ID GORS2_HUMAN Reviewed; 452 AA.
AC Q9H8Y8; B4DKT0; Q53TE3; Q96I74; Q96K84; Q9H946; Q9UFW4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 189.
DE RecName: Full=Golgi reassembly-stacking protein 2;
DE Short=GRS2;
DE AltName: Full=Golgi phosphoprotein 6;
DE Short=GOLPH6;
DE AltName: Full=Golgi reassembly-stacking protein of 55 kDa;
DE Short=GRASP55;
DE AltName: Full=p59;
GN Name=GORASP2; Synonyms=GOLPH6;
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), PROTEIN SEQUENCE OF 82-97; 134-141;
RP 164-175 AND 203-229, FUNCTION, SUBCELLULAR LOCATION, MYRISTOYLATION AT
RP GLY-2, PALMITOYLATION, AND INTERACTION WITH TGFA.
RX PubMed=11101516; DOI=10.1093/emboj/19.23.6427;
RA Kuo A., Zhong C., Lane W.S., Derynck R.;
RT "Transmembrane transforming growth factor-alpha tethers to the PDZ domain-
RT containing, Golgi membrane-associated protein p59/GRASP55.";
RL EMBO J. 19:6427-6439(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT THR-225, AND
RP MUTAGENESIS OF THR-222 AND THR-225.
RX PubMed=11408587; DOI=10.1091/mbc.12.6.1811;
RA Jesch S.A., Lewis T.S., Ahn N.G., Linstedt A.D.;
RT "Mitotic phosphorylation of Golgi reassembly stacking protein 55 by
RT mitogen-activated protein kinase ERK2.";
RL Mol. Biol. Cell 12:1811-1817(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP PHE-432.
RC TISSUE=Tongue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10487747; DOI=10.1093/emboj/18.18.4949;
RA Shorter J., Watson R., Giannakou M.-E., Clarke M., Warren G., Barr F.A.;
RT "GRASP55, a second mammalian GRASP protein involved in the stacking of
RT Golgi cisternae in a cell-free system.";
RL EMBO J. 18:4949-4960(1999).
RN [9]
RP INTERACTION WITH BLZF1/GOLGIN 45.
RX PubMed=11739401; DOI=10.1083/jcb.200108079;
RA Short B., Preisinger C., Koerner R., Kopajtich R., Byron O., Barr F.A.;
RT "A GRASP55-rab2 effector complex linking Golgi structure to membrane
RT traffic.";
RL J. Cell Biol. 155:877-883(2001).
RN [10]
RP INTERACTION WITH PROTEINS OF THE P24 CARGO FAMILY.
RX PubMed=11739402; DOI=10.1083/jcb.200108102;
RA Barr F.A., Preisinger C., Kopajtich R., Koerner R.;
RT "Golgi matrix proteins interact with p24 cargo receptors and aid their
RT efficient retention in the Golgi apparatus.";
RL J. Cell Biol. 155:885-891(2001).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-222; THR-225 AND THR-415, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-415, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [13]
RP INTERACTION WITH CNIH1 AND TGFA.
RX PubMed=17607000; DOI=10.1242/jcs.004200;
RA Perez Castro C., Piscopo D., Nakagawa T., Derynck R.;
RT "Cornichon regulates transport and secretion of TGFalpha-related proteins
RT in metazoan cells.";
RL J. Cell Sci. 120:2454-2466(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-415; THR-433; SER-436;
RP SER-449 AND SER-451, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP IDENTIFICATION BY MASS 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 [16]
RP INTERACTION WITH KCTD5.
RX PubMed=19361449; DOI=10.1016/j.jmb.2009.01.030;
RA Dementieva I.S., Tereshko V., McCrossan Z.A., Solomaha E., Araki D., Xu C.,
RA Grigorieff N., Goldstein S.A.;
RT "Pentameric assembly of potassium channel tetramerization domain-containing
RT protein 5.";
RL J. Mol. Biol. 387:175-191(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, AND IDENTIFICATION BY
RP 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; THR-222; THR-225 AND
RP THR-415, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
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 [20]
RP FUNCTION, INTERACTION WITH CFTR, MUTAGENESIS OF GLY-2 AND SER-441, AND
RP PHOSPHORYLATION AT SER-441.
RX PubMed=21884936; DOI=10.1016/j.cell.2011.07.021;
RA Gee H.Y., Noh S.H., Tang B.L., Kim K.H., Lee M.G.;
RT "Rescue of DeltaF508-CFTR trafficking via a GRASP-dependent unconventional
RT secretion pathway.";
RL Cell 146:746-760(2011).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-222; THR-225 AND SER-451, AND
RP IDENTIFICATION BY 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; THR-222 AND THR-225, AND
RP IDENTIFICATION BY 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 [24]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [25]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25807930; DOI=10.1002/anie.201500342;
RA Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I.,
RA Tate E.W.;
RT "Multifunctional reagents for quantitative proteome-wide analysis of
RT protein modification in human cells and dynamic profiling of protein
RT lipidation during vertebrate development.";
RL Angew. Chem. Int. Ed. 54:5948-5951(2015).
