with
RT multiple partners through overlapping but distinct sites.";
RL J. Biol. Chem. 279:31409-31418(2004).
RN [26]
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 [27]
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 [28]
RP INTERACTION WITH AFTPH; HEATR5B AND SYNRG.
RX PubMed=15758025; DOI=10.1091/mbc.e04-12-1077;
RA Hirst J., Borner G.H., Harbour M., Robinson M.S.;
RT "The aftiphilin/p200/gamma-synergin complex.";
RL Mol. Biol. Cell 16:2554-2565(2005).
RN [29]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BACE1.
RX PubMed=15886016; DOI=10.1016/j.mcn.2005.03.014;
RA Wahle T., Prager K., Raffler N., Haass C., Famulok M., Walter J.;
RT "GGA proteins regulate retrograde transport of BACE1 from endosomes to the
RT trans-Golgi network.";
RL Mol. Cell. Neurosci. 29:453-461(2005).
RN [30]
RP INTERACTION WITH SORL1.
RX PubMed=17855360; DOI=10.1074/jbc.m705073200;
RA Schmidt V., Sporbert A., Rohe M., Reimer T., Rehm A., Andersen O.M.,
RA Willnow T.E.;
RT "SorLA/LR11 regulates processing of amyloid precursor protein via
RT interaction with adaptors GGA and PACS-1.";
RL J. Biol. Chem. 282:32956-32964(2007).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [33]
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 [34]
RP INTERACTION WITH RNF11.
RX PubMed=20676133; DOI=10.1038/onc.2010.294;
RA Santonico E., Belleudi F., Panni S., Torrisi M.R., Cesareni G.,
RA Castagnoli L.;
RT "Multiple modification and protein interaction signals drive the Ring
RT finger protein 11 (RNF11) E3 ligase to the endosomal compartment.";
RL Oncogene 29:5604-5618(2010).
RN [35]
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 [36]
RP INTERACTION WITH ARF6.
RX PubMed=22522702; DOI=10.1038/emboj.2012.89;
RA Makyio H., Ohgi M., Takei T., Takahashi S., Takatsu H., Katoh Y., Hanai A.,
RA Ueda T., Kanaho Y., Xie Y., Shin H.W., Kamikubo H., Kataoka M.,
RA Kawasaki M., Kato R., Wakatsuki S., Nakayama K.;
RT "Structural basis for Arf6-MKLP1 complex formation on the Flemming body
RT responsible for cytokinesis.";
RL EMBO J. 31:2590-2603(2012).
RN [37]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [38]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [40]
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 [41]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-147.
RX PubMed=11859376; DOI=10.1038/415937a;
RA Shiba T., Takatsu H., Nogi T., Matsugaki N., Kawasaki M., Igarashi N.,
RA Suzuki M., Kato R., Earnest T., Nakayama K., Wakatsuki S.;
RT "Structural basis for recognition of acidic-cluster dileucine sequence by
RT GGA1.";
RL Nature 415:937-941(2002).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 168-208 IN COMPLEX WITH MOUSE
RP ARF1.
RX PubMed=12679809; DOI=10.1038/nsb920;
RA Shiba T., Kawasaki M., Takatsu H., Nogi T., Matsugaki N., Igarashi N.,
RA Suzuki M., Kato R., Nakayama K., Wakatsuki S.;
RT "Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal
RT protein transport.";
RL Nat. Struct. Biol. 10:386-393(2003).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-16 IN COMPLEX WITH CCDC91.
RX PubMed=12858163; DOI=10.1038/nsb955;
RA Collins B.M., Praefcke G.J., Robinson M.S., Owen D.J.;
RT "Structural basis for binding of accessory proteins by the appendage domain
RT of GGAs.";
RL Nat. Struct. Biol. 10:607-613(2003).
RN [44] {ECO:0007744|PDB:3G2S, ECO:0007744|PDB:3G2T, ECO:0007744|PDB:3G2U, ECO:0007744|PDB:3G2V, ECO:0007744|PDB:3G2W}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-147 IN COMPLEX WITH SORL1 AND
RP SORT1, INTERACTION WITH SORL1 AND SORT1, AND MUTAGENESIS OF SER-355.
RX PubMed=20015111; DOI=10.1111/j.1600-0854.2009.01017.x;
RA Cramer J.F., Gustafsen C., Behrens M.A., Oliveira C.L., Pedersen J.S.,
RA Madsen P., Petersen C.M., Thirup S.S.;
RT "GGA autoinhibition revisited.";
RL Traffic 11:259-273(2010).
