GGYF2_HUMAN
ID GGYF2_HUMAN Reviewed; 1299 AA.
AC Q6Y7W6; A6H8W4; B9EG55; E9PBB0; O75137; Q7Z2Z8; Q7Z3I2; Q96HU4; Q9NV82;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=GRB10-interacting GYF protein 2 {ECO:0000303|PubMed:12771153};
DE AltName: Full=PERQ amino acid-rich with GYF domain-containing protein 2;
DE AltName: Full=Trinucleotide repeat-containing gene 15 protein {ECO:0000303|PubMed:18358451};
GN Name=GIGYF2 {ECO:0000303|PubMed:12771153, ECO:0000312|HGNC:HGNC:11960};
GN Synonyms=KIAA0642 {ECO:0000303|PubMed:9734811}, PERQ2,
GN TNRC15 {ECO:0000303|PubMed:18358451};
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), AND FUNCTION.
RC TISSUE=Kidney;
RX PubMed=12771153; DOI=10.1074/jbc.m211572200;
RA Giovannone B., Lee E., Laviola L., Giorgino F., Cleveland K.A., Smith R.J.;
RT "Two novel proteins that are linked to insulin-like growth factor (IGF-I)
RT receptors by the Grb10 adapter and modulate IGF-I signaling.";
RL J. Biol. Chem. 278:31564-31573(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Uterus;
RA Lauber J., Bahr A., Mewes H.W., Weil B., Amid C., Osanger A., Fobo G.,
RA Han M., Wiemann S.;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1096 (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
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 MRNA] (ISOFORM 1), AND VARIANT GLN-1211
RP DEL.
RC TISSUE=Fetal kidney, and Uterus;
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-1211 DEL.
RA Mural R.J., Istrail S., Sutton 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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP GLN-1211 DEL.
RC TISSUE=Lymph, and Testis;
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-30; SER-160; SER-189
RP AND THR-382, 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [17]
RP LACK OF INVOLVEMENT IN PARK11.
RX PubMed=19279319; DOI=10.1212/01.wnl.0000346517.98982.1b;
RG Parkinson Study Group-PROGENI Investigators;
RA Nichols W.C., Kissell D.K., Pankratz N., Pauciulo M.W., Elsaesser V.E.,
RA Clark K.A., Halter C.A., Rudolph A., Wojcieszek J., Pfeiffer R.F.,
RA Foroud T.;
RT "Variation in GIGYF2 is not associated with Parkinson disease.";
RL Neurology 72:1886-1892(2009).
RN [18]
RP LACK OF INVOLVEMENT IN PARK11.
RX PubMed=19482505; DOI=10.1016/j.parkreldis.2009.05.001;
RG Italian Parkinson Genetics Network;
RA Di Fonzo A., Fabrizio E., Thomas A., Fincati E., Marconi R., Tinazzi M.,
RA Breedveld G.J., Simons E.J., Chien H.F., Ferreira J.J., Horstink M.W.,
RA Abbruzzese G., Borroni B., Cossu G., Dalla Libera A., Fabbrini G.,
RA Guidi M., De Mari M., Lopiano L., Martignoni E., Marini P., Onofrj M.,
RA Padovani A., Stocchi F., Toni V., Sampaio C., Barbosa E.R., Meco G.,
RA Oostra B.A., Bonifati V.;
RT "GIGYF2 mutations are not a frequent cause of familial Parkinson's
RT disease.";
RL Parkinsonism Relat. Disord. 15:703-705(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-30; SER-139 AND
RP THR-382, AND 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 [20]
RP LACK OF INVOLVEMENT IN PARK11.
RX PubMed=20004041; DOI=10.1016/j.neurobiolaging.2009.06.008;
RG French Parkinson's Disease Genetics Study Group (FPDGSG);
RA Lesage S., Condroyer C., Lohman E., Troiano A., Tison F., Viallet F.,
RA Damier P., Tranchant C., Vidhaillet M., Ouvrard-Hernandez A.M., Duerr A.,
RA Brice A.;
RT "Follow-up study of the GIGYF2 gene in French families with Parkinson's
RT disease.";
RL Neurobiol. Aging 31:1069-1071(2010).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-236; THR-382 AND
RP SER-593, 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 [22]
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 [23]
RP LACK OF INVOLVEMENT IN PARK11.
