GOGA2_RAT
ID GOGA2_RAT Reviewed; 998 AA.
AC Q62839; F1LSS0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 4.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Golgin subfamily A member 2 {ECO:0000305};
DE AltName: Full=130 kDa cis-Golgi matrix protein {ECO:0000303|PubMed:8557739};
DE Short=GM130 {ECO:0000303|PubMed:8557739};
GN Name=Golga2 {ECO:0000312|RGD:620282};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=Sprague-Dawley;
RX PubMed=8557739; DOI=10.1083/jcb.131.6.1715;
RA Nakamura N., Rabouille C., Watson R., Nilsson T., Hui N., Slusarewicz P.,
RA Kreis T.E., Warren G.;
RT "Characterization of a cis-Golgi matrix protein, GM130.";
RL J. Cell Biol. 131:1715-1726(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP SEQUENCE REVISION, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH USO1,
RP AND PHOSPHORYLATION.
RC STRAIN=Sprague-Dawley;
RX PubMed=9150144; DOI=10.1016/s0092-8674(00)80225-1;
RA Nakamura N., Lowe M., Levine T.P., Rabouille C., Warren G.;
RT "The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein,
RT in a mitotically regulated manner.";
RL Cell 89:445-455(1997).
RN [4]
RP PROTEIN SEQUENCE OF 175-184 AND 199-207, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH GORASP1.
RX PubMed=9346242; DOI=10.1016/s0092-8674(00)80407-9;
RA Barr F.A., Puype M., Vandekerckhove J., Warren G.;
RT "GRASP65, a protein involved in the stacking of Golgi cisternae.";
RL Cell 91:253-262(1997).
RN [6]
RP FUNCTION, PHOSPHORYLATION AT SER-37, INTERACTION WITH USO1, AND MUTAGENESIS
RP OF SER-37; SER-55 AND SER-94.
RX PubMed=9753325; DOI=10.1016/s0092-8674(00)81737-7;
RA Lowe M., Rabouille C., Nakamura N., Watson R., Jackman M., Jamsa E.,
RA Rahman D., Pappin D.J.C., Warren G.;
RT "Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and
RT is required for Golgi fragmentation in mitosis.";
RL Cell 94:783-793(1998).
RN [7]
RP INTERACTION WITH GORASP1, AND MUTAGENESIS OF ASP-988; GLU-989; ASN-990;
RP ASP-991; GLU-992; VAL-993; LYS-994; ILE-995; MET-996; VAL-997 AND ILE-998.
RX PubMed=9628863; DOI=10.1093/emboj/17.12.3258;
RA Barr F.A., Nakamura N., Warren G.;
RT "Mapping the interaction between GRASP65 and GM130, components of a protein
RT complex involved in the stacking of Golgi cisternae.";
RL EMBO J. 17:3258-3268(1998).
RN [8]
RP INTERACTION WITH USO1.
RX PubMed=10744704; DOI=10.1074/jbc.275.14.10196;
RA Linstedt A.D., Jesch S.A., Mehta A., Lee T.H., Garcia-Mata R., Nelson D.S.,
RA Sztul E.;
RT "Binding relationships of membrane tethering components. The giantin N
RT terminus and the GM130 N terminus compete for binding to the p115 C
RT terminus.";
RL J. Biol. Chem. 275:10196-10201(2000).
RN [9]
RP SUBCELLULAR LOCATION, INTERACTION WITH USO1, AND PHOSPHORYLATION AT SER-37.
RX PubMed=10769027; DOI=10.1083/jcb.149.2.341;
RA Lowe M., Gonatas N.K., Warren G.;
RT "The mitotic phosphorylation cycle of the cis-Golgi matrix protein GM130.";
RL J. Cell Biol. 149:341-356(2000).
RN [10]
RP FUNCTION.
RX PubMed=10679020; DOI=10.1091/mbc.11.2.635;
RA Seemann J., Jokitalo E.J., Warren G.;
RT "The role of the tethering proteins p115 and GM130 in transport through the
RT Golgi apparatus in vivo.";
RL Mol. Biol. Cell 11:635-645(2000).
RN [11]
RP FUNCTION.
RX PubMed=11035033; DOI=10.1074/jbc.m007957200;
RA Alvarez C., Garcia-Mata R., Hauri H.P., Sztul E.;
RT "The p115-interactive proteins GM130 and giantin participate in endoplasmic
RT reticulum-Golgi traffic.";
RL J. Biol. Chem. 276:2693-2700(2001).
RN [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GORASP1.
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 [13]
RP SUBCELLULAR LOCATION.
