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Golgi reassembly-stacking protein 2 (GRS2) (Golgi phosphoprotein 6) (GOLPH6) (Golgi reassembly-stacking protein of 55 kDa) (GRASP55) (p59)

 GORS2_HUMAN             Reviewed;         452 AA.
Q9H8Y8; B4DKT0; Q53TE3; Q96I74; Q96K84; Q9H946; Q9UFW4;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 148.
RecName: Full=Golgi reassembly-stacking protein 2;
Short=GRS2;
AltName: Full=Golgi phosphoprotein 6;
Short=GOLPH6;
AltName: Full=Golgi reassembly-stacking protein of 55 kDa;
Short=GRASP55;
AltName: Full=p59;
Name=GORASP2; Synonyms=GOLPH6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 82-97;
134-141; 164-175 AND 203-229, CHARACTERIZATION, MYRISTOYLATION AT
GLY-2, PALMITOYLATION, AND INTERACTION WITH TGFA.
PubMed=11101516; DOI=10.1093/emboj/19.23.6427;
Kuo A., Zhong C., Lane W.S., Derynck R.;
"Transmembrane transforming growth factor-alpha tethers to the PDZ
domain-containing, Golgi membrane-associated protein p59/GRASP55.";
EMBO J. 19:6427-6439(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT THR-225,
AND MUTAGENESIS.
PubMed=11408587; DOI=10.1091/mbc.12.6.1811;
Jesch S.A., Lewis T.S., Ahn N.G., Linstedt A.D.;
"Mitotic phosphorylation of Golgi reassembly stacking protein 55 by
mitogen-activated protein kinase ERK2.";
Mol. Biol. Cell 12:1811-1817(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
PHE-432.
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10487747; DOI=10.1093/emboj/18.18.4949;
Shorter J., Watson R., Giannakou M.-E., Clarke M., Warren G.,
Barr F.A.;
"GRASP55, a second mammalian GRASP protein involved in the stacking of
Golgi cisternae in a cell-free system.";
EMBO J. 18:4949-4960(1999).
[9]
INTERACTION WITH BLZF1/GOLGIN 45.
PubMed=11739401; DOI=10.1083/jcb.200108079;
Short B., Preisinger C., Koerner R., Kopajtich R., Byron O.,
Barr F.A.;
"A GRASP55-rab2 effector complex linking Golgi structure to membrane
traffic.";
J. Cell Biol. 155:877-883(2001).
[10]
INTERACTION WITH PROTEINS OF THE P24 CARGO FAMILY.
PubMed=11739402; DOI=10.1083/jcb.200108102;
Barr F.A., Preisinger C., Kopajtich R., Koerner R.;
"Golgi matrix proteins interact with p24 cargo receptors and aid their
efficient retention in the Golgi apparatus.";
J. Cell Biol. 155:885-891(2001).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-222; THR-225 AND
THR-415, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-415, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[13]
INTERACTION WITH CNIH AND TGFA.
PubMed=17607000; DOI=10.1242/jcs.004200;
Perez Castro C., Piscopo D., Nakagawa T., Derynck R.;
"Cornichon regulates transport and secretion of TGFalpha-related
proteins in metazoan cells.";
J. Cell Sci. 120:2454-2466(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-415; THR-433; SER-436;
SER-449 AND SER-451, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
INTERACTION WITH KCTD5.
PubMed=19361449; DOI=10.1016/j.jmb.2009.01.030;
Dementieva I.S., Tereshko V., McCrossan Z.A., Solomaha E., Araki D.,
Xu C., Grigorieff N., Goldstein S.A.;
"Pentameric assembly of potassium channel tetramerization domain-
containing protein 5.";
J. Mol. Biol. 387:175-191(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; THR-222; THR-225
AND THR-415, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-222; THR-225 AND
SER-451, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; THR-222 AND
THR-225, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25255805; DOI=10.1038/ncomms5919;
Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U.,
Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
"Global profiling of co- and post-translationally N-myristoylated
proteomes in human cells.";
Nat. Commun. 5:4919-4919(2014).