RN [26]
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 [27]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MYRISTOYLATION AT GLY-2,
RP MUTAGENESIS OF GLY-2; ASP-148; SER-441; SER-449 AND SER-451, AND
RP PHOSPHORYLATION AT SER-441; SER-449 AND SER-451.
RX PubMed=27062250; DOI=10.1111/tra.12403;
RA Kim J., Noh S.H., Piao H., Kim D.H., Kim K., Cha J.S., Chung W.Y.,
RA Cho H.S., Kim J.Y., Lee M.G.;
RT "Monomerization and ER relocalization of GRASP Is a requisite for
RT unconventional secretion of CFTR.";
RL Traffic 17:733-753(2016).
RN [28]
RP FUNCTION, INTERACTION WITH SEC16A, AND SUBCELLULAR LOCATION.
RX PubMed=28067262; DOI=10.1038/srep39887;
RA Piao H., Kim J., Noh S.H., Kweon H.S., Kim J.Y., Lee M.G.;
RT "Sec16A is critical for both conventional and unconventional secretion of
RT CFTR.";
RL Sci. Rep. 7:39887-39887(2017).
RN [29]
RP FUNCTION.
RX PubMed=33301566; DOI=10.1083/jcb.202007052;
RA Zhang Y., Seemann J.;
RT "Rapid degradation of GRASP55 and GRASP65 reveals their immediate impact on
RT the Golgi structure.";
RL J. Cell Biol. 220:0-0(2021).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-208, FUNCTION, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LEU-59 AND ILE-100.
RX PubMed=21515684; DOI=10.1074/jbc.c111.245324;
RA Truschel S.T., Sengupta D., Foote A., Heroux A., Macbeth M.R.,
RA Linstedt A.D.;
RT "Structure of the membrane-tethering GRASP domain reveals a unique PDZ
RT ligand interaction that mediates Golgi biogenesis.";
RL J. Biol. Chem. 286:20125-20129(2011).
RN [31] {ECO:0007744|PDB:4EDJ}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-208 OF MUTANT ASP-189,
RP MUTAGENESIS OF SER-189, AND FUNCTION.
RX PubMed=22523075; DOI=10.1074/jbc.m111.326256;
RA Truschel S.T., Zhang M., Bachert C., Macbeth M.R., Linstedt A.D.;
RT "Allosteric regulation of GRASP protein-dependent Golgi membrane tethering
RT by mitotic phosphorylation.";
RL J. Biol. Chem. 287:19870-19875(2012).
CC -!- FUNCTION: Key structural protein of the Golgi apparatus
CC (PubMed:33301566). The membrane cisternae of the Golgi apparatus adhere
CC to each other to form stacks, which are aligned side by side to form
CC the Golgi ribbon (PubMed:33301566). Acting in concert with
CC GORASP1/GRASP65, is required for the formation and maintenance of the
CC Golgi ribbon, and may be dispensable for the formation of stacks
CC (PubMed:33301566). However, other studies suggest that GORASP2 plays a
CC role in the assembly and membrane stacking of the Golgi cisternae, and
CC in the process by which Golgi stacks reform after breakdown during
CC mitosis and meiosis (PubMed:10487747, PubMed:21515684,
CC PubMed:22523075). May regulate the intracellular transport and
CC presentation of a defined set of transmembrane proteins, such as
CC transmembrane TGFA (PubMed:11101516). Required for normal acrosome
CC formation during spermiogenesis and normal male fertility, probably by
CC promoting colocalization of JAM2 and JAM3 at contact sites between germ
CC cells and Sertoli cells (By similarity). Mediates ER stress-induced
CC unconventional (ER/Golgi-independent) trafficking of core-glycosylated
CC CFTR to cell membrane (PubMed:21884936, PubMed:27062250,
CC PubMed:28067262). {ECO:0000250|UniProtKB:Q99JX3,
CC ECO:0000269|PubMed:10487747, ECO:0000269|PubMed:11101516,
CC ECO:0000269|PubMed:21515684, ECO:0000269|PubMed:21884936,
CC ECO:0000269|PubMed:22523075, ECO:0000269|PubMed:27062250,
CC ECO:0000269|PubMed:28067262}.
CC -!- SUBUNIT: Homodimer. Homooligomer. ER stress induces phosphorylation-
CC dependent monomerization (PubMed:27062250). Interacts with BLZF1/Golgin
CC 45 (PubMed:11739401). Identified in a complex with RAB2 and GORASP2
CC (PubMed:11739401). Interacts with JAM2 and JAM3 (By similarity).
CC Interacts with members of the p24 cargo receptors (PubMed:11739402).
CC Interacts with CNIH1 and the cytoplasmic domain of transmembrane TGFA,
CC prior its transit in the trans-Golgi (PubMed:11101516,
CC PubMed:17607000). Interacts with KCTD5 (PubMed:19361449). Interacts
CC with TMED2 and TMED3 (By similarity). Interacts with SEC16A in response
CC to ER stress (PubMed:28067262). Interacts (via PDZ GRASP-type 1 domain)
CC with core-glycosylated CFTR in response to ER stress (PubMed:21884936).