RX PubMed=14742712; DOI=10.1091/mbc.e03-08-0625;
RA Volchuk A., Ravazzola M., Perrelet A., Eng W.S., Di Liberto M.,
RA Varlamov O., Fukasawa M., Engel T., Sollner T.H., Rothman J.E., Orci L.;
RT "Countercurrent distribution of two distinct SNARE complexes mediating
RT transport within the Golgi stack.";
RL Mol. Biol. Cell 15:1506-1518(2004).
RN [14]
RP FUNCTION, AND INTERACTION WITH STX5; USO1 AND RAB1B.
RX PubMed=18167358; DOI=10.1074/jbc.m708401200;
RA Diao A., Frost L., Morohashi Y., Lowe M.;
RT "Coordination of golgin tethering and SNARE assembly: GM130 binds syntaxin
RT 5 in a p115-regulated manner.";
RL J. Biol. Chem. 283:6957-6967(2008).
RN [15]
RP PHOSPHORYLATION AT SER-37.
RX PubMed=20699666; DOI=10.4161/cc.9.15.12522;
RA Sundaramoorthy S., Goh J.B., Rafee S., Murata-Hori M.;
RT "Mitotic Golgi vesiculation involves mechanisms independent of Ser25
RT phosphorylation of GM130.";
RL Cell Cycle 9:3100-3105(2010).
RN [16]
RP REVIEW.
RX PubMed=20197635; DOI=10.1254/jphs.09r03cr;
RA Nakamura N.;
RT "Emerging new roles of GM130, a cis-Golgi matrix protein, in higher order
RT cell functions.";
RL J. Pharmacol. Sci. 112:255-264(2010).
RN [17]
RP SUBUNIT, INTERACTION WITH GORASP1, DOMAIN, AND ELECTRON MICROSCOPY OF
RP COILED COIL DOMAIN.
RX PubMed=25787021; DOI=10.1111/febs.13271;
RA Ishida R., Yamamoto A., Nakayama K., Sohda M., Misumi Y., Yasunaga T.,
RA Nakamura N.;
RT "GM130 is a parallel tetramer with a flexible rod-like structure and N-
RT terminally open (Y-shaped) and closed (I-shaped) conformations.";
RL FEBS J. 282:2232-2244(2015).
RN [18]
RP FUNCTION.
RX PubMed=26165940; DOI=10.1016/j.cell.2015.06.014;
RA Wei J.H., Zhang Z.C., Wynn R.M., Seemann J.;
RT "GM130 regulates Golgi-derived spindle assembly by activating TPX2 and
RT capturing microtubules.";
RL Cell 162:287-299(2015).
CC -!- FUNCTION: Peripheral membrane component of the cis-Golgi stack that
CC acts as a membrane skeleton that maintains the structure of the Golgi
CC apparatus, and as a vesicle thether that facilitates vesicle fusion to
CC the Golgi membrane (PubMed:9150144, PubMed:20197635). Required for
CC normal protein transport from the endoplasmic reticulum to the Golgi
CC apparatus and the cell membrane (By similarity). Together with
CC p115/USO1 and STX5, involved in vesicle tethering and fusion at the
CC cis-Golgi membrane to maintain the stacked and inter-connected
CC structure of the Golgi apparatus (PubMed:10679020, PubMed:11035033,
CC PubMed:18167358). Plays a central role in mitotic Golgi disassembly:
CC phosphorylation at Ser-37 by CDK1 at the onset of mitosis inhibits the
CC interaction with p115/USO1, preventing tethering of COPI vesicles and
CC thereby inhibiting transport through the Golgi apparatus during mitosis
CC (PubMed:9753325). Also plays a key role in spindle pole assembly and
CC centrosome organization (PubMed:26165940). Promotes the mitotic spindle
CC pole assembly by activating the spindle assembly factor TPX2 to
CC nucleate microtubules around the Golgi and capture them to couple
CC mitotic membranes to the spindle: upon phosphorylation at the onset of
CC mitosis, GOLGA2 interacts with importin-alpha via the nuclear
CC localization signal region, leading to recruit importin-alpha to the
CC Golgi membranes and liberate the spindle assembly factor TPX2 from
CC importin-alpha. TPX2 then activates AURKA kinase and stimulates local
CC microtubule nucleation. Upon filament assembly, nascent microtubules
CC are further captured by GOLGA2, thus linking Golgi membranes to the
CC spindle (By similarity). Regulates the meiotic spindle pole assembly,
CC probably via the same mechanism (By similarity). Also regulates the
CC centrosome organization (By similarity). Also required for the Golgi
CC ribbon formation and glycosylation of membrane and secretory proteins
CC (By similarity). {ECO:0000250|UniProtKB:Q08379,
CC ECO:0000250|UniProtKB:Q921M4, ECO:0000269|PubMed:10679020,
CC ECO:0000269|PubMed:11035033, ECO:0000269|PubMed:18167358,
CC ECO:0000269|PubMed:26165940, ECO:0000269|PubMed:9150144,
CC ECO:0000269|PubMed:9753325, ECO:0000303|PubMed:20197635}.