RN [45]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-239 AND ALA-484.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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:11301005, PubMed:15886016). Mediates export of
CC the GPCR receptor ADRA2B to the cell surface (PubMed:27901063).
CC Required for targeting PKD1:PKD2 complex from the trans-Golgi network
CC to the cilium membrane (By similarity). Regulates retrograde transport
CC of proteins such as phosphorylated form of BACE1 from endosomes to the
CC trans-Golgi network (PubMed:15886016, PubMed:15615712).
CC {ECO:0000250|UniProtKB:Q8R0H9, ECO:0000269|PubMed:11301005,
CC ECO:0000269|PubMed:15615712, ECO:0000269|PubMed:15886016,
CC ECO:0000269|PubMed:27901063}.
CC -!- SUBUNIT: Monomer (Probable). Interacts with GGA2 and GGA3
CC (PubMed:14638859). Binds to clathrin and activated ARFs, including
CC ARF1, ARF5 and ARF6 (PubMed:11301005, PubMed:11950392, PubMed:12679809,
CC PubMed:15143060, PubMed:22522702). Interacts with RABEP1
CC (PubMed:12505986, PubMed:15143060, PubMed:14665628). Interacts with
CC RABGEF1 (PubMed:12505986, PubMed:15143060). Interacts with the type-I
CC membrane proteins LRP3, M6PR/CD-MPR and IGF2R/CI-MPR (PubMed:11390366,
CC PubMed:11387475, PubMed:12060753). Interacts (via N-terminal VHS
CC domain) with SORL1/sorLA and SORT1 (via C-terminal cytosolic domain)
CC (PubMed:11821067, PubMed:17855360, PubMed:20015111). Interacts with
CC EPN4 (PubMed:12538641). Interacts with CCDC91 (PubMed:12808037,
CC PubMed:12858163). Interacts with HEATR5B/p200a (PubMed:12808037,
CC PubMed:15758025). Interacts with SYNRG/gamma-synergin (PubMed:10814529,
CC PubMed:12808037, PubMed:15758025). Interacts (via GAE doamin) with
CC NECAP1 and NECAP2 (PubMed:14665628). Interacts (via GAE domain) with
CC AFTPH/aftiphilin (PubMed:14665628, PubMed:15758025). Interacts with
CC TSG101 and UBC (PubMed:14660606, PubMed:15143060). Interacts with RNF11
CC (PubMed:20676133). Interacts (via VHS domain) with BACE1 (via DXXLL
CC motif); the interaction highly increases when BACE1 is phosphorylated
CC at 'Ser-498' (PubMed:14567678, PubMed:15886016). Interacts with CNST
CC (By similarity). Interacts with ADRA2B (PubMed:27901063). Interacts
CC with ARL3; the interaction recruits, in collaboration with RABEP1,
CC PKD1:PKD2 complex to trans-Golgi network and is required for ciliary
CC targeting (By similarity). {ECO:0000250|UniProtKB:Q8R0H9,
CC ECO:0000269|PubMed:10814529, ECO:0000269|PubMed:11301005,
CC ECO:0000269|PubMed:11387475, ECO:0000269|PubMed:11390366,
CC ECO:0000269|PubMed:11821067, ECO:0000269|PubMed:11950392,
CC ECO:0000269|PubMed:12060753, ECO:0000269|PubMed:12505986,
CC ECO:0000269|PubMed:12538641, ECO:0000269|PubMed:12679809,
CC ECO:0000269|PubMed:12808037, ECO:0000269|PubMed:12858163,
CC ECO:0000269|PubMed:14567678, ECO:0000269|PubMed:14638859,
CC ECO:0000269|PubMed:14660606, ECO:0000269|PubMed:14665628,
CC ECO:0000269|PubMed:15143060, ECO:0000269|PubMed:15758025,
CC ECO:0000269|PubMed:15886016, ECO:0000269|PubMed:17855360,
CC ECO:0000269|PubMed:20015111, ECO:0000269|PubMed:20676133,
CC ECO:0000269|PubMed:22522702, ECO:0000269|PubMed:27901063, ECO:0000305}.