CC {ECO:0000250|UniProtKB:Q99JX3, ECO:0000250|UniProtKB:Q9R064,
CC ECO:0000269|PubMed:11101516, ECO:0000269|PubMed:11739401,
CC ECO:0000269|PubMed:11739402, ECO:0000269|PubMed:17607000,
CC ECO:0000269|PubMed:19361449, ECO:0000269|PubMed:21884936,
CC ECO:0000269|PubMed:27062250, ECO:0000269|PubMed:28067262}.
CC -!- INTERACTION:
CC Q9H8Y8; Q9H7C9: AAMDC; NbExp=3; IntAct=EBI-739467, EBI-10308705;
CC Q9H8Y8; Q96HD9: ACY3; NbExp=15; IntAct=EBI-739467, EBI-3916242;
CC Q9H8Y8; Q9NXW9: ALKBH4; NbExp=3; IntAct=EBI-739467, EBI-8637516;
CC Q9H8Y8; Q96GX9: APIP; NbExp=3; IntAct=EBI-739467, EBI-359248;
CC Q9H8Y8; O94989: ARHGEF15; NbExp=3; IntAct=EBI-739467, EBI-740691;
CC Q9H8Y8; Q15041: ARL6IP1; NbExp=4; IntAct=EBI-739467, EBI-714543;
CC Q9H8Y8; O95671: ASMTL; NbExp=3; IntAct=EBI-739467, EBI-743231;
CC Q9H8Y8; O75348: ATP6V1G1; NbExp=5; IntAct=EBI-739467, EBI-711802;
CC Q9H8Y8; P54253: ATXN1; NbExp=3; IntAct=EBI-739467, EBI-930964;
CC Q9H8Y8; P54252: ATXN3; NbExp=3; IntAct=EBI-739467, EBI-946046;
CC Q9H8Y8; Q7L4P6: BEND5; NbExp=4; IntAct=EBI-739467, EBI-724373;
CC Q9H8Y8; Q9Y2F9: BTBD3; NbExp=3; IntAct=EBI-739467, EBI-311155;
CC Q9H8Y8; Q6P1W5: C1orf94; NbExp=7; IntAct=EBI-739467, EBI-946029;
CC Q9H8Y8; Q9Y2V2: CARHSP1; NbExp=3; IntAct=EBI-739467, EBI-718719;
CC Q9H8Y8; Q13191: CBLB; NbExp=8; IntAct=EBI-739467, EBI-744027;
CC Q9H8Y8; Q9Y3M2: CBY1; NbExp=3; IntAct=EBI-739467, EBI-947308;
CC Q9H8Y8; Q494R4: CCDC153; NbExp=4; IntAct=EBI-739467, EBI-10241443;
CC Q9H8Y8; Q9GZT6: CCDC90B; NbExp=3; IntAct=EBI-739467, EBI-713148;
CC Q9H8Y8; P32320: CDA; NbExp=3; IntAct=EBI-739467, EBI-9250559;
CC Q9H8Y8; Q9UJX2: CDC23; NbExp=9; IntAct=EBI-739467, EBI-396137;
CC Q9H8Y8; Q07002: CDK18; NbExp=3; IntAct=EBI-739467, EBI-746238;
CC Q9H8Y8; P55273: CDKN2D; NbExp=3; IntAct=EBI-739467, EBI-745859;
CC Q9H8Y8; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-739467, EBI-742887;
CC Q9H8Y8; P13569: CFTR; NbExp=6; IntAct=EBI-739467, EBI-349854;
CC Q9H8Y8; Q9UFW8: CGGBP1; NbExp=3; IntAct=EBI-739467, EBI-723153;
CC Q9H8Y8; Q9HD42: CHMP1A; NbExp=3; IntAct=EBI-739467, EBI-1057156;
CC Q9H8Y8; Q9UHC6: CNTNAP2; NbExp=3; IntAct=EBI-739467, EBI-310892;
CC Q9H8Y8; P02489: CRYAA; NbExp=12; IntAct=EBI-739467, EBI-6875961;
CC Q9H8Y8; P02511: CRYAB; NbExp=3; IntAct=EBI-739467, EBI-739060;
CC Q9H8Y8; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-739467, EBI-9087876;
CC Q9H8Y8; P32321: DCTD; NbExp=7; IntAct=EBI-739467, EBI-739870;
CC Q9H8Y8; Q14565: DMC1; NbExp=8; IntAct=EBI-739467, EBI-930865;
CC Q9H8Y8; P59910: DNAJB13; NbExp=3; IntAct=EBI-739467, EBI-11514233;
CC Q9H8Y8; Q16555: DPYSL2; NbExp=15; IntAct=EBI-739467, EBI-1104711;
CC Q9H8Y8; Q9H596: DUSP21; NbExp=7; IntAct=EBI-739467, EBI-7357329;
CC Q9H8Y8; Q13115: DUSP4; NbExp=3; IntAct=EBI-739467, EBI-6591081;
CC Q9H8Y8; O43781-2: DYRK3; NbExp=5; IntAct=EBI-739467, EBI-13332019;
CC Q9H8Y8; Q9NTX5: ECHDC1; NbExp=3; IntAct=EBI-739467, EBI-2807146;