CC -!- SUBUNIT: Homodimer, may assemble into homohexamers (By similarity).
CC Homotetramer; forms a parallel homotetramer with a flexible rod-like
CC structure that can give rise to I- and Y-shaped conformations
CC (PubMed:25787021). Interacts with GORASP1/GRASP65 (PubMed:11739401,
CC PubMed:25787021, PubMed:9346242, PubMed:9628863). The homooligomer
CC forms a complex with GORASP1 with a 1:1 stoichiometry
CC (PubMed:25787021). Interacts with RAB1B that has been activated by GTP-
CC binding (PubMed:18167358). Interacts with p115/USO1; interaction with
CC p115/USO1 inhibits interaction with STX5 and/or RAB1B (PubMed:9150144,
CC PubMed:9753325, PubMed:10744704, PubMed:10769027, PubMed:18167358).
CC Interacts with STX5 (PubMed:18167358). Interacts with ZFPL1 (By
CC similarity). Interacts with AKAP450/AKAP9; leading to recruit
CC AKAP450/AKAP9 to the cis-Golgi (By similarity).
CC {ECO:0000250|UniProtKB:Q08379, ECO:0000269|PubMed:10744704,
CC ECO:0000269|PubMed:10769027, ECO:0000269|PubMed:11739401,
CC ECO:0000269|PubMed:18167358, ECO:0000269|PubMed:25787021,
CC ECO:0000269|PubMed:8557739, ECO:0000269|PubMed:9150144,
CC ECO:0000269|PubMed:9346242, ECO:0000269|PubMed:9628863}.
CC -!- INTERACTION:
CC Q62839; O35254: Gorasp1; NbExp=2; IntAct=EBI-618335, EBI-4422879;
CC Q62839; O00506: STK25; Xeno; NbExp=2; IntAct=EBI-618335, EBI-618295;
CC Q62839; Q9DB43: Zfpl1; Xeno; NbExp=14; IntAct=EBI-618335, EBI-7836139;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000269|PubMed:10769027, ECO:0000269|PubMed:11739401,
CC ECO:0000269|PubMed:14742712, ECO:0000269|PubMed:20699666,
CC ECO:0000269|PubMed:8557739, ECO:0000269|PubMed:9150144}; Peripheral
CC membrane protein {ECO:0000269|PubMed:10769027,
CC ECO:0000269|PubMed:14742712, ECO:0000269|PubMed:8557739,
CC ECO:0000269|PubMed:9150144}; Cytoplasmic side
CC {ECO:0000269|PubMed:8557739}. Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000250|UniProtKB:Q08379}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:Q08379}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q08379}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q08379}. Note=Associates with the mitotic
CC spindle during mitosis. {ECO:0000250|UniProtKB:Q08379}.
CC -!- DOMAIN: Extended rod-like protein with long coiled-coil domains.
CC {ECO:0000269|PubMed:25787021}.
CC -!- DOMAIN: The nuclear localization signal (cNLS) mediates interaction
CC with importin-alpha, recruiting importin-alpha to the Golgi membrane
CC and liberating TPX2. {ECO:0000250|UniProtKB:Q08379}.
CC -!- PTM: Phosphorylated at Ser-37 by CDK1 at the onset of mitosis,
CC inhibiting the interaction with p115/USO1 and triggering Golgi
CC disassembly (PubMed:9150144, PubMed:9753325). A report however suggests
CC that Golgi disassembly is independent of phosphorylation at Ser-37
CC (PubMed:20699666). Phosphorylated at Ser-37 in prophase as the Golgi
CC complex starts to break down, and remains phosphorylated during further
CC breakdown and partitioning of the Golgi fragments in metaphase and
CC anaphase. In telophase, GM130 is dephosphorylated by PP2A as the Golgi
CC fragments start to reassemble (PubMed:10769027).
CC {ECO:0000269|PubMed:10769027, ECO:0000269|PubMed:20699666,
CC ECO:0000269|PubMed:9150144, ECO:0000269|PubMed:9753325}.
CC -!- PTM: Cleaved by caspases at the onset of apoptosis.
CC {ECO:0000250|UniProtKB:Q08379}.