CC -!- INTERACTION:
CC Q9UJY5; P56817: BACE1; NbExp=4; IntAct=EBI-447141, EBI-2433139;
CC Q9UJY5; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-447141, EBI-747505;
CC Q9UJY5; O60941: DTNB; NbExp=4; IntAct=EBI-447141, EBI-740402;
CC Q9UJY5; Q9UJY4: GGA2; NbExp=7; IntAct=EBI-447141, EBI-447646;
CC Q9UJY5; Q9NZ52: GGA3; NbExp=4; IntAct=EBI-447141, EBI-447404;
CC Q9UJY5; P11717: IGF2R; NbExp=4; IntAct=EBI-447141, EBI-1048580;
CC Q9UJY5; Q7Z3U7: MON2; NbExp=2; IntAct=EBI-447141, EBI-358882;
CC Q9UJY5; Q15276: RABEP1; NbExp=8; IntAct=EBI-447141, EBI-447043;
CC Q9UJY5; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-447141, EBI-396669;
CC Q9UJY5; Q92673: SORL1; NbExp=4; IntAct=EBI-447141, EBI-1171329;
CC Q9UJY5; Q99523: SORT1; NbExp=2; IntAct=EBI-447141, EBI-1057058;
CC Q9UJY5; P0CG47: UBB; NbExp=3; IntAct=EBI-447141, EBI-413034;
CC Q9UJY5; P19328: Adra2b; Xeno; NbExp=3; IntAct=EBI-447141, EBI-21453893;
CC Q9UJY5; P62331: Arf6; Xeno; NbExp=2; IntAct=EBI-447141, EBI-988682;
CC Q9UJY5; O18973: RABGEF1; Xeno; NbExp=2; IntAct=EBI-447141, EBI-447376;
CC Q9UJY5-4; P05067: APP; NbExp=3; IntAct=EBI-12108696, EBI-77613;
CC Q9UJY5-4; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-12108696, EBI-747505;
CC Q9UJY5-4; Q8NE08: COL25A1; NbExp=3; IntAct=EBI-12108696, EBI-25836642;
CC Q9UJY5-4; Q9BY27: DGCR6L; NbExp=3; IntAct=EBI-12108696, EBI-742953;
CC Q9UJY5-4; O60941-5: DTNB; NbExp=3; IntAct=EBI-12108696, EBI-11984733;
CC Q9UJY5-4; Q8WYH8: ING5; NbExp=3; IntAct=EBI-12108696, EBI-488533;
CC Q9UJY5-4; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-12108696, EBI-1055254;
CC Q9UJY5-4; A4D0Q3: KIAA1218; NbExp=3; IntAct=EBI-12108696, EBI-14308786;
CC Q9UJY5-4; I6L9F6: NEFL; NbExp=3; IntAct=EBI-12108696, EBI-10178578;
CC Q9UJY5-5; Q14114-3: LRP8; NbExp=3; IntAct=EBI-25903400, EBI-25832196;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:15886016}; Peripheral membrane protein. Endosome
CC membrane {ECO:0000269|PubMed:15886016}; Peripheral membrane protein.
CC Early endosome membrane {ECO:0000269|PubMed:15886016}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9UJY5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJY5-2; Sequence=VSP_001744;
CC Name=3;
CC IsoId=Q9UJY5-3; Sequence=VSP_042806;
CC Name=4;
CC IsoId=Q9UJY5-4; Sequence=VSP_042809;
CC Name=5;
CC IsoId=Q9UJY5-5; Sequence=VSP_042807, VSP_042808;
CC Name=6;
CC IsoId=Q9UJY5-6; Sequence=VSP_057352;
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).
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. {ECO:0000269|PubMed:15143060}.
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: Phosphorylated by CK2 and dephosphorylated by PP2A.
CC Phosphorylation of GGA1 allows the internal DXXLL motif to bind the VHS
CC domain and to inhibit the recognition of cargo signals.
CC {ECO:0000269|PubMed:12060753}.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GGA protein family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AF190862; AAF05707.1; -; mRNA.
DR EMBL; AF218584; AAF42847.1; -; mRNA.
DR EMBL; AF233521; AAF35393.1; -; mRNA.
DR EMBL; CR456493; CAG30379.1; -; mRNA.
DR EMBL; AK075256; BAC11501.1; -; mRNA.
DR EMBL; AK122898; BAG53788.1; -; mRNA.
DR EMBL; AK290548; BAF83237.1; -; mRNA.
DR EMBL; AL035496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z83844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60169.1; -; Genomic_DNA.