CC Q9H8Y8; Q14232: EIF2B1; NbExp=8; IntAct=EBI-739467, EBI-491065;
CC Q9H8Y8; Q9NT22: EMILIN3; NbExp=5; IntAct=EBI-739467, EBI-3197883;
CC Q9H8Y8; Q8TC92: ENOX1; NbExp=3; IntAct=EBI-739467, EBI-713221;
CC Q9H8Y8; O95571: ETHE1; NbExp=3; IntAct=EBI-739467, EBI-715318;
CC Q9H8Y8; Q9NYK6-3: EURL; NbExp=5; IntAct=EBI-739467, EBI-13371226;
CC Q9H8Y8; Q92562: FIG4; NbExp=3; IntAct=EBI-739467, EBI-4290773;
CC Q9H8Y8; Q8TAK5: GABPB2; NbExp=6; IntAct=EBI-739467, EBI-8468945;
CC Q9H8Y8; O60262: GNG7; NbExp=6; IntAct=EBI-739467, EBI-717760;
CC Q9H8Y8; P63211: GNGT1; NbExp=5; IntAct=EBI-739467, EBI-10220715;
CC Q9H8Y8; Q08379: GOLGA2; NbExp=7; IntAct=EBI-739467, EBI-618309;
CC Q9H8Y8; Q8N9W4-2: GOLGA6L2; NbExp=3; IntAct=EBI-739467, EBI-10268729;
CC Q9H8Y8; O43708: GSTZ1; NbExp=3; IntAct=EBI-739467, EBI-748043;
CC Q9H8Y8; Q9UHL9: GTF2IRD1; NbExp=3; IntAct=EBI-739467, EBI-372530;
CC Q9H8Y8; Q00444: HOXC5; NbExp=3; IntAct=EBI-739467, EBI-11955357;
CC Q9H8Y8; O75506: HSBP1; NbExp=3; IntAct=EBI-739467, EBI-748664;
CC Q9H8Y8; Q9Y547: IFT25; NbExp=3; IntAct=EBI-739467, EBI-747101;
CC Q9H8Y8; Q9NQC1-2: JADE2; NbExp=3; IntAct=EBI-739467, EBI-10311936;
CC Q9H8Y8; Q8WZ19: KCTD13; NbExp=3; IntAct=EBI-739467, EBI-742916;
CC Q9H8Y8; Q96MP8-2: KCTD7; NbExp=5; IntAct=EBI-739467, EBI-11954971;
CC Q9H8Y8; Q7L273: KCTD9; NbExp=7; IntAct=EBI-739467, EBI-4397613;
CC Q9H8Y8; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-739467, EBI-2125614;
CC Q9H8Y8; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-739467, EBI-14069005;
CC Q9H8Y8; Q6L8G4: KRTAP5-11; NbExp=5; IntAct=EBI-739467, EBI-11993296;
CC Q9H8Y8; Q17RB8: LONRF1; NbExp=10; IntAct=EBI-739467, EBI-2341787;
CC Q9H8Y8; Q9GZQ8: MAP1LC3B; NbExp=6; IntAct=EBI-739467, EBI-373144;
CC Q9H8Y8; O95460-2: MATN4; NbExp=3; IntAct=EBI-739467, EBI-12072296;
CC Q9H8Y8; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-739467, EBI-10172526;
CC Q9H8Y8; Q9BRT3: MIEN1; NbExp=3; IntAct=EBI-739467, EBI-6137472;
CC Q9H8Y8; Q502X0: MORN2; NbExp=3; IntAct=EBI-739467, EBI-725982;
CC Q9H8Y8; Q8TAP9: MPLKIP; NbExp=5; IntAct=EBI-739467, EBI-11603426;
CC Q9H8Y8; O60682: MSC; NbExp=5; IntAct=EBI-739467, EBI-740310;
CC Q9H8Y8; Q5VTT5-2: MYOM3; NbExp=3; IntAct=EBI-739467, EBI-12247808;
CC Q9H8Y8; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-739467, EBI-2859639;
CC Q9H8Y8; Q9HAN9: NMNAT1; NbExp=3; IntAct=EBI-739467, EBI-3917542;
CC Q9H8Y8; P16083: NQO2; NbExp=5; IntAct=EBI-739467, EBI-358466;
CC Q9H8Y8; Q9UKK9: NUDT5; NbExp=3; IntAct=EBI-739467, EBI-721623;
CC Q9H8Y8; P11926: ODC1; NbExp=11; IntAct=EBI-739467, EBI-1044287;
CC Q9H8Y8; P61457: PCBD1; NbExp=6; IntAct=EBI-739467, EBI-740475;
CC Q9H8Y8; O76083: PDE9A; NbExp=4; IntAct=EBI-739467, EBI-742764;
CC Q9H8Y8; Q96PV4: PNMA5; NbExp=7; IntAct=EBI-739467, EBI-10171633;
CC Q9H8Y8; P30048: PRDX3; NbExp=6; IntAct=EBI-739467, EBI-748336;
CC Q9H8Y8; O43741: PRKAB2; NbExp=3; IntAct=EBI-739467, EBI-1053424;
CC Q9H8Y8; P60891: PRPS1; NbExp=6; IntAct=EBI-739467, EBI-749195;