[24]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25807930; DOI=10.1002/anie.201500342;
Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J.,
Magee A.I., Tate E.W.;
"Multifunctional reagents for quantitative proteome-wide analysis of
protein modification in human cells and dynamic profiling of protein
lipidation during vertebrate development.";
Angew. Chem. Int. Ed. 54:5948-5951(2015).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[26]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-208, FUNCTION, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF LEU-59 AND ILE-100.
PubMed=21515684; DOI=10.1074/jbc.C111.245324;
Truschel S.T., Sengupta D., Foote A., Heroux A., Macbeth M.R.,
Linstedt A.D.;
"Structure of the membrane-tethering GRASP domain reveals a unique PDZ
ligand interaction that mediates Golgi biogenesis.";
J. Biol. Chem. 286:20125-20129(2011).
-!- FUNCTION: Plays a role in the assembly and membrane stacking of
the Golgi cisternae, and in the process by which Golgi stacks
reform after mitotic breakdown. May regulate the intracellular
transport and presentation of a defined set of transmembrane
proteins, such as transmembrane TGFA.
{ECO:0000269|PubMed:10487747, ECO:0000269|PubMed:21515684}.
-!- SUBUNIT: Forms a RAB2 effector complex with BLZF1/Golgin 45 in the
medial Golgi. Interacts with members of the p24 cargo receptors.
Interacts with CNIH and the cytoplasmic domain of transmembrane
TGFA, prior its transit in the trans-Golgi. Does not interact with
GM130. Interacts with KCTD5. Interacts with TMED2 and TMED3 (By
similarity). {ECO:0000250}.
-!- INTERACTION:
Q99IB8:- (xeno); NbExp=3; IntAct=EBI-739467, EBI-6927928;
Q9H7C9:AAMDC; NbExp=3; IntAct=EBI-739467, EBI-10308705;
Q96HD9:ACY3; NbExp=10; IntAct=EBI-739467, EBI-3916242;
Q08117:AES; NbExp=3; IntAct=EBI-739467, EBI-717810;
Q15041:ARL6IP1; NbExp=3; IntAct=EBI-739467, EBI-714543;
Q7L4P6:BEND5; NbExp=3; IntAct=EBI-739467, EBI-724373;
Q6P1W5:C1orf94; NbExp=5; IntAct=EBI-739467, EBI-946029;
Q13191:CBLB; NbExp=6; IntAct=EBI-739467, EBI-744027;
Q494R4:CCDC153; NbExp=3; IntAct=EBI-739467, EBI-10241443;
Q9UJX2:CDC23; NbExp=7; IntAct=EBI-739467, EBI-396137;
P13569:CFTR; NbExp=3; IntAct=EBI-739467, EBI-349854;
P02489:CRYAA; NbExp=10; IntAct=EBI-739467, EBI-6875961;
P32321:DCTD; NbExp=5; IntAct=EBI-739467, EBI-739870;
Q14565:DMC1; NbExp=5; IntAct=EBI-739467, EBI-930865;
Q16555:DPYSL2; NbExp=7; IntAct=EBI-739467, EBI-1104711;
Q9H596:DUSP21; NbExp=5; IntAct=EBI-739467, EBI-7357329;
Q14232:EIF2B1; NbExp=5; IntAct=EBI-739467, EBI-491065;
Q8TC92:ENOX1; NbExp=3; IntAct=EBI-739467, EBI-713221;
Q8TAK5:GABPB2; NbExp=5; IntAct=EBI-739467, EBI-8468945;
Q08379:GOLGA2; NbExp=4; IntAct=EBI-739467, EBI-618309;
