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 28-JAN-2026, entry version 176. 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, GN ECO:0000312|HGNC:HGNC:11960}; GN Synonyms=KIAA0642 {ECO:0000303|PubMed:9734811}, PERQ2, TNRC15 GN {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 FUNCTION, AND IDENTIFICATION IN THE 4EHP-GYF2 COMPLEX. RX PubMed=32726578; DOI=10.1016/j.molcel.2020.07.007; RA Hickey K.L., Dickson K., Cogan J.Z., Replogle J.M., Schoof M., RA D'Orazio K.N., Sinha N.K., Hussmann J.A., Jost M., Frost A., Green R., RA Weissman J.S., Kostova K.K.; RT "GIGYF2 and 4EHP Inhibit Translation Initiation of Defective Messenger RNAs RT to Assist Ribosome-Associated Quality Control."; RL Mol. Cell 79:950.e6-962.e6(2020). RN [33] RP FUNCTION, FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH SARS-COV RP NON-STRUCTURAL PROTEIN 2 PROTEIN (MICROBIAL INFECTION). RX PubMed=35878012; DOI=10.1073/pnas.2204539119; RA Xu Z., Choi J.H., Dai D.L., Luo J., Ladak R.J., Li Q., Wang Y., Zhang C., RA Wiebe S., Liu A.C.H., Ran X., Yang J., Naeli P., Garzia A., Zhou L., RA Mahmood N., Deng Q., Elaish M., Lin R., Mahal L.K., Hobman T.C., RA Pelletier J., Alain T., Vidal S.M., Duchaine T., Mazhab-Jafari M.T., RA Mao X., Jafarnejad S.M., Sonenberg N.; RT "SARS-CoV-2 impairs interferon production via NSP2-induced repression of RT mRNA translation."; RL Proc. Natl. Acad. Sci. U.S.A. 119:e2204539119-e2204539119(2022). RN [34] 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 [35] 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 [36] 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 [37] 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 [38] 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 [39] 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, PubMed:35878012). In the 4EHP-GYF2 CC complex, acts as a factor that bridges EIF4E2 to ZFP36/TTP, linking CC translation repression with mRNA decay (PubMed:31439631). Also recruits CC and bridges the association of the 4EHP complex with the decapping CC effector protein DDX6, which is required for the ZFP36/TTP-mediated CC down-regulation of AU-rich mRNA (PubMed:31439631). May act CC cooperatively with GRB10 to regulate tyrosine kinase receptor CC signaling, including IGF1 and insulin receptors (PubMed:12771153). In CC association with EIF4E2, assists ribosome-associated quality control CC (RQC) by sequestering the mRNA cap, blocking ribosome initiation and CC decreasing the translational load on problematic messages. Part of a CC pathway that works in parallel to RQC-mediated degradation of the CC stalled nascent polypeptide (PubMed:32726578). GIGYF2 and EIF4E2 work CC downstream and independently of ZNF598, which seems to work as a CC scaffold that can recruit them to faulty mRNA even if alternative CC recruitment mechanisms may exist (PubMed:32726578). CC {ECO:0000269|PubMed:12771153, ECO:0000269|PubMed:22751931, CC ECO:0000269|PubMed:31439631, ECO:0000269|PubMed:32726578, CC ECO:0000269|PubMed:35878012}. CC -!- FUNCTION: (Microbial infection) Upon SARS coronavirus-2/SARS-CoV-2 CC infection, the interaction with non-structural protein 2 (nsp2) CC enhances GIGYF2 binding to EIF4E2 and increases repression of CC translation initiation of genes involved in antiviral innate immune CC response such as IFNB1. {ECO:0000269|PubMed:35878012}. CC -!- SUBUNIT: Component of the 4EHP-GYF2 complex, at least composed of CC EIF4E2, GIGYF2 and ZNF598 (PubMed:22751931, PubMed:31439631, CC PubMed:32726578). Interacts (via the 4EHP-binding motif) with EIF4E2; CC the interaction is direct (PubMed:22751931, PubMed:31439631, CC PubMed:32726578). Interacts with ZFP36/TTP (via P-P-P-P-G repeats); the CC interaction is direct (PubMed:31439631). Interacts with GRB10 (By CC similarity). Interacts (via DDX6 motif) with DDX6 (via RecA-like domain CC 2) (PubMed:31439631). {ECO:0000250|UniProtKB:Q6Y7W8, CC ECO:0000269|PubMed:22751931, ECO:0000269|PubMed:31439631, CC ECO:0000269|PubMed:32726578}. CC -!