RX PubMed=19321232; DOI=10.1016/j.neurobiolaging.2009.02.016;
RA Meeus B., Nuytemans K., Crosiers D., Engelborghs S., Pals P., Pickut B.,
RA Peeters K., Mattheijssens M., Corsmit E., Cras P., De Deyn P.P., Theuns J.,
RA Van Broeckhoven C.;
RT "GIGYF2 has no major role in Parkinson genetic etiology in a Belgian
RT population.";
RL Neurobiol. Aging 32:308-312(2011).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-30; SER-139 AND
RP SER-236, AND 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 [25]
RP FUNCTION, IDENTIFICATION IN THE 4EHP-GYF2 COMPLEX, AND MUTAGENESIS OF
RP 41-TYR--LEU-49.
RX PubMed=22751931; DOI=10.1128/mcb.00455-12;
RA Morita M., Ler L.W., Fabian M.R., Siddiqui N., Mullin M., Henderson V.C.,
RA Alain T., Fonseca B.D., Karashchuk G., Bennett C.F., Kabuta T., Higashi S.,
RA Larsson O., Topisirovic I., Smith R.J., Gingras A.C., Sonenberg N.;
RT "A novel 4EHP-GIGYF2 translational repressor complex is essential for
RT mammalian development.";
RL Mol. Cell. Biol. 32:3585-3593(2012).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-26; SER-30; SER-139;
RP SER-160; SER-189; THR-382; SER-993 AND SER-1284, AND IDENTIFICATION BY MASS
RP 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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-236 AND SER-388, 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 [29]
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 [30]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1123, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [31]
RP FUNCTION, INTERACTION WITH DDX6; EIF4E2 AND TTP, AND MUTAGENESIS OF
RP TRP-288; PHE-300 AND PHE-306.
RX PubMed=31439631; DOI=10.1101/gad.329219.119;
RA Peter D., Ruscica V., Bawankar P., Weber R., Helms S., Valkov E.,
RA Igreja C., Izaurralde E.;
RT "Molecular basis for GIGYF-Me31B complex assembly in 4EHP-mediated
RT translational repression.";
RL Genes Dev. 33:1355-1360(2019).
RN [32]
RP VARIANTS PARK11 ALA-112; VAL-278; THR-335; THR-457; GLU-606 AND ILE-1242,
RP AND VARIANTS SER-56; THR-460; ARG-1171; GLN-1211 DEL AND GLN-1212 INS.
RX PubMed=18358451; DOI=10.1016/j.ajhg.2008.01.015;
RA Lautier C., Goldwurm S., Duerr A., Giovannone B., Tsiaras W.G., Pezzoli G.,
RA Brice A., Smith R.J.;
RT "Mutations in the GIGYF2 (TNRC15) gene at the PARK11 locus in familial
RT Parkinson disease.";
RL Am. J. Hum. Genet. 82:822-833(2008).
RN [33]
RP VARIANT THR-460.
RX PubMed=19429085; DOI=10.1016/j.neulet.2009.03.039;
RA Guo Y., Jankovic J., Zhu S., Le W., Song Z., Xie W., Liao D., Yang H.,
RA Deng H.;
RT "GIGYF2 Asn56Ser and Asn457Thr mutations in Parkinson disease patients.";
RL Neurosci. Lett. 454:209-211(2009).
RN [34]
RP VARIANT SER-56.
RX PubMed=19638301; DOI=10.1016/j.neulet.2009.07.067;
RA Zhang Y., Zheng L., Zhang T., Wang Y., Xiao Q., Fei Q.Z., Cui P.J., Cao L.,
RA Chen S.D.;
RT "GIGYF2 Asn56Ser mutation is rare in Chinese Parkinson's disease
RT patients.";
RL Neurosci. Lett. 463:172-175(2009).
RN [35]
RP VARIANTS PARK11 LYS-256; VAL-345; TYR-377; SER-473; LYS-492; TYR-519;
RP PHE-580; GLN-979 DEL AND HIS-1070.
RX PubMed=20178831; DOI=10.1016/j.neulet.2010.02.037;
RA Wang L., Guo J.F., Zhang W.W., Xu Q., Zuo X., Shi C.H., Luo L.Z., Liu J.,
RA Hu L., Hu Y.C., She L., Jiang H., Yan X.X., Xia K., Pan Q., Tang B.S.;
RT "Novel GIGYF2 gene variants in patients with Parkinson's disease in Chinese
RT population.";
RL Neurosci. Lett. 473:131-135(2010).