CC -!- PTM: Methylation by PRMT5 is required for Golgi ribbon formation.
CC {ECO:0000250|UniProtKB:Q08379}.
CC -!- SIMILARITY: Belongs to the GOLGA2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB53335.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U35022; AAB53335.2; ALT_INIT; mRNA.
DR EMBL; AABR07051438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07051439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T10754; T10754.
DR RefSeq; NP_072118.2; NM_022596.2.
DR RefSeq; XP_006234060.1; XM_006233998.3.
DR AlphaFoldDB; Q62839; -.
DR SMR; Q62839; -.
DR BioGRID; 249112; 2.
DR CORUM; Q62839; -.
DR IntAct; Q62839; 21.
DR MINT; Q62839; -.
DR STRING; 10116.ENSRNOP00000016341; -.
DR iPTMnet; Q62839; -.
DR PhosphoSitePlus; Q62839; -.
DR jPOST; Q62839; -.
DR PaxDb; Q62839; -.
DR PeptideAtlas; Q62839; -.
DR PRIDE; Q62839; -.
DR Ensembl; ENSRNOT00000016341; ENSRNOP00000016341; ENSRNOG00000011884.
DR GeneID; 64528; -.
DR KEGG; rno:64528; -.
DR UCSC; RGD:620282; rat.
DR CTD; 2801; -.
DR RGD; 620282; Golga2.
DR eggNOG; KOG4725; Eukaryota.
DR GeneTree; ENSGT00530000062932; -.
DR InParanoid; Q62839; -.
DR OrthoDB; 358120at2759; -.
DR Reactome; R-RNO-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR PRO; PR:Q62839; -.
DR Proteomes; UP000002494; Chromosome 3.
DR GO; GO:0005801; C:cis-Golgi network; IDA:RGD.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000137; C:Golgi cis cisterna; IDA:RGD.
DR GO; GO:0032580; C:Golgi cisterna membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0061676; F:importin-alpha family protein binding; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0019905; F:syntaxin binding; ISO:RGD.
DR GO; GO:0008356; P:asymmetric cell division; ISS:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:UniProtKB.
DR GO; GO:0090166; P:Golgi disassembly; IDA:UniProtKB.
DR GO; GO:0051645; P:Golgi localization; ISO:RGD.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0090161; P:Golgi ribbon formation; ISS:UniProtKB.
DR GO; GO:0090306; P:meiotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0007020; P:microtubule nucleation; ISS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; ISO:RGD.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:0050772; P:positive regulation of axonogenesis; ISO:RGD.
DR GO; GO:0060050; P:positive regulation of protein glycosylation; ISO:RGD.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0051225; P:spindle assembly; ISS:UniProtKB.
DR InterPro; IPR043937; GM130_C.
DR InterPro; IPR043976; GOLGA_cons_dom.
DR InterPro; IPR024858; Golgin_A.
DR PANTHER; PTHR10881; PTHR10881; 1.
DR Pfam; PF19046; GM130_C; 1.
DR Pfam; PF15070; GOLGA2L5; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Golgi apparatus; Membrane; Methylation;
KW Microtubule; Mitosis; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..998
FT /note="Golgin subfamily A member 2"
FT /id="PRO_0000190056"
FT REGION 1..86
FT /note="Interaction with p115/USO1"
FT /evidence="ECO:0000269|PubMed:9150144"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..998
FT /note="Interaction with GORASP1/GRASP65"
FT /evidence="ECO:0000269|PubMed:9628863"
FT COILED 147..894
FT /evidence="ECO:0000255"
FT MOTIF 26..49
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q08379"
FT COMPBIAS 57..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q08379"
FT MOD_RES 30
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q08379"
FT MOD_RES 37
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:10769027,
FT ECO:0000269|PubMed:20699666, ECO:0000269|PubMed:9753325"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08379"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08379"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08379"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08379"
FT MOD_RES 933
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08379"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08379"
FT MUTAGEN 37
FT /note="S->A: Constitutive interaction with p115/USO1; under
FT mitotic as well as interphase conditions."
FT /evidence="ECO:0000269|PubMed:9753325"
FT MUTAGEN 37
FT /note="S->D: Phosphomimetic mutant that strongly reduces
FT interaction with p115/USO1."
FT /evidence="ECO:0000269|PubMed:9753325"
FT MUTAGEN 55
FT /note="S->A: Does not affect interaction with p115/USO1."
FT /evidence="ECO:0000269|PubMed:9753325"
FT MUTAGEN 94
FT /note="S->A: Does not affect interaction with p115/USO1."
FT /evidence="ECO:0000269|PubMed:9753325"
FT MUTAGEN 988
FT /note="D->A: Does not affect with GORASP1/GRASP65."