- SUBUNIT: (Microbial infection) Interacts with SARS coronavirus-2/SARS- CC CoV-2 non-structural protein 2 (nsp2); the interaction enhances GIGYF2 CC binding to EIF4E2. {ECO:0000269|PubMed:35878012}. CC -!- INTERACTION: CC Q6Y7W6; O60573: EIF4E2; NbExp=4; IntAct=EBI-765394, EBI-398610; CC Q6Y7W6; O60573-1: EIF4E2; NbExp=6; IntAct=EBI-765394, EBI-32715389; CC Q6Y7W6; P63104: YWHAZ; NbExp=2; IntAct=EBI-765394, EBI-347088; CC Q6Y7W6-1; O60573-1: EIF4E2; NbExp=11; IntAct=EBI-25762361, EBI-32715389; 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:19321232, PubMed:19429085, PubMed:19482505, CC PubMed:19638301, PubMed:20004041, 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; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA91873.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001103146.3. [Q6Y7W6-1] DR RefSeq; NP_001096617.1; NM_001103147.2. [Q6Y7W6-3] DR RefSeq; NP_001096618.1; NM_001103148.2. [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 PDB; 7RUP; X-ray; 1.23 A; A=529-597. DR PDBsum; 5NVL; -. DR PDBsum; 5NVM; -. DR PDBsum; 7RUP; -. DR AlphaFoldDB; Q6Y7W6; -. DR SMR; Q6Y7W6; -. DR BioGRID; 117520; 294. DR ComplexPortal; CPX-2332; 4EHP-GIGYF2 co-translational mRNA decay complex, ZNF598 variant. DR ComplexPortal; CPX-2338; 4EHP-GIGYF2 co-translational mRNA decay complex, DDX6 variant. DR CORUM; Q6Y7W6; -. DR FunCoup; Q6Y7W6; 3093. DR IntAct; Q6Y7W6; 146. DR MINT; Q6Y7W6; -. DR STRING; 9606.ENSP00000387170; -. DR BindingDB; Q6Y7W6; -. DR ChEMBL; CHEMBL2331055; -. DR GlyCosmos; Q6Y7W6; 3 sites, 1 glycan. DR GlyGen; Q6Y7W6; 10 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (8 sites). DR iPTMnet; Q6Y7W6; -. DR MetOSite; Q6Y7W6; -. DR PhosphoSitePlus; Q6Y7W6; -. DR BioMuta; GIGYF2; -. DR DMDM; 74710467; -. DR CPTAC; CPTAC-969; -. DR jPOST; Q6Y7W6; -. DR MassIVE; Q6Y7W6; -. DR PaxDb; 9606-ENSP00000387170; -. DR PeptideAtlas; Q6Y7W6; -. DR ProteomicsDB; 19183; -. DR ProteomicsDB; 67836; -. [Q6Y7W6-1] DR ProteomicsDB; 67837; -. [Q6Y7W6-3] DR Pumba; Q6Y7W6; -. DR Antibodypedia; 62944; 87 antibodies from 25 providers. DR DNASU; 26058; -. DR Ensembl; ENST00000373563.9; ENSP00000362664.5; ENSG00000204120.17. [Q6Y7W6-1] DR Ensembl; ENST00000409196.7; ENSP00000387070.3; ENSG00000204120.17. [Q6Y7W6-5] DR Ensembl; ENST00000409451.7; ENSP00000387170.3; ENSG00000204120.17. [Q6Y7W6-3] DR Ensembl; ENST00000409547.5; ENSP00000386537.1; ENSG00000204120.17. [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 AGR; HGNC:11960; -. DR ClinPGx; PA36647; -. 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 OpenTargets; ENSG00000204120; -. DR Orphanet; 411602; Hereditary late-onset Parkinson disease. DR VEuPathDB; HostDB:ENSG00000204120; -. DR eggNOG; KOG1862; Eukaryota. DR GeneTree; ENSGT00940000156108; -. DR HOGENOM; CLU_007300_0_0_1; -. DR InParanoid; Q6Y7W6; -. DR OMA; QNRICLQ; -. DR OrthoDB; 9539369at2759; -. DR PAN-GO; Q6Y7W6; 6 GO annotations based on evolutionary models. DR PhylomeDB; Q6Y7W6; -. DR PathwayCommons; Q6Y7W6; -. DR SignaLink; Q6Y7W6; -. DR SIGNOR; Q6Y7W6; -. DR Agora; ENSG00000204120; -. DR BioGRID-ORCS; 26058; 91 hits in 1193 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; DEE660B4; Stress granule. 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 211 other cell types or tissues. DR ExpressionAtlas; Q6Y7W6; baseline and differential. 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: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:0060090; F:molecular adaptor activity; IDA:UniProt. 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:0045947; P:negative regulation of translational initiation; IDA:UniProt. DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IDA:UniProt. 