RN [36]
RP VARIANTS SER-56; VAL-560; VAL-1131 AND ARG-1171, AND VARIANTS PARK11
RP CYS-273; GLU-349; THR-457 AND PRO-1209.
RX PubMed=20060621; DOI=10.1016/j.neurobiolaging.2009.12.016;
RA Guella I., Pistocchi A., Asselta R., Rimoldi V., Ghilardi A., Sironi F.,
RA Trotta L., Primignani P., Zini M., Zecchinelli A., Coviello D., Pezzoli G.,
RA Del Giacco L., Duga S., Goldwurm S.;
RT "Mutational screening and zebrafish functional analysis of GIGYF2 as a
RT Parkinson-disease gene.";
RL Neurobiol. Aging 32:1994-2005(2011).
RN [37]
RP VARIANT PARK11 GLY-589.
RX PubMed=26134514; DOI=10.1038/jhg.2015.69;
RA Ruiz-Martinez J., Krebs C.E., Makarov V., Gorostidi A., Marti-Masso J.F.,
RA Paisan-Ruiz C.;
RT "GIGYF2 mutation in late-onset Parkinson's disease with cognitive
RT impairment.";
RL J. Hum. Genet. 60:637-640(2015).
CC -!- FUNCTION: Key component of the 4EHP-GYF2 complex, a multiprotein
CC complex that acts as a repressor of translation initiation
CC (PubMed:22751931, PubMed:31439631). In the 4EHP-GYF2 complex, acts as a
CC factor that bridges EIF4E2 to ZFP36/TTP, linking translation repression
CC with mRNA decay (PubMed:31439631). Also recruits and bridges the
CC association of the 4EHP complex with the decapping effector protein
CC DDX6, which is required for the ZFP36/TTP-mediated down-regulation of
CC AU-rich mRNA (PubMed:31439631). May act cooperatively with GRB10 to
CC regulate tyrosine kinase receptor signaling, including IGF1 and insulin
CC receptors (PubMed:12771153). {ECO:0000269|PubMed:12771153,
CC ECO:0000269|PubMed:22751931, ECO:0000269|PubMed:31439631}.
CC -!- SUBUNIT: Component of the 4EHP-GYF2 complex, at least composed of
CC EIF4E2, GIGYF2 and ZNF598 (PubMed:22751931, PubMed:31439631). Interacts
CC (via the 4EHP-binding motif) with EIF4E2; the interaction is direct
CC (PubMed:22751931, PubMed:31439631). Interacts with ZFP36/TTP (via P-P-
CC P-P-G repeats); the interaction is direct (PubMed:31439631). Interacts
CC with GRB10 (By similarity). Interacts (via DDX6 motif) with DDX6 (via
CC RecA-like domain 2) (PubMed:31439631). {ECO:0000250|UniProtKB:Q6Y7W8,
CC ECO:0000269|PubMed:22751931, ECO:0000269|PubMed:31439631}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6Y7W6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6Y7W6-3; Sequence=VSP_022244, VSP_043471;
CC Name=3;
CC IsoId=Q6Y7W6-4; Sequence=VSP_044996, VSP_044997;
CC Name=4;
CC IsoId=Q6Y7W6-5; Sequence=VSP_044996;
CC -!- DISEASE: Parkinson disease 11 (PARK11) [MIM:607688]: A complex
CC neurodegenerative disorder characterized by bradykinesia, resting
CC tremor, muscular rigidity and postural instability, as well as by a
CC clinically significant response to treatment with levodopa. The
CC pathology involves the loss of dopaminergic neurons in the substantia
CC nigra and the presence of Lewy bodies (intraneuronal accumulations of
CC aggregated proteins), in surviving neurons in various areas of the
CC brain. {ECO:0000269|PubMed:18358451, ECO:0000269|PubMed:20060621,
CC ECO:0000269|PubMed:20178831, ECO:0000269|PubMed:26134514}. Note=Disease
CC susceptibility may be associated with variants affecting the gene
CC represented in this entry. Its association with Parkinson disease is
CC however unclear. According to a number of studies, variations affecting
CC this gene are not a frequent cause of Parkinson disease, suggesting
CC that GIGYF2 does not play a major role in Parkinson disease etiology
CC (PubMed:19279319, PubMed:19429085, PubMed:19638301, PubMed:19482505,
CC PubMed:20004041, PubMed:19321232, PubMed:20060621).