Q9NQC1-2:JADE2; NbExp=3; IntAct=EBI-739467, EBI-10311936;
Q7L273:KCTD9; NbExp=7; IntAct=EBI-739467, EBI-4397613;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-739467, EBI-2125614;
Q17RB8:LONRF1; NbExp=5; IntAct=EBI-739467, EBI-2341787;
Q9GZQ8:MAP1LC3B; NbExp=5; IntAct=EBI-739467, EBI-373144;
Q9UJV3-2:MID2; NbExp=5; IntAct=EBI-739467, EBI-10172526;
Q502X0:MORN2; NbExp=3; IntAct=EBI-739467, EBI-725982;
P16083:NQO2; NbExp=3; IntAct=EBI-739467, EBI-358466;
P11926:ODC1; NbExp=9; IntAct=EBI-739467, EBI-1044287;
P61457:PCBD1; NbExp=3; IntAct=EBI-739467, EBI-740475;
O76083:PDE9A; NbExp=3; IntAct=EBI-739467, EBI-742764;
Q96PV4:PNMA5; NbExp=5; IntAct=EBI-739467, EBI-10171633;
P30048:PRDX3; NbExp=3; IntAct=EBI-739467, EBI-748336;
P60891:PRPS1; NbExp=3; IntAct=EBI-739467, EBI-749195;
P25788:PSMA3; NbExp=3; IntAct=EBI-739467, EBI-348380;
P49796-8:RGS3; NbExp=3; IntAct=EBI-739467, EBI-10211517;
P49247:RPIA; NbExp=6; IntAct=EBI-739467, EBI-744831;
P57086:SCAND1; NbExp=5; IntAct=EBI-739467, EBI-745846;
Q6ZVD7:STOX1; NbExp=3; IntAct=EBI-739467, EBI-3923644;
P15884:TCF4; NbExp=3; IntAct=EBI-739467, EBI-533224;
Q9BXF9:TEKT3; NbExp=4; IntAct=EBI-739467, EBI-8644516;
P17752:TPH1; NbExp=4; IntAct=EBI-739467, EBI-3956833;
Q13077:TRAF1; NbExp=7; IntAct=EBI-739467, EBI-359224;
Q12933:TRAF2; NbExp=6; IntAct=EBI-739467, EBI-355744;
Q9BUZ4:TRAF4; NbExp=3; IntAct=EBI-739467, EBI-3650647;
O00463:TRAF5; NbExp=3; IntAct=EBI-739467, EBI-523498;
O00635:TRIM38; NbExp=5; IntAct=EBI-739467, EBI-2130415;
Q15714-2:TSC22D1; NbExp=4; IntAct=EBI-739467, EBI-12034704;
P40222:TXLNA; NbExp=5; IntAct=EBI-739467, EBI-359793;
O43829:ZBTB14; NbExp=3; IntAct=EBI-739467, EBI-10176632;
Q9UQR1:ZNF148; NbExp=3; IntAct=EBI-739467, EBI-2688184;
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor.
Membrane; Peripheral membrane protein. Membrane {ECO:0000305};
Lipid-anchor {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9H8Y8-1; Sequence=Displayed;
Name=2;
IsoId=Q9H8Y8-2; Sequence=VSP_011300;
Name=3;
IsoId=Q9H8Y8-3; Sequence=VSP_054364;
Note=No experimental confirmation available.;
-!- PTM: Myristoylated. Myristoylation is essential for the Golgi
targeting (By similarity). {ECO:0000250}.
-!- PTM: Palmitoylated. {ECO:0000269|PubMed:11101516}.
-!- PTM: Phosphorylated in mitotic cells.
{ECO:0000269|PubMed:11408587}.
-!- SIMILARITY: Belongs to the GORASP family. {ECO:0000305}.
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EMBL; AK027349; BAB55054.1; -; mRNA.
EMBL; AK023082; BAB14395.1; -; mRNA.
EMBL; AK023201; BAB14459.1; -; mRNA.
EMBL; AK296698; BAG59292.1; -; mRNA.
EMBL; AL117430; CAB55919.1; -; mRNA.
EMBL; AC010092; AAY15076.1; -; Genomic_DNA.
EMBL; CH471058; EAX11227.1; -; Genomic_DNA.