DR EMBL; BC000538; AAH00538.2; -; mRNA.
DR EMBL; BC010917; AAH10917.1; -; mRNA.
DR EMBL; BC029388; AAH29388.1; -; mRNA.
DR EMBL; BC044629; AAH44629.1; -; mRNA.
DR EMBL; AL110219; CAB53679.1; -; mRNA.
DR CCDS; CCDS13951.1; -. [Q9UJY5-1]
DR CCDS; CCDS33643.1; -. [Q9UJY5-4]
DR CCDS; CCDS54526.1; -. [Q9UJY5-3]
DR CCDS; CCDS87022.1; -. [Q9UJY5-6]
DR PIR; T14759; T14759.
DR RefSeq; NP_001001560.1; NM_001001560.2. [Q9UJY5-4]
DR RefSeq; NP_001166158.1; NM_001172687.1.
DR RefSeq; NP_001166159.1; NM_001172688.1. [Q9UJY5-3]
DR RefSeq; NP_037497.1; NM_013365.4. [Q9UJY5-1]
DR RefSeq; XP_005261574.1; XM_005261517.3.
DR RefSeq; XP_005261577.1; XM_005261520.1. [Q9UJY5-3]
DR RefSeq; XP_006724292.1; XM_006724229.1. [Q9UJY5-3]
DR RefSeq; XP_011528424.1; XM_011530122.1.
DR RefSeq; XP_016884249.1; XM_017028760.1.
DR RefSeq; XP_016884250.1; XM_017028761.1. [Q9UJY5-3]
DR RefSeq; XP_016884251.1; XM_017028762.1.
DR PDB; 1J2J; X-ray; 1.60 A; B=166-210.
DR PDB; 1JWF; X-ray; 2.10 A; A=1-147.
DR PDB; 1JWG; X-ray; 2.00 A; A/B=1-147.
DR PDB; 1NA8; X-ray; 2.30 A; A/B=494-639.
DR PDB; 1NAF; X-ray; 2.80 A; A=165-314.
DR PDB; 1NWM; X-ray; 2.40 A; X=166-302.
DR PDB; 1O3X; X-ray; 2.10 A; A=166-305.
DR PDB; 1OM9; X-ray; 2.50 A; A/B=494-639.
DR PDB; 1OXZ; X-ray; 2.80 A; A=141-326.
DR PDB; 1PY1; X-ray; 2.60 A; A/B/C/D=2-157.
DR PDB; 1UJJ; X-ray; 2.60 A; A/B=1-147.
DR PDB; 1UJK; X-ray; 1.90 A; A/B=1-147.
DR PDB; 1X79; X-ray; 2.41 A; A=210-302.
DR PDB; 2DWX; X-ray; 2.55 A; A/B/C/D=507-639, P/Q=376-388.
DR PDB; 2DWY; X-ray; 2.30 A; A/B/C/D=507-639.
DR PDB; 3G2S; X-ray; 1.70 A; A/B=1-147.
DR PDB; 3G2T; X-ray; 2.00 A; A/B=1-147.
DR PDB; 3G2U; X-ray; 2.30 A; A/B=1-147.
DR PDB; 3G2V; X-ray; 2.10 A; A/B=1-147.
DR PDB; 3G2W; X-ray; 2.40 A; A/B=1-147, C/D=351-364.
DR PDBsum; 1J2J; -.
DR PDBsum; 1JWF; -.
DR PDBsum; 1JWG; -.
DR PDBsum; 1NA8; -.
DR PDBsum; 1NAF; -.
DR PDBsum; 1NWM; -.
DR PDBsum; 1O3X; -.
DR PDBsum; 1OM9; -.
DR PDBsum; 1OXZ; -.
DR PDBsum; 1PY1; -.
DR PDBsum; 1UJJ; -.
DR PDBsum; 1UJK; -.
DR PDBsum; 1X79; -.
DR PDBsum; 2DWX; -.
DR PDBsum; 2DWY; -.
DR PDBsum; 3G2S; -.
DR PDBsum; 3G2T; -.
DR PDBsum; 3G2U; -.
DR PDBsum; 3G2V; -.
DR PDBsum; 3G2W; -.
DR AlphaFoldDB; Q9UJY5; -.
DR SMR; Q9UJY5; -.
DR BioGRID; 117540; 100.
DR ELM; Q9UJY5; -.
DR IntAct; Q9UJY5; 67.