CC {ECO:0000269|PubMed:19279319, ECO:0000269|PubMed:19321232,
CC ECO:0000269|PubMed:19429085, ECO:0000269|PubMed:19482505,
CC ECO:0000269|PubMed:19638301, ECO:0000269|PubMed:20004041,
CC ECO:0000269|PubMed:20060621}.
CC -!- SIMILARITY: Belongs to the GIGYF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31617.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA91873.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform.; Evidence={ECO:0000305};
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DR EMBL; AY176045; AAO46889.1; -; mRNA.
DR EMBL; AB014542; BAA31617.2; ALT_INIT; mRNA.
DR EMBL; BX538172; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK001739; BAA91873.1; ALT_SEQ; mRNA.
DR EMBL; BX537885; CAD97881.1; -; mRNA.
DR EMBL; BX538321; CAD98095.1; -; mRNA.
DR EMBL; AC016692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC064852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471063; EAW71016.1; -; Genomic_DNA.
DR EMBL; BC008072; AAH08072.2; -; mRNA.
DR EMBL; BC136251; AAI36252.1; -; mRNA.
DR EMBL; BC146775; AAI46776.1; -; mRNA.
DR CCDS; CCDS33401.1; -. [Q6Y7W6-1]
DR CCDS; CCDS46542.1; -. [Q6Y7W6-3]
DR CCDS; CCDS46543.1; -. [Q6Y7W6-5]
DR PIR; T00377; T00377.
DR RefSeq; NP_001096616.1; NM_001103146.1. [Q6Y7W6-1]
DR RefSeq; NP_001096617.1; NM_001103147.1. [Q6Y7W6-3]
DR RefSeq; NP_001096618.1; NM_001103148.1. [Q6Y7W6-5]
DR RefSeq; NP_056390.2; NM_015575.3. [Q6Y7W6-1]
DR PDB; 5NVL; X-ray; 2.30 A; B/D=35-105.
DR PDB; 5NVM; X-ray; 2.00 A; B/D=35-72.
DR PDBsum; 5NVL; -.
DR PDBsum; 5NVM; -.
DR AlphaFoldDB; Q6Y7W6; -.
DR SMR; Q6Y7W6; -.
DR BioGRID; 117520; 205.
DR IntAct; Q6Y7W6; 51.
DR MINT; Q6Y7W6; -.
DR STRING; 9606.ENSP00000387170; -.
DR BindingDB; Q6Y7W6; -.
DR ChEMBL; CHEMBL2331055; -.
DR GlyGen; Q6Y7W6; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q6Y7W6; -.
DR MetOSite; Q6Y7W6; -.
DR PhosphoSitePlus; Q6Y7W6; -.
DR BioMuta; GIGYF2; -.
DR DMDM; 74710467; -.
DR CPTAC; CPTAC-969; -.
DR EPD; Q6Y7W6; -.
DR jPOST; Q6Y7W6; -.
DR MassIVE; Q6Y7W6; -.
DR MaxQB; Q6Y7W6; -.
DR PaxDb; Q6Y7W6; -.
DR PeptideAtlas; Q6Y7W6; -.
DR PRIDE; Q6Y7W6; -.
DR ProteomicsDB; 19183; -.
DR ProteomicsDB; 67836; -. [Q6Y7W6-1]
DR ProteomicsDB; 67837; -. [Q6Y7W6-3]
DR Antibodypedia; 62944; 90 antibodies from 25 providers.
DR DNASU; 26058; -.
DR Ensembl; ENST00000373563.9; ENSP00000362664.5; ENSG00000204120.16. [Q6Y7W6-1]
DR Ensembl; ENST00000409196.7; ENSP00000387070.3; ENSG00000204120.16. [Q6Y7W6-5]
DR Ensembl; ENST00000409451.7; ENSP00000387170.3; ENSG00000204120.16. [Q6Y7W6-3]
DR Ensembl; ENST00000409547.5; ENSP00000386537.1; ENSG00000204120.16. [Q6Y7W6-1]
DR GeneID; 26058; -.
DR KEGG; hsa:26058; -.
DR MANE-Select; ENST00000373563.9; ENSP00000362664.5; NM_001103146.3; NP_001096616.1.
DR UCSC; uc002vth.6; human. [Q6Y7W6-1]
DR CTD; 26058; -.
DR DisGeNET; 26058; -.
DR GeneCards; GIGYF2; -.
DR HGNC; HGNC:11960; GIGYF2.