EMBL; BC007770; AAH07770.1; -; mRNA.
CCDS; CCDS33325.1; -. [Q9H8Y8-1]
PIR; T17229; T17229.
RefSeq; NP_001188357.1; NM_001201428.1. [Q9H8Y8-2]
RefSeq; NP_056345.3; NM_015530.4. [Q9H8Y8-1]
RefSeq; XP_006712471.1; XM_006712408.2. [Q9H8Y8-2]
UniGene; Hs.431317; -.
PDB; 3RLE; X-ray; 1.65 A; A=2-208.
PDB; 4EDJ; X-ray; 1.90 A; A/B=1-208.
PDBsum; 3RLE; -.
PDBsum; 4EDJ; -.
ProteinModelPortal; Q9H8Y8; -.
SMR; Q9H8Y8; -.
BioGrid; 117479; 108.
IntAct; Q9H8Y8; 106.
MINT; MINT-152892; -.
STRING; 9606.ENSP00000234160; -.
iPTMnet; Q9H8Y8; -.
PhosphoSitePlus; Q9H8Y8; -.
SwissPalm; Q9H8Y8; -.
BioMuta; GORASP2; -.
DMDM; 51316097; -.
EPD; Q9H8Y8; -.
MaxQB; Q9H8Y8; -.
PaxDb; Q9H8Y8; -.
PeptideAtlas; Q9H8Y8; -.
PRIDE; Q9H8Y8; -.
DNASU; 26003; -.
Ensembl; ENST00000234160; ENSP00000234160; ENSG00000115806. [Q9H8Y8-1]
GeneID; 26003; -.
KEGG; hsa:26003; -.
UCSC; uc002ugk.4; human. [Q9H8Y8-1]
CTD; 26003; -.
DisGeNET; 26003; -.
GeneCards; GORASP2; -.
HGNC; HGNC:17500; GORASP2.
HPA; HPA035274; -.
HPA; HPA035275; -.
MIM; 608693; gene.
neXtProt; NX_Q9H8Y8; -.
OpenTargets; ENSG00000115806; -.
PharmGKB; PA38457; -.
eggNOG; KOG3834; Eukaryota.
eggNOG; COG5233; LUCA.
GeneTree; ENSGT00390000008686; -.
HOGENOM; HOG000231920; -.
HOVERGEN; HBG051826; -.
InParanoid; Q9H8Y8; -.
OMA; MPSEFLP; -.
OrthoDB; EOG091G0E90; -.
PhylomeDB; Q9H8Y8; -.
TreeFam; TF314053; -.
Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
SIGNOR; Q9H8Y8; -.
ChiTaRS; GORASP2; human.
EvolutionaryTrace; Q9H8Y8; -.
GeneWiki; GORASP2; -.
GenomeRNAi; 26003; -.
PRO; PR:Q9H8Y8; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115806; -.
CleanEx; HS_GORASP2; -.
ExpressionAtlas; Q9H8Y8; baseline and differential.
Genevisible; Q9H8Y8; HS.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016020; C:membrane; TAS:UniProtKB.
GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
GO; GO:0006996; P:organelle organization; IMP:UniProtKB.
InterPro; IPR024958; GRASP55/65_PDZ.
InterPro; IPR007583; GRASP55_65.
InterPro; IPR001478; PDZ.
PANTHER; PTHR12893; PTHR12893; 1.
Pfam; PF04495; GRASP55_65; 1.
SUPFAM; SSF50156; SSF50156; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Golgi apparatus; Lipoprotein; Membrane;
Methylation; Myristate; Palmitate; Phosphoprotein; Polymorphism;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:25255805,
ECO:0000269|PubMed:25807930}.
CHAIN 2 452 Golgi reassembly-stacking protein 2.
/FTId=PRO_0000087545.
DOMAIN 5 75 PDZ.
REGION 194 199 Important for membrane binding.
COMPBIAS 277 372 Pro-rich.