CC Q9H8Y8; P25788: PSMA3; NbExp=3; IntAct=EBI-739467, EBI-348380;
CC Q9H8Y8; Q13200: PSMD2; NbExp=3; IntAct=EBI-739467, EBI-357648;
CC Q9H8Y8; Q15008: PSMD6; NbExp=5; IntAct=EBI-739467, EBI-359701;
CC Q9H8Y8; O00194: RAB27B; NbExp=3; IntAct=EBI-739467, EBI-10179046;
CC Q9H8Y8; Q14964: RAB39A; NbExp=3; IntAct=EBI-739467, EBI-3048577;
CC Q9H8Y8; Q8TBY0: RBM46; NbExp=3; IntAct=EBI-739467, EBI-12068216;
CC Q9H8Y8; O15211: RGL2; NbExp=3; IntAct=EBI-739467, EBI-712355;
CC Q9H8Y8; P49796-8: RGS3; NbExp=3; IntAct=EBI-739467, EBI-10211517;
CC Q9H8Y8; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-739467, EBI-17589229;
CC Q9H8Y8; P49247: RPIA; NbExp=8; IntAct=EBI-739467, EBI-744831;
CC Q9H8Y8; P57086: SCAND1; NbExp=6; IntAct=EBI-739467, EBI-745846;
CC Q9H8Y8; Q8WYJ6: SEPTIN1; NbExp=3; IntAct=EBI-739467, EBI-693002;
CC Q9H8Y8; Q6ZU15: SEPTIN14; NbExp=3; IntAct=EBI-739467, EBI-2009297;
CC Q9H8Y8; P34896: SHMT1; NbExp=3; IntAct=EBI-739467, EBI-715117;
CC Q9H8Y8; Q16560-2: SNRNP35; NbExp=3; IntAct=EBI-739467, EBI-12938570;
CC Q9H8Y8; Q6ZVD7: STOX1; NbExp=4; IntAct=EBI-739467, EBI-3923644;
CC Q9H8Y8; Q01995: TAGLN; NbExp=6; IntAct=EBI-739467, EBI-1054248;
CC Q9H8Y8; P15884: TCF4; NbExp=4; IntAct=EBI-739467, EBI-533224;
CC Q9H8Y8; Q9BXF9: TEKT3; NbExp=4; IntAct=EBI-739467, EBI-8644516;
CC Q9H8Y8; Q08117: TLE5; NbExp=4; IntAct=EBI-739467, EBI-717810;
CC Q9H8Y8; Q08117-2: TLE5; NbExp=3; IntAct=EBI-739467, EBI-11741437;
CC Q9H8Y8; Q96S44: TP53RK; NbExp=3; IntAct=EBI-739467, EBI-739588;
CC Q9H8Y8; P17752: TPH1; NbExp=5; IntAct=EBI-739467, EBI-3956833;
CC Q9H8Y8; Q13077: TRAF1; NbExp=7; IntAct=EBI-739467, EBI-359224;
CC Q9H8Y8; Q12933: TRAF2; NbExp=8; IntAct=EBI-739467, EBI-355744;
CC Q9H8Y8; Q9BUZ4: TRAF4; NbExp=4; IntAct=EBI-739467, EBI-3650647;
CC Q9H8Y8; O00463: TRAF5; NbExp=3; IntAct=EBI-739467, EBI-523498;
CC Q9H8Y8; O75865-2: TRAPPC6A; NbExp=5; IntAct=EBI-739467, EBI-8451480;
CC Q9H8Y8; O00635: TRIM38; NbExp=6; IntAct=EBI-739467, EBI-2130415;
CC Q9H8Y8; Q86TN4-2: TRPT1; NbExp=3; IntAct=EBI-739467, EBI-12403619;
CC Q9H8Y8; Q15714-2: TSC22D1; NbExp=8; IntAct=EBI-739467, EBI-12034704;
CC Q9H8Y8; Q8WW01: TSEN15; NbExp=3; IntAct=EBI-739467, EBI-372432;
CC Q9H8Y8; Q15631: TSN; NbExp=6; IntAct=EBI-739467, EBI-1044160;
CC Q9H8Y8; Q6DKK2: TTC19; NbExp=5; IntAct=EBI-739467, EBI-948354;
CC Q9H8Y8; P40222: TXLNA; NbExp=7; IntAct=EBI-739467, EBI-359793;
CC Q9H8Y8; Q9H832: UBE2Z; NbExp=3; IntAct=EBI-739467, EBI-720977;
CC Q9H8Y8; O95164: UBL3; NbExp=3; IntAct=EBI-739467, EBI-12876508;
CC Q9H8Y8; Q9H9H4: VPS37B; NbExp=3; IntAct=EBI-739467, EBI-4400866;
CC Q9H8Y8; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-739467, EBI-2799833;
CC Q9H8Y8; Q9NQW7-3: XPNPEP1; NbExp=3; IntAct=EBI-739467, EBI-12079490;
CC Q9H8Y8; O96006: ZBED1; NbExp=3; IntAct=EBI-739467, EBI-740037;
CC Q9H8Y8; O43829: ZBTB14; NbExp=4; IntAct=EBI-739467, EBI-10176632;
CC Q9H8Y8; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-739467, EBI-746595;