DR HPA; ENSG00000204120; Low tissue specificity.
DR MalaCards; GIGYF2; -.
DR MIM; 607688; phenotype.
DR MIM; 612003; gene.
DR neXtProt; NX_Q6Y7W6; -.
DR OpenTargets; ENSG00000204120; -.
DR Orphanet; 411602; Hereditary late-onset Parkinson disease.
DR PharmGKB; PA36647; -.
DR VEuPathDB; HostDB:ENSG00000204120; -.
DR eggNOG; KOG1862; Eukaryota.
DR GeneTree; ENSGT00940000156108; -.
DR HOGENOM; CLU_007300_0_0_1; -.
DR InParanoid; Q6Y7W6; -.
DR OMA; AIEMTEW; -.
DR OrthoDB; 412069at2759; -.
DR PhylomeDB; Q6Y7W6; -.
DR TreeFam; TF325513; -.
DR PathwayCommons; Q6Y7W6; -.
DR SignaLink; Q6Y7W6; -.
DR SIGNOR; Q6Y7W6; -.
DR BioGRID-ORCS; 26058; 84 hits in 1098 CRISPR screens.
DR ChiTaRS; GIGYF2; human.
DR GeneWiki; TNRC15; -.
DR GenomeRNAi; 26058; -.
DR Pharos; Q6Y7W6; Tchem.
DR PRO; PR:Q6Y7W6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6Y7W6; protein.
DR Bgee; ENSG00000204120; Expressed in calcaneal tendon and 209 other tissues.
DR ExpressionAtlas; Q6Y7W6; baseline and differential.
DR Genevisible; Q6Y7W6; HS.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005768; C:endosome; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:1990635; C:proximal dendrite; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0070064; F:proline-rich region binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0007631; P:feeding behavior; IEA:Ensembl.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IEA:Ensembl.
DR GO; GO:0061157; P:mRNA destabilization; IDA:ParkinsonsUK-UCL.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0050881; P:musculoskeletal movement; IEA:Ensembl.
DR GO; GO:0017148; P:negative regulation of translation; IMP:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0016441; P:post-transcriptional gene silencing; IDA:ParkinsonsUK-UCL.
DR GO; GO:0019538; P:protein metabolic process; IEA:Ensembl.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IEA:Ensembl.
DR CDD; cd00072; GYF; 1.
DR Gene3D; 3.30.1490.40; -; 1.
DR InterPro; IPR003169; GYF.
DR InterPro; IPR035445; GYF-like_dom_sf.
DR Pfam; PF02213; GYF; 1.
DR SMART; SM00444; GYF; 1.
DR SUPFAM; SSF55277; SSF55277; 1.
DR PROSITE; PS50829; GYF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Disease variant;
KW Isopeptide bond; Methylation; Neurodegeneration; Parkinson disease;
KW Parkinsonism; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..1299
FT /note="GRB10-interacting GYF protein 2"
FT /id="PRO_0000270837"
FT DOMAIN 533..581
FT /note="GYF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00101"
FT REGION 112..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..563
FT /note="Required for GRB10-binding"
FT /evidence="ECO:0000250"
FT REGION 733..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 40..50
FT /note="4EHP-binding motif"
FT /evidence="ECO:0000269|PubMed:22751931"
FT MOTIF 280..310
FT /note="DDX6 binding motif"
FT /evidence="ECO:0000269|PubMed:31439631"
FT COMPBIAS 147..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..997
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 107
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6Y7W8"
FT MOD_RES 118
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6Y7W8"
FT MOD_RES 120
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6Y7W8"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 149
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6Y7W8"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 382
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 993
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 1123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 177
FT /note="V -> VGKKNGYYCMYSPVLLLGQPLCQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9734811"
FT /id="VSP_022244"
FT VAR_SEQ 238..243
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_044996"
FT VAR_SEQ 365
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9734811"