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:0072344; P:rescue of stalled ribosome; IDA:UniProt. DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IEA:Ensembl. DR CDD; cd00072; GYF; 1. DR FunFam; 3.30.1490.40:FF:000001; GRB10-interacting GYF protein 2 isoform X1; 1. DR Gene3D; 3.30.1490.40; -; 1. DR InterPro; IPR051640; GRB10-interact_GYF. DR InterPro; IPR003169; GYF. DR InterPro; IPR035445; GYF-like_dom_sf. DR PANTHER; PTHR14445; GRB10 INTERACTING GYF PROTEIN; 1. DR PANTHER; PTHR14445:SF38; GRB10-INTERACTING GYF PROTEIN 2; 1. DR Pfam; PF02213; GYF; 1. DR SMART; SM00444; GYF; 1. DR SUPFAM; SSF55277; GYF domain; 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; Proteomics identification; KW 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 860..919 FT /note="Required for interaction with SARS-CoV-2 non- FT structural protein 2 (nsp2)" FT /evidence="ECO:0000269|PubMed:35878012" 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 151..182 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 225..247 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 289..298 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 312..329 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 338..363 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 369..392 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 393..414 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 924..936 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 957..972 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1013..1025 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1026..1048 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1090..1104 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1202..1217 FT /note="Low complexity" 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 (probable risk factor for 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; uncertain significance; FT dbSNP:rs1171688751)" FT /evidence="ECO:0000269|PubMed:18358451" FT /id="VAR_044440" FT VARIANT 256 FT /note="E -> K (in PARK11; uncertain significance)" FT /evidence="ECO:0000269|PubMed:20178831" FT /id="VAR_077935" FT VARIANT 273 FT /note="S -> C (in PARK11; uncertain significance; FT dbSNP:rs141225775)" FT /evidence="ECO:0000269|PubMed:20060621" FT /id="VAR_077936" FT VARIANT 278 FT /note="I -> V (probable risk factor for PARK11; FT dbSNP:rs118203904)" FT /evidence="ECO:0000269|PubMed:18358451" FT /id="VAR_044441" FT VARIANT 335 FT /note="S -> T (in PARK11; uncertain significance; FT dbSNP:rs776898936)" FT /evidence="ECO:0000269|PubMed:18358451" FT /id="VAR_044442" FT VARIANT 345 FT /note="A -> V (in PARK11; uncertain significance)" FT /evidence="ECO:0000269|PubMed:20178831" FT /id="VAR_077937" FT VARIANT 349 FT /note="D -> E (in PARK11; uncertain significance; FT dbSNP:rs148277228)" FT /evidence="ECO:0000269|PubMed:20060621" FT /id="VAR_077938" FT VARIANT 377 FT /note="S -> Y (in PARK11; uncertain 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 (probable risk factor for PARK11; FT 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; uncertain significance; FT dbSNP:rs1384919564)" FT /evidence="ECO:0000269|PubMed:20178831" FT /id="VAR_077940" FT VARIANT 492 FT /note="E -> K (in PARK11; uncertain significance)" FT /evidence="ECO:0000269|PubMed:20178831" FT /id="VAR_077941" FT VARIANT 519 FT /note="H -> Y (in PARK11; uncertain 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; uncertain significance)" FT /evidence="ECO:0000269|PubMed:20178831" FT /id="VAR_077944" FT VARIANT 589 FT /note="R -> G (probable risk factor for PARK11)" FT /evidence="ECO:0000269|PubMed:26134514" FT /id="VAR_077945" FT VARIANT 606 FT /note="D -> E (probable risk factor for PARK11; FT dbSNP:rs118203903)" FT /evidence="ECO:0000269|PubMed:18358451" FT /id="VAR_044445" FT VARIANT 979 FT /note="Missing (in PARK11; uncertain significance)" FT /evidence="ECO:0000269|PubMed:20178831" FT /id="VAR_077946" FT VARIANT 1070 FT /note="D -> H (in PARK11; uncertain 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; uncertain significance; FT 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" FT STRAND 536..539 FT /evidence="ECO:0007829|PDB:7RUP" FT STRAND 545..549 FT /evidence="ECO:0007829|PDB:7RUP" FT HELIX 551..560 FT /evidence="ECO:0007829|PDB:7RUP" FT STRAND 568..571 FT /evidence="ECO:0007829|PDB:7RUP" FT STRAND 574..576 FT /evidence="ECO:0007829|PDB:7RUP" FT HELIX 580..587 FT /evidence="ECO:0007829|PDB:7RUP" 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 //