CC Q9H8Y8; Q9UQR1: ZNF148; NbExp=3; IntAct=EBI-739467, EBI-2688184;
CC Q9H8Y8; Q9UQR1-2: ZNF148; NbExp=5; IntAct=EBI-739467, EBI-11742222;
CC Q9H8Y8; PRO_0000045603 [Q99IB8]; Xeno; NbExp=3; IntAct=EBI-739467, EBI-6927928;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:10487747, ECO:0000269|PubMed:11101516,
CC ECO:0000269|PubMed:27062250}; Lipid-anchor
CC {ECO:0000269|PubMed:11101516}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:27062250}. Golgi apparatus
CC {ECO:0000269|PubMed:28067262}. Note=Detected in the intermediate Golgi,
CC membrane-associated (By similarity). ER stress triggers its
CC relocalization from Golgi to ER membrane (PubMed:27062250,
CC PubMed:28067262). {ECO:0000250|UniProtKB:Q9R064,
CC ECO:0000269|PubMed:27062250, ECO:0000269|PubMed:28067262}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H8Y8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H8Y8-2; Sequence=VSP_011300;
CC Name=3;
CC IsoId=Q9H8Y8-3; Sequence=VSP_054364;
CC -!- PTM: Myristoylated (PubMed:11101516). Myristoylation is essential for
CC the Golgi targeting (By similarity). {ECO:0000250|UniProtKB:Q9R064,
CC ECO:0000269|PubMed:11101516}.
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:11101516}.
CC -!- PTM: Phosphorylated in mitotic cells (PubMed:11408587). ER stress-
CC induced phosphorylation at Ser-441 induces monomerization and
CC subsequent relocalization from Golgi to ER which is essential for
CC mediating unconventional (ER/Golgi-independent) trafficking of CFTR to
CC the cell membrane (PubMed:21884936, PubMed:27062250).
CC {ECO:0000269|PubMed:11408587, ECO:0000269|PubMed:21884936,
CC ECO:0000269|PubMed:27062250}.
CC -!- SIMILARITY: Belongs to the GORASP family. {ECO:0000305}.
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DR EMBL; AK027349; BAB55054.1; -; mRNA.
DR EMBL; AK023082; BAB14395.1; -; mRNA.
DR EMBL; AK023201; BAB14459.1; -; mRNA.
DR EMBL; AK296698; BAG59292.1; -; mRNA.
DR EMBL; AL117430; CAB55919.1; -; mRNA.
DR EMBL; AC010092; AAY15076.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11227.1; -; Genomic_DNA.
DR EMBL; BC007770; AAH07770.1; -; mRNA.
DR CCDS; CCDS33325.1; -. [Q9H8Y8-1]
DR PIR; T17229; T17229.
DR RefSeq; NP_001188357.1; NM_001201428.1. [Q9H8Y8-2]
DR RefSeq; NP_056345.3; NM_015530.4. [Q9H8Y8-1]
DR RefSeq; XP_006712471.1; XM_006712408.2.
DR PDB; 3RLE; X-ray; 1.65 A; A=2-208.
DR PDB; 4EDJ; X-ray; 1.90 A; A/B=1-208.
DR PDBsum; 3RLE; -.
DR PDBsum; 4EDJ; -.
DR AlphaFoldDB; Q9H8Y8; -.
DR SMR; Q9H8Y8; -.
DR BioGRID; 117479; 386.
DR ComplexPortal; CPX-6092; GRASP55-GM45 Golgi stacking complex.
DR IntAct; Q9H8Y8; 198.
DR MINT; Q9H8Y8; -.
DR STRING; 9606.ENSP00000234160; -.
DR GlyCosmos; Q9H8Y8; 9 sites, 1 glycan.
DR GlyGen; Q9H8Y8; 10 sites, 1 O-linked glycan (10 sites).
DR iPTMnet; Q9H8Y8; -.
DR MetOSite; Q9H8Y8; -.
DR PhosphoSitePlus; Q9H8Y8; -.
DR SwissPalm; Q9H8Y8; -.
DR BioMuta; GORASP2; -.
DR DMDM; 51316097; -.
DR EPD; Q9H8Y8; -.