MOD_RES 30 30 Dimethylated arginine; alternate.
{ECO:0000250|UniProtKB:Q9R064}.
MOD_RES 30 30 Omega-N-methylated arginine; alternate.
{ECO:0000250}.
MOD_RES 47 47 Dimethylated arginine; alternate.
{ECO:0000250|UniProtKB:Q9R064}.
MOD_RES 47 47 Omega-N-methylated arginine; alternate.
{ECO:0000250}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 222 222 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 225 225 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:11408587}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000250|UniProtKB:Q99JX3}.
MOD_RES 415 415 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 433 433 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 436 436 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000250|UniProtKB:Q99JX3}.
MOD_RES 449 449 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 451 451 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:25255805,
ECO:0000269|PubMed:25807930,
ECO:0000305|PubMed:11101516}.
VAR_SEQ 1 68 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_011300.
VAR_SEQ 1 21 MGSSQSVEIPGGGTEGYHVLR -> MREGSSTLSEIRKLKP
GIMVCTCNPSYSNQETE (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054364.
VARIANT 432 432 S -> F (in dbSNP:rs3770436).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_051013.
MUTAGEN 59 59 L->A: Abolishes organelle clustering;
when associated with S-100.
{ECO:0000269|PubMed:21515684}.
MUTAGEN 100 100 I->S: Abolishes organelle clustering;
when associated with A-59.
{ECO:0000269|PubMed:21515684}.
MUTAGEN 222 222 T->A: Abolishes mitotic phosphorylation;
when associated with A-225.
{ECO:0000269|PubMed:11408587}.
MUTAGEN 225 225 T->A: Abolishes mitotic phosphorylation;
when associated with A-222.
{ECO:0000269|PubMed:11408587}.
CONFLICT 20 20 L -> Q (in Ref. 3; BAB14459).
{ECO:0000305}.
CONFLICT 34 34 E -> G (in Ref. 3; BAB14395).
{ECO:0000305}.
CONFLICT 83 83 S -> P (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 299 299 A -> T (in Ref. 3; BAB14395).
{ECO:0000305}.
STRAND 12 22 {ECO:0000244|PDB:3RLE}.
HELIX 27 30 {ECO:0000244|PDB:3RLE}.
TURN 35 37 {ECO:0000244|PDB:3RLE}.
STRAND 38 43 {ECO:0000244|PDB:3RLE}.
STRAND 50 53 {ECO:0000244|PDB:3RLE}.
HELIX 54 61 {ECO:0000244|PDB:3RLE}.
TURN 62 64 {ECO:0000244|PDB:3RLE}.
STRAND 67 73 {ECO:0000244|PDB:3RLE}.
TURN 74 76 {ECO:0000244|PDB:3RLE}.
STRAND 79 84 {ECO:0000244|PDB:3RLE}.
STRAND 88 96 {ECO:0000244|PDB:3RLE}.
STRAND 98 104 {ECO:0000244|PDB:3RLE}.
HELIX 108 110 {ECO:0000244|PDB:3RLE}.
STRAND 113 118 {ECO:0000244|PDB:3RLE}.
HELIX 123 127 {ECO:0000244|PDB:3RLE}.
TURN 131 133 {ECO:0000244|PDB:3RLE}.
STRAND 134 141 {ECO:0000244|PDB:3RLE}.
STRAND 145 147 {ECO:0000244|PDB:3RLE}.
HELIX 149 155 {ECO:0000244|PDB:3RLE}.
TURN 156 158 {ECO:0000244|PDB:3RLE}.
STRAND 161 167 {ECO:0000244|PDB:3RLE}.
TURN 168 171 {ECO:0000244|PDB:3RLE}.
STRAND 172 178 {ECO:0000244|PDB:3RLE}.
STRAND 184 190 {ECO:0000244|PDB:3RLE}.
STRAND 192 195 {ECO:0000244|PDB:3RLE}.
HELIX 198 200 {ECO:0000244|PDB:3RLE}.
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


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