DR MINT; Q9UJY5; -.
DR STRING; 9606.ENSP00000341344; -.
DR TCDB; 9.B.278.1.2; the organellar-targeting adaptor protein complex (o-apc) family.
DR GlyGen; Q9UJY5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UJY5; -.
DR PhosphoSitePlus; Q9UJY5; -.
DR BioMuta; GGA1; -.
DR DMDM; 14548066; -.
DR EPD; Q9UJY5; -.
DR jPOST; Q9UJY5; -.
DR MassIVE; Q9UJY5; -.
DR MaxQB; Q9UJY5; -.
DR PaxDb; Q9UJY5; -.
DR PeptideAtlas; Q9UJY5; -.
DR PRIDE; Q9UJY5; -.
DR ProteomicsDB; 66377; -.
DR ProteomicsDB; 84692; -. [Q9UJY5-1]
DR ProteomicsDB; 84693; -. [Q9UJY5-2]
DR ProteomicsDB; 84694; -. [Q9UJY5-3]
DR ProteomicsDB; 84695; -. [Q9UJY5-4]
DR ProteomicsDB; 84696; -. [Q9UJY5-5]
DR Antibodypedia; 12029; 239 antibodies from 28 providers.
DR DNASU; 26088; -.
DR Ensembl; ENST00000325180.12; ENSP00000321288.8; ENSG00000100083.19. [Q9UJY5-4]
DR Ensembl; ENST00000343632.9; ENSP00000341344.4; ENSG00000100083.19. [Q9UJY5-1]
DR Ensembl; ENST00000381756.9; ENSP00000371175.5; ENSG00000100083.19. [Q9UJY5-6]
DR Ensembl; ENST00000406772.5; ENSP00000385287.1; ENSG00000100083.19. [Q9UJY5-3]
DR GeneID; 26088; -.
DR KEGG; hsa:26088; -.
DR MANE-Select; ENST00000343632.9; ENSP00000341344.4; NM_013365.5; NP_037497.1.
DR UCSC; uc003atc.4; human. [Q9UJY5-1]
DR CTD; 26088; -.
DR DisGeNET; 26088; -.
DR GeneCards; GGA1; -.
DR HGNC; HGNC:17842; GGA1.
DR HPA; ENSG00000100083; Tissue enhanced (testis).
DR MIM; 606004; gene.
DR neXtProt; NX_Q9UJY5; -.
DR OpenTargets; ENSG00000100083; -.
DR PharmGKB; PA28657; -.
DR VEuPathDB; HostDB:ENSG00000100083; -.
DR eggNOG; KOG1086; Eukaryota.
DR GeneTree; ENSGT00940000156448; -.
DR HOGENOM; CLU_015010_0_0_1; -.
DR InParanoid; Q9UJY5; -.
DR OMA; DEWNFAS; -.
DR OrthoDB; 594067at2759; -.
DR PhylomeDB; Q9UJY5; -.
DR TreeFam; TF318574; -.
DR PathwayCommons; Q9UJY5; -.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR SignaLink; Q9UJY5; -.
DR BioGRID-ORCS; 26088; 9 hits in 1072 CRISPR screens.
DR ChiTaRS; GGA1; human.
DR EvolutionaryTrace; Q9UJY5; -.
DR GeneWiki; GGA1; -.
DR GenomeRNAi; 26088; -.
DR Pharos; Q9UJY5; Tbio.
DR PRO; PR:Q9UJY5; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9UJY5; protein.
DR Bgee; ENSG00000100083; Expressed in pancreatic ductal cell and 193 other tissues.
DR ExpressionAtlas; Q9UJY5; baseline and differential.
DR Genevisible; Q9UJY5; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; 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:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IPI:CAFA.
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; IDA:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IDA:UniProtKB.
DR GO; GO:0034394; P:protein localization to cell surface; IDA:UniProtKB.
DR GO; GO:1903441; P:protein localization to ciliary membrane; IEA:Ensembl.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:UniProtKB.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR DisProt; DP00314; -.
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; Acetylation; Alternative splicing; Endosome; Golgi apparatus;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport;
KW Ubl conjugation.