DR jPOST; Q9H8Y8; -.
DR MassIVE; Q9H8Y8; -.
DR MaxQB; Q9H8Y8; -.
DR PaxDb; 9606-ENSP00000234160; -.
DR PeptideAtlas; Q9H8Y8; -.
DR ProteomicsDB; 4483; -.
DR ProteomicsDB; 81257; -. [Q9H8Y8-1]
DR ProteomicsDB; 81258; -. [Q9H8Y8-2]
DR Pumba; Q9H8Y8; -.
DR Antibodypedia; 33839; 340 antibodies from 31 providers.
DR DNASU; 26003; -.
DR Ensembl; ENST00000234160.5; ENSP00000234160.4; ENSG00000115806.13. [Q9H8Y8-1]
DR GeneID; 26003; -.
DR KEGG; hsa:26003; -.
DR MANE-Select; ENST00000234160.5; ENSP00000234160.4; NM_015530.5; NP_056345.3.
DR UCSC; uc002ugk.4; human. [Q9H8Y8-1]
DR AGR; HGNC:17500; -.
DR CTD; 26003; -.
DR DisGeNET; 26003; -.
DR GeneCards; GORASP2; -.
DR HGNC; HGNC:17500; GORASP2.
DR HPA; ENSG00000115806; Low tissue specificity.
DR MIM; 608693; gene.
DR neXtProt; NX_Q9H8Y8; -.
DR OpenTargets; ENSG00000115806; -.
DR PharmGKB; PA38457; -.
DR VEuPathDB; HostDB:ENSG00000115806; -.
DR eggNOG; KOG3834; Eukaryota.
DR GeneTree; ENSGT00390000008686; -.
DR HOGENOM; CLU_025095_5_0_1; -.
DR InParanoid; Q9H8Y8; -.
DR OMA; HIVPEIV; -.
DR OrthoDB; 36330at2759; -.
DR PhylomeDB; Q9H8Y8; -.
DR TreeFam; TF314053; -.
DR PathwayCommons; Q9H8Y8; -.
DR Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR SignaLink; Q9H8Y8; -.
DR SIGNOR; Q9H8Y8; -.
DR BioGRID-ORCS; 26003; 13 hits in 1168 CRISPR screens.
DR ChiTaRS; GORASP2; human.
DR EvolutionaryTrace; Q9H8Y8; -.
DR GeneWiki; GORASP2; -.
DR GenomeRNAi; 26003; -.
DR Pharos; Q9H8Y8; Tbio.
DR PRO; PR:Q9H8Y8; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H8Y8; Protein.
DR Bgee; ENSG00000115806; Expressed in sperm and 214 other cell types or tissues.
DR ExpressionAtlas; Q9H8Y8; baseline and differential.
DR Genevisible; Q9H8Y8; HS.
DR GO; GO:0005801; C:cis-Golgi network; NAS:ComplexPortal.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; TAS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0061951; P:establishment of protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0070925; P:organelle assembly; IMP:UniProtKB.
DR GO; GO:0006996; P:organelle organization; IMP:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd00136; PDZ; 1.
DR DisProt; DP02592; -.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR007583; GRASP55_65.
DR InterPro; IPR024958; GRASP_PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR12893; GOLGI REASSEMBLY STACKING PROTEIN GRASP; 1.
DR PANTHER; PTHR12893:SF1; GOLGI REASSEMBLY-STACKING PROTEIN 2; 1.
DR Pfam; PF04495; GRASP55_65; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR PROSITE; PS51865; PDZ_GRASP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Differentiation;
KW Direct protein sequencing; Endoplasmic reticulum; Golgi apparatus;
KW Lipoprotein; Membrane; Methylation; Myristate; Palmitate; Phosphoprotein;
KW Reference proteome; Repeat; Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:25807930"
FT CHAIN 2..452
FT /note="Golgi reassembly-stacking protein 2"
FT /id="PRO_0000087545"
FT DOMAIN 15..105
FT /note="PDZ GRASP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01212"
FT DOMAIN 111..199
FT /note="PDZ GRASP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01212"
FT REGION 15..215
FT /note="GRASP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01214"
FT REGION 194..199
FT /note="Important for membrane binding"
FT REGION 372..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q9R064"
FT MOD_RES 47
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q9R064"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 222
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 225
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11408587,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99JX3"
FT MOD_RES 415
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 433
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21884936,
FT ECO:0000269|PubMed:27062250"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27062250,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27062250,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:25807930, ECO:0000269|PubMed:27062250,
FT ECO:0000305|PubMed:11101516"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_011300"
FT VAR_SEQ 1..21
FT /note="MGSSQSVEIPGGGTEGYHVLR -> MREGSSTLSEIRKLKPGIMVCTCNPSY
FT SNQETE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054364"
FT VARIANT 432
FT /note="S -> F (in dbSNP:rs3770436)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_051013"
FT MUTAGEN 2
FT /note="G->A: Abolishes myristoylation. Loss of its ability
FT to mediate unconventional (ER/Golgi-independent)
FT trafficking of CFTR to the cell membrane. No effect on ER
FT stress-induced relocalization from Golgi to ER."