FT /id="VSP_043471"
FT VAR_SEQ 1205..1211
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_044997"
FT VARIANT 56
FT /note="N -> S (may be associated with PARK11;
FT dbSNP:rs72554080)"
FT /evidence="ECO:0000269|PubMed:18358451,
FT ECO:0000269|PubMed:19638301, ECO:0000269|PubMed:20060621"
FT /id="VAR_044439"
FT VARIANT 112
FT /note="T -> A (in PARK11; dbSNP:rs1171688751)"
FT /evidence="ECO:0000269|PubMed:18358451"
FT /id="VAR_044440"
FT VARIANT 256
FT /note="E -> K (in PARK11; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:20178831"
FT /id="VAR_077935"
FT VARIANT 273
FT /note="S -> C (in PARK11; unknown pathological
FT significance; dbSNP:rs141225775)"
FT /evidence="ECO:0000269|PubMed:20060621"
FT /id="VAR_077936"
FT VARIANT 278
FT /note="I -> V (in PARK11; dbSNP:rs118203904)"
FT /evidence="ECO:0000269|PubMed:18358451"
FT /id="VAR_044441"
FT VARIANT 335
FT /note="S -> T (in PARK11; dbSNP:rs776898936)"
FT /evidence="ECO:0000269|PubMed:18358451"
FT /id="VAR_044442"
FT VARIANT 345
FT /note="A -> V (in PARK11; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:20178831"
FT /id="VAR_077937"
FT VARIANT 349
FT /note="D -> E (in PARK11; unknown pathological
FT significance; dbSNP:rs148277228)"
FT /evidence="ECO:0000269|PubMed:20060621"
FT /id="VAR_077938"
FT VARIANT 377
FT /note="S -> Y (in PARK11; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:20178831"
FT /id="VAR_077939"
FT VARIANT 423
FT /note="P -> L (in dbSNP:rs34845648)"
FT /id="VAR_051268"
FT VARIANT 457
FT /note="N -> T (in PARK11; unknown pathological
FT significance; dbSNP:rs116074753)"
FT /evidence="ECO:0000269|PubMed:18358451,
FT ECO:0000269|PubMed:20060621"
FT /id="VAR_044443"
FT VARIANT 460
FT /note="P -> T (in dbSNP:rs2289912)"
FT /evidence="ECO:0000269|PubMed:18358451,
FT ECO:0000269|PubMed:19429085"
FT /id="VAR_044444"
FT VARIANT 473
FT /note="P -> S (in PARK11; unknown pathological
FT significance; dbSNP:rs1384919564)"
FT /evidence="ECO:0000269|PubMed:20178831"
FT /id="VAR_077940"
FT VARIANT 492
FT /note="E -> K (in PARK11; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:20178831"
FT /id="VAR_077941"
FT VARIANT 519
FT /note="H -> Y (in PARK11; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:20178831"
FT /id="VAR_077942"
FT VARIANT 560
FT /note="A -> V (in dbSNP:rs761136505)"
FT /evidence="ECO:0000269|PubMed:20060621"
FT /id="VAR_077943"
FT VARIANT 580
FT /note="L -> F (in PARK11; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:20178831"
FT /id="VAR_077944"
FT VARIANT 589
FT /note="R -> G (in PARK11)"
FT /evidence="ECO:0000269|PubMed:26134514"
FT /id="VAR_077945"
FT VARIANT 606
FT /note="D -> E (in PARK11; dbSNP:rs118203903)"
FT /evidence="ECO:0000269|PubMed:18358451"
FT /id="VAR_044445"
FT VARIANT 979
FT /note="Missing (in PARK11; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:20178831"
FT /id="VAR_077946"
FT VARIANT 1070
FT /note="D -> H (in PARK11; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:20178831"
FT /id="VAR_077947"
FT VARIANT 1131
FT /note="A -> V (in dbSNP:rs773011114)"
FT /evidence="ECO:0000269|PubMed:20060621"
FT /id="VAR_077948"
FT VARIANT 1171
FT /note="H -> R (in dbSNP:rs72554081)"
FT /evidence="ECO:0000269|PubMed:18358451,
FT ECO:0000269|PubMed:20060621"
FT /id="VAR_044446"
FT VARIANT 1209
FT /note="L -> P (in PARK11; unknown pathological
FT significance; dbSNP:rs114013774)"
FT /evidence="ECO:0000269|PubMed:20060621"
FT /id="VAR_077949"
FT VARIANT 1211
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:18358451,
FT ECO:0000269|Ref.8"
FT /id="VAR_044447"
FT VARIANT 1212
FT /note="Q -> QQ"
FT /evidence="ECO:0000269|PubMed:18358451"
FT /id="VAR_044448"
FT VARIANT 1242
FT /note="V -> I (in PARK11; dbSNP:rs769022021)"
FT /evidence="ECO:0000269|PubMed:18358451"
FT /id="VAR_044449"
FT MUTAGEN 41..49
FT /note="YRYGREEML->ARAGREEAA: Abolishes interaction with
FT EIF4E2."