FT CHAIN 1..639
FT /note="ADP-ribosylation factor-binding protein GGA1"
FT /id="PRO_0000212680"
FT DOMAIN 17..147
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 171..299
FT /note="GAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00373"
FT DOMAIN 510..631
FT /note="GAE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00093"
FT REGION 114..274
FT /note="Interaction with ARF3"
FT REGION 300..509
FT /note="Unstructured hinge"
FT REGION 320..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 358..362
FT /note="Autoinhibitory"
FT COMPBIAS 369..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 355
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000305|PubMed:12060753"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042806"
FT VAR_SEQ 68
FT /note="T -> TVRRGEATIRPPPCDDTK (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15461802"
FT /id="VSP_057352"
FT VAR_SEQ 69..101
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001744"
FT VAR_SEQ 70..89
FT /note="LETCMKSCGKRFHDEVGKFR -> RRGEATIRPPPCDDTKGGQD (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042807"
FT VAR_SEQ 90..639
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042808"
FT VAR_SEQ 277..363
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042809"
FT VARIANT 239
FT /note="G -> S (in a breast cancer sample; somatic mutation;
FT dbSNP:rs765255006)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036522"
FT VARIANT 484
FT /note="P -> A (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036523"
FT MUTAGEN 92
FT /note="N->A: Abolishes interaction with IGF2R."
FT /evidence="ECO:0000269|PubMed:12060753"
FT MUTAGEN 182
FT /note="L->A: Abolishes interaction with ARF1, UBC and
FT TSG101."
FT /evidence="ECO:0000269|PubMed:15143060"
FT MUTAGEN 194
FT /note="N->A: Abolishes interaction with ARF1 and RABEP1."
FT /evidence="ECO:0000269|PubMed:15143060"
FT MUTAGEN 197
FT /note="I->A: Abolishes interaction with ARF1, UBC and
FT TSG101."
FT /evidence="ECO:0000269|PubMed:15143060"
FT MUTAGEN 198
FT /note="K->A: Abolishes interaction with ARF1."
FT /evidence="ECO:0000269|PubMed:15143060"
FT MUTAGEN 200
FT /note="M->A: Abolishes interaction with ARF1."
FT /evidence="ECO:0000269|PubMed:15143060"
FT MUTAGEN 204
FT /note="D->A: Abolishes interaction with ARF1."
FT /evidence="ECO:0000269|PubMed:15143060"
FT MUTAGEN 259
FT /note="M->K: Abolishes interaction with RABEP1."
FT /evidence="ECO:0000269|PubMed:15143060"
FT MUTAGEN 260
FT /note="R->A: No effect on interaction with RABEP1."
FT /evidence="ECO:0000269|PubMed:15143060"
FT MUTAGEN 260
FT /note="R->E: Abolishes interaction with RABEP1 and UBC."
FT /evidence="ECO:0000269|PubMed:15143060"
FT MUTAGEN 264
FT /note="F->A: Abolishes interaction with RABEP1."
FT /evidence="ECO:0000269|PubMed:15143060"
FT MUTAGEN 267
FT /note="A->D: Abolishes interaction with RABEP1 and UBC."
FT /evidence="ECO:0000269|PubMed:15143060"
FT MUTAGEN 277
FT /note="L->A: Abolishes interaction with RABEP1, UBC and
FT TSG101."
FT /evidence="ECO:0000269|PubMed:15143060"
FT MUTAGEN 281
FT /note="L->A: Abolishes interaction with RABEP1."
FT /evidence="ECO:0000269|PubMed:15143060"
FT MUTAGEN 284
FT /note="N->A: Abolishes interaction with RABEP1."
FT /evidence="ECO:0000269|PubMed:15143060"
FT MUTAGEN 284
FT /note="N->S: Abolishes interaction with RABEP1."
FT /evidence="ECO:0000269|PubMed:15143060"
FT MUTAGEN 355
FT /note="S->A: Increased interaction with IGF2R. Reduced
FT phosphorylation. No effect on the interaction with SORL1."
FT /evidence="ECO:0000269|PubMed:12060753,
FT ECO:0000269|PubMed:20015111"
FT MUTAGEN 355
FT /note="S->D: Abolishes interaction with IGF2R. No effect on
FT the interaction with SORL1."
FT /evidence="ECO:0000269|PubMed:12060753,
FT ECO:0000269|PubMed:20015111"
FT MUTAGEN 356..360
FT /note="LLDDE->AADAA: Partial loss of clathrin-binding."
FT /evidence="ECO:0000269|PubMed:11301005"
FT MUTAGEN 358
FT /note="D->A: Increased interaction with IGF2R."