FT /evidence="ECO:0000269|PubMed:9628863"
FT MUTAGEN 989
FT /note="E->A: Does not affect with GORASP1/GRASP65."
FT /evidence="ECO:0000269|PubMed:9628863"
FT MUTAGEN 990
FT /note="N->A: Strongly impairs interaction with
FT GORASP1/GRASP65."
FT /evidence="ECO:0000269|PubMed:9628863"
FT MUTAGEN 991
FT /note="D->A: Strongly impairs interaction with
FT GORASP1/GRASP65."
FT /evidence="ECO:0000269|PubMed:9628863"
FT MUTAGEN 992
FT /note="E->A: Does not affect with GORASP1/GRASP65."
FT /evidence="ECO:0000269|PubMed:9628863"
FT MUTAGEN 993
FT /note="V->A: Does not affect with GORASP1/GRASP65."
FT /evidence="ECO:0000269|PubMed:9628863"
FT MUTAGEN 994
FT /note="K->A: Does not affect with GORASP1/GRASP65."
FT /evidence="ECO:0000269|PubMed:9628863"
FT MUTAGEN 995
FT /note="I->A: Strongly impairs interaction with
FT GORASP1/GRASP65."
FT /evidence="ECO:0000269|PubMed:9628863"
FT MUTAGEN 996
FT /note="M->A: Strongly impairs interaction with
FT GORASP1/GRASP65."
FT /evidence="ECO:0000269|PubMed:9628863"
FT MUTAGEN 997
FT /note="V->A: Impairs interaction with GORASP1/GRASP65."
FT /evidence="ECO:0000269|PubMed:9628863"
FT MUTAGEN 998
FT /note="I->A: Impairs interaction with GORASP1/GRASP65."
FT /evidence="ECO:0000269|PubMed:9628863"
FT CONFLICT 112
FT /note="M -> L (in Ref. 1; AAB53335)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="L -> M (in Ref. 1; AAB53335)"
FT /evidence="ECO:0000305"
FT CONFLICT 806
FT /note="N -> S (in Ref. 1; AAB53335)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 998 AA; 112872 MW; 3AA8CBC61F98A6A4 CRC64;
MWPPRFPPPR PGMSEETRQS KLAAAKKKLR EYQQKNSPGV PAGAKKKKKI KNGHSPERTS
ASDCQSAENV PTDHTAPAPP STAAATMFLG VVPSPDADLI QSHDAGNCSN LMEETKTFSS
TESLRQLSQQ LNGLVSESTS YINGEGLTSS NMKELESRYQ ELAVALDSSY VTNKQLSSTI
EELKQQNQDT LDQLEKEKKD YQQKLAKEQG ALREQLQVHI QTIGILVSEK AELQTALAHT
QQAARQKAGE SEDLASRLQS SRQRVGELER TLSTVSTQQK QADRYNKDLT KERDALKLEL
YKNGKSNEDL RQQNSELEEK LRVLVAEKAA AQLGAEELQK KLEMSELLLQ QFSSQSEASG
SNEQLQQAME ERAQLESHVG QLMESLKQLQ VERDQYAENL KGESAMWQQR VQQMAEQVHA
LKEEKEQRES QVQELEASLA ELRSQMEEPP PPEPPTGPSE AEERLQGEVE QLQKELEGLT
GQLRAQVQDN ESLSHLNREQ EGRLLELERE AQHWSEQAEE RKQILESMQS DRTTISRALS
QNRELKEQLA ELQNGFVRLT NENMEITSAL QSEQHVKKEL ARKLGELQER LGELKETVEL
KSQEAQGLQE QRDQCLSHLQ QYAAAYQQHL TAYEQLTSEK EALHKQLLLQ TQLMDQLQHE
EVQGKMAAEM ARQELQEAQE RLKASSQENQ QLQAQLSLLV LPGEDMDQEE QDEEVPQPSL
TIPEDLVSRE AMVAFCNAAI ARAEEEQARL RVQLREQKAR CRSLAHLAAP VQSKLEKEAV
VPRDMGDSVS EESNQALHVA MEKLQNRFLE VMQEKVELKE RVEELEHCCI QLSGETDTIG
EYIALYQNQR AVLKARHLEK EEYISRLAQD KEEMKVKLLE LQELVLRLVN ERNEWQGKFL
AVSQNPADVP APVPTGSQEF GAADQQGDLR EVSLADDTEP AQGEAGVPAP QENPTAQQIM
QLLREIQNPQ ERPGLGSNPC IPFFYRADEN DEVKIMVI