FT /evidence="ECO:0000269|PubMed:22751931"
FT MUTAGEN 288
FT /note="W->A: Abolishes interaction with DDX6."
FT /evidence="ECO:0000269|PubMed:31439631"
FT MUTAGEN 300
FT /note="F->A: Abolishes interaction with DDX6; when
FT associated with A-306."
FT /evidence="ECO:0000269|PubMed:31439631"
FT MUTAGEN 306
FT /note="F->A: Abolishes interaction with DDX6; when
FT associated with A-300."
FT /evidence="ECO:0000269|PubMed:31439631"
FT CONFLICT 565
FT /note="M -> T (in Ref. 4; BX538172)"
FT /evidence="ECO:0000305"
FT CONFLICT 792
FT /note="E -> G (in Ref. 6; CAD98095)"
FT /evidence="ECO:0000305"
FT CONFLICT 1153
FT /note="D -> G (in Ref. 6; CAD98095)"
FT /evidence="ECO:0000305"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:5NVM"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:5NVM"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:5NVM"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:5NVL"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:5NVL"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:5NVL"
SQ SEQUENCE 1299 AA; 150070 MW; 2282458102F64B71 CRC64;
MAAETQTLNF GPEWLRALSS GGSITSPPLS PALPKYKLAD YRYGREEMLA LFLKDNKIPS
DLLDKEFLPI LQEEPLPPLA LVPFTEEEQR NFSMSVNSAA VLRLTGRGGG GTVVGAPRGR
SSSRGRGRGR GECGFYQRSF DEVEGVFGRG GGREMHRSQS WEERGDRRFE KPGRKDVGRP
NFEEGGPTSV GRKHEFIRSE SENWRIFREE QNGEDEDGGW RLAGSRRDGE RWRPHSPDGP
RSAGWREHME RRRRFEFDFR DRDDERGYRR VRSGSGSIDD DRDSLPEWCL EDAEEEMGTF
DSSGAFLSLK KVQKEPIPEE QEMDFRPVDE GEECSDSEGS HNEEAKEPDK TNKKEGEKTD
RVGVEASEET PQTSSSSARP GTPSDHQSQE ASQFERKDEP KTEQTEKAEE ETRMENSLPA
KVPSRGDEMV ADVQQPLSQI PSDTASPLLI LPPPVPNPSP TLRPVETPVV GAPGMGSVST
EPDDEEGLKH LEQQAEKMVA YLQDSALDDE RLASKLQEHR AKGVSIPLMH EAMQKWYYKD
PQGEIQGPFN NQEMAEWFQA GYFTMSLLVK RACDESFQPL GDIMKMWGRV PFSPGPAPPP
HMGELDQERL TRQQELTALY QMQHLQYQQF LIQQQYAQVL AQQQKAALSS QQQQQLALLL
QQFQTLKMRI SDQNIIPSVT RSVSVPDTGS IWELQPTASQ PTVWEGGSVW DLPLDTTTPG
PALEQLQQLE KAKAAKLEQE RREAEMRAKR EEEERKRQEE LRRQQEEILR RQQEEERKRR
EEEELARRKQ EEALRRQREQ EIALRRQREE EERQQQEEAL RRLEERRREE EERRKQEELL
RKQEEEAAKW AREEEEAQRR LEENRLRMEE EAARLRHEEE ERKRKELEVQ RQKELMRQRQ
QQQEALRRLQ QQQQQQQLAQ MKLPSSSTWG QQSNTTACQS QATLSLAEIQ KLEEERERQL
REEQRRQQRE LMKALQQQQQ QQQQKLSGWG NVSKPSGTTK SLLEIQQEEA RQMQKQQQQQ
QQHQQPNRAR NNTHSNLHTS IGNSVWGSIN TGPPNQWASD LVSSIWSNAD TKNSNMGFWD
DAVKEVGPRN STNKNKNNAS LSKSVGVSNR QNKKVEEEEK LLKLFQGVNK AQDGFTQWCE
QMLHALNTAN NLDVPTFVSF LKEVESPYEV HDYIRAYLGD TSEAKEFAKQ FLERRAKQKA
NQQRQQQQLP QQQQQQPPQQ PPQQPQQQDS VWGMNHSTLH SVFQTNQSNN QQSNFEAVQS
GKKKKKQKMV RADPSLLGFS VNASSERLNM GEIETLDDY