FT /evidence="ECO:0000269|PubMed:21884936,
FT ECO:0000269|PubMed:27062250"
FT MUTAGEN 59
FT /note="L->A: Abolishes organelle clustering; when
FT associated with S-100."
FT /evidence="ECO:0000269|PubMed:21515684"
FT MUTAGEN 100
FT /note="I->S: Abolishes organelle clustering; when
FT associated with A-59."
FT /evidence="ECO:0000269|PubMed:21515684"
FT MUTAGEN 148
FT /note="D->N: Enhances homodimerization. Loss of ER stress-
FT induced relocalization from Golgi to ER."
FT /evidence="ECO:0000269|PubMed:27062250"
FT MUTAGEN 189
FT /note="S->D: Phosphomimetic mutation that decreases the
FT ability to promote organelle clustering."
FT /evidence="ECO:0000269|PubMed:22523075"
FT MUTAGEN 222
FT /note="T->A: Abolishes mitotic phosphorylation; when
FT associated with A-225."
FT /evidence="ECO:0000269|PubMed:11408587"
FT MUTAGEN 225
FT /note="T->A: Abolishes mitotic phosphorylation; when
FT associated with A-222."
FT /evidence="ECO:0000269|PubMed:11408587"
FT MUTAGEN 441
FT /note="S->A: Loss of phosphorylation and its ability to
FT mediate unconventional (ER/Golgi-independent) trafficking
FT of CFTR to the cell membrane. Inhibits ER stress-mediated
FT disruption of homodimerization. Loss of ER stress-induced
FT relocalization from Golgi to ER."
FT /evidence="ECO:0000269|PubMed:21884936,
FT ECO:0000269|PubMed:27062250"
FT MUTAGEN 441
FT /note="S->D: Phosphomimetic mutant. No loss of its ability
FT to mediate unconventional (ER/Golgi-independent)
FT trafficking of CFTR to the cell membrane. Disrupts
FT homodimerization. No loss of ER stress-induced
FT relocalization from Golgi to ER."
FT /evidence="ECO:0000269|PubMed:21884936,
FT ECO:0000269|PubMed:27062250"
FT MUTAGEN 449
FT /note="S->A: Loss of phosphorylation. Does not inhibit ER
FT stress-mediated disruption of homodimerization."
FT /evidence="ECO:0000269|PubMed:27062250"
FT MUTAGEN 449
FT /note="S->D: Phosphomimetic mutant. No disruption of
FT homodimerization."
FT /evidence="ECO:0000269|PubMed:27062250"
FT MUTAGEN 451
FT /note="S->A: Loss of phosphorylation. Does not inhibit ER
FT stress-mediated disruption of homodimerization."
FT /evidence="ECO:0000269|PubMed:27062250"
FT MUTAGEN 451
FT /note="S->D: Phosphomimetic mutant. Partial disruption of
FT homodimerization."
FT /evidence="ECO:0000269|PubMed:27062250"
FT CONFLICT 20
FT /note="L -> Q (in Ref. 3; BAB14459)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="E -> G (in Ref. 3; BAB14395)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="S -> P (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="A -> T (in Ref. 3; BAB14395)"
FT /evidence="ECO:0000305"
FT STRAND 12..22
FT /evidence="ECO:0007829|PDB:3RLE"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:3RLE"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:3RLE"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:3RLE"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:3RLE"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:3RLE"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:3RLE"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:3RLE"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:3RLE"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:3RLE"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:3RLE"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:3RLE"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:3RLE"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:3RLE"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:3RLE"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:3RLE"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:3RLE"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3RLE"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:3RLE"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:3RLE"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:3RLE"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:3RLE"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:3RLE"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:3RLE"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:3RLE"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3RLE"
SQ SEQUENCE 452 AA; 47145 MW; 326EA6C107D2EA8B CRC64;
MGSSQSVEIP GGGTEGYHVL RVQENSPGHR AGLEPFFDFI VSINGSRLNK DNDTLKDLLK
ANVEKPVKML IYSSKTLELR ETSVTPSNLW GGQGLLGVSI RFCSFDGANE NVWHVLEVES
NSPAALAGLR PHSDYIIGAD TVMNESEDLF SLIETHEAKP LKLYVYNTDT DNCREVIITP
NSAWGGEGSL GCGIGYGYLH RIPTRPFEEG KKISLPGQMA GTPITPLKDG FTEVQLSSVN
PPSLSPPGTT GIEQSLTGLS ISSTPPAVSS VLSTGVPTVP LLPPQVNQSL TSVPPMNPAT
TLPGLMPLPA GLPNLPNLNL NLPAPHIMPG VGLPELVNPG LPPLPSMPPR NLPGIAPLPL
PSEFLPSFPL VPESSSAASS GELLSSLPPT SNAPSDPATT TAKADAASSL TVDVTPPTAK
APTTVEDRVG DSTPVSEKPV SAAVDANASE SP
//