FT /evidence="ECO:0000269|PubMed:12060753"
FT MUTAGEN 361..362
FT /note="LM->AA: Increased interaction with IGF2R."
FT /evidence="ECO:0000269|PubMed:12060753"
FT MUTAGEN 563
FT /note="A->D: Abolishes interaction with CCDC91."
FT /evidence="ECO:0000269|PubMed:12808037"
FT MUTAGEN 564
FT /note="V->D: Abolishes interaction with CCDC91."
FT /evidence="ECO:0000269|PubMed:12808037"
FT MUTAGEN 570
FT /note="V->E: Abolishes interaction with CCDC91."
FT /evidence="ECO:0000269|PubMed:12808037"
FT MUTAGEN 572
FT /note="L->E: Abolishes interaction with CCDC91."
FT /evidence="ECO:0000269|PubMed:12808037"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:1UJK"
FT HELIX 10..17
FT /evidence="ECO:0007829|PDB:3G2S"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:3G2S"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:3G2S"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3G2S"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:3G2S"
FT HELIX 60..76
FT /evidence="ECO:0007829|PDB:3G2S"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:3G2S"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:3G2S"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:3G2S"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:3G2S"
FT HELIX 109..125
FT /evidence="ECO:0007829|PDB:3G2S"
FT HELIX 130..141
FT /evidence="ECO:0007829|PDB:3G2S"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:1J2J"
FT HELIX 187..205
FT /evidence="ECO:0007829|PDB:1J2J"
FT HELIX 212..233
FT /evidence="ECO:0007829|PDB:1X79"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:1O3X"
FT HELIX 243..267
FT /evidence="ECO:0007829|PDB:1O3X"
FT HELIX 274..298
FT /evidence="ECO:0007829|PDB:1O3X"
FT HELIX 494..497
FT /evidence="ECO:0007829|PDB:1NA8"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:1NA8"
FT STRAND 515..520
FT /evidence="ECO:0007829|PDB:1NA8"
FT STRAND 523..531
FT /evidence="ECO:0007829|PDB:1NA8"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:2DWY"
FT STRAND 540..549
FT /evidence="ECO:0007829|PDB:1NA8"
FT STRAND 555..563
FT /evidence="ECO:0007829|PDB:1NA8"
FT STRAND 568..572
FT /evidence="ECO:0007829|PDB:1NA8"
FT STRAND 592..599
FT /evidence="ECO:0007829|PDB:1NA8"
FT STRAND 608..616
FT /evidence="ECO:0007829|PDB:1NA8"
FT STRAND 619..627
FT /evidence="ECO:0007829|PDB:1NA8"
FT TURN 633..635
FT /evidence="ECO:0007829|PDB:1NA8"
FT HELIX 636..638
FT /evidence="ECO:0007829|PDB:1NA8"
SQ SEQUENCE 639 AA; 70384 MW; B0B6F089FA0F7DD5 CRC64;
MEPAMEPETL EARINRATNP LNKELDWASI NGFCEQLNED FEGPPLATRL LAHKIQSPQE
WEAIQALTVL ETCMKSCGKR FHDEVGKFRF LNELIKVVSP KYLGSRTSEK VKNKILELLY
SWTVGLPEEV KIAEAYQMLK KQGIVKSDPK LPDDTTFPLP PPRPKNVIFE DEEKSKMLAR
LLKSSHPEDL RAANKLIKEM VQEDQKRMEK ISKRVNAIEE VNNNVKLLTE MVMSHSQGGA
AAGSSEDLMK ELYQRCERMR PTLFRLASDT EDNDEALAEI LQANDNLTQV INLYKQLVRG
EEVNGDATAG SIPGSTSALL DLSGLDLPPA GTTYPAMPTR PGEQASPEQP SASVSLLDDE
LMSLGLSDPT PPSGPSLDGT GWNSFQSSDA TEPPAPALAQ APSMESRPPA QTSLPASSGL
DDLDLLGKTL LQQSLPPESQ QVRWEKQQPT PRLTLRDLQN KSSSCSSPSS SATSLLHTVS
PEPPRPPQQP VPTELSLASI TVPLESIKPS NILPVTVYDQ HGFRILFHFA RDPLPGRSDV
LVVVVSMLST APQPIRNIVF QSAVPKVMKV KLQPPSGTEL PAFNPIVHPS AITQVLLLAN
PQKEKVRLRY KLTFTMGDQT YNEMGDVDQF PPPETWGSL
